CNRS Nantes University US2B US2B
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***  wewe  ***

elNémo ID: 250201224349801369

Job options:

ID        	=	 250201224349801369
JOBID     	=	 wewe
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 10
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER wewe

HEADER    TRANSFERASE                             19-SEP-17   6B2E              
TITLE     STRUCTURE OF FULL LENGTH HUMAN AMPK (A2B2G1) IN COMPLEX WITH A SMALL  
TITLE    2 MOLECULE ACTIVATOR SC4.                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-2; 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: AMPK SUBUNIT ALPHA-2,ACETYL-COA CARBOXYLASE KINASE,ACACA    
COMPND   5 KINASE,HYDROXYMETHYLGLUTARYL-COA REDUCTASE KINASE,HMGCR KINASE;      
COMPND   6 EC: 2.7.11.1,2.7.11.27,2.7.11.31;                                    
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-2;            
COMPND  10 CHAIN: B;                                                            
COMPND  11 SYNONYM: AMPK SUBUNIT BETA-2;                                        
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1;           
COMPND  15 CHAIN: C;                                                            
COMPND  16 SYNONYM: AMPKG;                                                      
COMPND  17 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PRKAA2, AMPK, AMPK2;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3);                             
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PETDUET-1;                                
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: PRKAB2;                                                        
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3);                             
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PRSFDUET-1;                               
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  21 ORGANISM_COMMON: HUMAN;                                              
SOURCE  22 ORGANISM_TAXID: 9606;                                                
SOURCE  23 GENE: PRKAG1;                                                        
SOURCE  24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  26 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3);                             
SOURCE  27 EXPRESSION_SYSTEM_PLASMID: PETDUET-1                                 
KEYWDS    PHOSPHORYLATED, ACTIVE, HETEROTRIMER, KINASE., TRANSFERASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.R.W.NGOEI,C.G.LANGENDORF,N.X.Y.LING,A.HOQUE,S.JOHNSON,M.C.CAMERINO, 
AUTHOR   2 S.R.WALKER,Y.E.BOZIKIS,T.A.DITE,A.J.OVENS,W.J.SMILES,R.JACOBS,       
AUTHOR   3 H.HUANG,M.W.PARKER,J.W.SCOTT,M.H.RIDER,B.E.KEMP,R.C.FOITZIK,         
AUTHOR   4 J.B.BAELL,J.S.OAKHILL                                                
REVDAT   7   13-NOV-24 6B2E    1       REMARK                                   
REVDAT   6   04-OCT-23 6B2E    1       HETSYN                                   
REVDAT   5   29-JUL-20 6B2E    1       COMPND REMARK HET    HETNAM              
REVDAT   5 2                   1       HETSYN FORMUL LINK   SITE                
REVDAT   5 3                   1       ATOM                                     
REVDAT   4   01-JAN-20 6B2E    1       REMARK                                   
REVDAT   3   04-JUL-18 6B2E    1       JRNL                                     
REVDAT   2   02-MAY-18 6B2E    1       JRNL                                     
REVDAT   1   25-APR-18 6B2E    0                                                
JRNL        AUTH   K.R.W.NGOEI,C.G.LANGENDORF,N.X.Y.LING,A.HOQUE,S.VARGHESE,    
JRNL        AUTH 2 M.A.CAMERINO,S.R.WALKER,Y.E.BOZIKIS,T.A.DITE,A.J.OVENS,      
JRNL        AUTH 3 W.J.SMILES,R.JACOBS,H.HUANG,M.W.PARKER,J.W.SCOTT,M.H.RIDER,  
JRNL        AUTH 4 R.C.FOITZIK,B.E.KEMP,J.B.BAELL,J.S.OAKHILL                   
JRNL        TITL   STRUCTURAL DETERMINANTS FOR SMALL-MOLECULE ACTIVATION OF     
JRNL        TITL 2 SKELETAL MUSCLE AMPK ALPHA 2 BETA 2 GAMMA 1 BY THE GLUCOSE   
JRNL        TITL 3 IMPORTAGOG SC4.                                              
JRNL        REF    CELL CHEM BIOL                V.  25   728 2018              
JRNL        REFN                   ESSN 2451-9448                               
JRNL        PMID   29657085                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2018.03.008                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.2                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.15                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 17764                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.246                          
REMARK   3   R VALUE            (WORKING SET)  : 0.244                          
REMARK   3   FREE R VALUE                      : 0.277                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.180                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 920                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.000                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 9                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.80                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 4.03                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 83.29                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2512                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2680                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2379                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2670                   
REMARK   3   BIN FREE R VALUE                        : 0.2840                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.29                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 133                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6528                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 192                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 89.66                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 136.9                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 11.52240                                             
REMARK   3    B22 (A**2) : -16.35700                                            
REMARK   3    B33 (A**2) : 4.83470                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.630               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.658               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.895                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.886                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 7098   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 9751   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2232   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 115    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1050   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 7098   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1031   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 7482   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.01                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.34                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.56                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|9 - A|552 A|601 - A|601 }                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -18.6611  -20.5496   15.8347           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.4847 T22:   -0.1769                                    
REMARK   3     T33:   -0.2514 T12:    0.1438                                    
REMARK   3     T13:    0.0672 T23:    0.0757                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.1155 L22:    3.2536                                    
REMARK   3     L33:    2.8008 L12:   -0.4531                                    
REMARK   3     L13:   -0.8657 L23:    2.0652                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0087 S12:    0.0066 S13:   -0.1455                     
REMARK   3     S21:    0.3517 S22:   -0.0502 S23:    0.2623                     
REMARK   3     S31:    0.2468 S32:   -0.0367 S33:    0.0589                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|59 - B|272 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):  -31.4872  -34.3204   13.2296           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3950 T22:   -0.4119                                    
REMARK   3     T33:   -0.1499 T12:    0.0025                                    
REMARK   3     T13:    0.2156 T23:    0.1044                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.9287 L22:    2.2293                                    
REMARK   3     L33:    3.3594 L12:    0.5128                                    
REMARK   3     L13:    0.2894 L23:    2.6167                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0331 S12:   -0.1364 S13:   -0.5852                     
REMARK   3     S21:    0.7034 S22:   -0.0831 S23:    0.2423                     
REMARK   3     S31:    0.7823 S32:   -0.2177 S33:    0.1162                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { B|301 - B|301 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -32.6858   19.6855   26.1641           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.5181 T22:   -0.4628                                    
REMARK   3     T33:   -0.7714 T12:    0.2237                                    
REMARK   3     T13:    0.0469 T23:    0.1203                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.4124 L22:    6.4808                                    
REMARK   3     L33:    4.5312 L12:   -1.8865                                    
REMARK   3     L13:   -1.1867 L23:    2.2976                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2445 S12:    0.3394 S13:    0.2515                     
REMARK   3     S21:   -1.2246 S22:   -0.4172 S23:    0.1296                     
REMARK   3     S31:   -0.9460 S32:   -0.3132 S33:    0.1727                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6B2E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000230157.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JUL-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17814                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.150                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.20200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.25                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.86800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 6BIU, 4RER                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 6-8% PEG 3350, 0.1 M MGCL2, 0.001%       
REMARK 280  COCAMIDOPROPYL BETAINE AND 0.1 M IMIDAZOLE, PH 6.0, VAPOR           
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       56.96800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.04800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       59.42400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       69.04800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       56.96800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       59.42400            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14990 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 44300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -114.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     GLN A    -1                                                      
REMARK 465     ASP A     0                                                      
REMARK 465     PRO A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     ASP A   319                                                      
REMARK 465     GLN A   320                                                      
REMARK 465     LEU A   321                                                      
REMARK 465     ALA A   322                                                      
REMARK 465     VAL A   323                                                      
REMARK 465     PRO A   348                                                      
REMARK 465     SER A   349                                                      
REMARK 465     GLY A   350                                                      
REMARK 465     SER A   351                                                      
REMARK 465     PHE A   352                                                      
REMARK 465     MET A   353                                                      
REMARK 465     ASP A   354                                                      
REMARK 465     ASP A   355                                                      
REMARK 465     SER A   356                                                      
REMARK 465     ALA A   357                                                      
REMARK 465     MET A   358                                                      
REMARK 465     HIS A   359                                                      
REMARK 465     ILE A   360                                                      
REMARK 465     PRO A   361                                                      
REMARK 465     PRO A   362                                                      
REMARK 465     GLY A   363                                                      
REMARK 465     ASP A   377                                                      
REMARK 465     SER A   378                                                      
REMARK 465     PRO A   379                                                      
REMARK 465     LYS A   380                                                      
REMARK 465     ALA A   381                                                      
REMARK 465     ARG A   382                                                      
REMARK 465     CYS A   383                                                      
REMARK 465     PRO A   384                                                      
REMARK 465     LEU A   385                                                      
REMARK 465     ASP A   386                                                      
REMARK 465     ALA A   387                                                      
REMARK 465     LEU A   388                                                      
REMARK 465     ASN A   389                                                      
REMARK 465     THR A   390                                                      
REMARK 465     THR A   391                                                      
REMARK 465     LYS A   392                                                      
REMARK 465     PRO A   393                                                      
REMARK 465     LYS A   394                                                      
REMARK 465     SER A   395                                                      
REMARK 465     LEU A   396                                                      
REMARK 465     ALA A   397                                                      
REMARK 465     VAL A   398                                                      
REMARK 465     GLU A   476                                                      
REMARK 465     VAL A   477                                                      
REMARK 465     VAL A   478                                                      
REMARK 465     GLU A   479                                                      
REMARK 465     GLN A   480                                                      
REMARK 465     ARG A   481                                                      
REMARK 465     SER A   482                                                      
REMARK 465     GLY A   483                                                      
REMARK 465     SER A   484                                                      
REMARK 465     SER A   485                                                      
REMARK 465     THR A   486                                                      
REMARK 465     PRO A   487                                                      
REMARK 465     GLN A   488                                                      
REMARK 465     ARG A   489                                                      
REMARK 465     SER A   490                                                      
REMARK 465     CYS A   491                                                      
REMARK 465     SER A   492                                                      
REMARK 465     ALA A   493                                                      
REMARK 465     ALA A   494                                                      
REMARK 465     GLY A   495                                                      
REMARK 465     LEU A   496                                                      
REMARK 465     HIS A   497                                                      
REMARK 465     ARG A   498                                                      
REMARK 465     PRO A   499                                                      
REMARK 465     ARG A   500                                                      
REMARK 465     SER A   501                                                      
REMARK 465     SER A   502                                                      
REMARK 465     PHE A   503                                                      
REMARK 465     ASP A   504                                                      
REMARK 465     SER A   505                                                      
REMARK 465     THR A   506                                                      
REMARK 465     THR A   507                                                      
REMARK 465     ALA A   508                                                      
REMARK 465     GLU A   509                                                      
REMARK 465     SER A   510                                                      
REMARK 465     HIS A   511                                                      
REMARK 465     SER A   512                                                      
REMARK 465     LEU A   513                                                      
REMARK 465     SER A   514                                                      
REMARK 465     GLY A   515                                                      
REMARK 465     SER A   516                                                      
REMARK 465     LEU A   517                                                      
REMARK 465     THR A   518                                                      
REMARK 465     GLY A   519                                                      
REMARK 465     SER A   520                                                      
REMARK 465     LEU A   521                                                      
REMARK 465     THR A   522                                                      
REMARK 465     GLY A   523                                                      
REMARK 465     SER A   524                                                      
REMARK 465     THR A   525                                                      
REMARK 465     LEU A   526                                                      
REMARK 465     SER A   527                                                      
REMARK 465     SER A   528                                                      
REMARK 465     VAL A   529                                                      
REMARK 465     SER A   530                                                      
REMARK 465     PRO A   531                                                      
REMARK 465     ARG A   532                                                      
REMARK 465     ARG A   553                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ASN B     3                                                      
REMARK 465     THR B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     ASP B     7                                                      
REMARK 465     ARG B     8                                                      
REMARK 465     VAL B     9                                                      
REMARK 465     SER B    10                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     GLU B    12                                                      
REMARK 465     ARG B    13                                                      
REMARK 465     HIS B    14                                                      
REMARK 465     GLY B    15                                                      
REMARK 465     ALA B    16                                                      
REMARK 465     LYS B    17                                                      
REMARK 465     ALA B    18                                                      
REMARK 465     ALA B    19                                                      
REMARK 465     ARG B    20                                                      
REMARK 465     SER B    21                                                      
REMARK 465     GLU B    22                                                      
REMARK 465     GLY B    23                                                      
REMARK 465     ALA B    24                                                      
REMARK 465     GLY B    25                                                      
REMARK 465     GLY B    26                                                      
REMARK 465     HIS B    27                                                      
REMARK 465     ALA B    28                                                      
REMARK 465     PRO B    29                                                      
REMARK 465     GLY B    30                                                      
REMARK 465     LYS B    31                                                      
REMARK 465     GLU B    32                                                      
REMARK 465     HIS B    33                                                      
REMARK 465     LYS B    34                                                      
REMARK 465     ILE B    35                                                      
REMARK 465     MET B    36                                                      
REMARK 465     VAL B    37                                                      
REMARK 465     GLY B    38                                                      
REMARK 465     SER B    39                                                      
REMARK 465     THR B    40                                                      
REMARK 465     ASP B    41                                                      
REMARK 465     ASP B    42                                                      
REMARK 465     PRO B    43                                                      
REMARK 465     SER B    44                                                      
REMARK 465     VAL B    45                                                      
REMARK 465     PHE B    46                                                      
REMARK 465     SER B    47                                                      
REMARK 465     LEU B    48                                                      
REMARK 465     PRO B    49                                                      
REMARK 465     ASP B    50                                                      
REMARK 465     SER B    51                                                      
REMARK 465     LYS B    52                                                      
REMARK 465     LEU B    53                                                      
REMARK 465     PRO B    54                                                      
REMARK 465     GLY B    55                                                      
REMARK 465     ASP B    56                                                      
REMARK 465     LYS B    57                                                      
REMARK 465     GLU B    58                                                      
REMARK 465     GLU B   172                                                      
REMARK 465     SER B   173                                                      
REMARK 465     SER B   174                                                      
REMARK 465     GLU B   175                                                      
REMARK 465     THR B   176                                                      
REMARK 465     SER B   177                                                      
REMARK 465     CYS B   178                                                      
REMARK 465     ARG B   179                                                      
REMARK 465     ASP B   180                                                      
REMARK 465     LEU B   181                                                      
REMARK 465     SER B   182                                                      
REMARK 465     SER B   183                                                      
REMARK 465     SER B   184                                                      
REMARK 465     PRO B   185                                                      
REMARK 465     PRO B   186                                                      
REMARK 465     GLY B   187                                                      
REMARK 465     PRO B   188                                                      
REMARK 465     TYR B   189                                                      
REMARK 465     ARG B   201                                                      
REMARK 465     PHE B   202                                                      
REMARK 465     LYS B   203                                                      
REMARK 465     MET C    -4                                                      
REMARK 465     ALA C    -3                                                      
REMARK 465     ASP C    -2                                                      
REMARK 465     LEU C    -1                                                      
REMARK 465     ASN C     0                                                      
REMARK 465     TRP C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     THR C     3                                                      
REMARK 465     VAL C     4                                                      
REMARK 465     ILE C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     SER C     7                                                      
REMARK 465     ASP C     8                                                      
REMARK 465     SER C     9                                                      
REMARK 465     SER C    10                                                      
REMARK 465     PRO C    11                                                      
REMARK 465     ALA C    12                                                      
REMARK 465     VAL C    13                                                      
REMARK 465     GLU C    14                                                      
REMARK 465     ASN C    15                                                      
REMARK 465     GLU C    16                                                      
REMARK 465     HIS C    17                                                      
REMARK 465     PRO C    18                                                      
REMARK 465     GLN C    19                                                      
REMARK 465     GLU C    20                                                      
REMARK 465     THR C    21                                                      
REMARK 465     PRO C    22                                                      
REMARK 465     GLU C    23                                                      
REMARK 465     SER C    24                                                      
REMARK 465     GLN C   123                                                      
REMARK 465     ASP C   124                                                      
REMARK 465     SER C   125                                                      
REMARK 465     PHE C   126                                                      
REMARK 465     LYS C   127                                                      
REMARK 465     THR C   325                                                      
REMARK 465     GLY C   326                                                      
REMARK 465     GLY C   327                                                      
REMARK 465     GLU C   328                                                      
REMARK 465     LYS C   329                                                      
REMARK 465     LYS C   330                                                      
REMARK 465     PRO C   331                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  10    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  12    CE   NZ                                             
REMARK 470     LYS A  29    CG   CD   CE   NZ                                   
REMARK 470     LYS A  31    CG   CD   CE   NZ                                   
REMARK 470     ILE A  32    CG1  CG2  CD1                                       
REMARK 470     GLN A  36    CD   OE1  NE2                                       
REMARK 470     ARG A  49    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  51    CG   CD   CE   NZ                                   
REMARK 470     ARG A  53    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  60    CG   CD   CE   NZ                                   
REMARK 470     LYS A  62    CG   CD   CE   NZ                                   
REMARK 470     ARG A  63    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  64    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  69    CG   CD   CE   NZ                                   
REMARK 470     ARG A  72    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  78    CE   NZ                                             
REMARK 470     GLU A 100    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 103    CG   OD1  OD2                                       
REMARK 470     LYS A 107    CG   CD   CE   NZ                                   
REMARK 470     HIS A 108    CG   ND1  CD2  CE1  NE2                             
REMARK 470     VAL A 111    CG1  CG2                                            
REMARK 470     GLU A 112    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 113    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 154    CD   CE   NZ                                        
REMARK 470     LEU A 160    CG   CD1  CD2                                       
REMARK 470     GLU A 168    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 171    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 188    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 224    CG   CD   CE   NZ                                   
REMARK 470     LYS A 225    CE   NZ                                             
REMARK 470     ARG A 227    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A 235    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 239    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 255    CG   CD   CE   NZ                                   
REMARK 470     ILE A 259    CG1  CG2  CD1                                       
REMARK 470     LYS A 260    CG   CD   CE   NZ                                   
REMARK 470     ARG A 263    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 266    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 269    CG   CD   CE   NZ                                   
REMARK 470     ASP A 280    CG   OD1  OD2                                       
REMARK 470     TYR A 283    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN A 286    CG   OD1  ND2                                       
REMARK 470     ILE A 288    CG1  CG2  CD1                                       
REMARK 470     ASP A 290    CG   OD1  OD2                                       
REMARK 470     GLU A 291    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 294    CG   CD   CE   NZ                                   
REMARK 470     GLU A 295    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 298    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 299    CG   CD   CE   NZ                                   
REMARK 470     PHE A 300    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A 301    CG   CD   OE1  OE2                                  
REMARK 470     THR A 303    OG1  CG2                                            
REMARK 470     GLU A 304    CG   CD   OE1  OE2                                  
REMARK 470     SER A 305    OG                                                  
REMARK 470     VAL A 307    CG1  CG2                                            
REMARK 470     MET A 308    CG   SD   CE                                        
REMARK 470     ASN A 309    CG   OD1  ND2                                       
REMARK 470     SER A 310    OG                                                  
REMARK 470     TYR A 325    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 327    CG   CD1  CD2                                       
REMARK 470     ILE A 328    CG1  CG2  CD1                                       
REMARK 470     ILE A 329    CG1  CG2  CD1                                       
REMARK 470     ASP A 330    CG   OD1  OD2                                       
REMARK 470     ASN A 331    CG   OD1  ND2                                       
REMARK 470     ARG A 332    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 333    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A 335    CG   SD   CE                                        
REMARK 470     GLN A 337    CG   CD   OE1  NE2                                  
REMARK 470     PHE A 341    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     TYR A 342    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 364    CG   CD1  CD2                                       
REMARK 470     LYS A 365    CG   CD   CE   NZ                                   
REMARK 470     GLU A 369    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 374    CG   CD1  CD2                                       
REMARK 470     LYS A 399    CG   CD   CE   NZ                                   
REMARK 470     LYS A 400    CG   CD   CE   NZ                                   
REMARK 470     LYS A 402    CG   CD   CE   NZ                                   
REMARK 470     ARG A 408    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 410    CD   OE1  NE2                                       
REMARK 470     GLU A 419    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 422    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A 424    CG   SD   CE                                        
REMARK 470     LYS A 425    CG   CD   CE   NZ                                   
REMARK 470     GLU A 430    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 432    CG   CD   CE   NZ                                   
REMARK 470     ARG A 440    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 442    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 444    CG   CD   CE   NZ                                   
REMARK 470     ASP A 462    CG   OD1  OD2                                       
REMARK 470     ARG A 464    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 467    CG   CD1  CD2                                       
REMARK 470     ASP A 475    CG   OD1  OD2                                       
REMARK 470     SER A 535    OG                                                  
REMARK 470     THR A 537    OG1  CG2                                            
REMARK 470     PHE B  59    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     VAL B  60    CG1  CG2                                            
REMARK 470     TRP B  62    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B  62    CZ3  CH2                                            
REMARK 470     GLN B  63    CG   CD   OE1  NE2                                  
REMARK 470     ASP B  65    CG   OD1  OD2                                       
REMARK 470     LEU B  66    CG   CD1  CD2                                       
REMARK 470     GLU B  67    CG   CD   OE1  OE2                                  
REMARK 470     ASP B  68    CG   OD1  OD2                                       
REMARK 470     VAL B  70    CG1  CG2                                            
REMARK 470     LYS B  71    CG   CD   CE   NZ                                   
REMARK 470     GLN B  75    CG   CD   OE1  NE2                                  
REMARK 470     ARG B  77    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B  80    CG1  CG2                                            
REMARK 470     ILE B  81    CG1  CG2  CD1                                       
REMARK 470     GLU B  85    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  88    CG   CD   CE   NZ                                   
REMARK 470     PHE B  91    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE B  92    CG1  CG2  CD1                                       
REMARK 470     PHE B  96    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN B  97    CG   OD1  ND2                                       
REMARK 470     ASN B  98    CG   OD1  ND2                                       
REMARK 470     TRP B  99    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B  99    CZ3  CH2                                            
REMARK 470     LYS B 102    CG   CD   CE   NZ                                   
REMARK 470     LYS B 107    CG   CD   CE   NZ                                   
REMARK 470     ASN B 110    CG   OD1  ND2                                       
REMARK 470     VAL B 113    CG1  CG2                                            
REMARK 470     LEU B 118    CG   CD1  CD2                                       
REMARK 470     GLU B 120    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 122    CG   CD   OE1  OE2                                  
REMARK 470     HIS B 123    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN B 124    CG   CD   OE1  NE2                                  
REMARK 470     TYR B 125    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS B 126    CG   CD   CE   NZ                                   
REMARK 470     PHE B 128    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN B 132    OE1  NE2                                            
REMARK 470     TRP B 133    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B 133    CZ3  CH2                                            
REMARK 470     VAL B 141    CG1  CG2                                            
REMARK 470     VAL B 142    CG1  CG2                                            
REMARK 470     THR B 143    OG1  CG2                                            
REMARK 470     SER B 144    OG                                                  
REMARK 470     GLN B 145    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 146    CG   CD1  CD2                                       
REMARK 470     THR B 148    OG1  CG2                                            
REMARK 470     ILE B 149    CG1  CG2  CD1                                       
REMARK 470     ASN B 151    CG   OD1  ND2                                       
REMARK 470     LEU B 152    CG   CD1  CD2                                       
REMARK 470     ILE B 153    CG1  CG2  CD1                                       
REMARK 470     VAL B 155    CG1  CG2                                            
REMARK 470     LYS B 156    CG   CD   CE   NZ                                   
REMARK 470     LYS B 157    CG   CD   CE   NZ                                   
REMARK 470     PHE B 160    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE B 163    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP B 164    CG   OD1  OD2                                       
REMARK 470     LEU B 166    CG   CD1  CD2                                       
REMARK 470     LEU B 168    CG   CD1  CD2                                       
REMARK 470     ASP B 169    CG   OD1  OD2                                       
REMARK 470     MET B 171    CG   SD   CE                                        
REMARK 470     GLN B 191    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 192    CG   CD   OE1  OE2                                  
REMARK 470     MET B 193    CG   SD   CE                                        
REMARK 470     TYR B 194    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     PHE B 196    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG B 197    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 199    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 200    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 213    CG   CD1  CD2                                       
REMARK 470     LYS B 219    CG   CD   CE   NZ                                   
REMARK 470     GLU B 232    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 241    CG   CD1  CD2                                       
REMARK 470     LYS B 247    CE   NZ                                             
REMARK 470     ARG B 258    NE   CZ   NH1  NH2                                  
REMARK 470     TYR B 259    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS B 260    CG   CD   CE   NZ                                   
REMARK 470     LYS B 261    CG   CD   CE   NZ                                   
REMARK 470     LYS B 262    CG   CD   CE   NZ                                   
REMARK 470     LYS B 270    CG   CD   CE   NZ                                   
REMARK 470     ILE B 272    CG1  CG2  CD1                                       
REMARK 470     ASN C  25    CG   OD1  ND2                                       
REMARK 470     ASN C  26    CG   OD1  ND2                                       
REMARK 470     TYR C  29    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     PHE C  32    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     MET C  33    CG   SD   CE                                        
REMARK 470     LYS C  34    CG   CD   CE   NZ                                   
REMARK 470     HIS C  36    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG C  37    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C  40    CG   OD1  OD2                                       
REMARK 470     LYS C  47    CG   CD   CE   NZ                                   
REMARK 470     GLN C  56    CG   CD   OE1  NE2                                  
REMARK 470     LYS C  58    CG   CD   CE   NZ                                   
REMARK 470     LYS C  59    CG   CD   CE   NZ                                   
REMARK 470     LYS C  78    CG   CD   CE   NZ                                   
REMARK 470     LYS C  79    CG   CD   CE   NZ                                   
REMARK 470     HIS C  96    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG C  97    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 100    CG   CD   CE   NZ                                   
REMARK 470     GLN C 105    CD   OE1  NE2                                       
REMARK 470     GLU C 111    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 113    CG   CD   CE   NZ                                   
REMARK 470     ILE C 114    CG1  CG2  CD1                                       
REMARK 470     GLU C 115    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 118    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 119    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 122    CG   CD1  CD2                                       
REMARK 470     PHE C 139    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU C 145    CG   CD1  CD2                                       
REMARK 470     LYS C 149    CG   CD   CE   NZ                                   
REMARK 470     ARG C 152    CZ   NH1  NH2                                       
REMARK 470     ASP C 157    CG   OD1  OD2                                       
REMARK 470     GLU C 159    CG   CD   OE1  OE2                                  
REMARK 470     SER C 160    OG                                                  
REMARK 470     ASN C 162    CG   OD1  ND2                                       
REMARK 470     LYS C 170    CG   CD   CE   NZ                                   
REMARK 470     LYS C 174    CG   CD   CE   NZ                                   
REMARK 470     LYS C 177    CG   CD   CE   NZ                                   
REMARK 470     PHE C 179    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE C 180    CG1  CG2  CD1                                       
REMARK 470     GLU C 182    CG   CD   OE1  OE2                                  
REMARK 470     PHE C 183    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS C 185    CG   CD   CE   NZ                                   
REMARK 470     GLU C 187    CG   CD   OE1  OE2                                  
REMARK 470     MET C 189    CG   SD   CE                                        
REMARK 470     LYS C 191    CG   CD   CE   NZ                                   
REMARK 470     LEU C 193    CG   CD1  CD2                                       
REMARK 470     GLU C 194    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 195    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 196    CG   CD1  CD2                                       
REMARK 470     GLN C 197    CG   CD   OE1  NE2                                  
REMARK 470     ILE C 198    CG1  CG2  CD1                                       
REMARK 470     TYR C 201    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     MET C 206    CG   SD   CE                                        
REMARK 470     SER C 226    OG                                                  
REMARK 470     LYS C 234    CG   CD   CE   NZ                                   
REMARK 470     ARG C 236    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL C 237    CG1  CG2                                            
REMARK 470     GLU C 252    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 253    CG   CD   CE   NZ                                   
REMARK 470     LYS C 264    CG   CD   CE   NZ                                   
REMARK 470     HIS C 271    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU C 274    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 277    CG   CD1  CD2                                       
REMARK 470     LYS C 278    CE   NZ                                             
REMARK 470     GLU C 283    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 286    CG   CD   OE1  OE2                                  
REMARK 470     ILE C 288    CG1  CG2  CD1                                       
REMARK 470     ASN C 290    CG   OD1  ND2                                       
REMARK 470     ARG C 291    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU C 292    CG   CD1  CD2                                       
REMARK 470     GLU C 294    CG   CD   OE1  OE2                                  
REMARK 470     VAL C 297    CG1  CG2                                            
REMARK 470     ARG C 299    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C 304    CG   OD1  OD2                                       
REMARK 470     GLU C 305    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 307    CG   OD1  OD2                                       
REMARK 470     VAL C 309    CG1  CG2                                            
REMARK 470     LYS C 310    CG   CD   CE   NZ                                   
REMARK 470     ILE C 312    CG1  CG2  CD1                                       
REMARK 470     GLN C 320    CG   CD   OE1  NE2                                  
REMARK 470     LEU C 324    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    LYS B   260     OH   TYR C    39              1.85            
REMARK 500   O    ASN A   309     CD2  TYR A   312              2.11            
REMARK 500   O    ASN A   309     CE2  TYR A   312              2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  38      -61.69    -94.73                                   
REMARK 500    ARG A  72       72.31   -152.95                                   
REMARK 500    ASP A 139       53.88   -104.66                                   
REMARK 500    ASP A 148     -169.82   -114.01                                   
REMARK 500    MET A 151       77.62     56.99                                   
REMARK 500    ASP A 157       73.12     60.25                                   
REMARK 500    TYR A 179       -7.49     66.63                                   
REMARK 500    LEU A 249       70.91   -107.42                                   
REMARK 500    CYS A 302      -59.23   -131.49                                   
REMARK 500    GLU A 306        3.08     83.25                                   
REMARK 500    ASP A 315        3.24     81.21                                   
REMARK 500    TRP A 431     -165.79   -129.64                                   
REMARK 500    ASP A 462     -167.73   -122.56                                   
REMARK 500    LYS B 156      -52.85   -120.03                                   
REMARK 500    ASN B 239        6.74     81.32                                   
REMARK 500    LYS C  34      -52.32     70.11                                   
REMARK 500    LYS C 100      -60.13    -96.56                                   
REMARK 500    GLU C 274       41.18    -95.90                                   
REMARK 500    GLU C 305      -59.23     70.45                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6BIU   RELATED DB: PDB                                   
REMARK 900 6BIU HAS A DIFFERENT AMPK BETA-SUBUNIT ISOFORM (1).                  
DBREF  6B2E A    2   553  UNP    P54646   AAPK2_HUMAN      2    552             
DBREF  6B2E B    1   272  UNP    O43741   AAKB2_HUMAN      1    272             
DBREF  6B2E C    2   331  UNP    P54619   AAKG1_HUMAN      2    331             
SEQADV 6B2E MET A  -12  UNP  P54646              INITIATING METHIONINE          
SEQADV 6B2E GLY A  -11  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E SER A  -10  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E SER A   -9  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E HIS A   -8  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E HIS A   -7  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E HIS A   -6  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E HIS A   -5  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E HIS A   -4  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E HIS A   -3  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E SER A   -2  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E GLN A   -1  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E ASP A    0  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E PRO A    1  UNP  P54646              EXPRESSION TAG                 
SEQADV 6B2E GLY A  271  UNP  P54646    ASP   271 CONFLICT                       
SEQADV 6B2E MET C   -4  UNP  P54619              INITIATING METHIONINE          
SEQADV 6B2E ALA C   -3  UNP  P54619              EXPRESSION TAG                 
SEQADV 6B2E ASP C   -2  UNP  P54619              EXPRESSION TAG                 
SEQADV 6B2E LEU C   -1  UNP  P54619              EXPRESSION TAG                 
SEQADV 6B2E ASN C    0  UNP  P54619              EXPRESSION TAG                 
SEQADV 6B2E TRP C    1  UNP  P54619              EXPRESSION TAG                 
SEQRES   1 A  565  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 A  565  PRO ALA GLU LYS GLN LYS HIS ASP GLY ARG VAL LYS ILE          
SEQRES   3 A  565  GLY HIS TYR VAL LEU GLY ASP THR LEU GLY VAL GLY THR          
SEQRES   4 A  565  PHE GLY LYS VAL LYS ILE GLY GLU HIS GLN LEU THR GLY          
SEQRES   5 A  565  HIS LYS VAL ALA VAL LYS ILE LEU ASN ARG GLN LYS ILE          
SEQRES   6 A  565  ARG SER LEU ASP VAL VAL GLY LYS ILE LYS ARG GLU ILE          
SEQRES   7 A  565  GLN ASN LEU LYS LEU PHE ARG HIS PRO HIS ILE ILE LYS          
SEQRES   8 A  565  LEU TYR GLN VAL ILE SER THR PRO THR ASP PHE PHE MET          
SEQRES   9 A  565  VAL MET GLU TYR VAL SER GLY GLY GLU LEU PHE ASP TYR          
SEQRES  10 A  565  ILE CYS LYS HIS GLY ARG VAL GLU GLU MET GLU ALA ARG          
SEQRES  11 A  565  ARG LEU PHE GLN GLN ILE LEU SER ALA VAL ASP TYR CYS          
SEQRES  12 A  565  HIS ARG HIS MET VAL VAL HIS ARG ASP LEU LYS PRO GLU          
SEQRES  13 A  565  ASN VAL LEU LEU ASP ALA HIS MET ASN ALA LYS ILE ALA          
SEQRES  14 A  565  ASP PHE GLY LEU SER ASN MET MET SER ASP GLY GLU PHE          
SEQRES  15 A  565  LEU ARG TPO SER CYS GLY SER PRO ASN TYR ALA ALA PRO          
SEQRES  16 A  565  GLU VAL ILE SER GLY ARG LEU TYR ALA GLY PRO GLU VAL          
SEQRES  17 A  565  ASP ILE TRP SER CYS GLY VAL ILE LEU TYR ALA LEU LEU          
SEQRES  18 A  565  CYS GLY THR LEU PRO PHE ASP ASP GLU HIS VAL PRO THR          
SEQRES  19 A  565  LEU PHE LYS LYS ILE ARG GLY GLY VAL PHE TYR ILE PRO          
SEQRES  20 A  565  GLU TYR LEU ASN ARG SER VAL ALA THR LEU LEU MET HIS          
SEQRES  21 A  565  MET LEU GLN VAL ASP PRO LEU LYS ARG ALA THR ILE LYS          
SEQRES  22 A  565  ASP ILE ARG GLU HIS GLU TRP PHE LYS GLN GLY LEU PRO          
SEQRES  23 A  565  SER TYR LEU PHE PRO GLU ASP PRO SER TYR ASP ALA ASN          
SEQRES  24 A  565  VAL ILE ASP ASP GLU ALA VAL LYS GLU VAL CYS GLU LYS          
SEQRES  25 A  565  PHE GLU CYS THR GLU SER GLU VAL MET ASN SER LEU TYR          
SEQRES  26 A  565  SER GLY ASP PRO GLN ASP GLN LEU ALA VAL ALA TYR HIS          
SEQRES  27 A  565  LEU ILE ILE ASP ASN ARG ARG ILE MET ASN GLN ALA SER          
SEQRES  28 A  565  GLU PHE TYR LEU ALA SER SER PRO PRO SER GLY SER PHE          
SEQRES  29 A  565  MET ASP ASP SER ALA MET HIS ILE PRO PRO GLY LEU LYS          
SEQRES  30 A  565  PRO HIS PRO GLU ARG MET PRO PRO LEU ILE ALA ASP SER          
SEQRES  31 A  565  PRO LYS ALA ARG CYS PRO LEU ASP ALA LEU ASN THR THR          
SEQRES  32 A  565  LYS PRO LYS SER LEU ALA VAL LYS LYS ALA LYS TRP HIS          
SEQRES  33 A  565  LEU GLY ILE ARG SER GLN SER LYS PRO TYR ASP ILE MET          
SEQRES  34 A  565  ALA GLU VAL TYR ARG ALA MET LYS GLN LEU ASP PHE GLU          
SEQRES  35 A  565  TRP LYS VAL VAL ASN ALA TYR HIS LEU ARG VAL ARG ARG          
SEQRES  36 A  565  LYS ASN PRO VAL THR GLY ASN TYR VAL LYS MET SER LEU          
SEQRES  37 A  565  GLN LEU TYR LEU VAL ASP ASN ARG SER TYR LEU LEU ASP          
SEQRES  38 A  565  PHE LYS SER ILE ASP ASP GLU VAL VAL GLU GLN ARG SER          
SEQRES  39 A  565  GLY SER SER THR PRO GLN ARG SER CYS SER ALA ALA GLY          
SEQRES  40 A  565  LEU HIS ARG PRO ARG SER SER PHE ASP SER THR THR ALA          
SEQRES  41 A  565  GLU SER HIS SER LEU SER GLY SER LEU THR GLY SER LEU          
SEQRES  42 A  565  THR GLY SER THR LEU SER SER VAL SER PRO ARG LEU GLY          
SEQRES  43 A  565  SER HIS THR MET ASP PHE PHE GLU MET CYS ALA SER LEU          
SEQRES  44 A  565  ILE THR THR LEU ALA ARG                                      
SEQRES   1 B  272  MET GLY ASN THR THR SER ASP ARG VAL SER GLY GLU ARG          
SEQRES   2 B  272  HIS GLY ALA LYS ALA ALA ARG SER GLU GLY ALA GLY GLY          
SEQRES   3 B  272  HIS ALA PRO GLY LYS GLU HIS LYS ILE MET VAL GLY SER          
SEQRES   4 B  272  THR ASP ASP PRO SER VAL PHE SER LEU PRO ASP SER LYS          
SEQRES   5 B  272  LEU PRO GLY ASP LYS GLU PHE VAL SER TRP GLN GLN ASP          
SEQRES   6 B  272  LEU GLU ASP SER VAL LYS PRO THR GLN GLN ALA ARG PRO          
SEQRES   7 B  272  THR VAL ILE ARG TRP SER GLU GLY GLY LYS GLU VAL PHE          
SEQRES   8 B  272  ILE SER GLY SER PHE ASN ASN TRP SER THR LYS ILE PRO          
SEQRES   9 B  272  LEU ILE LYS SEP HIS ASN ASP PHE VAL ALA ILE LEU ASP          
SEQRES  10 B  272  LEU PRO GLU GLY GLU HIS GLN TYR LYS PHE PHE VAL ASP          
SEQRES  11 B  272  GLY GLN TRP VAL HIS ASP PRO SER GLU PRO VAL VAL THR          
SEQRES  12 B  272  SER GLN LEU GLY THR ILE ASN ASN LEU ILE HIS VAL LYS          
SEQRES  13 B  272  LYS SER ASP PHE GLU VAL PHE ASP ALA LEU LYS LEU ASP          
SEQRES  14 B  272  SER MET GLU SER SER GLU THR SER CYS ARG ASP LEU SER          
SEQRES  15 B  272  SER SER PRO PRO GLY PRO TYR GLY GLN GLU MET TYR ALA          
SEQRES  16 B  272  PHE ARG SER GLU GLU ARG PHE LYS SER PRO PRO ILE LEU          
SEQRES  17 B  272  PRO PRO HIS LEU LEU GLN VAL ILE LEU ASN LYS ASP THR          
SEQRES  18 B  272  ASN ILE SER CYS ASP PRO ALA LEU LEU PRO GLU PRO ASN          
SEQRES  19 B  272  HIS VAL MET LEU ASN HIS LEU TYR ALA LEU SER ILE LYS          
SEQRES  20 B  272  ASP SER VAL MET VAL LEU SER ALA THR HIS ARG TYR LYS          
SEQRES  21 B  272  LYS LYS TYR VAL THR THR LEU LEU TYR LYS PRO ILE              
SEQRES   1 C  336  MET ALA ASP LEU ASN TRP GLU THR VAL ILE SER SER ASP          
SEQRES   2 C  336  SER SER PRO ALA VAL GLU ASN GLU HIS PRO GLN GLU THR          
SEQRES   3 C  336  PRO GLU SER ASN ASN SER VAL TYR THR SER PHE MET LYS          
SEQRES   4 C  336  SER HIS ARG CYS TYR ASP LEU ILE PRO THR SER SER LYS          
SEQRES   5 C  336  LEU VAL VAL PHE ASP THR SER LEU GLN VAL LYS LYS ALA          
SEQRES   6 C  336  PHE PHE ALA LEU VAL THR ASN GLY VAL ARG ALA ALA PRO          
SEQRES   7 C  336  LEU TRP ASP SER LYS LYS GLN SER PHE VAL GLY MET LEU          
SEQRES   8 C  336  THR ILE THR ASP PHE ILE ASN ILE LEU HIS ARG TYR TYR          
SEQRES   9 C  336  LYS SER ALA LEU VAL GLN ILE TYR GLU LEU GLU GLU HIS          
SEQRES  10 C  336  LYS ILE GLU THR TRP ARG GLU VAL TYR LEU GLN ASP SER          
SEQRES  11 C  336  PHE LYS PRO LEU VAL CYS ILE SER PRO ASN ALA SER LEU          
SEQRES  12 C  336  PHE ASP ALA VAL SER SER LEU ILE ARG ASN LYS ILE HIS          
SEQRES  13 C  336  ARG LEU PRO VAL ILE ASP PRO GLU SER GLY ASN THR LEU          
SEQRES  14 C  336  TYR ILE LEU THR HIS LYS ARG ILE LEU LYS PHE LEU LYS          
SEQRES  15 C  336  LEU PHE ILE THR GLU PHE PRO LYS PRO GLU PHE MET SER          
SEQRES  16 C  336  LYS SER LEU GLU GLU LEU GLN ILE GLY THR TYR ALA ASN          
SEQRES  17 C  336  ILE ALA MET VAL ARG THR THR THR PRO VAL TYR VAL ALA          
SEQRES  18 C  336  LEU GLY ILE PHE VAL GLN HIS ARG VAL SER ALA LEU PRO          
SEQRES  19 C  336  VAL VAL ASP GLU LYS GLY ARG VAL VAL ASP ILE TYR SER          
SEQRES  20 C  336  LYS PHE ASP VAL ILE ASN LEU ALA ALA GLU LYS THR TYR          
SEQRES  21 C  336  ASN ASN LEU ASP VAL SER VAL THR LYS ALA LEU GLN HIS          
SEQRES  22 C  336  ARG SER HIS TYR PHE GLU GLY VAL LEU LYS CYS TYR LEU          
SEQRES  23 C  336  HIS GLU THR LEU GLU THR ILE ILE ASN ARG LEU VAL GLU          
SEQRES  24 C  336  ALA GLU VAL HIS ARG LEU VAL VAL VAL ASP GLU ASN ASP          
SEQRES  25 C  336  VAL VAL LYS GLY ILE VAL SER LEU SER ASP ILE LEU GLN          
SEQRES  26 C  336  ALA LEU VAL LEU THR GLY GLY GLU LYS LYS PRO                  
MODRES 6B2E TPO A  172  THR  MODIFIED RESIDUE                                   
MODRES 6B2E SEP B  108  SER  MODIFIED RESIDUE                                   
HET    TPO  A 172      11                                                       
HET    SEP  B 108      10                                                       
HET    GLC  D   1      11                                                       
HET    GLC  D   2      11                                                       
HET    GLC  D   3      11                                                       
HET    GLC  D   4      11                                                       
HET    GLC  D   5      11                                                       
HET    GLC  D   6      11                                                       
HET    GLC  D   7      11                                                       
HET    STU  A 601      35                                                       
HET    CG7  A 602      34                                                       
HET    AMP  C 400      23                                                       
HET    AMP  C 401      23                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     GLC ALPHA-D-GLUCOPYRANOSE                                            
HETNAM     STU STAUROSPORINE                                                    
HETNAM     CG7 5-{[6-CHLORO-5-(2'-HYDROXY[1,1'-BIPHENYL]-4-YL)-1H-              
HETNAM   2 CG7  IMIDAZO[4,5-B]PYRIDIN-2-YL]OXY}-2-METHYLBENZOIC ACID            
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE                              
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   2  SEP    C3 H8 N O6 P                                                 
FORMUL   4  GLC    7(C6 H12 O6)                                                 
FORMUL   5  STU    C28 H26 N4 O3                                                
FORMUL   6  CG7    C26 H18 CL N3 O4                                             
FORMUL   7  AMP    2(C10 H14 N5 O7 P)                                           
HELIX    1 AA1 ARG A   49  SER A   54  1                                   6    
HELIX    2 AA2 VAL A   57  PHE A   71  1                                  15    
HELIX    3 AA3 LEU A  101  HIS A  108  1                                   8    
HELIX    4 AA4 GLU A  112  HIS A  133  1                                  22    
HELIX    5 AA5 ASP A  157  SER A  161  5                                   5    
HELIX    6 AA6 ALA A  181  GLY A  187  1                                   7    
HELIX    7 AA7 ALA A  191  GLY A  210  1                                  20    
HELIX    8 AA8 HIS A  218  GLY A  229  1                                  12    
HELIX    9 AA9 ASN A  238  LEU A  249  1                                  12    
HELIX   10 AB1 THR A  258  GLU A  264  1                                   7    
HELIX   11 AB2 HIS A  265  GLN A  270  1                                   6    
HELIX   12 AB3 GLU A  279  TYR A  283  5                                   5    
HELIX   13 AB4 GLU A  291  CYS A  302  1                                  12    
HELIX   14 AB5 MET A  308  ASP A  315  1                                   8    
HELIX   15 AB6 TYR A  325  ALA A  338  1                                  14    
HELIX   16 AB7 ALA A  338  LEU A  343  1                                   6    
HELIX   17 AB8 LYS A  412  LEU A  427  1                                  16    
HELIX   18 AB9 SER A  535  LEU A  551  1                                  17    
HELIX   19 AC1 VAL B   60  VAL B   70  1                                  11    
HELIX   20 AC2 ASP B  159  SER B  170  1                                  12    
HELIX   21 AC3 VAL C   28  MET C   33  1                                   6    
HELIX   22 AC4 ARG C   37  ILE C   42  5                                   6    
HELIX   23 AC5 GLN C   56  GLY C   68  1                                  13    
HELIX   24 AC6 THR C   87  TYR C   99  1                                  13    
HELIX   25 AC7 ILE C  106  HIS C  112  1                                   7    
HELIX   26 AC8 LYS C  113  TYR C  121  1                                   9    
HELIX   27 AC9 SER C  137  ASN C  148  1                                  12    
HELIX   28 AD1 THR C  168  ILE C  180  1                                  13    
HELIX   29 AD2 THR C  181  PHE C  183  5                                   3    
HELIX   30 AD3 PRO C  186  LYS C  191  5                                   6    
HELIX   31 AD4 PRO C  212  HIS C  223  1                                  12    
HELIX   32 AD5 PHE C  244  VAL C  246  5                                   3    
HELIX   33 AD6 ILE C  247  GLU C  252  1                                   6    
HELIX   34 AD7 SER C  261  LEU C  266  1                                   6    
HELIX   35 AD8 THR C  284  GLU C  296  1                                  13    
HELIX   36 AD9 LEU C  315  LEU C  324  1                                  10    
SHEET    1 AA1 6 LYS A  12  ILE A  13  0                                        
SHEET    2 AA1 6 TYR A  16  VAL A  24 -1  O  TYR A  16   N  ILE A  13           
SHEET    3 AA1 6 LYS A  29  HIS A  35 -1  O  GLU A  34   N  VAL A  17           
SHEET    4 AA1 6 LYS A  41  ASN A  48 -1  O  VAL A  42   N  GLY A  33           
SHEET    5 AA1 6 ASP A  88  GLU A  94 -1  O  PHE A  89   N  LEU A  47           
SHEET    6 AA1 6 LEU A  79  SER A  84 -1  N  ILE A  83   O  PHE A  90           
SHEET    1 AA2 3 GLY A  99  GLU A 100  0                                        
SHEET    2 AA2 3 VAL A 145  LEU A 147 -1  O  LEU A 147   N  GLY A  99           
SHEET    3 AA2 3 LYS A 154  ILE A 155 -1  O  LYS A 154   N  LEU A 146           
SHEET    1 AA3 2 VAL A 135  VAL A 136  0                                        
SHEET    2 AA3 2 ASN A 162  MET A 163 -1  O  ASN A 162   N  VAL A 136           
SHEET    1 AA4 7 HIS A 404  LEU A 405  0                                        
SHEET    2 AA4 7 TYR B 242  LEU B 244 -1  O  ALA B 243   N  HIS A 404           
SHEET    3 AA4 7 VAL B 250  TYR B 259 -1  O  SER B 254   N  TYR B 242           
SHEET    4 AA4 7 LYS B 262  PRO B 271 -1  O  VAL B 264   N  HIS B 257           
SHEET    5 AA4 7 SER C  45  ASP C  52  1  O  LEU C  48   N  LEU B 267           
SHEET    6 AA4 7 ALA C  72  ASP C  76  1  O  TRP C  75   N  PHE C  51           
SHEET    7 AA4 7 SER C  81  LEU C  86 -1  O  LEU C  86   N  ALA C  72           
SHEET    1 AA5 4 ILE A 407  SER A 409  0                                        
SHEET    2 AA5 4 TYR A 466  SER A 472 -1  O  TYR A 466   N  SER A 409           
SHEET    3 AA5 4 TYR A 451  TYR A 459 -1  N  TYR A 459   O  LEU A 467           
SHEET    4 AA5 4 HIS A 438  LYS A 444 -1  N  LEU A 439   O  LEU A 456           
SHEET    1 AA6 3 ARG B  82  SER B  84  0                                        
SHEET    2 AA6 3 ASP B 111  VAL B 113 -1  O  PHE B 112   N  TRP B  83           
SHEET    3 AA6 3 ILE B 106  LYS B 107 -1  N  ILE B 106   O  VAL B 113           
SHEET    1 AA7 5 ILE B 103  PRO B 104  0                                        
SHEET    2 AA7 5 VAL B  90  SER B  93 -1  N  ILE B  92   O  ILE B 103           
SHEET    3 AA7 5 GLY B 121  VAL B 129 -1  O  PHE B 128   N  PHE B  91           
SHEET    4 AA7 5 ILE B 149  VAL B 155 -1  O  ILE B 153   N  HIS B 123           
SHEET    5 AA7 5 VAL B 141  THR B 143 -1  N  VAL B 142   O  ASN B 150           
SHEET    1 AA8 2 LEU C 153  ILE C 156  0                                        
SHEET    2 AA8 2 THR C 163  LEU C 167 -1  O  TYR C 165   N  VAL C 155           
SHEET    1 AA9 2 ALA C 227  VAL C 231  0                                        
SHEET    2 AA9 2 VAL C 237  SER C 242 -1  O  TYR C 241   N  LEU C 228           
SHEET    1 AB1 3 LYS C 278  CYS C 279  0                                        
SHEET    2 AB1 3 ARG C 299  VAL C 302  1  O  VAL C 301   N  CYS C 279           
SHEET    3 AB1 3 VAL C 313  SER C 314 -1  O  VAL C 313   N  LEU C 300           
LINK         C   ARG A 171                 N   TPO A 172     1555   1555  1.33  
LINK         C   TPO A 172                 N   SER A 173     1555   1555  1.33  
LINK         C   LYS B 107                 N   SEP B 108     1555   1555  1.33  
LINK         C   SEP B 108                 N   HIS B 109     1555   1555  1.33  
LINK         O4  GLC D   1                 C1  GLC D   2     1555   1555  1.43  
LINK         C1  GLC D   1                 O4  GLC D   7     1555   1555  1.43  
LINK         O4  GLC D   2                 C1  GLC D   3     1555   1555  1.43  
LINK         O4  GLC D   3                 C1  GLC D   4     1555   1555  1.43  
LINK         O4  GLC D   4                 C1  GLC D   5     1555   1555  1.43  
LINK         O4  GLC D   5                 C1  GLC D   6     1555   1555  1.43  
LINK         O4  GLC D   6                 C1  GLC D   7     1555   1555  1.43  
CRYST1  113.936  118.848  138.096  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008777  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008414  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007241        0.00000                         
ATOM      1  N   GLY A   9     -20.735 -48.655 -19.614  1.00122.33           N  
ANISOU    1  N   GLY A   9    13740  16887  15853    495   -141  -3881       N  
ATOM      2  CA  GLY A   9     -21.670 -47.649 -19.131  1.00121.72           C  
ANISOU    2  CA  GLY A   9    13494  16969  15786    541   -322  -3856       C  
ATOM      3  C   GLY A   9     -21.813 -47.653 -17.624  1.00123.82           C  
ANISOU    3  C   GLY A   9    13647  17105  16295    458   -167  -3698       C  
ATOM      4  O   GLY A   9     -22.750 -48.254 -17.091  1.00124.66           O  
ANISOU    4  O   GLY A   9    13580  17163  16621    294   -114  -3878       O  
ATOM      5  N   ARG A  10     -20.890 -46.959 -16.931  1.00117.57           N  
ANISOU    5  N   ARG A  10    12957  16255  15460    566    -86  -3375       N  
ATOM      6  CA  ARG A  10     -20.831 -46.850 -15.468  1.00115.48           C  
ANISOU    6  CA  ARG A  10    12636  15862  15380    524     57  -3180       C  
ATOM      7  C   ARG A  10     -21.994 -46.049 -14.842  1.00118.86           C  
ANISOU    7  C   ARG A  10    12860  16419  15883    507    -70  -3207       C  
ATOM      8  O   ARG A  10     -22.853 -45.532 -15.561  1.00119.77           O  
ANISOU    8  O   ARG A  10    12864  16736  15908    551   -295  -3382       O  
ATOM      9  CB  ARG A  10     -19.469 -46.279 -15.036  1.00113.39           C  
ANISOU    9  CB  ARG A  10    12525  15532  15025    662    146  -2863       C  
ATOM     10  N   VAL A  11     -22.010 -45.970 -13.490  1.00113.68           N  
ANISOU   10  N   VAL A  11    12164  15641  15389    456     72  -3044       N  
ATOM     11  CA  VAL A  11     -22.999 -45.272 -12.655  1.00113.01           C  
ANISOU   11  CA  VAL A  11    11895  15634  15410    424     15  -3042       C  
ATOM     12  C   VAL A  11     -23.041 -43.771 -12.996  1.00115.42           C  
ANISOU   12  C   VAL A  11    12179  16157  15519    618   -219  -2923       C  
ATOM     13  O   VAL A  11     -22.005 -43.104 -12.951  1.00113.00           O  
ANISOU   13  O   VAL A  11    12027  15840  15067    751   -208  -2671       O  
ATOM     14  CB  VAL A  11     -22.721 -45.549 -11.147  1.00115.53           C  
ANISOU   14  CB  VAL A  11    12258  15740  15898    347    251  -2849       C  
ATOM     15  CG1 VAL A  11     -23.478 -44.589 -10.235  1.00114.55           C  
ANISOU   15  CG1 VAL A  11    11984  15700  15839    353    201  -2778       C  
ATOM     16  CG2 VAL A  11     -23.042 -46.995 -10.785  1.00117.09           C  
ANISOU   16  CG2 VAL A  11    12475  15715  16297    138    480  -3014       C  
ATOM     17  N   LYS A  12     -24.238 -43.256 -13.350  1.00113.33           N  
ANISOU   17  N   LYS A  12    11724  16082  15254    635   -425  -3122       N  
ATOM     18  CA  LYS A  12     -24.442 -41.857 -13.735  1.00112.65           C  
ANISOU   18  CA  LYS A  12    11634  16194  14975    836   -667  -3040       C  
ATOM     19  C   LYS A  12     -25.545 -41.170 -12.920  1.00116.42           C  
ANISOU   19  C   LYS A  12    11881  16763  15590    829   -744  -3088       C  
ATOM     20  O   LYS A  12     -26.629 -41.732 -12.746  1.00117.88           O  
ANISOU   20  O   LYS A  12    11837  16977  15973    689   -743  -3359       O  
ATOM     21  CB  LYS A  12     -24.735 -41.759 -15.243  1.00117.38           C  
ANISOU   21  CB  LYS A  12    12272  16964  15361    948   -912  -3245       C  
ATOM     22  CG  LYS A  12     -24.451 -40.389 -15.849  1.00131.67           C  
ANISOU   22  CG  LYS A  12    14238  18911  16880   1192  -1115  -3085       C  
ATOM     23  CD  LYS A  12     -24.690 -40.382 -17.351  1.00144.09           C  
ANISOU   23  CD  LYS A  12    15913  20626  18207   1313  -1344  -3280       C  
ATOM     24  N   ILE A  13     -25.266 -39.943 -12.502  1.00110.97           N  
ANISOU   24  N   ILE A  13    11249  16112  14802    972   -794  -2839       N  
ATOM     25  CA  ILE A  13     -26.287 -39.030 -12.034  1.00110.60           C  
ANISOU   25  CA  ILE A  13    11015  16153  14855   1003   -870  -2841       C  
ATOM     26  C   ILE A  13     -26.196 -37.712 -12.788  1.00114.44           C  
ANISOU   26  C   ILE A  13    11583  16811  15089   1258  -1132  -2756       C  
ATOM     27  O   ILE A  13     -25.134 -37.099 -12.847  1.00112.02           O  
ANISOU   27  O   ILE A  13    11462  16459  14643   1365  -1091  -2470       O  
ATOM     28  CB  ILE A  13     -26.129 -38.741 -10.537  1.00111.44           C  
ANISOU   28  CB  ILE A  13    11134  16093  15116    907   -625  -2606       C  
ATOM     29  CG1 ILE A  13     -26.167 -40.037  -9.730  1.00112.22           C  
ANISOU   29  CG1 ILE A  13    11222  15985  15432    673   -353  -2675       C  
ATOM     30  CG2 ILE A  13     -27.218 -37.796 -10.071  1.00112.00           C  
ANISOU   30  CG2 ILE A  13    11024  16253  15278    944   -692  -2602       C  
ATOM     31  CD1 ILE A  13     -27.440 -40.836  -9.897  1.00122.35           C  
ANISOU   31  CD1 ILE A  13    12253  17279  16957    473   -306  -3020       C  
ATOM     32  N   GLY A  14     -27.307 -37.273 -13.368  1.00113.50           N  
ANISOU   32  N   GLY A  14    11339  16876  14908   1357  -1397  -3020       N  
ATOM     33  CA  GLY A  14     -27.405 -35.923 -13.887  1.00114.08           C  
ANISOU   33  CA  GLY A  14    11509  17110  14726   1627  -1681  -2987       C  
ATOM     34  C   GLY A  14     -26.309 -35.516 -14.853  1.00116.77           C  
ANISOU   34  C   GLY A  14    12213  17403  14752   1767  -1680  -2748       C  
ATOM     35  O   GLY A  14     -25.792 -34.407 -14.759  1.00114.45           O  
ANISOU   35  O   GLY A  14    12078  17056  14352   1858  -1622  -2471       O  
ATOM     36  N   HIS A  15     -25.944 -36.409 -15.764  1.00114.56           N  
ANISOU   36  N   HIS A  15    12066  17129  14331   1762  -1715  -2867       N  
ATOM     37  CA  HIS A  15     -24.887 -36.140 -16.734  1.00113.90           C  
ANISOU   37  CA  HIS A  15    12334  16996  13949   1863  -1685  -2700       C  
ATOM     38  C   HIS A  15     -23.525 -36.294 -16.089  1.00114.48           C  
ANISOU   38  C   HIS A  15    12543  16878  14076   1740  -1368  -2432       C  
ATOM     39  O   HIS A  15     -22.505 -35.952 -16.683  1.00113.87           O  
ANISOU   39  O   HIS A  15    12712  16743  13809   1768  -1284  -2342       O  
ATOM     40  CB  HIS A  15     -25.004 -34.735 -17.323  1.00115.52           C  
ANISOU   40  CB  HIS A  15    12760  17295  13839   2133  -1901  -2593       C  
ATOM     41  CG  HIS A  15     -26.368 -34.403 -17.833  1.00121.94           C  
ANISOU   41  CG  HIS A  15    13445  18303  14583   2304  -2250  -2859       C  
ATOM     42  ND1 HIS A  15     -27.459 -35.213 -17.611  1.00126.51           N  
ANISOU   42  ND1 HIS A  15    14093  18985  14991   2381  -2447  -3101       N  
ATOM     43  CD2 HIS A  15     -26.819 -33.352 -18.556  1.00124.45           C  
ANISOU   43  CD2 HIS A  15    13559  18735  14992   2417  -2435  -2934       C  
ATOM     44  CE1 HIS A  15     -28.526 -34.675 -18.174  1.00128.37           C  
ANISOU   44  CE1 HIS A  15    14157  19401  15216   2549  -2763  -3323       C  
ATOM     45  NE2 HIS A  15     -28.164 -33.544 -18.754  1.00127.60           N  
ANISOU   45  NE2 HIS A  15    13884  19316  15280   2578  -2765  -3235       N  
ATOM     46  N   TYR A  16     -23.508 -36.804 -14.866  1.00108.76           N  
ANISOU   46  N   TYR A  16    11657  16059  13605   1611  -1194  -2326       N  
ATOM     47  CA  TYR A  16     -22.252 -36.978 -14.160  1.00106.05           C  
ANISOU   47  CA  TYR A  16    11408  15550  13338   1517   -926  -2099       C  
ATOM     48  C   TYR A  16     -21.992 -38.440 -13.871  1.00109.97           C  
ANISOU   48  C   TYR A  16    11819  15922  14042   1330   -750  -2209       C  
ATOM     49  O   TYR A  16     -22.852 -39.144 -13.355  1.00109.98           O  
ANISOU   49  O   TYR A  16    11617  15902  14266   1207   -721  -2344       O  
ATOM     50  CB  TYR A  16     -22.240 -36.160 -12.871  1.00105.14           C  
ANISOU   50  CB  TYR A  16    11220  15397  13330   1522   -854  -1896       C  
ATOM     51  CG  TYR A  16     -21.677 -34.773 -13.056  1.00105.87           C  
ANISOU   51  CG  TYR A  16    11497  15523  13204   1682   -905  -1690       C  
ATOM     52  CD1 TYR A  16     -20.907 -34.459 -14.163  1.00106.63           C  
ANISOU   52  CD1 TYR A  16    11805  15534  13177   1694   -751  -1510       C  
ATOM     53  CD2 TYR A  16     -21.917 -33.778 -12.129  1.00107.13           C  
ANISOU   53  CD2 TYR A  16    11617  15790  13297   1817  -1089  -1686       C  
ATOM     54  CE1 TYR A  16     -20.391 -33.193 -14.339  1.00106.81           C  
ANISOU   54  CE1 TYR A  16    12010  15567  13008   1812   -758  -1334       C  
ATOM     55  CE2 TYR A  16     -21.406 -32.508 -12.296  1.00107.40           C  
ANISOU   55  CE2 TYR A  16    11855  15827  13127   1960  -1112  -1492       C  
ATOM     56  CZ  TYR A  16     -20.645 -32.221 -13.403  1.00113.43           C  
ANISOU   56  CZ  TYR A  16    12840  16491  13765   1944   -934  -1316       C  
ATOM     57  OH  TYR A  16     -20.134 -30.956 -13.571  1.00113.75           O  
ANISOU   57  OH  TYR A  16    13093  16513  13612   2056   -920  -1140       O  
ATOM     58  N   VAL A  17     -20.797 -38.895 -14.220  1.00106.39           N  
ANISOU   58  N   VAL A  17    11534  15377  13513   1308   -619  -2161       N  
ATOM     59  CA  VAL A  17     -20.441 -40.303 -14.033  1.00106.53           C  
ANISOU   59  CA  VAL A  17    11526  15252  13698   1161   -444  -2248       C  
ATOM     60  C   VAL A  17     -19.581 -40.443 -12.771  1.00108.54           C  
ANISOU   60  C   VAL A  17    11795  15348  14097   1116   -234  -2033       C  
ATOM     61  O   VAL A  17     -18.526 -39.810 -12.671  1.00106.75           O  
ANISOU   61  O   VAL A  17    11688  15100  13770   1198   -172  -1840       O  
ATOM     62  CB  VAL A  17     -19.754 -40.910 -15.293  1.00111.60           C  
ANISOU   62  CB  VAL A  17    12336  15882  14186   1176   -424  -2343       C  
ATOM     63  CG1 VAL A  17     -19.397 -42.381 -15.083  1.00111.81           C  
ANISOU   63  CG1 VAL A  17    12347  15744  14391   1036   -240  -2437       C  
ATOM     64  CG2 VAL A  17     -20.627 -40.748 -16.535  1.00113.77           C  
ANISOU   64  CG2 VAL A  17    12621  16320  14286   1242   -658  -2562       C  
ATOM     65  N   LEU A  18     -20.043 -41.262 -11.808  1.00105.25           N  
ANISOU   65  N   LEU A  18    11264  14817  13911    987   -122  -2080       N  
ATOM     66  CA  LEU A  18     -19.331 -41.512 -10.554  1.00103.52           C  
ANISOU   66  CA  LEU A  18    11081  14434  13819    959     61  -1893       C  
ATOM     67  C   LEU A  18     -18.141 -42.449 -10.772  1.00107.69           C  
ANISOU   67  C   LEU A  18    11748  14818  14349    963    207  -1865       C  
ATOM     68  O   LEU A  18     -18.252 -43.424 -11.518  1.00108.77           O  
ANISOU   68  O   LEU A  18    11913  14912  14503    900    233  -2042       O  
ATOM     69  CB  LEU A  18     -20.280 -42.069  -9.479  1.00103.99           C  
ANISOU   69  CB  LEU A  18    11020  14397  14095    822    149  -1957       C  
ATOM     70  CG  LEU A  18     -21.142 -41.047  -8.735  1.00108.02           C  
ANISOU   70  CG  LEU A  18    11394  15005  14644    831     70  -1907       C  
ATOM     71  CD1 LEU A  18     -22.351 -41.706  -8.119  1.00109.56           C  
ANISOU   71  CD1 LEU A  18    11440  15143  15046    661    147  -2084       C  
ATOM     72  CD2 LEU A  18     -20.349 -40.335  -7.650  1.00108.40           C  
ANISOU   72  CD2 LEU A  18    11514  14994  14679    907    143  -1636       C  
ATOM     73  N   GLY A  19     -17.022 -42.136 -10.119  1.00102.99           N  
ANISOU   73  N   GLY A  19    11229  14157  13744   1045    293  -1663       N  
ATOM     74  CA  GLY A  19     -15.785 -42.902 -10.221  1.00102.97           C  
ANISOU   74  CA  GLY A  19    11338  14031  13755   1086    419  -1632       C  
ATOM     75  C   GLY A  19     -15.159 -43.265  -8.891  1.00106.20           C  
ANISOU   75  C   GLY A  19    11783  14281  14288   1119    537  -1485       C  
ATOM     76  O   GLY A  19     -15.850 -43.738  -7.984  1.00106.01           O  
ANISOU   76  O   GLY A  19    11744  14148  14388   1045    592  -1481       O  
ATOM     77  N   ASP A  20     -13.831 -43.049  -8.782  1.00102.20           N  
ANISOU   77  N   ASP A  20    11330  13759  13742   1235    580  -1379       N  
ATOM     78  CA  ASP A  20     -13.003 -43.337  -7.606  1.00101.55           C  
ANISOU   78  CA  ASP A  20    11290  13548  13747   1321    657  -1249       C  
ATOM     79  C   ASP A  20     -13.470 -42.583  -6.353  1.00104.22           C  
ANISOU   79  C   ASP A  20    11585  13897  14118   1322    626  -1103       C  
ATOM     80  O   ASP A  20     -13.948 -41.453  -6.454  1.00102.82           O  
ANISOU   80  O   ASP A  20    11329  13866  13872   1303    540  -1062       O  
ATOM     81  CB  ASP A  20     -11.525 -43.027  -7.916  1.00103.13           C  
ANISOU   81  CB  ASP A  20    11499  13793  13893   1447    678  -1212       C  
ATOM     82  CG  ASP A  20     -10.533 -43.545  -6.892  1.00113.97           C  
ANISOU   82  CG  ASP A  20    12910  15036  15356   1573    732  -1135       C  
ATOM     83  OD1 ASP A  20     -10.327 -44.777  -6.835  1.00115.87           O  
ANISOU   83  OD1 ASP A  20    13240  15113  15671   1602    801  -1197       O  
ATOM     84  OD2 ASP A  20      -9.928 -42.714  -6.181  1.00119.02           O  
ANISOU   84  OD2 ASP A  20    13498  15738  15986   1657    700  -1023       O  
ATOM     85  N   THR A  21     -13.343 -43.228  -5.179  1.00101.10           N  
ANISOU   85  N   THR A  21    11266  13333  13816   1353    699  -1025       N  
ATOM     86  CA  THR A  21     -13.740 -42.670  -3.884  1.00100.10           C  
ANISOU   86  CA  THR A  21    11133  13184  13716   1356    694   -888       C  
ATOM     87  C   THR A  21     -12.641 -41.751  -3.338  1.00102.85           C  
ANISOU   87  C   THR A  21    11455  13612  14011   1499    640   -752       C  
ATOM     88  O   THR A  21     -11.488 -42.174  -3.219  1.00102.80           O  
ANISOU   88  O   THR A  21    11497  13550  14014   1625    658   -740       O  
ATOM     89  CB  THR A  21     -14.120 -43.805  -2.907  1.00109.33           C  
ANISOU   89  CB  THR A  21    12446  14115  14980   1322    814   -873       C  
ATOM     90  OG1 THR A  21     -15.052 -44.684  -3.539  1.00110.79           O  
ANISOU   90  OG1 THR A  21    12640  14226  15228   1168    884  -1037       O  
ATOM     91  CG2 THR A  21     -14.711 -43.289  -1.597  1.00107.09           C  
ANISOU   91  CG2 THR A  21    12181  13795  14715   1297    834   -748       C  
ATOM     92  N   LEU A  22     -13.005 -40.495  -3.013  1.00 98.26           N  
ANISOU   92  N   LEU A  22    10787  13164  13383   1481    574   -670       N  
ATOM     93  CA  LEU A  22     -12.084 -39.500  -2.452  1.00 97.01           C  
ANISOU   93  CA  LEU A  22    10589  13090  13181   1586    531   -558       C  
ATOM     94  C   LEU A  22     -11.770 -39.817  -0.992  1.00101.28           C  
ANISOU   94  C   LEU A  22    11209  13505  13766   1672    551   -451       C  
ATOM     95  O   LEU A  22     -10.634 -39.638  -0.551  1.00100.77           O  
ANISOU   95  O   LEU A  22    11140  13454  13694   1805    523   -410       O  
ATOM     96  CB  LEU A  22     -12.660 -38.076  -2.569  1.00 95.87           C  
ANISOU   96  CB  LEU A  22    10355  13104  12969   1536    466   -509       C  
ATOM     97  CG  LEU A  22     -12.679 -37.454  -3.963  1.00100.58           C  
ANISOU   97  CG  LEU A  22    10914  13836  13466   1506    427   -583       C  
ATOM     98  CD1 LEU A  22     -13.574 -36.236  -4.003  1.00100.09           C  
ANISOU   98  CD1 LEU A  22    10803  13887  13338   1468    354   -539       C  
ATOM     99  CD2 LEU A  22     -11.282 -37.091  -4.432  1.00102.93           C  
ANISOU   99  CD2 LEU A  22    11208  14185  13713   1580    460   -589       C  
ATOM    100  N   GLY A  23     -12.784 -40.289  -0.274  1.00 98.49           N  
ANISOU  100  N   GLY A  23    10932  13032  13458   1595    604   -423       N  
ATOM    101  CA  GLY A  23     -12.700 -40.659   1.132  1.00 98.82           C  
ANISOU  101  CA  GLY A  23    11110  12923  13514   1662    643   -316       C  
ATOM    102  C   GLY A  23     -14.063 -40.868   1.757  1.00103.52           C  
ANISOU  102  C   GLY A  23    11763  13419  14152   1516    733   -305       C  
ATOM    103  O   GLY A  23     -15.087 -40.804   1.069  1.00103.17           O  
ANISOU  103  O   GLY A  23    11623  13431  14148   1366    752   -406       O  
ATOM    104  N   VAL A  24     -14.078 -41.118   3.072  1.00100.96           N  
ANISOU  104  N   VAL A  24    11597  12946  13816   1564    789   -198       N  
ATOM    105  CA  VAL A  24     -15.305 -41.330   3.837  1.00101.62           C  
ANISOU  105  CA  VAL A  24    11763  12908  13940   1418    917   -186       C  
ATOM    106  C   VAL A  24     -15.318 -40.412   5.071  1.00105.07           C  
ANISOU  106  C   VAL A  24    12229  13376  14320   1468    893    -48       C  
ATOM    107  O   VAL A  24     -14.397 -40.451   5.891  1.00104.78           O  
ANISOU  107  O   VAL A  24    12324  13278  14208   1637    847     58       O  
ATOM    108  CB  VAL A  24     -15.584 -42.837   4.147  1.00107.65           C  
ANISOU  108  CB  VAL A  24    12767  13391  14745   1372   1086   -221       C  
ATOM    109  CG1 VAL A  24     -14.417 -43.515   4.869  1.00108.36           C  
ANISOU  109  CG1 VAL A  24    13099  13313  14759   1592   1072   -116       C  
ATOM    110  CG2 VAL A  24     -16.896 -43.033   4.905  1.00108.45           C  
ANISOU  110  CG2 VAL A  24    12947  13358  14899   1183   1264   -236       C  
ATOM    111  N   GLY A  25     -16.341 -39.564   5.148  1.00101.23           N  
ANISOU  111  N   GLY A  25    11604  12995  13865   1335    906    -66       N  
ATOM    112  CA  GLY A  25     -16.525 -38.625   6.248  1.00100.41           C  
ANISOU  112  CA  GLY A  25    11508  12928  13716   1353    898     46       C  
ATOM    113  C   GLY A  25     -17.278 -39.231   7.415  1.00105.85           C  
ANISOU  113  C   GLY A  25    12400  13402  14415   1268   1078     85       C  
ATOM    114  O   GLY A  25     -17.451 -40.454   7.478  1.00107.14           O  
ANISOU  114  O   GLY A  25    12744  13359  14607   1220   1214     47       O  
ATOM    115  N   THR A  26     -17.735 -38.374   8.349  1.00101.89           N  
ANISOU  115  N   THR A  26    11892  12936  13886   1240   1101    158       N  
ATOM    116  CA  THR A  26     -18.499 -38.786   9.536  1.00103.05           C  
ANISOU  116  CA  THR A  26    12243  12883  14028   1144   1298    198       C  
ATOM    117  C   THR A  26     -19.846 -39.398   9.145  1.00107.86           C  
ANISOU  117  C   THR A  26    12789  13414  14781    903   1486     36       C  
ATOM    118  O   THR A  26     -20.300 -40.348   9.786  1.00109.30           O  
ANISOU  118  O   THR A  26    13202  13352  14976    805   1703     27       O  
ATOM    119  CB  THR A  26     -18.646 -37.629  10.537  1.00110.86           C  
ANISOU  119  CB  THR A  26    13214  13951  14955   1170   1273    297       C  
ATOM    120  OG1 THR A  26     -19.079 -36.450   9.854  1.00108.99           O  
ANISOU  120  OG1 THR A  26    12674  13957  14781   1119   1163    235       O  
ATOM    121  CG2 THR A  26     -17.359 -37.354  11.304  1.00109.28           C  
ANISOU  121  CG2 THR A  26    13168  13748  14606   1397   1142    444       C  
ATOM    122  N   PHE A  27     -20.465 -38.860   8.079  1.00103.41           N  
ANISOU  122  N   PHE A  27    11921  13052  14318    813   1401   -105       N  
ATOM    123  CA  PHE A  27     -21.738 -39.325   7.531  1.00104.43           C  
ANISOU  123  CA  PHE A  27    11908  13168  14601    597   1527   -311       C  
ATOM    124  C   PHE A  27     -21.593 -39.442   6.013  1.00106.88           C  
ANISOU  124  C   PHE A  27    12028  13631  14951    614   1373   -440       C  
ATOM    125  O   PHE A  27     -21.315 -38.447   5.337  1.00104.91           O  
ANISOU  125  O   PHE A  27    11600  13603  14659    712   1173   -426       O  
ATOM    126  CB  PHE A  27     -22.899 -38.379   7.914  1.00106.29           C  
ANISOU  126  CB  PHE A  27    11946  13521  14920    479   1566   -384       C  
ATOM    127  CG  PHE A  27     -22.872 -37.864   9.335  1.00107.83           C  
ANISOU  127  CG  PHE A  27    12299  13633  15040    504   1660   -232       C  
ATOM    128  CD1 PHE A  27     -23.307 -38.659  10.390  1.00112.98           C  
ANISOU  128  CD1 PHE A  27    13201  14028  15699    383   1929   -219       C  
ATOM    129  CD2 PHE A  27     -22.402 -36.587   9.620  1.00108.25           C  
ANISOU  129  CD2 PHE A  27    12278  13849  15004    644   1494   -107       C  
ATOM    130  CE1 PHE A  27     -23.264 -38.188  11.706  1.00113.97           C  
ANISOU  130  CE1 PHE A  27    13504  14071  15728    414   2016    -77       C  
ATOM    131  CE2 PHE A  27     -22.363 -36.115  10.936  1.00111.09           C  
ANISOU  131  CE2 PHE A  27    12789  14134  15284    669   1575     22       C  
ATOM    132  CZ  PHE A  27     -22.794 -36.919  11.970  1.00111.09           C  
ANISOU  132  CZ  PHE A  27    13042  13889  15278    560   1829     38       C  
ATOM    133  N   GLY A  28     -21.712 -40.669   5.510  1.00104.08           N  
ANISOU  133  N   GLY A  28    11749  13137  14660    526   1479   -557       N  
ATOM    134  CA  GLY A  28     -21.599 -40.979   4.089  1.00103.43           C  
ANISOU  134  CA  GLY A  28    11524  13166  14607    528   1360   -696       C  
ATOM    135  C   GLY A  28     -20.192 -40.951   3.520  1.00104.58           C  
ANISOU  135  C   GLY A  28    11740  13361  14634    729   1204   -585       C  
ATOM    136  O   GLY A  28     -19.231 -40.637   4.229  1.00103.14           O  
ANISOU  136  O   GLY A  28    11691  13146  14351    883   1162   -405       O  
ATOM    137  N   LYS A  29     -20.089 -41.249   2.230  1.00100.21           N  
ANISOU  137  N   LYS A  29    11086  12895  14095    726   1117   -714       N  
ATOM    138  CA  LYS A  29     -18.810 -41.326   1.546  1.00 98.62           C  
ANISOU  138  CA  LYS A  29    10923  12748  13799    888    993   -658       C  
ATOM    139  C   LYS A  29     -18.794 -40.387   0.352  1.00100.07           C  
ANISOU  139  C   LYS A  29    10905  13188  13931    930    807   -716       C  
ATOM    140  O   LYS A  29     -19.815 -40.187  -0.295  1.00100.15           O  
ANISOU  140  O   LYS A  29    10755  13307  13990    828    766   -866       O  
ATOM    141  CB  LYS A  29     -18.553 -42.756   1.079  1.00102.70           C  
ANISOU  141  CB  LYS A  29    11573  13093  14356    858   1090   -752       C  
ATOM    142  N   VAL A  30     -17.632 -39.812   0.062  1.00 94.42           N  
ANISOU  142  N   VAL A  30    10204  12561  13109   1085    701   -612       N  
ATOM    143  CA  VAL A  30     -17.501 -38.887  -1.050  1.00 92.91           C  
ANISOU  143  CA  VAL A  30     9890  12579  12832   1139    554   -639       C  
ATOM    144  C   VAL A  30     -16.851 -39.575  -2.230  1.00 96.27           C  
ANISOU  144  C   VAL A  30    10353  13008  13219   1175    535   -726       C  
ATOM    145  O   VAL A  30     -15.775 -40.141  -2.102  1.00 96.01           O  
ANISOU  145  O   VAL A  30    10424  12878  13179   1259    582   -674       O  
ATOM    146  CB  VAL A  30     -16.598 -37.711  -0.687  1.00 95.17           C  
ANISOU  146  CB  VAL A  30    10162  12966  13031   1253    483   -480       C  
ATOM    147  CG1 VAL A  30     -16.513 -36.752  -1.856  1.00 94.41           C  
ANISOU  147  CG1 VAL A  30     9983  13054  12835   1291    364   -506       C  
ATOM    148  CG2 VAL A  30     -17.106 -37.014   0.560  1.00 94.52           C  
ANISOU  148  CG2 VAL A  30    10066  12860  12986   1221    517   -392       C  
ATOM    149  N   LYS A  31     -17.497 -39.507  -3.385  1.00 92.53           N  
ANISOU  149  N   LYS A  31     9796  12647  12714   1126    459   -870       N  
ATOM    150  CA  LYS A  31     -17.013 -40.205  -4.564  1.00 92.72           C  
ANISOU  150  CA  LYS A  31     9860  12685  12685   1147    443   -972       C  
ATOM    151  C   LYS A  31     -16.744 -39.234  -5.691  1.00 95.48           C  
ANISOU  151  C   LYS A  31    10173  13220  12887   1208    318   -989       C  
ATOM    152  O   LYS A  31     -17.461 -38.258  -5.863  1.00 94.66           O  
ANISOU  152  O   LYS A  31     9997  13233  12738   1214    222   -973       O  
ATOM    153  CB  LYS A  31     -18.018 -41.263  -5.010  1.00 97.00           C  
ANISOU  153  CB  LYS A  31    10392  13147  13318   1020    495  -1165       C  
ATOM    154  N   ILE A  32     -15.698 -39.499  -6.457  1.00 91.86           N  
ANISOU  154  N   ILE A  32     9784  12773  12344   1259    328  -1023       N  
ATOM    155  CA  ILE A  32     -15.292 -38.587  -7.513  1.00 91.46           C  
ANISOU  155  CA  ILE A  32     9762  12863  12124   1313    248  -1038       C  
ATOM    156  C   ILE A  32     -16.413 -38.478  -8.524  1.00 96.19           C  
ANISOU  156  C   ILE A  32    10333  13552  12662   1271    132  -1202       C  
ATOM    157  O   ILE A  32     -17.022 -39.478  -8.884  1.00 96.94           O  
ANISOU  157  O   ILE A  32    10420  13595  12820   1201    152  -1355       O  
ATOM    158  CB  ILE A  32     -14.036 -39.083  -8.263  1.00 94.72           C  
ANISOU  158  CB  ILE A  32    10264  13253  12473   1366    330  -1040       C  
ATOM    159  N   GLY A  33     -16.683 -37.267  -8.990  1.00 92.46           N  
ANISOU  159  N   GLY A  33     9853  13211  12066   1326      8  -1178       N  
ATOM    160  CA  GLY A  33     -17.717 -37.081  -9.988  1.00 93.74           C  
ANISOU  160  CA  GLY A  33     9993  13487  12136   1337   -151  -1334       C  
ATOM    161  C   GLY A  33     -17.140 -36.556 -11.279  1.00 98.06           C  
ANISOU  161  C   GLY A  33    10706  14110  12444   1430   -205  -1330       C  
ATOM    162  O   GLY A  33     -16.511 -35.502 -11.302  1.00 97.10           O  
ANISOU  162  O   GLY A  33    10663  14045  12186   1516   -249  -1212       O  
ATOM    163  N   GLU A  34     -17.372 -37.285 -12.363  1.00 95.79           N  
ANISOU  163  N   GLU A  34    10497  13803  12096   1407   -178  -1456       N  
ATOM    164  CA  GLU A  34     -16.820 -36.914 -13.654  1.00 96.50           C  
ANISOU  164  CA  GLU A  34    10781  13943  11941   1480   -197  -1470       C  
ATOM    165  C   GLU A  34     -17.912 -36.730 -14.691  1.00101.88           C  
ANISOU  165  C   GLU A  34    11494  14744  12471   1538   -410  -1634       C  
ATOM    166  O   GLU A  34     -18.760 -37.600 -14.871  1.00102.65           O  
ANISOU  166  O   GLU A  34    11486  14855  12662   1475   -473  -1826       O  
ATOM    167  CB  GLU A  34     -15.837 -37.984 -14.125  1.00 98.31           C  
ANISOU  167  CB  GLU A  34    11086  14082  12184   1431    -35  -1522       C  
ATOM    168  CG  GLU A  34     -15.459 -37.881 -15.592  1.00110.53           C  
ANISOU  168  CG  GLU A  34    12844  15644  13508   1485     43  -1479       C  
ATOM    169  CD  GLU A  34     -14.106 -38.491 -15.884  1.00135.72           C  
ANISOU  169  CD  GLU A  34    16110  18769  16687   1442    179  -1587       C  
ATOM    170  OE1 GLU A  34     -13.213 -38.394 -15.020  1.00132.38           O  
ANISOU  170  OE1 GLU A  34    15592  18250  16457   1396    310  -1583       O  
ATOM    171  OE2 GLU A  34     -13.937 -39.068 -16.978  1.00132.84           O  
ANISOU  171  OE2 GLU A  34    15918  18446  16109   1469    154  -1678       O  
ATOM    172  N   HIS A  35     -17.883 -35.599 -15.382  1.00 98.70           N  
ANISOU  172  N   HIS A  35    11248  14421  11832   1666   -521  -1570       N  
ATOM    173  CA  HIS A  35     -18.842 -35.350 -16.445  1.00100.60           C  
ANISOU  173  CA  HIS A  35    11557  14785  11883   1777   -762  -1716       C  
ATOM    174  C   HIS A  35     -18.589 -36.243 -17.649  1.00106.07           C  
ANISOU  174  C   HIS A  35    12392  15481  12428   1767   -763  -1876       C  
ATOM    175  O   HIS A  35     -17.447 -36.500 -18.013  1.00105.57           O  
ANISOU  175  O   HIS A  35    12515  15342  12253   1747   -589  -1804       O  
ATOM    176  CB  HIS A  35     -18.800 -33.891 -16.872  1.00101.63           C  
ANISOU  176  CB  HIS A  35    11887  14961  11767   1940   -854  -1575       C  
ATOM    177  CG  HIS A  35     -20.067 -33.422 -17.510  1.00107.08           C  
ANISOU  177  CG  HIS A  35    12578  15787  12321   2097  -1154  -1708       C  
ATOM    178  ND1 HIS A  35     -20.139 -32.274 -18.268  1.00108.53           N  
ANISOU  178  ND1 HIS A  35    12596  16037  12605   2166  -1294  -1689       N  
ATOM    179  CD2 HIS A  35     -21.313 -33.949 -17.505  1.00111.36           C  
ANISOU  179  CD2 HIS A  35    13264  16414  12635   2209  -1344  -1873       C  
ATOM    180  CE1 HIS A  35     -21.376 -32.112 -18.698  1.00110.36           C  
ANISOU  180  CE1 HIS A  35    12857  16397  12679   2328  -1573  -1851       C  
ATOM    181  NE2 HIS A  35     -22.108 -33.116 -18.251  1.00112.51           N  
ANISOU  181  NE2 HIS A  35    13320  16687  12742   2365  -1623  -1965       N  
ATOM    182  N   GLN A  36     -19.664 -36.700 -18.276  1.00104.14           N  
ANISOU  182  N   GLN A  36    12044  15326  12200   1768   -947  -2115       N  
ATOM    183  CA  GLN A  36     -19.565 -37.540 -19.471  1.00105.76           C  
ANISOU  183  CA  GLN A  36    12364  15546  12274   1754   -975  -2304       C  
ATOM    184  C   GLN A  36     -19.363 -36.716 -20.746  1.00110.61           C  
ANISOU  184  C   GLN A  36    13312  16214  12499   1921  -1078  -2280       C  
ATOM    185  O   GLN A  36     -18.511 -37.061 -21.567  1.00110.89           O  
ANISOU  185  O   GLN A  36    13558  16190  12383   1897   -945  -2290       O  
ATOM    186  CB  GLN A  36     -20.806 -38.443 -19.594  1.00108.93           C  
ANISOU  186  CB  GLN A  36    12533  16037  12820   1700  -1151  -2593       C  
ATOM    187  CG  GLN A  36     -20.597 -39.669 -20.477  1.00127.06           C  
ANISOU  187  CG  GLN A  36    14876  18305  15097   1611  -1105  -2801       C  
ATOM    188  N   LEU A  37     -20.141 -35.631 -20.900  1.00107.41           N  
ANISOU  188  N   LEU A  37    12973  15910  11928   2097  -1304  -2251       N  
ATOM    189  CA  LEU A  37     -20.129 -34.752 -22.070  1.00108.98           C  
ANISOU  189  CA  LEU A  37    13531  16150  11725   2294  -1437  -2224       C  
ATOM    190  C   LEU A  37     -18.911 -33.827 -22.152  1.00111.08           C  
ANISOU  190  C   LEU A  37    14108  16290  11807   2310  -1199  -1963       C  
ATOM    191  O   LEU A  37     -18.264 -33.775 -23.199  1.00112.05           O  
ANISOU  191  O   LEU A  37    14551  16365  11657   2341  -1112  -1960       O  
ATOM    192  CB  LEU A  37     -21.437 -33.937 -22.157  1.00110.63           C  
ANISOU  192  CB  LEU A  37    13701  16503  11831   2505  -1779  -2295       C  
ATOM    193  CG  LEU A  37     -22.754 -34.719 -22.070  1.00116.79           C  
ANISOU  193  CG  LEU A  37    14135  17432  12807   2493  -2029  -2596       C  
ATOM    194  CD1 LEU A  37     -23.873 -33.844 -21.549  1.00117.44           C  
ANISOU  194  CD1 LEU A  37    14053  17630  12940   2650  -2276  -2617       C  
ATOM    195  CD2 LEU A  37     -23.130 -35.335 -23.405  1.00122.44           C  
ANISOU  195  CD2 LEU A  37    14976  18242  13304   2570  -2222  -2853       C  
ATOM    196  N   THR A  38     -18.608 -33.092 -21.065  1.00104.88           N  
ANISOU  196  N   THR A  38    13234  15448  11168   2279  -1082  -1761       N  
ATOM    197  CA  THR A  38     -17.501 -32.131 -21.020  1.00103.59           C  
ANISOU  197  CA  THR A  38    13326  15168  10866   2275   -846  -1534       C  
ATOM    198  C   THR A  38     -16.213 -32.721 -20.448  1.00104.92           C  
ANISOU  198  C   THR A  38    13388  15227  11249   2076   -523  -1469       C  
ATOM    199  O   THR A  38     -15.196 -32.760 -21.141  1.00105.13           O  
ANISOU  199  O   THR A  38    13638  15177  11132   2028   -317  -1451       O  
ATOM    200  CB  THR A  38     -17.914 -30.845 -20.280  1.00110.70           C  
ANISOU  200  CB  THR A  38    14230  16071  11759   2381   -921  -1367       C  
ATOM    201  OG1 THR A  38     -18.263 -31.171 -18.935  1.00107.80           O  
ANISOU  201  OG1 THR A  38    13481  15728  11750   2282   -920  -1355       O  
ATOM    202  CG2 THR A  38     -19.061 -30.114 -20.958  1.00111.81           C  
ANISOU  202  CG2 THR A  38    14534  16308  11641   2626  -1242  -1423       C  
ATOM    203  N   GLY A  39     -16.272 -33.152 -19.190  1.00 98.88           N  
ANISOU  203  N   GLY A  39    12295  14456  10820   1973   -481  -1442       N  
ATOM    204  CA  GLY A  39     -15.138 -33.711 -18.465  1.00 96.68           C  
ANISOU  204  CA  GLY A  39    11883  14082  10768   1822   -221  -1385       C  
ATOM    205  C   GLY A  39     -14.872 -33.012 -17.147  1.00 97.86           C  
ANISOU  205  C   GLY A  39    11892  14198  11092   1794   -141  -1213       C  
ATOM    206  O   GLY A  39     -13.821 -33.228 -16.538  1.00 96.16           O  
ANISOU  206  O   GLY A  39    11597  13911  11029   1702     66  -1151       O  
ATOM    207  N   HIS A  40     -15.828 -32.165 -16.700  1.00 93.80           N  
ANISOU  207  N   HIS A  40    11341  13743  10557   1887   -314  -1149       N  
ATOM    208  CA  HIS A  40     -15.759 -31.408 -15.446  1.00 91.54           C  
ANISOU  208  CA  HIS A  40    10930  13434  10418   1873   -267   -993       C  
ATOM    209  C   HIS A  40     -15.823 -32.354 -14.248  1.00 93.09           C  
ANISOU  209  C   HIS A  40    10822  13611  10939   1764   -227  -1017       C  
ATOM    210  O   HIS A  40     -16.587 -33.321 -14.270  1.00 93.15           O  
ANISOU  210  O   HIS A  40    10685  13649  11057   1733   -330  -1160       O  
ATOM    211  CB  HIS A  40     -16.891 -30.367 -15.380  1.00 92.94           C  
ANISOU  211  CB  HIS A  40    11145  13681  10488   2015   -481   -952       C  
ATOM    212  CG  HIS A  40     -16.798 -29.445 -14.203  1.00 94.63           C  
ANISOU  212  CG  HIS A  40    11276  13865  10814   2009   -423   -789       C  
ATOM    213  ND1 HIS A  40     -17.494 -29.694 -13.034  1.00 95.13           N  
ANISOU  213  ND1 HIS A  40    11060  13960  11124   1972   -491   -795       N  
ATOM    214  CD2 HIS A  40     -16.083 -28.307 -14.051  1.00 95.93           C  
ANISOU  214  CD2 HIS A  40    11613  13964  10871   2023   -287   -632       C  
ATOM    215  CE1 HIS A  40     -17.185 -28.703 -12.214  1.00 93.28           C  
ANISOU  215  CE1 HIS A  40    10837  13688  10917   1977   -412   -638       C  
ATOM    216  NE2 HIS A  40     -16.341 -27.843 -12.782  1.00 94.05           N  
ANISOU  216  NE2 HIS A  40    11194  13727  10813   2005   -290   -540       N  
ATOM    217  N   LYS A  41     -15.013 -32.080 -13.214  1.00 87.51           N  
ANISOU  217  N   LYS A  41    10034  12843  10374   1705    -72   -889       N  
ATOM    218  CA  LYS A  41     -14.951 -32.915 -12.016  1.00 85.84           C  
ANISOU  218  CA  LYS A  41     9591  12588  10435   1624    -22   -887       C  
ATOM    219  C   LYS A  41     -15.574 -32.256 -10.790  1.00 88.18           C  
ANISOU  219  C   LYS A  41     9757  12899  10847   1637    -80   -784       C  
ATOM    220  O   LYS A  41     -15.281 -31.097 -10.489  1.00 87.15           O  
ANISOU  220  O   LYS A  41     9695  12772  10645   1676    -50   -658       O  
ATOM    221  CB  LYS A  41     -13.512 -33.379 -11.739  1.00 87.72           C  
ANISOU  221  CB  LYS A  41     9820  12747  10763   1564    182   -859       C  
ATOM    222  CG  LYS A  41     -13.028 -34.441 -12.719  1.00103.49           C  
ANISOU  222  CG  LYS A  41    11879  14716  12728   1533    246   -996       C  
ATOM    223  CD  LYS A  41     -11.563 -34.777 -12.525  1.00113.13           C  
ANISOU  223  CD  LYS A  41    13083  15870  14030   1499    442   -988       C  
ATOM    224  CE  LYS A  41     -11.095 -35.776 -13.553  1.00126.22           C  
ANISOU  224  CE  LYS A  41    14811  17498  15648   1475    514  -1133       C  
ATOM    225  NZ  LYS A  41      -9.653 -36.096 -13.392  1.00136.45           N  
ANISOU  225  NZ  LYS A  41    16068  18740  17039   1457    703  -1153       N  
ATOM    226  N   VAL A  42     -16.458 -33.002 -10.101  1.00 84.34           N  
ANISOU  226  N   VAL A  42     9092  12412  10539   1592   -147   -851       N  
ATOM    227  CA  VAL A  42     -17.162 -32.574  -8.883  1.00 83.04           C  
ANISOU  227  CA  VAL A  42     8789  12253  10508   1584   -185   -781       C  
ATOM    228  C   VAL A  42     -16.983 -33.617  -7.770  1.00 85.75           C  
ANISOU  228  C   VAL A  42     9009  12501  11073   1491    -78   -779       C  
ATOM    229  O   VAL A  42     -16.628 -34.760  -8.054  1.00 85.81           O  
ANISOU  229  O   VAL A  42     9021  12446  11137   1441    -15   -863       O  
ATOM    230  CB  VAL A  42     -18.670 -32.250  -9.114  1.00 88.08           C  
ANISOU  230  CB  VAL A  42     9346  12989  11131   1633   -375   -883       C  
ATOM    231  CG1 VAL A  42     -18.862 -31.070 -10.062  1.00 88.83           C  
ANISOU  231  CG1 VAL A  42     9606  13163  10984   1771   -500   -856       C  
ATOM    232  CG2 VAL A  42     -19.456 -33.474  -9.585  1.00 89.34           C  
ANISOU  232  CG2 VAL A  42     9402  13167  11378   1569   -439  -1094       C  
ATOM    233  N   ALA A  43     -17.247 -33.228  -6.513  1.00 81.07           N  
ANISOU  233  N   ALA A  43     8331  11884  10590   1475    -55   -683       N  
ATOM    234  CA  ALA A  43     -17.188 -34.139  -5.373  1.00 80.36           C  
ANISOU  234  CA  ALA A  43     8170  11685  10677   1403     44   -666       C  
ATOM    235  C   ALA A  43     -18.629 -34.459  -4.974  1.00 85.03           C  
ANISOU  235  C   ALA A  43     8637  12285  11385   1335     -3   -768       C  
ATOM    236  O   ALA A  43     -19.392 -33.550  -4.642  1.00 84.45           O  
ANISOU  236  O   ALA A  43     8496  12283  11307   1361    -76   -744       O  
ATOM    237  CB  ALA A  43     -16.437 -33.496  -4.219  1.00 79.62           C  
ANISOU  237  CB  ALA A  43     8089  11553  10611   1431    116   -501       C  
ATOM    238  N   VAL A  44     -19.021 -35.737  -5.078  1.00 82.66           N  
ANISOU  238  N   VAL A  44     8303  11913  11192   1243     45   -903       N  
ATOM    239  CA  VAL A  44     -20.387 -36.162  -4.769  1.00 83.56           C  
ANISOU  239  CA  VAL A  44     8280  12028  11441   1144     34  -1049       C  
ATOM    240  C   VAL A  44     -20.445 -36.895  -3.425  1.00 87.48           C  
ANISOU  240  C   VAL A  44     8784  12361  12092   1045    205   -999       C  
ATOM    241  O   VAL A  44     -20.021 -38.049  -3.324  1.00 87.62           O  
ANISOU  241  O   VAL A  44     8884  12238  12169    988    321  -1026       O  
ATOM    242  CB  VAL A  44     -21.044 -36.960  -5.933  1.00 89.27           C  
ANISOU  242  CB  VAL A  44     8949  12798  12172   1092    -35  -1284       C  
ATOM    243  CG1 VAL A  44     -22.485 -37.343  -5.604  1.00 90.58           C  
ANISOU  243  CG1 VAL A  44     8934  12980  12503    972    -37  -1478       C  
ATOM    244  CG2 VAL A  44     -20.989 -36.176  -7.243  1.00 89.51           C  
ANISOU  244  CG2 VAL A  44     9020  12982  12007   1216   -215  -1322       C  
ATOM    245  N   LYS A  45     -20.959 -36.206  -2.393  1.00 83.72           N  
ANISOU  245  N   LYS A  45     8250  11891  11668   1034    226   -923       N  
ATOM    246  CA  LYS A  45     -21.118 -36.763  -1.053  1.00 83.80           C  
ANISOU  246  CA  LYS A  45     8301  11742  11797    944    395   -868       C  
ATOM    247  C   LYS A  45     -22.444 -37.525  -1.018  1.00 90.37           C  
ANISOU  247  C   LYS A  45     9015  12536  12787    779    470  -1082       C  
ATOM    248  O   LYS A  45     -23.506 -36.926  -1.214  1.00 90.72           O  
ANISOU  248  O   LYS A  45     8882  12711  12879    755    384  -1207       O  
ATOM    249  CB  LYS A  45     -21.066 -35.652   0.014  1.00 84.96           C  
ANISOU  249  CB  LYS A  45     8447  11914  11920    997    397   -704       C  
ATOM    250  CG  LYS A  45     -21.017 -36.171   1.452  1.00 99.49           C  
ANISOU  250  CG  LYS A  45    10391  13576  13833    933    572   -613       C  
ATOM    251  CD  LYS A  45     -20.583 -35.100   2.447  1.00108.61           C  
ANISOU  251  CD  LYS A  45    11587  14754  14926   1016    559   -430       C  
ATOM    252  CE  LYS A  45     -21.727 -34.278   2.993  1.00120.67           C  
ANISOU  252  CE  LYS A  45    12985  16350  16514    963    561   -466       C  
ATOM    253  NZ  LYS A  45     -21.243 -33.199   3.893  1.00129.02           N  
ANISOU  253  NZ  LYS A  45    14091  17431  17500   1046    547   -292       N  
ATOM    254  N   ILE A  46     -22.374 -38.850  -0.812  1.00 88.54           N  
ANISOU  254  N   ILE A  46     8879  12124  12639    670    632  -1143       N  
ATOM    255  CA  ILE A  46     -23.557 -39.712  -0.785  1.00 90.73           C  
ANISOU  255  CA  ILE A  46     9057  12334  13081    478    750  -1372       C  
ATOM    256  C   ILE A  46     -23.991 -40.014   0.653  1.00 95.70           C  
ANISOU  256  C   ILE A  46     9763  12785  13816    356    976  -1320       C  
ATOM    257  O   ILE A  46     -23.375 -40.841   1.327  1.00 95.44           O  
ANISOU  257  O   ILE A  46     9957  12531  13774    337   1141  -1212       O  
ATOM    258  CB  ILE A  46     -23.390 -40.998  -1.648  1.00 95.27           C  
ANISOU  258  CB  ILE A  46     9690  12820  13689    404    802  -1525       C  
ATOM    259  CG1 ILE A  46     -23.275 -40.674  -3.155  1.00 95.07           C  
ANISOU  259  CG1 ILE A  46     9653  12949  13522    542    599  -1537       C  
ATOM    260  CG2 ILE A  46     -24.534 -41.979  -1.377  1.00 98.47           C  
ANISOU  260  CG2 ILE A  46     9932  13209  14275    193    894  -1821       C  
ATOM    261  CD1 ILE A  46     -22.850 -41.846  -4.022  1.00102.24           C  
ANISOU  261  CD1 ILE A  46    10741  13720  14384    571    668  -1503       C  
ATOM    262  N   LEU A  47     -25.061 -39.343   1.107  1.00 93.24           N  
ANISOU  262  N   LEU A  47     9273  12560  13593    285    983  -1405       N  
ATOM    263  CA  LEU A  47     -25.623 -39.516   2.447  1.00 94.03           C  
ANISOU  263  CA  LEU A  47     9430  12504  13792    151   1214  -1383       C  
ATOM    264  C   LEU A  47     -26.796 -40.495   2.384  1.00101.05           C  
ANISOU  264  C   LEU A  47    10209  13304  14879    -97   1405  -1670       C  
ATOM    265  O   LEU A  47     -27.840 -40.163   1.819  1.00101.73           O  
ANISOU  265  O   LEU A  47    10008  13565  15079   -162   1316  -1914       O  
ATOM    266  CB  LEU A  47     -26.081 -38.163   3.031  1.00 93.11           C  
ANISOU  266  CB  LEU A  47     9178  12532  13667    213   1135  -1319       C  
ATOM    267  CG  LEU A  47     -25.006 -37.103   3.261  1.00 95.34           C  
ANISOU  267  CG  LEU A  47     9566  12888  13772    425    985  -1050       C  
ATOM    268  CD1 LEU A  47     -25.580 -35.720   3.093  1.00 94.86           C  
ANISOU  268  CD1 LEU A  47     9303  13039  13700    509    819  -1070       C  
ATOM    269  CD2 LEU A  47     -24.385 -37.237   4.634  1.00 97.21           C  
ANISOU  269  CD2 LEU A  47    10046  12936  13954    434   1149   -837       C  
ATOM    270  N   ASN A  48     -26.617 -41.708   2.944  1.00 99.22           N  
ANISOU  270  N   ASN A  48    10213  12797  14690   -228   1665  -1658       N  
ATOM    271  CA  ASN A  48     -27.654 -42.742   2.959  1.00102.06           C  
ANISOU  271  CA  ASN A  48    10512  13022  15244   -497   1907  -1934       C  
ATOM    272  C   ASN A  48     -28.787 -42.349   3.907  1.00107.43           C  
ANISOU  272  C   ASN A  48    11063  13690  16066   -664   2089  -2041       C  
ATOM    273  O   ASN A  48     -28.580 -42.295   5.121  1.00106.70           O  
ANISOU  273  O   ASN A  48    11197  13422  15923   -678   2274  -1855       O  
ATOM    274  CB  ASN A  48     -27.068 -44.117   3.303  1.00104.11           C  
ANISOU  274  CB  ASN A  48    11117  12957  15483   -574   2151  -1865       C  
ATOM    275  CG  ASN A  48     -28.072 -45.243   3.244  1.00130.00           C  
ANISOU  275  CG  ASN A  48    14363  16069  18962   -873   2431  -2160       C  
ATOM    276  OD1 ASN A  48     -28.626 -45.664   4.263  1.00125.69           O  
ANISOU  276  OD1 ASN A  48    13953  15304  18499  -1059   2743  -2186       O  
ATOM    277  ND2 ASN A  48     -28.332 -45.755   2.048  1.00122.99           N  
ANISOU  277  ND2 ASN A  48    13304  15273  18151   -937   2341  -2402       N  
ATOM    278  N   ARG A  49     -29.976 -42.051   3.333  1.00105.79           N  
ANISOU  278  N   ARG A  49    10486  13681  16030   -775   2023  -2356       N  
ATOM    279  CA  ARG A  49     -31.191 -41.625   4.039  1.00107.28           C  
ANISOU  279  CA  ARG A  49    10458  13908  16394   -937   2173  -2537       C  
ATOM    280  C   ARG A  49     -31.578 -42.525   5.212  1.00113.69           C  
ANISOU  280  C   ARG A  49    11490  14398  17308  -1200   2614  -2563       C  
ATOM    281  O   ARG A  49     -31.995 -42.009   6.249  1.00113.41           O  
ANISOU  281  O   ARG A  49    11470  14319  17303  -1255   2767  -2510       O  
ATOM    282  CB  ARG A  49     -32.365 -41.466   3.064  1.00109.49           C  
ANISOU  282  CB  ARG A  49    10298  14439  16865  -1017   2029  -2938       C  
ATOM    283  N   GLN A  50     -31.418 -43.859   5.056  1.00112.32           N  
ANISOU  283  N   GLN A  50    11519  13984  17173  -1356   2829  -2636       N  
ATOM    284  CA  GLN A  50     -31.708 -44.856   6.092  1.00114.63           C  
ANISOU  284  CA  GLN A  50    12103  13917  17535  -1608   3279  -2653       C  
ATOM    285  C   GLN A  50     -30.740 -44.719   7.278  1.00117.18           C  
ANISOU  285  C   GLN A  50    12869  14021  17633  -1460   3374  -2250       C  
ATOM    286  O   GLN A  50     -31.183 -44.781   8.427  1.00117.99           O  
ANISOU  286  O   GLN A  50    13138  13931  17760  -1606   3679  -2221       O  
ATOM    287  CB  GLN A  50     -31.701 -46.283   5.497  1.00118.23           C  
ANISOU  287  CB  GLN A  50    12685  14170  18069  -1781   3455  -2826       C  
ATOM    288  CG  GLN A  50     -31.909 -47.434   6.496  1.00136.93           C  
ANISOU  288  CG  GLN A  50    15435  16109  20481  -2037   3947  -2828       C  
ATOM    289  CD  GLN A  50     -33.149 -47.290   7.347  1.00159.57           C  
ANISOU  289  CD  GLN A  50    18171  18915  23542  -2324   4277  -3044       C  
ATOM    290  OE1 GLN A  50     -34.284 -47.358   6.862  1.00157.72           O  
ANISOU  290  OE1 GLN A  50    17539  18821  23566  -2553   4343  -3445       O  
ATOM    291  NE2 GLN A  50     -32.954 -47.093   8.643  1.00151.66           N  
ANISOU  291  NE2 GLN A  50    17498  17706  22421  -2314   4493  -2799       N  
ATOM    292  N   LYS A  51     -29.436 -44.503   6.997  1.00111.45           N  
ANISOU  292  N   LYS A  51    12324  13334  16688  -1169   3112  -1961       N  
ATOM    293  CA  LYS A  51     -28.399 -44.322   8.019  1.00109.89           C  
ANISOU  293  CA  LYS A  51    12513  12974  16266   -979   3128  -1597       C  
ATOM    294  C   LYS A  51     -28.541 -42.977   8.745  1.00112.41           C  
ANISOU  294  C   LYS A  51    12718  13462  16532   -879   3025  -1472       C  
ATOM    295  O   LYS A  51     -28.129 -42.860   9.900  1.00111.69           O  
ANISOU  295  O   LYS A  51    12932  13203  16304   -818   3146  -1247       O  
ATOM    296  CB  LYS A  51     -26.996 -44.485   7.421  1.00110.43           C  
ANISOU  296  CB  LYS A  51    12740  13064  16154   -707   2873  -1386       C  
ATOM    297  N   ILE A  52     -29.133 -41.972   8.068  1.00108.36           N  
ANISOU  297  N   ILE A  52    11784  13272  16117   -852   2797  -1623       N  
ATOM    298  CA  ILE A  52     -29.403 -40.642   8.622  1.00106.96           C  
ANISOU  298  CA  ILE A  52    11451  13271  15917   -765   2692  -1548       C  
ATOM    299  C   ILE A  52     -30.651 -40.738   9.522  1.00113.60           C  
ANISOU  299  C   ILE A  52    12228  14004  16930  -1032   3028  -1735       C  
ATOM    300  O   ILE A  52     -30.672 -40.147  10.603  1.00112.64           O  
ANISOU  300  O   ILE A  52    12230  13829  16740  -1012   3128  -1590       O  
ATOM    301  CB  ILE A  52     -29.528 -39.569   7.486  1.00108.48           C  
ANISOU  301  CB  ILE A  52    11260  13827  16131   -606   2316  -1636       C  
ATOM    302  CG1 ILE A  52     -28.215 -39.422   6.649  1.00106.59           C  
ANISOU  302  CG1 ILE A  52    11118  13676  15704   -354   2025  -1439       C  
ATOM    303  CG2 ILE A  52     -30.021 -38.205   7.994  1.00108.31           C  
ANISOU  303  CG2 ILE A  52    11047  13984  16124   -539   2228  -1613       C  
ATOM    304  CD1 ILE A  52     -26.867 -39.032   7.403  1.00111.75           C  
ANISOU  304  CD1 ILE A  52    12077  14249  16133   -143   1960  -1082       C  
ATOM    305  N   ARG A  53     -31.667 -41.515   9.084  1.00113.36           N  
ANISOU  305  N   ARG A  53    12013  13935  17124  -1292   3217  -2070       N  
ATOM    306  CA  ARG A  53     -32.916 -41.743   9.817  1.00116.32           C  
ANISOU  306  CA  ARG A  53    12291  14200  17705  -1592   3580  -2317       C  
ATOM    307  C   ARG A  53     -32.735 -42.670  11.027  1.00122.40           C  
ANISOU  307  C   ARG A  53    13550  14561  18396  -1753   4007  -2178       C  
ATOM    308  O   ARG A  53     -33.511 -42.569  11.980  1.00123.85           O  
ANISOU  308  O   ARG A  53    13762  14631  18666  -1947   4318  -2264       O  
ATOM    309  CB  ARG A  53     -34.013 -42.282   8.886  1.00119.31           C  
ANISOU  309  CB  ARG A  53    12285  14687  18361  -1818   3631  -2758       C  
ATOM    310  N   SER A  54     -31.716 -43.565  10.992  1.00118.87           N  
ANISOU  310  N   SER A  54    13502  13887  17777  -1662   4028  -1969       N  
ATOM    311  CA  SER A  54     -31.402 -44.505  12.080  1.00120.58           C  
ANISOU  311  CA  SER A  54    14260  13687  17867  -1755   4397  -1803       C  
ATOM    312  C   SER A  54     -30.916 -43.774  13.340  1.00123.39           C  
ANISOU  312  C   SER A  54    14899  13974  18008  -1598   4411  -1498       C  
ATOM    313  O   SER A  54     -31.054 -44.294  14.448  1.00125.07           O  
ANISOU  313  O   SER A  54    15513  13867  18141  -1721   4768  -1415       O  
ATOM    314  CB  SER A  54     -30.369 -45.534  11.630  1.00123.95           C  
ANISOU  314  CB  SER A  54    15014  13925  18157  -1632   4343  -1657       C  
ATOM    315  OG  SER A  54     -29.110 -44.940  11.363  1.00129.43           O  
ANISOU  315  OG  SER A  54    15764  14774  18639  -1273   3953  -1373       O  
ATOM    316  N   LEU A  55     -30.353 -42.567  13.153  1.00116.85           N  
ANISOU  316  N   LEU A  55    13878  13438  17080  -1331   4030  -1340       N  
ATOM    317  CA  LEU A  55     -29.856 -41.685  14.210  1.00115.17           C  
ANISOU  317  CA  LEU A  55    13856  13230  16674  -1158   3971  -1075       C  
ATOM    318  C   LEU A  55     -30.698 -40.392  14.215  1.00118.44           C  
ANISOU  318  C   LEU A  55    13840  13934  17226  -1192   3874  -1213       C  
ATOM    319  O   LEU A  55     -31.638 -40.276  13.424  1.00118.86           O  
ANISOU  319  O   LEU A  55    13478  14166  17517  -1336   3854  -1514       O  
ATOM    320  CB  LEU A  55     -28.366 -41.363  13.967  1.00112.29           C  
ANISOU  320  CB  LEU A  55    13637  12953  16075   -806   3605   -781       C  
ATOM    321  CG  LEU A  55     -27.377 -42.528  14.053  1.00117.62           C  
ANISOU  321  CG  LEU A  55    14704  13378  16609   -705   3633   -642       C  
ATOM    322  CD1 LEU A  55     -25.986 -42.088  13.650  1.00115.23           C  
ANISOU  322  CD1 LEU A  55    14252  13288  16242   -450   3240   -557       C  
ATOM    323  CD2 LEU A  55     -27.363 -43.142  15.441  1.00120.97           C  
ANISOU  323  CD2 LEU A  55    15659  13515  16788   -594   3782   -381       C  
ATOM    324  N   ASP A  56     -30.376 -39.431  15.104  1.00113.74           N  
ANISOU  324  N   ASP A  56    13345  13386  16484  -1051   3807  -1012       N  
ATOM    325  CA  ASP A  56     -31.090 -38.152  15.187  1.00112.79           C  
ANISOU  325  CA  ASP A  56    12859  13522  16474  -1052   3711  -1116       C  
ATOM    326  C   ASP A  56     -30.326 -37.032  14.443  1.00113.07           C  
ANISOU  326  C   ASP A  56    12675  13864  16421   -757   3252   -984       C  
ATOM    327  O   ASP A  56     -30.513 -35.845  14.728  1.00111.40           O  
ANISOU  327  O   ASP A  56    12294  13827  16205   -671   3133   -954       O  
ATOM    328  CB  ASP A  56     -31.383 -37.784  16.659  1.00115.67           C  
ANISOU  328  CB  ASP A  56    13464  13729  16754  -1126   3980  -1019       C  
ATOM    329  CG  ASP A  56     -32.578 -36.866  16.882  1.00126.70           C  
ANISOU  329  CG  ASP A  56    14492  15298  18352  -1256   4064  -1240       C  
ATOM    330  OD1 ASP A  56     -33.247 -36.499  15.887  1.00127.12           O  
ANISOU  330  OD1 ASP A  56    14082  15600  18618  -1281   3900  -1487       O  
ATOM    331  OD2 ASP A  56     -32.844 -36.514  18.051  1.00133.65           O  
ANISOU  331  OD2 ASP A  56    15551  16062  19167  -1321   4288  -1175       O  
ATOM    332  N   VAL A  57     -29.496 -37.426  13.454  1.00108.17           N  
ANISOU  332  N   VAL A  57    12063  13300  15739   -616   3018   -922       N  
ATOM    333  CA  VAL A  57     -28.681 -36.522  12.629  1.00105.05           C  
ANISOU  333  CA  VAL A  57    11503  13160  15251   -357   2620   -805       C  
ATOM    334  C   VAL A  57     -29.531 -35.841  11.525  1.00108.47           C  
ANISOU  334  C   VAL A  57    11472  13879  15863   -369   2430  -1047       C  
ATOM    335  O   VAL A  57     -29.065 -34.883  10.905  1.00106.00           O  
ANISOU  335  O   VAL A  57    11017  13781  15478   -169   2129   -967       O  
ATOM    336  CB  VAL A  57     -27.401 -37.222  12.070  1.00107.93           C  
ANISOU  336  CB  VAL A  57    12082  13457  15469   -201   2470   -647       C  
ATOM    337  CG1 VAL A  57     -26.633 -36.306  11.118  1.00104.91           C  
ANISOU  337  CG1 VAL A  57    11615  13292  14953     61   2123   -483       C  
ATOM    338  CG2 VAL A  57     -26.478 -37.685  13.196  1.00108.75           C  
ANISOU  338  CG2 VAL A  57    12650  13250  15419   -194   2677   -465       C  
ATOM    339  N   VAL A  58     -30.795 -36.295  11.328  1.00107.21           N  
ANISOU  339  N   VAL A  58    11087  13717  15932   -598   2612  -1353       N  
ATOM    340  CA  VAL A  58     -31.746 -35.773  10.332  1.00107.50           C  
ANISOU  340  CA  VAL A  58    10675  14017  16154   -609   2438  -1635       C  
ATOM    341  C   VAL A  58     -31.914 -34.226  10.427  1.00109.34           C  
ANISOU  341  C   VAL A  58    10710  14476  16358   -432   2220  -1581       C  
ATOM    342  O   VAL A  58     -32.093 -33.568   9.400  1.00108.22           O  
ANISOU  342  O   VAL A  58    10306  14571  16241   -289   1930  -1676       O  
ATOM    343  CB  VAL A  58     -33.100 -36.546  10.357  1.00114.86           C  
ANISOU  343  CB  VAL A  58    11398  14888  17355   -909   2719  -2002       C  
ATOM    344  CG1 VAL A  58     -33.947 -36.216  11.587  1.00116.22           C  
ANISOU  344  CG1 VAL A  58    11556  14972  17630  -1075   3019  -2076       C  
ATOM    345  CG2 VAL A  58     -33.888 -36.346   9.065  1.00115.67           C  
ANISOU  345  CG2 VAL A  58    11059  15258  17631   -892   2485  -2321       C  
ATOM    346  N   GLY A  59     -31.794 -33.680  11.638  1.00105.13           N  
ANISOU  346  N   GLY A  59    10343  13853  15749   -428   2359  -1418       N  
ATOM    347  CA  GLY A  59     -31.864 -32.246  11.893  1.00103.42           C  
ANISOU  347  CA  GLY A  59     9999  13805  15489   -268   2193  -1340       C  
ATOM    348  C   GLY A  59     -30.565 -31.547  11.541  1.00103.89           C  
ANISOU  348  C   GLY A  59    10204  13945  15322     -9   1907  -1059       C  
ATOM    349  O   GLY A  59     -30.585 -30.462  10.954  1.00102.27           O  
ANISOU  349  O   GLY A  59     9819  13942  15097    159   1656  -1057       O  
ATOM    350  N   LYS A  60     -29.425 -32.179  11.895  1.00 99.19           N  
ANISOU  350  N   LYS A  60     9945  13185  14558     27   1951   -834       N  
ATOM    351  CA  LYS A  60     -28.069 -31.684  11.634  1.00 96.44           C  
ANISOU  351  CA  LYS A  60     9747  12891  14007    247   1719   -588       C  
ATOM    352  C   LYS A  60     -27.737 -31.675  10.139  1.00 99.22           C  
ANISOU  352  C   LYS A  60     9947  13401  14353    358   1462   -645       C  
ATOM    353  O   LYS A  60     -27.010 -30.790   9.686  1.00 97.02           O  
ANISOU  353  O   LYS A  60     9660  13248  13956    536   1243   -519       O  
ATOM    354  CB  LYS A  60     -27.033 -32.514  12.407  1.00 98.76           C  
ANISOU  354  CB  LYS A  60    10414  12964  14148    259   1837   -388       C  
ATOM    355  N   ILE A  61     -28.266 -32.660   9.381  1.00 97.05           N  
ANISOU  355  N   ILE A  61     9567  13108  14198    242   1506   -843       N  
ATOM    356  CA  ILE A  61     -28.078 -32.787   7.930  1.00 96.44           C  
ANISOU  356  CA  ILE A  61     9356  13171  14116    327   1282   -931       C  
ATOM    357  C   ILE A  61     -28.853 -31.668   7.215  1.00100.00           C  
ANISOU  357  C   ILE A  61     9514  13860  14623    425   1071  -1068       C  
ATOM    358  O   ILE A  61     -28.323 -31.066   6.280  1.00 98.35           O  
ANISOU  358  O   ILE A  61     9283  13784  14301    598    829  -1007       O  
ATOM    359  CB  ILE A  61     -28.445 -34.228   7.434  1.00101.46           C  
ANISOU  359  CB  ILE A  61     9985  13701  14865    159   1411  -1117       C  
ATOM    360  CG1 ILE A  61     -27.480 -35.314   8.002  1.00101.78           C  
ANISOU  360  CG1 ILE A  61    10371  13493  14809    124   1578   -947       C  
ATOM    361  CG2 ILE A  61     -28.574 -34.337   5.902  1.00102.47           C  
ANISOU  361  CG2 ILE A  61     9922  13998  15014    224   1184  -1279       C  
ATOM    362  CD1 ILE A  61     -25.935 -35.238   7.610  1.00107.30           C  
ANISOU  362  CD1 ILE A  61    11259  14200  15311    329   1396   -716       C  
ATOM    363  N   LYS A  62     -30.082 -31.371   7.691  1.00 97.97           N  
ANISOU  363  N   LYS A  62     9051  13643  14531    325   1171  -1254       N  
ATOM    364  CA  LYS A  62     -30.956 -30.322   7.154  1.00 98.36           C  
ANISOU  364  CA  LYS A  62     8815  13907  14652    435    978  -1411       C  
ATOM    365  C   LYS A  62     -30.308 -28.937   7.250  1.00100.10           C  
ANISOU  365  C   LYS A  62     9123  14209  14704    653    803  -1184       C  
ATOM    366  O   LYS A  62     -30.344 -28.184   6.276  1.00 99.46           O  
ANISOU  366  O   LYS A  62     8947  14286  14558    831    548  -1209       O  
ATOM    367  CB  LYS A  62     -32.318 -30.334   7.865  1.00103.16           C  
ANISOU  367  CB  LYS A  62     9193  14516  15485    273   1167  -1655       C  
ATOM    368  N   ARG A  63     -29.693 -28.621   8.409  1.00 95.31           N  
ANISOU  368  N   ARG A  63     8719  13480  14012    639    942   -967       N  
ATOM    369  CA  ARG A  63     -29.007 -27.350   8.657  1.00 93.20           C  
ANISOU  369  CA  ARG A  63     8554  13264  13594    811    820   -755       C  
ATOM    370  C   ARG A  63     -27.728 -27.231   7.826  1.00 95.02           C  
ANISOU  370  C   ARG A  63     8943  13521  13641    950    646   -584       C  
ATOM    371  O   ARG A  63     -27.439 -26.146   7.320  1.00 93.72           O  
ANISOU  371  O   ARG A  63     8773  13459  13376   1112    471   -512       O  
ATOM    372  CB  ARG A  63     -28.700 -27.178  10.152  1.00 93.10           C  
ANISOU  372  CB  ARG A  63     8718  13113  13542    742   1022   -601       C  
ATOM    373  N   GLU A  64     -26.980 -28.350   7.669  1.00 91.12           N  
ANISOU  373  N   GLU A  64     8594  12922  13105    887    709   -532       N  
ATOM    374  CA  GLU A  64     -25.737 -28.428   6.891  1.00 89.50           C  
ANISOU  374  CA  GLU A  64     8526  12729  12749    995    580   -401       C  
ATOM    375  C   GLU A  64     -25.973 -28.133   5.407  1.00 93.66           C  
ANISOU  375  C   GLU A  64     8931  13406  13249   1098    370   -511       C  
ATOM    376  O   GLU A  64     -25.120 -27.511   4.773  1.00 92.11           O  
ANISOU  376  O   GLU A  64     8828  13262  12908   1226    241   -396       O  
ATOM    377  CB  GLU A  64     -25.064 -29.797   7.069  1.00 90.96           C  
ANISOU  377  CB  GLU A  64     8872  12764  12925    908    703   -362       C  
ATOM    378  N   ILE A  65     -27.134 -28.564   4.866  1.00 91.94           N  
ANISOU  378  N   ILE A  65     8511  13255  13166   1040    340   -749       N  
ATOM    379  CA  ILE A  65     -27.542 -28.330   3.475  1.00 92.58           C  
ANISOU  379  CA  ILE A  65     8472  13488  13218   1152    118   -891       C  
ATOM    380  C   ILE A  65     -27.908 -26.845   3.298  1.00 96.35           C  
ANISOU  380  C   ILE A  65     8893  14087  13630   1331    -46   -864       C  
ATOM    381  O   ILE A  65     -27.489 -26.224   2.318  1.00 95.66           O  
ANISOU  381  O   ILE A  65     8886  14074  13387   1491   -226   -809       O  
ATOM    382  CB  ILE A  65     -28.678 -29.312   3.042  1.00 97.95           C  
ANISOU  382  CB  ILE A  65     8935  14207  14077   1030    136  -1188       C  
ATOM    383  CG1 ILE A  65     -28.135 -30.757   2.921  1.00 98.49           C  
ANISOU  383  CG1 ILE A  65     9114  14143  14165    886    271  -1198       C  
ATOM    384  CG2 ILE A  65     -29.357 -28.873   1.728  1.00100.07           C  
ANISOU  384  CG2 ILE A  65     9040  14663  14319   1180   -133  -1375       C  
ATOM    385  CD1 ILE A  65     -29.182 -31.876   3.041  1.00108.30           C  
ANISOU  385  CD1 ILE A  65    10190  15340  15620    679    420  -1466       C  
ATOM    386  N   GLN A  66     -28.657 -26.280   4.268  1.00 93.27           N  
ANISOU  386  N   GLN A  66     8394  13697  13347   1302     34   -897       N  
ATOM    387  CA  GLN A  66     -29.089 -24.879   4.281  1.00 93.19           C  
ANISOU  387  CA  GLN A  66     8333  13779  13297   1470    -96   -878       C  
ATOM    388  C   GLN A  66     -27.911 -23.910   4.416  1.00 94.83           C  
ANISOU  388  C   GLN A  66     8782  13940  13310   1579   -118   -608       C  
ATOM    389  O   GLN A  66     -27.902 -22.880   3.743  1.00 94.43           O  
ANISOU  389  O   GLN A  66     8780  13960  13141   1759   -284   -571       O  
ATOM    390  CB  GLN A  66     -30.118 -24.630   5.395  1.00 95.54           C  
ANISOU  390  CB  GLN A  66     8456  14070  13774   1387     38   -989       C  
ATOM    391  CG  GLN A  66     -31.495 -25.221   5.105  1.00114.78           C  
ANISOU  391  CG  GLN A  66    10590  16597  16424   1315     24  -1319       C  
ATOM    392  CD  GLN A  66     -32.360 -25.312   6.340  1.00137.30           C  
ANISOU  392  CD  GLN A  66    13295  19398  19475   1153    253  -1434       C  
ATOM    393  OE1 GLN A  66     -31.956 -25.838   7.385  1.00132.72           O  
ANISOU  393  OE1 GLN A  66    12857  18661  18908    982    504  -1316       O  
ATOM    394  NE2 GLN A  66     -33.593 -24.843   6.230  1.00132.20           N  
ANISOU  394  NE2 GLN A  66    12363  18881  18987   1208    176  -1686       N  
ATOM    395  N   ASN A  67     -26.922 -24.245   5.272  1.00 89.81           N  
ANISOU  395  N   ASN A  67     8306  13182  12636   1475     48   -435       N  
ATOM    396  CA  ASN A  67     -25.734 -23.421   5.501  1.00 87.96           C  
ANISOU  396  CA  ASN A  67     8272  12905  12243   1546     51   -213       C  
ATOM    397  C   ASN A  67     -24.785 -23.402   4.305  1.00 91.41           C  
ANISOU  397  C   ASN A  67     8842  13366  12524   1631    -60   -147       C  
ATOM    398  O   ASN A  67     -24.295 -22.329   3.951  1.00 90.54           O  
ANISOU  398  O   ASN A  67     8846  13272  12283   1745   -127    -45       O  
ATOM    399  CB  ASN A  67     -24.998 -23.834   6.782  1.00 88.02           C  
ANISOU  399  CB  ASN A  67     8391  12793  12261   1428    235    -84       C  
ATOM    400  CG  ASN A  67     -25.718 -23.518   8.080  1.00113.07           C  
ANISOU  400  CG  ASN A  67    11506  15924  15530   1360    365    -99       C  
ATOM    401  OD1 ASN A  67     -26.478 -22.548   8.164  1.00107.70           O  
ANISOU  401  OD1 ASN A  67    10895  15140  14887   1242    528    -62       O  
ATOM    402  ND2 ASN A  67     -25.534 -24.338   9.112  1.00105.67           N  
ANISOU  402  ND2 ASN A  67    10467  15058  14624   1442    304   -150       N  
ATOM    403  N   LEU A  68     -24.536 -24.574   3.675  1.00 88.31           N  
ANISOU  403  N   LEU A  68     8449  12962  12144   1570    -61   -213       N  
ATOM    404  CA  LEU A  68     -23.659 -24.697   2.502  1.00 87.86           C  
ANISOU  404  CA  LEU A  68     8515  12923  11946   1634   -144   -173       C  
ATOM    405  C   LEU A  68     -24.194 -23.943   1.281  1.00 92.79           C  
ANISOU  405  C   LEU A  68     9142  13647  12466   1791   -332   -243       C  
ATOM    406  O   LEU A  68     -23.400 -23.433   0.488  1.00 92.10           O  
ANISOU  406  O   LEU A  68     9223  13560  12212   1875   -379   -154       O  
ATOM    407  CB  LEU A  68     -23.362 -26.166   2.163  1.00 88.20           C  
ANISOU  407  CB  LEU A  68     8551  12923  12038   1533    -93   -245       C  
ATOM    408  CG  LEU A  68     -22.245 -26.832   2.970  1.00 91.81           C  
ANISOU  408  CG  LEU A  68     9119  13266  12501   1450     54   -124       C  
ATOM    409  CD1 LEU A  68     -22.379 -28.337   2.939  1.00 92.77           C  
ANISOU  409  CD1 LEU A  68     9215  13316  12717   1340    130   -221       C  
ATOM    410  CD2 LEU A  68     -20.864 -26.427   2.460  1.00 93.38           C  
ANISOU  410  CD2 LEU A  68     9463  13462  12555   1517     36     -4       C  
ATOM    411  N   LYS A  69     -25.532 -23.855   1.146  1.00 90.78           N  
ANISOU  411  N   LYS A  69     8711  13476  12305   1838   -435   -411       N  
ATOM    412  CA  LYS A  69     -26.191 -23.112   0.073  1.00 92.11           C  
ANISOU  412  CA  LYS A  69     8879  13747  12372   2029   -650   -498       C  
ATOM    413  C   LYS A  69     -26.139 -21.611   0.373  1.00 95.81           C  
ANISOU  413  C   LYS A  69     9459  14200  12743   2167   -679   -366       C  
ATOM    414  O   LYS A  69     -26.004 -20.811  -0.553  1.00 96.13           O  
ANISOU  414  O   LYS A  69     9665  14260  12601   2337   -809   -322       O  
ATOM    415  CB  LYS A  69     -27.644 -23.574  -0.105  1.00 96.69           C  
ANISOU  415  CB  LYS A  69     9191  14434  13112   2039   -761   -762       C  
ATOM    416  N   LEU A  70     -26.234 -21.239   1.670  1.00 91.53           N  
ANISOU  416  N   LEU A  70     8856  13610  12311   2091   -545   -303       N  
ATOM    417  CA  LEU A  70     -26.190 -19.859   2.171  1.00 90.97           C  
ANISOU  417  CA  LEU A  70     8878  13508  12178   2190   -537   -185       C  
ATOM    418  C   LEU A  70     -24.804 -19.226   1.966  1.00 93.15           C  
ANISOU  418  C   LEU A  70     9421  13699  12272   2201   -467     19       C  
ATOM    419  O   LEU A  70     -24.720 -18.026   1.695  1.00 93.02           O  
ANISOU  419  O   LEU A  70     9557  13658  12129   2335   -512     98       O  
ATOM    420  CB  LEU A  70     -26.578 -19.832   3.666  1.00 90.47           C  
ANISOU  420  CB  LEU A  70     8682  13409  12284   2070   -384   -184       C  
ATOM    421  CG  LEU A  70     -26.788 -18.466   4.327  1.00 95.15           C  
ANISOU  421  CG  LEU A  70     9323  13976  12855   2162   -368   -104       C  
ATOM    422  CD1 LEU A  70     -28.243 -18.028   4.238  1.00 97.34           C  
ANISOU  422  CD1 LEU A  70     9408  14342  13235   2293   -495   -281       C  
ATOM    423  CD2 LEU A  70     -26.351 -18.498   5.778  1.00 96.26           C  
ANISOU  423  CD2 LEU A  70     9468  14036  13071   2006   -165     -9       C  
ATOM    424  N   PHE A  71     -23.729 -20.030   2.106  1.00 88.19           N  
ANISOU  424  N   PHE A  71     8849  13020  11638   2061   -347     86       N  
ATOM    425  CA  PHE A  71     -22.350 -19.565   1.946  1.00 86.85           C  
ANISOU  425  CA  PHE A  71     8885  12782  11332   2041   -258    235       C  
ATOM    426  C   PHE A  71     -21.989 -19.256   0.496  1.00 91.38           C  
ANISOU  426  C   PHE A  71     9642  13361  11717   2149   -343    244       C  
ATOM    427  O   PHE A  71     -22.506 -19.890  -0.428  1.00 92.09           O  
ANISOU  427  O   PHE A  71     9696  13510  11783   2204   -465    135       O  
ATOM    428  CB  PHE A  71     -21.342 -20.568   2.543  1.00 87.37           C  
ANISOU  428  CB  PHE A  71     8929  12804  11463   1885   -125    273       C  
ATOM    429  CG  PHE A  71     -21.427 -20.825   4.032  1.00 88.11           C  
ANISOU  429  CG  PHE A  71     8926  12862  11689   1785    -18    298       C  
ATOM    430  CD1 PHE A  71     -21.727 -19.795   4.919  1.00 90.94           C  
ANISOU  430  CD1 PHE A  71     9284  13205  12065   1806     18    351       C  
ATOM    431  CD2 PHE A  71     -21.138 -22.080   4.554  1.00 89.90           C  
ANISOU  431  CD2 PHE A  71     9099  13055  12004   1677     55    277       C  
ATOM    432  CE1 PHE A  71     -21.791 -20.032   6.295  1.00 91.25           C  
ANISOU  432  CE1 PHE A  71     9265  13205  12201   1716    122    374       C  
ATOM    433  CE2 PHE A  71     -21.201 -22.315   5.930  1.00 92.24           C  
ANISOU  433  CE2 PHE A  71     9361  13300  12387   1598    159    310       C  
ATOM    434  CZ  PHE A  71     -21.523 -21.289   6.790  1.00 90.08           C  
ANISOU  434  CZ  PHE A  71     9085  13020  12121   1616    192    357       C  
ATOM    435  N   ARG A  72     -21.095 -18.269   0.311  1.00 87.38           N  
ANISOU  435  N   ARG A  72     9346  12784  11071   2171   -263    365       N  
ATOM    436  CA  ARG A  72     -20.572 -17.814  -0.977  1.00 88.03           C  
ANISOU  436  CA  ARG A  72     9671  12830  10945   2252   -281    400       C  
ATOM    437  C   ARG A  72     -19.179 -17.223  -0.732  1.00 90.50           C  
ANISOU  437  C   ARG A  72    10135  13053  11197   2149    -84    508       C  
ATOM    438  O   ARG A  72     -18.996 -16.002  -0.746  1.00 90.57           O  
ANISOU  438  O   ARG A  72    10322  12988  11104   2198    -26    587       O  
ATOM    439  CB  ARG A  72     -21.526 -16.797  -1.636  1.00 90.23           C  
ANISOU  439  CB  ARG A  72    10085  13110  11088   2465   -432    394       C  
ATOM    440  N   HIS A  73     -18.206 -18.108  -0.455  1.00 85.50           N  
ANISOU  440  N   HIS A  73     9420  12424  10643   2006     21    496       N  
ATOM    441  CA  HIS A  73     -16.827 -17.725  -0.156  1.00 84.44           C  
ANISOU  441  CA  HIS A  73     9360  12231  10493   1894    200    548       C  
ATOM    442  C   HIS A  73     -15.816 -18.450  -1.058  1.00 87.98           C  
ANISOU  442  C   HIS A  73     9866  12675  10887   1830    274    505       C  
ATOM    443  O   HIS A  73     -15.970 -19.654  -1.283  1.00 87.37           O  
ANISOU  443  O   HIS A  73     9676  12648  10873   1818    207    438       O  
ATOM    444  CB  HIS A  73     -16.517 -17.983   1.326  1.00 83.81           C  
ANISOU  444  CB  HIS A  73     9099  12165  10581   1798    258    558       C  
ATOM    445  CG  HIS A  73     -15.315 -17.247   1.825  1.00 86.83           C  
ANISOU  445  CG  HIS A  73     9534  12501  10956   1709    413    591       C  
ATOM    446  ND1 HIS A  73     -14.070 -17.844   1.867  1.00 88.28           N  
ANISOU  446  ND1 HIS A  73     9664  12696  11183   1614    504    545       N  
ATOM    447  CD2 HIS A  73     -15.203 -15.969   2.254  1.00 88.71           C  
ANISOU  447  CD2 HIS A  73     9866  12684  11155   1703    490    643       C  
ATOM    448  CE1 HIS A  73     -13.246 -16.921   2.336  1.00 87.71           C  
ANISOU  448  CE1 HIS A  73     9631  12588  11107   1546    629    553       C  
ATOM    449  NE2 HIS A  73     -13.883 -15.778   2.586  1.00 88.27           N  
ANISOU  449  NE2 HIS A  73     9800  12612  11126   1587    634    616       N  
ATOM    450  N   PRO A  74     -14.757 -17.754  -1.554  1.00 84.60           N  
ANISOU  450  N   PRO A  74     9611  12180  10354   1775    433    527       N  
ATOM    451  CA  PRO A  74     -13.774 -18.432  -2.420  1.00 84.68           C  
ANISOU  451  CA  PRO A  74     9666  12186  10322   1706    526    466       C  
ATOM    452  C   PRO A  74     -12.850 -19.428  -1.707  1.00 86.85           C  
ANISOU  452  C   PRO A  74     9724  12507  10768   1602    581    402       C  
ATOM    453  O   PRO A  74     -12.085 -20.122  -2.378  1.00 86.90           O  
ANISOU  453  O   PRO A  74     9733  12519  10766   1557    645    333       O  
ATOM    454  CB  PRO A  74     -12.990 -17.270  -3.034  1.00 87.62           C  
ANISOU  454  CB  PRO A  74    10289  12458  10544   1662    713    497       C  
ATOM    455  CG  PRO A  74     -13.072 -16.192  -2.021  1.00 91.62           C  
ANISOU  455  CG  PRO A  74    10787  12927  11099   1645    760    556       C  
ATOM    456  CD  PRO A  74     -14.430 -16.320  -1.396  1.00 86.54           C  
ANISOU  456  CD  PRO A  74    10027  12338  10517   1762    557    593       C  
ATOM    457  N   HIS A  75     -12.915 -19.500  -0.362  1.00 81.67           N  
ANISOU  457  N   HIS A  75     8898  11878  10255   1579    553    419       N  
ATOM    458  CA  HIS A  75     -12.085 -20.411   0.430  1.00 80.47           C  
ANISOU  458  CA  HIS A  75     8567  11762  10247   1521    575    364       C  
ATOM    459  C   HIS A  75     -12.925 -21.418   1.244  1.00 82.95           C  
ANISOU  459  C   HIS A  75     8744  12104  10670   1561    445    374       C  
ATOM    460  O   HIS A  75     -12.482 -21.925   2.279  1.00 81.88           O  
ANISOU  460  O   HIS A  75     8496  11977  10638   1543    445    364       O  
ATOM    461  CB  HIS A  75     -11.083 -19.623   1.292  1.00 81.01           C  
ANISOU  461  CB  HIS A  75     8590  11824  10366   1450    688    351       C  
ATOM    462  CG  HIS A  75     -10.187 -18.738   0.480  1.00 85.42           C  
ANISOU  462  CG  HIS A  75     9279  12338  10837   1375    861    312       C  
ATOM    463  ND1 HIS A  75      -9.290 -19.263  -0.436  1.00 87.96           N  
ANISOU  463  ND1 HIS A  75     9615  12664  11144   1325    958    220       N  
ATOM    464  CD2 HIS A  75     -10.100 -17.388   0.451  1.00 87.68           C  
ANISOU  464  CD2 HIS A  75     9705  12562  11047   1334    974    348       C  
ATOM    465  CE1 HIS A  75      -8.692 -18.221  -0.989  1.00 88.44           C  
ANISOU  465  CE1 HIS A  75     9824  12662  11118   1244   1140    200       C  
ATOM    466  NE2 HIS A  75      -9.137 -17.073  -0.479  1.00 88.68           N  
ANISOU  466  NE2 HIS A  75     9942  12643  11107   1245   1158    277       N  
ATOM    467  N   ILE A  76     -14.128 -21.731   0.725  1.00 79.39           N  
ANISOU  467  N   ILE A  76     8314  11662  10189   1618    341    377       N  
ATOM    468  CA  ILE A  76     -15.100 -22.688   1.262  1.00 78.73           C  
ANISOU  468  CA  ILE A  76     8117  11592  10205   1632    247    359       C  
ATOM    469  C   ILE A  76     -15.643 -23.501   0.075  1.00 83.16           C  
ANISOU  469  C   ILE A  76     8697  12173  10729   1660    175    285       C  
ATOM    470  O   ILE A  76     -15.939 -22.917  -0.972  1.00 83.53           O  
ANISOU  470  O   ILE A  76     8856  12232  10647   1713    137    278       O  
ATOM    471  CB  ILE A  76     -16.216 -21.955   2.077  1.00 81.57           C  
ANISOU  471  CB  ILE A  76     8442  11955  10597   1662    199    405       C  
ATOM    472  CG1 ILE A  76     -15.712 -21.595   3.493  1.00 81.13           C  
ANISOU  472  CG1 ILE A  76     8341  11878  10607   1621    265    459       C  
ATOM    473  CG2 ILE A  76     -17.524 -22.771   2.157  1.00 82.74           C  
ANISOU  473  CG2 ILE A  76     8490  12122  10826   1674    112    346       C  
ATOM    474  CD1 ILE A  76     -16.465 -20.455   4.210  1.00 88.24           C  
ANISOU  474  CD1 ILE A  76     9248  12773  11506   1644    260    512       C  
ATOM    475  N   ILE A  77     -15.748 -24.843   0.232  1.00 79.57           N  
ANISOU  475  N   ILE A  77     8155  11710  10370   1629    158    227       N  
ATOM    476  CA  ILE A  77     -16.255 -25.761  -0.798  1.00 80.20           C  
ANISOU  476  CA  ILE A  77     8232  11806  10435   1637     95    132       C  
ATOM    477  C   ILE A  77     -17.685 -25.369  -1.207  1.00 84.71           C  
ANISOU  477  C   ILE A  77     8782  12427  10979   1692    -27     88       C  
ATOM    478  O   ILE A  77     -18.614 -25.451  -0.399  1.00 84.20           O  
ANISOU  478  O   ILE A  77     8606  12367  11019   1677    -56     72       O  
ATOM    479  CB  ILE A  77     -16.098 -27.260  -0.376  1.00 83.26           C  
ANISOU  479  CB  ILE A  77     8543  12147  10944   1584    124     79       C  
ATOM    480  CG1 ILE A  77     -14.603 -27.687  -0.265  1.00 83.32           C  
ANISOU  480  CG1 ILE A  77     8578  12121  10961   1574    212     90       C  
ATOM    481  CG2 ILE A  77     -16.902 -28.223  -1.274  1.00 85.10           C  
ANISOU  481  CG2 ILE A  77     8749  12393  11191   1572     59    -41       C  
ATOM    482  CD1 ILE A  77     -13.748 -27.764  -1.604  1.00 90.99           C  
ANISOU  482  CD1 ILE A  77     9625  13112  11836   1581    247     32       C  
ATOM    483  N   LYS A  78     -17.826 -24.887  -2.452  1.00 82.11           N  
ANISOU  483  N   LYS A  78     8567  12132  10499   1765    -96     60       N  
ATOM    484  CA  LYS A  78     -19.093 -24.428  -3.022  1.00 83.01           C  
ANISOU  484  CA  LYS A  78     8680  12307  10554   1865   -250      0       C  
ATOM    485  C   LYS A  78     -20.006 -25.600  -3.356  1.00 87.17           C  
ANISOU  485  C   LYS A  78     9065  12880  11174   1843   -343   -156       C  
ATOM    486  O   LYS A  78     -19.596 -26.510  -4.076  1.00 87.05           O  
ANISOU  486  O   LYS A  78     9077  12858  11138   1806   -330   -222       O  
ATOM    487  CB  LYS A  78     -18.849 -23.564  -4.275  1.00 86.84           C  
ANISOU  487  CB  LYS A  78     9389  12796  10811   1973   -294     26       C  
ATOM    488  CG  LYS A  78     -18.148 -22.239  -3.997  1.00103.18           C  
ANISOU  488  CG  LYS A  78    11615  14805  12784   1990   -190    162       C  
ATOM    489  CD  LYS A  78     -17.806 -21.507  -5.290  1.00115.80           C  
ANISOU  489  CD  LYS A  78    13493  16370  14137   2077   -188    190       C  
ATOM    490  N   LEU A  79     -21.241 -25.576  -2.830  1.00 83.89           N  
ANISOU  490  N   LEU A  79     8491  12509  10873   1855   -423   -233       N  
ATOM    491  CA  LEU A  79     -22.239 -26.612  -3.085  1.00 84.78           C  
ANISOU  491  CA  LEU A  79     8439  12671  11102   1814   -498   -419       C  
ATOM    492  C   LEU A  79     -23.046 -26.233  -4.330  1.00 90.20           C  
ANISOU  492  C   LEU A  79     9146  13462  11663   1960   -706   -543       C  
ATOM    493  O   LEU A  79     -23.710 -25.194  -4.340  1.00 90.51           O  
ANISOU  493  O   LEU A  79     9185  13553  11650   2091   -821   -539       O  
ATOM    494  CB  LEU A  79     -23.143 -26.810  -1.848  1.00 84.73           C  
ANISOU  494  CB  LEU A  79     8238  12656  11300   1731   -445   -469       C  
ATOM    495  CG  LEU A  79     -24.355 -27.744  -1.977  1.00 91.08           C  
ANISOU  495  CG  LEU A  79     8837  13511  12259   1664   -497   -699       C  
ATOM    496  CD1 LEU A  79     -23.936 -29.204  -2.132  1.00 91.36           C  
ANISOU  496  CD1 LEU A  79     8874  13475  12365   1528   -395   -765       C  
ATOM    497  CD2 LEU A  79     -25.261 -27.600  -0.783  1.00 93.79           C  
ANISOU  497  CD2 LEU A  79     9011  13845  12779   1594   -426   -744       C  
ATOM    498  N   TYR A  80     -22.961 -27.065  -5.385  1.00 87.41           N  
ANISOU  498  N   TYR A  80     8827  13135  11248   1956   -764   -656       N  
ATOM    499  CA  TYR A  80     -23.650 -26.822  -6.652  1.00 89.14           C  
ANISOU  499  CA  TYR A  80     9094  13457  11317   2109   -982   -789       C  
ATOM    500  C   TYR A  80     -25.129 -27.209  -6.611  1.00 94.28           C  
ANISOU  500  C   TYR A  80     9483  14219  12120   2125  -1136  -1028       C  
ATOM    501  O   TYR A  80     -25.980 -26.347  -6.835  1.00 95.26           O  
ANISOU  501  O   TYR A  80     9574  14432  12189   2294  -1318  -1089       O  
ATOM    502  CB  TYR A  80     -22.927 -27.503  -7.830  1.00 90.99           C  
ANISOU  502  CB  TYR A  80     9488  13678  11405   2101   -979   -823       C  
ATOM    503  CG  TYR A  80     -21.469 -27.124  -8.002  1.00 91.62           C  
ANISOU  503  CG  TYR A  80     9809  13659  11341   2081   -817   -631       C  
ATOM    504  CD1 TYR A  80     -21.081 -25.790  -8.107  1.00 93.44           C  
ANISOU  504  CD1 TYR A  80    10242  13860  11402   2188   -806   -478       C  
ATOM    505  CD2 TYR A  80     -20.489 -28.100  -8.146  1.00 91.76           C  
ANISOU  505  CD2 TYR A  80     9859  13613  11392   1958   -670   -627       C  
ATOM    506  CE1 TYR A  80     -19.744 -25.437  -8.284  1.00 93.40           C  
ANISOU  506  CE1 TYR A  80    10439  13765  11283   2144   -631   -338       C  
ATOM    507  CE2 TYR A  80     -19.152 -27.760  -8.345  1.00 91.88           C  
ANISOU  507  CE2 TYR A  80    10061  13553  11295   1937   -517   -493       C  
ATOM    508  CZ  TYR A  80     -18.782 -26.427  -8.407  1.00 99.28           C  
ANISOU  508  CZ  TYR A  80    11176  14466  12081   2018   -490   -357       C  
ATOM    509  OH  TYR A  80     -17.464 -26.089  -8.597  1.00100.16           O  
ANISOU  509  OH  TYR A  80    11451  14502  12103   1970   -311   -257       O  
ATOM    510  N   GLN A  81     -25.434 -28.495  -6.332  1.00 90.67           N  
ANISOU  510  N   GLN A  81     8841  13752  11858   1954  -1058  -1179       N  
ATOM    511  CA  GLN A  81     -26.806 -29.012  -6.271  1.00 92.23           C  
ANISOU  511  CA  GLN A  81     8757  14048  12237   1918  -1160  -1452       C  
ATOM    512  C   GLN A  81     -26.927 -30.222  -5.341  1.00 95.13           C  
ANISOU  512  C   GLN A  81     8962  14323  12858   1671   -943  -1525       C  
ATOM    513  O   GLN A  81     -25.992 -31.018  -5.230  1.00 93.54           O  
ANISOU  513  O   GLN A  81     8880  14004  12657   1555   -779  -1428       O  
ATOM    514  CB  GLN A  81     -27.319 -29.362  -7.686  1.00 96.00           C  
ANISOU  514  CB  GLN A  81     9224  14648  12603   2023  -1387  -1673       C  
ATOM    515  CG  GLN A  81     -28.824 -29.645  -7.771  1.00115.79           C  
ANISOU  515  CG  GLN A  81    11412  17298  15286   2030  -1546  -2001       C  
ATOM    516  CD  GLN A  81     -29.419 -29.359  -9.127  1.00139.62           C  
ANISOU  516  CD  GLN A  81    14447  20478  18126   2256  -1868  -2188       C  
ATOM    517  OE1 GLN A  81     -29.027 -29.935 -10.149  1.00136.54           O  
ANISOU  517  OE1 GLN A  81    14188  20102  17588   2276  -1937  -2246       O  
ATOM    518  NE2 GLN A  81     -30.423 -28.496  -9.155  1.00133.80           N  
ANISOU  518  NE2 GLN A  81    13570  19868  17401   2442  -2080  -2307       N  
ATOM    519  N   VAL A  82     -28.093 -30.354  -4.684  1.00 92.47           N  
ANISOU  519  N   VAL A  82     8365  14034  12734   1597   -934  -1709       N  
ATOM    520  CA  VAL A  82     -28.421 -31.469  -3.799  1.00 92.29           C  
ANISOU  520  CA  VAL A  82     8202  13912  12953   1353   -710  -1812       C  
ATOM    521  C   VAL A  82     -29.456 -32.336  -4.529  1.00 98.61           C  
ANISOU  521  C   VAL A  82     8776  14810  13881   1283   -802  -2165       C  
ATOM    522  O   VAL A  82     -30.634 -31.974  -4.592  1.00100.10           O  
ANISOU  522  O   VAL A  82     8720  15139  14176   1333   -938  -2394       O  
ATOM    523  CB  VAL A  82     -28.901 -31.014  -2.389  1.00 95.61           C  
ANISOU  523  CB  VAL A  82     8515  14282  13531   1278   -561  -1759       C  
ATOM    524  CG1 VAL A  82     -29.136 -32.212  -1.470  1.00 95.77           C  
ANISOU  524  CG1 VAL A  82     8467  14157  13765   1018   -288  -1841       C  
ATOM    525  CG2 VAL A  82     -27.912 -30.046  -1.752  1.00 92.99           C  
ANISOU  525  CG2 VAL A  82     8395  13878  13059   1368   -507  -1437       C  
ATOM    526  N   ILE A  83     -28.998 -33.451  -5.123  1.00 95.44           N  
ANISOU  526  N   ILE A  83     8450  14344  13468   1179   -741  -2227       N  
ATOM    527  CA  ILE A  83     -29.856 -34.384  -5.857  1.00 97.95           C  
ANISOU  527  CA  ILE A  83     8572  14741  13903   1087   -810  -2573       C  
ATOM    528  C   ILE A  83     -30.441 -35.401  -4.874  1.00103.08           C  
ANISOU  528  C   ILE A  83     9063  15266  14837    807   -536  -2726       C  
ATOM    529  O   ILE A  83     -29.692 -36.106  -4.197  1.00101.31           O  
ANISOU  529  O   ILE A  83     9010  14840  14644    665   -285  -2562       O  
ATOM    530  CB  ILE A  83     -29.116 -35.035  -7.066  1.00101.20           C  
ANISOU  530  CB  ILE A  83     9158  15146  14146   1123   -886  -2582       C  
ATOM    531  CG1 ILE A  83     -28.716 -33.962  -8.109  1.00101.41           C  
ANISOU  531  CG1 ILE A  83     9351  15299  13879   1399  -1153  -2471       C  
ATOM    532  CG2 ILE A  83     -29.965 -36.143  -7.718  1.00104.67           C  
ANISOU  532  CG2 ILE A  83     9396  15645  14730    988   -921  -2956       C  
ATOM    533  CD1 ILE A  83     -27.503 -34.305  -8.982  1.00108.12           C  
ANISOU  533  CD1 ILE A  83    10481  16084  14515   1440  -1140  -2333       C  
ATOM    534  N   SER A  84     -31.778 -35.454  -4.784  1.00102.44           N  
ANISOU  534  N   SER A  84     8663  15299  14958    736   -579  -3048       N  
ATOM    535  CA  SER A  84     -32.479 -36.361  -3.880  1.00103.79           C  
ANISOU  535  CA  SER A  84     8672  15353  15412    448   -292  -3236       C  
ATOM    536  C   SER A  84     -33.082 -37.552  -4.617  1.00111.04           C  
ANISOU  536  C   SER A  84     9427  16294  16470    280   -276  -3598       C  
ATOM    537  O   SER A  84     -33.776 -37.375  -5.619  1.00112.75           O  
ANISOU  537  O   SER A  84     9437  16726  16679    389   -550  -3874       O  
ATOM    538  CB  SER A  84     -33.556 -35.612  -3.099  1.00108.26           C  
ANISOU  538  CB  SER A  84     8974  16010  16151    438   -280  -3370       C  
ATOM    539  OG  SER A  84     -34.223 -36.459  -2.177  1.00118.29           O  
ANISOU  539  OG  SER A  84    10108  17147  17691    138     42  -3556       O  
ATOM    540  N   THR A  85     -32.787 -38.768  -4.126  1.00108.24           N  
ANISOU  540  N   THR A  85     9187  15710  16229     26     39  -3597       N  
ATOM    541  CA  THR A  85     -33.317 -40.037  -4.640  1.00111.00           C  
ANISOU  541  CA  THR A  85     9412  16022  16742   -192    138  -3937       C  
ATOM    542  C   THR A  85     -34.065 -40.724  -3.471  1.00117.06           C  
ANISOU  542  C   THR A  85    10070  16614  17795   -508    515  -4094       C  
ATOM    543  O   THR A  85     -33.797 -40.362  -2.321  1.00115.01           O  
ANISOU  543  O   THR A  85     9946  16218  17536   -532    704  -3848       O  
ATOM    544  CB  THR A  85     -32.218 -40.918  -5.296  1.00118.51           C  
ANISOU  544  CB  THR A  85    10652  16836  17541   -195    175  -3801       C  
ATOM    545  OG1 THR A  85     -31.355 -41.475  -4.308  1.00116.67           O  
ANISOU  545  OG1 THR A  85    10712  16315  17302   -306    486  -3518       O  
ATOM    546  CG2 THR A  85     -31.421 -40.192  -6.380  1.00115.61           C  
ANISOU  546  CG2 THR A  85    10426  16620  16880    100   -147  -3628       C  
ATOM    547  N   PRO A  86     -35.004 -41.680  -3.699  1.00117.51           N  
ANISOU  547  N   PRO A  86     9894  16663  18091   -759    647  -4506       N  
ATOM    548  CA  PRO A  86     -35.726 -42.281  -2.557  1.00119.36           C  
ANISOU  548  CA  PRO A  86    10049  16709  18594  -1079   1049  -4659       C  
ATOM    549  C   PRO A  86     -34.874 -43.078  -1.567  1.00122.41           C  
ANISOU  549  C   PRO A  86    10845  16726  18939  -1235   1434  -4355       C  
ATOM    550  O   PRO A  86     -35.265 -43.209  -0.406  1.00122.62           O  
ANISOU  550  O   PRO A  86    10908  16583  19099  -1420   1753  -4340       O  
ATOM    551  CB  PRO A  86     -36.787 -43.165  -3.225  1.00125.11           C  
ANISOU  551  CB  PRO A  86    10452  17516  19569  -1308   1087  -5186       C  
ATOM    552  CG  PRO A  86     -36.872 -42.685  -4.634  1.00129.91           C  
ANISOU  552  CG  PRO A  86    10884  18432  20043  -1051    623  -5336       C  
ATOM    553  CD  PRO A  86     -35.497 -42.228  -4.978  1.00121.71           C  
ANISOU  553  CD  PRO A  86    10222  17357  18667   -777    450  -4876       C  
ATOM    554  N   THR A  87     -33.718 -43.598  -2.017  1.00117.72           N  
ANISOU  554  N   THR A  87    10569  16007  18153  -1144   1403  -4120       N  
ATOM    555  CA  THR A  87     -32.811 -44.399  -1.192  1.00116.65           C  
ANISOU  555  CA  THR A  87    10845  15526  17952  -1235   1717  -3833       C  
ATOM    556  C   THR A  87     -31.777 -43.543  -0.441  1.00117.44           C  
ANISOU  556  C   THR A  87    11211  15577  17835  -1008   1663  -3375       C  
ATOM    557  O   THR A  87     -31.550 -43.789   0.745  1.00116.67           O  
ANISOU  557  O   THR A  87    11347  15238  17745  -1099   1944  -3192       O  
ATOM    558  CB  THR A  87     -32.158 -45.514  -2.034  1.00125.67           C  
ANISOU  558  CB  THR A  87    12170  16548  19032  -1265   1732  -3864       C  
ATOM    559  OG1 THR A  87     -33.167 -46.384  -2.552  1.00128.48           O  
ANISOU  559  OG1 THR A  87    12229  17019  19569  -1437   1700  -4314       O  
ATOM    560  CG2 THR A  87     -31.132 -46.328  -1.249  1.00124.64           C  
ANISOU  560  CG2 THR A  87    12437  16026  18895  -1407   2103  -3676       C  
ATOM    561  N   ASP A  88     -31.138 -42.564  -1.126  1.00112.01           N  
ANISOU  561  N   ASP A  88    10509  15104  16947   -718   1315  -3200       N  
ATOM    562  CA  ASP A  88     -30.094 -41.716  -0.527  1.00108.84           C  
ANISOU  562  CA  ASP A  88    10337  14676  16343   -503   1246  -2795       C  
ATOM    563  C   ASP A  88     -29.982 -40.300  -1.121  1.00110.83           C  
ANISOU  563  C   ASP A  88    10450  15210  16451   -240    894  -2710       C  
ATOM    564  O   ASP A  88     -30.401 -40.063  -2.251  1.00111.30           O  
ANISOU  564  O   ASP A  88    10313  15480  16495   -160    649  -2912       O  
ATOM    565  CB  ASP A  88     -28.716 -42.420  -0.573  1.00109.43           C  
ANISOU  565  CB  ASP A  88    10765  14555  16259   -429   1309  -2540       C  
ATOM    566  CG  ASP A  88     -28.151 -42.667  -1.960  1.00122.58           C  
ANISOU  566  CG  ASP A  88    12450  16186  17940   -492   1294  -2721       C  
ATOM    567  OD1 ASP A  88     -28.729 -42.148  -2.938  1.00123.43           O  
ANISOU  567  OD1 ASP A  88    12411  16514  17972   -372   1023  -2831       O  
ATOM    568  OD2 ASP A  88     -27.126 -43.375  -2.065  1.00130.27           O  
ANISOU  568  OD2 ASP A  88    13608  16901  18989   -657   1559  -2752       O  
ATOM    569  N   PHE A  89     -29.398 -39.366  -0.345  1.00105.02           N  
ANISOU  569  N   PHE A  89     9842  14465  15597   -100    875  -2412       N  
ATOM    570  CA  PHE A  89     -29.161 -37.977  -0.746  1.00103.14           C  
ANISOU  570  CA  PHE A  89     9543  14441  15206    145    591  -2282       C  
ATOM    571  C   PHE A  89     -27.777 -37.835  -1.388  1.00104.55           C  
ANISOU  571  C   PHE A  89     9954  14615  15154    327    460  -2039       C  
ATOM    572  O   PHE A  89     -26.801 -38.393  -0.880  1.00102.97           O  
ANISOU  572  O   PHE A  89     9994  14229  14900    310    610  -1842       O  
ATOM    573  CB  PHE A  89     -29.263 -37.028   0.463  1.00103.83           C  
ANISOU  573  CB  PHE A  89     9642  14509  15300    178    666  -2109       C  
ATOM    574  CG  PHE A  89     -30.659 -36.660   0.907  1.00107.41           C  
ANISOU  574  CG  PHE A  89     9807  15052  15950     76    710  -2350       C  
ATOM    575  CD1 PHE A  89     -31.405 -35.720   0.204  1.00111.44           C  
ANISOU  575  CD1 PHE A  89    10059  15815  16469    219    440  -2515       C  
ATOM    576  CD2 PHE A  89     -31.202 -37.201   2.066  1.00110.82           C  
ANISOU  576  CD2 PHE A  89    10246  15311  16548   -147   1025  -2407       C  
ATOM    577  CE1 PHE A  89     -32.689 -35.362   0.629  1.00114.34           C  
ANISOU  577  CE1 PHE A  89    10132  16278  17034    143    472  -2761       C  
ATOM    578  CE2 PHE A  89     -32.484 -36.840   2.492  1.00115.60           C  
ANISOU  578  CE2 PHE A  89    10567  16005  17352   -252   1089  -2651       C  
ATOM    579  CZ  PHE A  89     -33.219 -35.922   1.771  1.00114.49           C  
ANISOU  579  CZ  PHE A  89    10127  16133  17242   -103    805  -2835       C  
ATOM    580  N   PHE A  90     -27.696 -37.079  -2.495  1.00100.53           N  
ANISOU  580  N   PHE A  90     9383  14307  14508    508    183  -2064       N  
ATOM    581  CA  PHE A  90     -26.453 -36.810  -3.221  1.00 98.51           C  
ANISOU  581  CA  PHE A  90     9330  14067  14032    674     65  -1866       C  
ATOM    582  C   PHE A  90     -26.138 -35.320  -3.147  1.00100.48           C  
ANISOU  582  C   PHE A  90     9613  14432  14133    867    -87  -1674       C  
ATOM    583  O   PHE A  90     -27.009 -34.497  -3.434  1.00100.92           O  
ANISOU  583  O   PHE A  90     9508  14646  14191    951   -252  -1786       O  
ATOM    584  CB  PHE A  90     -26.561 -37.256  -4.690  1.00101.70           C  
ANISOU  584  CB  PHE A  90     9696  14579  14368    711   -100  -2061       C  
ATOM    585  CG  PHE A  90     -26.643 -38.748  -4.908  1.00104.73           C  
ANISOU  585  CG  PHE A  90    10089  14833  14870    529     52  -2235       C  
ATOM    586  CD1 PHE A  90     -25.497 -39.494  -5.150  1.00106.96           C  
ANISOU  586  CD1 PHE A  90    10592  14976  15071    532    145  -2109       C  
ATOM    587  CD2 PHE A  90     -27.869 -39.401  -4.907  1.00109.37           C  
ANISOU  587  CD2 PHE A  90    10457  15438  15662    355    107  -2547       C  
ATOM    588  CE1 PHE A  90     -25.573 -40.873  -5.367  1.00109.43           C  
ANISOU  588  CE1 PHE A  90    10936  15152  15492    372    292  -2271       C  
ATOM    589  CE2 PHE A  90     -27.945 -40.781  -5.119  1.00113.79           C  
ANISOU  589  CE2 PHE A  90    11042  15858  16334    170    270  -2718       C  
ATOM    590  CZ  PHE A  90     -26.796 -41.508  -5.347  1.00110.95           C  
ANISOU  590  CZ  PHE A  90    10932  15345  15878    185    360  -2569       C  
ATOM    591  N   MET A  91     -24.905 -34.974  -2.750  1.00 94.79           N  
ANISOU  591  N   MET A  91     9097  13629  13289    943    -30  -1403       N  
ATOM    592  CA  MET A  91     -24.473 -33.582  -2.633  1.00 93.09           C  
ANISOU  592  CA  MET A  91     8942  13494  12933   1103   -135  -1215       C  
ATOM    593  C   MET A  91     -23.361 -33.258  -3.630  1.00 96.25           C  
ANISOU  593  C   MET A  91     9513  13929  13128   1232   -227  -1104       C  
ATOM    594  O   MET A  91     -22.189 -33.557  -3.378  1.00 94.71           O  
ANISOU  594  O   MET A  91     9466  13632  12887   1228   -120   -954       O  
ATOM    595  CB  MET A  91     -24.055 -33.246  -1.191  1.00 93.90           C  
ANISOU  595  CB  MET A  91     9113  13486  13078   1071     20  -1017       C  
ATOM    596  CG  MET A  91     -25.217 -33.086  -0.241  1.00 98.35           C  
ANISOU  596  CG  MET A  91     9519  14046  13802    979     95  -1107       C  
ATOM    597  SD  MET A  91     -24.682 -32.573   1.408  1.00100.85           S  
ANISOU  597  SD  MET A  91     9958  14241  14122    965    259   -865       S  
ATOM    598  CE  MET A  91     -24.700 -30.818   1.220  1.00 96.54           C  
ANISOU  598  CE  MET A  91     9378  13849  13454   1144     81   -764       C  
ATOM    599  N   VAL A  92     -23.737 -32.662  -4.774  1.00 93.75           N  
ANISOU  599  N   VAL A  92     9182  13754  12685   1353   -425  -1193       N  
ATOM    600  CA  VAL A  92     -22.794 -32.275  -5.826  1.00 93.25           C  
ANISOU  600  CA  VAL A  92     9306  13720  12404   1469   -498  -1106       C  
ATOM    601  C   VAL A  92     -22.134 -30.953  -5.415  1.00 95.69           C  
ANISOU  601  C   VAL A  92     9735  14028  12596   1572   -489   -884       C  
ATOM    602  O   VAL A  92     -22.809 -29.923  -5.332  1.00 95.55           O  
ANISOU  602  O   VAL A  92     9678  14087  12541   1668   -599   -876       O  
ATOM    603  CB  VAL A  92     -23.457 -32.225  -7.233  1.00 99.15           C  
ANISOU  603  CB  VAL A  92    10042  14599  13030   1565   -707  -1293       C  
ATOM    604  CG1 VAL A  92     -22.495 -31.681  -8.286  1.00 98.79           C  
ANISOU  604  CG1 VAL A  92    10238  14566  12729   1687   -755  -1186       C  
ATOM    605  CG2 VAL A  92     -23.975 -33.601  -7.646  1.00100.51           C  
ANISOU  605  CG2 VAL A  92    10096  14765  13327   1440   -695  -1528       C  
ATOM    606  N   MET A  93     -20.823 -31.001  -5.120  1.00 90.96           N  
ANISOU  606  N   MET A  93     9270  13338  11953   1551   -353   -724       N  
ATOM    607  CA  MET A  93     -20.056 -29.834  -4.678  1.00 89.55           C  
ANISOU  607  CA  MET A  93     9196  13145  11683   1615   -310   -534       C  
ATOM    608  C   MET A  93     -18.685 -29.701  -5.371  1.00 93.37           C  
ANISOU  608  C   MET A  93     9855  13598  12024   1642   -240   -453       C  
ATOM    609  O   MET A  93     -18.264 -30.598  -6.104  1.00 93.55           O  
ANISOU  609  O   MET A  93     9918  13600  12027   1611   -214   -531       O  
ATOM    610  CB  MET A  93     -19.927 -29.790  -3.137  1.00 90.56           C  
ANISOU  610  CB  MET A  93     9256  13200  11954   1547   -191   -430       C  
ATOM    611  CG  MET A  93     -19.417 -31.080  -2.506  1.00 93.94           C  
ANISOU  611  CG  MET A  93     9669  13517  12507   1444    -60   -439       C  
ATOM    612  SD  MET A  93     -19.327 -31.039  -0.698  1.00 97.08           S  
ANISOU  612  SD  MET A  93    10041  13818  13028   1390     65   -317       S  
ATOM    613  CE  MET A  93     -21.055 -31.153  -0.274  1.00 94.87           C  
ANISOU  613  CE  MET A  93     9599  13564  12883   1317     43   -450       C  
ATOM    614  N   GLU A  94     -18.017 -28.553  -5.138  1.00 89.38           N  
ANISOU  614  N   GLU A  94     9450  13085  11427   1690   -195   -313       N  
ATOM    615  CA  GLU A  94     -16.719 -28.147  -5.680  1.00 89.12           C  
ANISOU  615  CA  GLU A  94     9572  13022  11268   1700    -94   -243       C  
ATOM    616  C   GLU A  94     -15.608 -29.156  -5.393  1.00 92.73           C  
ANISOU  616  C   GLU A  94     9995  13416  11821   1625     35   -254       C  
ATOM    617  O   GLU A  94     -15.406 -29.543  -4.241  1.00 91.35           O  
ANISOU  617  O   GLU A  94     9722  13196  11789   1585     87   -214       O  
ATOM    618  CB  GLU A  94     -16.353 -26.755  -5.130  1.00 89.77           C  
ANISOU  618  CB  GLU A  94     9722  13093  11294   1731    -44   -109       C  
ATOM    619  CG  GLU A  94     -15.188 -26.064  -5.822  1.00100.94           C  
ANISOU  619  CG  GLU A  94    11316  14477  12561   1731     74    -60       C  
ATOM    620  CD  GLU A  94     -14.924 -24.642  -5.361  1.00121.42           C  
ANISOU  620  CD  GLU A  94    13994  17048  15094   1749    134     53       C  
ATOM    621  OE1 GLU A  94     -14.911 -24.398  -4.132  1.00114.29           O  
ANISOU  621  OE1 GLU A  94    12971  16137  14317   1719    157    109       O  
ATOM    622  OE2 GLU A  94     -14.705 -23.772  -6.235  1.00116.67           O  
ANISOU  622  OE2 GLU A  94    13602  16420  14305   1791    172     83       O  
ATOM    623  N   TYR A  95     -14.895 -29.577  -6.452  1.00 90.50           N  
ANISOU  623  N   TYR A  95     9808  13127  11450   1621     82   -315       N  
ATOM    624  CA  TYR A  95     -13.771 -30.506  -6.347  1.00 90.40           C  
ANISOU  624  CA  TYR A  95     9768  13060  11520   1575    199   -347       C  
ATOM    625  C   TYR A  95     -12.449 -29.746  -6.403  1.00 94.64           C  
ANISOU  625  C   TYR A  95    10369  13588  12001   1569    332   -296       C  
ATOM    626  O   TYR A  95     -12.289 -28.838  -7.222  1.00 94.90           O  
ANISOU  626  O   TYR A  95    10546  13639  11873   1582    364   -279       O  
ATOM    627  CB  TYR A  95     -13.831 -31.603  -7.434  1.00 92.78           C  
ANISOU  627  CB  TYR A  95    10107  13354  11790   1561    186   -479       C  
ATOM    628  CG  TYR A  95     -12.571 -32.438  -7.543  1.00 94.63           C  
ANISOU  628  CG  TYR A  95    10337  13534  12085   1537    313   -524       C  
ATOM    629  CD1 TYR A  95     -12.256 -33.393  -6.580  1.00 96.14           C  
ANISOU  629  CD1 TYR A  95    10427  13654  12446   1527    348   -526       C  
ATOM    630  CD2 TYR A  95     -11.682 -32.260  -8.599  1.00 96.25           C  
ANISOU  630  CD2 TYR A  95    10654  13747  12170   1534    406   -571       C  
ATOM    631  CE1 TYR A  95     -11.085 -34.145  -6.661  1.00 97.33           C  
ANISOU  631  CE1 TYR A  95    10568  13757  12656   1539    445   -578       C  
ATOM    632  CE2 TYR A  95     -10.508 -33.007  -8.692  1.00 97.50           C  
ANISOU  632  CE2 TYR A  95    10781  13864  12402   1520    527   -636       C  
ATOM    633  CZ  TYR A  95     -10.214 -33.951  -7.722  1.00104.47           C  
ANISOU  633  CZ  TYR A  95    11541  14688  13464   1534    532   -643       C  
ATOM    634  OH  TYR A  95      -9.061 -34.694  -7.811  1.00105.83           O  
ANISOU  634  OH  TYR A  95    11677  14821  13712   1552    630   -720       O  
ATOM    635  N   VAL A  96     -11.501 -30.139  -5.541  1.00 90.99           N  
ANISOU  635  N   VAL A  96     9810  13092  11669   1553    412   -287       N  
ATOM    636  CA  VAL A  96     -10.167 -29.543  -5.467  1.00 91.03           C  
ANISOU  636  CA  VAL A  96     9817  13101  11671   1535    543   -286       C  
ATOM    637  C   VAL A  96      -9.094 -30.621  -5.685  1.00 96.20           C  
ANISOU  637  C   VAL A  96    10411  13730  12411   1536    621   -392       C  
ATOM    638  O   VAL A  96      -8.965 -31.551  -4.886  1.00 95.47           O  
ANISOU  638  O   VAL A  96    10223  13601  12451   1573    583   -404       O  
ATOM    639  CB  VAL A  96      -9.943 -28.679  -4.198  1.00 93.91           C  
ANISOU  639  CB  VAL A  96    10106  13475  12101   1537    551   -198       C  
ATOM    640  CG1 VAL A  96     -10.872 -27.470  -4.191  1.00 93.59           C  
ANISOU  640  CG1 VAL A  96    10171  13453  11936   1530    542   -116       C  
ATOM    641  CG2 VAL A  96     -10.108 -29.495  -2.919  1.00 92.91           C  
ANISOU  641  CG2 VAL A  96     9876  13321  12104   1568    459   -154       C  
ATOM    642  N   SER A  97      -8.372 -30.510  -6.813  1.00 94.45           N  
ANISOU  642  N   SER A  97    10271  13516  12101   1503    736   -474       N  
ATOM    643  CA  SER A  97      -7.344 -31.449  -7.277  1.00 95.53           C  
ANISOU  643  CA  SER A  97    10361  13635  12303   1503    830   -602       C  
ATOM    644  C   SER A  97      -6.124 -31.614  -6.361  1.00100.10           C  
ANISOU  644  C   SER A  97    10771  14220  13042   1533    886   -653       C  
ATOM    645  O   SER A  97      -5.564 -32.710  -6.301  1.00100.29           O  
ANISOU  645  O   SER A  97    10718  14217  13171   1586    888   -742       O  
ATOM    646  CB  SER A  97      -6.884 -31.077  -8.683  1.00100.51           C  
ANISOU  646  CB  SER A  97    11136  14270  12781   1445    969   -677       C  
ATOM    647  OG  SER A  97      -6.424 -29.736  -8.739  1.00109.68           O  
ANISOU  647  OG  SER A  97    12365  15446  13863   1390   1087   -640       O  
ATOM    648  N   GLY A  98      -5.722 -30.538  -5.684  1.00 96.74           N  
ANISOU  648  N   GLY A  98    10292  13831  12633   1511    923   -612       N  
ATOM    649  CA  GLY A  98      -4.557 -30.504  -4.800  1.00 96.99           C  
ANISOU  649  CA  GLY A  98    10148  13895  12810   1544    957   -686       C  
ATOM    650  C   GLY A  98      -4.566 -31.446  -3.609  1.00100.87           C  
ANISOU  650  C   GLY A  98    10533  14362  13430   1665    815   -665       C  
ATOM    651  O   GLY A  98      -3.498 -31.847  -3.136  1.00101.27           O  
ANISOU  651  O   GLY A  98    10444  14435  13598   1739    819   -772       O  
ATOM    652  N   GLY A  99      -5.757 -31.788  -3.120  1.00 96.75           N  
ANISOU  652  N   GLY A  99    10084  13791  12885   1692    695   -541       N  
ATOM    653  CA  GLY A  99      -5.924 -32.686  -1.982  1.00 96.52           C  
ANISOU  653  CA  GLY A  99    10024  13703  12946   1797    584   -500       C  
ATOM    654  C   GLY A  99      -5.789 -32.010  -0.632  1.00100.14           C  
ANISOU  654  C   GLY A  99    10420  14188  13438   1840    522   -430       C  
ATOM    655  O   GLY A  99      -5.618 -30.790  -0.559  1.00 99.27           O  
ANISOU  655  O   GLY A  99    10276  14146  13294   1776    566   -416       O  
ATOM    656  N   GLU A 100      -5.868 -32.813   0.449  1.00 97.13           N  
ANISOU  656  N   GLU A 100    10052  13740  13112   1951    427   -388       N  
ATOM    657  CA  GLU A 100      -5.795 -32.368   1.845  1.00 96.72           C  
ANISOU  657  CA  GLU A 100     9978  13698  13075   2017    348   -319       C  
ATOM    658  C   GLU A 100      -4.474 -31.690   2.218  1.00101.67           C  
ANISOU  658  C   GLU A 100    10449  14428  13752   2065    347   -428       C  
ATOM    659  O   GLU A 100      -3.421 -32.050   1.688  1.00102.42           O  
ANISOU  659  O   GLU A 100    10443  14562  13911   2109    383   -578       O  
ATOM    660  CB  GLU A 100      -6.095 -33.532   2.801  1.00 98.54           C  
ANISOU  660  CB  GLU A 100    10310  13805  13327   2141    265   -261       C  
ATOM    661  N   LEU A 101      -4.548 -30.704   3.134  1.00 97.93           N  
ANISOU  661  N   LEU A 101     9946  14002  13259   2051    313   -373       N  
ATOM    662  CA  LEU A 101      -3.411 -29.933   3.645  1.00 98.56           C  
ANISOU  662  CA  LEU A 101     9867  14189  13392   2078    305   -491       C  
ATOM    663  C   LEU A 101      -2.478 -30.804   4.499  1.00104.20           C  
ANISOU  663  C   LEU A 101    10507  14908  14174   2284    172   -586       C  
ATOM    664  O   LEU A 101      -1.264 -30.596   4.468  1.00105.01           O  
ANISOU  664  O   LEU A 101    10426  15110  14361   2329    172   -770       O  
ATOM    665  CB  LEU A 101      -3.921 -28.705   4.437  1.00 97.64           C  
ANISOU  665  CB  LEU A 101     9768  14104  13225   2006    298   -396       C  
ATOM    666  CG  LEU A 101      -2.903 -27.803   5.157  1.00103.09           C  
ANISOU  666  CG  LEU A 101    10300  14903  13966   2018    282   -516       C  
ATOM    667  CD1 LEU A 101      -2.053 -27.013   4.178  1.00103.97           C  
ANISOU  667  CD1 LEU A 101    10285  15092  14126   1883    446   -673       C  
ATOM    668  CD2 LEU A 101      -3.601 -26.857   6.107  1.00104.67           C  
ANISOU  668  CD2 LEU A 101    10561  15101  14106   1975    251   -396       C  
ATOM    669  N   PHE A 102      -3.045 -31.786   5.237  1.00101.19           N  
ANISOU  669  N   PHE A 102    10279  14413  13756   2412     66   -475       N  
ATOM    670  CA  PHE A 102      -2.316 -32.723   6.102  1.00102.78           C  
ANISOU  670  CA  PHE A 102    10490  14578  13982   2650    -81   -532       C  
ATOM    671  C   PHE A 102      -1.242 -33.506   5.335  1.00108.48           C  
ANISOU  671  C   PHE A 102    11089  15327  14800   2750    -77   -716       C  
ATOM    672  O   PHE A 102      -0.150 -33.715   5.866  1.00109.63           O  
ANISOU  672  O   PHE A 102    11109  15539  15006   2932   -193   -864       O  
ATOM    673  CB  PHE A 102      -3.294 -33.680   6.807  1.00104.55           C  
ANISOU  673  CB  PHE A 102    10972  14625  14125   2730   -133   -360       C  
ATOM    674  CG  PHE A 102      -2.698 -34.487   7.937  1.00107.91           C  
ANISOU  674  CG  PHE A 102    11494  14986  14523   2994   -295   -372       C  
ATOM    675  CD1 PHE A 102      -2.609 -33.959   9.220  1.00111.36           C  
ANISOU  675  CD1 PHE A 102    11970  15450  14890   3086   -408   -329       C  
ATOM    676  CD2 PHE A 102      -2.254 -35.788   7.727  1.00111.68           C  
ANISOU  676  CD2 PHE A 102    12048  15359  15026   3167   -339   -425       C  
ATOM    677  CE1 PHE A 102      -2.067 -34.709  10.268  1.00114.21           C  
ANISOU  677  CE1 PHE A 102    12459  15743  15192   3361   -577   -338       C  
ATOM    678  CE2 PHE A 102      -1.710 -36.537   8.774  1.00116.45           C  
ANISOU  678  CE2 PHE A 102    12782  15886  15580   3447   -504   -430       C  
ATOM    679  CZ  PHE A 102      -1.621 -35.993  10.038  1.00114.92           C  
ANISOU  679  CZ  PHE A 102    12641  15725  15300   3549   -628   -384       C  
ATOM    680  N   ASP A 103      -1.553 -33.920   4.089  1.00105.02           N  
ANISOU  680  N   ASP A 103    10681  14846  14377   2638     49   -725       N  
ATOM    681  CA  ASP A 103      -0.638 -34.648   3.207  1.00106.42           C  
ANISOU  681  CA  ASP A 103    10752  15040  14644   2703     89   -901       C  
ATOM    682  C   ASP A 103       0.498 -33.743   2.713  1.00111.43           C  
ANISOU  682  C   ASP A 103    11128  15842  15369   2630    172  -1110       C  
ATOM    683  O   ASP A 103       1.621 -34.219   2.537  1.00112.80           O  
ANISOU  683  O   ASP A 103    11138  16070  15650   2754    150  -1312       O  
ATOM    684  CB  ASP A 103      -1.401 -35.253   2.020  1.00107.65           C  
ANISOU  684  CB  ASP A 103    11033  15102  14767   2581    209   -847       C  
ATOM    685  N   TYR A 104       0.200 -32.440   2.499  1.00107.08           N  
ANISOU  685  N   TYR A 104    10544  15362  14780   2429    280  -1074       N  
ATOM    686  CA  TYR A 104       1.160 -31.427   2.046  1.00107.75           C  
ANISOU  686  CA  TYR A 104    10420  15581  14940   2309    410  -1264       C  
ATOM    687  C   TYR A 104       2.207 -31.114   3.124  1.00112.81           C  
ANISOU  687  C   TYR A 104    10846  16337  15678   2442    285  -1429       C  
ATOM    688  O   TYR A 104       3.373 -30.898   2.788  1.00114.05           O  
ANISOU  688  O   TYR A 104    10767  16604  15962   2431    355  -1681       O  
ATOM    689  CB  TYR A 104       0.430 -30.149   1.578  1.00107.60           C  
ANISOU  689  CB  TYR A 104    10490  15565  14827   2073    560  -1151       C  
ATOM    690  CG  TYR A 104       1.338 -29.075   1.014  1.00110.50           C  
ANISOU  690  CG  TYR A 104    10701  16029  15253   1912    749  -1335       C  
ATOM    691  CD1 TYR A 104       1.844 -29.169  -0.279  1.00113.51           C  
ANISOU  691  CD1 TYR A 104    11057  16412  15658   1804    945  -1467       C  
ATOM    692  CD2 TYR A 104       1.657 -27.942   1.758  1.00111.37           C  
ANISOU  692  CD2 TYR A 104    10711  16216  15390   1848    758  -1381       C  
ATOM    693  CE1 TYR A 104       2.675 -28.181  -0.806  1.00115.51           C  
ANISOU  693  CE1 TYR A 104    11195  16732  15964   1631   1164  -1644       C  
ATOM    694  CE2 TYR A 104       2.486 -26.947   1.242  1.00113.45           C  
ANISOU  694  CE2 TYR A 104    10843  16547  15714   1673    968  -1564       C  
ATOM    695  CZ  TYR A 104       2.992 -27.070  -0.041  1.00122.00           C  
ANISOU  695  CZ  TYR A 104    11912  17619  16822   1560   1182  -1695       C  
ATOM    696  OH  TYR A 104       3.804 -26.088  -0.557  1.00124.45           O  
ANISOU  696  OH  TYR A 104    12120  17974  17190   1364   1431  -1883       O  
ATOM    697  N   ILE A 105       1.792 -31.100   4.411  1.00108.74           N  
ANISOU  697  N   ILE A 105    10413  15801  15104   2567    104  -1305       N  
ATOM    698  CA  ILE A 105       2.673 -30.851   5.561  1.00109.95           C  
ANISOU  698  CA  ILE A 105    10396  16063  15316   2727    -62  -1449       C  
ATOM    699  C   ILE A 105       3.632 -32.046   5.747  1.00116.21           C  
ANISOU  699  C   ILE A 105    11086  16871  16198   3003   -217  -1621       C  
ATOM    700  O   ILE A 105       4.785 -31.848   6.126  1.00117.83           O  
ANISOU  700  O   ILE A 105    11033  17217  16518   3114   -303  -1874       O  
ATOM    701  CB  ILE A 105       1.862 -30.497   6.851  1.00111.93           C  
ANISOU  701  CB  ILE A 105    10813  16270  15445   2780   -200  -1251       C  
ATOM    702  CG1 ILE A 105       0.964 -29.255   6.625  1.00110.36           C  
ANISOU  702  CG1 ILE A 105    10692  16063  15176   2519    -45  -1109       C  
ATOM    703  CG2 ILE A 105       2.782 -30.282   8.070  1.00114.38           C  
ANISOU  703  CG2 ILE A 105    10969  16698  15794   2972   -401  -1411       C  
ATOM    704  CD1 ILE A 105      -0.270 -29.160   7.541  1.00116.21           C  
ANISOU  704  CD1 ILE A 105    11666  16706  15782   2531   -121   -856       C  
ATOM    705  N   CYS A 106       3.163 -33.270   5.443  1.00112.75           N  
ANISOU  705  N   CYS A 106    10839  16287  15715   3113   -247  -1506       N  
ATOM    706  CA  CYS A 106       3.968 -34.488   5.544  1.00114.82           C  
ANISOU  706  CA  CYS A 106    11054  16526  16047   3391   -385  -1645       C  
ATOM    707  C   CYS A 106       4.980 -34.604   4.400  1.00119.98           C  
ANISOU  707  C   CYS A 106    11452  17275  16862   3338   -248  -1912       C  
ATOM    708  O   CYS A 106       6.146 -34.913   4.651  1.00121.96           O  
ANISOU  708  O   CYS A 106    11472  17630  17239   3536   -361  -2166       O  
ATOM    709  CB  CYS A 106       3.078 -35.725   5.631  1.00114.72           C  
ANISOU  709  CB  CYS A 106    11362  16299  15929   3505   -433  -1429       C  
ATOM    710  SG  CYS A 106       2.120 -35.845   7.163  1.00117.95           S  
ANISOU  710  SG  CYS A 106    12080  16575  16159   3629   -599  -1165       S  
ATOM    711  N   LYS A 107       4.535 -34.354   3.151  1.00115.20           N  
ANISOU  711  N   LYS A 107    10890  16635  16246   3081     -7  -1868       N  
ATOM    712  CA  LYS A 107       5.362 -34.454   1.947  1.00116.27           C  
ANISOU  712  CA  LYS A 107    10837  16833  16506   2991    175  -2099       C  
ATOM    713  C   LYS A 107       6.378 -33.317   1.787  1.00121.16           C  
ANISOU  713  C   LYS A 107    11147  17634  17254   2850    300  -2362       C  
ATOM    714  O   LYS A 107       7.574 -33.590   1.674  1.00123.18           O  
ANISOU  714  O   LYS A 107    11130  17998  17677   2959    290  -2659       O  
ATOM    715  CB  LYS A 107       4.485 -34.590   0.691  1.00117.29           C  
ANISOU  715  CB  LYS A 107    11167  16854  16545   2777    381  -1954       C  
ATOM    716  N   HIS A 108       5.907 -32.053   1.768  1.00116.08           N  
ANISOU  716  N   HIS A 108    10544  17019  16543   2608    428  -2269       N  
ATOM    717  CA  HIS A 108       6.753 -30.869   1.583  1.00116.94           C  
ANISOU  717  CA  HIS A 108    10404  17268  16761   2422    598  -2503       C  
ATOM    718  C   HIS A 108       7.431 -30.356   2.869  1.00121.85           C  
ANISOU  718  C   HIS A 108    10800  18028  17469   2545    413  -2659       C  
ATOM    719  O   HIS A 108       8.251 -29.436   2.801  1.00122.77           O  
ANISOU  719  O   HIS A 108    10668  18272  17709   2398    548  -2907       O  
ATOM    720  CB  HIS A 108       5.956 -29.744   0.901  1.00115.87           C  
ANISOU  720  CB  HIS A 108    10450  17072  16501   2112    838  -2337       C  
ATOM    721  N   GLY A 109       7.102 -30.959   4.011  1.00118.04           N  
ANISOU  721  N   GLY A 109    10417  17515  16918   2807    119  -2530       N  
ATOM    722  CA  GLY A 109       7.644 -30.566   5.308  1.00119.05           C  
ANISOU  722  CA  GLY A 109    10381  17767  17087   2964   -101  -2655       C  
ATOM    723  C   GLY A 109       6.993 -29.297   5.820  1.00121.11           C  
ANISOU  723  C   GLY A 109    10730  18034  17253   2765    -42  -2510       C  
ATOM    724  O   GLY A 109       5.805 -29.067   5.573  1.00118.22           O  
ANISOU  724  O   GLY A 109    10645  17537  16737   2623     50  -2214       O  
ATOM    725  N   ARG A 110       7.765 -28.457   6.529  1.00119.08           N  
ANISOU  725  N   ARG A 110    10224  17934  17089   2754    -98  -2737       N  
ATOM    726  CA  ARG A 110       7.252 -27.187   7.045  1.00117.52           C  
ANISOU  726  CA  ARG A 110    10092  17746  16816   2563    -32  -2633       C  
ATOM    727  C   ARG A 110       7.289 -26.099   5.968  1.00121.00           C  
ANISOU  727  C   ARG A 110    10492  18179  17304   2200    330  -2693       C  
ATOM    728  O   ARG A 110       8.330 -25.880   5.343  1.00122.66           O  
ANISOU  728  O   ARG A 110    10435  18485  17684   2093    496  -3003       O  
ATOM    729  CB  ARG A 110       7.944 -26.754   8.359  1.00119.45           C  
ANISOU  729  CB  ARG A 110    10128  18145  17113   2710   -260  -2832       C  
ATOM    730  CG  ARG A 110       9.463 -26.582   8.298  1.00132.66           C  
ANISOU  730  CG  ARG A 110    11361  20022  19022   2737   -261  -3295       C  
ATOM    731  CD  ARG A 110      10.004 -25.973   9.576  1.00143.21           C  
ANISOU  731  CD  ARG A 110    12506  21517  20392   2844   -478  -3489       C  
ATOM    732  NE  ARG A 110      11.379 -25.497   9.417  1.00154.20           N  
ANISOU  732  NE  ARG A 110    13441  23114  22035   2774   -410  -3966       N  
ATOM    733  CZ  ARG A 110      11.711 -24.260   9.060  1.00168.40           C  
ANISOU  733  CZ  ARG A 110    15070  24971  23945   2434   -125  -4149       C  
ATOM    734  NH1 ARG A 110      10.770 -23.355   8.817  1.00153.14           N  
ANISOU  734  NH1 ARG A 110    13403  22901  21881   2158    100  -3878       N  
ATOM    735  NH2 ARG A 110      12.987 -23.917   8.942  1.00158.14           N  
ANISOU  735  NH2 ARG A 110    13335  23860  22893   2370    -55  -4617       N  
ATOM    736  N   VAL A 111       6.133 -25.460   5.720  1.00115.12           N  
ANISOU  736  N   VAL A 111    10032  17306  16404   2019    459  -2400       N  
ATOM    737  CA  VAL A 111       5.977 -24.392   4.732  1.00114.48           C  
ANISOU  737  CA  VAL A 111    10014  17175  16309   1700    792  -2395       C  
ATOM    738  C   VAL A 111       6.704 -23.125   5.179  1.00119.84           C  
ANISOU  738  C   VAL A 111    10484  17959  17092   1533    905  -2627       C  
ATOM    739  O   VAL A 111       6.716 -22.818   6.375  1.00119.46           O  
ANISOU  739  O   VAL A 111    10371  17980  17038   1632    710  -2641       O  
ATOM    740  CB  VAL A 111       4.487 -24.109   4.439  1.00115.58           C  
ANISOU  740  CB  VAL A 111    10519  17153  16244   1611    844  -2021       C  
ATOM    741  N   GLU A 112       7.318 -22.400   4.218  1.00117.81           N  
ANISOU  741  N   GLU A 112    10136  17703  16922   1272   1235  -2821       N  
ATOM    742  CA  GLU A 112       8.059 -21.154   4.451  1.00119.33           C  
ANISOU  742  CA  GLU A 112    10137  17970  17231   1053   1423  -3076       C  
ATOM    743  C   GLU A 112       7.156 -20.085   5.068  1.00121.40           C  
ANISOU  743  C   GLU A 112    10621  18154  17353    954   1427  -2848       C  
ATOM    744  O   GLU A 112       5.986 -19.997   4.700  1.00118.63           O  
ANISOU  744  O   GLU A 112    10604  17654  16816    931   1456  -2512       O  
ATOM    745  CB  GLU A 112       8.681 -20.642   3.143  1.00122.33           C  
ANISOU  745  CB  GLU A 112    10486  18305  17689    765   1836  -3265       C  
ATOM    746  N   GLU A 113       7.705 -19.287   6.012  1.00119.22           N  
ANISOU  746  N   GLU A 113    10142  17984  17170    906   1387  -3049       N  
ATOM    747  CA  GLU A 113       7.021 -18.224   6.768  1.00117.75           C  
ANISOU  747  CA  GLU A 113    10112  17746  16881    821   1379  -2893       C  
ATOM    748  C   GLU A 113       6.064 -17.348   5.947  1.00119.75           C  
ANISOU  748  C   GLU A 113    10725  17800  16976    601   1655  -2627       C  
ATOM    749  O   GLU A 113       4.970 -17.052   6.422  1.00117.20           O  
ANISOU  749  O   GLU A 113    10644  17391  16497    653   1550  -2338       O  
ATOM    750  CB  GLU A 113       8.038 -17.344   7.510  1.00121.56           C  
ANISOU  750  CB  GLU A 113    10286  18371  17531    709   1417  -3252       C  
ATOM    751  N   MET A 114       6.470 -16.951   4.724  1.00117.31           N  
ANISOU  751  N   MET A 114    10461  17414  16699    372   2004  -2732       N  
ATOM    752  CA  MET A 114       5.671 -16.115   3.823  1.00116.01           C  
ANISOU  752  CA  MET A 114    10666  17048  16366    182   2277  -2504       C  
ATOM    753  C   MET A 114       4.550 -16.906   3.131  1.00116.59           C  
ANISOU  753  C   MET A 114    11036  17012  16253    321   2176  -2166       C  
ATOM    754  O   MET A 114       3.437 -16.392   3.005  1.00114.35           O  
ANISOU  754  O   MET A 114    11059  16596  15792    310   2185  -1884       O  
ATOM    755  CB  MET A 114       6.577 -15.427   2.788  1.00121.03           C  
ANISOU  755  CB  MET A 114    11275  17625  17085   -111   2703  -2753       C  
ATOM    756  CG  MET A 114       5.959 -14.195   2.163  1.00124.67           C  
ANISOU  756  CG  MET A 114    12114  17874  17381   -327   3007  -2579       C  
ATOM    757  SD  MET A 114       7.075 -13.411   0.979  1.00132.50           S  
ANISOU  757  SD  MET A 114    13117  18768  18460   -688   3553  -2886       S  
ATOM    758  CE  MET A 114       6.048 -12.083   0.410  1.00128.59           C  
ANISOU  758  CE  MET A 114    13176  17987  17695   -841   3814  -2576       C  
ATOM    759  N   GLU A 115       4.852 -18.140   2.673  1.00112.71           N  
ANISOU  759  N   GLU A 115    10441  16576  15808    453   2081  -2217       N  
ATOM    760  CA  GLU A 115       3.905 -19.027   1.986  1.00110.42           C  
ANISOU  760  CA  GLU A 115    10388  16198  15368    580   1985  -1952       C  
ATOM    761  C   GLU A 115       2.849 -19.582   2.945  1.00110.84           C  
ANISOU  761  C   GLU A 115    10522  16256  15335    804   1649  -1699       C  
ATOM    762  O   GLU A 115       1.683 -19.705   2.563  1.00108.63           O  
ANISOU  762  O   GLU A 115    10508  15871  14896    844   1606  -1429       O  
ATOM    763  CB  GLU A 115       4.652 -20.168   1.276  1.00113.06           C  
ANISOU  763  CB  GLU A 115    10569  16589  15799    642   2002  -2121       C  
ATOM    764  CG  GLU A 115       4.044 -20.573  -0.059  1.00123.46           C  
ANISOU  764  CG  GLU A 115    12164  17779  16965    609   2128  -1954       C  
ATOM    765  CD  GLU A 115       2.795 -21.434  -0.012  1.00142.46           C  
ANISOU  765  CD  GLU A 115    14760  20135  19233    803   1874  -1661       C  
ATOM    766  OE1 GLU A 115       2.734 -22.365   0.825  1.00136.58           O  
ANISOU  766  OE1 GLU A 115    13876  19463  18555   1005   1605  -1649       O  
ATOM    767  OE2 GLU A 115       1.896 -21.210  -0.854  1.00135.96           O  
ANISOU  767  OE2 GLU A 115    14233  19192  18232    755   1953  -1460       O  
ATOM    768  N   ALA A 116       3.258 -19.907   4.190  1.00106.78           N  
ANISOU  768  N   ALA A 116     9785  15865  14923    951   1416  -1802       N  
ATOM    769  CA  ALA A 116       2.388 -20.417   5.253  1.00104.43           C  
ANISOU  769  CA  ALA A 116     9565  15567  14546   1155   1121  -1593       C  
ATOM    770  C   ALA A 116       1.446 -19.318   5.750  1.00105.79           C  
ANISOU  770  C   ALA A 116     9927  15664  14604   1072   1148  -1402       C  
ATOM    771  O   ALA A 116       0.338 -19.622   6.192  1.00103.51           O  
ANISOU  771  O   ALA A 116     9807  15317  14206   1182    994  -1160       O  
ATOM    772  CB  ALA A 116       3.225 -20.949   6.406  1.00106.41           C  
ANISOU  772  CB  ALA A 116     9554  15962  14916   1336    887  -1785       C  
ATOM    773  N   ARG A 117       1.893 -18.044   5.666  1.00102.60           N  
ANISOU  773  N   ARG A 117     9496  15252  14235    869   1362  -1525       N  
ATOM    774  CA  ARG A 117       1.132 -16.849   6.044  1.00101.10           C  
ANISOU  774  CA  ARG A 117     9487  14978  13949    769   1432  -1377       C  
ATOM    775  C   ARG A 117      -0.056 -16.684   5.095  1.00102.25           C  
ANISOU  775  C   ARG A 117     9955  14970  13927    741   1522  -1107       C  
ATOM    776  O   ARG A 117      -1.173 -16.474   5.562  1.00100.15           O  
ANISOU  776  O   ARG A 117     9850  14646  13557    811   1409   -887       O  
ATOM    777  CB  ARG A 117       2.034 -15.602   5.988  1.00103.55           C  
ANISOU  777  CB  ARG A 117     9700  15295  14348    539   1688  -1610       C  
ATOM    778  CG  ARG A 117       1.398 -14.330   6.540  1.00114.11           C  
ANISOU  778  CG  ARG A 117    11203  16549  15607    444   1757  -1495       C  
ATOM    779  CD  ARG A 117       2.084 -13.092   5.999  1.00127.07           C  
ANISOU  779  CD  ARG A 117    12868  18118  17295    174   2104  -1672       C  
ATOM    780  NE  ARG A 117       3.339 -12.802   6.694  1.00138.89           N  
ANISOU  780  NE  ARG A 117    14032  19757  18983     85   2133  -2021       N  
ATOM    781  CZ  ARG A 117       4.279 -11.982   6.235  1.00156.49           C  
ANISOU  781  CZ  ARG A 117    16176  21964  21320   -167   2449  -2284       C  
ATOM    782  NH1 ARG A 117       4.126 -11.372   5.065  1.00144.44           N  
ANISOU  782  NH1 ARG A 117    14917  20257  19706   -350   2778  -2215       N  
ATOM    783  NH2 ARG A 117       5.386 -11.774   6.935  1.00146.26           N  
ANISOU  783  NH2 ARG A 117    14535  20821  20217   -236   2444  -2632       N  
ATOM    784  N   ARG A 118       0.195 -16.794   3.768  1.00 98.68           N  
ANISOU  784  N   ARG A 118     9592  14456  13447    647   1718  -1142       N  
ATOM    785  CA  ARG A 118      -0.801 -16.681   2.699  1.00 97.19           C  
ANISOU  785  CA  ARG A 118     9712  14131  13085    634   1798   -925       C  
ATOM    786  C   ARG A 118      -1.912 -17.724   2.872  1.00 98.12           C  
ANISOU  786  C   ARG A 118     9897  14251  13133    831   1538   -716       C  
ATOM    787  O   ARG A 118      -3.086 -17.382   2.732  1.00 96.53           O  
ANISOU  787  O   ARG A 118     9908  13966  12801    866   1496   -509       O  
ATOM    788  CB  ARG A 118      -0.126 -16.811   1.322  1.00 98.84           C  
ANISOU  788  CB  ARG A 118     9978  14295  13283    517   2039  -1043       C  
ATOM    789  CG  ARG A 118      -1.033 -16.468   0.140  1.00108.51           C  
ANISOU  789  CG  ARG A 118    11562  15369  14299    492   2151   -847       C  
ATOM    790  CD  ARG A 118      -0.364 -16.727  -1.200  1.00119.59           C  
ANISOU  790  CD  ARG A 118    13044  16726  15669    389   2382   -962       C  
ATOM    791  NE  ARG A 118      -0.067 -18.146  -1.414  1.00127.04           N  
ANISOU  791  NE  ARG A 118    13812  17764  16693    501   2245  -1033       N  
ATOM    792  CZ  ARG A 118      -0.890 -19.012  -1.998  1.00139.53           C  
ANISOU  792  CZ  ARG A 118    15526  19322  18168    627   2104   -882       C  
ATOM    793  NH1 ARG A 118      -2.078 -18.616  -2.440  1.00125.30           N  
ANISOU  793  NH1 ARG A 118    14011  17422  16174    671   2060   -664       N  
ATOM    794  NH2 ARG A 118      -0.532 -20.279  -2.146  1.00126.51           N  
ANISOU  794  NH2 ARG A 118    13716  17747  16606    718   2001   -966       N  
ATOM    795  N   LEU A 119      -1.538 -18.976   3.209  1.00 93.77           N  
ANISOU  795  N   LEU A 119     9165  13791  12674    960   1370   -786       N  
ATOM    796  CA  LEU A 119      -2.473 -20.076   3.452  1.00 91.75           C  
ANISOU  796  CA  LEU A 119     8962  13526  12373   1129   1149   -621       C  
ATOM    797  C   LEU A 119      -3.258 -19.860   4.746  1.00 93.60           C  
ANISOU  797  C   LEU A 119     9215  13764  12587   1211    983   -489       C  
ATOM    798  O   LEU A 119      -4.428 -20.242   4.817  1.00 91.82           O  
ANISOU  798  O   LEU A 119     9118  13485  12284   1285    878   -309       O  
ATOM    799  CB  LEU A 119      -1.730 -21.419   3.488  1.00 92.41           C  
ANISOU  799  CB  LEU A 119     8872  13680  12559   1244   1044   -747       C  
ATOM    800  CG  LEU A 119      -1.487 -22.090   2.137  1.00 97.36           C  
ANISOU  800  CG  LEU A 119     9574  14266  13152   1245   1108   -747       C  
ATOM    801  CD1 LEU A 119      -0.534 -21.277   1.269  1.00 99.22           C  
ANISOU  801  CD1 LEU A 119     9783  14503  13414   1087   1364   -922       C  
ATOM    802  CD2 LEU A 119      -0.918 -23.470   2.327  1.00100.05           C  
ANISOU  802  CD2 LEU A 119     9795  14647  13574   1407    947   -802       C  
ATOM    803  N   PHE A 120      -2.621 -19.233   5.758  1.00 90.24           N  
ANISOU  803  N   PHE A 120     8656  13402  12231   1189    968   -599       N  
ATOM    804  CA  PHE A 120      -3.264 -18.918   7.033  1.00 88.91           C  
ANISOU  804  CA  PHE A 120     8513  13236  12032   1253    833   -494       C  
ATOM    805  C   PHE A 120      -4.237 -17.745   6.890  1.00 91.54           C  
ANISOU  805  C   PHE A 120     9034  13478  12268   1162    933   -345       C  
ATOM    806  O   PHE A 120      -5.246 -17.701   7.595  1.00 90.07           O  
ANISOU  806  O   PHE A 120     8932  13260  12029   1228    827   -195       O  
ATOM    807  CB  PHE A 120      -2.238 -18.663   8.150  1.00 91.80           C  
ANISOU  807  CB  PHE A 120     8680  13709  12492   1274    766   -679       C  
ATOM    808  CG  PHE A 120      -2.858 -18.284   9.476  1.00 92.60           C  
ANISOU  808  CG  PHE A 120     8832  13809  12543   1335    639   -578       C  
ATOM    809  CD1 PHE A 120      -3.487 -19.239  10.268  1.00 94.92           C  
ANISOU  809  CD1 PHE A 120     9187  14088  12788   1501    448   -452       C  
ATOM    810  CD2 PHE A 120      -2.828 -16.969   9.925  1.00 94.96           C  
ANISOU  810  CD2 PHE A 120     9142  14104  12837   1218    735   -611       C  
ATOM    811  CE1 PHE A 120      -4.072 -18.885  11.485  1.00 95.31           C  
ANISOU  811  CE1 PHE A 120     9309  14126  12779   1547    358   -361       C  
ATOM    812  CE2 PHE A 120      -3.414 -16.616  11.142  1.00 97.16           C  
ANISOU  812  CE2 PHE A 120     9476  14378  13063   1271    628   -523       C  
ATOM    813  CZ  PHE A 120      -4.028 -17.576  11.914  1.00 94.52           C  
ANISOU  813  CZ  PHE A 120     9202  14036  12675   1436    442   -399       C  
ATOM    814  N   GLN A 121      -3.927 -16.793   5.990  1.00 88.45           N  
ANISOU  814  N   GLN A 121     8720  13036  11853   1015   1147   -394       N  
ATOM    815  CA  GLN A 121      -4.774 -15.631   5.716  1.00 87.67           C  
ANISOU  815  CA  GLN A 121     8834  12830  11648    947   1253   -261       C  
ATOM    816  C   GLN A 121      -6.073 -16.086   5.053  1.00 90.38           C  
ANISOU  816  C   GLN A 121     9353  13106  11881   1040   1172    -67       C  
ATOM    817  O   GLN A 121      -7.146 -15.607   5.420  1.00 89.13           O  
ANISOU  817  O   GLN A 121     9308  12899  11659   1084   1117     73       O  
ATOM    818  CB  GLN A 121      -4.034 -14.612   4.837  1.00 90.44           C  
ANISOU  818  CB  GLN A 121     9267  13114  11982    772   1524   -369       C  
ATOM    819  CG  GLN A 121      -3.015 -13.776   5.604  1.00104.51           C  
ANISOU  819  CG  GLN A 121    10896  14941  13871    646   1632   -562       C  
ATOM    820  CD  GLN A 121      -2.035 -13.037   4.724  1.00124.08           C  
ANISOU  820  CD  GLN A 121    13410  17362  16373    446   1934   -730       C  
ATOM    821  OE1 GLN A 121      -1.760 -13.407   3.575  1.00120.13           O  
ANISOU  821  OE1 GLN A 121    12987  16821  15836    406   2058   -754       O  
ATOM    822  NE2 GLN A 121      -1.445 -11.992   5.273  1.00116.79           N  
ANISOU  822  NE2 GLN A 121    12429  16431  15515    303   2076   -870       N  
ATOM    823  N   GLN A 122      -5.971 -17.052   4.118  1.00 87.05           N  
ANISOU  823  N   GLN A 122     8934  12694  11449   1076   1157    -81       N  
ATOM    824  CA  GLN A 122      -7.098 -17.631   3.384  1.00 86.16           C  
ANISOU  824  CA  GLN A 122     8956  12537  11244   1161   1070     56       C  
ATOM    825  C   GLN A 122      -7.990 -18.491   4.284  1.00 88.77           C  
ANISOU  825  C   GLN A 122     9218  12899  11611   1278    868    146       C  
ATOM    826  O   GLN A 122      -9.214 -18.384   4.191  1.00 87.64           O  
ANISOU  826  O   GLN A 122     9176  12717  11407   1329    801    266       O  
ATOM    827  CB  GLN A 122      -6.606 -18.440   2.171  1.00 88.22           C  
ANISOU  827  CB  GLN A 122     9232  12800  11488   1150   1126    -14       C  
ATOM    828  CG  GLN A 122      -5.935 -17.587   1.091  1.00105.54           C  
ANISOU  828  CG  GLN A 122    11566  14930  13606   1025   1361    -81       C  
ATOM    829  CD  GLN A 122      -5.372 -18.384  -0.065  1.00126.73           C  
ANISOU  829  CD  GLN A 122    14262  17616  16273   1004   1439   -169       C  
ATOM    830  OE1 GLN A 122      -5.076 -19.582   0.037  1.00122.20           O  
ANISOU  830  OE1 GLN A 122    13533  17111  15788   1066   1338   -231       O  
ATOM    831  NE2 GLN A 122      -5.179 -17.718  -1.193  1.00120.72           N  
ANISOU  831  NE2 GLN A 122    13712  16768  15389    915   1638   -181       N  
ATOM    832  N   ILE A 123      -7.381 -19.330   5.157  1.00 85.37           N  
ANISOU  832  N   ILE A 123     8626  12532  11278   1326    779     76       N  
ATOM    833  CA  ILE A 123      -8.104 -20.213   6.081  1.00 84.46           C  
ANISOU  833  CA  ILE A 123     8482  12420  11188   1427    622    153       C  
ATOM    834  C   ILE A 123      -8.875 -19.403   7.142  1.00 87.91           C  
ANISOU  834  C   ILE A 123     8960  12838  11604   1429    591    243       C  
ATOM    835  O   ILE A 123      -9.997 -19.778   7.478  1.00 86.77           O  
ANISOU  835  O   ILE A 123     8865  12661  11444   1477    519    343       O  
ATOM    836  CB  ILE A 123      -7.195 -21.326   6.692  1.00 88.08           C  
ANISOU  836  CB  ILE A 123     8812  12928  11726   1506    534     59       C  
ATOM    837  CG1 ILE A 123      -8.027 -22.519   7.215  1.00 88.01           C  
ANISOU  837  CG1 ILE A 123     8848  12876  11716   1605    412    151       C  
ATOM    838  CG2 ILE A 123      -6.218 -20.799   7.754  1.00 89.53           C  
ANISOU  838  CG2 ILE A 123     8879  13177  11960   1509    516    -45       C  
ATOM    839  CD1 ILE A 123      -7.215 -23.686   7.778  1.00 96.49           C  
ANISOU  839  CD1 ILE A 123     9854  13966  12841   1717    318     78       C  
ATOM    840  N   LEU A 124      -8.288 -18.291   7.637  1.00 85.21           N  
ANISOU  840  N   LEU A 124     8593  12514  11269   1365    663    190       N  
ATOM    841  CA  LEU A 124      -8.915 -17.428   8.638  1.00 84.81           C  
ANISOU  841  CA  LEU A 124     8583  12444  11198   1360    651    258       C  
ATOM    842  C   LEU A 124     -10.043 -16.593   8.031  1.00 89.01           C  
ANISOU  842  C   LEU A 124     9258  12904  11659   1343    704    368       C  
ATOM    843  O   LEU A 124     -11.014 -16.296   8.727  1.00 88.02           O  
ANISOU  843  O   LEU A 124     9169  12754  11522   1377    658    451       O  
ATOM    844  CB  LEU A 124      -7.881 -16.529   9.330  1.00 85.58           C  
ANISOU  844  CB  LEU A 124     8604  12583  11330   1291    713    141       C  
ATOM    845  CG  LEU A 124      -8.451 -15.539  10.343  1.00 90.02           C  
ANISOU  845  CG  LEU A 124     9164  13152  11886   1316    650    175       C  
ATOM    846  CD1 LEU A 124      -9.114 -16.259  11.504  1.00 90.54           C  
ANISOU  846  CD1 LEU A 124     9133  13287  11982   1412    509    113       C  
ATOM    847  CD2 LEU A 124      -7.379 -14.611  10.853  1.00 93.12           C  
ANISOU  847  CD2 LEU A 124     9559  13539  12283   1209    768    102       C  
ATOM    848  N   SER A 125      -9.920 -16.237   6.732  1.00 86.66           N  
ANISOU  848  N   SER A 125     9052  12569  11307   1303    798    360       N  
ATOM    849  CA  SER A 125     -10.920 -15.475   5.974  1.00 86.85           C  
ANISOU  849  CA  SER A 125     9244  12520  11236   1325    827    454       C  
ATOM    850  C   SER A 125     -12.226 -16.272   5.867  1.00 90.57           C  
ANISOU  850  C   SER A 125     9713  12998  11702   1425    687    531       C  
ATOM    851  O   SER A 125     -13.309 -15.691   5.946  1.00 90.02           O  
ANISOU  851  O   SER A 125     9709  12896  11598   1477    652    601       O  
ATOM    852  CB  SER A 125     -10.392 -15.146   4.581  1.00 91.52           C  
ANISOU  852  CB  SER A 125     9964  13065  11745   1278    951    421       C  
ATOM    853  OG  SER A 125     -11.317 -14.372   3.834  1.00101.05           O  
ANISOU  853  OG  SER A 125    11372  14191  12830   1333    960    513       O  
ATOM    854  N   ALA A 126     -12.107 -17.604   5.705  1.00 87.32           N  
ANISOU  854  N   ALA A 126     9214  12627  11337   1450    616    500       N  
ATOM    855  CA  ALA A 126     -13.225 -18.539   5.614  1.00 87.00           C  
ANISOU  855  CA  ALA A 126     9148  12593  11317   1514    506    536       C  
ATOM    856  C   ALA A 126     -13.861 -18.768   6.990  1.00 90.78           C  
ANISOU  856  C   ALA A 126     9558  13071  11861   1529    457    571       C  
ATOM    857  O   ALA A 126     -15.082 -18.903   7.077  1.00 90.32           O  
ANISOU  857  O   ALA A 126     9494  13003  11820   1562    408    601       O  
ATOM    858  CB  ALA A 126     -12.752 -19.854   5.022  1.00 87.88           C  
ANISOU  858  CB  ALA A 126     9211  12725  11455   1519    477    480       C  
ATOM    859  N   VAL A 127     -13.034 -18.798   8.059  1.00 87.56           N  
ANISOU  859  N   VAL A 127     9101  12678  11489   1508    473    550       N  
ATOM    860  CA  VAL A 127     -13.467 -18.963   9.454  1.00 87.31           C  
ANISOU  860  CA  VAL A 127     9048  12635  11491   1522    444    585       C  
ATOM    861  C   VAL A 127     -14.251 -17.704   9.883  1.00 91.80           C  
ANISOU  861  C   VAL A 127     9658  13183  12040   1510    479    632       C  
ATOM    862  O   VAL A 127     -15.302 -17.823  10.520  1.00 91.21           O  
ANISOU  862  O   VAL A 127     9579  13086  11990   1525    465    668       O  
ATOM    863  CB  VAL A 127     -12.264 -19.310  10.386  1.00 91.36           C  
ANISOU  863  CB  VAL A 127     9518  13176  12018   1533    424    535       C  
ATOM    864  CG1 VAL A 127     -12.590 -19.096  11.863  1.00 91.08           C  
ANISOU  864  CG1 VAL A 127     9509  13125  11974   1547    409    571       C  
ATOM    865  CG2 VAL A 127     -11.788 -20.741  10.152  1.00 91.42           C  
ANISOU  865  CG2 VAL A 127     9500  13184  12052   1581    370    501       C  
ATOM    866  N   ASP A 128     -13.759 -16.512   9.475  1.00 89.23           N  
ANISOU  866  N   ASP A 128     9379  12852  11672   1479    545    621       N  
ATOM    867  CA  ASP A 128     -14.379 -15.209   9.736  1.00 89.47           C  
ANISOU  867  CA  ASP A 128     9476  12845  11674   1478    590    661       C  
ATOM    868  C   ASP A 128     -15.732 -15.096   9.021  1.00 94.09           C  
ANISOU  868  C   ASP A 128    10101  13407  12243   1548    544    704       C  
ATOM    869  O   ASP A 128     -16.678 -14.560   9.601  1.00 93.70           O  
ANISOU  869  O   ASP A 128    10051  13339  12213   1580    538    731       O  
ATOM    870  CB  ASP A 128     -13.435 -14.072   9.305  1.00 91.92           C  
ANISOU  870  CB  ASP A 128     9858  13129  11937   1419    696    628       C  
ATOM    871  CG  ASP A 128     -14.033 -12.682   9.391  1.00102.93           C  
ANISOU  871  CG  ASP A 128    11364  14456  13288   1427    758    673       C  
ATOM    872  OD1 ASP A 128     -14.135 -12.149  10.515  1.00103.33           O  
ANISOU  872  OD1 ASP A 128    11394  14503  13366   1407    777    674       O  
ATOM    873  OD2 ASP A 128     -14.391 -12.125   8.331  1.00109.66           O  
ANISOU  873  OD2 ASP A 128    12345  15252  14068   1466    786    707       O  
ATOM    874  N   TYR A 129     -15.817 -15.610   7.771  1.00 91.37           N  
ANISOU  874  N   TYR A 129     9780  13071  11865   1581    506    691       N  
ATOM    875  CA  TYR A 129     -17.032 -15.619   6.949  1.00 91.87           C  
ANISOU  875  CA  TYR A 129     9867  13133  11905   1669    426    699       C  
ATOM    876  C   TYR A 129     -18.119 -16.481   7.599  1.00 96.08           C  
ANISOU  876  C   TYR A 129    10271  13697  12539   1682    362    676       C  
ATOM    877  O   TYR A 129     -19.295 -16.122   7.536  1.00 96.20           O  
ANISOU  877  O   TYR A 129    10259  13718  12576   1748    312    662       O  
ATOM    878  CB  TYR A 129     -16.721 -16.115   5.523  1.00 93.53           C  
ANISOU  878  CB  TYR A 129    10138  13353  12046   1693    396    674       C  
ATOM    879  CG  TYR A 129     -17.900 -16.073   4.572  1.00 96.12           C  
ANISOU  879  CG  TYR A 129    10502  13693  12327   1806    286    662       C  
ATOM    880  CD1 TYR A 129     -18.224 -14.908   3.883  1.00 99.10           C  
ANISOU  880  CD1 TYR A 129    11046  14023  12586   1901    276    697       C  
ATOM    881  CD2 TYR A 129     -18.670 -17.208   4.332  1.00 96.96           C  
ANISOU  881  CD2 TYR A 129    10487  13852  12500   1827    188    600       C  
ATOM    882  CE1 TYR A 129     -19.302 -14.865   2.999  1.00101.01           C  
ANISOU  882  CE1 TYR A 129    11324  14286  12770   2042    138    669       C  
ATOM    883  CE2 TYR A 129     -19.753 -17.176   3.455  1.00 98.89           C  
ANISOU  883  CE2 TYR A 129    10736  14128  12708   1940     63    551       C  
ATOM    884  CZ  TYR A 129     -20.064 -16.003   2.788  1.00107.10           C  
ANISOU  884  CZ  TYR A 129    11934  15136  13622   2062     22    585       C  
ATOM    885  OH  TYR A 129     -21.129 -15.967   1.921  1.00109.10           O  
ANISOU  885  OH  TYR A 129    12194  15432  13826   2209   -136    522       O  
ATOM    886  N   CYS A 130     -17.720 -17.611   8.219  1.00 92.59           N  
ANISOU  886  N   CYS A 130     9757  13265  12158   1623    374    658       N  
ATOM    887  CA  CYS A 130     -18.620 -18.532   8.912  1.00 92.72           C  
ANISOU  887  CA  CYS A 130     9686  13279  12264   1603    363    632       C  
ATOM    888  C   CYS A 130     -19.219 -17.880  10.159  1.00 97.07           C  
ANISOU  888  C   CYS A 130    10224  13807  12851   1589    414    655       C  
ATOM    889  O   CYS A 130     -20.421 -18.013  10.395  1.00 97.14           O  
ANISOU  889  O   CYS A 130    10162  13817  12931   1594    414    615       O  
ATOM    890  CB  CYS A 130     -17.908 -19.839   9.249  1.00 92.82           C  
ANISOU  890  CB  CYS A 130     9690  13276  12303   1559    376    623       C  
ATOM    891  SG  CYS A 130     -17.657 -20.936   7.828  1.00 97.03           S  
ANISOU  891  SG  CYS A 130    10208  13828  12831   1570    322    568       S  
ATOM    892  N   HIS A 131     -18.384 -17.156  10.938  1.00 93.64           N  
ANISOU  892  N   HIS A 131     9848  13357  12374   1567    464    698       N  
ATOM    893  CA  HIS A 131     -18.787 -16.454  12.161  1.00 93.66           C  
ANISOU  893  CA  HIS A 131     9860  13334  12390   1551    521    718       C  
ATOM    894  C   HIS A 131     -19.775 -15.313  11.898  1.00 98.11           C  
ANISOU  894  C   HIS A 131    10419  13894  12964   1605    519    714       C  
ATOM    895  O   HIS A 131     -20.614 -15.028  12.756  1.00 97.87           O  
ANISOU  895  O   HIS A 131    10355  13848  12984   1599    562    702       O  
ATOM    896  CB  HIS A 131     -17.559 -15.946  12.937  1.00 94.14           C  
ANISOU  896  CB  HIS A 131     9980  13393  12396   1519    556    739       C  
ATOM    897  CG  HIS A 131     -16.693 -17.028  13.513  1.00 97.43           C  
ANISOU  897  CG  HIS A 131    10402  13814  12802   1503    536    731       C  
ATOM    898  ND1 HIS A 131     -15.383 -16.779  13.879  1.00 99.16           N  
ANISOU  898  ND1 HIS A 131    10636  14060  12979   1496    526    708       N  
ATOM    899  CD2 HIS A 131     -16.980 -18.325  13.781  1.00 99.30           C  
ANISOU  899  CD2 HIS A 131    10641  14025  13065   1504    526    732       C  
ATOM    900  CE1 HIS A 131     -14.919 -17.923  14.354  1.00 98.72           C  
ANISOU  900  CE1 HIS A 131    10592  14002  12917   1521    484    701       C  
ATOM    901  NE2 HIS A 131     -15.842 -18.882  14.310  1.00 99.15           N  
ANISOU  901  NE2 HIS A 131    10659  14010  13003   1524    493    726       N  
ATOM    902  N   ARG A 132     -19.678 -14.671  10.713  1.00 95.15           N  
ANISOU  902  N   ARG A 132    10094  13523  12533   1668    475    719       N  
ATOM    903  CA  ARG A 132     -20.565 -13.584  10.285  1.00 95.85           C  
ANISOU  903  CA  ARG A 132    10214  13596  12607   1764    446    717       C  
ATOM    904  C   ARG A 132     -21.979 -14.112  10.017  1.00100.52           C  
ANISOU  904  C   ARG A 132    10678  14230  13286   1827    369    642       C  
ATOM    905  O   ARG A 132     -22.953 -13.396  10.256  1.00100.90           O  
ANISOU  905  O   ARG A 132    10687  14276  13375   1899    356    610       O  
ATOM    906  CB  ARG A 132     -20.021 -12.896   9.021  1.00 97.04           C  
ANISOU  906  CB  ARG A 132    10507  13720  12643   1826    423    748       C  
ATOM    907  CG  ARG A 132     -18.840 -11.963   9.259  1.00108.63           C  
ANISOU  907  CG  ARG A 132    12103  15130  14041   1762    532    791       C  
ATOM    908  CD  ARG A 132     -18.516 -11.179   8.001  1.00121.74           C  
ANISOU  908  CD  ARG A 132    13947  16730  15579   1821    547    820       C  
ATOM    909  NE  ARG A 132     -17.216 -10.512   8.083  1.00133.23           N  
ANISOU  909  NE  ARG A 132    15509  18130  16984   1715    686    828       N  
ATOM    910  CZ  ARG A 132     -16.700  -9.750   7.122  1.00150.51           C  
ANISOU  910  CZ  ARG A 132    17893  20234  19058   1720    766    849       C  
ATOM    911  NH1 ARG A 132     -17.372  -9.542   5.996  1.00140.06           N  
ANISOU  911  NH1 ARG A 132    16713  18871  17634   1855    697    883       N  
ATOM    912  NH2 ARG A 132     -15.510  -9.186   7.282  1.00137.89           N  
ANISOU  912  NH2 ARG A 132    16362  18589  17443   1591    920    824       N  
ATOM    913  N   HIS A 133     -22.081 -15.362   9.520  1.00 97.04           N  
ANISOU  913  N   HIS A 133    10158  13828  12883   1798    323    593       N  
ATOM    914  CA  HIS A 133     -23.344 -16.031   9.198  1.00 97.76           C  
ANISOU  914  CA  HIS A 133    10100  13969  13076   1829    257    482       C  
ATOM    915  C   HIS A 133     -23.858 -16.935  10.339  1.00101.48           C  
ANISOU  915  C   HIS A 133    10461  14426  13670   1711    358    431       C  
ATOM    916  O   HIS A 133     -24.768 -17.743  10.128  1.00101.90           O  
ANISOU  916  O   HIS A 133    10379  14511  13827   1687    342    317       O  
ATOM    917  CB  HIS A 133     -23.223 -16.787   7.863  1.00 98.87           C  
ANISOU  917  CB  HIS A 133    10236  14151  13177   1865    153    439       C  
ATOM    918  CG  HIS A 133     -22.996 -15.881   6.693  1.00102.75           C  
ANISOU  918  CG  HIS A 133    10863  14643  13532   1997     62    474       C  
ATOM    919  ND1 HIS A 133     -21.754 -15.329   6.440  1.00103.83           N  
ANISOU  919  ND1 HIS A 133    11175  14727  13547   1977    121    575       N  
ATOM    920  CD2 HIS A 133     -23.867 -15.444   5.756  1.00105.86           C  
ANISOU  920  CD2 HIS A 133    11256  15076  13889   2152    -77    411       C  
ATOM    921  CE1 HIS A 133     -21.906 -14.582   5.360  1.00104.22           C  
ANISOU  921  CE1 HIS A 133    11357  14764  13478   2107     44    587       C  
ATOM    922  NE2 HIS A 133     -23.160 -14.622   4.910  1.00105.81           N  
ANISOU  922  NE2 HIS A 133    11470  15021  13713   2233    -93    497       N  
ATOM    923  N   MET A 134     -23.292 -16.753  11.557  1.00 97.22           N  
ANISOU  923  N   MET A 134     9993  13833  13113   1636    469    505       N  
ATOM    924  CA  MET A 134     -23.620 -17.444  12.815  1.00 97.14           C  
ANISOU  924  CA  MET A 134     9962  13777  13171   1529    595    487       C  
ATOM    925  C   MET A 134     -23.469 -18.985  12.736  1.00100.71           C  
ANISOU  925  C   MET A 134    10408  14201  13656   1447    625    459       C  
ATOM    926  O   MET A 134     -24.263 -19.721  13.331  1.00101.08           O  
ANISOU  926  O   MET A 134    10404  14208  13794   1362    727    390       O  
ATOM    927  CB  MET A 134     -25.013 -17.028  13.349  1.00100.64           C  
ANISOU  927  CB  MET A 134    10283  14227  13729   1527    654    391       C  
ATOM    928  CG  MET A 134     -25.171 -15.529  13.571  1.00104.43           C  
ANISOU  928  CG  MET A 134    10789  14713  14178   1614    640    420       C  
ATOM    929  SD  MET A 134     -24.247 -14.890  14.990  1.00107.86           S  
ANISOU  929  SD  MET A 134    11384  15078  14521   1552    756    533       S  
ATOM    930  CE  MET A 134     -25.522 -14.899  16.227  1.00105.68           C  
ANISOU  930  CE  MET A 134    11024  14770  14359   1485    908    446       C  
ATOM    931  N   VAL A 135     -22.428 -19.460  12.021  1.00 96.32           N  
ANISOU  931  N   VAL A 135     9917  13653  13027   1466    557    506       N  
ATOM    932  CA  VAL A 135     -22.116 -20.889  11.857  1.00 96.14           C  
ANISOU  932  CA  VAL A 135     9916  13592  13021   1410    576    489       C  
ATOM    933  C   VAL A 135     -20.690 -21.136  12.369  1.00 98.97           C  
ANISOU  933  C   VAL A 135    10410  13913  13281   1417    581    585       C  
ATOM    934  O   VAL A 135     -19.776 -20.397  12.006  1.00 97.83           O  
ANISOU  934  O   VAL A 135    10296  13810  13065   1469    521    628       O  
ATOM    935  CB  VAL A 135     -22.302 -21.385  10.391  1.00100.41           C  
ANISOU  935  CB  VAL A 135    10380  14188  13583   1442    475    415       C  
ATOM    936  CG1 VAL A 135     -22.061 -22.890  10.273  1.00100.50           C  
ANISOU  936  CG1 VAL A 135    10417  14144  13624   1376    513    386       C  
ATOM    937  CG2 VAL A 135     -23.683 -21.028   9.845  1.00101.31           C  
ANISOU  937  CG2 VAL A 135    10341  14365  13788   1472    427    293       C  
ATOM    938  N   VAL A 136     -20.502 -22.164  13.216  1.00 95.81           N  
ANISOU  938  N   VAL A 136    10098  13428  12877   1370    657    604       N  
ATOM    939  CA  VAL A 136     -19.185 -22.486  13.769  1.00 95.26           C  
ANISOU  939  CA  VAL A 136    10154  13328  12713   1411    633    674       C  
ATOM    940  C   VAL A 136     -18.747 -23.901  13.368  1.00 99.54           C  
ANISOU  940  C   VAL A 136    10746  13815  13258   1416    622    660       C  
ATOM    941  O   VAL A 136     -19.338 -24.886  13.817  1.00100.07           O  
ANISOU  941  O   VAL A 136    10883  13782  13356   1362    715    646       O  
ATOM    942  CB  VAL A 136     -19.114 -22.220  15.299  1.00 99.39           C  
ANISOU  942  CB  VAL A 136    10797  13791  13175   1405    704    727       C  
ATOM    943  CG1 VAL A 136     -17.917 -22.912  15.950  1.00 99.41           C  
ANISOU  943  CG1 VAL A 136    10944  13748  13079   1470    663    774       C  
ATOM    944  CG2 VAL A 136     -19.075 -20.724  15.578  1.00 98.67           C  
ANISOU  944  CG2 VAL A 136    10664  13766  13062   1421    688    741       C  
ATOM    945  N   HIS A 137     -17.709 -23.984  12.513  1.00 95.46           N  
ANISOU  945  N   HIS A 137    10205  13353  12711   1474    528    656       N  
ATOM    946  CA  HIS A 137     -17.126 -25.239  12.041  1.00 95.55           C  
ANISOU  946  CA  HIS A 137    10259  13320  12723   1499    505    637       C  
ATOM    947  C   HIS A 137     -16.228 -25.766  13.162  1.00 99.75           C  
ANISOU  947  C   HIS A 137    10937  13782  13180   1569    499    688       C  
ATOM    948  O   HIS A 137     -15.060 -25.386  13.261  1.00 99.17           O  
ANISOU  948  O   HIS A 137    10857  13769  13055   1647    418    690       O  
ATOM    949  CB  HIS A 137     -16.341 -25.008  10.736  1.00 95.78           C  
ANISOU  949  CB  HIS A 137    10207  13439  12746   1536    422    600       C  
ATOM    950  CG  HIS A 137     -15.883 -26.268  10.073  1.00 99.57           C  
ANISOU  950  CG  HIS A 137    10709  13880  13242   1557    405    561       C  
ATOM    951  ND1 HIS A 137     -14.689 -26.871  10.418  1.00101.58           N  
ANISOU  951  ND1 HIS A 137    11028  14108  13460   1637    368    569       N  
ATOM    952  CD2 HIS A 137     -16.472 -26.994   9.095  1.00101.63           C  
ANISOU  952  CD2 HIS A 137    10932  14128  13555   1516    413    501       C  
ATOM    953  CE1 HIS A 137     -14.591 -27.941   9.647  1.00101.43           C  
ANISOU  953  CE1 HIS A 137    11018  14049  13472   1642    367    524       C  
ATOM    954  NE2 HIS A 137     -15.640 -28.055   8.834  1.00101.79           N  
ANISOU  954  NE2 HIS A 137    11006  14101  13569   1560    398    482       N  
ATOM    955  N   ARG A 138     -16.804 -26.602  14.039  1.00 97.05           N  
ANISOU  955  N   ARG A 138    10737  13310  12827   1542    592    715       N  
ATOM    956  CA  ARG A 138     -16.136 -27.152  15.222  1.00 97.66           C  
ANISOU  956  CA  ARG A 138    11015  13292  12800   1631    587    774       C  
ATOM    957  C   ARG A 138     -15.006 -28.157  14.926  1.00101.89           C  
ANISOU  957  C   ARG A 138    11621  13795  13299   1752    497    765       C  
ATOM    958  O   ARG A 138     -14.154 -28.364  15.793  1.00102.19           O  
ANISOU  958  O   ARG A 138    11793  13800  13236   1880    428    798       O  
ATOM    959  CB  ARG A 138     -17.167 -27.762  16.187  1.00 99.13           C  
ANISOU  959  CB  ARG A 138    11378  13318  12970   1555    750    808       C  
ATOM    960  CG  ARG A 138     -17.979 -26.714  16.948  1.00109.01           C  
ANISOU  960  CG  ARG A 138    12605  14594  14221   1480    830    822       C  
ATOM    961  CD  ARG A 138     -18.941 -27.326  17.950  1.00119.64           C  
ANISOU  961  CD  ARG A 138    14141  15771  15546   1391   1025    842       C  
ATOM    962  NE  ARG A 138     -20.153 -27.844  17.312  1.00128.06           N  
ANISOU  962  NE  ARG A 138    15106  16794  16758   1241   1163    755       N  
ATOM    963  CZ  ARG A 138     -20.673 -29.045  17.549  1.00143.71           C  
ANISOU  963  CZ  ARG A 138    17245  18601  18756   1159   1326    737       C  
ATOM    964  NH1 ARG A 138     -20.092 -29.870  18.413  1.00132.72           N  
ANISOU  964  NH1 ARG A 138    16160  17044  17222   1234   1370    824       N  
ATOM    965  NH2 ARG A 138     -21.775 -29.432  16.923  1.00130.66           N  
ANISOU  965  NH2 ARG A 138    15454  16932  17258   1008   1447    619       N  
ATOM    966  N   ASP A 139     -14.978 -28.756  13.719  1.00 98.09           N  
ANISOU  966  N   ASP A 139    11048  13327  12893   1728    487    710       N  
ATOM    967  CA  ASP A 139     -13.964 -29.750  13.352  1.00 98.41           C  
ANISOU  967  CA  ASP A 139    11143  13331  12917   1843    414    687       C  
ATOM    968  C   ASP A 139     -12.877 -29.205  12.395  1.00100.67           C  
ANISOU  968  C   ASP A 139    11245  13773  13231   1897    300    618       C  
ATOM    969  O   ASP A 139     -12.614 -29.803  11.347  1.00100.30           O  
ANISOU  969  O   ASP A 139    11141  13735  13235   1897    290    562       O  
ATOM    970  CB  ASP A 139     -14.643 -31.017  12.794  1.00101.16           C  
ANISOU  970  CB  ASP A 139    11563  13549  13323   1777    511    662       C  
ATOM    971  CG  ASP A 139     -13.860 -32.307  12.964  1.00113.46           C  
ANISOU  971  CG  ASP A 139    13298  14977  14835   1907    484    670       C  
ATOM    972  OD1 ASP A 139     -13.310 -32.532  14.068  1.00115.12           O  
ANISOU  972  OD1 ASP A 139    13696  15109  14937   2040    445    731       O  
ATOM    973  OD2 ASP A 139     -13.861 -33.128  12.021  1.00119.81           O  
ANISOU  973  OD2 ASP A 139    14076  15745  15702   1885    504    614       O  
ATOM    974  N   LEU A 140     -12.225 -28.089  12.779  1.00 96.03           N  
ANISOU  974  N   LEU A 140    10577  13299  12611   1931    234    610       N  
ATOM    975  CA  LEU A 140     -11.155 -27.483  11.978  1.00 95.13           C  
ANISOU  975  CA  LEU A 140    10296  13320  12527   1957    166    526       C  
ATOM    976  C   LEU A 140      -9.832 -28.223  12.186  1.00 99.27           C  
ANISOU  976  C   LEU A 140    10832  13850  13036   2115     63    462       C  
ATOM    977  O   LEU A 140      -9.330 -28.290  13.312  1.00 99.76           O  
ANISOU  977  O   LEU A 140    10979  13895  13030   2234    -15    471       O  
ATOM    978  CB  LEU A 140     -10.989 -25.983  12.288  1.00 94.51           C  
ANISOU  978  CB  LEU A 140    10125  13348  12434   1910    162    519       C  
ATOM    979  CG  LEU A 140     -12.046 -25.031  11.732  1.00 98.21           C  
ANISOU  979  CG  LEU A 140    10544  13844  12929   1781    241    552       C  
ATOM    980  CD1 LEU A 140     -12.109 -23.765  12.553  1.00 98.06           C  
ANISOU  980  CD1 LEU A 140    10515  13869  12876   1755    251    575       C  
ATOM    981  CD2 LEU A 140     -11.784 -24.694  10.271  1.00100.23           C  
ANISOU  981  CD2 LEU A 140    10695  14167  13219   1732    258    495       C  
ATOM    982  N   LYS A 141      -9.284 -28.792  11.094  1.00 95.26           N  
ANISOU  982  N   LYS A 141    10243  13365  12586   2131     56    385       N  
ATOM    983  CA  LYS A 141      -8.026 -29.556  11.066  1.00 95.91           C  
ANISOU  983  CA  LYS A 141    10300  13460  12682   2289    -38    293       C  
ATOM    984  C   LYS A 141      -7.456 -29.657   9.630  1.00 98.79           C  
ANISOU  984  C   LYS A 141    10514  13897  13127   2244     -4    186       C  
ATOM    985  O   LYS A 141      -8.250 -29.614   8.686  1.00 97.57           O  
ANISOU  985  O   LYS A 141    10354  13726  12992   2116     84    213       O  
ATOM    986  CB  LYS A 141      -8.198 -30.955  11.710  1.00 99.61           C  
ANISOU  986  CB  LYS A 141    10985  13761  13099   2420    -67    352       C  
ATOM    987  CG  LYS A 141      -9.305 -31.827  11.122  1.00112.56           C  
ANISOU  987  CG  LYS A 141    12738  15267  14765   2316     51    411       C  
ATOM    988  CD  LYS A 141      -9.639 -32.979  12.054  1.00123.17           C  
ANISOU  988  CD  LYS A 141    14351  16411  16036   2411     67    490       C  
ATOM    989  CE  LYS A 141     -10.649 -33.921  11.452  1.00133.65           C  
ANISOU  989  CE  LYS A 141    15775  17597  17409   2293    203    512       C  
ATOM    990  NZ  LYS A 141     -11.160 -34.891  12.454  1.00143.95           N  
ANISOU  990  NZ  LYS A 141    17380  18677  18636   2338    277    598       N  
ATOM    991  N   PRO A 142      -6.116 -29.827   9.428  1.00 95.69           N  
ANISOU  991  N   PRO A 142     9997  13582  12778   2353    -72     48       N  
ATOM    992  CA  PRO A 142      -5.578 -29.932   8.053  1.00 95.31           C  
ANISOU  992  CA  PRO A 142     9820  13592  12803   2295     -8    -63       C  
ATOM    993  C   PRO A 142      -6.134 -31.089   7.218  1.00 98.39           C  
ANISOU  993  C   PRO A 142    10306  13874  13204   2282     40    -34       C  
ATOM    994  O   PRO A 142      -5.958 -31.097   6.000  1.00 97.90           O  
ANISOU  994  O   PRO A 142    10169  13849  13178   2205    113   -104       O  
ATOM    995  CB  PRO A 142      -4.066 -30.066   8.269  1.00 98.62           C  
ANISOU  995  CB  PRO A 142    10089  14102  13279   2440    -98   -234       C  
ATOM    996  CG  PRO A 142      -3.820 -29.513   9.622  1.00103.53           C  
ANISOU  996  CG  PRO A 142    10716  14765  13857   2527   -206   -225       C  
ATOM    997  CD  PRO A 142      -5.024 -29.893  10.419  1.00 98.54           C  
ANISOU  997  CD  PRO A 142    10320  13992  13127   2535   -212    -35       C  
ATOM    998  N   GLU A 143      -6.807 -32.055   7.869  1.00 94.61           N  
ANISOU  998  N   GLU A 143    10008  13251  12687   2347     16     62       N  
ATOM    999  CA  GLU A 143      -7.454 -33.195   7.220  1.00 94.35           C  
ANISOU  999  CA  GLU A 143    10084  13093  12670   2318     76     84       C  
ATOM   1000  C   GLU A 143      -8.741 -32.710   6.540  1.00 96.02           C  
ANISOU 1000  C   GLU A 143    10294  13311  12879   2124    170    139       C  
ATOM   1001  O   GLU A 143      -9.033 -33.123   5.417  1.00 95.57           O  
ANISOU 1001  O   GLU A 143    10217  13246  12848   2053    221     91       O  
ATOM   1002  CB  GLU A 143      -7.766 -34.303   8.244  1.00 96.84           C  
ANISOU 1002  CB  GLU A 143    10625  13230  12941   2436     50    164       C  
ATOM   1003  CG  GLU A 143      -6.534 -34.991   8.814  1.00109.30           C  
ANISOU 1003  CG  GLU A 143    12241  14781  14507   2677    -71    102       C  
ATOM   1004  CD  GLU A 143      -6.005 -34.443  10.127  1.00130.72           C  
ANISOU 1004  CD  GLU A 143    14979  17539  17151   2816   -192    123       C  
ATOM   1005  OE1 GLU A 143      -5.876 -33.204  10.258  1.00123.72           O  
ANISOU 1005  OE1 GLU A 143    13940  16799  16270   2734   -204    103       O  
ATOM   1006  OE2 GLU A 143      -5.674 -35.263  11.014  1.00127.07           O  
ANISOU 1006  OE2 GLU A 143    14703  16960  16619   3020   -282    151       O  
ATOM   1007  N   ASN A 144      -9.488 -31.811   7.218  1.00 91.00           N  
ANISOU 1007  N   ASN A 144     9672  12696  12207   2054    182    223       N  
ATOM   1008  CA  ASN A 144     -10.730 -31.213   6.725  1.00 89.53           C  
ANISOU 1008  CA  ASN A 144     9466  12531  12020   1902    244    262       C  
ATOM   1009  C   ASN A 144     -10.481 -30.025   5.787  1.00 91.98           C  
ANISOU 1009  C   ASN A 144     9651  12977  12319   1835    254    221       C  
ATOM   1010  O   ASN A 144     -11.386 -29.635   5.046  1.00 91.11           O  
ANISOU 1010  O   ASN A 144     9529  12890  12197   1743    283    228       O  
ATOM   1011  CB  ASN A 144     -11.638 -30.808   7.893  1.00 89.72           C  
ANISOU 1011  CB  ASN A 144     9566  12507  12018   1868    263    358       C  
ATOM   1012  CG  ASN A 144     -12.408 -31.946   8.530  1.00112.93           C  
ANISOU 1012  CG  ASN A 144    12666  15281  14963   1862    320    400       C  
ATOM   1013  OD1 ASN A 144     -12.056 -33.128   8.423  1.00107.86           O  
ANISOU 1013  OD1 ASN A 144    12117  14534  14330   1926    327    376       O  
ATOM   1014  ND2 ASN A 144     -13.477 -31.606   9.231  1.00104.88           N  
ANISOU 1014  ND2 ASN A 144    11693  14219  13937   1780    382    457       N  
ATOM   1015  N   VAL A 145      -9.256 -29.461   5.816  1.00 88.14           N  
ANISOU 1015  N   VAL A 145     9082  12575  11835   1884    234    163       N  
ATOM   1016  CA  VAL A 145      -8.857 -28.327   4.978  1.00 87.34           C  
ANISOU 1016  CA  VAL A 145     8896  12574  11716   1810    283    115       C  
ATOM   1017  C   VAL A 145      -8.156 -28.844   3.723  1.00 91.53           C  
ANISOU 1017  C   VAL A 145     9388  13125  12264   1805    327      9       C  
ATOM   1018  O   VAL A 145      -7.141 -29.533   3.816  1.00 91.82           O  
ANISOU 1018  O   VAL A 145     9372  13166  12352   1890    307    -78       O  
ATOM   1019  CB  VAL A 145      -8.027 -27.278   5.761  1.00 91.13           C  
ANISOU 1019  CB  VAL A 145     9301  13129  12197   1823    275     91       C  
ATOM   1020  CG1 VAL A 145      -7.590 -26.124   4.860  1.00 90.83           C  
ANISOU 1020  CG1 VAL A 145     9210  13162  12139   1725    370     35       C  
ATOM   1021  CG2 VAL A 145      -8.816 -26.755   6.957  1.00 90.34           C  
ANISOU 1021  CG2 VAL A 145     9258  13003  12066   1821    242    197       C  
ATOM   1022  N   LEU A 146      -8.723 -28.522   2.554  1.00 87.90           N  
ANISOU 1022  N   LEU A 146     8965  12677  11755   1721    379     10       N  
ATOM   1023  CA  LEU A 146      -8.231 -28.971   1.253  1.00 88.45           C  
ANISOU 1023  CA  LEU A 146     9034  12757  11814   1701    436    -84       C  
ATOM   1024  C   LEU A 146      -7.589 -27.857   0.422  1.00 92.85           C  
ANISOU 1024  C   LEU A 146     9584  13378  12317   1627    541   -137       C  
ATOM   1025  O   LEU A 146      -7.812 -26.675   0.687  1.00 91.89           O  
ANISOU 1025  O   LEU A 146     9484  13280  12150   1581    566    -81       O  
ATOM   1026  CB  LEU A 146      -9.371 -29.643   0.472  1.00 88.46           C  
ANISOU 1026  CB  LEU A 146     9118  12713  11780   1671    414    -64       C  
ATOM   1027  CG  LEU A 146      -9.927 -30.936   1.063  1.00 93.33           C  
ANISOU 1027  CG  LEU A 146     9761  13239  12461   1715    365    -53       C  
ATOM   1028  CD1 LEU A 146     -11.127 -31.411   0.287  1.00 93.16           C  
ANISOU 1028  CD1 LEU A 146     9783  13187  12425   1657    336     -5       C  
ATOM   1029  CD2 LEU A 146      -8.872 -32.013   1.108  1.00 96.71           C  
ANISOU 1029  CD2 LEU A 146    10196  13630  12921   1746    390   -152       C  
ATOM   1030  N   LEU A 147      -6.785 -28.250  -0.582  1.00 90.65           N  
ANISOU 1030  N   LEU A 147     9292  13112  12041   1611    621   -249       N  
ATOM   1031  CA  LEU A 147      -6.072 -27.357  -1.500  1.00 91.33           C  
ANISOU 1031  CA  LEU A 147     9401  13232  12071   1524    769   -322       C  
ATOM   1032  C   LEU A 147      -6.371 -27.738  -2.950  1.00 96.58           C  
ANISOU 1032  C   LEU A 147    10189  13870  12638   1489    825   -351       C  
ATOM   1033  O   LEU A 147      -6.821 -28.856  -3.205  1.00 96.19           O  
ANISOU 1033  O   LEU A 147    10152  13790  12604   1537    751   -359       O  
ATOM   1034  CB  LEU A 147      -4.554 -27.442  -1.249  1.00 92.33           C  
ANISOU 1034  CB  LEU A 147     9365  13407  12308   1530    845   -478       C  
ATOM   1035  CG  LEU A 147      -4.041 -26.918   0.089  1.00 96.76           C  
ANISOU 1035  CG  LEU A 147     9794  14015  12953   1565    793   -493       C  
ATOM   1036  CD1 LEU A 147      -2.807 -27.675   0.524  1.00 98.03           C  
ANISOU 1036  CD1 LEU A 147     9773  14224  13249   1659    760   -656       C  
ATOM   1037  CD2 LEU A 147      -3.764 -25.426   0.029  1.00 99.31           C  
ANISOU 1037  CD2 LEU A 147    10130  14365  13238   1444    923   -507       C  
ATOM   1038  N   ASP A 148      -6.109 -26.816  -3.897  1.00 94.50           N  
ANISOU 1038  N   ASP A 148    10039  13606  12262   1405    965   -374       N  
ATOM   1039  CA  ASP A 148      -6.313 -27.039  -5.332  1.00 95.60           C  
ANISOU 1039  CA  ASP A 148    10337  13718  12270   1377   1030   -406       C  
ATOM   1040  C   ASP A 148      -4.968 -27.037  -6.090  1.00102.02           C  
ANISOU 1040  C   ASP A 148    11133  14534  13097   1302   1236   -560       C  
ATOM   1041  O   ASP A 148      -3.910 -27.056  -5.454  1.00101.90           O  
ANISOU 1041  O   ASP A 148    10936  14556  13226   1289   1299   -663       O  
ATOM   1042  CB  ASP A 148      -7.297 -25.997  -5.907  1.00 97.38           C  
ANISOU 1042  CB  ASP A 148    10778  13916  12308   1364   1018   -295       C  
ATOM   1043  CG  ASP A 148      -6.739 -24.591  -6.027  1.00107.39           C  
ANISOU 1043  CG  ASP A 148    12149  15157  13497   1282   1189   -283       C  
ATOM   1044  OD1 ASP A 148      -6.232 -24.065  -5.015  1.00107.13           O  
ANISOU 1044  OD1 ASP A 148    11985  15144  13574   1250   1222   -288       O  
ATOM   1045  OD2 ASP A 148      -6.819 -24.016  -7.132  1.00114.62           O  
ANISOU 1045  OD2 ASP A 148    13298  16022  14231   1249   1294   -274       O  
ATOM   1046  N   ALA A 149      -5.014 -27.020  -7.440  1.00100.57           N  
ANISOU 1046  N   ALA A 149    11137  14316  12761   1258   1341   -593       N  
ATOM   1047  CA  ALA A 149      -3.834 -27.001  -8.311  1.00102.47           C  
ANISOU 1047  CA  ALA A 149    11398  14544  12991   1168   1574   -747       C  
ATOM   1048  C   ALA A 149      -3.040 -25.692  -8.199  1.00107.98           C  
ANISOU 1048  C   ALA A 149    12119  15227  13680   1047   1789   -786       C  
ATOM   1049  O   ALA A 149      -1.821 -25.703  -8.380  1.00108.90           O  
ANISOU 1049  O   ALA A 149    12121  15360  13895    961   1984   -959       O  
ATOM   1050  CB  ALA A 149      -4.249 -27.238  -9.754  1.00104.32           C  
ANISOU 1050  CB  ALA A 149    11882  14731  13024   1156   1626   -750       C  
ATOM   1051  N   HIS A 150      -3.732 -24.575  -7.897  1.00104.56           N  
ANISOU 1051  N   HIS A 150    11825  14761  13142   1036   1761   -645       N  
ATOM   1052  CA  HIS A 150      -3.134 -23.242  -7.757  1.00105.50           C  
ANISOU 1052  CA  HIS A 150    12005  14841  13239    913   1969   -666       C  
ATOM   1053  C   HIS A 150      -2.762 -22.902  -6.299  1.00108.62           C  
ANISOU 1053  C   HIS A 150    12142  15300  13828    912   1905   -688       C  
ATOM   1054  O   HIS A 150      -2.359 -21.769  -6.016  1.00108.72           O  
ANISOU 1054  O   HIS A 150    12183  15284  13840    808   2057   -707       O  
ATOM   1055  CB  HIS A 150      -4.055 -22.174  -8.374  1.00106.73           C  
ANISOU 1055  CB  HIS A 150    12510  14900  13144    915   1995   -507       C  
ATOM   1056  CG  HIS A 150      -4.414 -22.451  -9.800  1.00111.50           C  
ANISOU 1056  CG  HIS A 150    13396  15443  13526    937   2038   -492       C  
ATOM   1057  ND1 HIS A 150      -5.605 -23.068 -10.137  1.00112.63           N  
ANISOU 1057  ND1 HIS A 150    13622  15607  13566   1078   1792   -397       N  
ATOM   1058  CD2 HIS A 150      -3.707 -22.219 -10.931  1.00115.39           C  
ANISOU 1058  CD2 HIS A 150    14096  15859  13887    831   2304   -581       C  
ATOM   1059  CE1 HIS A 150      -5.594 -23.174 -11.455  1.00113.71           C  
ANISOU 1059  CE1 HIS A 150    14018  15687  13500   1069   1889   -426       C  
ATOM   1060  NE2 HIS A 150      -4.472 -22.678 -11.977  1.00115.73           N  
ANISOU 1060  NE2 HIS A 150    14375  15875  13722    923   2204   -526       N  
ATOM   1061  N   MET A 151      -2.868 -23.903  -5.393  1.00104.21           N  
ANISOU 1061  N   MET A 151    11352  14818  13424   1028   1691   -693       N  
ATOM   1062  CA  MET A 151      -2.564 -23.840  -3.957  1.00103.32           C  
ANISOU 1062  CA  MET A 151    11003  14773  13479   1071   1579   -715       C  
ATOM   1063  C   MET A 151      -3.358 -22.754  -3.209  1.00106.01           C  
ANISOU 1063  C   MET A 151    11429  15090  13759   1066   1516   -562       C  
ATOM   1064  O   MET A 151      -2.831 -21.681  -2.905  1.00106.04           O  
ANISOU 1064  O   MET A 151    11419  15088  13783    966   1654   -611       O  
ATOM   1065  CB  MET A 151      -1.049 -23.722  -3.697  1.00107.20           C  
ANISOU 1065  CB  MET A 151    11266  15328  14138    993   1733   -947       C  
ATOM   1066  CG  MET A 151      -0.331 -25.058  -3.683  1.00111.61           C  
ANISOU 1066  CG  MET A 151    11619  15947  14839   1088   1665  -1096       C  
ATOM   1067  SD  MET A 151      -0.791 -26.129  -2.292  1.00114.50           S  
ANISOU 1067  SD  MET A 151    11839  16356  15308   1302   1337  -1011       S  
ATOM   1068  CE  MET A 151      -0.020 -25.254  -0.929  1.00111.52           C  
ANISOU 1068  CE  MET A 151    11247  16066  15059   1294   1311  -1110       C  
ATOM   1069  N   ASN A 152      -4.638 -23.047  -2.927  1.00101.25           N  
ANISOU 1069  N   ASN A 152    10909  14470  13092   1168   1321   -395       N  
ATOM   1070  CA  ASN A 152      -5.552 -22.165  -2.197  1.00100.02           C  
ANISOU 1070  CA  ASN A 152    10823  14294  12886   1188   1237   -251       C  
ATOM   1071  C   ASN A 152      -6.406 -22.995  -1.241  1.00102.42           C  
ANISOU 1071  C   ASN A 152    11029  14626  13258   1305   1011   -165       C  
ATOM   1072  O   ASN A 152      -6.973 -24.012  -1.649  1.00101.70           O  
ANISOU 1072  O   ASN A 152    10957  14528  13155   1368    914   -145       O  
ATOM   1073  CB  ASN A 152      -6.431 -21.345  -3.154  1.00101.28           C  
ANISOU 1073  CB  ASN A 152    11262  14376  12845   1177   1284   -139       C  
ATOM   1074  CG  ASN A 152      -5.665 -20.416  -4.069  1.00126.75           C  
ANISOU 1074  CG  ASN A 152    14657  17533  15968   1054   1542   -203       C  
ATOM   1075  OD1 ASN A 152      -4.998 -19.472  -3.630  1.00122.14           O  
ANISOU 1075  OD1 ASN A 152    14049  16930  15428    953   1692   -253       O  
ATOM   1076  ND2 ASN A 152      -5.760 -20.655  -5.368  1.00119.57           N  
ANISOU 1076  ND2 ASN A 152    13943  16575  14912   1051   1612   -210       N  
ATOM   1077  N   ALA A 153      -6.470 -22.571   0.037  1.00 98.30           N  
ANISOU 1077  N   ALA A 153    10412  14128  12808   1323    945   -127       N  
ATOM   1078  CA  ALA A 153      -7.217 -23.244   1.104  1.00 97.05           C  
ANISOU 1078  CA  ALA A 153    10187  13980  12709   1418    769    -47       C  
ATOM   1079  C   ALA A 153      -8.725 -23.269   0.852  1.00100.34           C  
ANISOU 1079  C   ALA A 153    10723  14358  13043   1453    678     80       C  
ATOM   1080  O   ALA A 153      -9.288 -22.287   0.368  1.00100.02           O  
ANISOU 1080  O   ALA A 153    10811  14293  12900   1429    715    140       O  
ATOM   1081  CB  ALA A 153      -6.919 -22.591   2.445  1.00 97.42           C  
ANISOU 1081  CB  ALA A 153    10142  14055  12817   1418    744    -42       C  
ATOM   1082  N   LYS A 154      -9.364 -24.414   1.154  1.00 96.54           N  
ANISOU 1082  N   LYS A 154    10204  13866  12610   1516    563    104       N  
ATOM   1083  CA  LYS A 154     -10.800 -24.662   0.997  1.00 96.02           C  
ANISOU 1083  CA  LYS A 154    10198  13777  12508   1542    472    176       C  
ATOM   1084  C   LYS A 154     -11.272 -25.514   2.181  1.00 99.76           C  
ANISOU 1084  C   LYS A 154    10601  14226  13076   1580    393    208       C  
ATOM   1085  O   LYS A 154     -10.759 -26.616   2.379  1.00 99.58           O  
ANISOU 1085  O   LYS A 154    10539  14182  13116   1611    380    162       O  
ATOM   1086  CB  LYS A 154     -11.094 -25.394  -0.333  1.00 99.14           C  
ANISOU 1086  CB  LYS A 154    10655  14166  12848   1547    460    125       C  
ATOM   1087  CG  LYS A 154     -10.792 -24.611  -1.613  1.00113.78           C  
ANISOU 1087  CG  LYS A 154    12642  16022  14566   1519    544    103       C  
ATOM   1088  N   ILE A 155     -12.226 -25.000   2.976  1.00 96.22           N  
ANISOU 1088  N   ILE A 155    10157  13768  12633   1581    354    283       N  
ATOM   1089  CA  ILE A 155     -12.747 -25.707   4.152  1.00 96.06           C  
ANISOU 1089  CA  ILE A 155    10110  13705  12684   1599    315    318       C  
ATOM   1090  C   ILE A 155     -13.946 -26.592   3.778  1.00101.28           C  
ANISOU 1090  C   ILE A 155    10778  14331  13375   1584    282    300       C  
ATOM   1091  O   ILE A 155     -14.900 -26.115   3.160  1.00101.02           O  
ANISOU 1091  O   ILE A 155    10746  14327  13311   1570    252    293       O  
ATOM   1092  CB  ILE A 155     -13.030 -24.722   5.330  1.00 98.59           C  
ANISOU 1092  CB  ILE A 155    10426  14029  13003   1595    319    388       C  
ATOM   1093  CG1 ILE A 155     -11.699 -24.176   5.904  1.00 98.97           C  
ANISOU 1093  CG1 ILE A 155    10444  14110  13049   1608    345    368       C  
ATOM   1094  CG2 ILE A 155     -13.888 -25.371   6.438  1.00 99.31           C  
ANISOU 1094  CG2 ILE A 155    10529  14060  13145   1597    305    429       C  
ATOM   1095  CD1 ILE A 155     -11.805 -22.954   6.823  1.00106.02           C  
ANISOU 1095  CD1 ILE A 155    11340  15019  13924   1590    361    415       C  
ATOM   1096  N   ALA A 156     -13.879 -27.885   4.158  1.00 99.03           N  
ANISOU 1096  N   ALA A 156    10501  13977  13149   1592    287    278       N  
ATOM   1097  CA  ALA A 156     -14.920 -28.886   3.906  1.00 99.83           C  
ANISOU 1097  CA  ALA A 156    10605  14024  13302   1552    287    234       C  
ATOM   1098  C   ALA A 156     -15.337 -29.623   5.194  1.00104.92           C  
ANISOU 1098  C   ALA A 156    11296  14563  14006   1537    333    271       C  
ATOM   1099  O   ALA A 156     -14.813 -29.319   6.270  1.00104.16           O  
ANISOU 1099  O   ALA A 156    11240  14445  13892   1578    341    339       O  
ATOM   1100  CB  ALA A 156     -14.440 -29.879   2.857  1.00101.20           C  
ANISOU 1100  CB  ALA A 156    10793  14182  13477   1559    287    154       C  
ATOM   1101  N   ASP A 157     -16.287 -30.586   5.072  1.00103.09           N  
ANISOU 1101  N   ASP A 157    11072  14260  13838   1471    372    213       N  
ATOM   1102  CA  ASP A 157     -16.850 -31.422   6.144  1.00104.00           C  
ANISOU 1102  CA  ASP A 157    11268  14239  14006   1426    462    231       C  
ATOM   1103  C   ASP A 157     -17.539 -30.582   7.235  1.00108.34           C  
ANISOU 1103  C   ASP A 157    11812  14792  14560   1394    499    291       C  
ATOM   1104  O   ASP A 157     -17.022 -30.442   8.347  1.00107.73           O  
ANISOU 1104  O   ASP A 157    11831  14663  14439   1442    521    378       O  
ATOM   1105  CB  ASP A 157     -15.801 -32.405   6.723  1.00106.36           C  
ANISOU 1105  CB  ASP A 157    11710  14421  14282   1506    486    274       C  
ATOM   1106  CG  ASP A 157     -16.378 -33.642   7.392  1.00117.78           C  
ANISOU 1106  CG  ASP A 157    13299  15682  15769   1454    602    268       C  
ATOM   1107  OD1 ASP A 157     -16.033 -34.763   6.963  1.00119.15           O  
ANISOU 1107  OD1 ASP A 157    13548  15764  15961   1473    627    225       O  
ATOM   1108  OD2 ASP A 157     -17.142 -33.489   8.373  1.00123.95           O  
ANISOU 1108  OD2 ASP A 157    14137  16396  16561   1392    688    306       O  
ATOM   1109  N   PHE A 158     -18.722 -30.034   6.902  1.00105.66           N  
ANISOU 1109  N   PHE A 158    11356  14517  14271   1324    497    228       N  
ATOM   1110  CA  PHE A 158     -19.532 -29.213   7.806  1.00105.71           C  
ANISOU 1110  CA  PHE A 158    11329  14534  14300   1289    540    257       C  
ATOM   1111  C   PHE A 158     -20.505 -30.044   8.671  1.00111.76           C  
ANISOU 1111  C   PHE A 158    12142  15171  15152   1175    692    214       C  
ATOM   1112  O   PHE A 158     -21.398 -29.481   9.309  1.00111.59           O  
ANISOU 1112  O   PHE A 158    12067  15157  15175   1120    754    198       O  
ATOM   1113  CB  PHE A 158     -20.275 -28.118   7.017  1.00107.28           C  
ANISOU 1113  CB  PHE A 158    11380  14871  14509   1300    452    200       C  
ATOM   1114  CG  PHE A 158     -19.484 -26.851   6.798  1.00107.75           C  
ANISOU 1114  CG  PHE A 158    11452  15019  14471   1393    369    284       C  
ATOM   1115  CD1 PHE A 158     -18.653 -26.712   5.692  1.00110.58           C  
ANISOU 1115  CD1 PHE A 158    11826  15433  14756   1449    295    281       C  
ATOM   1116  CD2 PHE A 158     -19.586 -25.786   7.685  1.00109.38           C  
ANISOU 1116  CD2 PHE A 158    11664  15239  14656   1409    387    354       C  
ATOM   1117  CE1 PHE A 158     -17.925 -25.536   5.487  1.00110.80           C  
ANISOU 1117  CE1 PHE A 158    11882  15519  14697   1508    259    345       C  
ATOM   1118  CE2 PHE A 158     -18.858 -24.610   7.478  1.00111.43           C  
ANISOU 1118  CE2 PHE A 158    11946  15562  14831   1474    335    417       C  
ATOM   1119  CZ  PHE A 158     -18.034 -24.492   6.381  1.00109.35           C  
ANISOU 1119  CZ  PHE A 158    11704  15343  14501   1517    280    411       C  
ATOM   1120  N   GLY A 159     -20.292 -31.362   8.710  1.00110.02           N  
ANISOU 1120  N   GLY A 159    12034  14818  14950   1140    771    192       N  
ATOM   1121  CA  GLY A 159     -21.103 -32.308   9.473  1.00111.69           C  
ANISOU 1121  CA  GLY A 159    12342  14865  15232   1015    957    148       C  
ATOM   1122  C   GLY A 159     -21.000 -32.182  10.982  1.00116.66           C  
ANISOU 1122  C   GLY A 159    13154  15375  15796   1021   1068    263       C  
ATOM   1123  O   GLY A 159     -21.842 -32.724  11.704  1.00117.53           O  
ANISOU 1123  O   GLY A 159    13350  15347  15958    897   1256    224       O  
ATOM   1124  N   LEU A 160     -19.966 -31.469  11.469  1.00112.91           N  
ANISOU 1124  N   LEU A 160    12747  14950  15203   1159    962    391       N  
ATOM   1125  CA  LEU A 160     -19.717 -31.238  12.895  1.00113.34           C  
ANISOU 1125  CA  LEU A 160    12985  14915  15163   1198   1026    503       C  
ATOM   1126  C   LEU A 160     -19.967 -29.770  13.295  1.00116.97           C  
ANISOU 1126  C   LEU A 160    13328  15506  15610   1207    978    531       C  
ATOM   1127  O   LEU A 160     -19.748 -29.404  14.453  1.00116.61           O  
ANISOU 1127  O   LEU A 160    13417  15412  15477   1244   1013    616       O  
ATOM   1128  CB  LEU A 160     -18.289 -31.677  13.273  1.00113.42           C  
ANISOU 1128  CB  LEU A 160    13179  14869  15046   1365    933    601       C  
ATOM   1129  N   SER A 161     -20.444 -28.942  12.342  1.00113.44           N  
ANISOU 1129  N   SER A 161    12650  15214  15237   1184    898    458       N  
ATOM   1130  CA  SER A 161     -20.737 -27.525  12.566  1.00112.74           C  
ANISOU 1130  CA  SER A 161    12453  15240  15144   1201    853    475       C  
ATOM   1131  C   SER A 161     -22.109 -27.308  13.204  1.00118.32           C  
ANISOU 1131  C   SER A 161    13106  15912  15940   1086    996    409       C  
ATOM   1132  O   SER A 161     -23.044 -28.060  12.921  1.00119.07           O  
ANISOU 1132  O   SER A 161    13139  15958  16146    976   1096    293       O  
ATOM   1133  CB  SER A 161     -20.618 -26.731  11.267  1.00115.35           C  
ANISOU 1133  CB  SER A 161    12612  15726  15489   1255    705    433       C  
ATOM   1134  OG  SER A 161     -21.689 -26.992  10.375  1.00124.67           O  
ANISOU 1134  OG  SER A 161    13645  16950  16775   1192    703    303       O  
ATOM   1135  N   ASN A 162     -22.228 -26.271  14.056  1.00115.17           N  
ANISOU 1135  N   ASN A 162    12717  15541  15503   1104   1015    461       N  
ATOM   1136  CA  ASN A 162     -23.477 -25.932  14.740  1.00116.24           C  
ANISOU 1136  CA  ASN A 162    12792  15650  15724   1002   1160    391       C  
ATOM   1137  C   ASN A 162     -23.773 -24.431  14.716  1.00120.02           C  
ANISOU 1137  C   ASN A 162    13135  16254  16213   1058   1082    388       C  
ATOM   1138  O   ASN A 162     -22.847 -23.616  14.682  1.00118.31           O  
ANISOU 1138  O   ASN A 162    12957  16099  15898   1160    965    482       O  
ATOM   1139  CB  ASN A 162     -23.478 -26.465  16.176  1.00118.34           C  
ANISOU 1139  CB  ASN A 162    13295  15747  15920    942   1344    456       C  
ATOM   1140  CG  ASN A 162     -24.789 -26.283  16.909  1.00144.16           C  
ANISOU 1140  CG  ASN A 162    16541  18921  19313    772   1578    335       C  
ATOM   1141  OD1 ASN A 162     -25.637 -25.454  16.551  1.00139.15           O  
ANISOU 1141  OD1 ASN A 162    15672  18376  18822    710   1601    199       O  
ATOM   1142  ND2 ASN A 162     -24.975 -27.044  17.977  1.00137.71           N  
ANISOU 1142  ND2 ASN A 162    15975  17909  18439    696   1765    372       N  
ATOM   1143  N   MET A 163     -25.071 -24.077  14.738  1.00118.22           N  
ANISOU 1143  N   MET A 163    12744  16058  16115    990   1157    263       N  
ATOM   1144  CA  MET A 163     -25.560 -22.696  14.710  1.00118.14           C  
ANISOU 1144  CA  MET A 163    12601  16152  16133   1053   1095    238       C  
ATOM   1145  C   MET A 163     -25.287 -21.937  16.007  1.00122.41           C  
ANISOU 1145  C   MET A 163    13275  16644  16590   1057   1178    337       C  
ATOM   1146  O   MET A 163     -25.277 -22.536  17.085  1.00122.61           O  
ANISOU 1146  O   MET A 163    13461  16549  16576    976   1337    372       O  
ATOM   1147  CB  MET A 163     -27.062 -22.658  14.378  1.00122.04           C  
ANISOU 1147  CB  MET A 163    12861  16699  16809    993   1145     40       C  
ATOM   1148  CG  MET A 163     -27.371 -22.877  12.906  1.00126.09           C  
ANISOU 1148  CG  MET A 163    13201  17320  17388   1050    981    -74       C  
ATOM   1149  SD  MET A 163     -26.873 -21.508  11.826  1.00129.22           S  
ANISOU 1149  SD  MET A 163    13567  17850  17681   1259    725     -4       S  
ATOM   1150  CE  MET A 163     -28.181 -20.333  12.156  1.00127.10           C  
ANISOU 1150  CE  MET A 163    13116  17652  17525   1315    727   -126       C  
ATOM   1151  N   MET A 164     -25.080 -20.612  15.894  1.00118.79           N  
ANISOU 1151  N   MET A 164    12773  16268  16092   1154   1077    377       N  
ATOM   1152  CA  MET A 164     -24.823 -19.723  17.028  1.00118.62           C  
ANISOU 1152  CA  MET A 164    12859  16219  15994   1166   1137    453       C  
ATOM   1153  C   MET A 164     -26.127 -19.084  17.514  1.00124.37           C  
ANISOU 1153  C   MET A 164    13463  16955  16837   1126   1248    348       C  
ATOM   1154  O   MET A 164     -26.580 -18.083  16.951  1.00123.93           O  
ANISOU 1154  O   MET A 164    13271  16983  16833   1210   1158    300       O  
ATOM   1155  CB  MET A 164     -23.771 -18.656  16.673  1.00119.65           C  
ANISOU 1155  CB  MET A 164    13029  16415  16019   1276    991    546       C  
ATOM   1156  CG  MET A 164     -22.366 -19.201  16.584  1.00122.52           C  
ANISOU 1156  CG  MET A 164    13518  16764  16268   1305    916    634       C  
ATOM   1157  SD  MET A 164     -21.115 -17.947  16.946  1.00125.79           S  
ANISOU 1157  SD  MET A 164    14016  17218  16560   1372    843    715       S  
ATOM   1158  CE  MET A 164     -20.829 -17.290  15.331  1.00121.86           C  
ANISOU 1158  CE  MET A 164    13420  16803  16077   1441    719    700       C  
ATOM   1159  N   SER A 165     -26.742 -19.687  18.545  1.00122.75           N  
ANISOU 1159  N   SER A 165    13318  16652  16669   1001   1454    303       N  
ATOM   1160  CA  SER A 165     -27.998 -19.214  19.130  1.00124.19           C  
ANISOU 1160  CA  SER A 165    13378  16830  16977    937   1605    177       C  
ATOM   1161  C   SER A 165     -27.748 -18.163  20.210  1.00128.32           C  
ANISOU 1161  C   SER A 165    14022  17328  17405    964   1660    255       C  
ATOM   1162  O   SER A 165     -26.808 -18.303  20.998  1.00127.33           O  
ANISOU 1162  O   SER A 165    14129  17133  17117    961   1682    385       O  
ATOM   1163  CB  SER A 165     -28.798 -20.380  19.701  1.00129.53           C  
ANISOU 1163  CB  SER A 165    14077  17397  17743    761   1846     72       C  
ATOM   1164  OG  SER A 165     -29.127 -21.324  18.695  1.00138.91           O  
ANISOU 1164  OG  SER A 165    15130  18609  19040    721   1807    -32       O  
ATOM   1165  N   ASP A 166     -28.591 -17.111  20.241  1.00125.92           N  
ANISOU 1165  N   ASP A 166    13558  17083  17202   1004   1671    163       N  
ATOM   1166  CA  ASP A 166     -28.503 -16.016  21.209  1.00125.90           C  
ANISOU 1166  CA  ASP A 166    13646  17060  17132   1028   1732    211       C  
ATOM   1167  C   ASP A 166     -28.870 -16.508  22.610  1.00131.72           C  
ANISOU 1167  C   ASP A 166    14535  17675  17838    883   1992    196       C  
ATOM   1168  O   ASP A 166     -29.979 -17.005  22.822  1.00132.93           O  
ANISOU 1168  O   ASP A 166    14578  17794  18136    770   2174     49       O  
ATOM   1169  CB  ASP A 166     -29.400 -14.833  20.785  1.00128.28           C  
ANISOU 1169  CB  ASP A 166    13733  17444  17563   1125   1678     99       C  
ATOM   1170  CG  ASP A 166     -29.047 -14.171  19.460  1.00137.10           C  
ANISOU 1170  CG  ASP A 166    14767  18654  18670   1291   1432    128       C  
ATOM   1171  OD1 ASP A 166     -29.679 -13.146  19.124  1.00138.05           O  
ANISOU 1171  OD1 ASP A 166    14766  18826  18863   1406   1369     57       O  
ATOM   1172  OD2 ASP A 166     -28.146 -14.683  18.755  1.00141.90           O  
ANISOU 1172  OD2 ASP A 166    15448  19276  19191   1313   1310    219       O  
ATOM   1173  N   GLY A 167     -27.918 -16.396  23.532  1.00128.32           N  
ANISOU 1173  N   GLY A 167    14363  17180  17215    888   2008    334       N  
ATOM   1174  CA  GLY A 167     -28.075 -16.829  24.916  1.00129.72           C  
ANISOU 1174  CA  GLY A 167    14767  17225  17296    777   2238    352       C  
ATOM   1175  C   GLY A 167     -28.001 -18.333  25.098  1.00135.30           C  
ANISOU 1175  C   GLY A 167    15637  17814  17957    680   2354    373       C  
ATOM   1176  O   GLY A 167     -28.713 -18.888  25.939  1.00136.61           O  
ANISOU 1176  O   GLY A 167    15918  17855  18132    543   2617    316       O  
ATOM   1177  N   GLU A 168     -27.135 -19.002  24.310  1.00131.55           N  
ANISOU 1177  N   GLU A 168    15192  17362  17430    746   2179    451       N  
ATOM   1178  CA  GLU A 168     -26.933 -20.453  24.352  1.00132.53           C  
ANISOU 1178  CA  GLU A 168    15489  17365  17503    682   2261    483       C  
ATOM   1179  C   GLU A 168     -25.462 -20.827  24.193  1.00135.84           C  
ANISOU 1179  C   GLU A 168    16084  17787  17742    811   2055    631       C  
ATOM   1180  O   GLU A 168     -24.768 -20.262  23.345  1.00133.72           O  
ANISOU 1180  O   GLU A 168    15675  17648  17482    921   1829    659       O  
ATOM   1181  CB  GLU A 168     -27.777 -21.158  23.279  1.00134.51           C  
ANISOU 1181  CB  GLU A 168    15502  17642  17963    601   2295    344       C  
ATOM   1182  N   PHE A 169     -24.996 -21.791  25.004  1.00134.14           N  
ANISOU 1182  N   PHE A 169    16185  17420  17361    804   2142    714       N  
ATOM   1183  CA  PHE A 169     -23.619 -22.285  24.982  1.00133.72           C  
ANISOU 1183  CA  PHE A 169    16314  17359  17137    945   1950    833       C  
ATOM   1184  C   PHE A 169     -23.587 -23.748  24.550  1.00139.32           C  
ANISOU 1184  C   PHE A 169    17130  17950  17856    916   2002    841       C  
ATOM   1185  O   PHE A 169     -24.341 -24.565  25.086  1.00140.68           O  
ANISOU 1185  O   PHE A 169    17472  17952  18029    791   2251    816       O  
ATOM   1186  CB  PHE A 169     -22.951 -22.116  26.358  1.00136.38           C  
ANISOU 1186  CB  PHE A 169    16970  17618  17229   1021   1956    926       C  
ATOM   1187  CG  PHE A 169     -22.800 -20.689  26.830  1.00137.23           C  
ANISOU 1187  CG  PHE A 169    16998  17837  17305   1058   1890    917       C  
ATOM   1188  CD1 PHE A 169     -21.662 -19.954  26.520  1.00138.94           C  
ANISOU 1188  CD1 PHE A 169    17128  18194  17469   1189   1639    944       C  
ATOM   1189  CD2 PHE A 169     -23.780 -20.091  27.614  1.00140.32           C  
ANISOU 1189  CD2 PHE A 169    17409  18184  17724    952   2099    866       C  
ATOM   1190  CE1 PHE A 169     -21.517 -18.637  26.967  1.00139.37           C  
ANISOU 1190  CE1 PHE A 169    17122  18335  17498   1207   1598    923       C  
ATOM   1191  CE2 PHE A 169     -23.637 -18.773  28.056  1.00142.58           C  
ANISOU 1191  CE2 PHE A 169    17633  18560  17979    987   2045    853       C  
ATOM   1192  CZ  PHE A 169     -22.505 -18.056  27.732  1.00139.27           C  
ANISOU 1192  CZ  PHE A 169    17140  18271  17506   1112   1795    884       C  
ATOM   1193  N   LEU A 170     -22.726 -24.086  23.597  1.00135.51           N  
ANISOU 1193  N   LEU A 170    16555  17548  17386   1019   1790    867       N  
ATOM   1194  CA  LEU A 170     -22.723 -25.438  23.058  1.00136.38           C  
ANISOU 1194  CA  LEU A 170    16756  17554  17509   1009   1814    873       C  
ATOM   1195  C   LEU A 170     -21.654 -26.292  23.714  1.00142.34           C  
ANISOU 1195  C   LEU A 170    17883  18166  18032   1135   1780    990       C  
ATOM   1196  O   LEU A 170     -20.465 -26.001  23.617  1.00141.25           O  
ANISOU 1196  O   LEU A 170    17800  18109  17760   1295   1580   1052       O  
ATOM   1197  CB  LEU A 170     -22.507 -25.404  21.546  1.00134.87           C  
ANISOU 1197  CB  LEU A 170    16299  17510  17438   1064   1613    833       C  
ATOM   1198  CG  LEU A 170     -22.950 -24.125  20.837  1.00138.92           C  
ANISOU 1198  CG  LEU A 170    16474  18145  18163    969   1624    708       C  
ATOM   1199  CD1 LEU A 170     -21.818 -23.547  20.004  1.00137.41           C  
ANISOU 1199  CD1 LEU A 170    16078  18117  18014   1069   1389    704       C  
ATOM   1200  CD2 LEU A 170     -24.169 -24.386  19.970  1.00142.82           C  
ANISOU 1200  CD2 LEU A 170    16925  18541  18801    811   1818    595       C  
ATOM   1201  N   ARG A 171     -22.093 -27.350  24.386  1.00141.64           N  
ANISOU 1201  N   ARG A 171    18060  17860  17897   1065   1981   1007       N  
ATOM   1202  CA  ARG A 171     -21.188 -28.239  25.101  1.00143.44           C  
ANISOU 1202  CA  ARG A 171    18706  17910  17885   1202   1970   1123       C  
ATOM   1203  C   ARG A 171     -20.793 -29.486  24.318  1.00148.68           C  
ANISOU 1203  C   ARG A 171    19463  18472  18557   1259   1930   1139       C  
ATOM   1204  O   ARG A 171     -19.993 -30.288  24.791  1.00149.62           O  
ANISOU 1204  O   ARG A 171    19920  18455  18475   1424   1867   1234       O  
ATOM   1205  CB  ARG A 171     -21.799 -28.644  26.444  1.00146.18           C  
ANISOU 1205  CB  ARG A 171    19411  18031  18098   1099   2267   1157       C  
HETATM 1206  N   TPO A 172     -21.337 -29.653  23.121  1.00144.98           N  
ANISOU 1206  N   TPO A 172    18705  18068  18311   1141   1952   1039       N  
HETATM 1207  CA  TPO A 172     -21.057 -30.856  22.368  1.00145.52           C  
ANISOU 1207  CA  TPO A 172    18826  18049  18416   1172   1926   1033       C  
HETATM 1208  CB  TPO A 172     -21.861 -30.892  21.079  1.00145.75           C  
ANISOU 1208  CB  TPO A 172    18549  18130  18699    986   2017    889       C  
HETATM 1209  CG2 TPO A 172     -21.613 -32.210  20.356  1.00147.15           C  
ANISOU 1209  CG2 TPO A 172    18913  18119  18877    977   2097    884       C  
HETATM 1210  OG1 TPO A 172     -23.245 -30.755  21.400  1.00147.17           O  
ANISOU 1210  OG1 TPO A 172    18627  18281  19009    762   2270    783       O  
HETATM 1211  P   TPO A 172     -24.404 -31.292  20.419  1.00147.14           P  
ANISOU 1211  P   TPO A 172    18222  18410  19274    598   2303    598       P  
HETATM 1212  O1P TPO A 172     -23.774 -31.240  19.051  1.00149.42           O  
ANISOU 1212  O1P TPO A 172    18622  18493  19659    409   2575    496       O  
HETATM 1213  O2P TPO A 172     -24.688 -32.688  20.917  1.00147.04           O  
ANISOU 1213  O2P TPO A 172    17996  18507  19365    495   2388    511       O  
HETATM 1214  O3P TPO A 172     -25.537 -30.317  20.623  1.00145.19           O  
ANISOU 1214  O3P TPO A 172    17691  18374  19102    711   2016    574       O  
HETATM 1215  C   TPO A 172     -19.588 -30.861  22.083  1.00147.97           C  
ANISOU 1215  C   TPO A 172    19126  18469  18627   1421   1613   1095       C  
HETATM 1216  O   TPO A 172     -19.005 -29.785  21.851  1.00145.56           O  
ANISOU 1216  O   TPO A 172    18505  18390  18410   1468   1414   1054       O  
ATOM   1217  N   SER A 173     -18.966 -32.032  22.122  1.00145.87           N  
ANISOU 1217  N   SER A 173    19221  18030  18172   1585   1580   1186       N  
ATOM   1218  CA  SER A 173     -17.524 -32.120  21.949  1.00145.22           C  
ANISOU 1218  CA  SER A 173    19156  18031  17992   1844   1291   1222       C  
ATOM   1219  C   SER A 173     -17.107 -32.951  20.740  1.00147.88           C  
ANISOU 1219  C   SER A 173    19309  18409  18472   1855   1212   1161       C  
ATOM   1220  O   SER A 173     -17.581 -34.069  20.547  1.00148.26           O  
ANISOU 1220  O   SER A 173    19417  18307  18607   1718   1399   1130       O  
ATOM   1221  CB  SER A 173     -16.879 -32.674  23.216  1.00151.30           C  
ANISOU 1221  CB  SER A 173    20397  18593  18496   2049   1271   1329       C  
ATOM   1222  OG  SER A 173     -17.056 -31.775  24.293  1.00160.90           O  
ANISOU 1222  OG  SER A 173    21793  19788  19555   2059   1317   1382       O  
ATOM   1223  N   CYS A 174     -16.215 -32.385  19.933  1.00142.68           N  
ANISOU 1223  N   CYS A 174    18426  17949  17838   2006    951   1128       N  
ATOM   1224  CA  CYS A 174     -15.672 -33.058  18.757  1.00141.52           C  
ANISOU 1224  CA  CYS A 174    18091  17868  17814   2035    855   1062       C  
ATOM   1225  C   CYS A 174     -14.738 -34.210  19.121  1.00146.13           C  
ANISOU 1225  C   CYS A 174    18961  18271  18291   2221    810   1101       C  
ATOM   1226  O   CYS A 174     -14.062 -34.175  20.147  1.00147.27           O  
ANISOU 1226  O   CYS A 174    19398  18314  18243   2415    736   1173       O  
ATOM   1227  CB  CYS A 174     -14.942 -32.058  17.862  1.00140.02           C  
ANISOU 1227  CB  CYS A 174    17561  17947  17693   2101    637    997       C  
ATOM   1228  SG  CYS A 174     -13.650 -31.124  18.708  1.00141.87           S  
ANISOU 1228  SG  CYS A 174    17481  18372  18053   1903    687    954       S  
ATOM   1229  N   GLY A 175     -14.713 -35.231  18.271  1.00141.74           N  
ANISOU 1229  N   GLY A 175    18328  17673  17853   2174    846   1046       N  
ATOM   1230  CA  GLY A 175     -13.903 -36.410  18.513  1.00142.86           C  
ANISOU 1230  CA  GLY A 175    18719  17635  17926   2339    819   1067       C  
ATOM   1231  C   GLY A 175     -12.399 -36.209  18.558  1.00145.66           C  
ANISOU 1231  C   GLY A 175    19044  18099  18200   2634    536   1053       C  
ATOM   1232  O   GLY A 175     -11.727 -36.789  19.409  1.00147.35           O  
ANISOU 1232  O   GLY A 175    19579  18148  18260   2861    471   1107       O  
ATOM   1233  N   SER A 176     -11.858 -35.398  17.654  1.00139.19           N  
ANISOU 1233  N   SER A 176    17847  17554  17487   2638    372    965       N  
ATOM   1234  CA  SER A 176     -10.407 -35.227  17.593  1.00138.67           C  
ANISOU 1234  CA  SER A 176    17665  17634  17391   2884    115    900       C  
ATOM   1235  C   SER A 176      -9.860 -34.630  18.904  1.00141.94           C  
ANISOU 1235  C   SER A 176    18207  18089  17635   3058    -28    935       C  
ATOM   1236  O   SER A 176     -10.258 -33.517  19.265  1.00140.30           O  
ANISOU 1236  O   SER A 176    17881  17997  17430   2936     -2    943       O  
ATOM   1237  CB  SER A 176     -10.015 -34.363  16.396  1.00140.13           C  
ANISOU 1237  CB  SER A 176    17425  18074  17744   2788     43    784       C  
ATOM   1238  OG  SER A 176     -10.619 -33.081  16.455  1.00147.08           O  
ANISOU 1238  OG  SER A 176    18129  19090  18665   2612     95    790       O  
ATOM   1239  N   PRO A 177      -8.972 -35.352  19.642  1.00139.60           N  
ANISOU 1239  N   PRO A 177    18166  17696  17181   3357   -187    949       N  
ATOM   1240  CA  PRO A 177      -8.431 -34.789  20.897  1.00140.05           C  
ANISOU 1240  CA  PRO A 177    18349  17805  17058   3544   -353    963       C  
ATOM   1241  C   PRO A 177      -7.532 -33.577  20.650  1.00141.02           C  
ANISOU 1241  C   PRO A 177    18070  18238  17274   3570   -547    818       C  
ATOM   1242  O   PRO A 177      -7.555 -32.624  21.430  1.00140.29           O  
ANISOU 1242  O   PRO A 177    17955  18241  17108   3552   -593    817       O  
ATOM   1243  CB  PRO A 177      -7.685 -35.965  21.531  1.00144.91           C  
ANISOU 1243  CB  PRO A 177    19324  18242  17493   3883   -496    993       C  
ATOM   1244  CG  PRO A 177      -7.340 -36.858  20.400  1.00149.56           C  
ANISOU 1244  CG  PRO A 177    19807  18795  18222   3913   -492    931       C  
ATOM   1245  CD  PRO A 177      -8.407 -36.689  19.359  1.00142.89           C  
ANISOU 1245  CD  PRO A 177    18768  17954  17568   3556   -240    942       C  
ATOM   1246  N   ASN A 178      -6.776 -33.602  19.535  1.00135.68           N  
ANISOU 1246  N   ASN A 178    17079  17708  16764   3587   -631    685       N  
ATOM   1247  CA  ASN A 178      -5.926 -32.505  19.081  1.00133.84           C  
ANISOU 1247  CA  ASN A 178    16446  17754  16655   3563   -758    523       C  
ATOM   1248  C   ASN A 178      -6.839 -31.507  18.360  1.00133.77           C  
ANISOU 1248  C   ASN A 178    16223  17828  16777   3234   -565    549       C  
ATOM   1249  O   ASN A 178      -7.979 -31.854  18.035  1.00132.53           O  
ANISOU 1249  O   ASN A 178    16177  17533  16643   3061   -372    656       O  
ATOM   1250  CB  ASN A 178      -4.846 -33.022  18.125  1.00134.99           C  
ANISOU 1250  CB  ASN A 178    16372  17991  16927   3688   -873    370       C  
ATOM   1251  CG  ASN A 178      -3.915 -34.035  18.740  1.00160.11           C  
ANISOU 1251  CG  ASN A 178    19746  21095  19994   4046  -1083    326       C  
ATOM   1252  OD1 ASN A 178      -2.924 -33.690  19.388  1.00155.62           O  
ANISOU 1252  OD1 ASN A 178    19096  20662  19372   4263  -1312    201       O  
ATOM   1253  ND2 ASN A 178      -4.210 -35.310  18.540  1.00153.00           N  
ANISOU 1253  ND2 ASN A 178    19108  19973  19054   4126  -1016    414       N  
ATOM   1254  N   TYR A 179      -6.350 -30.270  18.120  1.00128.24           N  
ANISOU 1254  N   TYR A 179    15223  17343  16161   3153   -616    437       N  
ATOM   1255  CA  TYR A 179      -7.074 -29.171  17.451  1.00125.32           C  
ANISOU 1255  CA  TYR A 179    14657  17060  15898   2880   -462    449       C  
ATOM   1256  C   TYR A 179      -8.280 -28.640  18.261  1.00127.14           C  
ANISOU 1256  C   TYR A 179    15054  17207  16047   2750   -336    583       C  
ATOM   1257  O   TYR A 179      -8.862 -27.620  17.883  1.00125.12           O  
ANISOU 1257  O   TYR A 179    14650  17026  15864   2561   -234    588       O  
ATOM   1258  CB  TYR A 179      -7.490 -29.522  15.996  1.00125.26           C  
ANISOU 1258  CB  TYR A 179    14527  17039  16029   2730   -334    445       C  
ATOM   1259  CG  TYR A 179      -6.422 -30.223  15.181  1.00127.78           C  
ANISOU 1259  CG  TYR A 179    14721  17406  16425   2851   -422    322       C  
ATOM   1260  CD1 TYR A 179      -5.361 -29.513  14.628  1.00129.68           C  
ANISOU 1260  CD1 TYR A 179    14680  17833  16760   2851   -487    157       C  
ATOM   1261  CD2 TYR A 179      -6.493 -31.590  14.932  1.00129.53           C  
ANISOU 1261  CD2 TYR A 179    15105  17475  16633   2949   -414    358       C  
ATOM   1262  CE1 TYR A 179      -4.372 -30.154  13.885  1.00131.40           C  
ANISOU 1262  CE1 TYR A 179    14767  18098  17062   2956   -550     21       C  
ATOM   1263  CE2 TYR A 179      -5.516 -32.241  14.180  1.00131.28           C  
ANISOU 1263  CE2 TYR A 179    15210  17739  16932   3067   -490    235       C  
ATOM   1264  CZ  TYR A 179      -4.458 -31.517  13.655  1.00138.53           C  
ANISOU 1264  CZ  TYR A 179    15831  18856  17949   3072   -558     63       C  
ATOM   1265  OH  TYR A 179      -3.493 -32.154  12.911  1.00140.32           O  
ANISOU 1265  OH  TYR A 179    15926  19126  18264   3182   -614    -78       O  
ATOM   1266  N   ALA A 180      -8.632 -29.313  19.377  1.00124.00           N  
ANISOU 1266  N   ALA A 180    14977  16646  15492   2861   -338    684       N  
ATOM   1267  CA  ALA A 180      -9.741 -28.939  20.253  1.00123.05           C  
ANISOU 1267  CA  ALA A 180    15046  16427  15283   2748   -199    798       C  
ATOM   1268  C   ALA A 180      -9.252 -28.110  21.439  1.00126.13           C  
ANISOU 1268  C   ALA A 180    15483  16896  15542   2848   -321    772       C  
ATOM   1269  O   ALA A 180      -8.305 -28.505  22.124  1.00127.44           O  
ANISOU 1269  O   ALA A 180    15768  17070  15585   3087   -509    729       O  
ATOM   1270  CB  ALA A 180     -10.471 -30.183  20.737  1.00125.17           C  
ANISOU 1270  CB  ALA A 180    15670  16442  15448   2777    -77    918       C  
ATOM   1271  N   ALA A 181      -9.913 -26.959  21.671  1.00120.35           N  
ANISOU 1271  N   ALA A 181    14662  16227  14837   2677   -221    787       N  
ATOM   1272  CA  ALA A 181      -9.634 -25.989  22.737  1.00120.13           C  
ANISOU 1272  CA  ALA A 181    14659  16281  14704   2718   -299    756       C  
ATOM   1273  C   ALA A 181      -9.667 -26.610  24.157  1.00124.85           C  
ANISOU 1273  C   ALA A 181    15644  16732  15061   2891   -346    835       C  
ATOM   1274  O   ALA A 181     -10.351 -27.621  24.338  1.00125.19           O  
ANISOU 1274  O   ALA A 181    15962  16571  15034   2893   -221    950       O  
ATOM   1275  CB  ALA A 181     -10.625 -24.837  22.643  1.00119.22           C  
ANISOU 1275  CB  ALA A 181    14430  16201  14666   2486   -130    786       C  
ATOM   1276  N   PRO A 182      -8.968 -26.029  25.178  1.00121.62           N  
ANISOU 1276  N   PRO A 182    15286  16412  14513   3031   -513    770       N  
ATOM   1277  CA  PRO A 182      -8.996 -26.625  26.531  1.00123.44           C  
ANISOU 1277  CA  PRO A 182    15933  16492  14477   3218   -567    851       C  
ATOM   1278  C   PRO A 182     -10.384 -26.816  27.151  1.00126.40           C  
ANISOU 1278  C   PRO A 182    16617  16653  14756   3068   -297   1012       C  
ATOM   1279  O   PRO A 182     -10.551 -27.708  27.980  1.00128.03           O  
ANISOU 1279  O   PRO A 182    17232  16660  14753   3201   -271   1111       O  
ATOM   1280  CB  PRO A 182      -8.133 -25.669  27.360  1.00126.15           C  
ANISOU 1280  CB  PRO A 182    16195  17011  14725   3337   -777    722       C  
ATOM   1281  CG  PRO A 182      -7.245 -25.012  26.373  1.00129.49           C  
ANISOU 1281  CG  PRO A 182    16171  17664  15365   3293   -889    545       C  
ATOM   1282  CD  PRO A 182      -8.089 -24.841  25.150  1.00122.62           C  
ANISOU 1282  CD  PRO A 182    15112  16770  14708   3030   -658    606       C  
ATOM   1283  N   GLU A 183     -11.373 -25.997  26.744  1.00120.26           N  
ANISOU 1283  N   GLU A 183    15658  15907  14129   2798    -90   1029       N  
ATOM   1284  CA  GLU A 183     -12.755 -26.099  27.223  1.00119.87           C  
ANISOU 1284  CA  GLU A 183    15826  15677  14041   2623    191   1141       C  
ATOM   1285  C   GLU A 183     -13.495 -27.299  26.603  1.00123.26           C  
ANISOU 1285  C   GLU A 183    16371  15919  14542   2538    377   1216       C  
ATOM   1286  O   GLU A 183     -14.425 -27.823  27.219  1.00124.01           O  
ANISOU 1286  O   GLU A 183    16762  15807  14549   2454    601   1302       O  
ATOM   1287  CB  GLU A 183     -13.533 -24.782  27.010  1.00119.32           C  
ANISOU 1287  CB  GLU A 183    15502  15717  14118   2394    326   1107       C  
ATOM   1288  CG  GLU A 183     -13.620 -24.301  25.567  1.00127.12           C  
ANISOU 1288  CG  GLU A 183    16092  16844  15364   2258    335   1043       C  
ATOM   1289  CD  GLU A 183     -12.765 -23.097  25.222  1.00144.68           C  
ANISOU 1289  CD  GLU A 183    18019  19287  17665   2269    177    931       C  
ATOM   1290  OE1 GLU A 183     -11.543 -23.130  25.496  1.00138.75           O  
ANISOU 1290  OE1 GLU A 183    17254  18628  16837   2442    -37    855       O  
ATOM   1291  OE2 GLU A 183     -13.313 -22.131  24.644  1.00136.37           O  
ANISOU 1291  OE2 GLU A 183    16747  18310  16757   2107    271    906       O  
ATOM   1292  N   VAL A 184     -13.077 -27.726  25.392  1.00118.31           N  
ANISOU 1292  N   VAL A 184    15516  15361  14077   2548    301   1167       N  
ATOM   1293  CA  VAL A 184     -13.661 -28.852  24.648  1.00117.99           C  
ANISOU 1293  CA  VAL A 184    15538  15167  14127   2468    451   1207       C  
ATOM   1294  C   VAL A 184     -13.236 -30.187  25.278  1.00123.78           C  
ANISOU 1294  C   VAL A 184    16683  15685  14662   2673    419   1280       C  
ATOM   1295  O   VAL A 184     -14.090 -31.042  25.519  1.00124.50           O  
ANISOU 1295  O   VAL A 184    17052  15541  14709   2582    649   1357       O  
ATOM   1296  CB  VAL A 184     -13.339 -28.792  23.125  1.00120.07           C  
ANISOU 1296  CB  VAL A 184    15426  15581  14614   2412    377   1122       C  
ATOM   1297  CG1 VAL A 184     -14.088 -29.875  22.351  1.00120.01           C  
ANISOU 1297  CG1 VAL A 184    15465  15422  14709   2298    548   1145       C  
ATOM   1298  CG2 VAL A 184     -13.653 -27.418  22.546  1.00117.73           C  
ANISOU 1298  CG2 VAL A 184    14779  15480  14473   2250    390   1058       C  
ATOM   1299  N   ILE A 185     -11.921 -30.354  25.547  1.00121.00           N  
ANISOU 1299  N   ILE A 185    16374  15408  14193   2952    139   1243       N  
ATOM   1300  CA  ILE A 185     -11.348 -31.566  26.153  1.00123.34           C  
ANISOU 1300  CA  ILE A 185    17071  15513  14279   3216     48   1304       C  
ATOM   1301  C   ILE A 185     -11.826 -31.755  27.605  1.00129.00           C  
ANISOU 1301  C   ILE A 185    18276  16021  14717   3274    157   1419       C  
ATOM   1302  O   ILE A 185     -11.911 -32.891  28.075  1.00130.92           O  
ANISOU 1302  O   ILE A 185    18954  16003  14786   3396    231   1515       O  
ATOM   1303  CB  ILE A 185      -9.799 -31.650  26.013  1.00127.25           C  
ANISOU 1303  CB  ILE A 185    17436  16171  14742   3522   -307   1196       C  
ATOM   1304  CG1 ILE A 185      -9.070 -30.477  26.705  1.00127.77           C  
ANISOU 1304  CG1 ILE A 185    17355  16458  14733   3626   -526   1100       C  
ATOM   1305  CG2 ILE A 185      -9.375 -31.787  24.548  1.00126.25           C  
ANISOU 1305  CG2 ILE A 185    16916  16182  14870   3464   -357   1095       C  
ATOM   1306  CD1 ILE A 185      -7.577 -30.641  26.772  1.00138.21           C  
ANISOU 1306  CD1 ILE A 185    18955  17757  15800   3996   -803   1075       C  
ATOM   1307  N   SER A 186     -12.151 -30.643  28.296  1.00124.62           N  
ANISOU 1307  N   SER A 186    17670  15565  14116   3180    187   1408       N  
ATOM   1308  CA  SER A 186     -12.670 -30.639  29.666  1.00126.30           C  
ANISOU 1308  CA  SER A 186    18322  15600  14068   3200    316   1504       C  
ATOM   1309  C   SER A 186     -14.181 -30.906  29.668  1.00129.54           C  
ANISOU 1309  C   SER A 186    18868  15803  14549   2892    726   1579       C  
ATOM   1310  O   SER A 186     -14.728 -31.331  30.687  1.00131.34           O  
ANISOU 1310  O   SER A 186    19551  15792  14560   2886    919   1675       O  
ATOM   1311  CB  SER A 186     -12.378 -29.304  30.344  1.00129.33           C  
ANISOU 1311  CB  SER A 186    18560  16187  14392   3214    182   1437       C  
ATOM   1312  OG  SER A 186     -10.985 -29.046  30.403  1.00138.77           O  
ANISOU 1312  OG  SER A 186    19616  17580  15530   3487   -189   1331       O  
ATOM   1313  N   GLY A 187     -14.826 -30.655  28.527  1.00123.40           N  
ANISOU 1313  N   GLY A 187    17699  15118  14069   2644    856   1519       N  
ATOM   1314  CA  GLY A 187     -16.260 -30.841  28.334  1.00122.83           C  
ANISOU 1314  CA  GLY A 187    17637  14902  14130   2340   1222   1533       C  
ATOM   1315  C   GLY A 187     -17.103 -29.774  29.001  1.00125.76           C  
ANISOU 1315  C   GLY A 187    17954  15322  14508   2162   1385   1517       C  
ATOM   1316  O   GLY A 187     -18.204 -30.063  29.478  1.00126.56           O  
ANISOU 1316  O   GLY A 187    18258  15232  14596   1972   1708   1543       O  
ATOM   1317  N   ARG A 188     -16.591 -28.530  29.032  1.00120.34           N  
ANISOU 1317  N   ARG A 188    16989  14883  13850   2213   1179   1459       N  
ATOM   1318  CA  ARG A 188     -17.258 -27.377  29.646  1.00119.39           C  
ANISOU 1318  CA  ARG A 188    16791  14833  13739   2072   1296   1433       C  
ATOM   1319  C   ARG A 188     -17.993 -26.528  28.604  1.00120.12           C  
ANISOU 1319  C   ARG A 188    16410  15093  14139   1851   1374   1343       C  
ATOM   1320  O   ARG A 188     -17.655 -26.584  27.419  1.00118.03           O  
ANISOU 1320  O   ARG A 188    15844  14950  14050   1853   1250   1295       O  
ATOM   1321  CB  ARG A 188     -16.253 -26.527  30.447  1.00119.96           C  
ANISOU 1321  CB  ARG A 188    16898  15051  13630   2269   1034   1416       C  
ATOM   1322  N   LEU A 189     -19.008 -25.755  29.051  1.00116.09           N  
ANISOU 1322  N   LEU A 189    15851  14577  13681   1674   1580   1315       N  
ATOM   1323  CA  LEU A 189     -19.823 -24.881  28.197  1.00113.69           C  
ANISOU 1323  CA  LEU A 189    15135  14416  13645   1490   1657   1224       C  
ATOM   1324  C   LEU A 189     -18.998 -23.735  27.617  1.00114.73           C  
ANISOU 1324  C   LEU A 189    14944  14796  13853   1574   1394   1176       C  
ATOM   1325  O   LEU A 189     -18.207 -23.118  28.336  1.00114.48           O  
ANISOU 1325  O   LEU A 189    14990  14834  13671   1695   1246   1183       O  
ATOM   1326  CB  LEU A 189     -21.036 -24.327  28.965  1.00114.54           C  
ANISOU 1326  CB  LEU A 189    15296  14450  13774   1313   1935   1194       C  
ATOM   1327  CG  LEU A 189     -22.138 -25.323  29.324  1.00121.21           C  
ANISOU 1327  CG  LEU A 189    16360  15060  14634   1142   2277   1191       C  
ATOM   1328  CD1 LEU A 189     -22.794 -24.944  30.626  1.00123.17           C  
ANISOU 1328  CD1 LEU A 189    16880  15181  14738   1062   2514   1203       C  
ATOM   1329  CD2 LEU A 189     -23.182 -25.423  28.221  1.00122.77           C  
ANISOU 1329  CD2 LEU A 189    16199  15311  15139    949   2413   1072       C  
ATOM   1330  N   TYR A 190     -19.177 -23.463  26.312  1.00108.97           N  
ANISOU 1330  N   TYR A 190    13865  14191  13347   1506   1345   1116       N  
ATOM   1331  CA  TYR A 190     -18.444 -22.420  25.594  1.00106.72           C  
ANISOU 1331  CA  TYR A 190    13289  14114  13146   1561   1139   1067       C  
ATOM   1332  C   TYR A 190     -19.260 -21.764  24.480  1.00108.19           C  
ANISOU 1332  C   TYR A 190    13152  14396  13561   1433   1194   1003       C  
ATOM   1333  O   TYR A 190     -20.291 -22.296  24.061  1.00107.91           O  
ANISOU 1333  O   TYR A 190    13066  14290  13644   1319   1348    976       O  
ATOM   1334  CB  TYR A 190     -17.140 -23.005  24.997  1.00107.73           C  
ANISOU 1334  CB  TYR A 190    13389  14304  13240   1716    912   1068       C  
ATOM   1335  CG  TYR A 190     -17.353 -24.121  23.990  1.00109.53           C  
ANISOU 1335  CG  TYR A 190    13572  14471  13573   1688    945   1071       C  
ATOM   1336  CD1 TYR A 190     -17.656 -23.841  22.659  1.00109.98           C  
ANISOU 1336  CD1 TYR A 190    13334  14631  13823   1606    931   1015       C  
ATOM   1337  CD2 TYR A 190     -17.214 -25.455  24.360  1.00111.96           C  
ANISOU 1337  CD2 TYR A 190    14159  14610  13772   1755    986   1126       C  
ATOM   1338  CE1 TYR A 190     -17.856 -24.862  21.732  1.00110.73           C  
ANISOU 1338  CE1 TYR A 190    13388  14675  14009   1578    957   1002       C  
ATOM   1339  CE2 TYR A 190     -17.399 -26.485  23.437  1.00112.91           C  
ANISOU 1339  CE2 TYR A 190    14243  14665  13993   1722   1025   1117       C  
ATOM   1340  CZ  TYR A 190     -17.719 -26.183  22.123  1.00118.63           C  
ANISOU 1340  CZ  TYR A 190    14647  15510  14919   1628   1007   1049       C  
ATOM   1341  OH  TYR A 190     -17.902 -27.192  21.209  1.00119.68           O  
ANISOU 1341  OH  TYR A 190    14744  15584  15145   1593   1041   1026       O  
ATOM   1342  N   ALA A 191     -18.746 -20.636  23.961  1.00102.90           N  
ANISOU 1342  N   ALA A 191    12270  13882  12946   1463   1059    965       N  
ATOM   1343  CA  ALA A 191     -19.295 -19.931  22.808  1.00101.21           C  
ANISOU 1343  CA  ALA A 191    11781  13762  12911   1395   1060    913       C  
ATOM   1344  C   ALA A 191     -18.451 -20.375  21.607  1.00103.61           C  
ANISOU 1344  C   ALA A 191    11968  14137  13260   1457    909    903       C  
ATOM   1345  O   ALA A 191     -17.251 -20.628  21.754  1.00103.42           O  
ANISOU 1345  O   ALA A 191    12008  14143  13144   1558    776    913       O  
ATOM   1346  CB  ALA A 191     -19.196 -18.428  23.004  1.00101.30           C  
ANISOU 1346  CB  ALA A 191    11695  13866  12930   1393   1030    887       C  
ATOM   1347  N   GLY A 192     -19.097 -20.506  20.456  1.00 98.85           N  
ANISOU 1347  N   GLY A 192    11198  13562  12797   1402    929    868       N  
ATOM   1348  CA  GLY A 192     -18.500 -20.976  19.208  1.00 97.61           C  
ANISOU 1348  CA  GLY A 192    10936  13461  12691   1441    818    850       C  
ATOM   1349  C   GLY A 192     -17.203 -20.372  18.681  1.00 99.56           C  
ANISOU 1349  C   GLY A 192    11105  13816  12907   1515    671    836       C  
ATOM   1350  O   GLY A 192     -16.311 -21.141  18.308  1.00 99.10           O  
ANISOU 1350  O   GLY A 192    11063  13765  12824   1579    585    830       O  
ATOM   1351  N   PRO A 193     -17.053 -19.022  18.567  1.00 94.77           N  
ANISOU 1351  N   PRO A 193    10410  13287  12313   1503    653    816       N  
ATOM   1352  CA  PRO A 193     -15.834 -18.464  17.943  1.00 93.80           C  
ANISOU 1352  CA  PRO A 193    10206  13253  12179   1539    554    778       C  
ATOM   1353  C   PRO A 193     -14.486 -18.802  18.585  1.00 97.21           C  
ANISOU 1353  C   PRO A 193    10691  13717  12528   1617    455    748       C  
ATOM   1354  O   PRO A 193     -13.533 -19.031  17.840  1.00 96.65           O  
ANISOU 1354  O   PRO A 193    10539  13703  12479   1650    380    697       O  
ATOM   1355  CB  PRO A 193     -16.082 -16.952  17.966  1.00 95.27           C  
ANISOU 1355  CB  PRO A 193    10342  13473  12382   1498    596    765       C  
ATOM   1356  CG  PRO A 193     -17.557 -16.811  18.034  1.00 99.87           C  
ANISOU 1356  CG  PRO A 193    10919  14006  13021   1459    688    789       C  
ATOM   1357  CD  PRO A 193     -18.007 -17.944  18.899  1.00 96.16           C  
ANISOU 1357  CD  PRO A 193    10552  13459  12523   1450    739    814       C  
ATOM   1358  N   GLU A 194     -14.400 -18.835  19.933  1.00 93.84           N  
ANISOU 1358  N   GLU A 194    10396  13256  12003   1655    449    763       N  
ATOM   1359  CA  GLU A 194     -13.160 -19.099  20.688  1.00 94.24           C  
ANISOU 1359  CA  GLU A 194    10505  13346  11956   1763    322    715       C  
ATOM   1360  C   GLU A 194     -12.460 -20.408  20.329  1.00 97.62           C  
ANISOU 1360  C   GLU A 194    10961  13761  12370   1867    225    705       C  
ATOM   1361  O   GLU A 194     -11.229 -20.448  20.310  1.00 97.76           O  
ANISOU 1361  O   GLU A 194    10909  13862  12372   1955     95    616       O  
ATOM   1362  CB  GLU A 194     -13.384 -19.032  22.207  1.00 96.68           C  
ANISOU 1362  CB  GLU A 194    11004  13601  12131   1802    333    746       C  
ATOM   1363  CG  GLU A 194     -14.003 -17.737  22.702  1.00107.77           C  
ANISOU 1363  CG  GLU A 194    12391  15016  13541   1710    428    743       C  
ATOM   1364  CD  GLU A 194     -15.512 -17.797  22.814  1.00130.28           C  
ANISOU 1364  CD  GLU A 194    15303  17766  16432   1621    597    817       C  
ATOM   1365  OE1 GLU A 194     -16.014 -18.645  23.587  1.00126.70           O  
ANISOU 1365  OE1 GLU A 194    15035  17206  15897   1637    660    871       O  
ATOM   1366  OE2 GLU A 194     -16.193 -16.988  22.143  1.00124.26           O  
ANISOU 1366  OE2 GLU A 194    14410  17025  15779   1540    671    809       O  
ATOM   1367  N   VAL A 195     -13.239 -21.472  20.059  1.00 93.42           N  
ANISOU 1367  N   VAL A 195    10521  13121  11854   1856    293    777       N  
ATOM   1368  CA  VAL A 195     -12.725 -22.797  19.694  1.00 93.49           C  
ANISOU 1368  CA  VAL A 195    10586  13085  11853   1952    226    777       C  
ATOM   1369  C   VAL A 195     -12.091 -22.757  18.298  1.00 95.74           C  
ANISOU 1369  C   VAL A 195    10664  13464  12249   1937    177    705       C  
ATOM   1370  O   VAL A 195     -11.001 -23.302  18.113  1.00 96.01           O  
ANISOU 1370  O   VAL A 195    10666  13539  12274   2047     62    642       O  
ATOM   1371  CB  VAL A 195     -13.807 -23.902  19.842  1.00 97.89           C  
ANISOU 1371  CB  VAL A 195    11318  13478  12399   1915    350    861       C  
ATOM   1372  CG1 VAL A 195     -13.275 -25.275  19.430  1.00 98.48           C  
ANISOU 1372  CG1 VAL A 195    11471  13484  12461   2016    292    861       C  
ATOM   1373  CG2 VAL A 195     -14.337 -23.947  21.270  1.00 98.79           C  
ANISOU 1373  CG2 VAL A 195    11671  13483  12383   1924    427    925       C  
ATOM   1374  N   ASP A 196     -12.753 -22.073  17.338  1.00 90.38           N  
ANISOU 1374  N   ASP A 196     9855  12819  11666   1813    261    706       N  
ATOM   1375  CA  ASP A 196     -12.289 -21.907  15.957  1.00 89.17           C  
ANISOU 1375  CA  ASP A 196     9544  12741  11597   1782    246    647       C  
ATOM   1376  C   ASP A 196     -10.952 -21.170  15.862  1.00 92.43           C  
ANISOU 1376  C   ASP A 196     9839  13266  12015   1808    177    543       C  
ATOM   1377  O   ASP A 196     -10.163 -21.469  14.966  1.00 92.11           O  
ANISOU 1377  O   ASP A 196     9700  13274  12022   1823    148    470       O  
ATOM   1378  CB  ASP A 196     -13.362 -21.218  15.098  1.00 90.03           C  
ANISOU 1378  CB  ASP A 196     9588  12850  11769   1672    338    675       C  
ATOM   1379  CG  ASP A 196     -14.551 -22.095  14.738  1.00 99.32           C  
ANISOU 1379  CG  ASP A 196    10804  13947  12987   1636    397    717       C  
ATOM   1380  OD1 ASP A 196     -14.621 -23.242  15.237  1.00100.44           O  
ANISOU 1380  OD1 ASP A 196    11053  14005  13106   1674    400    739       O  
ATOM   1381  OD2 ASP A 196     -15.409 -21.638  13.953  1.00104.35           O  
ANISOU 1381  OD2 ASP A 196    11371  14598  13677   1576    438    715       O  
ATOM   1382  N   ILE A 197     -10.691 -20.230  16.794  1.00 88.59           N  
ANISOU 1382  N   ILE A 197     9358  12819  11484   1803    163    516       N  
ATOM   1383  CA  ILE A 197      -9.438 -19.473  16.860  1.00 88.64           C  
ANISOU 1383  CA  ILE A 197     9238  12934  11506   1808    110    382       C  
ATOM   1384  C   ILE A 197      -8.322 -20.381  17.409  1.00 93.14           C  
ANISOU 1384  C   ILE A 197     9800  13547  12041   1964    -43    294       C  
ATOM   1385  O   ILE A 197      -7.221 -20.380  16.856  1.00 93.26           O  
ANISOU 1385  O   ILE A 197     9661  13652  12121   1983    -89    157       O  
ATOM   1386  CB  ILE A 197      -9.598 -18.130  17.635  1.00 91.71           C  
ANISOU 1386  CB  ILE A 197     9632  13347  11866   1740    155    366       C  
ATOM   1387  CG1 ILE A 197     -10.711 -17.258  17.001  1.00 91.03           C  
ANISOU 1387  CG1 ILE A 197     9561  13210  11817   1620    295    449       C  
ATOM   1388  CG2 ILE A 197      -8.271 -17.353  17.688  1.00 93.31           C  
ANISOU 1388  CG2 ILE A 197     9687  13663  12104   1720    118    192       C  
ATOM   1389  CD1 ILE A 197     -11.516 -16.412  17.981  1.00 98.33           C  
ANISOU 1389  CD1 ILE A 197    10568  14097  12697   1583    350    501       C  
ATOM   1390  N   TRP A 198      -8.625 -21.185  18.461  1.00 89.94           N  
ANISOU 1390  N   TRP A 198     9574  13069  11531   2082   -114    367       N  
ATOM   1391  CA  TRP A 198      -7.686 -22.148  19.055  1.00 91.12           C  
ANISOU 1391  CA  TRP A 198     9776  13232  11616   2278   -282    304       C  
ATOM   1392  C   TRP A 198      -7.338 -23.214  18.015  1.00 94.41           C  
ANISOU 1392  C   TRP A 198    10140  13629  12103   2328   -300    284       C  
ATOM   1393  O   TRP A 198      -6.175 -23.602  17.906  1.00 95.10           O  
ANISOU 1393  O   TRP A 198    10120  13796  12218   2452   -426    149       O  
ATOM   1394  CB  TRP A 198      -8.277 -22.807  20.314  1.00 90.77           C  
ANISOU 1394  CB  TRP A 198    10011  13064  11414   2386   -315    420       C  
ATOM   1395  CG  TRP A 198      -7.242 -23.398  21.229  1.00 93.79           C  
ANISOU 1395  CG  TRP A 198    10480  13475  11682   2619   -521    342       C  
ATOM   1396  CD1 TRP A 198      -6.670 -22.798  22.311  1.00 97.92           C  
ANISOU 1396  CD1 TRP A 198    11022  14077  12106   2709   -647    257       C  
ATOM   1397  CD2 TRP A 198      -6.648 -24.701  21.133  1.00 94.97           C  
ANISOU 1397  CD2 TRP A 198    10713  13575  11796   2814   -642    327       C  
ATOM   1398  NE1 TRP A 198      -5.757 -23.644  22.897  1.00 99.45           N  
ANISOU 1398  NE1 TRP A 198    11305  14284  12198   2964   -859    186       N  
ATOM   1399  CE2 TRP A 198      -5.730 -24.824  22.200  1.00101.00           C  
ANISOU 1399  CE2 TRP A 198    11550  14394  12431   3039   -858    234       C  
ATOM   1400  CE3 TRP A 198      -6.817 -25.790  20.258  1.00 96.03           C  
ANISOU 1400  CE3 TRP A 198    10878  13618  11989   2830   -596    377       C  
ATOM   1401  CZ2 TRP A 198      -4.969 -25.982  22.405  1.00102.29           C  
ANISOU 1401  CZ2 TRP A 198    11820  14522  12523   3300  -1036    193       C  
ATOM   1402  CZ3 TRP A 198      -6.051 -26.930  20.453  1.00 99.33           C  
ANISOU 1402  CZ3 TRP A 198    11400  13995  12347   3067   -750    339       C  
ATOM   1403  CH2 TRP A 198      -5.151 -27.024  21.523  1.00102.13           C  
ANISOU 1403  CH2 TRP A 198    11835  14399  12570   3309   -971    254       C  
ATOM   1404  N   SER A 199      -8.350 -23.648  17.227  1.00 89.43           N  
ANISOU 1404  N   SER A 199     9565  12902  11514   2230   -173    396       N  
ATOM   1405  CA  SER A 199      -8.217 -24.621  16.141  1.00 88.95           C  
ANISOU 1405  CA  SER A 199     9467  12809  11521   2247   -161    385       C  
ATOM   1406  C   SER A 199      -7.385 -24.046  14.988  1.00 91.88           C  
ANISOU 1406  C   SER A 199     9605  13304  12002   2178   -144    254       C  
ATOM   1407  O   SER A 199      -6.746 -24.807  14.266  1.00 91.81           O  
ANISOU 1407  O   SER A 199     9529  13309  12045   2238   -178    183       O  
ATOM   1408  CB  SER A 199      -9.589 -25.056  15.637  1.00 91.59           C  
ANISOU 1408  CB  SER A 199     9899  13027  11874   2137    -28    510       C  
ATOM   1409  OG  SER A 199     -10.349 -25.675  16.662  1.00100.96           O  
ANISOU 1409  OG  SER A 199    11310  14079  12971   2176      0    614       O  
ATOM   1410  N   CYS A 200      -7.394 -22.707  14.822  1.00 87.55           N  
ANISOU 1410  N   CYS A 200     8952  12829  11484   2049    -71    218       N  
ATOM   1411  CA  CYS A 200      -6.617 -22.007  13.797  1.00 87.26           C  
ANISOU 1411  CA  CYS A 200     8734  12885  11535   1956     -9     91       C  
ATOM   1412  C   CYS A 200      -5.161 -21.822  14.231  1.00 92.17           C  
ANISOU 1412  C   CYS A 200     9197  13628  12195   2032   -107   -105       C  
ATOM   1413  O   CYS A 200      -4.266 -21.845  13.384  1.00 92.32           O  
ANISOU 1413  O   CYS A 200     9060  13716  12303   2004    -76   -248       O  
ATOM   1414  CB  CYS A 200      -7.266 -20.677  13.426  1.00 86.61           C  
ANISOU 1414  CB  CYS A 200     8650  12799  11458   1793    126    138       C  
ATOM   1415  SG  CYS A 200      -8.887 -20.839  12.635  1.00 89.31           S  
ANISOU 1415  SG  CYS A 200     9067  13059  11806   1702    239    263       S  
ATOM   1416  N   GLY A 201      -4.948 -21.641  15.537  1.00 89.18           N  
ANISOU 1416  N   GLY A 201     8857  13278  11750   2126   -222   -129       N  
ATOM   1417  CA  GLY A 201      -3.629 -21.472  16.141  1.00 90.61           C  
ANISOU 1417  CA  GLY A 201     8880  13588  11958   2225   -356   -340       C  
ATOM   1418  C   GLY A 201      -2.766 -22.710  15.998  1.00 95.55           C  
ANISOU 1418  C   GLY A 201     9451  14243  12612   2417   -499   -439       C  
ATOM   1419  O   GLY A 201      -1.591 -22.609  15.638  1.00 96.36           O  
ANISOU 1419  O   GLY A 201     9324  14467  12820   2438   -535   -661       O  
ATOM   1420  N   VAL A 202      -3.363 -23.890  16.259  1.00 91.87           N  
ANISOU 1420  N   VAL A 202     9195  13652  12058   2554   -563   -286       N  
ATOM   1421  CA  VAL A 202      -2.721 -25.204  16.132  1.00 92.94           C  
ANISOU 1421  CA  VAL A 202     9345  13769  12199   2760   -693   -341       C  
ATOM   1422  C   VAL A 202      -2.445 -25.513  14.637  1.00 96.06           C  
ANISOU 1422  C   VAL A 202     9591  14178  12727   2665   -577   -405       C  
ATOM   1423  O   VAL A 202      -1.415 -26.117  14.324  1.00 97.15           O  
ANISOU 1423  O   VAL A 202     9592  14382  12938   2793   -666   -568       O  
ATOM   1424  CB  VAL A 202      -3.503 -26.317  16.898  1.00 97.14           C  
ANISOU 1424  CB  VAL A 202    10197  14127  12583   2912   -756   -150       C  
ATOM   1425  CG1 VAL A 202      -4.950 -26.411  16.444  1.00 95.10           C  
ANISOU 1425  CG1 VAL A 202    10099  13726  12308   2736   -566     57       C  
ATOM   1426  CG2 VAL A 202      -2.816 -27.676  16.818  1.00 98.64           C  
ANISOU 1426  CG2 VAL A 202    10441  14274  12765   3151   -894   -204       C  
ATOM   1427  N   ILE A 203      -3.331 -25.037  13.724  1.00 90.45           N  
ANISOU 1427  N   ILE A 203     8905  13416  12045   2449   -385   -294       N  
ATOM   1428  CA  ILE A 203      -3.164 -25.166  12.271  1.00 89.64           C  
ANISOU 1428  CA  ILE A 203     8696  13323  12038   2339   -257   -345       C  
ATOM   1429  C   ILE A 203      -1.991 -24.271  11.837  1.00 94.32           C  
ANISOU 1429  C   ILE A 203     9035  14063  12741   2254   -204   -574       C  
ATOM   1430  O   ILE A 203      -1.143 -24.722  11.070  1.00 94.95           O  
ANISOU 1430  O   ILE A 203     8971  14192  12912   2277   -185   -725       O  
ATOM   1431  CB  ILE A 203      -4.491 -24.897  11.495  1.00 90.83           C  
ANISOU 1431  CB  ILE A 203     8972  13378  12160   2167    -99   -168       C  
ATOM   1432  CG1 ILE A 203      -5.392 -26.155  11.514  1.00 90.97           C  
ANISOU 1432  CG1 ILE A 203     9179  13259  12128   2241   -124    -22       C  
ATOM   1433  CG2 ILE A 203      -4.234 -24.431  10.046  1.00 91.06           C  
ANISOU 1433  CG2 ILE A 203     8892  13447  12260   2016     52   -243       C  
ATOM   1434  CD1 ILE A 203      -6.885 -25.929  11.124  1.00 96.83           C  
ANISOU 1434  CD1 ILE A 203    10043  13913  12835   2101    -11    141       C  
ATOM   1435  N   LEU A 204      -1.913 -23.033  12.382  1.00 90.65           N  
ANISOU 1435  N   LEU A 204     8513  13660  12271   2154   -169   -618       N  
ATOM   1436  CA  LEU A 204      -0.823 -22.084  12.117  1.00 91.50           C  
ANISOU 1436  CA  LEU A 204     8385  13894  12487   2044    -92   -857       C  
ATOM   1437  C   LEU A 204       0.524 -22.686  12.550  1.00 97.49           C  
ANISOU 1437  C   LEU A 204     8934  14779  13330   2225   -262  -1107       C  
ATOM   1438  O   LEU A 204       1.519 -22.515  11.846  1.00 98.25           O  
ANISOU 1438  O   LEU A 204     8807  14966  13559   2158   -179  -1334       O  
ATOM   1439  CB  LEU A 204      -1.090 -20.732  12.817  1.00 91.18           C  
ANISOU 1439  CB  LEU A 204     8357  13875  12414   1921    -38   -848       C  
ATOM   1440  CG  LEU A 204      -0.027 -19.620  12.692  1.00 97.22           C  
ANISOU 1440  CG  LEU A 204     8894  14753  13291   1775     69  -1107       C  
ATOM   1441  CD1 LEU A 204       0.083 -19.093  11.267  1.00 97.11           C  
ANISOU 1441  CD1 LEU A 204     8856  14701  13343   1563    330  -1143       C  
ATOM   1442  CD2 LEU A 204      -0.340 -18.474  13.624  1.00 99.50           C  
ANISOU 1442  CD2 LEU A 204     9225  15049  13530   1696     81  -1089       C  
ATOM   1443  N   TYR A 205       0.536 -23.427  13.676  1.00 94.77           N  
ANISOU 1443  N   TYR A 205     8675  14432  12902   2463   -495  -1072       N  
ATOM   1444  CA  TYR A 205       1.720 -24.117  14.188  1.00 97.00           C  
ANISOU 1444  CA  TYR A 205     8795  14825  13236   2703   -712  -1296       C  
ATOM   1445  C   TYR A 205       2.064 -25.308  13.280  1.00101.49           C  
ANISOU 1445  C   TYR A 205     9335  15357  13870   2804   -714  -1328       C  
ATOM   1446  O   TYR A 205       3.245 -25.593  13.082  1.00103.17           O  
ANISOU 1446  O   TYR A 205     9303  15692  14207   2908   -790  -1592       O  
ATOM   1447  CB  TYR A 205       1.485 -24.598  15.634  1.00 98.88           C  
ANISOU 1447  CB  TYR A 205     9224  15031  13316   2949   -957  -1204       C  
ATOM   1448  CG  TYR A 205       2.744 -25.010  16.369  1.00103.44           C  
ANISOU 1448  CG  TYR A 205     9631  15750  13922   3221  -1223  -1465       C  
ATOM   1449  CD1 TYR A 205       3.418 -24.115  17.194  1.00106.82           C  
ANISOU 1449  CD1 TYR A 205     9883  16336  14370   3232  -1331  -1676       C  
ATOM   1450  CD2 TYR A 205       3.241 -26.307  16.270  1.00105.72           C  
ANISOU 1450  CD2 TYR A 205     9941  16014  14213   3484  -1381  -1511       C  
ATOM   1451  CE1 TYR A 205       4.570 -24.494  17.883  1.00110.56           C  
ANISOU 1451  CE1 TYR A 205    10182  16958  14867   3507  -1610  -1944       C  
ATOM   1452  CE2 TYR A 205       4.395 -26.694  16.946  1.00109.60           C  
ANISOU 1452  CE2 TYR A 205    10275  16642  14727   3774  -1656  -1765       C  
ATOM   1453  CZ  TYR A 205       5.053 -25.787  17.759  1.00118.37           C  
ANISOU 1453  CZ  TYR A 205    11192  17927  15857   3791  -1781  -1987       C  
ATOM   1454  OH  TYR A 205       6.189 -26.176  18.425  1.00122.46           O  
ANISOU 1454  OH  TYR A 205    11536  18596  16396   4100  -2083  -2265       O  
ATOM   1455  N   ALA A 206       1.034 -25.989  12.728  1.00 96.41           N  
ANISOU 1455  N   ALA A 206     8925  14553  13155   2771   -627  -1083       N  
ATOM   1456  CA  ALA A 206       1.186 -27.162  11.863  1.00 96.62           C  
ANISOU 1456  CA  ALA A 206     8968  14517  13227   2854   -614  -1085       C  
ATOM   1457  C   ALA A 206       1.952 -26.898  10.562  1.00101.10           C  
ANISOU 1457  C   ALA A 206     9293  15168  13950   2706   -445  -1283       C  
ATOM   1458  O   ALA A 206       2.899 -27.631  10.287  1.00102.46           O  
ANISOU 1458  O   ALA A 206     9310  15401  14220   2850   -520  -1474       O  
ATOM   1459  CB  ALA A 206      -0.166 -27.799  11.574  1.00 95.55           C  
ANISOU 1459  CB  ALA A 206     9122  14196  12987   2808   -537   -801       C  
ATOM   1460  N   LEU A 207       1.573 -25.869   9.768  1.00 96.50           N  
ANISOU 1460  N   LEU A 207     8696  14583  13387   2431   -215  -1248       N  
ATOM   1461  CA  LEU A 207       2.304 -25.596   8.522  1.00 97.17           C  
ANISOU 1461  CA  LEU A 207     8598  14725  13596   2276    -20  -1434       C  
ATOM   1462  C   LEU A 207       3.624 -24.836   8.754  1.00103.61           C  
ANISOU 1462  C   LEU A 207     9099  15710  14557   2233      0  -1760       C  
ATOM   1463  O   LEU A 207       4.500 -24.894   7.892  1.00104.57           O  
ANISOU 1463  O   LEU A 207     9027  15895  14810   2162    131  -1980       O  
ATOM   1464  CB  LEU A 207       1.475 -24.933   7.380  1.00 95.49           C  
ANISOU 1464  CB  LEU A 207     8527  14424  13332   2021    233  -1287       C  
ATOM   1465  CG  LEU A 207       0.808 -23.538   7.488  1.00 98.25           C  
ANISOU 1465  CG  LEU A 207     9065  14700  13564   1878    306  -1070       C  
ATOM   1466  CD1 LEU A 207      -0.066 -23.414   8.717  1.00 99.05           C  
ANISOU 1466  CD1 LEU A 207     9410  14678  13545   1958    216   -802       C  
ATOM   1467  CD2 LEU A 207       1.768 -22.374   7.268  1.00 98.84           C  
ANISOU 1467  CD2 LEU A 207     9047  14853  13655   1835    278  -1154       C  
ATOM   1468  N   LEU A 208       3.786 -24.158   9.908  1.00101.00           N  
ANISOU 1468  N   LEU A 208     8710  15456  14210   2272   -121  -1814       N  
ATOM   1469  CA  LEU A 208       5.020 -23.423  10.208  1.00103.29           C  
ANISOU 1469  CA  LEU A 208     8680  15917  14649   2224   -114  -2156       C  
ATOM   1470  C   LEU A 208       6.129 -24.293  10.796  1.00110.80           C  
ANISOU 1470  C   LEU A 208     9399  17003  15696   2509   -371  -2416       C  
ATOM   1471  O   LEU A 208       7.296 -24.093  10.454  1.00112.54           O  
ANISOU 1471  O   LEU A 208     9296  17365  16099   2467   -313  -2757       O  
ATOM   1472  CB  LEU A 208       4.762 -22.213  11.117  1.00102.89           C  
ANISOU 1472  CB  LEU A 208     8648  15898  14547   2119   -117  -2139       C  
ATOM   1473  CG  LEU A 208       4.234 -20.943  10.453  1.00106.17           C  
ANISOU 1473  CG  LEU A 208     9157  16237  14946   1798    185  -2053       C  
ATOM   1474  CD1 LEU A 208       3.744 -19.973  11.493  1.00107.92           C  
ANISOU 1474  CD1 LEU A 208     9463  16457  15086   1751    139  -1973       C  
ATOM   1475  CD2 LEU A 208       5.312 -20.255   9.617  1.00108.18           C  
ANISOU 1475  CD2 LEU A 208     9159  16570  15374   1579    435  -2363       C  
ATOM   1476  N   CYS A 209       5.774 -25.235  11.691  1.00108.27           N  
ANISOU 1476  N   CYS A 209     9251  16636  15253   2803   -648  -2269       N  
ATOM   1477  CA  CYS A 209       6.736 -26.114  12.362  1.00111.24           C  
ANISOU 1477  CA  CYS A 209     9472  17119  15677   3138   -940  -2483       C  
ATOM   1478  C   CYS A 209       6.831 -27.510  11.747  1.00116.55           C  
ANISOU 1478  C   CYS A 209    10215  17707  16362   3327   -993  -2442       C  
ATOM   1479  O   CYS A 209       7.913 -28.101  11.751  1.00118.82           O  
ANISOU 1479  O   CYS A 209    10266  18107  16773   3535  -1137  -2717       O  
ATOM   1480  CB  CYS A 209       6.456 -26.185  13.860  1.00112.01           C  
ANISOU 1480  CB  CYS A 209     9734  17216  15610   3369  -1224  -2386       C  
ATOM   1481  SG  CYS A 209       6.401 -24.572  14.683  1.00115.67           S  
ANISOU 1481  SG  CYS A 209    10112  17783  16056   3167  -1182  -2459       S  
ATOM   1482  N   GLY A 210       5.708 -28.024  11.248  1.00111.46           N  
ANISOU 1482  N   GLY A 210     9880  16870  15599   3262   -883  -2121       N  
ATOM   1483  CA  GLY A 210       5.629 -29.355  10.655  1.00111.83           C  
ANISOU 1483  CA  GLY A 210    10044  16806  15642   3414   -908  -2050       C  
ATOM   1484  C   GLY A 210       4.989 -30.370  11.581  1.00116.56           C  
ANISOU 1484  C   GLY A 210    10969  17255  16064   3686  -1125  -1820       C  
ATOM   1485  O   GLY A 210       4.390 -31.344  11.118  1.00115.37           O  
ANISOU 1485  O   GLY A 210    11039  16941  15857   3728  -1081  -1643       O  
ATOM   1486  N   THR A 211       5.114 -30.140  12.903  1.00114.90           N  
ANISOU 1486  N   THR A 211    10810  17092  15756   3865  -1347  -1829       N  
ATOM   1487  CA  THR A 211       4.570 -31.000  13.960  1.00115.57           C  
ANISOU 1487  CA  THR A 211    11244  17025  15640   4134  -1550  -1621       C  
ATOM   1488  C   THR A 211       3.463 -30.291  14.756  1.00118.37           C  
ANISOU 1488  C   THR A 211    11845  17300  15830   3997  -1502  -1373       C  
ATOM   1489  O   THR A 211       3.181 -29.116  14.510  1.00116.30           O  
ANISOU 1489  O   THR A 211    11464  17110  15615   3717  -1338  -1374       O  
ATOM   1490  CB  THR A 211       5.700 -31.510  14.877  1.00127.48           C  
ANISOU 1490  CB  THR A 211    12657  18640  17141   4527  -1883  -1848       C  
ATOM   1491  OG1 THR A 211       6.426 -30.396  15.401  1.00128.23           O  
ANISOU 1491  OG1 THR A 211    12457  18957  17307   4485  -1966  -2094       O  
ATOM   1492  CG2 THR A 211       6.643 -32.482  14.174  1.00128.37           C  
ANISOU 1492  CG2 THR A 211    12593  18786  17396   4724  -1950  -2058       C  
ATOM   1493  N   LEU A 212       2.834 -31.016  15.701  1.00116.03           N  
ANISOU 1493  N   LEU A 212    11911  16839  15336   4194  -1629  -1163       N  
ATOM   1494  CA  LEU A 212       1.769 -30.500  16.564  1.00114.80           C  
ANISOU 1494  CA  LEU A 212    12020  16588  15011   4095  -1585   -932       C  
ATOM   1495  C   LEU A 212       2.357 -29.895  17.853  1.00121.35           C  
ANISOU 1495  C   LEU A 212    12811  17546  15752   4266  -1814  -1057       C  
ATOM   1496  O   LEU A 212       3.346 -30.431  18.362  1.00123.69           O  
ANISOU 1496  O   LEU A 212    13050  17915  16030   4583  -2073  -1236       O  
ATOM   1497  CB  LEU A 212       0.759 -31.613  16.907  1.00114.62           C  
ANISOU 1497  CB  LEU A 212    12431  16300  14819   4192  -1558   -652       C  
ATOM   1498  CG  LEU A 212      -0.082 -32.165  15.751  1.00117.50           C  
ANISOU 1498  CG  LEU A 212    12874  16522  15250   3993  -1322   -508       C  
ATOM   1499  CD1 LEU A 212      -0.615 -33.543  16.079  1.00118.66           C  
ANISOU 1499  CD1 LEU A 212    13403  16418  15264   4165  -1339   -332       C  
ATOM   1500  CD2 LEU A 212      -1.225 -31.230  15.396  1.00117.16           C  
ANISOU 1500  CD2 LEU A 212    12832  16464  15221   3650  -1092   -363       C  
ATOM   1501  N   PRO A 213       1.783 -28.792  18.398  1.00117.35           N  
ANISOU 1501  N   PRO A 213    12332  17071  15184   4078  -1738   -983       N  
ATOM   1502  CA  PRO A 213       2.347 -28.209  19.631  1.00119.31           C  
ANISOU 1502  CA  PRO A 213    12547  17446  15339   4236  -1960  -1118       C  
ATOM   1503  C   PRO A 213       2.079 -29.036  20.889  1.00125.75           C  
ANISOU 1503  C   PRO A 213    13766  18117  15894   4549  -2166   -970       C  
ATOM   1504  O   PRO A 213       2.899 -29.030  21.809  1.00127.95           O  
ANISOU 1504  O   PRO A 213    14020  18506  16088   4822  -2445  -1138       O  
ATOM   1505  CB  PRO A 213       1.705 -26.822  19.698  1.00118.90           C  
ANISOU 1505  CB  PRO A 213    12431  17439  15306   3915  -1772  -1061       C  
ATOM   1506  CG  PRO A 213       0.427 -26.957  18.965  1.00120.47           C  
ANISOU 1506  CG  PRO A 213    12813  17459  15500   3682  -1505   -790       C  
ATOM   1507  CD  PRO A 213       0.610 -28.026  17.925  1.00115.99           C  
ANISOU 1507  CD  PRO A 213    12221  16825  15024   3734  -1463   -790       C  
ATOM   1508  N   PHE A 214       0.938 -29.750  20.920  1.00121.70           N  
ANISOU 1508  N   PHE A 214    13633  17355  15252   4510  -2023   -670       N  
ATOM   1509  CA  PHE A 214       0.528 -30.605  22.033  1.00123.42           C  
ANISOU 1509  CA  PHE A 214    14313  17376  15206   4766  -2143   -491       C  
ATOM   1510  C   PHE A 214       0.260 -32.016  21.498  1.00128.30           C  
ANISOU 1510  C   PHE A 214    15165  17777  15805   4878  -2085   -359       C  
ATOM   1511  O   PHE A 214      -0.796 -32.267  20.911  1.00125.71           O  
ANISOU 1511  O   PHE A 214    14967  17290  15508   4643  -1825   -167       O  
ATOM   1512  CB  PHE A 214      -0.711 -30.025  22.753  1.00123.66           C  
ANISOU 1512  CB  PHE A 214    14615  17284  15085   4571  -1974   -263       C  
ATOM   1513  CG  PHE A 214      -0.657 -28.543  23.051  1.00124.17           C  
ANISOU 1513  CG  PHE A 214    14440  17538  15203   4378  -1953   -369       C  
ATOM   1514  CD1 PHE A 214       0.022 -28.064  24.166  1.00129.39           C  
ANISOU 1514  CD1 PHE A 214    15097  18326  15739   4571  -2195   -512       C  
ATOM   1515  CD2 PHE A 214      -1.300 -27.627  22.225  1.00123.42           C  
ANISOU 1515  CD2 PHE A 214    14142  17483  15268   4015  -1695   -329       C  
ATOM   1516  CE1 PHE A 214       0.070 -26.694  24.440  1.00129.47           C  
ANISOU 1516  CE1 PHE A 214    14891  18499  15804   4380  -2160   -622       C  
ATOM   1517  CE2 PHE A 214      -1.251 -26.257  22.500  1.00125.48           C  
ANISOU 1517  CE2 PHE A 214    14210  17893  15573   3842  -1660   -424       C  
ATOM   1518  CZ  PHE A 214      -0.567 -25.800  23.606  1.00125.63           C  
ANISOU 1518  CZ  PHE A 214    14216  18032  15483   4012  -1882   -572       C  
ATOM   1519  N   ASP A 215       1.246 -32.919  21.655  1.00128.28           N  
ANISOU 1519  N   ASP A 215    15191  17780  15769   5240  -2332   -488       N  
ATOM   1520  CA  ASP A 215       1.157 -34.302  21.182  1.00129.27           C  
ANISOU 1520  CA  ASP A 215    15542  17697  15877   5389  -2301   -393       C  
ATOM   1521  C   ASP A 215       1.730 -35.293  22.193  1.00137.55           C  
ANISOU 1521  C   ASP A 215    16940  18626  16699   5858  -2587   -393       C  
ATOM   1522  O   ASP A 215       2.806 -35.057  22.749  1.00139.53           O  
ANISOU 1522  O   ASP A 215    17029  19061  16924   6140  -2894   -616       O  
ATOM   1523  CB  ASP A 215       1.833 -34.457  19.806  1.00130.51           C  
ANISOU 1523  CB  ASP A 215    15299  17983  16306   5312  -2252   -582       C  
ATOM   1524  CG  ASP A 215       1.662 -35.823  19.163  1.00141.06           C  
ANISOU 1524  CG  ASP A 215    16841  19104  17653   5414  -2180   -488       C  
ATOM   1525  OD1 ASP A 215       2.686 -36.434  18.790  1.00143.51           O  
ANISOU 1525  OD1 ASP A 215    16990  19481  18056   5656  -2342   -680       O  
ATOM   1526  OD2 ASP A 215       0.503 -36.275  19.021  1.00145.62           O  
ANISOU 1526  OD2 ASP A 215    17726  19446  18156   5245  -1954   -243       O  
ATOM   1527  N   ASP A 216       1.001 -36.401  22.424  1.00135.39           N  
ANISOU 1527  N   ASP A 216    17156  18032  16255   5944  -2483   -153       N  
ATOM   1528  CA  ASP A 216       1.378 -37.474  23.350  1.00139.19           C  
ANISOU 1528  CA  ASP A 216    18088  18320  16479   6391  -2708    -97       C  
ATOM   1529  C   ASP A 216       0.749 -38.813  22.939  1.00143.96           C  
ANISOU 1529  C   ASP A 216    19083  18584  17030   6408  -2515    102       C  
ATOM   1530  O   ASP A 216      -0.244 -38.826  22.206  1.00140.74           O  
ANISOU 1530  O   ASP A 216    18668  18070  16735   6039  -2189    237       O  
ATOM   1531  CB  ASP A 216       0.984 -37.109  24.793  1.00142.33           C  
ANISOU 1531  CB  ASP A 216    18867  18639  16574   6497  -2791     31       C  
ATOM   1532  CG  ASP A 216       1.855 -37.770  25.841  1.00156.82           C  
ANISOU 1532  CG  ASP A 216    21015  20420  18148   7037  -3163    -32       C  
ATOM   1533  OD1 ASP A 216       1.616 -38.958  26.147  1.00159.47           O  
ANISOU 1533  OD1 ASP A 216    21861  20445  18287   7266  -3149    137       O  
ATOM   1534  OD2 ASP A 216       2.775 -37.100  26.355  1.00164.30           O  
ANISOU 1534  OD2 ASP A 216    21709  21633  19084   7236  -3471   -261       O  
ATOM   1535  N   GLU A 217       1.335 -39.936  23.414  1.00144.59           N  
ANISOU 1535  N   GLU A 217    19507  18492  16939   6846  -2725    106       N  
ATOM   1536  CA  GLU A 217       0.877 -41.301  23.132  1.00145.73           C  
ANISOU 1536  CA  GLU A 217    20075  18284  17010   6921  -2566    277       C  
ATOM   1537  C   GLU A 217      -0.496 -41.565  23.767  1.00149.47           C  
ANISOU 1537  C   GLU A 217    21090  18432  17271   6717  -2266    580       C  
ATOM   1538  O   GLU A 217      -1.463 -41.790  23.035  1.00146.81           O  
ANISOU 1538  O   GLU A 217    20764  17959  17057   6358  -1926    695       O  
ATOM   1539  CB  GLU A 217       1.930 -42.334  23.591  1.00151.53           C  
ANISOU 1539  CB  GLU A 217    21061  18921  17592   7487  -2898    191       C  
ATOM   1540  CG  GLU A 217       1.730 -43.739  23.039  1.00163.51           C  
ANISOU 1540  CG  GLU A 217    22907  20115  19104   7584  -2756    300       C  
ATOM   1541  CD  GLU A 217       0.790 -44.627  23.832  1.00185.52           C  
ANISOU 1541  CD  GLU A 217    26446  22460  21585   7632  -2563    599       C  
ATOM   1542  OE1 GLU A 217       1.133 -44.984  24.983  1.00183.03           O  
ANISOU 1542  OE1 GLU A 217    26583  22004  20955   8034  -2788    661       O  
ATOM   1543  OE2 GLU A 217      -0.287 -44.975  23.297  1.00177.50           O  
ANISOU 1543  OE2 GLU A 217    25573  21230  20638   7267  -2182    760       O  
ATOM   1544  N   HIS A 218      -0.582 -41.531  25.114  1.00148.56           N  
ANISOU 1544  N   HIS A 218    21414  18196  16837   6940  -2384    688       N  
ATOM   1545  CA  HIS A 218      -1.837 -41.763  25.830  1.00148.50           C  
ANISOU 1545  CA  HIS A 218    21944  17870  16608   6755  -2085    957       C  
ATOM   1546  C   HIS A 218      -2.595 -40.467  26.111  1.00149.32           C  
ANISOU 1546  C   HIS A 218    21844  18139  16754   6383  -1930    989       C  
ATOM   1547  O   HIS A 218      -1.989 -39.416  26.331  1.00148.11           O  
ANISOU 1547  O   HIS A 218    21328  18298  16648   6421  -2151    832       O  
ATOM   1548  CB  HIS A 218      -1.639 -42.610  27.101  1.00153.78           C  
ANISOU 1548  CB  HIS A 218    23315  18241  16875   7190  -2234   1090       C  
ATOM   1549  CG  HIS A 218      -0.613 -42.084  28.056  1.00159.63           C  
ANISOU 1549  CG  HIS A 218    24029  19193  17429   7593  -2667    953       C  
ATOM   1550  ND1 HIS A 218       0.740 -42.160  27.775  1.00163.04           N  
ANISOU 1550  ND1 HIS A 218    24120  19868  17961   7960  -3063    700       N  
ATOM   1551  CD2 HIS A 218      -0.775 -41.546  29.286  1.00162.72           C  
ANISOU 1551  CD2 HIS A 218    24712  19575  17537   7688  -2757   1021       C  
ATOM   1552  CE1 HIS A 218       1.353 -41.638  28.825  1.00164.71           C  
ANISOU 1552  CE1 HIS A 218    24397  20226  17959   8262  -3394    609       C  
ATOM   1553  NE2 HIS A 218       0.483 -41.259  29.761  1.00164.92           N  
ANISOU 1553  NE2 HIS A 218    24816  20106  17740   8116  -3228    804       N  
ATOM   1554  N   VAL A 219      -3.935 -40.564  26.077  1.00144.42           N  
ANISOU 1554  N   VAL A 219    21446  17299  16129   6019  -1537   1176       N  
ATOM   1555  CA  VAL A 219      -4.919 -39.489  26.254  1.00141.56           C  
ANISOU 1555  CA  VAL A 219    20939  17027  15822   5625  -1310   1232       C  
ATOM   1556  C   VAL A 219      -4.759 -38.685  27.589  1.00146.58           C  
ANISOU 1556  C   VAL A 219    21745  17741  16206   5767  -1474   1246       C  
ATOM   1557  O   VAL A 219      -4.818 -37.455  27.501  1.00143.77           O  
ANISOU 1557  O   VAL A 219    20985  17657  15982   5563  -1493   1155       O  
ATOM   1558  CB  VAL A 219      -6.379 -40.006  26.070  1.00144.69           C  
ANISOU 1558  CB  VAL A 219    21618  17121  16236   5267   -861   1412       C  
ATOM   1559  CG1 VAL A 219      -7.349 -38.855  25.823  1.00141.15           C  
ANISOU 1559  CG1 VAL A 219    20841  16833  15957   4833   -637   1411       C  
ATOM   1560  CG2 VAL A 219      -6.476 -41.026  24.935  1.00144.23           C  
ANISOU 1560  CG2 VAL A 219    21512  16929  16359   5196   -724   1400       C  
ATOM   1561  N   PRO A 220      -4.565 -39.289  28.802  1.00146.78           N  
ANISOU 1561  N   PRO A 220    22363  17539  15868   6106  -1590   1353       N  
ATOM   1562  CA  PRO A 220      -4.473 -38.463  30.027  1.00147.65           C  
ANISOU 1562  CA  PRO A 220    22624  17737  15738   6213  -1735   1357       C  
ATOM   1563  C   PRO A 220      -3.363 -37.406  30.060  1.00150.74           C  
ANISOU 1563  C   PRO A 220    22504  18544  16225   6365  -2115   1112       C  
ATOM   1564  O   PRO A 220      -3.628 -36.288  30.505  1.00148.89           O  
ANISOU 1564  O   PRO A 220    22107  18477  15987   6188  -2094   1080       O  
ATOM   1565  CB  PRO A 220      -4.297 -39.497  31.144  1.00154.02           C  
ANISOU 1565  CB  PRO A 220    24179  18212  16130   6616  -1829   1499       C  
ATOM   1566  CG  PRO A 220      -4.868 -40.748  30.593  1.00159.09           C  
ANISOU 1566  CG  PRO A 220    25140  18506  16801   6537  -1542   1641       C  
ATOM   1567  CD  PRO A 220      -4.500 -40.726  29.143  1.00151.87           C  
ANISOU 1567  CD  PRO A 220    23614  17810  16281   6395  -1569   1486       C  
ATOM   1568  N   THR A 221      -2.141 -37.742  29.596  1.00148.40           N  
ANISOU 1568  N   THR A 221    21948  18412  16026   6676  -2442    923       N  
ATOM   1569  CA  THR A 221      -1.010 -36.800  29.575  1.00148.10           C  
ANISOU 1569  CA  THR A 221    21390  18772  16109   6815  -2793    644       C  
ATOM   1570  C   THR A 221      -1.172 -35.720  28.502  1.00147.57           C  
ANISOU 1570  C   THR A 221    20666  18984  16419   6386  -2634    517       C  
ATOM   1571  O   THR A 221      -0.653 -34.614  28.672  1.00146.47           O  
ANISOU 1571  O   THR A 221    20153  19139  16361   6347  -2792    332       O  
ATOM   1572  CB  THR A 221       0.340 -37.519  29.478  1.00159.25           C  
ANISOU 1572  CB  THR A 221    22733  20268  17506   7296  -3188    454       C  
ATOM   1573  OG1 THR A 221       0.253 -38.594  28.541  1.00158.75           O  
ANISOU 1573  OG1 THR A 221    22720  20022  17574   7295  -3048    516       O  
ATOM   1574  CG2 THR A 221       0.829 -38.023  30.827  1.00162.35           C  
ANISOU 1574  CG2 THR A 221    23665  20530  17489   7800  -3502    485       C  
ATOM   1575  N   LEU A 222      -1.898 -36.038  27.409  1.00141.42           N  
ANISOU 1575  N   LEU A 222    19772  18103  15858   6069  -2320    611       N  
ATOM   1576  CA  LEU A 222      -2.190 -35.115  26.308  1.00137.37           C  
ANISOU 1576  CA  LEU A 222    18717  17803  15675   5663  -2136    526       C  
ATOM   1577  C   LEU A 222      -3.107 -33.988  26.804  1.00139.01           C  
ANISOU 1577  C   LEU A 222    18916  18052  15851   5353  -1948    611       C  
ATOM   1578  O   LEU A 222      -2.871 -32.824  26.477  1.00136.66           O  
ANISOU 1578  O   LEU A 222    18181  18017  15724   5175  -1974    468       O  
ATOM   1579  CB  LEU A 222      -2.830 -35.880  25.127  1.00135.70           C  
ANISOU 1579  CB  LEU A 222    18483  17432  15645   5443  -1861    622       C  
ATOM   1580  CG  LEU A 222      -3.290 -35.068  23.905  1.00136.65           C  
ANISOU 1580  CG  LEU A 222    18125  17722  16072   5029  -1645    568       C  
ATOM   1581  CD1 LEU A 222      -2.116 -34.637  23.044  1.00136.37           C  
ANISOU 1581  CD1 LEU A 222    17570  17979  16265   5083  -1830    313       C  
ATOM   1582  CD2 LEU A 222      -4.252 -35.869  23.065  1.00137.87           C  
ANISOU 1582  CD2 LEU A 222    18403  17660  16322   4809  -1349    706       C  
ATOM   1583  N   PHE A 223      -4.126 -34.341  27.618  1.00136.13           N  
ANISOU 1583  N   PHE A 223    19047  17414  15261   5297  -1750    832       N  
ATOM   1584  CA  PHE A 223      -5.087 -33.408  28.212  1.00134.43           C  
ANISOU 1584  CA  PHE A 223    18896  17193  14987   5028  -1550    925       C  
ATOM   1585  C   PHE A 223      -4.414 -32.461  29.208  1.00139.36           C  
ANISOU 1585  C   PHE A 223    19463  18019  15467   5192  -1812    803       C  
ATOM   1586  O   PHE A 223      -4.818 -31.302  29.312  1.00136.91           O  
ANISOU 1586  O   PHE A 223    18932  17851  15237   4944  -1715    772       O  
ATOM   1587  CB  PHE A 223      -6.245 -34.171  28.885  1.00137.38           C  
ANISOU 1587  CB  PHE A 223    19849  17204  15145   4958  -1268   1166       C  
ATOM   1588  CG  PHE A 223      -7.305 -34.777  27.985  1.00137.23           C  
ANISOU 1588  CG  PHE A 223    19845  16997  15298   4655   -913   1277       C  
ATOM   1589  CD1 PHE A 223      -7.307 -34.535  26.614  1.00137.54           C  
ANISOU 1589  CD1 PHE A 223    19398  17202  15660   4444   -857   1182       C  
ATOM   1590  CD2 PHE A 223      -8.320 -35.565  28.515  1.00140.78           C  
ANISOU 1590  CD2 PHE A 223    20800  17105  15584   4570   -625   1461       C  
ATOM   1591  CE1 PHE A 223      -8.289 -35.091  25.790  1.00137.13           C  
ANISOU 1591  CE1 PHE A 223    19352  16992  15760   4177   -554   1261       C  
ATOM   1592  CE2 PHE A 223      -9.306 -36.114  27.690  1.00142.28           C  
ANISOU 1592  CE2 PHE A 223    20973  17137  15952   4277   -299   1526       C  
ATOM   1593  CZ  PHE A 223      -9.289 -35.865  26.335  1.00137.61           C  
ANISOU 1593  CZ  PHE A 223    19878  16731  15678   4089   -281   1421       C  
ATOM   1594  N   LYS A 224      -3.378 -32.953  29.923  1.00139.32           N  
ANISOU 1594  N   LYS A 224    19653  18028  15253   5621  -2154    719       N  
ATOM   1595  CA  LYS A 224      -2.590 -32.183  30.892  1.00140.97           C  
ANISOU 1595  CA  LYS A 224    19811  18442  15310   5839  -2464    562       C  
ATOM   1596  C   LYS A 224      -1.759 -31.107  30.184  1.00142.85           C  
ANISOU 1596  C   LYS A 224    19376  19053  15847   5727  -2608    285       C  
ATOM   1597  O   LYS A 224      -1.554 -30.027  30.742  1.00142.33           O  
ANISOU 1597  O   LYS A 224    19145  19174  15759   5673  -2700    165       O  
ATOM   1598  CB  LYS A 224      -1.674 -33.107  31.711  1.00148.08           C  
ANISOU 1598  CB  LYS A 224    21080  19263  15920   6365  -2820    522       C  
ATOM   1599  N   LYS A 225      -1.290 -31.406  28.954  1.00138.01           N  
ANISOU 1599  N   LYS A 225    18395  18532  15510   5678  -2603    177       N  
ATOM   1600  CA  LYS A 225      -0.499 -30.494  28.123  1.00136.28           C  
ANISOU 1600  CA  LYS A 225    17555  18632  15592   5544  -2682    -88       C  
ATOM   1601  C   LYS A 225      -1.364 -29.368  27.547  1.00136.28           C  
ANISOU 1601  C   LYS A 225    17301  18696  15785   5080  -2369    -34       C  
ATOM   1602  O   LYS A 225      -0.902 -28.227  27.482  1.00135.15           O  
ANISOU 1602  O   LYS A 225    16791  18791  15771   4957  -2423   -223       O  
ATOM   1603  CB  LYS A 225       0.220 -31.258  27.000  1.00138.97           C  
ANISOU 1603  CB  LYS A 225    17641  19017  16143   5641  -2743   -206       C  
ATOM   1604  CG  LYS A 225       1.400 -32.093  27.483  1.00157.65           C  
ANISOU 1604  CG  LYS A 225    20096  21420  18383   6132  -3126   -365       C  
ATOM   1605  CD  LYS A 225       2.051 -32.860  26.343  1.00168.36           C  
ANISOU 1605  CD  LYS A 225    21201  22808  19960   6214  -3157   -483       C  
ATOM   1606  N   ILE A 226      -2.613 -29.688  27.136  1.00130.60           N  
ANISOU 1606  N   ILE A 226    16780  17759  15084   4830  -2045    207       N  
ATOM   1607  CA  ILE A 226      -3.576 -28.727  26.575  1.00127.06           C  
ANISOU 1607  CA  ILE A 226    16136  17340  14801   4421  -1750    277       C  
ATOM   1608  C   ILE A 226      -4.076 -27.770  27.675  1.00130.72           C  
ANISOU 1608  C   ILE A 226    16739  17817  15110   4339  -1714    320       C  
ATOM   1609  O   ILE A 226      -4.119 -26.558  27.449  1.00128.55           O  
ANISOU 1609  O   ILE A 226    16160  17709  14975   4120  -1650    227       O  
ATOM   1610  CB  ILE A 226      -4.728 -29.432  25.787  1.00128.37           C  
ANISOU 1610  CB  ILE A 226    16441  17288  15046   4207  -1446    479       C  
ATOM   1611  CG1 ILE A 226      -4.167 -30.298  24.631  1.00128.75           C  
ANISOU 1611  CG1 ILE A 226    16318  17342  15258   4277  -1484    412       C  
ATOM   1612  CG2 ILE A 226      -5.756 -28.417  25.248  1.00126.07           C  
ANISOU 1612  CG2 ILE A 226    15951  17035  14913   3824  -1174    536       C  
ATOM   1613  CD1 ILE A 226      -5.051 -31.488  24.204  1.00135.98           C  
ANISOU 1613  CD1 ILE A 226    17519  17988  16158   4219  -1276    597       C  
ATOM   1614  N   ARG A 227      -4.414 -28.314  28.867  1.00129.32           N  
ANISOU 1614  N   ARG A 227    17043  17455  14635   4521  -1752    453       N  
ATOM   1615  CA  ARG A 227      -4.878 -27.535  30.024  1.00129.59           C  
ANISOU 1615  CA  ARG A 227    17277  17479  14482   4475  -1720    498       C  
ATOM   1616  C   ARG A 227      -3.784 -26.615  30.579  1.00134.45           C  
ANISOU 1616  C   ARG A 227    17651  18362  15072   4619  -2016    255       C  
ATOM   1617  O   ARG A 227      -4.095 -25.547  31.108  1.00133.32           O  
ANISOU 1617  O   ARG A 227    17455  18297  14904   4467  -1956    226       O  
ATOM   1618  CB  ARG A 227      -5.438 -28.445  31.128  1.00132.57           C  
ANISOU 1618  CB  ARG A 227    18272  17572  14525   4649  -1675    695       C  
ATOM   1619  CG  ARG A 227      -6.816 -29.009  30.812  1.00142.50           C  
ANISOU 1619  CG  ARG A 227    19770  18562  15811   4399  -1294    921       C  
ATOM   1620  CD  ARG A 227      -7.427 -29.708  32.007  1.00156.52           C  
ANISOU 1620  CD  ARG A 227    22173  20048  17250   4516  -1189   1102       C  
ATOM   1621  N   GLY A 228      -2.527 -27.038  30.446  1.00132.78           N  
ANISOU 1621  N   GLY A 228    17282  18288  14880   4907  -2326     63       N  
ATOM   1622  CA  GLY A 228      -1.360 -26.272  30.868  1.00134.14           C  
ANISOU 1622  CA  GLY A 228    17162  18737  15066   5058  -2630   -227       C  
ATOM   1623  C   GLY A 228      -1.060 -25.129  29.917  1.00135.27           C  
ANISOU 1623  C   GLY A 228    16745  19111  15540   4756  -2529   -415       C  
ATOM   1624  O   GLY A 228      -0.656 -24.047  30.350  1.00135.18           O  
ANISOU 1624  O   GLY A 228    16525  19285  15553   4693  -2612   -597       O  
ATOM   1625  N   GLY A 229      -1.264 -25.382  28.622  1.00129.32           N  
ANISOU 1625  N   GLY A 229    15778  18330  15026   4570  -2340   -371       N  
ATOM   1626  CA  GLY A 229      -1.057 -24.420  27.545  1.00126.73           C  
ANISOU 1626  CA  GLY A 229    14978  18172  15001   4273  -2196   -514       C  
ATOM   1627  C   GLY A 229       0.389 -24.073  27.252  1.00131.83           C  
ANISOU 1627  C   GLY A 229    15197  19082  15810   4379  -2421   -863       C  
ATOM   1628  O   GLY A 229       0.657 -23.033  26.645  1.00130.17           O  
ANISOU 1628  O   GLY A 229    14625  19022  15814   4129  -2305  -1020       O  
ATOM   1629  N   VAL A 230       1.328 -24.943  27.668  1.00131.08           N  
ANISOU 1629  N   VAL A 230    15147  19037  15620   4752  -2735   -999       N  
ATOM   1630  CA  VAL A 230       2.764 -24.749  27.454  1.00132.88           C  
ANISOU 1630  CA  VAL A 230    14952  19527  16008   4897  -2980  -1373       C  
ATOM   1631  C   VAL A 230       3.191 -25.518  26.199  1.00135.83           C  
ANISOU 1631  C   VAL A 230    15115  19900  16594   4906  -2927  -1424       C  
ATOM   1632  O   VAL A 230       3.127 -26.750  26.171  1.00136.30           O  
ANISOU 1632  O   VAL A 230    15429  19810  16549   5147  -3011  -1296       O  
ATOM   1633  CB  VAL A 230       3.616 -25.108  28.706  1.00140.85           C  
ANISOU 1633  CB  VAL A 230    16090  20632  16794   5328  -3396  -1547       C  
ATOM   1634  CG1 VAL A 230       5.105 -24.872  28.453  1.00143.16           C  
ANISOU 1634  CG1 VAL A 230    15882  21223  17291   5469  -3651  -1985       C  
ATOM   1635  CG2 VAL A 230       3.155 -24.324  29.933  1.00141.13           C  
ANISOU 1635  CG2 VAL A 230    16355  20663  16604   5303  -3432  -1494       C  
ATOM   1636  N   PHE A 231       3.600 -24.776  25.158  1.00130.74           N  
ANISOU 1636  N   PHE A 231    14034  19405  16238   4633  -2764  -1608       N  
ATOM   1637  CA  PHE A 231       4.046 -25.332  23.880  1.00129.94           C  
ANISOU 1637  CA  PHE A 231    13692  19322  16357   4593  -2676  -1690       C  
ATOM   1638  C   PHE A 231       5.446 -24.841  23.519  1.00135.21           C  
ANISOU 1638  C   PHE A 231    13849  20266  17260   4608  -2796  -2119       C  
ATOM   1639  O   PHE A 231       5.818 -23.722  23.885  1.00135.33           O  
ANISOU 1639  O   PHE A 231    13637  20443  17339   4470  -2801  -2324       O  
ATOM   1640  CB  PHE A 231       3.036 -25.023  22.757  1.00128.15           C  
ANISOU 1640  CB  PHE A 231    13479  18963  16248   4213  -2292  -1466       C  
ATOM   1641  CG  PHE A 231       2.833 -23.561  22.425  1.00128.05           C  
ANISOU 1641  CG  PHE A 231    13244  19041  16367   3852  -2069  -1533       C  
ATOM   1642  CD1 PHE A 231       1.882 -22.804  23.099  1.00129.80           C  
ANISOU 1642  CD1 PHE A 231    13677  19184  16458   3704  -1963  -1352       C  
ATOM   1643  CD2 PHE A 231       3.557 -22.955  21.405  1.00130.16           C  
ANISOU 1643  CD2 PHE A 231    13117  19452  16887   3652  -1937  -1771       C  
ATOM   1644  CE1 PHE A 231       1.686 -21.455  22.784  1.00129.31           C  
ANISOU 1644  CE1 PHE A 231    13435  19183  16511   3387  -1754  -1410       C  
ATOM   1645  CE2 PHE A 231       3.363 -21.607  21.092  1.00131.66           C  
ANISOU 1645  CE2 PHE A 231    13153  19692  17181   3322  -1710  -1823       C  
ATOM   1646  CZ  PHE A 231       2.427 -20.867  21.781  1.00128.39           C  
ANISOU 1646  CZ  PHE A 231    12956  19194  16632   3201  -1628  -1638       C  
ATOM   1647  N   TYR A 232       6.214 -25.674  22.794  1.00132.54           N  
ANISOU 1647  N   TYR A 232    13324  19975  17061   4763  -2874  -2272       N  
ATOM   1648  CA  TYR A 232       7.575 -25.355  22.362  1.00134.40           C  
ANISOU 1648  CA  TYR A 232    13050  20467  17547   4784  -2968  -2710       C  
ATOM   1649  C   TYR A 232       7.580 -24.283  21.271  1.00135.68           C  
ANISOU 1649  C   TYR A 232    12896  20696  17961   4332  -2610  -2810       C  
ATOM   1650  O   TYR A 232       6.780 -24.349  20.337  1.00132.29           O  
ANISOU 1650  O   TYR A 232    12591  20107  17565   4095  -2319  -2564       O  
ATOM   1651  CB  TYR A 232       8.311 -26.629  21.899  1.00137.60           C  
ANISOU 1651  CB  TYR A 232    13379  20880  18023   5092  -3137  -2826       C  
ATOM   1652  CG  TYR A 232       9.737 -26.398  21.444  1.00142.03           C  
ANISOU 1652  CG  TYR A 232    13391  21710  18862   5131  -3232  -3310       C  
ATOM   1653  CD1 TYR A 232      10.760 -26.192  22.365  1.00147.72           C  
ANISOU 1653  CD1 TYR A 232    13878  22662  19587   5401  -3581  -3671       C  
ATOM   1654  CD2 TYR A 232      10.071 -26.421  20.093  1.00141.93           C  
ANISOU 1654  CD2 TYR A 232    13092  21725  19109   4906  -2975  -3426       C  
ATOM   1655  CE1 TYR A 232      12.075 -25.981  21.952  1.00151.36           C  
ANISOU 1655  CE1 TYR A 232    13794  23383  20332   5427  -3659  -4157       C  
ATOM   1656  CE2 TYR A 232      11.383 -26.216  19.668  1.00145.59           C  
ANISOU 1656  CE2 TYR A 232    13041  22432  19844   4922  -3026  -3894       C  
ATOM   1657  CZ  TYR A 232      12.382 -25.996  20.601  1.00156.84           C  
ANISOU 1657  CZ  TYR A 232    14203  24092  21296   5177  -3366  -4269       C  
ATOM   1658  OH  TYR A 232      13.677 -25.796  20.188  1.00161.06           O  
ANISOU 1658  OH  TYR A 232    14193  24879  22125   5183  -3408  -4770       O  
ATOM   1659  N   ILE A 233       8.477 -23.293  21.404  1.00133.70           N  
ANISOU 1659  N   ILE A 233    12253  20672  17876   4217  -2630  -3180       N  
ATOM   1660  CA  ILE A 233       8.631 -22.201  20.440  1.00132.15           C  
ANISOU 1660  CA  ILE A 233    11765  20534  17912   3793  -2283  -3321       C  
ATOM   1661  C   ILE A 233      10.007 -22.344  19.751  1.00138.32           C  
ANISOU 1661  C   ILE A 233    12064  21518  18974   3817  -2304  -3765       C  
ATOM   1662  O   ILE A 233      11.034 -22.066  20.379  1.00141.16           O  
ANISOU 1662  O   ILE A 233    12110  22101  19423   3954  -2529  -4154       O  
ATOM   1663  CB  ILE A 233       8.377 -20.797  21.077  1.00134.81           C  
ANISOU 1663  CB  ILE A 233    12080  20921  18222   3552  -2187  -3366       C  
ATOM   1664  CG1 ILE A 233       6.958 -20.709  21.692  1.00132.57           C  
ANISOU 1664  CG1 ILE A 233    12270  20426  17673   3524  -2139  -2926       C  
ATOM   1665  CG2 ILE A 233       8.594 -19.669  20.054  1.00134.68           C  
ANISOU 1665  CG2 ILE A 233    11794  20939  18440   3119  -1808  -3523       C  
ATOM   1666  CD1 ILE A 233       6.845 -19.845  22.956  1.00140.82           C  
ANISOU 1666  CD1 ILE A 233    13382  21537  18584   3532  -2265  -2980       C  
ATOM   1667  N   PRO A 234      10.043 -22.809  18.477  1.00133.46           N  
ANISOU 1667  N   PRO A 234    11380  20830  18497   3696  -2080  -3728       N  
ATOM   1668  CA  PRO A 234      11.335 -23.002  17.791  1.00135.87           C  
ANISOU 1668  CA  PRO A 234    11230  21318  19075   3715  -2072  -4156       C  
ATOM   1669  C   PRO A 234      12.121 -21.723  17.506  1.00140.72           C  
ANISOU 1669  C   PRO A 234    11430  22106  19931   3386  -1858  -4546       C  
ATOM   1670  O   PRO A 234      11.553 -20.630  17.470  1.00138.46           O  
ANISOU 1670  O   PRO A 234    11241  21752  19618   3063  -1612  -4432       O  
ATOM   1671  CB  PRO A 234      10.951 -23.734  16.499  1.00135.72           C  
ANISOU 1671  CB  PRO A 234    11326  21138  19102   3623  -1836  -3955       C  
ATOM   1672  CG  PRO A 234       9.560 -24.234  16.718  1.00137.08           C  
ANISOU 1672  CG  PRO A 234    12010  21065  19011   3677  -1836  -3448       C  
ATOM   1673  CD  PRO A 234       8.923 -23.227  17.613  1.00131.52           C  
ANISOU 1673  CD  PRO A 234    11462  20343  18167   3551  -1832  -3319       C  
ATOM   1674  N   GLU A 235      13.440 -21.879  17.302  1.00140.46           N  
ANISOU 1674  N   GLU A 235    10935  22291  20142   3471  -1945  -5026       N  
ATOM   1675  CA  GLU A 235      14.394 -20.796  17.047  1.00142.40           C  
ANISOU 1675  CA  GLU A 235    10721  22724  20659   3177  -1747  -5491       C  
ATOM   1676  C   GLU A 235      14.257 -20.128  15.673  1.00143.77           C  
ANISOU 1676  C   GLU A 235    10857  22784  20986   2709  -1221  -5466       C  
ATOM   1677  O   GLU A 235      14.571 -18.941  15.557  1.00144.19           O  
ANISOU 1677  O   GLU A 235    10721  22891  21174   2370   -965  -5689       O  
ATOM   1678  CB  GLU A 235      15.840 -21.287  17.249  1.00148.49           C  
ANISOU 1678  CB  GLU A 235    10992  23771  21658   3440  -2014  -6037       C  
ATOM   1679  N   TYR A 236      13.822 -20.879  14.635  1.00137.57           N  
ANISOU 1679  N   TYR A 236    10262  21836  20174   2691  -1054  -5212       N  
ATOM   1680  CA  TYR A 236      13.711 -20.355  13.268  1.00135.76           C  
ANISOU 1680  CA  TYR A 236    10036  21488  20057   2286   -570  -5184       C  
ATOM   1681  C   TYR A 236      12.613 -19.303  13.072  1.00135.65           C  
ANISOU 1681  C   TYR A 236    10367  21280  19894   1956   -278  -4842       C  
ATOM   1682  O   TYR A 236      12.841 -18.353  12.323  1.00135.54           O  
ANISOU 1682  O   TYR A 236    10261  21233  20004   1585    106  -4979       O  
ATOM   1683  CB  TYR A 236      13.584 -21.468  12.209  1.00135.95           C  
ANISOU 1683  CB  TYR A 236    10165  21404  20085   2372   -491  -5032       C  
ATOM   1684  CG  TYR A 236      12.618 -22.588  12.533  1.00135.21           C  
ANISOU 1684  CG  TYR A 236    10468  21161  19744   2686   -749  -4599       C  
ATOM   1685  CD1 TYR A 236      11.261 -22.471  12.242  1.00133.40           C  
ANISOU 1685  CD1 TYR A 236    10683  20701  19301   2553   -601  -4121       C  
ATOM   1686  CD2 TYR A 236      13.073 -23.802  13.036  1.00137.73           C  
ANISOU 1686  CD2 TYR A 236    10721  21557  20054   3112  -1118  -4684       C  
ATOM   1687  CE1 TYR A 236      10.372 -23.513  12.504  1.00132.19           C  
ANISOU 1687  CE1 TYR A 236    10880  20403  18943   2808   -799  -3752       C  
ATOM   1688  CE2 TYR A 236      12.197 -24.856  13.291  1.00136.71           C  
ANISOU 1688  CE2 TYR A 236    10984  21260  19700   3377  -1311  -4293       C  
ATOM   1689  CZ  TYR A 236      10.846 -24.705  13.027  1.00140.10           C  
ANISOU 1689  CZ  TYR A 236    11834  21465  19932   3207  -1138  -3835       C  
ATOM   1690  OH  TYR A 236       9.979 -25.739  13.289  1.00139.13           O  
ANISOU 1690  OH  TYR A 236    12085  21174  19606   3440  -1300  -3480       O  
ATOM   1691  N   LEU A 237      11.441 -19.454  13.718  1.00128.82           N  
ANISOU 1691  N   LEU A 237     9902  20277  18768   2086   -439  -4412       N  
ATOM   1692  CA  LEU A 237      10.353 -18.481  13.563  1.00125.48           C  
ANISOU 1692  CA  LEU A 237     9800  19672  18204   1809   -187  -4092       C  
ATOM   1693  C   LEU A 237      10.605 -17.192  14.351  1.00129.76           C  
ANISOU 1693  C   LEU A 237    10218  20299  18787   1636   -147  -4288       C  
ATOM   1694  O   LEU A 237      11.000 -17.243  15.518  1.00130.92           O  
ANISOU 1694  O   LEU A 237    10231  20596  18917   1847   -462  -4454       O  
ATOM   1695  CB  LEU A 237       8.959 -19.069  13.853  1.00122.23           C  
ANISOU 1695  CB  LEU A 237     9840  19077  17526   1971   -321  -3587       C  
ATOM   1696  CG  LEU A 237       8.667 -19.603  15.250  1.00127.30           C  
ANISOU 1696  CG  LEU A 237    10586  19763  18018   2363   -744  -3490       C  
ATOM   1697  CD1 LEU A 237       8.339 -18.474  16.210  1.00126.95           C  
ANISOU 1697  CD1 LEU A 237    10689  19717  17831   2361   -854  -3389       C  
ATOM   1698  CD2 LEU A 237       7.508 -20.568  15.207  1.00127.46           C  
ANISOU 1698  CD2 LEU A 237    10944  19607  17878   2527   -804  -3108       C  
ATOM   1699  N   ASN A 238      10.388 -16.041  13.683  1.00125.14           N  
ANISOU 1699  N   ASN A 238     9698  19604  18246   1255    248  -4273       N  
ATOM   1700  CA  ASN A 238      10.602 -14.677  14.185  1.00125.77           C  
ANISOU 1700  CA  ASN A 238     9686  19718  18384   1008    395  -4461       C  
ATOM   1701  C   ASN A 238       9.764 -14.297  15.418  1.00127.42           C  
ANISOU 1701  C   ASN A 238    10128  19894  18392   1122    176  -4230       C  
ATOM   1702  O   ASN A 238       8.811 -14.998  15.766  1.00124.54           O  
ANISOU 1702  O   ASN A 238    10063  19436  17821   1346    -23  -3860       O  
ATOM   1703  CB  ASN A 238      10.396 -13.654  13.057  1.00126.00           C  
ANISOU 1703  CB  ASN A 238     9844  19572  18460    599    891  -4416       C  
ATOM   1704  CG  ASN A 238       9.036 -13.712  12.407  1.00144.98           C  
ANISOU 1704  CG  ASN A 238    12712  21727  20646    565   1022  -3910       C  
ATOM   1705  OD1 ASN A 238       8.056 -13.151  12.906  1.00137.47           O  
ANISOU 1705  OD1 ASN A 238    12041  20662  19530    548   1004  -3630       O  
ATOM   1706  ND2 ASN A 238       8.950 -14.389  11.272  1.00135.89           N  
ANISOU 1706  ND2 ASN A 238    11642  20494  19496    558   1154  -3802       N  
ATOM   1707  N   ARG A 239      10.137 -13.172  16.069  1.00125.17           N  
ANISOU 1707  N   ARG A 239     9701  19683  18175    950    238  -4471       N  
ATOM   1708  CA  ARG A 239       9.496 -12.616  17.267  1.00123.96           C  
ANISOU 1708  CA  ARG A 239     9726  19516  17858   1012     72  -4331       C  
ATOM   1709  C   ARG A 239       8.042 -12.189  17.039  1.00123.60           C  
ANISOU 1709  C   ARG A 239    10138  19216  17609    906    247  -3847       C  
ATOM   1710  O   ARG A 239       7.232 -12.291  17.963  1.00121.67           O  
ANISOU 1710  O   ARG A 239    10122  18933  17175   1072     39  -3603       O  
ATOM   1711  CB  ARG A 239      10.304 -11.424  17.812  1.00127.24           C  
ANISOU 1711  CB  ARG A 239     9862  20057  18427    792    168  -4745       C  
ATOM   1712  N   SER A 240       7.721 -11.694  15.825  1.00118.54           N  
ANISOU 1712  N   SER A 240     9634  18403  17003    637    627  -3724       N  
ATOM   1713  CA  SER A 240       6.381 -11.228  15.457  1.00115.09           C  
ANISOU 1713  CA  SER A 240     9608  17729  16391    537    805  -3300       C  
ATOM   1714  C   SER A 240       5.359 -12.365  15.369  1.00115.55           C  
ANISOU 1714  C   SER A 240     9928  17703  16274    791    610  -2907       C  
ATOM   1715  O   SER A 240       4.278 -12.244  15.942  1.00113.13           O  
ANISOU 1715  O   SER A 240     9888  17298  15798    866    526  -2612       O  
ATOM   1716  CB  SER A 240       6.423 -10.431  14.156  1.00118.76           C  
ANISOU 1716  CB  SER A 240    10159  18037  16928    214   1244  -3308       C  
ATOM   1717  OG  SER A 240       5.182  -9.795  13.896  1.00125.09           O  
ANISOU 1717  OG  SER A 240    11346  18620  17563    129   1399  -2944       O  
ATOM   1718  N   VAL A 241       5.702 -13.467  14.672  1.00111.70           N  
ANISOU 1718  N   VAL A 241     9356  17251  15835    914    551  -2922       N  
ATOM   1719  CA  VAL A 241       4.817 -14.626  14.511  1.00109.09           C  
ANISOU 1719  CA  VAL A 241     9253  16836  15359   1138    387  -2588       C  
ATOM   1720  C   VAL A 241       4.677 -15.419  15.837  1.00112.54           C  
ANISOU 1720  C   VAL A 241     9715  17358  15686   1454      2  -2535       C  
ATOM   1721  O   VAL A 241       3.613 -15.989  16.092  1.00110.03           O  
ANISOU 1721  O   VAL A 241     9676  16929  15204   1590   -101  -2208       O  
ATOM   1722  CB  VAL A 241       5.215 -15.511  13.291  1.00113.23           C  
ANISOU 1722  CB  VAL A 241     9702  17352  15968   1151    474  -2625       C  
ATOM   1723  CG1 VAL A 241       6.561 -16.205  13.488  1.00115.83           C  
ANISOU 1723  CG1 VAL A 241     9667  17882  16461   1297    304  -2993       C  
ATOM   1724  CG2 VAL A 241       4.122 -16.515  12.937  1.00110.58           C  
ANISOU 1724  CG2 VAL A 241     9648  16886  15480   1309    386  -2257       C  
ATOM   1725  N   ALA A 242       5.731 -15.409  16.684  1.00111.38           N  
ANISOU 1725  N   ALA A 242     9292  17403  15623   1566   -199  -2867       N  
ATOM   1726  CA  ALA A 242       5.757 -16.091  17.982  1.00111.80           C  
ANISOU 1726  CA  ALA A 242     9382  17545  15553   1885   -576  -2859       C  
ATOM   1727  C   ALA A 242       4.738 -15.505  18.964  1.00113.72           C  
ANISOU 1727  C   ALA A 242     9902  17697  15609   1881   -617  -2621       C  
ATOM   1728  O   ALA A 242       4.133 -16.259  19.727  1.00112.58           O  
ANISOU 1728  O   ALA A 242     9984  17505  15286   2119   -836  -2408       O  
ATOM   1729  CB  ALA A 242       7.154 -16.035  18.579  1.00116.08           C  
ANISOU 1729  CB  ALA A 242     9543  18326  16235   1990   -773  -3314       C  
ATOM   1730  N   THR A 243       4.538 -14.169  18.928  1.00109.64           N  
ANISOU 1730  N   THR A 243     9388  17140  15129   1605   -385  -2657       N  
ATOM   1731  CA  THR A 243       3.579 -13.464  19.787  1.00108.03           C  
ANISOU 1731  CA  THR A 243     9431  16845  14769   1568   -381  -2454       C  
ATOM   1732  C   THR A 243       2.134 -13.774  19.393  1.00108.53           C  
ANISOU 1732  C   THR A 243     9843  16702  14692   1568   -280  -2025       C  
ATOM   1733  O   THR A 243       1.259 -13.785  20.261  1.00107.07           O  
ANISOU 1733  O   THR A 243     9888  16449  14345   1661   -374  -1818       O  
ATOM   1734  CB  THR A 243       3.859 -11.953  19.834  1.00116.95           C  
ANISOU 1734  CB  THR A 243    10455  17985  15994   1280   -155  -2644       C  
ATOM   1735  OG1 THR A 243       3.920 -11.431  18.507  1.00115.85           O  
ANISOU 1735  OG1 THR A 243    10290  17749  15980   1018    185  -2651       O  
ATOM   1736  CG2 THR A 243       5.133 -11.612  20.599  1.00118.92           C  
ANISOU 1736  CG2 THR A 243    10373  18454  16356   1303   -309  -3082       C  
ATOM   1737  N   LEU A 244       1.888 -14.036  18.090  1.00103.68           N  
ANISOU 1737  N   LEU A 244     9263  15993  14139   1466    -87  -1910       N  
ATOM   1738  CA  LEU A 244       0.564 -14.374  17.561  1.00100.83           C  
ANISOU 1738  CA  LEU A 244     9189  15455  13669   1465      3  -1546       C  
ATOM   1739  C   LEU A 244       0.135 -15.773  18.017  1.00104.13           C  
ANISOU 1739  C   LEU A 244     9741  15853  13970   1733   -234  -1376       C  
ATOM   1740  O   LEU A 244      -0.976 -15.919  18.526  1.00102.28           O  
ANISOU 1740  O   LEU A 244     9751  15512  13599   1788   -263  -1125       O  
ATOM   1741  CB  LEU A 244       0.524 -14.242  16.022  1.00100.12           C  
ANISOU 1741  CB  LEU A 244     9095  15282  13664   1291    258  -1509       C  
ATOM   1742  CG  LEU A 244      -0.837 -14.439  15.327  1.00102.32           C  
ANISOU 1742  CG  LEU A 244     9647  15390  13842   1271    360  -1172       C  
ATOM   1743  CD1 LEU A 244      -1.757 -13.243  15.538  1.00101.41           C  
ANISOU 1743  CD1 LEU A 244     9708  15164  13658   1137    504  -1029       C  
ATOM   1744  CD2 LEU A 244      -0.657 -14.669  13.844  1.00104.57           C  
ANISOU 1744  CD2 LEU A 244     9915  15625  14192   1173    535  -1172       C  
ATOM   1745  N   LEU A 245       1.026 -16.783  17.868  1.00102.03           N  
ANISOU 1745  N   LEU A 245     9320  15682  13763   1900   -391  -1527       N  
ATOM   1746  CA  LEU A 245       0.789 -18.177  18.269  1.00101.82           C  
ANISOU 1746  CA  LEU A 245     9433  15624  13631   2170   -610  -1394       C  
ATOM   1747  C   LEU A 245       0.493 -18.317  19.765  1.00106.52           C  
ANISOU 1747  C   LEU A 245    10195  16222  14056   2356   -826  -1330       C  
ATOM   1748  O   LEU A 245      -0.317 -19.163  20.148  1.00105.26           O  
ANISOU 1748  O   LEU A 245    10295  15944  13754   2497   -900  -1096       O  
ATOM   1749  CB  LEU A 245       1.976 -19.070  17.877  1.00103.76           C  
ANISOU 1749  CB  LEU A 245     9453  15984  13986   2324   -742  -1623       C  
ATOM   1750  CG  LEU A 245       2.020 -19.534  16.425  1.00107.61           C  
ANISOU 1750  CG  LEU A 245     9888  16419  14581   2228   -569  -1594       C  
ATOM   1751  CD1 LEU A 245       3.446 -19.680  15.945  1.00110.13           C  
ANISOU 1751  CD1 LEU A 245     9869  16894  15083   2244   -588  -1941       C  
ATOM   1752  CD2 LEU A 245       1.265 -20.838  16.239  1.00108.82           C  
ANISOU 1752  CD2 LEU A 245    10273  16441  14632   2393   -645  -1343       C  
ATOM   1753  N   MET A 246       1.142 -17.481  20.598  1.00104.94           N  
ANISOU 1753  N   MET A 246     9857  16149  13866   2343   -909  -1548       N  
ATOM   1754  CA  MET A 246       0.957 -17.447  22.051  1.00105.83           C  
ANISOU 1754  CA  MET A 246    10127  16279  13804   2508  -1110  -1523       C  
ATOM   1755  C   MET A 246      -0.410 -16.856  22.407  1.00107.88           C  
ANISOU 1755  C   MET A 246    10662  16384  13942   2375   -952  -1245       C  
ATOM   1756  O   MET A 246      -1.078 -17.367  23.307  1.00107.37           O  
ANISOU 1756  O   MET A 246    10864  16236  13695   2524  -1058  -1068       O  
ATOM   1757  CB  MET A 246       2.084 -16.647  22.723  1.00110.67           C  
ANISOU 1757  CB  MET A 246    10477  17089  14482   2509  -1235  -1878       C  
ATOM   1758  CG  MET A 246       3.381 -17.420  22.848  1.00117.12           C  
ANISOU 1758  CG  MET A 246    11056  18077  15365   2750  -1499  -2167       C  
ATOM   1759  SD  MET A 246       4.803 -16.372  23.240  1.00124.46           S  
ANISOU 1759  SD  MET A 246    11558  19266  16466   2672  -1579  -2670       S  
ATOM   1760  CE  MET A 246       4.553 -16.116  24.993  1.00122.46           C  
ANISOU 1760  CE  MET A 246    11516  19051  15964   2864  -1846  -2656       C  
ATOM   1761  N   HIS A 247      -0.825 -15.792  21.689  1.00103.17           N  
ANISOU 1761  N   HIS A 247    10014  15741  13446   2100   -690  -1213       N  
ATOM   1762  CA  HIS A 247      -2.106 -15.110  21.882  1.00101.24           C  
ANISOU 1762  CA  HIS A 247     9989  15357  13120   1967   -524   -979       C  
ATOM   1763  C   HIS A 247      -3.273 -15.946  21.344  1.00103.23           C  
ANISOU 1763  C   HIS A 247    10454  15451  13317   1994   -448   -684       C  
ATOM   1764  O   HIS A 247      -4.382 -15.855  21.875  1.00101.77           O  
ANISOU 1764  O   HIS A 247    10486  15156  13025   1985   -396   -487       O  
ATOM   1765  CB  HIS A 247      -2.076 -13.716  21.226  1.00101.53           C  
ANISOU 1765  CB  HIS A 247     9912  15386  13281   1695   -280  -1060       C  
ATOM   1766  CG  HIS A 247      -3.208 -12.808  21.613  1.00103.63           C  
ANISOU 1766  CG  HIS A 247    10369  15534  13472   1580   -138   -885       C  
ATOM   1767  ND1 HIS A 247      -3.635 -11.795  20.772  1.00104.37           N  
ANISOU 1767  ND1 HIS A 247    10472  15542  13641   1369    108   -837       N  
ATOM   1768  CD2 HIS A 247      -3.950 -12.772  22.747  1.00105.18           C  
ANISOU 1768  CD2 HIS A 247    10758  15683  13522   1659   -208   -762       C  
ATOM   1769  CE1 HIS A 247      -4.622 -11.188  21.410  1.00102.96           C  
ANISOU 1769  CE1 HIS A 247    10469  15276  13377   1339    166   -693       C  
ATOM   1770  NE2 HIS A 247      -4.851 -11.744  22.600  1.00103.71           N  
ANISOU 1770  NE2 HIS A 247    10671  15392  13343   1497     -7   -647       N  
ATOM   1771  N   MET A 248      -3.020 -16.763  20.303  1.00 99.58           N  
ANISOU 1771  N   MET A 248     9920  14982  12936   2021   -434   -677       N  
ATOM   1772  CA  MET A 248      -4.023 -17.633  19.680  1.00 97.92           C  
ANISOU 1772  CA  MET A 248     9877  14635  12693   2040   -367   -440       C  
ATOM   1773  C   MET A 248      -4.262 -18.916  20.473  1.00102.60           C  
ANISOU 1773  C   MET A 248    10661  15170  13152   2264   -536   -334       C  
ATOM   1774  O   MET A 248      -5.384 -19.426  20.474  1.00101.08           O  
ANISOU 1774  O   MET A 248    10672  14841  12894   2260   -464   -122       O  
ATOM   1775  CB  MET A 248      -3.636 -17.978  18.236  1.00 99.84           C  
ANISOU 1775  CB  MET A 248     9981  14889  13065   1974   -276   -486       C  
ATOM   1776  CG  MET A 248      -3.879 -16.850  17.260  1.00102.49           C  
ANISOU 1776  CG  MET A 248    10258  15199  13486   1743    -50   -487       C  
ATOM   1777  SD  MET A 248      -3.715 -17.384  15.545  1.00106.11           S  
ANISOU 1777  SD  MET A 248    10647  15629  14040   1677     71   -483       S  
ATOM   1778  CE  MET A 248      -5.345 -18.015  15.261  1.00100.92           C  
ANISOU 1778  CE  MET A 248    10226  14821  13296   1700    106   -190       C  
ATOM   1779  N   LEU A 249      -3.210 -19.450  21.122  1.00101.32           N  
ANISOU 1779  N   LEU A 249    10442  15104  12952   2464   -755   -492       N  
ATOM   1780  CA  LEU A 249      -3.291 -20.681  21.909  1.00102.34           C  
ANISOU 1780  CA  LEU A 249    10794  15161  12928   2712   -928   -403       C  
ATOM   1781  C   LEU A 249      -3.220 -20.390  23.417  1.00107.97           C  
ANISOU 1781  C   LEU A 249    11659  15896  13467   2841  -1077   -428       C  
ATOM   1782  O   LEU A 249      -2.215 -20.679  24.076  1.00109.79           O  
ANISOU 1782  O   LEU A 249    11844  16232  13638   3055  -1314   -598       O  
ATOM   1783  CB  LEU A 249      -2.224 -21.703  21.459  1.00103.87           C  
ANISOU 1783  CB  LEU A 249    10864  15421  13182   2902  -1088   -543       C  
ATOM   1784  CG  LEU A 249      -2.320 -22.208  20.015  1.00107.32           C  
ANISOU 1784  CG  LEU A 249    11199  15816  13760   2803   -950   -506       C  
ATOM   1785  CD1 LEU A 249      -0.954 -22.577  19.477  1.00109.11           C  
ANISOU 1785  CD1 LEU A 249    11160  16181  14115   2909  -1066   -756       C  
ATOM   1786  CD2 LEU A 249      -3.277 -23.386  19.897  1.00109.05           C  
ANISOU 1786  CD2 LEU A 249    11692  15849  13894   2869   -907   -270       C  
ATOM   1787  N   GLN A 250      -4.301 -19.795  23.949  1.00103.66           N  
ANISOU 1787  N   GLN A 250    11293  15256  12838   2717   -940   -270       N  
ATOM   1788  CA  GLN A 250      -4.444 -19.438  25.364  1.00104.81           C  
ANISOU 1788  CA  GLN A 250    11625  15397  12801   2803  -1032   -265       C  
ATOM   1789  C   GLN A 250      -5.427 -20.379  26.058  1.00109.34           C  
ANISOU 1789  C   GLN A 250    12583  15778  13184   2906  -1003    -32       C  
ATOM   1790  O   GLN A 250      -6.398 -20.816  25.436  1.00107.42           O  
ANISOU 1790  O   GLN A 250    12429  15399  12988   2797   -821    142       O  
ATOM   1791  CB  GLN A 250      -4.916 -17.983  25.515  1.00105.00           C  
ANISOU 1791  CB  GLN A 250    11575  15448  12872   2575   -872   -282       C  
ATOM   1792  CG  GLN A 250      -3.840 -16.943  25.203  1.00118.98           C  
ANISOU 1792  CG  GLN A 250    13021  17397  14788   2480   -902   -547       C  
ATOM   1793  CD  GLN A 250      -3.356 -16.182  26.417  1.00138.45           C  
ANISOU 1793  CD  GLN A 250    15487  19964  17154   2529  -1032   -708       C  
ATOM   1794  OE1 GLN A 250      -3.270 -16.707  27.535  1.00135.47           O  
ANISOU 1794  OE1 GLN A 250    15315  19579  16580   2737  -1215   -694       O  
ATOM   1795  NE2 GLN A 250      -2.988 -14.927  26.211  1.00129.95           N  
ANISOU 1795  NE2 GLN A 250    14194  18979  16203   2340   -937   -877       N  
ATOM   1796  N   VAL A 251      -5.176 -20.681  27.347  1.00108.33           N  
ANISOU 1796  N   VAL A 251    12691  15634  12836   3113  -1175    -42       N  
ATOM   1797  CA  VAL A 251      -6.026 -21.558  28.166  1.00109.05           C  
ANISOU 1797  CA  VAL A 251    13203  15520  12710   3218  -1131    166       C  
ATOM   1798  C   VAL A 251      -7.358 -20.846  28.457  1.00111.73           C  
ANISOU 1798  C   VAL A 251    13666  15753  13035   2987   -870    313       C  
ATOM   1799  O   VAL A 251      -8.424 -21.440  28.279  1.00110.47           O  
ANISOU 1799  O   VAL A 251    13693  15417  12863   2906   -679    494       O  
ATOM   1800  CB  VAL A 251      -5.316 -22.034  29.467  1.00116.08           C  
ANISOU 1800  CB  VAL A 251    14350  16419  13338   3528  -1399    106       C  
ATOM   1801  CG1 VAL A 251      -6.180 -23.028  30.242  1.00116.97           C  
ANISOU 1801  CG1 VAL A 251    14953  16280  13209   3632  -1316    333       C  
ATOM   1802  CG2 VAL A 251      -3.950 -22.644  29.166  1.00117.66           C  
ANISOU 1802  CG2 VAL A 251    14374  16753  13577   3777  -1683    -83       C  
ATOM   1803  N   ASP A 252      -7.283 -19.569  28.878  1.00108.37           N  
ANISOU 1803  N   ASP A 252    13115  15435  12626   2879   -857    214       N  
ATOM   1804  CA  ASP A 252      -8.442 -18.734  29.184  1.00107.08           C  
ANISOU 1804  CA  ASP A 252    13030  15193  12463   2675   -626    316       C  
ATOM   1805  C   ASP A 252      -9.140 -18.301  27.879  1.00108.43           C  
ANISOU 1805  C   ASP A 252    12975  15350  12872   2442   -413    370       C  
ATOM   1806  O   ASP A 252      -8.469 -17.775  26.985  1.00107.15           O  
ANISOU 1806  O   ASP A 252    12522  15314  12877   2377   -446    248       O  
ATOM   1807  CB  ASP A 252      -8.015 -17.514  30.016  1.00109.81           C  
ANISOU 1807  CB  ASP A 252    13311  15660  12751   2652   -697    170       C  
ATOM   1808  CG  ASP A 252      -9.166 -16.797  30.686  1.00119.94           C  
ANISOU 1808  CG  ASP A 252    14759  16842  13969   2505   -490    273       C  
ATOM   1809  OD1 ASP A 252      -9.624 -17.273  31.747  1.00121.93           O  
ANISOU 1809  OD1 ASP A 252    15349  16977  14000   2598   -478    368       O  
ATOM   1810  OD2 ASP A 252      -9.593 -15.747  30.164  1.00124.56           O  
ANISOU 1810  OD2 ASP A 252    15153  17458  14716   2304   -334    253       O  
ATOM   1811  N   PRO A 253     -10.470 -18.532  27.731  1.00104.06           N  
ANISOU 1811  N   PRO A 253    12556  14646  12337   2322   -194    536       N  
ATOM   1812  CA  PRO A 253     -11.147 -18.142  26.478  1.00101.83           C  
ANISOU 1812  CA  PRO A 253    12065  14359  12265   2138    -29    574       C  
ATOM   1813  C   PRO A 253     -11.307 -16.634  26.276  1.00104.70           C  
ANISOU 1813  C   PRO A 253    12248  14801  12733   1984     57    507       C  
ATOM   1814  O   PRO A 253     -11.464 -16.192  25.137  1.00102.90           O  
ANISOU 1814  O   PRO A 253    11828  14602  12666   1874    134    498       O  
ATOM   1815  CB  PRO A 253     -12.496 -18.859  26.561  1.00103.33           C  
ANISOU 1815  CB  PRO A 253    12449  14377  12435   2075    158    730       C  
ATOM   1816  CG  PRO A 253     -12.747 -19.024  28.009  1.00109.42           C  
ANISOU 1816  CG  PRO A 253    13523  15059  12994   2146    172    774       C  
ATOM   1817  CD  PRO A 253     -11.411 -19.162  28.681  1.00106.60           C  
ANISOU 1817  CD  PRO A 253    13223  14793  12489   2348    -81    677       C  
ATOM   1818  N   LEU A 254     -11.269 -15.852  27.373  1.00102.14           N  
ANISOU 1818  N   LEU A 254    12011  14497  12301   1984     48    460       N  
ATOM   1819  CA  LEU A 254     -11.390 -14.392  27.347  1.00101.32           C  
ANISOU 1819  CA  LEU A 254    11774  14447  12276   1848    134    388       C  
ATOM   1820  C   LEU A 254     -10.052 -13.711  27.047  1.00105.36           C  
ANISOU 1820  C   LEU A 254    12069  15110  12852   1848      7    199       C  
ATOM   1821  O   LEU A 254     -10.036 -12.647  26.427  1.00104.11           O  
ANISOU 1821  O   LEU A 254    11754  14983  12820   1711    106    141       O  
ATOM   1822  CB  LEU A 254     -11.981 -13.871  28.667  1.00102.27           C  
ANISOU 1822  CB  LEU A 254    12092  14511  12255   1836    202    411       C  
ATOM   1823  CG  LEU A 254     -13.500 -13.689  28.709  1.00106.23           C  
ANISOU 1823  CG  LEU A 254    12684  14884  12795   1723    431    538       C  
ATOM   1824  CD1 LEU A 254     -14.214 -15.011  28.940  1.00106.82           C  
ANISOU 1824  CD1 LEU A 254    12962  14830  12793   1772    493    665       C  
ATOM   1825  CD2 LEU A 254     -13.893 -12.720  29.802  1.00109.62           C  
ANISOU 1825  CD2 LEU A 254    13221  15293  13136   1673    513    508       C  
ATOM   1826  N   LYS A 255      -8.936 -14.330  27.482  1.00103.25           N  
ANISOU 1826  N   LYS A 255    11799  14931  12501   2006   -205     89       N  
ATOM   1827  CA  LYS A 255      -7.575 -13.830  27.260  1.00103.94           C  
ANISOU 1827  CA  LYS A 255    11649  15180  12663   2016   -339   -138       C  
ATOM   1828  C   LYS A 255      -7.079 -14.160  25.845  1.00106.91           C  
ANISOU 1828  C   LYS A 255    11810  15597  13214   1973   -320   -176       C  
ATOM   1829  O   LYS A 255      -6.132 -13.532  25.365  1.00106.99           O  
ANISOU 1829  O   LYS A 255    11591  15718  13341   1903   -335   -364       O  
ATOM   1830  CB  LYS A 255      -6.608 -14.394  28.316  1.00108.81           C  
ANISOU 1830  CB  LYS A 255    12335  15887  13120   2233   -600   -266       C  
ATOM   1831  N   ARG A 256      -7.728 -15.143  25.184  1.00102.29           N  
ANISOU 1831  N   ARG A 256    11304  14914  12646   2002   -269    -11       N  
ATOM   1832  CA  ARG A 256      -7.421 -15.615  23.831  1.00101.18           C  
ANISOU 1832  CA  ARG A 256    11006  14790  12646   1972   -242    -19       C  
ATOM   1833  C   ARG A 256      -7.714 -14.549  22.771  1.00104.19           C  
ANISOU 1833  C   ARG A 256    11250  15164  13173   1771    -55    -24       C  
ATOM   1834  O   ARG A 256      -8.573 -13.689  22.979  1.00103.05           O  
ANISOU 1834  O   ARG A 256    11179  14955  13022   1669     77     51       O  
ATOM   1835  CB  ARG A 256      -8.229 -16.887  23.531  1.00 99.76           C  
ANISOU 1835  CB  ARG A 256    10984  14489  12430   2042   -218    163       C  
ATOM   1836  CG  ARG A 256      -7.529 -17.872  22.601  1.00106.21           C  
ANISOU 1836  CG  ARG A 256    11694  15339  13322   2120   -298    120       C  
ATOM   1837  CD  ARG A 256      -8.328 -19.151  22.427  1.00109.97           C  
ANISOU 1837  CD  ARG A 256    12351  15680  13753   2185   -268    288       C  
ATOM   1838  NE  ARG A 256      -8.417 -19.914  23.675  1.00114.37           N  
ANISOU 1838  NE  ARG A 256    13163  16163  14129   2347   -365    347       N  
ATOM   1839  CZ  ARG A 256      -9.254 -20.926  23.882  1.00124.77           C  
ANISOU 1839  CZ  ARG A 256    14713  17325  15370   2386   -300    499       C  
ATOM   1840  NH1 ARG A 256     -10.088 -21.316  22.926  1.00109.43           N  
ANISOU 1840  NH1 ARG A 256    12742  15305  13534   2274   -156    589       N  
ATOM   1841  NH2 ARG A 256      -9.266 -21.554  25.050  1.00111.50           N  
ANISOU 1841  NH2 ARG A 256    13307  15558  13499   2535   -372    551       N  
ATOM   1842  N   ALA A 257      -6.999 -14.622  21.631  1.00101.02           N  
ANISOU 1842  N   ALA A 257    10672  14817  12893   1727    -37   -115       N  
ATOM   1843  CA  ALA A 257      -7.143 -13.712  20.491  1.00100.13           C  
ANISOU 1843  CA  ALA A 257    10469  14682  12896   1555    142   -122       C  
ATOM   1844  C   ALA A 257      -8.493 -13.893  19.792  1.00102.91           C  
ANISOU 1844  C   ALA A 257    10939  14911  13251   1517    259     85       C  
ATOM   1845  O   ALA A 257      -9.086 -14.971  19.870  1.00102.17           O  
ANISOU 1845  O   ALA A 257    10938  14767  13115   1607    208    201       O  
ATOM   1846  CB  ALA A 257      -6.014 -13.948  19.499  1.00101.44           C  
ANISOU 1846  CB  ALA A 257    10447  14927  13169   1532    134   -274       C  
ATOM   1847  N   THR A 258      -8.982 -12.833  19.124  1.00 99.11           N  
ANISOU 1847  N   THR A 258    10462  14378  12819   1391    415    117       N  
ATOM   1848  CA  THR A 258     -10.243 -12.851  18.373  1.00 97.93           C  
ANISOU 1848  CA  THR A 258    10398  14130  12680   1370    507    278       C  
ATOM   1849  C   THR A 258      -9.980 -12.519  16.900  1.00102.01           C  
ANISOU 1849  C   THR A 258    10865  14632  13261   1298    599    259       C  
ATOM   1850  O   THR A 258      -8.851 -12.171  16.548  1.00102.34           O  
ANISOU 1850  O   THR A 258    10812  14728  13346   1237    629    119       O  
ATOM   1851  CB  THR A 258     -11.295 -11.918  19.005  1.00105.69           C  
ANISOU 1851  CB  THR A 258    11483  15043  13633   1334    591    354       C  
ATOM   1852  OG1 THR A 258     -10.787 -10.585  19.057  1.00105.88           O  
ANISOU 1852  OG1 THR A 258    11485  15068  13675   1237    679    261       O  
ATOM   1853  CG2 THR A 258     -11.749 -12.380  20.386  1.00104.61           C  
ANISOU 1853  CG2 THR A 258    11436  14897  13415   1402    528    395       C  
ATOM   1854  N   ILE A 259     -11.022 -12.622  16.044  1.00 98.11           N  
ANISOU 1854  N   ILE A 259    10439  14067  12771   1305    648    382       N  
ATOM   1855  CA  ILE A 259     -10.965 -12.319  14.604  1.00 98.02           C  
ANISOU 1855  CA  ILE A 259    10440  14023  12782   1260    732    390       C  
ATOM   1856  C   ILE A 259     -10.451 -10.895  14.328  1.00102.74           C  
ANISOU 1856  C   ILE A 259    11072  14583  13383   1152    873    320       C  
ATOM   1857  O   ILE A 259      -9.753 -10.679  13.336  1.00102.74           O  
ANISOU 1857  O   ILE A 259    11067  14572  13397   1086    960    258       O  
ATOM   1858  CB  ILE A 259     -12.312 -12.606  13.879  1.00100.55           C  
ANISOU 1858  CB  ILE A 259    10835  14280  13089   1314    727    521       C  
ATOM   1859  N   LYS A 260     -10.777  -9.944  15.229  1.00 99.72           N  
ANISOU 1859  N   LYS A 260    10738  14167  12983   1124    914    321       N  
ATOM   1860  CA  LYS A 260     -10.357  -8.544  15.163  1.00100.45           C  
ANISOU 1860  CA  LYS A 260    10887  14202  13079   1014   1064    250       C  
ATOM   1861  C   LYS A 260      -8.895  -8.392  15.606  1.00105.48           C  
ANISOU 1861  C   LYS A 260    11389  14924  13765    919   1081     51       C  
ATOM   1862  O   LYS A 260      -8.186  -7.542  15.064  1.00106.03           O  
ANISOU 1862  O   LYS A 260    11471  14953  13863    792   1237    -53       O  
ATOM   1863  CB  LYS A 260     -11.277  -7.672  16.032  1.00102.94           C  
ANISOU 1863  CB  LYS A 260    11294  14453  13365   1028   1093    313       C  
ATOM   1864  N   ASP A 261      -8.452  -9.210  16.591  1.00102.26           N  
ANISOU 1864  N   ASP A 261    10862  14629  13363    984    925    -17       N  
ATOM   1865  CA  ASP A 261      -7.085  -9.198  17.124  1.00103.47           C  
ANISOU 1865  CA  ASP A 261    10852  14895  13565    936    885   -237       C  
ATOM   1866  C   ASP A 261      -6.052  -9.649  16.090  1.00108.01           C  
ANISOU 1866  C   ASP A 261    11304  15521  14215    889    924   -360       C  
ATOM   1867  O   ASP A 261      -4.991  -9.030  15.988  1.00108.92           O  
ANISOU 1867  O   ASP A 261    11307  15676  14402    764   1023   -564       O  
ATOM   1868  CB  ASP A 261      -6.973 -10.058  18.398  1.00105.48           C  
ANISOU 1868  CB  ASP A 261    11056  15248  13776   1070    676   -259       C  
ATOM   1869  CG  ASP A 261      -7.700  -9.516  19.615  1.00115.66           C  
ANISOU 1869  CG  ASP A 261    12453  16504  14990   1092    656   -198       C  
ATOM   1870  OD1 ASP A 261      -7.516  -8.320  19.936  1.00116.96           O  
ANISOU 1870  OD1 ASP A 261    12624  16647  15169    983    760   -286       O  
ATOM   1871  OD2 ASP A 261      -8.385 -10.308  20.296  1.00120.96           O  
ANISOU 1871  OD2 ASP A 261    13205  17167  15587   1212    547    -81       O  
ATOM   1872  N   ILE A 262      -6.363 -10.723  15.329  1.00103.85           N  
ANISOU 1872  N   ILE A 262    10791  14990  13679    978    862   -255       N  
ATOM   1873  CA  ILE A 262      -5.485 -11.279  14.291  1.00104.31           C  
ANISOU 1873  CA  ILE A 262    10744  15089  13800    947    900   -358       C  
ATOM   1874  C   ILE A 262      -5.361 -10.306  13.107  1.00109.21           C  
ANISOU 1874  C   ILE A 262    11455  15608  14432    789   1142   -374       C  
ATOM   1875  O   ILE A 262      -4.254 -10.095  12.618  1.00110.09           O  
ANISOU 1875  O   ILE A 262    11455  15755  14620    675   1259   -563       O  
ATOM   1876  CB  ILE A 262      -5.889 -12.723  13.856  1.00106.41           C  
ANISOU 1876  CB  ILE A 262    11018  15368  14045   1086    769   -243       C  
ATOM   1877  CG1 ILE A 262      -6.200 -13.624  15.075  1.00106.42           C  
ANISOU 1877  CG1 ILE A 262    11015  15419  14003   1243    562   -189       C  
ATOM   1878  CG2 ILE A 262      -4.796 -13.362  12.983  1.00108.03           C  
ANISOU 1878  CG2 ILE A 262    11081  15638  14326   1068    790   -391       C  
ATOM   1879  CD1 ILE A 262      -7.278 -14.687  14.839  1.00112.25           C  
ANISOU 1879  CD1 ILE A 262    11862  16096  14692   1348    491      0       C  
ATOM   1880  N   ARG A 263      -6.484  -9.687  12.681  1.00105.46           N  
ANISOU 1880  N   ARG A 263    11191  15002  13878    789   1224   -190       N  
ATOM   1881  CA  ARG A 263      -6.521  -8.710  11.582  1.00106.18           C  
ANISOU 1881  CA  ARG A 263    11448  14960  13935    674   1448   -170       C  
ATOM   1882  C   ARG A 263      -5.706  -7.445  11.891  1.00111.91           C  
ANISOU 1882  C   ARG A 263    12167  15647  14707    496   1641   -339       C  
ATOM   1883  O   ARG A 263      -5.174  -6.823  10.969  1.00112.70           O  
ANISOU 1883  O   ARG A 263    12354  15657  14809    358   1864   -410       O  
ATOM   1884  CB  ARG A 263      -7.969  -8.348  11.217  1.00105.81           C  
ANISOU 1884  CB  ARG A 263    11626  14792  13786    764   1442     54       C  
ATOM   1885  N   GLU A 264      -5.600  -7.083  13.186  1.00108.85           N  
ANISOU 1885  N   GLU A 264    11687  15320  14352    492   1567   -414       N  
ATOM   1886  CA  GLU A 264      -4.851  -5.923  13.679  1.00110.34           C  
ANISOU 1886  CA  GLU A 264    11839  15488  14596    321   1726   -602       C  
ATOM   1887  C   GLU A 264      -3.356  -6.223  13.894  1.00115.73           C  
ANISOU 1887  C   GLU A 264    12244  16320  15407    224   1728   -900       C  
ATOM   1888  O   GLU A 264      -2.570  -5.287  14.065  1.00116.97           O  
ANISOU 1888  O   GLU A 264    12342  16464  15637     44   1900  -1109       O  
ATOM   1889  CB  GLU A 264      -5.486  -5.384  14.971  1.00111.31           C  
ANISOU 1889  CB  GLU A 264    11997  15611  14685    369   1638   -555       C  
ATOM   1890  CG  GLU A 264      -6.677  -4.471  14.730  1.00122.06           C  
ANISOU 1890  CG  GLU A 264    13626  16793  15960    385   1748   -359       C  
ATOM   1891  CD  GLU A 264      -7.414  -4.004  15.971  1.00144.26           C  
ANISOU 1891  CD  GLU A 264    16476  19599  18738    444   1667   -303       C  
ATOM   1892  OE1 GLU A 264      -6.749  -3.584  16.946  1.00141.14           O  
ANISOU 1892  OE1 GLU A 264    15968  19273  18386    365   1662   -475       O  
ATOM   1893  OE2 GLU A 264      -8.666  -4.019  15.950  1.00138.07           O  
ANISOU 1893  OE2 GLU A 264    15832  18742  17887    566   1616   -103       O  
ATOM   1894  N   HIS A 265      -2.970  -7.517  13.882  1.00111.96           N  
ANISOU 1894  N   HIS A 265    11594  15982  14965    347   1539   -938       N  
ATOM   1895  CA  HIS A 265      -1.591  -7.978  14.080  1.00113.44           C  
ANISOU 1895  CA  HIS A 265    11489  16333  15279    310   1490  -1230       C  
ATOM   1896  C   HIS A 265      -0.679  -7.602  12.907  1.00119.11           C  
ANISOU 1896  C   HIS A 265    12160  17007  16088    111   1763  -1406       C  
ATOM   1897  O   HIS A 265      -1.106  -7.658  11.753  1.00118.08           O  
ANISOU 1897  O   HIS A 265    12216  16753  15897     86   1901  -1255       O  
ATOM   1898  CB  HIS A 265      -1.560  -9.491  14.333  1.00113.37           C  
ANISOU 1898  CB  HIS A 265    11361  16452  15264    528   1213  -1188       C  
ATOM   1899  CG  HIS A 265      -0.289  -9.973  14.951  1.00118.48           C  
ANISOU 1899  CG  HIS A 265    11708  17288  16021    570   1070  -1483       C  
ATOM   1900  ND1 HIS A 265       0.783 -10.366  14.176  1.00121.65           N  
ANISOU 1900  ND1 HIS A 265    11910  17764  16547    510   1143  -1700       N  
ATOM   1901  CD2 HIS A 265       0.034 -10.122  16.257  1.00120.90           C  
ANISOU 1901  CD2 HIS A 265    11890  17722  16323    683    850  -1601       C  
ATOM   1902  CE1 HIS A 265       1.725 -10.733  15.029  1.00122.63           C  
ANISOU 1902  CE1 HIS A 265    11772  18067  16753    598    953  -1954       C  
ATOM   1903  NE2 HIS A 265       1.320 -10.605  16.292  1.00122.62           N  
ANISOU 1903  NE2 HIS A 265    11819  18105  16668    711    762  -1901       N  
ATOM   1904  N   GLU A 266       0.578  -7.222  13.219  1.00118.09           N  
ANISOU 1904  N   GLU A 266    11783  16983  16104    -32   1843  -1744       N  
ATOM   1905  CA  GLU A 266       1.602  -6.787  12.262  1.00120.11           C  
ANISOU 1905  CA  GLU A 266    11953  17207  16477   -262   2142  -1983       C  
ATOM   1906  C   GLU A 266       2.033  -7.859  11.255  1.00124.32           C  
ANISOU 1906  C   GLU A 266    12397  17789  17050   -211   2139  -2009       C  
ATOM   1907  O   GLU A 266       2.224  -7.535  10.082  1.00124.66           O  
ANISOU 1907  O   GLU A 266    12567  17707  17091   -369   2424  -2019       O  
ATOM   1908  CB  GLU A 266       2.825  -6.221  12.998  1.00124.07           C  
ANISOU 1908  CB  GLU A 266    12149  17842  17149   -416   2193  -2382       C  
ATOM   1909  N   TRP A 267       2.203  -9.117  11.709  1.00120.58           N  
ANISOU 1909  N   TRP A 267    11731  17482  16602     12   1830  -2024       N  
ATOM   1910  CA  TRP A 267       2.616 -10.242  10.862  1.00120.66           C  
ANISOU 1910  CA  TRP A 267    11641  17548  16657     90   1795  -2058       C  
ATOM   1911  C   TRP A 267       1.518 -10.653   9.874  1.00122.86           C  
ANISOU 1911  C   TRP A 267    12226  17674  16782    158   1831  -1720       C  
ATOM   1912  O   TRP A 267       1.824 -11.006   8.734  1.00122.93           O  
ANISOU 1912  O   TRP A 267    12261  17642  16806     98   1982  -1746       O  
ATOM   1913  CB  TRP A 267       3.054 -11.439  11.724  1.00119.50           C  
ANISOU 1913  CB  TRP A 267    11240  17601  16565    335   1443  -2160       C  
ATOM   1914  CG  TRP A 267       3.571 -12.610  10.940  1.00120.81           C  
ANISOU 1914  CG  TRP A 267    11280  17829  16794    428   1398  -2227       C  
ATOM   1915  CD1 TRP A 267       4.822 -12.761  10.419  1.00126.06           C  
ANISOU 1915  CD1 TRP A 267    11672  18592  17632    331   1519  -2556       C  
ATOM   1916  CD2 TRP A 267       2.849 -13.802  10.604  1.00118.79           C  
ANISOU 1916  CD2 TRP A 267    11158  17538  16438    631   1230  -1976       C  
ATOM   1917  NE1 TRP A 267       4.923 -13.970   9.773  1.00125.16           N  
ANISOU 1917  NE1 TRP A 267    11523  18505  17526    473   1431  -2515       N  
ATOM   1918  CE2 TRP A 267       3.725 -14.630   9.868  1.00123.97           C  
ANISOU 1918  CE2 TRP A 267    11627  18270  17207    655   1254  -2159       C  
ATOM   1919  CE3 TRP A 267       1.540 -14.252  10.849  1.00117.60           C  
ANISOU 1919  CE3 TRP A 267    11259  17298  16126    783   1077  -1634       C  
ATOM   1920  CZ2 TRP A 267       3.340 -15.885   9.383  1.00122.13           C  
ANISOU 1920  CZ2 TRP A 267    11468  18017  16920    830   1123  -2000       C  
ATOM   1921  CZ3 TRP A 267       1.157 -15.494  10.365  1.00118.02           C  
ANISOU 1921  CZ3 TRP A 267    11373  17334  16134    941    957  -1489       C  
ATOM   1922  CH2 TRP A 267       2.051 -16.296   9.642  1.00119.88           C  
ANISOU 1922  CH2 TRP A 267    11437  17638  16474    966    977  -1665       C  
ATOM   1923  N   PHE A 268       0.251 -10.607  10.317  1.00117.66           N  
ANISOU 1923  N   PHE A 268    11786  16938  15981    283   1694  -1427       N  
ATOM   1924  CA  PHE A 268      -0.921 -10.963   9.519  1.00115.84           C  
ANISOU 1924  CA  PHE A 268    11826  16581  15608    368   1687  -1122       C  
ATOM   1925  C   PHE A 268      -1.288  -9.872   8.504  1.00120.86           C  
ANISOU 1925  C   PHE A 268    12737  17026  16159    204   1983  -1034       C  
ATOM   1926  O   PHE A 268      -1.779 -10.201   7.423  1.00119.85           O  
ANISOU 1926  O   PHE A 268    12788  16810  15939    233   2041   -889       O  
ATOM   1927  CB  PHE A 268      -2.107 -11.282  10.444  1.00115.64           C  
ANISOU 1927  CB  PHE A 268    11898  16552  15486    551   1446   -889       C  
ATOM   1928  CG  PHE A 268      -3.350 -11.829   9.782  1.00115.38           C  
ANISOU 1928  CG  PHE A 268    12079  16428  15335    665   1385   -614       C  
ATOM   1929  CD1 PHE A 268      -3.470 -13.185   9.504  1.00117.72           C  
ANISOU 1929  CD1 PHE A 268    12318  16778  15630    804   1228   -561       C  
ATOM   1930  CD2 PHE A 268      -4.423 -10.997   9.486  1.00116.74           C  
ANISOU 1930  CD2 PHE A 268    12498  16459  15398    646   1470   -424       C  
ATOM   1931  CE1 PHE A 268      -4.631 -13.694   8.914  1.00117.23           C  
ANISOU 1931  CE1 PHE A 268    12429  16640  15472    896   1170   -340       C  
ATOM   1932  CE2 PHE A 268      -5.583 -11.507   8.898  1.00118.22           C  
ANISOU 1932  CE2 PHE A 268    12846  16584  15489    763   1389   -208       C  
ATOM   1933  CZ  PHE A 268      -5.675 -12.850   8.606  1.00115.66           C  
ANISOU 1933  CZ  PHE A 268    12447  16323  15175    875   1245   -175       C  
ATOM   1934  N   LYS A 269      -1.057  -8.584   8.854  1.00119.30           N  
ANISOU 1934  N   LYS A 269    12593  16756  15978     41   2166  -1123       N  
ATOM   1935  CA  LYS A 269      -1.351  -7.418   8.008  1.00120.35           C  
ANISOU 1935  CA  LYS A 269    13032  16678  16017   -112   2466  -1045       C  
ATOM   1936  C   LYS A 269      -0.566  -7.420   6.692  1.00127.02           C  
ANISOU 1936  C   LYS A 269    13935  17451  16875   -268   2743  -1166       C  
ATOM   1937  O   LYS A 269      -1.110  -7.018   5.662  1.00126.74           O  
ANISOU 1937  O   LYS A 269    14227  17236  16692   -290   2907  -1002       O  
ATOM   1938  CB  LYS A 269      -1.117  -6.109   8.774  1.00124.03           C  
ANISOU 1938  CB  LYS A 269    13518  17084  16524   -265   2614  -1158       C  
ATOM   1939  N   GLN A 270       0.704  -7.870   6.731  1.00125.97           N  
ANISOU 1939  N   GLN A 270    13491  17459  16913   -366   2792  -1462       N  
ATOM   1940  CA  GLN A 270       1.581  -7.972   5.558  1.00128.10           C  
ANISOU 1940  CA  GLN A 270    13763  17684  17227   -529   3070  -1626       C  
ATOM   1941  C   GLN A 270       1.127  -9.146   4.692  1.00131.77           C  
ANISOU 1941  C   GLN A 270    14301  18163  17601   -361   2935  -1458       C  
ATOM   1942  O   GLN A 270       0.633 -10.136   5.233  1.00129.46           O  
ANISOU 1942  O   GLN A 270    13887  17993  17308   -142   2608  -1347       O  
ATOM   1943  CB  GLN A 270       3.043  -8.182   5.986  1.00131.53           C  
ANISOU 1943  CB  GLN A 270    13779  18297  17900   -657   3123  -2028       C  
ATOM   1944  CG  GLN A 270       3.685  -6.978   6.665  1.00148.42           C  
ANISOU 1944  CG  GLN A 270    15819  20421  20152   -878   3317  -2270       C  
ATOM   1945  CD  GLN A 270       5.092  -7.283   7.113  1.00169.76           C  
ANISOU 1945  CD  GLN A 270    18060  23336  23106   -972   3317  -2697       C  
ATOM   1946  OE1 GLN A 270       6.068  -7.010   6.407  1.00167.86           O  
ANISOU 1946  OE1 GLN A 270    17725  23070  22986  -1205   3639  -2970       O  
ATOM   1947  NE2 GLN A 270       5.229  -7.863   8.297  1.00161.10           N  
ANISOU 1947  NE2 GLN A 270    16671  22451  22089   -784   2958  -2779       N  
ATOM   1948  N   GLY A 271       1.277  -9.026   3.351  1.00130.43           N  
ANISOU 1948  N   GLY A 271    14358  17857  17344   -469   3199  -1440       N  
ATOM   1949  CA  GLY A 271       0.906 -10.031   2.333  1.00129.93           C  
ANISOU 1949  CA  GLY A 271    14405  17784  17178   -344   3126  -1304       C  
ATOM   1950  C   GLY A 271      -0.623 -10.306   2.261  1.00132.21           C  
ANISOU 1950  C   GLY A 271    14947  18013  17276   -116   2879   -955       C  
ATOM   1951  O   GLY A 271      -1.056 -11.177   1.500  1.00131.02           O  
ANISOU 1951  O   GLY A 271    14882  17863  17036      3   2782   -839       O  
ATOM   1952  N   LEU A 272      -1.434  -9.534   3.016  1.00128.48           N  
ANISOU 1952  N   LEU A 272    14587  17485  16745    -64   2792   -810       N  
ATOM   1953  CA  LEU A 272      -2.890  -9.675   3.051  1.00126.68           C  
ANISOU 1953  CA  LEU A 272    14559  17208  16365    141   2570   -520       C  
ATOM   1954  C   LEU A 272      -3.548  -9.032   1.818  1.00132.14           C  
ANISOU 1954  C   LEU A 272    15675  17695  16838    144   2733   -353       C  
ATOM   1955  O   LEU A 272      -3.383  -7.827   1.603  1.00133.25           O  
ANISOU 1955  O   LEU A 272    16045  17673  16912     11   2988   -366       O  
ATOM   1956  CB  LEU A 272      -3.466  -9.088   4.358  1.00125.69           C  
ANISOU 1956  CB  LEU A 272    14382  17102  16270    195   2431   -455       C  
ATOM   1957  CG  LEU A 272      -4.956  -9.327   4.625  1.00128.41           C  
ANISOU 1957  CG  LEU A 272    14845  17435  16510    409   2180   -201       C  
ATOM   1958  CD1 LEU A 272      -5.182 -10.636   5.359  1.00126.92           C  
ANISOU 1958  CD1 LEU A 272    14396  17418  16410    554   1890   -191       C  
ATOM   1959  CD2 LEU A 272      -5.550  -8.187   5.424  1.00130.74           C  
ANISOU 1959  CD2 LEU A 272    15256  17646  16772    406   2198   -124       C  
ATOM   1960  N   PRO A 273      -4.305  -9.810   1.006  1.00128.54           N  
ANISOU 1960  N   PRO A 273    15346  17236  16258    302   2588   -202       N  
ATOM   1961  CA  PRO A 273      -4.960  -9.223  -0.175  1.00129.69           C  
ANISOU 1961  CA  PRO A 273    15914  17194  16167    344   2704    -47       C  
ATOM   1962  C   PRO A 273      -6.198  -8.399   0.184  1.00133.89           C  
ANISOU 1962  C   PRO A 273    16659  17631  16581    486   2586    149       C  
ATOM   1963  O   PRO A 273      -6.734  -8.532   1.287  1.00131.83           O  
ANISOU 1963  O   PRO A 273    16201  17469  16420    572   2377    189       O  
ATOM   1964  CB  PRO A 273      -5.310 -10.442  -1.041  1.00130.76           C  
ANISOU 1964  CB  PRO A 273    16049  17398  16236    474   2547      8       C  
ATOM   1965  CG  PRO A 273      -4.740 -11.645  -0.325  1.00133.82           C  
ANISOU 1965  CG  PRO A 273    16020  17989  16835    482   2385   -122       C  
ATOM   1966  CD  PRO A 273      -4.599 -11.251   1.104  1.00128.52           C  
ANISOU 1966  CD  PRO A 273    15128  17390  16313    454   2315   -174       C  
ATOM   1967  N   SER A 274      -6.646  -7.546  -0.753  1.00132.73           N  
ANISOU 1967  N   SER A 274    16933  17284  16216    520   2725    267       N  
ATOM   1968  CA  SER A 274      -7.792  -6.649  -0.582  1.00132.92           C  
ANISOU 1968  CA  SER A 274    17207  17189  16106    675   2635    442       C  
ATOM   1969  C   SER A 274      -9.160  -7.343  -0.586  1.00136.10           C  
ANISOU 1969  C   SER A 274    17566  17688  16457    941   2278    589       C  
ATOM   1970  O   SER A 274     -10.074  -6.870   0.092  1.00134.89           O  
ANISOU 1970  O   SER A 274    17417  17527  16308   1066   2134    681       O  
ATOM   1971  CB  SER A 274      -7.763  -5.544  -1.635  1.00139.08           C  
ANISOU 1971  CB  SER A 274    18488  17707  16650    648   2900    512       C  
ATOM   1972  OG  SER A 274      -6.557  -4.800  -1.579  1.00149.51           O  
ANISOU 1972  OG  SER A 274    19859  18916  18031    374   3269    360       O  
ATOM   1973  N   TYR A 275      -9.305  -8.443  -1.353  1.00133.16           N  
ANISOU 1973  N   TYR A 275    17146  17404  16045   1020   2150    591       N  
ATOM   1974  CA  TYR A 275     -10.566  -9.183  -1.496  1.00132.30           C  
ANISOU 1974  CA  TYR A 275    16985  17390  15894   1250   1831    691       C  
ATOM   1975  C   TYR A 275     -10.921 -10.092  -0.302  1.00134.81           C  
ANISOU 1975  C   TYR A 275    16897  17897  16426   1282   1605    661       C  
ATOM   1976  O   TYR A 275     -12.054 -10.577  -0.231  1.00133.53           O  
ANISOU 1976  O   TYR A 275    16672  17804  16258   1450   1365    728       O  
ATOM   1977  CB  TYR A 275     -10.579  -9.985  -2.818  1.00134.32           C  
ANISOU 1977  CB  TYR A 275    17371  17653  16011   1311   1796    691       C  
ATOM   1978  CG  TYR A 275      -9.702 -11.221  -2.833  1.00135.28           C  
ANISOU 1978  CG  TYR A 275    17210  17911  16279   1192   1813    561       C  
ATOM   1979  CD1 TYR A 275     -10.228 -12.477  -2.545  1.00135.62           C  
ANISOU 1979  CD1 TYR A 275    16983  18114  16430   1286   1561    551       C  
ATOM   1980  CD2 TYR A 275      -8.358 -11.143  -3.188  1.00137.21           C  
ANISOU 1980  CD2 TYR A 275    17469  18111  16553    990   2093    436       C  
ATOM   1981  CE1 TYR A 275      -9.429 -13.620  -2.568  1.00135.80           C  
ANISOU 1981  CE1 TYR A 275    16775  18243  16580   1201   1572    436       C  
ATOM   1982  CE2 TYR A 275      -7.552 -12.280  -3.224  1.00137.60           C  
ANISOU 1982  CE2 TYR A 275    17254  18287  16742    907   2097    303       C  
ATOM   1983  CZ  TYR A 275      -8.091 -13.517  -2.908  1.00143.23           C  
ANISOU 1983  CZ  TYR A 275    17720  19149  17550   1024   1829    312       C  
ATOM   1984  OH  TYR A 275      -7.302 -14.641  -2.938  1.00143.78           O  
ANISOU 1984  OH  TYR A 275    17552  19326  17752    964   1830    185       O  
ATOM   1985  N   LEU A 276      -9.964 -10.334   0.612  1.00131.44           N  
ANISOU 1985  N   LEU A 276    16208  17550  16182   1126   1684    548       N  
ATOM   1986  CA  LEU A 276     -10.136 -11.217   1.768  1.00129.86           C  
ANISOU 1986  CA  LEU A 276    15672  17508  16162   1152   1496    517       C  
ATOM   1987  C   LEU A 276     -11.142 -10.715   2.810  1.00134.16           C  
ANISOU 1987  C   LEU A 276    16175  18058  16743   1243   1367    600       C  
ATOM   1988  O   LEU A 276     -12.045 -11.471   3.176  1.00132.59           O  
ANISOU 1988  O   LEU A 276    15844  17943  16590   1357   1164    644       O  
ATOM   1989  CB  LEU A 276      -8.779 -11.521   2.414  1.00129.81           C  
ANISOU 1989  CB  LEU A 276    15430  17579  16312    990   1604    359       C  
ATOM   1990  CG  LEU A 276      -7.790 -12.317   1.562  1.00133.90           C  
ANISOU 1990  CG  LEU A 276    15731  18222  16923    999   1509    277       C  
ATOM   1991  CD1 LEU A 276      -6.425 -12.439   2.234  1.00135.14           C  
ANISOU 1991  CD1 LEU A 276    16036  18335  16977    981   1606    254       C  
ATOM   1992  CD2 LEU A 276      -8.328 -13.686   1.278  1.00136.51           C  
ANISOU 1992  CD2 LEU A 276    15811  18641  17415    889   1564    113       C  
ATOM   1993  N   PHE A 277     -10.997  -9.463   3.288  1.00132.51           N  
ANISOU 1993  N   PHE A 277    16078  17752  16517   1184   1500    609       N  
ATOM   1994  CA  PHE A 277     -11.910  -8.894   4.283  1.00132.23           C  
ANISOU 1994  CA  PHE A 277    16015  17711  16515   1265   1403    677       C  
ATOM   1995  C   PHE A 277     -12.606  -7.611   3.776  1.00139.08           C  
ANISOU 1995  C   PHE A 277    17200  18413  17232   1354   1469    775       C  
ATOM   1996  O   PHE A 277     -12.172  -6.502   4.105  1.00139.49           O  
ANISOU 1996  O   PHE A 277    17375  18354  17271   1261   1646    759       O  
ATOM   1997  CB  PHE A 277     -11.212  -8.687   5.642  1.00133.35           C  
ANISOU 1997  CB  PHE A 277    15957  17911  16799   1140   1454    588       C  
ATOM   1998  CG  PHE A 277     -10.664  -9.946   6.273  1.00133.71           C  
ANISOU 1998  CG  PHE A 277    15717  18113  16975   1110   1345    504       C  
ATOM   1999  CD1 PHE A 277     -11.499 -10.821   6.958  1.00135.46           C  
ANISOU 1999  CD1 PHE A 277    15794  18423  17251   1216   1147    555       C  
ATOM   2000  CD2 PHE A 277      -9.309 -10.243   6.206  1.00136.32           C  
ANISOU 2000  CD2 PHE A 277    15929  18492  17373    978   1451    360       C  
ATOM   2001  CE1 PHE A 277     -10.991 -11.983   7.545  1.00135.60           C  
ANISOU 2001  CE1 PHE A 277    15603  18556  17365   1206   1055    489       C  
ATOM   2002  CE2 PHE A 277      -8.801 -11.404   6.798  1.00138.36           C  
ANISOU 2002  CE2 PHE A 277    15944  18888  17740    988   1330    281       C  
ATOM   2003  CZ  PHE A 277      -9.645 -12.266   7.464  1.00135.17           C  
ANISOU 2003  CZ  PHE A 277    15445  18548  17364   1108   1132    358       C  
ATOM   2004  N   PRO A 278     -13.685  -7.736   2.964  1.00137.44           N  
ANISOU 2004  N   PRO A 278    17134  18180  16905   1544   1323    865       N  
ATOM   2005  CA  PRO A 278     -14.362  -6.529   2.462  1.00139.37           C  
ANISOU 2005  CA  PRO A 278    17705  18261  16990   1675   1358    957       C  
ATOM   2006  C   PRO A 278     -15.379  -5.943   3.443  1.00144.36           C  
ANISOU 2006  C   PRO A 278    18272  18895  17685   1787   1248    999       C  
ATOM   2007  O   PRO A 278     -15.986  -6.680   4.223  1.00142.48           O  
ANISOU 2007  O   PRO A 278    17756  18798  17581   1826   1082    977       O  
ATOM   2008  CB  PRO A 278     -15.014  -6.998   1.156  1.00141.99           C  
ANISOU 2008  CB  PRO A 278    18201  18587  17162   1849   1221   1005       C  
ATOM   2009  CG  PRO A 278     -14.965  -8.506   1.179  1.00144.78           C  
ANISOU 2009  CG  PRO A 278    18254  19124  17633   1823   1075    941       C  
ATOM   2010  CD  PRO A 278     -14.336  -8.960   2.459  1.00138.52           C  
ANISOU 2010  CD  PRO A 278    17151  18435  17046   1660   1115    870       C  
ATOM   2011  N   GLU A 279     -15.561  -4.608   3.399  1.00143.61           N  
ANISOU 2011  N   GLU A 279    18449  18627  17490   1836   1361   1055       N  
ATOM   2012  CA  GLU A 279     -16.486  -3.883   4.276  1.00143.98           C  
ANISOU 2012  CA  GLU A 279    18470  18648  17587   1947   1288   1088       C  
ATOM   2013  C   GLU A 279     -17.764  -3.447   3.554  1.00150.54           C  
ANISOU 2013  C   GLU A 279    19505  19413  18282   2237   1119   1165       C  
ATOM   2014  O   GLU A 279     -18.859  -3.721   4.048  1.00149.52           O  
ANISOU 2014  O   GLU A 279    19181  19386  18242   2381    921   1152       O  
ATOM   2015  CB  GLU A 279     -15.793  -2.680   4.945  1.00146.02           C  
ANISOU 2015  CB  GLU A 279    18858  18764  17859   1799   1528   1073       C  
ATOM   2016  CG  GLU A 279     -14.843  -3.049   6.076  1.00155.41           C  
ANISOU 2016  CG  GLU A 279    19759  20064  19225   1563   1616    966       C  
ATOM   2017  CD  GLU A 279     -13.461  -3.555   5.699  1.00176.15           C  
ANISOU 2017  CD  GLU A 279    22329  22724  21875   1355   1766    874       C  
ATOM   2018  OE1 GLU A 279     -13.081  -3.461   4.508  1.00171.57           O  
ANISOU 2018  OE1 GLU A 279    21979  22048  21163   1348   1870    894       O  
ATOM   2019  OE2 GLU A 279     -12.745  -4.029   6.609  1.00169.43           O  
ANISOU 2019  OE2 GLU A 279    21211  21995  21169   1206   1781    770       O  
ATOM   2020  N   ASP A 280     -17.624  -2.764   2.398  1.00150.25           N  
ANISOU 2020  N   ASP A 280    19865  19199  18025   2329   1201   1232       N  
ATOM   2021  CA  ASP A 280     -18.749  -2.286   1.588  1.00152.47           C  
ANISOU 2021  CA  ASP A 280    20399  19399  18133   2643   1026   1301       C  
ATOM   2022  C   ASP A 280     -19.530  -3.430   0.892  1.00157.20           C  
ANISOU 2022  C   ASP A 280    20837  20172  18720   2810    743   1267       C  
ATOM   2023  O   ASP A 280     -20.753  -3.459   1.051  1.00157.14           O  
ANISOU 2023  O   ASP A 280    20711  20242  18754   3033    509   1244       O  
ATOM   2024  CB  ASP A 280     -18.308  -1.205   0.586  1.00156.91           C  
ANISOU 2024  CB  ASP A 280    21491  19694  18432   2694   1215   1390       C  
ATOM   2025  N   PRO A 281     -18.900  -4.402   0.167  1.00154.07           N  
ANISOU 2025  N   PRO A 281    20402  19849  18288   2708    754   1238       N  
ATOM   2026  CA  PRO A 281     -19.700  -5.471  -0.458  1.00154.09           C  
ANISOU 2026  CA  PRO A 281    20245  20013  18286   2862    484   1187       C  
ATOM   2027  C   PRO A 281     -20.039  -6.647   0.474  1.00156.20           C  
ANISOU 2027  C   PRO A 281    20031  20501  18817   2763    365   1092       C  
ATOM   2028  O   PRO A 281     -20.301  -7.754  -0.006  1.00155.41           O  
ANISOU 2028  O   PRO A 281    19771  20533  18744   2783    222   1030       O  
ATOM   2029  CB  PRO A 281     -18.850  -5.896  -1.670  1.00156.61           C  
ANISOU 2029  CB  PRO A 281    20790  20283  18432   2796    579   1200       C  
ATOM   2030  CG  PRO A 281     -17.514  -5.208  -1.512  1.00161.09           C  
ANISOU 2030  CG  PRO A 281    21547  20690  18968   2554    922   1234       C  
ATOM   2031  CD  PRO A 281     -17.471  -4.575  -0.160  1.00155.47           C  
ANISOU 2031  CD  PRO A 281    20672  19967  18433   2453   1011   1227       C  
ATOM   2032  N   SER A 282     -20.066  -6.400   1.802  1.00151.81           N  
ANISOU 2032  N   SER A 282    19268  19971  18441   2659    430   1078       N  
ATOM   2033  CA  SER A 282     -20.400  -7.401   2.821  1.00149.90           C  
ANISOU 2033  CA  SER A 282    18626  19901  18429   2564    352   1000       C  
ATOM   2034  C   SER A 282     -21.906  -7.698   2.851  1.00154.83           C  
ANISOU 2034  C   SER A 282    19074  20630  19123   2768    111    933       C  
ATOM   2035  O   SER A 282     -22.307  -8.772   3.305  1.00153.33           O  
ANISOU 2035  O   SER A 282    18583  20581  19093   2707     30    851       O  
ATOM   2036  CB  SER A 282     -19.934  -6.935   4.202  1.00 20.00           C  
ATOM   2037  OG  SER A 282     -20.624  -5.764   4.604  1.00 20.00           O  
ATOM   2038  N   TYR A 283     -22.732  -6.746   2.368  1.00153.70           N  
ANISOU 2038  N   TYR A 283    19123  20411  18865   3013      5    954       N  
ATOM   2039  CA  TYR A 283     -24.191  -6.867   2.298  1.00154.85           C  
ANISOU 2039  CA  TYR A 283    19104  20658  19074   3243   -238    857       C  
ATOM   2040  C   TYR A 283     -24.617  -7.860   1.212  1.00159.83           C  
ANISOU 2040  C   TYR A 283    19669  21405  19652   3346   -439    774       C  
ATOM   2041  O   TYR A 283     -25.599  -8.581   1.396  1.00159.49           O  
ANISOU 2041  O   TYR A 283    19326  21514  19761   3402   -603    638       O  
ATOM   2042  CB  TYR A 283     -24.834  -5.495   2.054  1.00158.23           C  
ANISOU 2042  CB  TYR A 283    19787  20958  19375   3505   -301    900       C  
ATOM   2043  N   ASP A 284     -23.902  -7.871   0.097  1.00157.41           N  
ANISOU 2043  N   ASP A 284    19648  21026  19135   3357   -410    840       N  
ATOM   2044  CA  ASP A 284     -24.207  -8.788  -0.988  1.00158.32           C  
ANISOU 2044  CA  ASP A 284    19756  21236  19163   3448   -586    766       C  
ATOM   2045  C   ASP A 284     -23.406 -10.070  -0.825  1.00160.76           C  
ANISOU 2045  C   ASP A 284    19861  21635  19583   3190   -493    730       C  
ATOM   2046  O   ASP A 284     -23.504 -10.985  -1.639  1.00160.87           O  
ANISOU 2046  O   ASP A 284    19854  21730  19542   3231   -616    660       O  
ATOM   2047  CB  ASP A 284     -23.915  -8.139  -2.339  1.00162.38           C  
ANISOU 2047  CB  ASP A 284    20732  21609  19357   3634   -613    853       C  
ATOM   2048  CG  ASP A 284     -24.993  -7.161  -2.759  1.00174.34           C  
ANISOU 2048  CG  ASP A 284    22475  23037  20729   3961   -770    873       C  
ATOM   2049  OD1 ASP A 284     -25.944  -7.582  -3.448  1.00175.74           O  
ANISOU 2049  OD1 ASP A 284    22422  23349  21002   4165  -1027    742       O  
ATOM   2050  OD2 ASP A 284     -24.893  -5.971  -2.399  1.00181.32           O  
ANISOU 2050  OD2 ASP A 284    23777  23713  21403   4022   -634   1007       O  
ATOM   2051  N   ALA A 285     -22.611 -10.128   0.236  1.00155.65           N  
ANISOU 2051  N   ALA A 285    19073  20978  19090   2942   -290    767       N  
ATOM   2052  CA  ALA A 285     -21.703 -11.244   0.442  1.00153.89           C  
ANISOU 2052  CA  ALA A 285    18663  20827  18981   2715   -199    736       C  
ATOM   2053  C   ALA A 285     -22.461 -12.552   0.576  1.00157.95           C  
ANISOU 2053  C   ALA A 285    18848  21494  19671   2711   -349    603       C  
ATOM   2054  O   ALA A 285     -22.057 -13.568   0.021  1.00157.06           O  
ANISOU 2054  O   ALA A 285    18659  21442  19575   2631   -367    552       O  
ATOM   2055  CB  ALA A 285     -20.848 -11.004   1.675  1.00152.88           C  
ANISOU 2055  CB  ALA A 285    18471  20652  18963   2505     14    792       C  
ATOM   2056  N   ASN A 286     -23.572 -12.530   1.299  1.00155.40           N  
ANISOU 2056  N   ASN A 286    18336  21227  19483   2790   -439    534       N  
ATOM   2057  CA  ASN A 286     -24.354 -13.742   1.461  1.00155.58           C  
ANISOU 2057  CA  ASN A 286    18041  21382  19689   2776   -552    380       C  
ATOM   2058  C   ASN A 286     -25.254 -13.953   0.258  1.00162.02           C  
ANISOU 2058  C   ASN A 286    18862  22279  20418   2973   -787    261       C  
ATOM   2059  O   ASN A 286     -26.029 -13.077  -0.112  1.00163.30           O  
ANISOU 2059  O   ASN A 286    19255  22396  20397   3190   -900    296       O  
ATOM   2060  CB  ASN A 286     -25.190 -13.671   2.736  1.00156.62           C  
ANISOU 2060  CB  ASN A 286    17982  21538  19989   2793   -543    326       C  
ATOM   2061  N   VAL A 287     -25.146 -15.126  -0.349  1.00 30.00           N  
ATOM   2062  CA  VAL A 287     -25.932 -15.452  -1.530  1.00 30.00           C  
ATOM   2063  C   VAL A 287     -27.423 -15.504  -1.259  1.00 30.00           C  
ATOM   2064  O   VAL A 287     -28.230 -15.084  -2.085  1.00 30.00           O  
ATOM   2065  CB  VAL A 287     -25.517 -16.803  -2.136  1.00 20.00           C  
ATOM   2066  CG1 VAL A 287     -24.238 -16.653  -2.945  1.00 20.00           C  
ATOM   2067  CG2 VAL A 287     -25.363 -17.848  -1.042  1.00 20.00           C  
ATOM   2068  N   ILE A 288     -27.789 -16.037  -0.102  1.00 30.00           N  
ATOM   2069  CA  ILE A 288     -29.135 -16.536   0.106  1.00 30.00           C  
ATOM   2070  C   ILE A 288     -30.242 -15.507  -0.039  1.00 30.00           C  
ATOM   2071  O   ILE A 288     -31.261 -15.798  -0.667  1.00 30.00           O  
ATOM   2072  CB  ILE A 288     -29.278 -17.179   1.498  1.00 20.00           C  
ATOM   2073  N   ASP A 289     -30.070 -14.319   0.530  1.00164.13           N  
ANISOU 2073  N   ASP A 289    18451  22883  21029   3236  -1248   -271       N  
ATOM   2074  CA  ASP A 289     -31.139 -13.332   0.429  1.00166.35           C  
ANISOU 2074  CA  ASP A 289    18554  23252  21399   3451  -1431   -442       C  
ATOM   2075  C   ASP A 289     -30.790 -11.883   0.723  1.00170.66           C  
ANISOU 2075  C   ASP A 289    19248  23699  21896   3578  -1385   -319       C  
ATOM   2076  O   ASP A 289     -29.767 -11.579   1.334  1.00168.14           O  
ANISOU 2076  O   ASP A 289    19020  23271  21595   3406  -1155   -155       O  
ATOM   2077  CB  ASP A 289     -32.324 -13.756   1.293  1.00168.51           C  
ANISOU 2077  CB  ASP A 289    18405  23643  21977   3301  -1397   -675       C  
ATOM   2078  CG  ASP A 289     -33.595 -13.042   0.913  1.00181.39           C  
ANISOU 2078  CG  ASP A 289    19781  25430  23709   3526  -1655   -957       C  
ATOM   2079  OD1 ASP A 289     -33.506 -12.034   0.181  1.00183.04           O  
ANISOU 2079  OD1 ASP A 289    19961  25642  23942   3716  -1731   -989       O  
ATOM   2080  OD2 ASP A 289     -34.678 -13.484   1.345  1.00188.61           O  
ANISOU 2080  OD2 ASP A 289    20510  26465  24688   3514  -1784  -1164       O  
ATOM   2081  N   ASP A 290     -31.675 -10.998   0.281  1.00170.13           N  
ANISOU 2081  N   ASP A 290    19204  23672  21767   3892  -1614   -414       N  
ATOM   2082  CA  ASP A 290     -31.781  -9.657   0.815  1.00170.74           C  
ANISOU 2082  CA  ASP A 290    19425  23652  21795   4063  -1604   -326       C  
ATOM   2083  C   ASP A 290     -32.422  -9.846   2.179  1.00174.62           C  
ANISOU 2083  C   ASP A 290    19571  24202  22576   3966  -1506   -456       C  
ATOM   2084  O   ASP A 290     -33.111 -10.838   2.403  1.00174.94           O  
ANISOU 2084  O   ASP A 290    19246  24389  22834   3904  -1561   -691       O  
ATOM   2085  CB  ASP A 290     -32.663  -8.785  -0.074  1.00175.78           C  
ANISOU 2085  CB  ASP A 290    20238  24307  22244   4472  -1909   -390       C  
ATOM   2086  N   GLU A 291     -32.209  -8.913   3.097  1.00170.53           N  
ANISOU 2086  N   GLU A 291    19176  23559  22058   3941  -1341   -316       N  
ATOM   2087  CA  GLU A 291     -32.710  -9.114   4.446  1.00170.20           C  
ANISOU 2087  CA  GLU A 291    18873  23539  22256   3844  -1209   -406       C  
ATOM   2088  C   GLU A 291     -34.218  -9.279   4.382  1.00177.13           C  
ANISOU 2088  C   GLU A 291    19420  24566  23315   4052  -1409   -695       C  
ATOM   2089  O   GLU A 291     -34.904  -8.534   3.685  1.00179.12           O  
ANISOU 2089  O   GLU A 291    19761  24844  23454   4389  -1664   -759       O  
ATOM   2090  CB  GLU A 291     -32.349  -7.923   5.331  1.00170.70           C  
ANISOU 2090  CB  GLU A 291    19188  23436  22234   3854  -1049   -211       C  
ATOM   2091  N   ALA A 292     -34.734 -10.260   5.115  1.00173.81           N  
ANISOU 2091  N   ALA A 292    18625  24241  23174   3850  -1286   -882       N  
ATOM   2092  CA  ALA A 292     -36.153 -10.570   5.063  1.00176.48           C  
ANISOU 2092  CA  ALA A 292    18569  24736  23749   3976  -1419  -1209       C  
ATOM   2093  C   ALA A 292     -36.948  -9.372   5.546  1.00182.23           C  
ANISOU 2093  C   ALA A 292    19304  25431  24505   4226  -1476  -1243       C  
ATOM   2094  O   ALA A 292     -37.964  -9.009   4.960  1.00184.85           O  
ANISOU 2094  O   ALA A 292    19454  25880  24900   4520  -1732  -1474       O  
ATOM   2095  CB  ALA A 292     -36.461 -11.791   5.914  1.00176.56           C  
ANISOU 2095  CB  ALA A 292    18240  24808  24038   3642  -1187  -1371       C  
ATOM   2096  N   VAL A 293     -36.464  -8.746   6.610  1.00177.18           N  
ANISOU 2096  N   VAL A 293    18870  24633  23816   4124  -1250  -1027       N  
ATOM   2097  CA  VAL A 293     -37.078  -7.532   7.111  1.00178.39           C  
ANISOU 2097  CA  VAL A 293    19077  24720  23984   4334  -1259  -1027       C  
ATOM   2098  C   VAL A 293     -36.954  -6.465   6.038  1.00184.26           C  
ANISOU 2098  C   VAL A 293    20159  25390  24463   4722  -1519   -923       C  
ATOM   2099  O   VAL A 293     -37.871  -5.678   5.820  1.00186.51           O  
ANISOU 2099  O   VAL A 293    20388  25698  24780   5040  -1696  -1054       O  
ATOM   2100  CB  VAL A 293     -36.408  -7.050   8.407  1.00179.87           C  
ANISOU 2100  CB  VAL A 293    19408  24755  24181   4092   -936   -830       C  
ATOM   2101  CG1 VAL A 293     -36.910  -5.663   8.778  1.00181.26           C  
ANISOU 2101  CG1 VAL A 293    19572  24877  24423   4286   -925   -883       C  
ATOM   2102  CG2 VAL A 293     -36.672  -8.037   9.533  1.00178.02           C  
ANISOU 2102  CG2 VAL A 293    18932  24566  24142   3714   -680   -894       C  
ATOM   2103  N   LYS A 294     -35.810  -6.453   5.366  1.00179.81           N  
ANISOU 2103  N   LYS A 294    19950  24733  23636   4701  -1539   -701       N  
ATOM   2104  CA  LYS A 294     -35.524  -5.450   4.352  1.00181.38           C  
ANISOU 2104  CA  LYS A 294    20550  24829  23537   5032  -1743   -573       C  
ATOM   2105  C   LYS A 294     -36.518  -5.527   3.203  1.00188.88           C  
ANISOU 2105  C   LYS A 294    21358  25939  24467   5378  -2120   -809       C  
ATOM   2106  O   LYS A 294     -36.949  -4.504   2.675  1.00190.95           O  
ANISOU 2106  O   LYS A 294    21858  26141  24554   5763  -2341   -797       O  
ATOM   2107  CB  LYS A 294     -34.100  -5.620   3.822  1.00181.77           C  
ANISOU 2107  CB  LYS A 294    20974  24751  23340   4862  -1621   -310       C  
ATOM   2108  N   GLU A 295     -36.878  -6.741   2.811  1.00185.97           N  
ANISOU 2108  N   GLU A 295    20617  25768  24274   5248  -2195  -1033       N  
ATOM   2109  CA  GLU A 295     -37.829  -6.912   1.727  1.00189.27           C  
ANISOU 2109  CA  GLU A 295    20822  26376  24714   5535  -2555  -1314       C  
ATOM   2110  C   GLU A 295     -39.175  -6.307   2.102  1.00196.87           C  
ANISOU 2110  C   GLU A 295    21422  27463  25916   5772  -2705  -1612       C  
ATOM   2111  O   GLU A 295     -39.823  -5.661   1.282  1.00199.82           O  
ANISOU 2111  O   GLU A 295    21784  27924  26213   6183  -3057  -1781       O  
ATOM   2112  CB  GLU A 295     -37.995  -8.392   1.386  1.00189.78           C  
ANISOU 2112  CB  GLU A 295    20595  26598  24914   5269  -2540  -1471       C  
ATOM   2113  N   VAL A 296     -39.595  -6.512   3.346  1.00193.08           N  
ANISOU 2113  N   VAL A 296    20654  26991  25718   5524  -2440  -1686       N  
ATOM   2114  CA  VAL A 296     -40.890  -6.011   3.783  1.00195.92           C  
ANISOU 2114  CA  VAL A 296    20634  27459  26347   5681  -2501  -1978       C  
ATOM   2115  C   VAL A 296     -40.962  -4.489   3.735  1.00203.11           C  
ANISOU 2115  C   VAL A 296    21842  28236  27095   6079  -2637  -1870       C  
ATOM   2116  O   VAL A 296     -41.948  -3.928   3.267  1.00206.39           O  
ANISOU 2116  O   VAL A 296    22065  28766  27587   6453  -2923  -2128       O  
ATOM   2117  CB  VAL A 296     -41.231  -6.493   5.204  1.00197.83           C  
ANISOU 2117  CB  VAL A 296    20548  27716  26902   5265  -2128  -2059       C  
ATOM   2118  CG1 VAL A 296     -42.535  -5.870   5.677  1.00199.82           C  
ANISOU 2118  CG1 VAL A 296    20528  28006  27387   5411  -2106  -2274       C  
ATOM   2119  CG2 VAL A 296     -41.323  -8.010   5.237  1.00197.48           C  
ANISOU 2119  CG2 VAL A 296    20124  27837  27072   4975  -2068  -2293       C  
ATOM   2120  N   CYS A 297     -39.909  -3.820   4.190  1.00198.49           N  
ANISOU 2120  N   CYS A 297    21726  27407  26285   6005  -2436  -1505       N  
ATOM   2121  CA  CYS A 297     -39.874  -2.352   4.111  1.00200.26           C  
ANISOU 2121  CA  CYS A 297    22319  27448  26323   6336  -2503  -1354       C  
ATOM   2122  C   CYS A 297     -40.202  -1.841   2.704  1.00208.00           C  
ANISOU 2122  C   CYS A 297    23569  28426  27036   6829  -2904  -1376       C  
ATOM   2123  O   CYS A 297     -40.879  -0.821   2.570  1.00210.26           O  
ANISOU 2123  O   CYS A 297    23941  28668  27280   7230  -3095  -1446       O  
ATOM   2124  CB  CYS A 297     -38.537  -1.808   4.608  1.00197.52           C  
ANISOU 2124  CB  CYS A 297    22411  26845  25792   6095  -2182   -980       C  
ATOM   2125  SG  CYS A 297     -38.332  -1.871   6.407  1.00198.60           S  
ANISOU 2125  SG  CYS A 297    22317  26942  26201   5670  -1760   -958       S  
ATOM   2126  N   GLU A 298     -39.735  -2.560   1.664  1.00205.16           N  
ANISOU 2126  N   GLU A 298    23353  28111  26487   6810  -3035  -1323       N  
ATOM   2127  CA  GLU A 298     -39.996  -2.239   0.260  1.00208.67           C  
ANISOU 2127  CA  GLU A 298    24078  28563  26644   7259  -3421  -1347       C  
ATOM   2128  C   GLU A 298     -41.422  -2.647  -0.125  1.00217.20           C  
ANISOU 2128  C   GLU A 298    24672  29928  27927   7555  -3797  -1776       C  
ATOM   2129  O   GLU A 298     -42.017  -2.024  -1.006  1.00218.59           O  
ANISOU 2129  O   GLU A 298    25008  30003  28043   7777  -4020  -1686       O  
ATOM   2130  CB  GLU A 298     -38.976  -2.936  -0.652  1.00208.37           C  
ANISOU 2130  CB  GLU A 298    24344  28480  26348   7095  -3395  -1157       C  
ATOM   2131  N   LYS A 299     -41.965  -3.688   0.541  1.00214.13           N  
ANISOU 2131  N   LYS A 299    23693  29756  27910   7250  -3695  -2052       N  
ATOM   2132  CA  LYS A 299     -43.313  -4.211   0.312  1.00217.94           C  
ANISOU 2132  CA  LYS A 299    23620  30531  28658   7437  -3990  -2515       C  
ATOM   2133  C   LYS A 299     -44.400  -3.336   0.945  1.00221.36           C  
ANISOU 2133  C   LYS A 299    23886  30719  29502   7141  -3717  -2237       C  
ATOM   2134  O   LYS A 299     -45.438  -3.110   0.323  1.00221.82           O  
ANISOU 2134  O   LYS A 299    23819  30727  29733   7111  -3805  -2122       O  
ATOM   2135  CB  LYS A 299     -43.429  -5.660   0.808  1.00218.84           C  
ANISOU 2135  CB  LYS A 299    23243  30820  29087   6962  -3785  -2718       C  
ATOM   2136  N   PHE A 300     -44.161  -2.847   2.177  1.00219.69           N  
ANISOU 2136  N   PHE A 300    23596  30589  29287   7348  -3640  -2489       N  
ATOM   2137  CA  PHE A 300     -45.097  -1.997   2.917  1.00220.22           C  
ANISOU 2137  CA  PHE A 300    23486  30528  29662   7278  -3471  -2418       C  
ATOM   2138  C   PHE A 300     -45.168  -0.565   2.367  1.00224.83           C  
ANISOU 2138  C   PHE A 300    24559  30708  30159   7298  -3412  -1876       C  
ATOM   2139  O   PHE A 300     -46.156   0.130   2.614  1.00225.31           O  
ANISOU 2139  O   PHE A 300    24460  30678  30469   7299  -3350  -1807       O  
ATOM   2140  CB  PHE A 300     -44.744  -1.985   4.412  1.00221.69           C  
ANISOU 2140  CB  PHE A 300    23472  30827  29933   7249  -3259  -2694       C  
ATOM   2141  N   GLU A 301     -44.128  -0.130   1.627  1.00223.13           N  
ANISOU 2141  N   GLU A 301    24900  30388  29493   7588  -3583  -1736       N  
ATOM   2142  CA  GLU A 301     -44.037   1.211   1.047  1.00224.11           C  
ANISOU 2142  CA  GLU A 301    25514  30189  29450   7747  -3614  -1381       C  
ATOM   2143  C   GLU A 301     -44.628   1.332  -0.360  1.00228.32           C  
ANISOU 2143  C   GLU A 301    26129  30527  30096   7473  -3664   -989       C  
ATOM   2144  O   GLU A 301     -45.181   2.384  -0.686  1.00228.77           O  
ANISOU 2144  O   GLU A 301    26312  30378  30230   7529  -3674   -768       O  
ATOM   2145  CB  GLU A 301     -42.586   1.711   1.062  1.00224.41           C  
ANISOU 2145  CB  GLU A 301    26159  30042  29065   7842  -3512  -1175       C  
ATOM   2146  N   CYS A 302     -44.520   0.281  -1.166  1.00226.43           N  
ANISOU 2146  N   CYS A 302    25827  30496  29710   7524  -3885  -1136       N  
ATOM   2147  CA  CYS A 302     -44.976   0.349  -2.550  1.00227.36           C  
ANISOU 2147  CA  CYS A 302    26033  30549  29805   7468  -4056   -916       C  
ATOM   2148  C   CYS A 302     -45.858  -0.815  -2.988  1.00231.43           C  
ANISOU 2148  C   CYS A 302    26003  31231  30700   7089  -4008   -923       C  
ATOM   2149  O   CYS A 302     -46.996  -0.615  -3.408  1.00232.11           O  
ANISOU 2149  O   CYS A 302    25807  31321  31062   7065  -3991   -875       O  
ATOM   2150  CB  CYS A 302     -43.778   0.460  -3.496  1.00227.07           C  
ANISOU 2150  CB  CYS A 302    26500  30418  29358   7495  -4140   -752       C  
ATOM   2151  SG  CYS A 302     -42.713   1.888  -3.192  1.00229.49           S  
ANISOU 2151  SG  CYS A 302    27491  30329  29376   7474  -3915   -386       S  
ATOM   2152  N   THR A 303     -45.326  -2.029  -2.903  1.00229.08           N  
ANISOU 2152  N   THR A 303    25572  31188  30279   7120  -4166  -1205       N  
ATOM   2153  CA  THR A 303     -45.979  -3.194  -3.492  1.00229.54           C  
ANISOU 2153  CA  THR A 303    25160  31464  30590   6909  -4212  -1340       C  
ATOM   2154  C   THR A 303     -46.043  -4.411  -2.574  1.00231.73           C  
ANISOU 2154  C   THR A 303    25097  31893  31055   6580  -3976  -1544       C  
ATOM   2155  O   THR A 303     -45.293  -4.520  -1.606  1.00230.55           O  
ANISOU 2155  O   THR A 303    25131  31777  30689   6664  -3965  -1686       O  
ATOM   2156  CB  THR A 303     -45.304  -3.607  -4.813  1.00236.18           C  
ANISOU 2156  CB  THR A 303    26232  32144  31362   6482  -4167   -857       C  
ATOM   2157  N   GLU A 304     -46.953  -5.323  -2.897  1.00229.88           N  
ANISOU 2157  N   GLU A 304    24327  31892  31125   6501  -3978  -1825       N  
ATOM   2158  CA  GLU A 304     -47.157  -6.540  -2.122  1.00229.27           C  
ANISOU 2158  CA  GLU A 304    23826  32029  31256   6282  -3822  -2173       C  
ATOM   2159  C   GLU A 304     -45.932  -7.447  -2.170  1.00231.02           C  
ANISOU 2159  C   GLU A 304    24189  32271  31318   6053  -3760  -2167       C  
ATOM   2160  O   GLU A 304     -45.183  -7.448  -3.146  1.00230.66           O  
ANISOU 2160  O   GLU A 304    24437  32187  31015   6133  -3954  -2038       O  
ATOM   2161  CB  GLU A 304     -48.385  -7.297  -2.629  1.00230.95           C  
ANISOU 2161  CB  GLU A 304    23609  32341  31800   5988  -3708  -2146       C  
ATOM   2162  N   SER A 305     -45.734  -8.212  -1.102  1.00228.05           N  
ANISOU 2162  N   SER A 305    23482  32108  31057   6024  -3670  -2625       N  
ATOM   2163  CA  SER A 305     -44.556  -9.058  -0.954  1.00227.05           C  
ANISOU 2163  CA  SER A 305    23343  32111  30813   5931  -3659  -2852       C  
ATOM   2164  C   SER A 305     -44.503 -10.120  -2.040  1.00229.92           C  
ANISOU 2164  C   SER A 305    23838  32432  31089   5679  -3707  -2620       C  
ATOM   2165  O   SER A 305     -45.537 -10.601  -2.500  1.00230.29           O  
ANISOU 2165  O   SER A 305    23732  32501  31265   5579  -3778  -2538       O  
ATOM   2166  CB  SER A 305     -44.543  -9.722   0.423  1.00228.96           C  
ANISOU 2166  CB  SER A 305    23192  32419  31382   5528  -3298  -3030       C  
ATOM   2167  N   GLU A 306     -43.282 -10.450  -2.455  1.00226.96           N  
ANISOU 2167  N   GLU A 306    23630  32173  30433   5846  -3848  -2834       N  
ATOM   2168  CA  GLU A 306     -43.022 -11.347  -3.579  1.00226.82           C  
ANISOU 2168  CA  GLU A 306    23746  32199  30236   5792  -3994  -2813       C  
ATOM   2169  C   GLU A 306     -43.098 -10.566  -4.889  1.00230.28           C  
ANISOU 2169  C   GLU A 306    24738  32363  30396   5828  -4090  -2268       C  
ATOM   2170  O   GLU A 306     -42.952 -11.126  -5.974  1.00230.07           O  
ANISOU 2170  O   GLU A 306    24851  32356  30210   5795  -4232  -2218       O  
ATOM   2171  CB  GLU A 306     -43.991 -12.534  -3.580  1.00228.10           C  
ANISOU 2171  CB  GLU A 306    23505  32457  30707   5410  -3902  -2915       C  
ATOM   2172  CG  GLU A 306     -44.003 -13.353  -4.858  1.00234.40           C  
ANISOU 2172  CG  GLU A 306    24477  33132  31453   4936  -3678  -2639       C  
ATOM   2173  CD  GLU A 306     -44.891 -14.576  -4.750  1.00246.37           C  
ANISOU 2173  CD  GLU A 306    26115  34302  33192   4047  -3215  -1815       C  
ATOM   2174  OE1 GLU A 306     -45.591 -14.710  -3.725  1.00241.98           O  
ANISOU 2174  OE1 GLU A 306    25103  33944  32893   4005  -3165  -2192       O  
ATOM   2175  OE2 GLU A 306     -44.889 -15.402  -5.687  1.00241.74           O  
ANISOU 2175  OE2 GLU A 306    25607  33838  32407   4267  -3552  -1975       O  
ATOM   2176  N   VAL A 307     -43.311  -9.260  -4.768  1.00228.46           N  
ANISOU 2176  N   VAL A 307    24744  32029  30033   6163  -4186  -2168       N  
ATOM   2177  CA  VAL A 307     -43.381  -8.370  -5.918  1.00228.91           C  
ANISOU 2177  CA  VAL A 307    25290  31879  29806   6337  -4336  -1817       C  
ATOM   2178  C   VAL A 307     -42.029  -8.206  -6.602  1.00231.09           C  
ANISOU 2178  C   VAL A 307    26093  31989  29719   6300  -4253  -1571       C  
ATOM   2179  O   VAL A 307     -40.985  -8.189  -5.949  1.00229.94           O  
ANISOU 2179  O   VAL A 307    25948  31941  29477   6368  -4157  -1756       O  
ATOM   2180  CB  VAL A 307     -43.907  -6.979  -5.516  1.00232.21           C  
ANISOU 2180  CB  VAL A 307    25816  32042  30370   6293  -4187  -1470       C  
ATOM   2181  N   MET A 308     -42.059  -8.089  -7.924  1.00229.22           N  
ANISOU 2181  N   MET A 308    26267  31663  29162   6496  -4464  -1406       N  
ATOM   2182  CA  MET A 308     -40.861  -7.816  -8.704  1.00228.74           C  
ANISOU 2182  CA  MET A 308    26755  31489  28667   6617  -4473  -1253       C  
ATOM   2183  C   MET A 308     -39.831  -8.924  -8.556  1.00230.74           C  
ANISOU 2183  C   MET A 308    26920  31843  28908   6337  -4363  -1332       C  
ATOM   2184  O   MET A 308     -38.630  -8.682  -8.665  1.00229.93           O  
ANISOU 2184  O   MET A 308    27208  31695  28459   6460  -4315  -1274       O  
ATOM   2185  CB  MET A 308     -40.249  -6.476  -8.291  1.00229.96           C  
ANISOU 2185  CB  MET A 308    27301  31428  28644   6713  -4270  -1043       C  
ATOM   2186  N   ASN A 309     -40.300 -10.142  -8.317  1.00228.45           N  
ANISOU 2186  N   ASN A 309    26130  31822  28849   6286  -4494  -1685       N  
ATOM   2187  CA  ASN A 309     -39.391 -11.270  -8.232  1.00227.77           C  
ANISOU 2187  CA  ASN A 309    25874  31917  28752   6156  -4489  -1921       C  
ATOM   2188  C   ASN A 309     -38.709 -11.450  -9.574  1.00230.19           C  
ANISOU 2188  C   ASN A 309    26603  32056  28804   5970  -4485  -1605       C  
ATOM   2189  O   ASN A 309     -37.498 -11.653  -9.655  1.00229.36           O  
ANISOU 2189  O   ASN A 309    26640  32020  28486   6011  -4453  -1707       O  
ATOM   2190  CB  ASN A 309     -40.145 -12.538  -7.845  1.00228.83           C  
ANISOU 2190  CB  ASN A 309    25416  32215  29315   5860  -4460  -2151       C  
ATOM   2191  N   SER A 310     -39.503 -11.339 -10.631  1.00228.30           N  
ANISOU 2191  N   SER A 310    26537  31759  28449   6094  -4700  -1473       N  
ATOM   2192  CA  SER A 310     -38.983 -11.293 -11.985  1.00228.39           C  
ANISOU 2192  CA  SER A 310    26952  31679  28147   6073  -4792  -1285       C  
ATOM   2193  C   SER A 310     -38.150 -10.030 -12.099  1.00230.58           C  
ANISOU 2193  C   SER A 310    27816  31639  28154   6066  -4636   -865       C  
ATOM   2194  O   SER A 310     -37.097 -10.010 -12.735  1.00230.33           O  
ANISOU 2194  O   SER A 310    28197  31515  27802   6069  -4649   -722       O  
ATOM   2195  CB  SER A 310     -40.124 -11.274 -13.001  1.00231.89           C  
ANISOU 2195  CB  SER A 310    27223  32081  28804   5717  -4832  -1063       C  
ATOM   2196  N   LEU A 311     -38.639  -8.973 -11.461  1.00227.80           N  
ANISOU 2196  N   LEU A 311    27534  31247  27774   6401  -4660   -900       N  
ATOM   2197  CA  LEU A 311     -38.006  -7.669 -11.533  1.00227.58           C  
ANISOU 2197  CA  LEU A 311    28066  30960  27443   6562  -4574   -618       C  
ATOM   2198  C   LEU A 311     -36.601  -7.739 -10.968  1.00229.97           C  
ANISOU 2198  C   LEU A 311    28677  31169  27532   6551  -4314   -551       C  
ATOM   2199  O   LEU A 311     -35.679  -7.134 -11.514  1.00229.82           O  
ANISOU 2199  O   LEU A 311    29209  30931  27182   6622  -4212   -308       O  
ATOM   2200  CB  LEU A 311     -38.825  -6.634 -10.762  1.00227.84           C  
ANISOU 2200  CB  LEU A 311    28020  30873  27675   6629  -4562   -501       C  
ATOM   2201  CG  LEU A 311     -40.220  -6.325 -11.307  1.00231.61           C  
ANISOU 2201  CG  LEU A 311    28165  31299  28539   6254  -4578   -279       C  
ATOM   2202  CD1 LEU A 311     -40.966  -5.396 -10.362  1.00231.92           C  
ANISOU 2202  CD1 LEU A 311    27988  31279  28850   6320  -4529   -251       C  
ATOM   2203  CD2 LEU A 311     -40.132  -5.723 -12.700  1.00233.45           C  
ANISOU 2203  CD2 LEU A 311    28740  31339  28621   6038  -4572     95       C  
ATOM   2204  N   TYR A 312     -36.425  -8.482  -9.880  1.00226.77           N  
ANISOU 2204  N   TYR A 312    27985  31059  27119   6814  -4356   -943       N  
ATOM   2205  CA  TYR A 312     -35.098  -8.577  -9.291  1.00225.04           C  
ANISOU 2205  CA  TYR A 312    28039  30811  26656   6860  -4109   -881       C  
ATOM   2206  C   TYR A 312     -34.125  -9.213 -10.282  1.00227.34           C  
ANISOU 2206  C   TYR A 312    28617  31057  26706   6700  -4027   -777       C  
ATOM   2207  O   TYR A 312     -32.992  -8.758 -10.425  1.00224.14           O  
ANISOU 2207  O   TYR A 312    28523  30452  26190   6439  -3681   -504       O  
ATOM   2208  CB  TYR A 312     -35.114  -9.305  -7.934  1.00222.81           C  
ANISOU 2208  CB  TYR A 312    27233  30601  26823   6432  -3816   -936       C  
ATOM   2209  CG  TYR A 312     -35.555 -10.758  -7.941  1.00223.78           C  
ANISOU 2209  CG  TYR A 312    26829  30954  27242   6163  -3831  -1198       C  
ATOM   2210  CD1 TYR A 312     -34.644 -11.786  -8.134  1.00223.93           C  
ANISOU 2210  CD1 TYR A 312    26920  30962  27201   5879  -3677  -1129       C  
ATOM   2211  CD2 TYR A 312     -36.880 -11.100  -7.710  1.00225.24           C  
ANISOU 2211  CD2 TYR A 312    26443  31342  27797   6140  -3929  -1506       C  
ATOM   2212  CE1 TYR A 312     -35.043 -13.109  -8.130  1.00223.85           C  
ANISOU 2212  CE1 TYR A 312    26457  31134  27463   5622  -3663  -1362       C  
ATOM   2213  CE2 TYR A 312     -37.285 -12.421  -7.696  1.00225.30           C  
ANISOU 2213  CE2 TYR A 312    25990  31527  28085   5856  -3888  -1746       C  
ATOM   2214  CZ  TYR A 312     -36.362 -13.420  -7.907  1.00231.27           C  
ANISOU 2214  CZ  TYR A 312    26856  32262  28755   5604  -3762  -1667       C  
ATOM   2215  OH  TYR A 312     -36.759 -14.734  -7.898  1.00231.86           O  
ANISOU 2215  OH  TYR A 312    26508  32488  29099   5328  -3710  -1902       O  
ATOM   2216  N   SER A 313     -34.574 -10.251 -10.978  1.00226.02           N  
ANISOU 2216  N   SER A 313    28330  31081  26466   6862  -4346  -1018       N  
ATOM   2217  CA  SER A 313     -33.785 -10.836 -12.049  1.00225.51           C  
ANISOU 2217  CA  SER A 313    28506  31004  26171   6752  -4321   -974       C  
ATOM   2218  C   SER A 313     -33.626  -9.835 -13.185  1.00228.76           C  
ANISOU 2218  C   SER A 313    29406  31070  26444   6452  -4219   -543       C  
ATOM   2219  O   SER A 313     -32.548  -9.682 -13.755  1.00228.51           O  
ANISOU 2219  O   SER A 313    29804  30933  26086   6447  -4089   -422       O  
ATOM   2220  CB  SER A 313     -34.451 -12.113 -12.562  1.00227.73           C  
ANISOU 2220  CB  SER A 313    28246  31451  26831   6358  -4392  -1155       C  
ATOM   2221  OG  SER A 313     -33.717 -12.671 -13.638  1.00233.44           O  
ANISOU 2221  OG  SER A 313    28402  32257  28036   5964  -4182  -1251       O  
ATOM   2222  N   GLY A 314     -34.720  -9.152 -13.502  1.00226.97           N  
ANISOU 2222  N   GLY A 314    29171  30795  26272   6562  -4419   -486       N  
ATOM   2223  CA  GLY A 314     -34.741  -8.203 -14.597  1.00227.56           C  
ANISOU 2223  CA  GLY A 314    29668  30646  26148   6461  -4424   -182       C  
ATOM   2224  C   GLY A 314     -33.833  -7.010 -14.402  1.00229.93           C  
ANISOU 2224  C   GLY A 314    30387  30618  26358   6323  -4136    172       C  
ATOM   2225  O   GLY A 314     -33.188  -6.556 -15.344  1.00230.02           O  
ANISOU 2225  O   GLY A 314    30828  30445  26125   6230  -4065    405       O  
ATOM   2226  N   ASP A 315     -33.816  -6.491 -13.177  1.00226.96           N  
ANISOU 2226  N   ASP A 315    30006  30256  25973   6673  -4114     62       N  
ATOM   2227  CA  ASP A 315     -33.072  -5.283 -12.839  1.00226.74           C  
ANISOU 2227  CA  ASP A 315    30400  29964  25787   6761  -3895    286       C  
ATOM   2228  C   ASP A 315     -33.857  -4.024 -13.237  1.00230.35           C  
ANISOU 2228  C   ASP A 315    30878  30190  26455   6480  -3877    582       C  
ATOM   2229  O   ASP A 315     -33.365  -2.901 -13.062  1.00230.07           O  
ANISOU 2229  O   ASP A 315    31295  29898  26224   6469  -3679    804       O  
ATOM   2230  CB  ASP A 315     -31.678  -5.314 -13.481  1.00227.70           C  
ANISOU 2230  CB  ASP A 315    31045  29889  25581   6624  -3569    478       C  
ATOM   2231  CG  ASP A 315     -30.919  -4.018 -13.312  1.00234.48           C  
ANISOU 2231  CG  ASP A 315    31979  30487  26627   6215  -3128    729       C  
ATOM   2232  OD1 ASP A 315     -30.168  -3.891 -12.324  1.00234.28           O  
ANISOU 2232  OD1 ASP A 315    31740  30592  26683   6362  -3061    585       O  
ATOM   2233  OD2 ASP A 315     -31.077  -3.124 -14.171  1.00238.89           O  
ANISOU 2233  OD2 ASP A 315    32799  30751  27216   5795  -2872   1028       O  
ATOM   2234  N   PRO A 316     -35.142  -4.239 -13.772  1.00228.78           N  
ANISOU 2234  N   PRO A 316    30362  30130  26434   6636  -4185    477       N  
ATOM   2235  CA  PRO A 316     -35.820  -2.989 -14.171  1.00229.47           C  
ANISOU 2235  CA  PRO A 316    30574  30033  26582   6594  -4209    715       C  
ATOM   2236  C   PRO A 316     -36.103  -2.081 -12.982  1.00231.79           C  
ANISOU 2236  C   PRO A 316    30711  30198  27161   6545  -4057    784       C  
ATOM   2237  O   PRO A 316     -35.912  -0.868 -13.063  1.00231.67           O  
ANISOU 2237  O   PRO A 316    31082  29933  27010   6548  -3901    992       O  
ATOM   2238  CB  PRO A 316     -37.143  -3.464 -14.793  1.00231.53           C  
ANISOU 2238  CB  PRO A 316    30385  30458  27126   6391  -4427    714       C  
ATOM   2239  CG  PRO A 316     -36.900  -4.860 -15.224  1.00234.21           C  
ANISOU 2239  CG  PRO A 316    30322  31018  27648   6136  -4425    532       C  
ATOM   2240  CD  PRO A 316     -36.146  -5.376 -14.052  1.00230.06           C  
ANISOU 2240  CD  PRO A 316    29920  30562  26929   6522  -4382    261       C  
ATOM   2241  N   GLN A 317     -36.547  -2.679 -11.883  1.00228.87           N  
ANISOU 2241  N   GLN A 317    29933  30055  26973   6853  -4232    473       N  
ATOM   2242  CA  GLN A 317     -36.932  -1.929 -10.696  1.00245.49           C  
ANISOU 2242  CA  GLN A 317    31376  31856  30043   5635  -3617    927       C  
ATOM   2243  C   GLN A 317     -37.745  -2.804  -9.752  1.00260.21           C  
ANISOU 2243  C   GLN A 317    32456  33642  32769   4502  -3096   1127       C  
ATOM   2244  O   GLN A 317     -38.951  -2.971  -9.931  1.00232.15           O  
ANISOU 2244  O   GLN A 317    29106  30764  28337   6455  -4074    150       O  
ATOM   2245  CB  GLN A 317     -37.747  -0.695 -11.083  1.00247.34           C  
ANISOU 2245  CB  GLN A 317    31367  32033  30580   5531  -3687   1090       C  
ATOM   2246  CG  GLN A 317     -38.218   0.131  -9.897  1.00256.04           C  
ANISOU 2246  CG  GLN A 317    32171  32867  32245   4933  -3294   1378       C  
ATOM   2247  CD  GLN A 317     -39.497  -0.404  -9.281  1.00267.46           C  
ANISOU 2247  CD  GLN A 317    32848  34263  34510   4123  -2946   1615       C  
ATOM   2248  OE1 GLN A 317     -39.463  -1.159  -8.309  1.00265.08           O  
ANISOU 2248  OE1 GLN A 317    32404  34035  34279   4334  -3120   1634       O  
ATOM   2249  NE2 GLN A 317     -40.634  -0.016  -9.847  1.00260.87           N  
ANISOU 2249  NE2 GLN A 317    32016  33604  33498   4639  -3067   1217       N  
ATOM   2250  N   ALA A 324     -34.345  -0.808  -6.915  1.00160.82           N  
ANISOU 2250  N   ALA A 324    21867  21314  17923   7828  -3464    213       N  
ATOM   2251  CA  ALA A 324     -35.304  -0.232  -5.977  1.00161.48           C  
ANISOU 2251  CA  ALA A 324    21621  21465  18270   7999  -3564     67       C  
ATOM   2252  C   ALA A 324     -35.014  -0.671  -4.537  1.00161.11           C  
ANISOU 2252  C   ALA A 324    21084  21497  18632   7517  -3235     44       C  
ATOM   2253  O   ALA A 324     -34.839   0.185  -3.667  1.00159.86           O  
ANISOU 2253  O   ALA A 324    21005  21182  18554   7456  -3019    153       O  
ATOM   2254  CB  ALA A 324     -36.724  -0.609  -6.378  1.00165.51           C  
ANISOU 2254  CB  ALA A 324    21743  22260  18885   8389  -4050   -275       C  
ATOM   2255  N   TYR A 325     -34.952  -1.997  -4.292  1.00155.14           N  
ANISOU 2255  N   TYR A 325    19855  20973  18120   7183  -3192    -96       N  
ATOM   2256  CA  TYR A 325     -34.654  -2.576  -2.979  1.00151.10           C  
ANISOU 2256  CA  TYR A 325    18906  20539  17967   6725  -2888   -119       C  
ATOM   2257  C   TYR A 325     -33.154  -2.501  -2.695  1.00151.46           C  
ANISOU 2257  C   TYR A 325    19261  20379  17909   6339  -2484    167       C  
ATOM   2258  O   TYR A 325     -32.755  -2.425  -1.532  1.00148.37           O  
ANISOU 2258  O   TYR A 325    18703  19948  17723   6037  -2200    227       O  
ATOM   2259  CB  TYR A 325     -35.145  -4.028  -2.899  1.00151.36           C  
ANISOU 2259  CB  TYR A 325    18374  20866  18270   6536  -2992   -378       C  
ATOM   2260  N   HIS A 326     -32.330  -2.513  -3.766  1.00148.35           N  
ANISOU 2260  N   HIS A 326    19317  19856  17191   6357  -2458    327       N  
ATOM   2261  CA  HIS A 326     -30.869  -2.421  -3.712  1.00145.67           C  
ANISOU 2261  CA  HIS A 326    19302  19321  16725   6021  -2088    571       C  
ATOM   2262  C   HIS A 326     -30.406  -1.048  -3.216  1.00149.41           C  
ANISOU 2262  C   HIS A 326    20154  19517  17099   6037  -1852    763       C  
ATOM   2263  O   HIS A 326     -29.343  -0.955  -2.601  1.00146.44           O  
ANISOU 2263  O   HIS A 326    19843  19026  16774   5683  -1504    899       O  
ATOM   2264  CB  HIS A 326     -30.257  -2.733  -5.084  1.00147.64           C  
ANISOU 2264  CB  HIS A 326    19947  19504  16646   6081  -2138    656       C  
ATOM   2265  CG  HIS A 326     -30.297  -4.186  -5.441  1.00149.84           C  
ANISOU 2265  CG  HIS A 326    19875  20020  17038   5921  -2246    506       C  
ATOM   2266  ND1 HIS A 326     -29.165  -4.976  -5.367  1.00148.76           N  
ANISOU 2266  ND1 HIS A 326    19710  19875  16938   5528  -1979    590       N  
ATOM   2267  CD2 HIS A 326     -31.336  -4.947  -5.856  1.00153.08           C  
ANISOU 2267  CD2 HIS A 326    19948  20673  17540   6105  -2586    263       C  
ATOM   2268  CE1 HIS A 326     -29.547  -6.186  -5.743  1.00147.95           C  
ANISOU 2268  CE1 HIS A 326    19285  19992  16937   5489  -2156    415       C  
ATOM   2269  NE2 HIS A 326     -30.845  -6.217  -6.045  1.00150.84           N  
ANISOU 2269  NE2 HIS A 326    19451  20517  17343   5816  -2516    210       N  
ATOM   2270  N   LEU A 327     -31.208   0.009  -3.478  1.00148.93           N  
ANISOU 2270  N   LEU A 327    20335  19350  16900   6456  -2046    757       N  
ATOM   2271  CA  LEU A 327     -30.947   1.385  -3.045  1.00149.43           C  
ANISOU 2271  CA  LEU A 327    20777  19136  16865   6528  -1850    918       C  
ATOM   2272  C   LEU A 327     -31.090   1.503  -1.523  1.00150.47           C  
ANISOU 2272  C   LEU A 327    20494  19329  17350   6291  -1671    859       C  
ATOM   2273  O   LEU A 327     -30.366   2.280  -0.899  1.00148.99           O  
ANISOU 2273  O   LEU A 327    20523  18934  17150   6108  -1366   1007       O  
ATOM   2274  CB  LEU A 327     -31.903   2.358  -3.745  1.00153.96           C  
ANISOU 2274  CB  LEU A 327    21688  19601  17207   7087  -2156    898       C  
ATOM   2275  N   ILE A 328     -32.019   0.719  -0.936  1.00146.04           N  
ANISOU 2275  N   ILE A 328    19344  19047  17096   6282  -1848    632       N  
ATOM   2276  CA  ILE A 328     -32.269   0.664   0.505  1.00143.60           C  
ANISOU 2276  CA  ILE A 328    18611  18825  17127   6056  -1692    547       C  
ATOM   2277  C   ILE A 328     -31.145  -0.101   1.213  1.00143.11           C  
ANISOU 2277  C   ILE A 328    18392  18789  17197   5547  -1371    629       C  
ATOM   2278  O   ILE A 328     -30.740   0.290   2.309  1.00140.89           O  
ANISOU 2278  O   ILE A 328    18054  18431  17046   5322  -1119    687       O  
ATOM   2279  CB  ILE A 328     -33.654   0.046   0.798  1.00147.79           C  
ANISOU 2279  CB  ILE A 328    18591  19634  17930   6215  -1970    255       C  
ATOM   2280  N   ILE A 329     -30.642  -1.185   0.577  1.00138.22           N  
ANISOU 2280  N   ILE A 329    17710  18275  16532   5385  -1393    624       N  
ATOM   2281  CA  ILE A 329     -29.551  -2.025   1.084  1.00134.48           C  
ANISOU 2281  CA  ILE A 329    17101  17836  16161   4946  -1131    690       C  
ATOM   2282  C   ILE A 329     -28.211  -1.287   1.036  1.00137.31           C  
ANISOU 2282  C   ILE A 329    17892  17947  16332   4769   -831    907       C  
ATOM   2283  O   ILE A 329     -27.381  -1.477   1.928  1.00134.26           O  
ANISOU 2283  O   ILE A 329    17389  17549  16076   4433   -576    954       O  
ATOM   2284  CB  ILE A 329     -29.490  -3.371   0.331  1.00137.01           C  
ANISOU 2284  CB  ILE A 329    17243  18332  16482   4869  -1262    604       C  
ATOM   2285  N   ASP A 330     -28.005  -0.445  -0.003  1.00136.23           N  
ANISOU 2285  N   ASP A 330    18262  17611  15888   4998   -859   1024       N  
ATOM   2286  CA  ASP A 330     -26.799   0.371  -0.184  1.00135.97           C  
ANISOU 2286  CA  ASP A 330    18692  17312  15658   4848   -555   1211       C  
ATOM   2287  C   ASP A 330     -26.765   1.503   0.844  1.00139.56           C  
ANISOU 2287  C   ASP A 330    19224  17610  16194   4809   -366   1261       C  
ATOM   2288  O   ASP A 330     -25.682   1.905   1.273  1.00137.87           O  
ANISOU 2288  O   ASP A 330    19162  17251  15971   4527    -52   1355       O  
ATOM   2289  CB  ASP A 330     -26.731   0.939  -1.608  1.00140.94           C  
ANISOU 2289  CB  ASP A 330    19878  17754  15917   5127   -635   1312       C  
ATOM   2290  N   ASN A 331     -27.957   2.005   1.241  1.00137.50           N  
ANISOU 2290  N   ASN A 331    18837  17385  16023   5092   -559   1176       N  
ATOM   2291  CA  ASN A 331     -28.135   3.054   2.247  1.00137.45           C  
ANISOU 2291  CA  ASN A 331    18864  17248  16113   5097   -416   1197       C  
ATOM   2292  C   ASN A 331     -27.773   2.526   3.640  1.00137.95           C  
ANISOU 2292  C   ASN A 331    18498  17447  16471   4721   -230   1136       C  
ATOM   2293  O   ASN A 331     -27.283   3.290   4.473  1.00136.87           O  
ANISOU 2293  O   ASN A 331    18455  17172  16379   4561     11   1192       O  
ATOM   2294  CB  ASN A 331     -29.570   3.578   2.230  1.00140.75           C  
ANISOU 2294  CB  ASN A 331    19212  17702  16565   5521   -702   1089       C  
ATOM   2295  N   ARG A 332     -28.004   1.214   3.877  1.00132.57           N  
ANISOU 2295  N   ARG A 332    17369  17025  15975   4583   -337   1018       N  
ATOM   2296  CA  ARG A 332     -27.691   0.518   5.128  1.00129.40           C  
ANISOU 2296  CA  ARG A 332    16578  16762  15828   4246   -186    959       C  
ATOM   2297  C   ARG A 332     -26.177   0.407   5.327  1.00131.19           C  
ANISOU 2297  C   ARG A 332    16943  16900  16002   3898     93   1071       C  
ATOM   2298  O   ARG A 332     -25.715   0.425   6.468  1.00128.97           O  
ANISOU 2298  O   ARG A 332    16508  16632  15864   3654    274   1063       O  
ATOM   2299  CB  ARG A 332     -28.336  -0.875   5.150  1.00128.69           C  
ANISOU 2299  CB  ARG A 332    16049  16936  15913   4210   -367    809       C  
ATOM   2300  N   ARG A 333     -25.414   0.303   4.217  1.00128.29           N  
ANISOU 2300  N   ARG A 333    16867  16449  15429   3884    127   1157       N  
ATOM   2301  CA  ARG A 333     -23.950   0.221   4.213  1.00126.77           C  
ANISOU 2301  CA  ARG A 333    16816  16172  15180   3573    391   1234       C  
ATOM   2302  C   ARG A 333     -23.320   1.548   4.647  1.00131.36           C  
ANISOU 2302  C   ARG A 333    17703  16514  15693   3490    651   1313       C  
ATOM   2303  O   ARG A 333     -22.276   1.539   5.302  1.00129.34           O  
ANISOU 2303  O   ARG A 333    17393  16240  15512   3187    880   1312       O  
ATOM   2304  CB  ARG A 333     -23.434  -0.188   2.826  1.00128.04           C  
ANISOU 2304  CB  ARG A 333    17224  16295  15132   3606    363   1287       C  
ATOM   2305  N   ILE A 334     -23.960   2.682   4.285  1.00130.54           N  
ANISOU 2305  N   ILE A 334    17922  16227  15450   3768    608   1365       N  
ATOM   2306  CA  ILE A 334     -23.527   4.042   4.639  1.00131.61           C  
ANISOU 2306  CA  ILE A 334    18393  16103  15510   3729    851   1435       C  
ATOM   2307  C   ILE A 334     -23.764   4.266   6.144  1.00134.17           C  
ANISOU 2307  C   ILE A 334    18412  16497  16070   3602    918   1362       C  
ATOM   2308  O   ILE A 334     -22.922   4.869   6.814  1.00133.20           O  
ANISOU 2308  O   ILE A 334    18375  16257  15977   3365   1179   1374       O  
ATOM   2309  CB  ILE A 334     -24.220   5.121   3.748  1.00138.18           C  
ANISOU 2309  CB  ILE A 334    19692  16706  16105   4111    759   1517       C  
ATOM   2310  CG1 ILE A 334     -24.078   4.787   2.241  1.00140.25           C  
ANISOU 2310  CG1 ILE A 334    20260  16920  16109   4264    656   1583       C  
ATOM   2311  CG2 ILE A 334     -23.678   6.532   4.048  1.00140.37           C  
ANISOU 2311  CG2 ILE A 334    20374  16672  16287   4046   1055   1597       C  
ATOM   2312  CD1 ILE A 334     -25.191   5.340   1.332  1.00151.20           C  
ANISOU 2312  CD1 ILE A 334    21952  18210  17287   4747    387   1617       C  
ATOM   2313  N   MET A 335     -24.898   3.751   6.668  1.00130.40           N  
ANISOU 2313  N   MET A 335    17571  16215  15760   3748    693   1267       N  
ATOM   2314  CA  MET A 335     -25.274   3.826   8.082  1.00129.05           C  
ANISOU 2314  CA  MET A 335    17093  16131  15810   3645    741   1184       C  
ATOM   2315  C   MET A 335     -24.339   2.963   8.940  1.00130.28           C  
ANISOU 2315  C   MET A 335    16971  16426  16104   3273    881   1147       C  
ATOM   2316  O   MET A 335     -24.033   3.336  10.073  1.00128.95           O  
ANISOU 2316  O   MET A 335    16718  16240  16039   3100   1036   1118       O  
ATOM   2317  CB  MET A 335     -26.735   3.396   8.277  1.00131.92           C  
ANISOU 2317  CB  MET A 335    17142  16669  16314   3888    480   1070       C  
ATOM   2318  N   ASN A 336     -23.882   1.820   8.387  1.00125.86           N  
ANISOU 2318  N   ASN A 336    16287  16000  15534   3168    817   1144       N  
ATOM   2319  CA  ASN A 336     -22.959   0.887   9.038  1.00123.42           C  
ANISOU 2319  CA  ASN A 336    15737  15823  15333   2858    915   1109       C  
ATOM   2320  C   ASN A 336     -21.501   1.363   8.948  1.00127.32           C  
ANISOU 2320  C   ASN A 336    16454  16184  15740   2624   1162   1153       C  
ATOM   2321  O   ASN A 336     -20.668   0.915   9.739  1.00125.26           O  
ANISOU 2321  O   ASN A 336    16011  16005  15575   2375   1266   1105       O  
ATOM   2322  CB  ASN A 336     -23.100  -0.521   8.440  1.00123.50           C  
ANISOU 2322  CB  ASN A 336    15534  16017  15373   2860    747   1077       C  
ATOM   2323  CG  ASN A 336     -24.318  -1.297   8.893  1.00146.57           C  
ANISOU 2323  CG  ASN A 336    18118  19116  18454   2964    562    981       C  
ATOM   2324  OD1 ASN A 336     -25.381  -0.742   9.205  1.00142.10           O  
ANISOU 2324  OD1 ASN A 336    17507  18539  17946   3147    485    936       O  
ATOM   2325  ND2 ASN A 336     -24.197  -2.616   8.905  1.00137.08           N  
ANISOU 2325  ND2 ASN A 336    16672  18076  17336   2847    498    935       N  
ATOM   2326  N   GLN A 337     -21.198   2.265   7.984  1.00126.00           N  
ANISOU 2326  N   GLN A 337    16684  15805  15386   2709   1258   1229       N  
ATOM   2327  CA  GLN A 337     -19.861   2.826   7.760  1.00126.32           C  
ANISOU 2327  CA  GLN A 337    16970  15687  15339   2483   1530   1249       C  
ATOM   2328  C   GLN A 337     -19.406   3.717   8.921  1.00130.15           C  
ANISOU 2328  C   GLN A 337    17456  16083  15910   2307   1735   1203       C  
ATOM   2329  O   GLN A 337     -18.272   3.575   9.382  1.00128.87           O  
ANISOU 2329  O   GLN A 337    17202  15951  15811   2029   1902   1136       O  
ATOM   2330  CB  GLN A 337     -19.797   3.586   6.426  1.00130.19           C  
ANISOU 2330  CB  GLN A 337    17933  15943  15589   2635   1598   1346       C  
ATOM   2331  N   ALA A 338     -20.291   4.619   9.397  1.00127.74           N  
ANISOU 2331  N   ALA A 338    17243  15677  15615   2476   1714   1219       N  
ATOM   2332  CA  ALA A 338     -20.002   5.515  10.516  1.00127.64           C  
ANISOU 2332  CA  ALA A 338    17243  15575  15681   2333   1898   1169       C  
ATOM   2333  C   ALA A 338     -20.157   4.758  11.839  1.00129.26           C  
ANISOU 2333  C   ALA A 338    17025  16009  16077   2214   1815   1078       C  
ATOM   2334  O   ALA A 338     -21.271   4.379  12.216  1.00128.42           O  
ANISOU 2334  O   ALA A 338    16724  16018  16052   2382   1635   1067       O  
ATOM   2335  CB  ALA A 338     -20.920   6.728  10.475  1.00130.52           C  
ANISOU 2335  CB  ALA A 338    17880  15735  15975   2579   1904   1220       C  
ATOM   2336  N   SER A 339     -19.025   4.504  12.516  1.00124.57           N  
ANISOU 2336  N   SER A 339    16295  15485  15553   1927   1948    999       N  
ATOM   2337  CA  SER A 339     -18.969   3.767  13.779  1.00122.50           C  
ANISOU 2337  CA  SER A 339    15687  15423  15434   1801   1885    915       C  
ATOM   2338  C   SER A 339     -19.344   4.613  14.995  1.00126.52           C  
ANISOU 2338  C   SER A 339    16186  15879  16007   1784   1964    866       C  
ATOM   2339  O   SER A 339     -20.039   4.116  15.879  1.00125.11           O  
ANISOU 2339  O   SER A 339    15781  15833  15920   1825   1857    835       O  
ATOM   2340  CB  SER A 339     -17.588   3.147  13.973  1.00125.12           C  
ANISOU 2340  CB  SER A 339    15888  15855  15797   1541   1964    836       C  
ATOM   2341  OG  SER A 339     -16.572   4.137  13.984  1.00135.20           O  
ANISOU 2341  OG  SER A 339    17352  16977  17039   1361   2202    776       O  
ATOM   2342  N   GLU A 340     -18.883   5.881  15.034  1.00124.53           N  
ANISOU 2342  N   GLU A 340    16192  15421  15703   1711   2170    850       N  
ATOM   2343  CA  GLU A 340     -19.096   6.840  16.126  1.00124.95           C  
ANISOU 2343  CA  GLU A 340    16283  15389  15805   1673   2283    791       C  
ATOM   2344  C   GLU A 340     -20.576   7.196  16.396  1.00129.10           C  
ANISOU 2344  C   GLU A 340    16810  15882  16359   1936   2173    833       C  
ATOM   2345  O   GLU A 340     -20.905   7.573  17.522  1.00128.62           O  
ANISOU 2345  O   GLU A 340    16665  15834  16372   1904   2216    769       O  
ATOM   2346  CB  GLU A 340     -18.250   8.119  15.913  1.00128.21           C  
ANISOU 2346  CB  GLU A 340    17009  15557  16150   1533   2551    761       C  
ATOM   2347  CG  GLU A 340     -18.701   9.061  14.797  1.00141.34           C  
ANISOU 2347  CG  GLU A 340    19071  16955  17679   1727   2625    872       C  
ATOM   2348  CD  GLU A 340     -18.566   8.591  13.359  1.00163.14           C  
ANISOU 2348  CD  GLU A 340    21981  19686  20320   1822   2566    969       C  
ATOM   2349  OE1 GLU A 340     -17.637   7.805  13.062  1.00158.08           O  
ANISOU 2349  OE1 GLU A 340    21209  19163  19691   1639   2584    928       O  
ATOM   2350  OE2 GLU A 340     -19.381   9.036  12.519  1.00158.46           O  
ANISOU 2350  OE2 GLU A 340    21650  18946  19612   2093   2500   1077       O  
ATOM   2351  N   PHE A 341     -21.450   7.083  15.376  1.00126.13           N  
ANISOU 2351  N   PHE A 341    16524  15473  15928   2198   2030    920       N  
ATOM   2352  CA  PHE A 341     -22.874   7.407  15.490  1.00126.76           C  
ANISOU 2352  CA  PHE A 341    16581  15534  16047   2478   1904    930       C  
ATOM   2353  C   PHE A 341     -23.731   6.243  15.994  1.00128.88           C  
ANISOU 2353  C   PHE A 341    16473  16049  16446   2532   1716    879       C  
ATOM   2354  O   PHE A 341     -24.662   6.470  16.767  1.00128.75           O  
ANISOU 2354  O   PHE A 341    16333  16060  16526   2627   1692    821       O  
ATOM   2355  CB  PHE A 341     -23.418   7.935  14.155  1.00130.58           C  
ANISOU 2355  CB  PHE A 341    17360  15857  16397   2765   1825   1023       C  
ATOM   2356  N   TYR A 342     -23.426   5.007  15.550  1.00123.88           N  
ANISOU 2356  N   TYR A 342    15669  15582  15820   2466   1603    890       N  
ATOM   2357  CA  TYR A 342     -24.180   3.803  15.910  1.00122.47           C  
ANISOU 2357  CA  TYR A 342    15159  15617  15759   2495   1447    839       C  
ATOM   2358  C   TYR A 342     -23.591   2.994  17.077  1.00124.38           C  
ANISOU 2358  C   TYR A 342    15183  16002  16075   2244   1506    784       C  
ATOM   2359  O   TYR A 342     -24.335   2.255  17.725  1.00123.36           O  
ANISOU 2359  O   TYR A 342    14821  16002  16048   2254   1442    731       O  
ATOM   2360  CB  TYR A 342     -24.373   2.905  14.679  1.00123.51           C  
ANISOU 2360  CB  TYR A 342    15246  15833  15849   2609   1273    877       C  
ATOM   2361  N   LEU A 343     -22.270   3.106  17.335  1.00120.21           N  
ANISOU 2361  N   LEU A 343    14732  15448  15493   2027   1627    784       N  
ATOM   2362  CA  LEU A 343     -21.610   2.358  18.413  1.00118.55           C  
ANISOU 2362  CA  LEU A 343    14347  15372  15327   1821   1654    726       C  
ATOM   2363  C   LEU A 343     -20.648   3.188  19.264  1.00122.69           C  
ANISOU 2363  C   LEU A 343    14966  15826  15825   1641   1815    666       C  
ATOM   2364  O   LEU A 343     -20.079   4.170  18.782  1.00123.30           O  
ANISOU 2364  O   LEU A 343    15251  15752  15844   1606   1934    672       O  
ATOM   2365  CB  LEU A 343     -20.896   1.109  17.863  1.00117.34           C  
ANISOU 2365  CB  LEU A 343    14082  15344  15157   1740   1563    744       C  
ATOM   2366  CG  LEU A 343     -21.784  -0.083  17.496  1.00121.42           C  
ANISOU 2366  CG  LEU A 343    14419  15986  15729   1850   1406    762       C  
ATOM   2367  CD1 LEU A 343     -21.083  -1.006  16.525  1.00120.90           C  
ANISOU 2367  CD1 LEU A 343    14329  15984  15622   1814   1329    796       C  
ATOM   2368  CD2 LEU A 343     -22.228  -0.848  18.730  1.00123.11           C  
ANISOU 2368  CD2 LEU A 343    14445  16310  16020   1784   1397    711       C  
ATOM   2369  N   ALA A 344     -20.467   2.783  20.536  1.00118.55           N  
ANISOU 2369  N   ALA A 344    14305  15404  15334   1523   1826    599       N  
ATOM   2370  CA  ALA A 344     -19.574   3.450  21.484  1.00118.73           C  
ANISOU 2370  CA  ALA A 344    14382  15397  15334   1353   1949    510       C  
ATOM   2371  C   ALA A 344     -18.256   2.699  21.631  1.00121.78           C  
ANISOU 2371  C   ALA A 344    14673  15903  15694   1188   1914    452       C  
ATOM   2372  O   ALA A 344     -18.244   1.466  21.657  1.00120.20           O  
ANISOU 2372  O   ALA A 344    14329  15841  15503   1200   1789    474       O  
ATOM   2373  CB  ALA A 344     -20.248   3.584  22.837  1.00119.62           C  
ANISOU 2373  CB  ALA A 344    14436  15538  15477   1352   1978    459       C  
ATOM   2374  N   SER A 345     -17.150   3.451  21.736  1.00119.22           N  
ANISOU 2374  N   SER A 345    14428  15523  15348   1035   2030    360       N  
ATOM   2375  CA  SER A 345     -15.805   2.901  21.891  1.00118.83           C  
ANISOU 2375  CA  SER A 345    14269  15590  15292    881   2002    258       C  
ATOM   2376  C   SER A 345     -15.358   2.933  23.351  1.00122.93           C  
ANISOU 2376  C   SER A 345    14709  16199  15799    783   1989    131       C  
ATOM   2377  O   SER A 345     -15.571   3.933  24.041  1.00123.39           O  
ANISOU 2377  O   SER A 345    14858  16170  15853    746   2098     76       O  
ATOM   2378  CB  SER A 345     -14.810   3.653  21.011  1.00123.54           C  
ANISOU 2378  CB  SER A 345    14977  16079  15885    758   2148    198       C  
ATOM   2379  OG  SER A 345     -14.784   5.039  21.315  1.00133.92           O  
ANISOU 2379  OG  SER A 345    16459  17229  17197    688   2330    138       O  
ATOM   2380  N   SER A 346     -14.743   1.832  23.817  1.00118.86           N  
ANISOU 2380  N   SER A 346    14041  15853  15265    758   1850     83       N  
ATOM   2381  CA  SER A 346     -14.234   1.695  25.182  1.00119.10           C  
ANISOU 2381  CA  SER A 346    14011  15990  15253    696   1794    -42       C  
ATOM   2382  C   SER A 346     -12.697   1.800  25.199  1.00123.83           C  
ANISOU 2382  C   SER A 346    14517  16670  15864    554   1785   -229       C  
ATOM   2383  O   SER A 346     -12.045   1.147  24.379  1.00123.09           O  
ANISOU 2383  O   SER A 346    14333  16637  15799    543   1731   -236       O  
ATOM   2384  CB  SER A 346     -14.697   0.380  25.803  1.00121.71           C  
ANISOU 2384  CB  SER A 346    14272  16438  15534    798   1636     29       C  
ATOM   2385  OG  SER A 346     -14.311  -0.737  25.019  1.00129.62           O  
ANISOU 2385  OG  SER A 346    15178  17521  16549    839   1523     77       O  
ATOM   2386  N   PRO A 347     -12.095   2.622  26.097  1.00121.66           N  
ANISOU 2386  N   PRO A 347    14247  16402  15577    439   1843   -403       N  
ATOM   2387  CA  PRO A 347     -10.626   2.747  26.101  1.00126.23           C  
ANISOU 2387  CA  PRO A 347    14697  17073  16192    296   1836   -628       C  
ATOM   2388  C   PRO A 347      -9.910   1.531  26.686  1.00158.75           C  
ANISOU 2388  C   PRO A 347    18649  21401  20266    357   1602   -711       C  
ATOM   2389  O   PRO A 347      -8.806   1.201  26.258  1.00121.36           O  
ANISOU 2389  O   PRO A 347    13764  16764  15585    295   1555   -854       O  
ATOM   2390  CB  PRO A 347     -10.380   4.009  26.929  1.00129.04           C  
ANISOU 2390  CB  PRO A 347    15115  17365  16548    166   1966   -795       C  
ATOM   2391  CG  PRO A 347     -11.542   4.087  27.847  1.00131.81           C  
ANISOU 2391  CG  PRO A 347    15581  17677  16822    276   1942   -678       C  
ATOM   2392  CD  PRO A 347     -12.715   3.485  27.125  1.00124.91           C  
ANISOU 2392  CD  PRO A 347    14769  16742  15951    430   1922   -429       C  
ATOM   2393  N   LEU A 364      -8.886  13.054  24.500  1.00128.52           N  
ANISOU 2393  N   LEU A 364    16243  15809  16781   -922   3876  -1371       N  
ATOM   2394  CA  LEU A 364     -10.241  13.237  23.989  1.00127.31           C  
ANISOU 2394  CA  LEU A 364    16352  15476  16543   -671   3869  -1063       C  
ATOM   2395  C   LEU A 364     -11.029  14.245  24.828  1.00131.84           C  
ANISOU 2395  C   LEU A 364    17103  15897  17094   -622   3956  -1053       C  
ATOM   2396  O   LEU A 364     -11.031  14.156  26.059  1.00131.23           O  
ANISOU 2396  O   LEU A 364    16864  15972  17024   -645   3841  -1176       O  
ATOM   2397  CB  LEU A 364     -10.979  11.892  23.929  1.00124.71           C  
ANISOU 2397  CB  LEU A 364    15861  15354  16169   -419   3552   -860       C  
ATOM   2398  N   LYS A 365     -11.692  15.207  24.154  1.00129.32           N  
ANISOU 2398  N   LYS A 365    17133  15268  16734   -542   4157   -911       N  
ATOM   2399  CA  LYS A 365     -12.503  16.255  24.783  1.00130.02           C  
ANISOU 2399  CA  LYS A 365    17433  15165  16803   -470   4266   -887       C  
ATOM   2400  C   LYS A 365     -13.797  15.673  25.378  1.00131.53           C  
ANISOU 2400  C   LYS A 365    17531  15484  16960   -186   4014   -718       C  
ATOM   2401  O   LYS A 365     -14.416  14.825  24.732  1.00129.47           O  
ANISOU 2401  O   LYS A 365    17222  15303  16670     19   3837   -526       O  
ATOM   2402  CB  LYS A 365     -12.826  17.368  23.774  1.00134.52           C  
ANISOU 2402  CB  LYS A 365    18431  15355  17326   -428   4538   -770       C  
ATOM   2403  N   PRO A 366     -14.227  16.101  26.593  1.00128.05           N  
ANISOU 2403  N   PRO A 366    17063  15064  16527   -180   4008   -800       N  
ATOM   2404  CA  PRO A 366     -15.453  15.527  27.182  1.00126.12           C  
ANISOU 2404  CA  PRO A 366    16723  14937  16259     65   3803   -663       C  
ATOM   2405  C   PRO A 366     -16.747  15.897  26.459  1.00129.58           C  
ANISOU 2405  C   PRO A 366    17374  15182  16679    345   3817   -445       C  
ATOM   2406  O   PRO A 366     -16.891  17.023  25.980  1.00131.00           O  
ANISOU 2406  O   PRO A 366    17850  15077  16848    364   4022   -423       O  
ATOM   2407  CB  PRO A 366     -15.437  16.052  28.620  1.00128.72           C  
ANISOU 2407  CB  PRO A 366    17011  15303  16593    -37   3848   -838       C  
ATOM   2408  CG  PRO A 366     -14.650  17.305  28.557  1.00135.63           C  
ANISOU 2408  CG  PRO A 366    18076  15961  17496   -259   4125  -1008       C  
ATOM   2409  CD  PRO A 366     -13.605  17.088  27.502  1.00131.51           C  
ANISOU 2409  CD  PRO A 366    17546  15425  16997   -410   4194  -1043       C  
ATOM   2410  N   HIS A 367     -17.686  14.933  26.386  1.00124.01           N  
ANISOU 2410  N   HIS A 367    16519  14629  15971    567   3596   -299       N  
ATOM   2411  CA  HIS A 367     -19.002  15.082  25.758  1.00123.75           C  
ANISOU 2411  CA  HIS A 367    16608  14477  15936    865   3545   -121       C  
ATOM   2412  C   HIS A 367     -19.880  16.019  26.612  1.00128.56           C  
ANISOU 2412  C   HIS A 367    17322  14954  16570    960   3642   -163       C  
ATOM   2413  O   HIS A 367     -19.829  15.923  27.842  1.00127.86           O  
ANISOU 2413  O   HIS A 367    17095  14987  16498    853   3639   -283       O  
ATOM   2414  CB  HIS A 367     -19.668  13.703  25.607  1.00122.38           C  
ANISOU 2414  CB  HIS A 367    16184  14540  15777   1024   3290    -14       C  
ATOM   2415  CG  HIS A 367     -20.858  13.681  24.702  1.00125.91           C  
ANISOU 2415  CG  HIS A 367    16708  14904  16229   1325   3201    143       C  
ATOM   2416  ND1 HIS A 367     -22.119  14.008  25.161  1.00128.23           N  
ANISOU 2416  ND1 HIS A 367    16992  15159  16571   1529   3177    157       N  
ATOM   2417  CD2 HIS A 367     -20.942  13.347  23.394  1.00127.48           C  
ANISOU 2417  CD2 HIS A 367    16980  15067  16391   1457   3119    269       C  
ATOM   2418  CE1 HIS A 367     -22.925  13.876  24.121  1.00127.92           C  
ANISOU 2418  CE1 HIS A 367    17006  15070  16530   1787   3066    278       C  
ATOM   2419  NE2 HIS A 367     -22.262  13.479  23.036  1.00127.82           N  
ANISOU 2419  NE2 HIS A 367    17056  15055  16455   1756   3023    355       N  
ATOM   2420  N   PRO A 368     -20.680  16.932  26.001  1.00126.47           N  
ANISOU 2420  N   PRO A 368    17315  14438  16299   1172   3726    -72       N  
ATOM   2421  CA  PRO A 368     -21.502  17.854  26.812  1.00127.62           C  
ANISOU 2421  CA  PRO A 368    17560  14451  16480   1271   3827   -126       C  
ATOM   2422  C   PRO A 368     -22.600  17.200  27.655  1.00130.22           C  
ANISOU 2422  C   PRO A 368    17637  14972  16871   1416   3679   -131       C  
ATOM   2423  O   PRO A 368     -23.009  17.783  28.660  1.00130.60           O  
ANISOU 2423  O   PRO A 368    17698  14975  16949   1405   3775   -229       O  
ATOM   2424  CB  PRO A 368     -22.087  18.822  25.775  1.00131.42           C  
ANISOU 2424  CB  PRO A 368    18379  14625  16928   1511   3910    -11       C  
ATOM   2425  CG  PRO A 368     -21.259  18.640  24.549  1.00135.86           C  
ANISOU 2425  CG  PRO A 368    19084  15119  17416   1445   3931     71       C  
ATOM   2426  CD  PRO A 368     -20.847  17.209  24.562  1.00128.86           C  
ANISOU 2426  CD  PRO A 368    17859  14554  16548   1343   3735     75       C  
ATOM   2427  N   GLU A 369     -23.070  16.000  27.256  1.00125.01           N  
ANISOU 2427  N   GLU A 369    16754  14514  16230   1537   3467    -41       N  
ATOM   2428  CA  GLU A 369     -24.116  15.260  27.969  1.00123.92           C  
ANISOU 2428  CA  GLU A 369    16370  14557  16159   1652   3350    -54       C  
ATOM   2429  C   GLU A 369     -23.572  14.328  29.074  1.00126.05           C  
ANISOU 2429  C   GLU A 369    16423  15065  16407   1430   3306   -139       C  
ATOM   2430  O   GLU A 369     -24.359  13.620  29.710  1.00124.96           O  
ANISOU 2430  O   GLU A 369    16101  15070  16307   1490   3238   -152       O  
ATOM   2431  CB  GLU A 369     -25.019  14.499  26.983  1.00124.72           C  
ANISOU 2431  CB  GLU A 369    16353  14733  16302   1905   3161     63       C  
ATOM   2432  N   ARG A 370     -22.243  14.356  29.329  1.00122.21           N  
ANISOU 2432  N   ARG A 370    15969  14611  15856   1181   3354   -213       N  
ATOM   2433  CA  ARG A 370     -21.609  13.544  30.374  1.00120.95           C  
ANISOU 2433  CA  ARG A 370    15641  14666  15647    996   3291   -305       C  
ATOM   2434  C   ARG A 370     -21.903  14.126  31.755  1.00126.07           C  
ANISOU 2434  C   ARG A 370    16326  15295  16282    933   3405   -434       C  
ATOM   2435  O   ARG A 370     -21.658  15.312  31.992  1.00127.12           O  
ANISOU 2435  O   ARG A 370    16631  15255  16416    866   3569   -523       O  
ATOM   2436  CB  ARG A 370     -20.093  13.401  30.140  1.00120.65           C  
ANISOU 2436  CB  ARG A 370    15599  14684  15559    778   3282   -374       C  
ATOM   2437  CG  ARG A 370     -19.721  12.365  29.081  1.00128.51           C  
ANISOU 2437  CG  ARG A 370    16485  15790  16552    809   3131   -265       C  
ATOM   2438  CD  ARG A 370     -19.582  10.962  29.644  1.00135.26           C  
ANISOU 2438  CD  ARG A 370    17121  16900  17373    782   2951   -264       C  
ATOM   2439  NE  ARG A 370     -19.479   9.961  28.581  1.00141.12           N  
ANISOU 2439  NE  ARG A 370    17763  17729  18126    852   2811   -145       N  
ATOM   2440  CZ  ARG A 370     -19.398   8.650  28.785  1.00153.28           C  
ANISOU 2440  CZ  ARG A 370    19135  19463  19642    857   2652   -112       C  
ATOM   2441  NH1 ARG A 370     -19.404   8.161  30.020  1.00140.40           N  
ANISOU 2441  NH1 ARG A 370    17437  17954  17956    806   2611   -180       N  
ATOM   2442  NH2 ARG A 370     -19.312   7.817  27.757  1.00138.57           N  
ANISOU 2442  NH2 ARG A 370    17195  17661  17796    919   2540    -11       N  
ATOM   2443  N   MET A 371     -22.454  13.290  32.652  1.00122.25           N  
ANISOU 2443  N   MET A 371    15699  14972  15777    952   3335   -447       N  
ATOM   2444  CA  MET A 371     -22.849  13.676  34.010  1.00123.19           C  
ANISOU 2444  CA  MET A 371    15853  15089  15865    904   3441   -563       C  
ATOM   2445  C   MET A 371     -21.719  13.535  35.040  1.00127.60           C  
ANISOU 2445  C   MET A 371    16419  15763  16300    687   3424   -702       C  
ATOM   2446  O   MET A 371     -20.980  12.548  34.987  1.00126.05           O  
ANISOU 2446  O   MET A 371    16119  15735  16041    620   3273   -687       O  
ATOM   2447  CB  MET A 371     -24.095  12.893  34.462  1.00125.11           C  
ANISOU 2447  CB  MET A 371    15969  15423  16143   1032   3414   -518       C  
ATOM   2448  CG  MET A 371     -25.336  13.239  33.673  1.00129.22           C  
ANISOU 2448  CG  MET A 371    16464  15833  16801   1262   3439   -446       C  
ATOM   2449  SD  MET A 371     -26.868  12.791  34.508  1.00134.00           S  
ANISOU 2449  SD  MET A 371    16934  16495  17484   1371   3509   -494       S  
ATOM   2450  CE  MET A 371     -28.048  13.492  33.387  1.00131.80           C  
ANISOU 2450  CE  MET A 371    16629  16072  17376   1662   3505   -451       C  
ATOM   2451  N   PRO A 372     -21.580  14.490  35.997  1.00126.05           N  
ANISOU 2451  N   PRO A 372    16343  15484  16066    590   3564   -849       N  
ATOM   2452  CA  PRO A 372     -20.515  14.370  37.011  1.00126.49           C  
ANISOU 2452  CA  PRO A 372    16401  15665  15994    402   3521  -1010       C  
ATOM   2453  C   PRO A 372     -20.788  13.248  38.024  1.00130.15           C  
ANISOU 2453  C   PRO A 372    16800  16315  16337    420   3413  -1003       C  
ATOM   2454  O   PRO A 372     -21.960  12.936  38.254  1.00129.52           O  
ANISOU 2454  O   PRO A 372    16709  16218  16286    539   3466   -924       O  
ATOM   2455  CB  PRO A 372     -20.503  15.751  37.689  1.00130.24           C  
ANISOU 2455  CB  PRO A 372    17037  15977  16471    317   3717  -1166       C  
ATOM   2456  CG  PRO A 372     -21.380  16.633  36.845  1.00135.16           C  
ANISOU 2456  CG  PRO A 372    17759  16369  17227    459   3861  -1074       C  
ATOM   2457  CD  PRO A 372     -22.368  15.720  36.207  1.00129.24           C  
ANISOU 2457  CD  PRO A 372    16889  15680  16537    659   3757   -893       C  
ATOM   2458  N   PRO A 373     -19.746  12.624  38.638  1.00127.01           N  
ANISOU 2458  N   PRO A 373    16368  16088  15801    313   3269  -1095       N  
ATOM   2459  CA  PRO A 373     -20.005  11.531  39.597  1.00126.67           C  
ANISOU 2459  CA  PRO A 373    16326  16194  15610    349   3172  -1072       C  
ATOM   2460  C   PRO A 373     -20.722  11.961  40.877  1.00132.00           C  
ANISOU 2460  C   PRO A 373    17139  16818  16195    341   3316  -1154       C  
ATOM   2461  O   PRO A 373     -20.454  13.041  41.407  1.00132.98           O  
ANISOU 2461  O   PRO A 373    17359  16864  16304    253   3423  -1306       O  
ATOM   2462  CB  PRO A 373     -18.611  10.966  39.882  1.00128.55           C  
ANISOU 2462  CB  PRO A 373    16519  16605  15719    261   2970  -1176       C  
ATOM   2463  CG  PRO A 373     -17.683  12.089  39.602  1.00134.00           C  
ANISOU 2463  CG  PRO A 373    17205  17233  16475    125   3025  -1341       C  
ATOM   2464  CD  PRO A 373     -18.295  12.851  38.466  1.00129.05           C  
ANISOU 2464  CD  PRO A 373    16589  16411  16033    165   3186  -1236       C  
ATOM   2465  N   LEU A 374     -21.640  11.104  41.361  1.00128.37           N  
ANISOU 2465  N   LEU A 374    16697  16397  15681    422   3339  -1062       N  
ATOM   2466  CA  LEU A 374     -22.445  11.323  42.564  1.00129.66           C  
ANISOU 2466  CA  LEU A 374    16997  16514  15754    418   3500  -1126       C  
ATOM   2467  C   LEU A 374     -21.601  11.198  43.838  1.00135.06           C  
ANISOU 2467  C   LEU A 374    17831  17299  16186    328   3421  -1266       C  
ATOM   2468  O   LEU A 374     -20.762  10.299  43.936  1.00134.25           O  
ANISOU 2468  O   LEU A 374    17721  17340  15947    327   3216  -1254       O  
ATOM   2469  CB  LEU A 374     -23.617  10.324  42.593  1.00129.15           C  
ANISOU 2469  CB  LEU A 374    16896  16459  15716    509   3563   -997       C  
ATOM   2470  N   ILE A 375     -21.837  12.099  44.811  1.00133.50           N  
ANISOU 2470  N   ILE A 375    17776  17025  15921    270   3575  -1407       N  
ATOM   2471  CA  ILE A 375     -21.131  12.123  46.098  1.00135.07           C  
ANISOU 2471  CA  ILE A 375    18144  17310  15865    196   3508  -1566       C  
ATOM   2472  C   ILE A 375     -21.988  11.439  47.174  1.00139.88           C  
ANISOU 2472  C   ILE A 375    18932  17920  16296    236   3613  -1525       C  
ATOM   2473  O   ILE A 375     -23.168  11.769  47.322  1.00139.84           O  
ANISOU 2473  O   ILE A 375    18950  17793  16388    257   3850  -1497       O  
ATOM   2474  CB  ILE A 375     -20.694  13.568  46.502  1.00139.83           C  
ANISOU 2474  CB  ILE A 375    18809  17832  16488     85   3607  -1775       C  
ATOM   2475  CG1 ILE A 375     -19.945  14.280  45.347  1.00139.56           C  
ANISOU 2475  CG1 ILE A 375    18624  17752  16650     27   3568  -1810       C  
ATOM   2476  CG2 ILE A 375     -19.843  13.557  47.788  1.00142.54           C  
ANISOU 2476  CG2 ILE A 375    19308  18294  16557     15   3490  -1968       C  
ATOM   2477  CD1 ILE A 375     -19.939  15.814  45.410  1.00148.39           C  
ANISOU 2477  CD1 ILE A 375    19806  18701  17873    -68   3762  -1964       C  
ATOM   2478  N   ALA A 376     -21.387  10.486  47.915  1.00137.02           N  
ANISOU 2478  N   ALA A 376    18705  17689  15670    253   3443  -1531       N  
ATOM   2479  CA  ALA A 376     -22.045   9.732  48.985  1.00169.58           C  
ANISOU 2479  CA  ALA A 376    23062  21802  19568    284   3540  -1489       C  
ATOM   2480  C   ALA A 376     -22.311  10.600  50.217  1.00199.93           C  
ANISOU 2480  C   ALA A 376    27121  25579  23265    219   3713  -1653       C  
ATOM   2481  O   ALA A 376     -21.492  11.446  50.576  1.00161.85           O  
ANISOU 2481  O   ALA A 376    22324  20791  18382    157   3631  -1831       O  
ATOM   2482  CB  ALA A 376     -21.204   8.525  49.367  1.00170.59           C  
ANISOU 2482  CB  ALA A 376    23312  22071  19432    346   3284  -1448       C  
ATOM   2483  N   LYS A 399     -18.250   6.040  45.460  1.00136.62           N  
ANISOU 2483  N   LYS A 399    18269  18157  15484    528   2416  -1175       N  
ATOM   2484  CA  LYS A 399     -18.047   4.637  45.115  1.00135.54           C  
ANISOU 2484  CA  LYS A 399    18132  18091  15276    633   2253  -1032       C  
ATOM   2485  C   LYS A 399     -18.985   4.196  43.991  1.00137.10           C  
ANISOU 2485  C   LYS A 399    18181  18205  15706    646   2383   -840       C  
ATOM   2486  O   LYS A 399     -20.191   4.450  44.057  1.00136.56           O  
ANISOU 2486  O   LYS A 399    18144  18015  15728    621   2625   -778       O  
ATOM   2487  CB  LYS A 399     -18.220   3.741  46.352  1.00139.84           C  
ANISOU 2487  CB  LYS A 399    18994  18642  15498    715   2224   -998       C  
ATOM   2488  N   LYS A 400     -18.425   3.540  42.958  1.00132.01           N  
ANISOU 2488  N   LYS A 400    17362  17634  15163    690   2216   -766       N  
ATOM   2489  CA  LYS A 400     -19.175   3.051  41.800  1.00129.81           C  
ANISOU 2489  CA  LYS A 400    16929  17300  15095    713   2293   -600       C  
ATOM   2490  C   LYS A 400     -19.747   1.656  42.048  1.00133.33           C  
ANISOU 2490  C   LYS A 400    17501  17730  15428    783   2305   -455       C  
ATOM   2491  O   LYS A 400     -19.025   0.763  42.499  1.00133.58           O  
ANISOU 2491  O   LYS A 400    17659  17837  15256    853   2125   -446       O  
ATOM   2492  CB  LYS A 400     -18.298   3.064  40.538  1.00130.92           C  
ANISOU 2492  CB  LYS A 400    16837  17512  15393    713   2132   -599       C  
ATOM   2493  N   ALA A 401     -21.050   1.478  41.758  1.00129.07           N  
ANISOU 2493  N   ALA A 401    16931  17086  15024    769   2520   -357       N  
ATOM   2494  CA  ALA A 401     -21.764   0.208  41.921  1.00128.83           C  
ANISOU 2494  CA  ALA A 401    17008  17012  14930    799   2598   -235       C  
ATOM   2495  C   ALA A 401     -21.421  -0.759  40.786  1.00130.60           C  
ANISOU 2495  C   ALA A 401    17075  17291  15254    855   2441   -126       C  
ATOM   2496  O   ALA A 401     -21.248  -0.329  39.643  1.00128.63           O  
ANISOU 2496  O   ALA A 401    16588  17073  15213    855   2379   -119       O  
ATOM   2497  CB  ALA A 401     -23.262   0.454  41.967  1.00129.84           C  
ANISOU 2497  CB  ALA A 401    17104  17023  15208    748   2893   -220       C  
ATOM   2498  N   LYS A 402     -21.319  -2.064  41.104  1.00127.31           N  
ANISOU 2498  N   LYS A 402    16821  16874  14677    904   2388    -40       N  
ATOM   2499  CA  LYS A 402     -20.973  -3.097  40.125  1.00125.65           C  
ANISOU 2499  CA  LYS A 402    16494  16709  14538    961   2242     60       C  
ATOM   2500  C   LYS A 402     -22.061  -4.156  39.940  1.00129.15           C  
ANISOU 2500  C   LYS A 402    16977  17057  15035    941   2418    168       C  
ATOM   2501  O   LYS A 402     -22.479  -4.794  40.909  1.00130.26           O  
ANISOU 2501  O   LYS A 402    17387  17112  14992    929   2551    196       O  
ATOM   2502  CB  LYS A 402     -19.618  -3.745  40.458  1.00128.77           C  
ANISOU 2502  CB  LYS A 402    17011  17201  14716   1060   1967     47       C  
ATOM   2503  N   TRP A 403     -22.502  -4.342  38.681  1.00123.89           N  
ANISOU 2503  N   TRP A 403    16055  16401  14618    933   2424    217       N  
ATOM   2504  CA  TRP A 403     -23.525  -5.314  38.284  1.00123.51           C  
ANISOU 2504  CA  TRP A 403    15970  16281  14677    902   2577    287       C  
ATOM   2505  C   TRP A 403     -22.998  -6.748  38.349  1.00127.58           C  
ANISOU 2505  C   TRP A 403    16653  16787  15036    952   2473    381       C  
ATOM   2506  O   TRP A 403     -21.796  -6.971  38.191  1.00126.76           O  
ANISOU 2506  O   TRP A 403    16571  16768  14826   1039   2224    397       O  
ATOM   2507  CB  TRP A 403     -24.024  -5.011  36.864  1.00120.55           C  
ANISOU 2507  CB  TRP A 403    15263  15940  14598    904   2561    291       C  
ATOM   2508  CG  TRP A 403     -24.839  -3.758  36.758  1.00121.59           C  
ANISOU 2508  CG  TRP A 403    15251  16046  14901    877   2698    209       C  
ATOM   2509  CD1 TRP A 403     -24.378  -2.499  36.514  1.00124.02           C  
ANISOU 2509  CD1 TRP A 403    15477  16385  15259    900   2623    156       C  
ATOM   2510  CD2 TRP A 403     -26.263  -3.651  36.872  1.00122.31           C  
ANISOU 2510  CD2 TRP A 403    15262  16067  15145    829   2942    154       C  
ATOM   2511  NE1 TRP A 403     -25.426  -1.610  36.477  1.00123.95           N  
ANISOU 2511  NE1 TRP A 403    15366  16320  15410    890   2793     89       N  
ATOM   2512  CE2 TRP A 403     -26.596  -2.290  36.694  1.00126.20           C  
ANISOU 2512  CE2 TRP A 403    15630  16553  15768    853   2981     77       C  
ATOM   2513  CE3 TRP A 403     -27.295  -4.575  37.112  1.00124.62           C  
ANISOU 2513  CE3 TRP A 403    15571  16293  15485    764   3145    145       C  
ATOM   2514  CZ2 TRP A 403     -27.916  -1.829  36.753  1.00126.51           C  
ANISOU 2514  CZ2 TRP A 403    15546  16538  15984    839   3189    -11       C  
ATOM   2515  CZ3 TRP A 403     -28.602  -4.118  37.168  1.00127.10           C  
ANISOU 2515  CZ3 TRP A 403    15741  16563  15990    724   3368     39       C  
ATOM   2516  CH2 TRP A 403     -28.903  -2.761  36.987  1.00127.71           C  
ANISOU 2516  CH2 TRP A 403    15678  16649  16195    775   3375    -39       C  
ATOM   2517  N   HIS A 404     -23.904  -7.718  38.565  1.00124.98           N  
ANISOU 2517  N   HIS A 404    16435  16348  14702    897   2675    427       N  
ATOM   2518  CA  HIS A 404     -23.573  -9.145  38.637  1.00125.32           C  
ANISOU 2518  CA  HIS A 404    16676  16339  14599    939   2626    523       C  
ATOM   2519  C   HIS A 404     -24.674 -10.034  38.042  1.00128.94           C  
ANISOU 2519  C   HIS A 404    17041  16713  15238    849   2829    549       C  
ATOM   2520  O   HIS A 404     -25.834  -9.623  37.986  1.00128.78           O  
ANISOU 2520  O   HIS A 404    16876  16653  15401    746   3059    476       O  
ATOM   2521  CB  HIS A 404     -23.180  -9.583  40.064  1.00128.40           C  
ANISOU 2521  CB  HIS A 404    17504  16644  14637    981   2654    550       C  
ATOM   2522  CG  HIS A 404     -23.982  -8.964  41.169  1.00133.54           C  
ANISOU 2522  CG  HIS A 404    18331  17205  15204    889   2920    486       C  
ATOM   2523  ND1 HIS A 404     -25.072  -9.613  41.722  1.00137.02           N  
ANISOU 2523  ND1 HIS A 404    18966  17482  15613    776   3251    498       N  
ATOM   2524  CD2 HIS A 404     -23.795  -7.793  41.822  1.00135.71           C  
ANISOU 2524  CD2 HIS A 404    18626  17525  15413    887   2909    399       C  
ATOM   2525  CE1 HIS A 404     -25.522  -8.812  42.674  1.00137.78           C  
ANISOU 2525  CE1 HIS A 404    19187  17535  15628    715   3431    421       C  
ATOM   2526  NE2 HIS A 404     -24.789  -7.702  42.767  1.00137.36           N  
ANISOU 2526  NE2 HIS A 404    19037  17603  15550    783   3227    363       N  
ATOM   2527  N   LEU A 405     -24.296 -11.239  37.571  1.00125.21           N  
ANISOU 2527  N   LEU A 405    16630  16217  14727    893   2737    633       N  
ATOM   2528  CA  LEU A 405     -25.215 -12.192  36.945  1.00125.14           C  
ANISOU 2528  CA  LEU A 405    16530  16130  14886    803   2910    644       C  
ATOM   2529  C   LEU A 405     -26.129 -12.900  37.953  1.00131.53           C  
ANISOU 2529  C   LEU A 405    17637  16753  15585    682   3251    638       C  
ATOM   2530  O   LEU A 405     -25.653 -13.674  38.787  1.00132.61           O  
ANISOU 2530  O   LEU A 405    18166  16779  15440    726   3266    719       O  
ATOM   2531  CB  LEU A 405     -24.443 -13.203  36.065  1.00124.15           C  
ANISOU 2531  CB  LEU A 405    16372  16039  14760    889   2696    728       C  
ATOM   2532  CG  LEU A 405     -25.260 -14.277  35.324  1.00128.98           C  
ANISOU 2532  CG  LEU A 405    16888  16575  15542    799   2844    731       C  
ATOM   2533  CD1 LEU A 405     -25.956 -13.707  34.095  1.00127.62           C  
ANISOU 2533  CD1 LEU A 405    16282  16511  15699    754   2833    646       C  
ATOM   2534  CD2 LEU A 405     -24.377 -15.430  34.909  1.00131.16           C  
ANISOU 2534  CD2 LEU A 405    17287  16834  15714    895   2666    829       C  
ATOM   2535  N   GLY A 406     -27.429 -12.619  37.837  1.00128.76           N  
ANISOU 2535  N   GLY A 406    17098  16366  15459    539   3523    531       N  
ATOM   2536  CA  GLY A 406     -28.503 -13.187  38.650  1.00131.11           C  
ANISOU 2536  CA  GLY A 406    17598  16489  15730    377   3914    478       C  
ATOM   2537  C   GLY A 406     -28.300 -13.141  40.150  1.00137.23           C  
ANISOU 2537  C   GLY A 406    18832  17136  16174    370   4059    515       C  
ATOM   2538  O   GLY A 406     -27.814 -12.141  40.688  1.00136.49           O  
ANISOU 2538  O   GLY A 406    18784  17114  15962    445   3939    504       O  
ATOM   2539  N   ILE A 407     -28.672 -14.240  40.829  1.00136.31           N  
ANISOU 2539  N   ILE A 407    19080  16817  15894    277   4326    554       N  
ATOM   2540  CA  ILE A 407     -28.551 -14.403  42.279  1.00138.82           C  
ANISOU 2540  CA  ILE A 407    19920  16972  15853    270   4502    601       C  
ATOM   2541  C   ILE A 407     -27.639 -15.601  42.616  1.00144.04           C  
ANISOU 2541  C   ILE A 407    21032  17510  16185    396   4376    764       C  
ATOM   2542  O   ILE A 407     -27.721 -16.646  41.964  1.00143.44           O  
ANISOU 2542  O   ILE A 407    20944  17365  16192    369   4402    810       O  
ATOM   2543  CB  ILE A 407     -29.951 -14.441  42.979  1.00144.47           C  
ANISOU 2543  CB  ILE A 407    20725  17522  16643     34   5008    478       C  
ATOM   2544  CG1 ILE A 407     -29.845 -14.312  44.518  1.00147.63           C  
ANISOU 2544  CG1 ILE A 407    21660  17769  16662     29   5194    512       C  
ATOM   2545  CG2 ILE A 407     -30.803 -15.653  42.573  1.00146.41           C  
ANISOU 2545  CG2 ILE A 407    20969  17617  17045   -141   5309    443       C  
ATOM   2546  CD1 ILE A 407     -29.765 -12.875  45.047  1.00154.43           C  
ANISOU 2546  CD1 ILE A 407    22423  18751  17502     70   5125    432       C  
ATOM   2547  N   ARG A 408     -26.748 -15.423  43.611  1.00142.05           N  
ANISOU 2547  N   ARG A 408    21172  17239  15563    551   4218    839       N  
ATOM   2548  CA  ARG A 408     -25.793 -16.442  44.055  1.00143.42           C  
ANISOU 2548  CA  ARG A 408    21810  17305  15380    729   4049    984       C  
ATOM   2549  C   ARG A 408     -26.195 -17.098  45.379  1.00151.48           C  
ANISOU 2549  C   ARG A 408    23463  18048  16044    678   4380   1040       C  
ATOM   2550  O   ARG A 408     -26.845 -16.464  46.214  1.00152.49           O  
ANISOU 2550  O   ARG A 408    23711  18116  16111    558   4645    966       O  
ATOM   2551  CB  ARG A 408     -24.377 -15.853  44.156  1.00142.56           C  
ANISOU 2551  CB  ARG A 408    21686  17387  15093    983   3575   1010       C  
ATOM   2552  N   SER A 409     -25.793 -18.369  45.565  1.00150.15           N  
ANISOU 2552  N   SER A 409    23723  17697  15630    777   4371   1173       N  
ATOM   2553  CA  SER A 409     -26.065 -19.166  46.764  1.00154.08           C  
ANISOU 2553  CA  SER A 409    24913  17890  15740    758   4677   1256       C  
ATOM   2554  C   SER A 409     -24.839 -19.999  47.154  1.00160.06           C  
ANISOU 2554  C   SER A 409    26153  18573  16090   1068   4352   1413       C  
ATOM   2555  O   SER A 409     -24.061 -20.391  46.283  1.00157.74           O  
ANISOU 2555  O   SER A 409    25641  18397  15895   1225   4014   1458       O  
ATOM   2556  CB  SER A 409     -27.270 -20.074  46.537  1.00158.97           C  
ANISOU 2556  CB  SER A 409    25599  18271  16533    482   5175   1233       C  
ATOM   2557  OG  SER A 409     -27.638 -20.758  47.723  1.00171.68           O  
ANISOU 2557  OG  SER A 409    27899  19558  17774    423   5543   1302       O  
ATOM   2558  N   GLN A 410     -24.671 -20.265  48.462  1.00160.74           N  
ANISOU 2558  N   GLN A 410    26902  18461  15712   1170   4451   1488       N  
ATOM   2559  CA  GLN A 410     -23.548 -21.051  48.985  1.00162.97           C  
ANISOU 2559  CA  GLN A 410    27716  18651  15553   1504   4140   1629       C  
ATOM   2560  C   GLN A 410     -23.960 -22.444  49.486  1.00171.09           C  
ANISOU 2560  C   GLN A 410    29419  19286  16303   1477   4488   1768       C  
ATOM   2561  O   GLN A 410     -23.095 -23.298  49.693  1.00172.40           O  
ANISOU 2561  O   GLN A 410    30006  19346  16151   1762   4240   1897       O  
ATOM   2562  CB  GLN A 410     -22.780 -20.269  50.065  1.00165.81           C  
ANISOU 2562  CB  GLN A 410    28347  19114  15540   1729   3865   1607       C  
ATOM   2563  CG  GLN A 410     -21.891 -19.168  49.500  1.00178.63           C  
ANISOU 2563  CG  GLN A 410    29385  21120  17368   1859   3385   1490       C  
ATOM   2564  N   SER A 411     -25.278 -22.675  49.653  1.00169.84           N  
ANISOU 2564  N   SER A 411    29351  18906  16277   1134   5069   1728       N  
ATOM   2565  CA  SER A 411     -25.852 -23.944  50.114  1.00173.90           C  
ANISOU 2565  CA  SER A 411    30493  19011  16569   1027   5511   1833       C  
ATOM   2566  C   SER A 411     -25.780 -25.055  49.047  1.00178.46           C  
ANISOU 2566  C   SER A 411    30938  19510  17358   1016   5490   1891       C  
ATOM   2567  O   SER A 411     -25.410 -24.784  47.901  1.00174.17           O  
ANISOU 2567  O   SER A 411    29765  19243  17169   1059   5165   1837       O  
ATOM   2568  CB  SER A 411     -27.289 -23.736  50.586  1.00179.12           C  
ANISOU 2568  CB  SER A 411    31213  19489  17354    632   6155   1721       C  
ATOM   2569  OG  SER A 411     -28.109 -23.217  49.552  1.00184.78           O  
ANISOU 2569  OG  SER A 411    31164  20399  18644    356   6288   1548       O  
ATOM   2570  N   LYS A 412     -26.129 -26.306  49.438  1.00180.14           N  
ANISOU 2570  N   LYS A 412    31775  19332  17339    958   5850   2001       N  
ATOM   2571  CA  LYS A 412     -26.133 -27.506  48.586  1.00180.62           C  
ANISOU 2571  CA  LYS A 412    31843  19241  17544    931   5909   2062       C  
ATOM   2572  C   LYS A 412     -27.003 -27.337  47.323  1.00183.36           C  
ANISOU 2572  C   LYS A 412    31418  19748  18502    603   6083   1892       C  
ATOM   2573  O   LYS A 412     -28.060 -26.708  47.416  1.00183.27           O  
ANISOU 2573  O   LYS A 412    31129  19769  18737    292   6443   1735       O  
ATOM   2574  CB  LYS A 412     -26.614 -28.732  49.383  1.00187.88           C  
ANISOU 2574  CB  LYS A 412    33607  19663  18115    842   6404   2180       C  
ATOM   2575  CG  LYS A 412     -25.566 -29.332  50.310  1.00199.13           C  
ANISOU 2575  CG  LYS A 412    34724  21538  19397   1041   5538   2316       C  
ATOM   2576  CD  LYS A 412     -26.023 -30.685  50.843  1.00206.16           C  
ANISOU 2576  CD  LYS A 412    34744  22897  20691    682   5109   2353       C  
ATOM   2577  CE  LYS A 412     -25.020 -31.323  51.774  1.00219.81           C  
ANISOU 2577  CE  LYS A 412    35888  25164  22467    762   4278   2469       C  
ATOM   2578  NZ  LYS A 412     -25.074 -30.737  53.139  1.00229.89           N  
ANISOU 2578  NZ  LYS A 412    36525  26988  23833    608   3887   2439       N  
ATOM   2579  N   PRO A 413     -26.601 -27.901  46.149  1.00178.33           N  
ANISOU 2579  N   PRO A 413    30436  19210  18111    672   5838   1906       N  
ATOM   2580  CA  PRO A 413     -27.426 -27.747  44.932  1.00175.43           C  
ANISOU 2580  CA  PRO A 413    29350  19002  18303    381   5978   1735       C  
ATOM   2581  C   PRO A 413     -28.815 -28.384  45.018  1.00180.87           C  
ANISOU 2581  C   PRO A 413    30151  19406  19165    -26   6638   1623       C  
ATOM   2582  O   PRO A 413     -29.740 -27.914  44.354  1.00178.69           O  
ANISOU 2582  O   PRO A 413    29282  19282  19330   -301   6822   1424       O  
ATOM   2583  CB  PRO A 413     -26.571 -28.386  43.834  1.00175.23           C  
ANISOU 2583  CB  PRO A 413    29103  19084  18393    583   5581   1803       C  
ATOM   2584  CG  PRO A 413     -25.674 -29.327  44.550  1.00182.68           C  
ANISOU 2584  CG  PRO A 413    30790  19771  18849    882   5454   2006       C  
ATOM   2585  CD  PRO A 413     -25.375 -28.677  45.865  1.00180.06           C  
ANISOU 2585  CD  PRO A 413    30890  19412  18114   1033   5408   2063       C  
ATOM   2586  N   TYR A 414     -28.957 -29.442  45.843  1.00181.68           N  
ANISOU 2586  N   TYR A 414    31021  19092  18916    -59   6998   1738       N  
ATOM   2587  CA  TYR A 414     -30.216 -30.148  46.091  1.00184.92           C  
ANISOU 2587  CA  TYR A 414    31660  19171  19431   -457   7686   1631       C  
ATOM   2588  C   TYR A 414     -31.172 -29.248  46.888  1.00190.43           C  
ANISOU 2588  C   TYR A 414    32305  19875  20175   -712   8071   1480       C  
ATOM   2589  O   TYR A 414     -32.383 -29.294  46.665  1.00190.99           O  
ANISOU 2589  O   TYR A 414    32094  19884  20588  -1095   8550   1268       O  
ATOM   2590  CB  TYR A 414     -29.942 -31.469  46.840  1.00190.20           C  
ANISOU 2590  CB  TYR A 414    33190  19417  19660   -378   7881   1824       C  
ATOM   2591  CG  TYR A 414     -31.176 -32.273  47.197  1.00190.83           C  
ANISOU 2591  CG  TYR A 414    32683  19746  20078   -800   7882   1720       C  
ATOM   2592  CD1 TYR A 414     -31.812 -33.071  46.250  1.00192.09           C  
ANISOU 2592  CD1 TYR A 414    32459  19905  20620  -1043   8018   1602       C  
ATOM   2593  CD2 TYR A 414     -31.674 -32.282  48.497  1.00191.87           C  
ANISOU 2593  CD2 TYR A 414    32736  20070  20097   -913   7777   1754       C  
ATOM   2594  CE1 TYR A 414     -32.939 -33.825  46.577  1.00193.09           C  
ANISOU 2594  CE1 TYR A 414    32205  20178  20984  -1372   8086   1519       C  
ATOM   2595  CE2 TYR A 414     -32.800 -33.031  48.836  1.00192.84           C  
ANISOU 2595  CE2 TYR A 414    32504  20316  20452  -1236   7886   1685       C  
ATOM   2596  CZ  TYR A 414     -33.428 -33.803  47.873  1.00197.08           C  
ANISOU 2596  CZ  TYR A 414    32312  21115  21454  -1427   7680   1584       C  
ATOM   2597  OH  TYR A 414     -34.536 -34.546  48.203  1.00197.10           O  
ANISOU 2597  OH  TYR A 414    31903  21307  21679  -1689   7676   1534       O  
ATOM   2598  N   ASP A 415     -30.616 -28.429  47.807  1.00187.54           N  
ANISOU 2598  N   ASP A 415    32190  19593  19475   -493   7856   1568       N  
ATOM   2599  CA  ASP A 415     -31.361 -27.492  48.651  1.00188.60           C  
ANISOU 2599  CA  ASP A 415    32318  19745  19597   -679   8163   1443       C  
ATOM   2600  C   ASP A 415     -31.900 -26.301  47.854  1.00188.98           C  
ANISOU 2600  C   ASP A 415    31453  20185  20165   -818   8041   1219       C  
ATOM   2601  O   ASP A 415     -33.004 -25.835  48.141  1.00190.09           O  
ANISOU 2601  O   ASP A 415    31408  20302  20514  -1119   8473   1024       O  
ATOM   2602  CB  ASP A 415     -30.492 -27.005  49.827  1.00191.60           C  
ANISOU 2602  CB  ASP A 415    33253  20107  19441   -368   7910   1607       C  
ATOM   2603  CG  ASP A 415     -29.980 -28.091  50.762  1.00196.85           C  
ANISOU 2603  CG  ASP A 415    33411  21339  20043   -270   6966   1795       C  
ATOM   2604  OD1 ASP A 415     -30.508 -29.226  50.709  1.00196.91           O  
ANISOU 2604  OD1 ASP A 415    33260  21350  20206   -456   7002   1819       O  
ATOM   2605  OD2 ASP A 415     -29.067 -27.800  51.563  1.00200.30           O  
ANISOU 2605  OD2 ASP A 415    33629  22174  20304    -36   6282   1898       O  
ATOM   2606  N   ILE A 416     -31.121 -25.809  46.862  1.00181.04           N  
ANISOU 2606  N   ILE A 416    29897  19528  19361   -590   7462   1240       N  
ATOM   2607  CA  ILE A 416     -31.501 -24.684  45.993  1.00177.14           C  
ANISOU 2607  CA  ILE A 416    28564  19406  19336   -666   7280   1055       C  
ATOM   2608  C   ILE A 416     -32.675 -25.097  45.086  1.00180.40           C  
ANISOU 2608  C   ILE A 416    28505  19805  20234   -998   7627    842       C  
ATOM   2609  O   ILE A 416     -33.582 -24.292  44.864  1.00179.31           O  
ANISOU 2609  O   ILE A 416    27865  19824  20441  -1191   7792    625       O  
ATOM   2610  CB  ILE A 416     -30.289 -24.098  45.200  1.00176.30           C  
ANISOU 2610  CB  ILE A 416    28073  19639  19272   -334   6594   1144       C  
ATOM   2611  CG1 ILE A 416     -29.095 -23.788  46.136  1.00177.45           C  
ANISOU 2611  CG1 ILE A 416    28695  19795  18933     -4   6248   1320       C  
ATOM   2612  CG2 ILE A 416     -30.691 -22.839  44.411  1.00173.82           C  
ANISOU 2612  CG2 ILE A 416    26978  19675  19391   -400   6431    965       C  
ATOM   2613  CD1 ILE A 416     -27.706 -23.899  45.484  1.00183.61           C  
ANISOU 2613  CD1 ILE A 416    29359  20769  19636    341   5640   1447       C  
ATOM   2614  N   MET A 417     -32.668 -26.359  44.600  1.00177.72           N  
ANISOU 2614  N   MET A 417    28340  19270  19913  -1058   7743    889       N  
ATOM   2615  CA  MET A 417     -33.731 -26.918  43.760  1.00177.85           C  
ANISOU 2615  CA  MET A 417    27962  19250  20365  -1376   8078    675       C  
ATOM   2616  C   MET A 417     -35.057 -27.002  44.517  1.00183.96           C  
ANISOU 2616  C   MET A 417    28876  19796  21225  -1755   8759    473       C  
ATOM   2617  O   MET A 417     -36.103 -26.702  43.943  1.00183.06           O  
ANISOU 2617  O   MET A 417    28183  19810  21560  -2009   8973    199       O  
ATOM   2618  CB  MET A 417     -33.338 -28.290  43.191  1.00181.11           C  
ANISOU 2618  CB  MET A 417    28619  19469  20725  -1347   8062    782       C  
ATOM   2619  CG  MET A 417     -32.510 -28.212  41.914  1.00180.98           C  
ANISOU 2619  CG  MET A 417    28126  19746  20893  -1110   7486    838       C  
ATOM   2620  SD  MET A 417     -33.277 -27.316  40.528  1.00181.96           S  
ANISOU 2620  SD  MET A 417    27225  20275  21636  -1247   7331    559       S  
ATOM   2621  CE  MET A 417     -34.646 -28.403  40.134  1.00181.85           C  
ANISOU 2621  CE  MET A 417    27105  20034  21954  -1675   7925    306       C  
ATOM   2622  N   ALA A 418     -35.005 -27.374  45.812  1.00183.69           N  
ANISOU 2622  N   ALA A 418    29607  19432  20755  -1782   9091    596       N  
ATOM   2623  CA  ALA A 418     -36.177 -27.452  46.686  1.00187.43           C  
ANISOU 2623  CA  ALA A 418    30318  19653  21244  -2141   9778    419       C  
ATOM   2624  C   ALA A 418     -36.682 -26.045  47.025  1.00190.83           C  
ANISOU 2624  C   ALA A 418    30336  20331  21838  -2186   9780    254       C  
ATOM   2625  O   ALA A 418     -37.887 -25.854  47.195  1.00190.58           O  
ANISOU 2625  O   ALA A 418    29858  20447  22106  -2458   9993     25       O  
ATOM   2626  CB  ALA A 418     -35.830 -28.205  47.961  1.00188.91           C  
ANISOU 2626  CB  ALA A 418    31004  19825  20950  -2016   9530    684       C  
ATOM   2627  N   GLU A 419     -35.756 -25.064  47.100  1.00185.20           N  
ANISOU 2627  N   GLU A 419    29523  19880  20964  -1853   9237    396       N  
ATOM   2628  CA  GLU A 419     -36.042 -23.657  47.388  1.00184.04           C  
ANISOU 2628  CA  GLU A 419    29009  19979  20940  -1837   9156    272       C  
ATOM   2629  C   GLU A 419     -36.750 -22.970  46.216  1.00185.87           C  
ANISOU 2629  C   GLU A 419    28327  20535  21760  -1939   9040     17       C  
ATOM   2630  O   GLU A 419     -37.669 -22.183  46.447  1.00185.75           O  
ANISOU 2630  O   GLU A 419    27991  20602  21983  -2112   9296   -210       O  
ATOM   2631  CB  GLU A 419     -34.752 -22.905  47.752  1.00183.11           C  
ANISOU 2631  CB  GLU A 419    29069  20031  20473  -1451   8594    495       C  
ATOM   2632  N   VAL A 420     -36.324 -23.261  44.966  1.00180.91           N  
ANISOU 2632  N   VAL A 420    27296  20087  21355  -1818   8652     48       N  
ATOM   2633  CA  VAL A 420     -36.928 -22.671  43.764  1.00178.90           C  
ANISOU 2633  CA  VAL A 420    26211  20138  21626  -1872   8491   -179       C  
ATOM   2634  C   VAL A 420     -38.295 -23.307  43.452  1.00184.48           C  
ANISOU 2634  C   VAL A 420    26654  20731  22710  -2245   9014   -479       C  
ATOM   2635  O   VAL A 420     -39.140 -22.645  42.847  1.00183.52           O  
ANISOU 2635  O   VAL A 420    25888  20828  23014  -2343   9032   -744       O  
ATOM   2636  CB  VAL A 420     -35.998 -22.621  42.515  1.00179.79           C  
ANISOU 2636  CB  VAL A 420    25967  20505  21840  -1604   7881    -56       C  
ATOM   2637  CG1 VAL A 420     -34.797 -21.709  42.751  1.00177.22           C  
ANISOU 2637  CG1 VAL A 420    25738  20354  21244  -1269   7379    153       C  
ATOM   2638  CG2 VAL A 420     -35.554 -24.011  42.065  1.00180.37           C  
ANISOU 2638  CG2 VAL A 420    26313  20400  21818  -1601   7869     68       C  
ATOM   2639  N   TYR A 421     -38.513 -24.574  43.876  1.00184.11           N  
ANISOU 2639  N   TYR A 421    27110  20337  22507  -2447   9440   -451       N  
ATOM   2640  CA  TYR A 421     -39.780 -25.283  43.673  1.00187.02           C  
ANISOU 2640  CA  TYR A 421    27288  20557  23213  -2838   9995   -753       C  
ATOM   2641  C   TYR A 421     -40.882 -24.737  44.585  1.00193.72           C  
ANISOU 2641  C   TYR A 421    28077  21374  24154  -3084  10448   -981       C  
ATOM   2642  O   TYR A 421     -41.991 -24.493  44.107  1.00193.11           O  
ANISOU 2642  O   TYR A 421    27334  21525  24513  -3254  10509  -1282       O  
ATOM   2643  CB  TYR A 421     -39.626 -26.807  43.862  1.00190.86           C  
ANISOU 2643  CB  TYR A 421    28368  20665  23484  -2977  10309   -641       C  
ATOM   2644  CG  TYR A 421     -39.137 -27.571  42.647  1.00190.14           C  
ANISOU 2644  CG  TYR A 421    28059  20653  23532  -2874   9973   -578       C  
ATOM   2645  CD1 TYR A 421     -39.588 -27.254  41.367  1.00189.82           C  
ANISOU 2645  CD1 TYR A 421    27217  20929  23976  -2897   9735   -805       C  
ATOM   2646  CD2 TYR A 421     -38.302 -28.676  42.785  1.00191.60           C  
ANISOU 2646  CD2 TYR A 421    28861  20570  23366  -2767   9933   -314       C  
ATOM   2647  CE1 TYR A 421     -39.157 -27.967  40.249  1.00189.38           C  
ANISOU 2647  CE1 TYR A 421    26977  20941  24039  -2812   9443   -757       C  
ATOM   2648  CE2 TYR A 421     -37.868 -29.400  41.675  1.00190.64           C  
ANISOU 2648  CE2 TYR A 421    28546  20510  23378  -2680   9648   -268       C  
ATOM   2649  CZ  TYR A 421     -38.299 -29.042  40.409  1.00195.71           C  
ANISOU 2649  CZ  TYR A 421    28384  21480  24497  -2714   9410   -491       C  
ATOM   2650  OH  TYR A 421     -37.877 -29.756  39.313  1.00195.02           O  
ANISOU 2650  OH  TYR A 421    28118  21450  24529  -2634   9138   -453       O  
ATOM   2651  N   ARG A 422     -40.575 -24.537  45.888  1.00191.84           N  
ANISOU 2651  N   ARG A 422    28412  21002  23477  -3019  10529   -792       N  
ATOM   2652  CA  ARG A 422     -41.524 -24.012  46.879  1.00192.03           C  
ANISOU 2652  CA  ARG A 422    28200  21273  23492  -3094  10502   -867       C  
ATOM   2653  C   ARG A 422     -41.893 -22.542  46.622  1.00195.02           C  
ANISOU 2653  C   ARG A 422    27997  21940  24161  -3022  10363  -1063       C  
ATOM   2654  O   ARG A 422     -43.000 -22.127  46.967  1.00194.79           O  
ANISOU 2654  O   ARG A 422    27567  22110  24336  -3148  10456  -1259       O  
ATOM   2655  CB  ARG A 422     -41.038 -24.246  48.327  1.00192.18           C  
ANISOU 2655  CB  ARG A 422    28818  21255  22947  -2952  10326   -553       C  
ATOM   2656  N   ALA A 423     -40.974 -21.772  46.003  1.00191.52           N  
ANISOU 2656  N   ALA A 423    27614  21393  23762  -2864  10335  -1052       N  
ATOM   2657  CA  ALA A 423     -41.183 -20.366  45.652  1.00189.18           C  
ANISOU 2657  CA  ALA A 423    26714  21433  23731  -2724  10039  -1186       C  
ATOM   2658  C   ALA A 423     -42.084 -20.255  44.418  1.00192.24           C  
ANISOU 2658  C   ALA A 423    26290  22054  24699  -2825   9998  -1502       C  
ATOM   2659  O   ALA A 423     -42.915 -19.347  44.350  1.00191.58           O  
ANISOU 2659  O   ALA A 423    25720  22139  24931  -2879  10085  -1767       O  
ATOM   2660  CB  ALA A 423     -39.848 -19.686  45.392  1.00185.83           C  
ANISOU 2660  CB  ALA A 423    26327  21212  23066  -2328   9372   -893       C  
ATOM   2661  N   MET A 424     -41.923 -21.186  43.453  1.00188.69           N  
ANISOU 2661  N   MET A 424    25704  21610  24378  -2838   9858  -1482       N  
ATOM   2662  CA  MET A 424     -42.708 -21.244  42.219  1.00188.09           C  
ANISOU 2662  CA  MET A 424    24899  21747  24819  -2920   9786  -1777       C  
ATOM   2663  C   MET A 424     -44.141 -21.706  42.484  1.00195.93           C  
ANISOU 2663  C   MET A 424    25701  22606  26139  -3323  10434  -2174       C  
ATOM   2664  O   MET A 424     -45.059 -21.245  41.805  1.00195.83           O  
ANISOU 2664  O   MET A 424    25004  22817  26584  -3384  10430  -2513       O  
ATOM   2665  CB  MET A 424     -42.032 -22.155  41.186  1.00188.43           C  
ANISOU 2665  CB  MET A 424    24926  21812  24856  -2818   9460  -1627       C  
ATOM   2666  N   LYS A 425     -44.331 -22.611  43.469  1.00194.44           N  
ANISOU 2666  N   LYS A 425    26043  22184  25651  -3505  10757  -2061       N  
ATOM   2667  CA  LYS A 425     -45.643 -23.138  43.857  1.00193.92           C  
ANISOU 2667  CA  LYS A 425    25625  22425  25630  -3594  10594  -2105       C  
ATOM   2668  C   LYS A 425     -46.504 -22.096  44.584  1.00195.81           C  
ANISOU 2668  C   LYS A 425    25507  23026  25865  -3474  10357  -2132       C  
ATOM   2669  O   LYS A 425     -47.731 -22.216  44.578  1.00195.67           O  
ANISOU 2669  O   LYS A 425    25039  23259  26048  -3545  10309  -2283       O  
ATOM   2670  CB  LYS A 425     -45.507 -24.427  44.693  1.00196.03           C  
ANISOU 2670  CB  LYS A 425    26378  22658  25446  -3580  10408  -1743       C  
ATOM   2671  N   GLN A 426     -45.861 -21.078  45.201  1.00192.98           N  
ANISOU 2671  N   GLN A 426    25489  22461  25375  -3436  10609  -2132       N  
ATOM   2672  CA  GLN A 426     -46.530 -19.980  45.908  1.00193.08           C  
ANISOU 2672  CA  GLN A 426    25282  22647  25431  -3399  10639  -2249       C  
ATOM   2673  C   GLN A 426     -47.301 -19.087  44.930  1.00195.79           C  
ANISOU 2673  C   GLN A 426    24798  23347  26245  -3289  10376  -2525       C  
ATOM   2674  O   GLN A 426     -48.397 -18.629  45.255  1.00195.58           O  
ANISOU 2674  O   GLN A 426    24393  23556  26362  -3294  10361  -2677       O  
ATOM   2675  CB  GLN A 426     -45.520 -19.156  46.724  1.00193.79           C  
ANISOU 2675  CB  GLN A 426    25881  22594  25156  -3242  10620  -2039       C  
ATOM   2676  CG  GLN A 426     -45.190 -19.774  48.080  1.00204.43           C  
ANISOU 2676  CG  GLN A 426    27576  24276  25822  -2958   9858  -1477       C  
ATOM   2677  CD  GLN A 426     -44.090 -19.038  48.807  1.00218.78           C  
ANISOU 2677  CD  GLN A 426    29466  26521  27141  -2480   8879  -1019       C  
ATOM   2678  OE1 GLN A 426     -44.208 -17.855  49.145  1.00215.67           O  
ANISOU 2678  OE1 GLN A 426    29095  26021  26828  -2517   9206  -1203       O  
ATOM   2679  NE2 GLN A 426     -43.007 -19.741  49.101  1.00213.31           N  
ANISOU 2679  NE2 GLN A 426    29543  25347  26159  -2574   9264   -901       N  
ATOM   2680  N   LEU A 427     -46.732 -18.863  43.729  1.00193.49           N  
ANISOU 2680  N   LEU A 427    24320  22876  26320  -3330  10556  -2756       N  
ATOM   2681  CA  LEU A 427     -47.342 -18.077  42.653  1.00193.86           C  
ANISOU 2681  CA  LEU A 427    23616  23097  26946  -3315  10550  -3166       C  
ATOM   2682  C   LEU A 427     -47.988 -19.022  41.624  1.00195.47           C  
ANISOU 2682  C   LEU A 427    23354  23600  27316  -3280  10149  -3186       C  
ATOM   2683  O   LEU A 427     -47.845 -20.242  41.743  1.00195.39           O  
ANISOU 2683  O   LEU A 427    23669  23456  27113  -3413  10226  -3031       O  
ATOM   2684  CB  LEU A 427     -46.294 -17.177  41.973  1.00190.12           C  
ANISOU 2684  CB  LEU A 427    23050  22773  26414  -2957  10003  -2960       C  
ATOM   2685  CG  LEU A 427     -45.674 -16.074  42.827  1.00193.69           C  
ANISOU 2685  CG  LEU A 427    23744  23251  26599  -2758   9862  -2775       C  
ATOM   2686  CD1 LEU A 427     -45.151 -16.630  44.141  1.00194.09           C  
ANISOU 2686  CD1 LEU A 427    24491  23147  26106  -2618   9658  -2324       C  
ATOM   2687  CD2 LEU A 427     -44.564 -15.370  42.076  1.00191.10           C  
ANISOU 2687  CD2 LEU A 427    22862  23243  26504  -2446   9360  -2832       C  
ATOM   2688  N   ASP A 428     -48.702 -18.468  40.626  1.00192.57           N  
ANISOU 2688  N   ASP A 428    22273  23383  27512  -3297  10190  -3631       N  
ATOM   2689  CA  ASP A 428     -49.363 -19.265  39.591  1.00191.91           C  
ANISOU 2689  CA  ASP A 428    21729  23499  27688  -3331   9992  -3787       C  
ATOM   2690  C   ASP A 428     -48.427 -19.556  38.405  1.00194.44           C  
ANISOU 2690  C   ASP A 428    21979  23693  28206  -3313   9923  -3854       C  
ATOM   2691  O   ASP A 428     -48.610 -19.016  37.309  1.00192.02           O  
ANISOU 2691  O   ASP A 428    21102  23663  28193  -3104   9523  -4013       O  
ATOM   2692  CB  ASP A 428     -50.695 -18.618  39.153  1.00193.45           C  
ANISOU 2692  CB  ASP A 428    21213  24126  28164  -3165   9673  -4006       C  
ATOM   2693  CG  ASP A 428     -51.723 -18.470  40.262  1.00200.26           C  
ANISOU 2693  CG  ASP A 428    22177  25432  28478  -2869   9099  -3494       C  
ATOM   2694  OD1 ASP A 428     -51.977 -19.466  40.978  1.00200.67           O  
ANISOU 2694  OD1 ASP A 428    22563  25452  28230  -2980   9133  -3249       O  
ATOM   2695  OD2 ASP A 428     -52.305 -17.371  40.387  1.00204.84           O  
ANISOU 2695  OD2 ASP A 428    22477  26336  29017  -2569   8726  -3418       O  
ATOM   2696  N   PHE A 429     -47.414 -20.414  38.641  1.00189.92           N  
ANISOU 2696  N   PHE A 429    22025  22876  27261  -3346   9948  -3506       N  
ATOM   2697  CA  PHE A 429     -46.425 -20.811  37.635  1.00186.06           C  
ANISOU 2697  CA  PHE A 429    21576  22477  26642  -3116   9429  -3231       C  
ATOM   2698  C   PHE A 429     -46.708 -22.192  37.044  1.00190.48           C  
ANISOU 2698  C   PHE A 429    22099  22925  27350  -3356   9623  -3370       C  
ATOM   2699  O   PHE A 429     -47.125 -23.103  37.763  1.00193.74           O  
ANISOU 2699  O   PHE A 429    22839  23076  27699  -3675  10139  -3438       O  
ATOM   2700  CB  PHE A 429     -44.997 -20.784  38.213  1.00185.27           C  
ANISOU 2700  CB  PHE A 429    22155  22234  26005  -2914   9202  -2724       C  
ATOM   2701  CG  PHE A 429     -44.357 -19.422  38.366  1.00184.03           C  
ANISOU 2701  CG  PHE A 429    21982  22252  25688  -2586   8791  -2523       C  
ATOM   2702  CD1 PHE A 429     -43.969 -18.687  37.251  1.00183.77           C  
ANISOU 2702  CD1 PHE A 429    21533  22511  25779  -2275   8213  -2472       C  
ATOM   2703  CD2 PHE A 429     -44.071 -18.909  39.624  1.00186.87           C  
ANISOU 2703  CD2 PHE A 429    22794  22466  25742  -2587   8982  -2369       C  
ATOM   2704  CE1 PHE A 429     -43.357 -17.438  37.395  1.00182.04           C  
ANISOU 2704  CE1 PHE A 429    21329  22427  25409  -1991   7865  -2290       C  
ATOM   2705  CE2 PHE A 429     -43.451 -17.663  39.767  1.00186.86           C  
ANISOU 2705  CE2 PHE A 429    22785  22618  25594  -2297   8610  -2196       C  
ATOM   2706  CZ  PHE A 429     -43.102 -16.935  38.651  1.00181.67           C  
ANISOU 2706  CZ  PHE A 429    21700  22241  25086  -2010   8065  -2160       C  
ATOM   2707  N   GLU A 430     -46.451 -22.341  35.735  1.00183.31           N  
ANISOU 2707  N   GLU A 430    20822  22231  26596  -3177   9161  -3374       N  
ATOM   2708  CA  GLU A 430     -46.605 -23.584  34.977  1.00183.26           C  
ANISOU 2708  CA  GLU A 430    20735  22162  26734  -3353   9238  -3492       C  
ATOM   2709  C   GLU A 430     -45.334 -23.788  34.153  1.00181.05           C  
ANISOU 2709  C   GLU A 430    20630  21953  26207  -3055   8681  -3116       C  
ATOM   2710  O   GLU A 430     -44.973 -22.915  33.363  1.00177.21           O  
ANISOU 2710  O   GLU A 430    19819  21745  25766  -2736   8151  -3044       O  
ATOM   2711  CB  GLU A 430     -47.849 -23.526  34.076  1.00186.76           C  
ANISOU 2711  CB  GLU A 430    20397  22848  27716  -3458   9255  -4008       C  
ATOM   2712  N   TRP A 431     -44.630 -24.913  34.369  1.00177.10           N  
ANISOU 2712  N   TRP A 431    20671  21188  25431  -3150   8810  -2874       N  
ATOM   2713  CA  TRP A 431     -43.367 -25.190  33.679  1.00173.24           C  
ANISOU 2713  CA  TRP A 431    20392  20740  24692  -2879   8321  -2518       C  
ATOM   2714  C   TRP A 431     -43.294 -26.576  33.023  1.00177.82           C  
ANISOU 2714  C   TRP A 431    21053  21186  25325  -3035   8410  -2554       C  
ATOM   2715  O   TRP A 431     -44.318 -27.232  32.834  1.00180.49           O  
ANISOU 2715  O   TRP A 431    21137  21468  25973  -3341   8779  -2913       O  
ATOM   2716  CB  TRP A 431     -42.178 -24.966  34.634  1.00170.27           C  
ANISOU 2716  CB  TRP A 431    20676  20198  23819  -2700   8229  -2079       C  
ATOM   2717  CG  TRP A 431     -42.202 -25.821  35.866  1.00174.56           C  
ANISOU 2717  CG  TRP A 431    21869  20353  24101  -2948   8769  -1993       C  
ATOM   2718  CD1 TRP A 431     -41.660 -27.063  36.014  1.00178.25           C  
ANISOU 2718  CD1 TRP A 431    22852  20540  24335  -3030   8920  -1812       C  
ATOM   2719  CD2 TRP A 431     -42.789 -25.485  37.129  1.00177.30           C  
ANISOU 2719  CD2 TRP A 431    22461  20533  24371  -3132   9236  -2077       C  
ATOM   2720  NE1 TRP A 431     -41.882 -27.528  37.289  1.00181.03           N  
ANISOU 2720  NE1 TRP A 431    23779  20548  24456  -3249   9454  -1772       N  
ATOM   2721  CE2 TRP A 431     -42.573 -26.579  37.996  1.00183.73           C  
ANISOU 2721  CE2 TRP A 431    23967  20955  24887  -3325   9664  -1934       C  
ATOM   2722  CE3 TRP A 431     -43.482 -24.363  37.616  1.00179.52           C  
ANISOU 2722  CE3 TRP A 431    22459  20949  24801  -3148   9343  -2263       C  
ATOM   2723  CZ2 TRP A 431     -43.026 -26.586  39.321  1.00186.53           C  
ANISOU 2723  CZ2 TRP A 431    24754  21047  25073  -3540  10202  -1968       C  
ATOM   2724  CZ3 TRP A 431     -43.935 -24.373  38.926  1.00184.37           C  
ANISOU 2724  CZ3 TRP A 431    23467  21315  25271  -3369   9877  -2309       C  
ATOM   2725  CH2 TRP A 431     -43.703 -25.472  39.765  1.00187.65           C  
ANISOU 2725  CH2 TRP A 431    24586  21340  25374  -3566  10303  -2159       C  
ATOM   2726  N   LYS A 432     -42.069 -26.988  32.641  1.00171.18           N  
ANISOU 2726  N   LYS A 432    20539  20305  24197  -2819   8060  -2202       N  
ATOM   2727  CA  LYS A 432     -41.732 -28.270  32.029  1.00171.14           C  
ANISOU 2727  CA  LYS A 432    20699  20160  24168  -2900   8074  -2155       C  
ATOM   2728  C   LYS A 432     -40.270 -28.567  32.366  1.00172.03           C  
ANISOU 2728  C   LYS A 432    21423  20121  23818  -2662   7832  -1693       C  
ATOM   2729  O   LYS A 432     -39.372 -27.871  31.884  1.00168.06           O  
ANISOU 2729  O   LYS A 432    20833  19830  23193  -2336   7316  -1477       O  
ATOM   2730  CB  LYS A 432     -41.961 -28.234  30.507  1.00172.32           C  
ANISOU 2730  CB  LYS A 432    20229  20607  24637  -2806   7692  -2354       C  
ATOM   2731  N   VAL A 433     -40.040 -29.559  33.245  1.00170.32           N  
ANISOU 2731  N   VAL A 433    21842  19534  23339  -2818   8218  -1552       N  
ATOM   2732  CA  VAL A 433     -38.699 -29.947  33.692  1.00168.29           C  
ANISOU 2732  CA  VAL A 433    22214  19100  22626  -2588   8025  -1138       C  
ATOM   2733  C   VAL A 433     -37.951 -30.694  32.561  1.00169.20           C  
ANISOU 2733  C   VAL A 433    22274  19268  22747  -2443   7675  -1029       C  
ATOM   2734  O   VAL A 433     -38.313 -31.815  32.193  1.00170.81           O  
ANISOU 2734  O   VAL A 433    22538  19297  23066  -2652   7927  -1153       O  
ATOM   2735  CB  VAL A 433     -38.696 -30.688  35.070  1.00175.74           C  
ANISOU 2735  CB  VAL A 433    23912  19617  23245  -2760   8539  -1012       C  
ATOM   2736  CG1 VAL A 433     -39.622 -31.907  35.090  1.00179.74           C  
ANISOU 2736  CG1 VAL A 433    24525  19837  23932  -3158   9114  -1256       C  
ATOM   2737  CG2 VAL A 433     -37.283 -31.053  35.521  1.00174.22           C  
ANISOU 2737  CG2 VAL A 433    24359  19265  22573  -2468   8280   -597       C  
ATOM   2738  N   VAL A 434     -36.936 -30.023  31.986  1.00161.18           N  
ANISOU 2738  N   VAL A 434    21118  18499  21623  -2096   7106   -821       N  
ATOM   2739  CA  VAL A 434     -36.109 -30.546  30.892  1.00158.39           C  
ANISOU 2739  CA  VAL A 434    20686  18234  21260  -1917   6722   -705       C  
ATOM   2740  C   VAL A 434     -34.945 -31.356  31.483  1.00161.83           C  
ANISOU 2740  C   VAL A 434    21803  18402  21284  -1767   6690   -374       C  
ATOM   2741  O   VAL A 434     -34.748 -32.514  31.109  1.00162.46           O  
ANISOU 2741  O   VAL A 434    22085  18299  21343  -1829   6780   -352       O  
ATOM   2742  CB  VAL A 434     -35.619 -29.419  29.931  1.00158.24           C  
ANISOU 2742  CB  VAL A 434    20180  18603  21340  -1634   6158   -668       C  
ATOM   2743  CG1 VAL A 434     -34.843 -29.993  28.747  1.00155.96           C  
ANISOU 2743  CG1 VAL A 434    19793  18402  21061  -1480   5804   -581       C  
ATOM   2744  CG2 VAL A 434     -36.781 -28.558  29.438  1.00158.26           C  
ANISOU 2744  CG2 VAL A 434    19558  18856  21717  -1737   6176   -988       C  
ATOM   2745  N   ASN A 435     -34.191 -30.739  32.409  1.00157.12           N  
ANISOU 2745  N   ASN A 435    21554  17783  20362  -1561   6556   -134       N  
ATOM   2746  CA  ASN A 435     -33.040 -31.321  33.101  1.00157.06           C  
ANISOU 2746  CA  ASN A 435    22193  17554  19930  -1357   6469    175       C  
ATOM   2747  C   ASN A 435     -33.184 -31.070  34.613  1.00162.92           C  
ANISOU 2747  C   ASN A 435    23435  18081  20387  -1403   6777    263       C  
ATOM   2748  O   ASN A 435     -33.998 -30.236  35.017  1.00163.00           O  
ANISOU 2748  O   ASN A 435    23218  18180  20535  -1546   6963    106       O  
ATOM   2749  CB  ASN A 435     -31.743 -30.700  32.543  1.00153.95           C  
ANISOU 2749  CB  ASN A 435    21659  17420  19414   -987   5866    372       C  
ATOM   2750  CG  ASN A 435     -30.450 -31.160  33.177  1.00176.91           C  
ANISOU 2750  CG  ASN A 435    25147  20168  21904   -716   5678    665       C  
ATOM   2751  OD1 ASN A 435     -30.156 -32.357  33.271  1.00173.30           O  
ANISOU 2751  OD1 ASN A 435    25108  19443  21294   -715   5808    756       O  
ATOM   2752  ND2 ASN A 435     -29.641 -30.208  33.617  1.00166.87           N  
ANISOU 2752  ND2 ASN A 435    23904  19060  20440   -469   5356    803       N  
ATOM   2753  N   ALA A 436     -32.396 -31.788  35.443  1.00160.84           N  
ANISOU 2753  N   ALA A 436    23862  17534  19715  -1267   6823    507       N  
ATOM   2754  CA  ALA A 436     -32.385 -31.665  36.906  1.00163.07           C  
ANISOU 2754  CA  ALA A 436    24730  17583  19649  -1268   7086    625       C  
ATOM   2755  C   ALA A 436     -31.972 -30.260  37.403  1.00164.32           C  
ANISOU 2755  C   ALA A 436    24747  17994  19695  -1069   6787    692       C  
ATOM   2756  O   ALA A 436     -32.101 -29.972  38.595  1.00165.87           O  
ANISOU 2756  O   ALA A 436    25346  18041  19638  -1091   7009    749       O  
ATOM   2757  CB  ALA A 436     -31.479 -32.729  37.510  1.00165.83           C  
ANISOU 2757  CB  ALA A 436    25832  17607  19570  -1086   7087    884       C  
ATOM   2758  N   TYR A 437     -31.492 -29.393  36.485  1.00156.68           N  
ANISOU 2758  N   TYR A 437    23228  17393  18909   -886   6307    679       N  
ATOM   2759  CA  TYR A 437     -31.073 -28.019  36.769  1.00154.05           C  
ANISOU 2759  CA  TYR A 437    22695  17318  18517   -704   6001    720       C  
ATOM   2760  C   TYR A 437     -31.692 -27.004  35.790  1.00154.90           C  
ANISOU 2760  C   TYR A 437    22057  17759  19040   -773   5855    515       C  
ATOM   2761  O   TYR A 437     -31.713 -25.808  36.091  1.00153.22           O  
ANISOU 2761  O   TYR A 437    21653  17725  18839   -706   5734    491       O  
ATOM   2762  CB  TYR A 437     -29.537 -27.905  36.787  1.00153.29           C  
ANISOU 2762  CB  TYR A 437    22804  17314  18124   -333   5503    957       C  
ATOM   2763  CG  TYR A 437     -28.865 -28.834  37.776  1.00157.73           C  
ANISOU 2763  CG  TYR A 437    24116  17566  18250   -200   5584   1160       C  
ATOM   2764  CD1 TYR A 437     -28.816 -28.523  39.132  1.00161.87           C  
ANISOU 2764  CD1 TYR A 437    25120  17944  18441   -160   5735   1242       C  
ATOM   2765  CD2 TYR A 437     -28.277 -30.023  37.358  1.00159.11           C  
ANISOU 2765  CD2 TYR A 437    24542  17584  18328    -96   5503   1267       C  
ATOM   2766  CE1 TYR A 437     -28.207 -29.378  40.049  1.00165.53           C  
ANISOU 2766  CE1 TYR A 437    26314  18109  18469     -6   5793   1431       C  
ATOM   2767  CE2 TYR A 437     -27.661 -30.885  38.265  1.00162.84           C  
ANISOU 2767  CE2 TYR A 437    25736  17755  18381     63   5562   1455       C  
ATOM   2768  CZ  TYR A 437     -27.626 -30.556  39.610  1.00172.58           C  
ANISOU 2768  CZ  TYR A 437    27457  18845  19271    116   5699   1539       C  
ATOM   2769  OH  TYR A 437     -27.019 -31.399  40.509  1.00176.78           O  
ANISOU 2769  OH  TYR A 437    28738  19072  19358    304   5738   1728       O  
ATOM   2770  N   HIS A 438     -32.199 -27.481  34.631  1.00150.55           N  
ANISOU 2770  N   HIS A 438    21105  17282  18814   -896   5865    362       N  
ATOM   2771  CA  HIS A 438     -32.825 -26.647  33.600  1.00148.16           C  
ANISOU 2771  CA  HIS A 438    20117  17279  18896   -939   5712    157       C  
ATOM   2772  C   HIS A 438     -34.355 -26.678  33.703  1.00154.02           C  
ANISOU 2772  C   HIS A 438    20608  17971  19942  -1262   6160   -139       C  
ATOM   2773  O   HIS A 438     -34.957 -27.754  33.666  1.00156.09           O  
ANISOU 2773  O   HIS A 438    20985  18028  20292  -1492   6506   -252       O  
ATOM   2774  CB  HIS A 438     -32.352 -27.066  32.196  1.00146.69           C  
ANISOU 2774  CB  HIS A 438    19626  17243  18866   -832   5379    162       C  
ATOM   2775  CG  HIS A 438     -32.788 -26.144  31.099  1.00147.85           C  
ANISOU 2775  CG  HIS A 438    19132  17707  19339   -801   5139     -6       C  
ATOM   2776  ND1 HIS A 438     -32.003 -25.078  30.700  1.00146.57           N  
ANISOU 2776  ND1 HIS A 438    18775  17785  19131   -554   4717    100       N  
ATOM   2777  CD2 HIS A 438     -33.908 -26.171  30.340  1.00150.30           C  
ANISOU 2777  CD2 HIS A 438    18987  18114  20004   -977   5265   -277       C  
ATOM   2778  CE1 HIS A 438     -32.670 -24.489  29.721  1.00144.96           C  
ANISOU 2778  CE1 HIS A 438    18046  17799  19234   -575   4605    -86       C  
ATOM   2779  NE2 HIS A 438     -33.823 -25.109  29.471  1.00147.49           N  
ANISOU 2779  NE2 HIS A 438    18180  18055  19803   -812   4905   -322       N  
ATOM   2780  N   LEU A 439     -34.975 -25.490  33.833  1.00149.70           N  
ANISOU 2780  N   LEU A 439    19712  17607  19559  -1280   6161   -281       N  
ATOM   2781  CA  LEU A 439     -36.428 -25.318  33.945  1.00151.71           C  
ANISOU 2781  CA  LEU A 439    19653  17862  20129  -1556   6550   -598       C  
ATOM   2782  C   LEU A 439     -36.937 -24.253  32.972  1.00153.17           C  
ANISOU 2782  C   LEU A 439    19163  18382  20652  -1473   6277   -792       C  
ATOM   2783  O   LEU A 439     -36.238 -23.272  32.716  1.00149.89           O  
ANISOU 2783  O   LEU A 439    18631  18162  20159  -1220   5882   -656       O  
ATOM   2784  CB  LEU A 439     -36.825 -24.938  35.385  1.00154.14           C  
ANISOU 2784  CB  LEU A 439    20302  17999  20266  -1674   6924   -601       C  
ATOM   2785  CG  LEU A 439     -36.647 -26.009  36.465  1.00161.88           C  
ANISOU 2785  CG  LEU A 439    21982  18600  20924  -1808   7313   -466       C  
ATOM   2786  CD1 LEU A 439     -36.371 -25.378  37.813  1.00162.93           C  
ANISOU 2786  CD1 LEU A 439    22544  18630  20734  -1746   7425   -328       C  
ATOM   2787  CD2 LEU A 439     -37.859 -26.928  36.546  1.00168.18           C  
ANISOU 2787  CD2 LEU A 439    22764  19189  21950  -2184   7873   -731       C  
ATOM   2788  N   ARG A 440     -38.159 -24.443  32.443  1.00151.18           N  
ANISOU 2788  N   ARG A 440    18479  18190  20773  -1682   6493  -1122       N  
ATOM   2789  CA  ARG A 440     -38.789 -23.507  31.511  1.00149.70           C  
ANISOU 2789  CA  ARG A 440    17654  18308  20917  -1594   6251  -1344       C  
ATOM   2790  C   ARG A 440     -40.132 -23.014  32.069  1.00156.03           C  
ANISOU 2790  C   ARG A 440    18187  19121  21976  -1796   6622  -1666       C  
ATOM   2791  O   ARG A 440     -41.195 -23.496  31.668  1.00158.01           O  
ANISOU 2791  O   ARG A 440    18097  19390  22549  -2009   6856  -1993       O  
ATOM   2792  CB  ARG A 440     -38.931 -24.135  30.112  1.00149.36           C  
ANISOU 2792  CB  ARG A 440    17253  18394  21103  -1585   6041  -1472       C  
ATOM   2793  N   VAL A 441     -40.067 -22.061  33.017  1.00152.24           N  
ANISOU 2793  N   VAL A 441    17857  18631  21355  -1733   6683  -1589       N  
ATOM   2794  CA  VAL A 441     -41.238 -21.481  33.687  1.00154.66           C  
ANISOU 2794  CA  VAL A 441    17953  18941  21869  -1901   7038  -1870       C  
ATOM   2795  C   VAL A 441     -42.037 -20.551  32.773  1.00158.02           C  
ANISOU 2795  C   VAL A 441    17703  19668  22670  -1787   6807  -2149       C  
ATOM   2796  O   VAL A 441     -41.458 -19.765  32.019  1.00154.47           O  
ANISOU 2796  O   VAL A 441    17073  19424  22196  -1496   6332  -2021       O  
ATOM   2797  CB  VAL A 441     -40.917 -20.803  35.046  1.00158.80           C  
ANISOU 2797  CB  VAL A 441    18894  19341  22103  -1875   7197  -1702       C  
ATOM   2798  CG1 VAL A 441     -40.730 -21.836  36.151  1.00161.05           C  
ANISOU 2798  CG1 VAL A 441    19808  19281  22103  -2091   7634  -1580       C  
ATOM   2799  CG2 VAL A 441     -39.707 -19.876  34.952  1.00154.87           C  
ANISOU 2799  CG2 VAL A 441    18524  18974  21347  -1540   6708  -1392       C  
ATOM   2800  N   ARG A 442     -43.374 -20.648  32.856  1.00158.05           N  
ANISOU 2800  N   ARG A 442    17345  19689  23018  -2013   7155  -2544       N  
ATOM   2801  CA  ARG A 442     -44.311 -19.838  32.083  1.00158.51           C  
ANISOU 2801  CA  ARG A 442    16746  20022  23457  -1912   6982  -2873       C  
ATOM   2802  C   ARG A 442     -45.427 -19.318  32.986  1.00165.91           C  
ANISOU 2802  C   ARG A 442    17518  20928  24591  -2087   7402  -3173       C  
ATOM   2803  O   ARG A 442     -46.077 -20.104  33.680  1.00168.89           O  
ANISOU 2803  O   ARG A 442    18018  21109  25042  -2424   7927  -3357       O  
ATOM   2804  CB  ARG A 442     -44.886 -20.638  30.904  1.00159.89           C  
ANISOU 2804  CB  ARG A 442    16499  20314  23941  -1989   6904  -3144       C  
ATOM   2805  N   ARG A 443     -45.630 -17.989  32.992  1.00161.99           N  
ANISOU 2805  N   ARG A 443    16768  20610  24172  -1863   7190  -3220       N  
ATOM   2806  CA  ARG A 443     -46.655 -17.331  33.801  1.00165.02           C  
ANISOU 2806  CA  ARG A 443    16957  20992  24752  -1980   7541  -3509       C  
ATOM   2807  C   ARG A 443     -47.525 -16.424  32.933  1.00170.30           C  
ANISOU 2807  C   ARG A 443    16951  21956  25801  -1774   7268  -3837       C  
ATOM   2808  O   ARG A 443     -46.999 -15.601  32.179  1.00166.93           O  
ANISOU 2808  O   ARG A 443    16406  21704  25315  -1431   6762  -3677       O  
ATOM   2809  CB  ARG A 443     -46.016 -16.538  34.954  1.00164.02           C  
ANISOU 2809  CB  ARG A 443    17289  20742  24290  -1905   7609  -3229       C  
ATOM   2810  CG  ARG A 443     -46.967 -16.270  36.117  1.00178.57           C  
ANISOU 2810  CG  ARG A 443    19138  22468  26243  -2142   8146  -3482       C  
ATOM   2811  CD  ARG A 443     -46.388 -15.295  37.125  1.00187.63           C  
ANISOU 2811  CD  ARG A 443    20659  23543  27089  -2018   8141  -3240       C  
ATOM   2812  NE  ARG A 443     -46.462 -13.910  36.657  1.00194.31           N  
ANISOU 2812  NE  ARG A 443    21142  24622  28064  -1702   7757  -3282       N  
ATOM   2813  CZ  ARG A 443     -46.096 -12.852  37.374  1.00209.83           C  
ANISOU 2813  CZ  ARG A 443    23309  26572  29844  -1564   7709  -3136       C  
ATOM   2814  NH1 ARG A 443     -45.627 -13.006  38.607  1.00196.92           N  
ANISOU 2814  NH1 ARG A 443    22227  24718  27877  -1706   8001  -2944       N  
ATOM   2815  NH2 ARG A 443     -46.199 -11.632  36.866  1.00194.93           N  
ANISOU 2815  NH2 ARG A 443    21093  24881  28092  -1277   7368  -3186       N  
ATOM   2816  N   LYS A 444     -48.855 -16.584  33.040  1.00171.37           N  
ANISOU 2816  N   LYS A 444    16652  22139  26323  -1980   7609  -4309       N  
ATOM   2817  CA  LYS A 444     -49.826 -15.790  32.290  1.00172.81           C  
ANISOU 2817  CA  LYS A 444    16163  22600  26896  -1786   7383  -4688       C  
ATOM   2818  C   LYS A 444     -50.136 -14.493  33.034  1.00177.03           C  
ANISOU 2818  C   LYS A 444    16648  23168  27447  -1648   7437  -4733       C  
ATOM   2819  O   LYS A 444     -50.520 -14.533  34.207  1.00179.32           O  
ANISOU 2819  O   LYS A 444    17126  23288  27721  -1900   7934  -4822       O  
ATOM   2820  CB  LYS A 444     -51.107 -16.598  32.030  1.00180.02           C  
ANISOU 2820  CB  LYS A 444    16588  23567  28245  -2071   7713  -5220       C  
ATOM   2821  N   ASN A 445     -49.943 -13.345  32.357  1.00171.07           N  
ANISOU 2821  N   ASN A 445    15681  22614  26705  -1248   6939  -4662       N  
ATOM   2822  CA  ASN A 445     -50.193 -12.016  32.918  1.00170.83           C  
ANISOU 2822  CA  ASN A 445    15591  22625  26693  -1063   6924  -4695       C  
ATOM   2823  C   ASN A 445     -51.707 -11.772  33.058  1.00178.60           C  
ANISOU 2823  C   ASN A 445    15996  23726  28137  -1148   7194  -5255       C  
ATOM   2824  O   ASN A 445     -52.445 -12.010  32.099  1.00180.18           O  
ANISOU 2824  O   ASN A 445    15670  24124  28666  -1076   7020  -5594       O  
ATOM   2825  CB  ASN A 445     -49.531 -10.933  32.062  1.00168.58           C  
ANISOU 2825  CB  ASN A 445    15273  22494  26285   -613   6321  -4458       C  
ATOM   2826  CG  ASN A 445     -49.465  -9.581  32.726  1.00190.40           C  
ANISOU 2826  CG  ASN A 445    18139  25242  28964   -426   6300  -4377       C  
ATOM   2827  OD1 ASN A 445     -50.443  -8.826  32.760  1.00186.59           O  
ANISOU 2827  OD1 ASN A 445    17256  24870  28768   -315   6340  -4709       O  
ATOM   2828  ND2 ASN A 445     -48.299  -9.234  33.248  1.00178.38           N  
ANISOU 2828  ND2 ASN A 445    17144  23583  27049   -378   6225  -3950       N  
ATOM   2829  N   PRO A 446     -52.196 -11.329  34.240  1.00177.80           N  
ANISOU 2829  N   PRO A 446    15971  23513  28072  -1304   7623  -5385       N  
ATOM   2830  CA  PRO A 446     -53.647 -11.130  34.404  1.00182.60           C  
ANISOU 2830  CA  PRO A 446    16006  24233  29141  -1403   7915  -5953       C  
ATOM   2831  C   PRO A 446     -54.213  -9.885  33.721  1.00187.65           C  
ANISOU 2831  C   PRO A 446    16138  25128  30031   -981   7500  -6173       C  
ATOM   2832  O   PRO A 446     -55.376  -9.899  33.316  1.00188.99           O  
ANISOU 2832  O   PRO A 446    15956  25583  30266   -812   7270  -6250       O  
ATOM   2833  CB  PRO A 446     -53.837 -11.072  35.928  1.00185.82           C  
ANISOU 2833  CB  PRO A 446    16786  24434  29384  -1677   8461  -5897       C  
ATOM   2834  CG  PRO A 446     -52.484 -11.364  36.532  1.00187.17           C  
ANISOU 2834  CG  PRO A 446    17685  24344  29085  -1774   8530  -5404       C  
ATOM   2835  CD  PRO A 446     -51.477 -11.023  35.490  1.00178.22           C  
ANISOU 2835  CD  PRO A 446    16625  23336  27754  -1407   7878  -5051       C  
ATOM   2836  N   VAL A 447     -53.406  -8.814  33.605  1.00180.39           N  
ANISOU 2836  N   VAL A 447    15473  24220  28846   -631   7107  -5814       N  
ATOM   2837  CA  VAL A 447     -53.818  -7.539  33.004  1.00180.37           C  
ANISOU 2837  CA  VAL A 447    15103  24414  29014   -193   6703  -5955       C  
ATOM   2838  C   VAL A 447     -53.912  -7.632  31.470  1.00183.70           C  
ANISOU 2838  C   VAL A 447    15159  25065  29574    113   6155  -6041       C  
ATOM   2839  O   VAL A 447     -54.947  -7.275  30.905  1.00186.57           O  
ANISOU 2839  O   VAL A 447    14950  25635  30302    310   6005  -6470       O  
ATOM   2840  CB  VAL A 447     -52.933  -6.345  33.476  1.00180.83           C  
ANISOU 2840  CB  VAL A 447    15600  24372  28737     44   6530  -5552       C  
ATOM   2841  CG1 VAL A 447     -53.458  -5.012  32.945  1.00181.60           C  
ANISOU 2841  CG1 VAL A 447    15343  24635  29023    485   6176  -5725       C  
ATOM   2842  CG2 VAL A 447     -52.824  -6.301  35.000  1.00181.20           C  
ANISOU 2842  CG2 VAL A 447    16032  24195  28620   -260   7062  -5472       C  
ATOM   2843  N   THR A 448     -52.838  -8.103  30.808  1.00176.22           N  
ANISOU 2843  N   THR A 448    14541  24084  28332    165   5855  -5650       N  
ATOM   2844  CA  THR A 448     -52.769  -8.209  29.346  1.00175.19           C  
ANISOU 2844  CA  THR A 448    14156  24146  28260    454   5328  -5671       C  
ATOM   2845  C   THR A 448     -53.452  -9.461  28.788  1.00180.67           C  
ANISOU 2845  C   THR A 448    14471  24943  29233    225   5435  -6025       C  
ATOM   2846  O   THR A 448     -54.081  -9.388  27.732  1.00181.98           O  
ANISOU 2846  O   THR A 448    14165  25336  29645    464   5094  -6321       O  
ATOM   2847  CB  THR A 448     -51.319  -8.093  28.851  1.00181.60           C  
ANISOU 2847  CB  THR A 448    15473  24881  28645    618   4965  -5118       C  
ATOM   2848  OG1 THR A 448     -50.547  -9.171  29.379  1.00179.23           O  
ANISOU 2848  OG1 THR A 448    15591  24398  28112    263   5242  -4858       O  
ATOM   2849  CG2 THR A 448     -50.679  -6.758  29.211  1.00177.64           C  
ANISOU 2849  CG2 THR A 448    15287  24305  27902    882   4802  -4813       C  
ATOM   2850  N   GLY A 449     -53.307 -10.586  29.487  1.00177.09           N  
ANISOU 2850  N   GLY A 449    14248  24315  28724   -222   5897  -5993       N  
ATOM   2851  CA  GLY A 449     -53.869 -11.868  29.076  1.00179.20           C  
ANISOU 2851  CA  GLY A 449    14230  24628  29231   -507   6077  -6306       C  
ATOM   2852  C   GLY A 449     -52.952 -12.661  28.165  1.00179.43           C  
ANISOU 2852  C   GLY A 449    14493  24650  29033   -479   5770  -6003       C  
ATOM   2853  O   GLY A 449     -53.378 -13.654  27.570  1.00181.15           O  
ANISOU 2853  O   GLY A 449    14444  24936  29447   -647   5810  -6260       O  
ATOM   2854  N   ASN A 450     -51.680 -12.223  28.055  1.00170.53           N  
ANISOU 2854  N   ASN A 450    13858  23437  27499   -275   5473  -5474       N  
ATOM   2855  CA  ASN A 450     -50.648 -12.850  27.226  1.00166.58           C  
ANISOU 2855  CA  ASN A 450    13633  22919  26742   -217   5164  -5136       C  
ATOM   2856  C   ASN A 450     -49.734 -13.750  28.060  1.00167.77           C  
ANISOU 2856  C   ASN A 450    14355  22801  26588   -547   5504  -4793       C  
ATOM   2857  O   ASN A 450     -49.495 -13.465  29.236  1.00167.18           O  
ANISOU 2857  O   ASN A 450    14611  22550  26358   -687   5826  -4645       O  
ATOM   2858  CB  ASN A 450     -49.815 -11.783  26.499  1.00163.71           C  
ANISOU 2858  CB  ASN A 450    13430  22636  26135    225   4619  -4799       C  
ATOM   2859  CG  ASN A 450     -50.612 -10.811  25.655  1.00188.02           C  
ANISOU 2859  CG  ASN A 450    16036  25953  29451    614   4241  -5083       C  
ATOM   2860  OD1 ASN A 450     -51.481 -11.190  24.859  1.00184.91           O  
ANISOU 2860  OD1 ASN A 450    15158  25746  29354    665   4111  -5473       O  
ATOM   2861  ND2 ASN A 450     -50.299  -9.531  25.782  1.00178.44           N  
ANISOU 2861  ND2 ASN A 450    14969  24733  28097    914   4037  -4893       N  
ATOM   2862  N   TYR A 451     -49.218 -14.829  27.444  1.00162.60           N  
ANISOU 2862  N   TYR A 451    13829  22112  25838   -654   5421  -4670       N  
ATOM   2863  CA  TYR A 451     -48.326 -15.785  28.099  1.00160.50           C  
ANISOU 2863  CA  TYR A 451    14109  21594  25279   -928   5694  -4350       C  
ATOM   2864  C   TYR A 451     -46.876 -15.299  28.070  1.00159.14           C  
ANISOU 2864  C   TYR A 451    14425  21354  24687   -704   5377  -3822       C  
ATOM   2865  O   TYR A 451     -46.374 -14.918  27.010  1.00156.57           O  
ANISOU 2865  O   TYR A 451    14027  21171  24293   -412   4904  -3685       O  
ATOM   2866  CB  TYR A 451     -48.449 -17.180  27.451  1.00162.67           C  
ANISOU 2866  CB  TYR A 451    14295  21853  25661  -1145   5766  -4483       C  
ATOM   2867  CG  TYR A 451     -48.509 -18.352  28.415  1.00166.24           C  
ANISOU 2867  CG  TYR A 451    15064  22036  26064  -1581   6337  -4495       C  
ATOM   2868  CD1 TYR A 451     -48.329 -18.168  29.784  1.00168.61           C  
ANISOU 2868  CD1 TYR A 451    15768  22117  26179  -1745   6730  -4343       C  
ATOM   2869  CD2 TYR A 451     -48.740 -19.645  27.956  1.00168.51           C  
ANISOU 2869  CD2 TYR A 451    15279  22271  26474  -1827   6491  -4657       C  
ATOM   2870  CE1 TYR A 451     -48.385 -19.242  30.672  1.00171.33           C  
ANISOU 2870  CE1 TYR A 451    16463  22188  26447  -2132   7265  -4344       C  
ATOM   2871  CE2 TYR A 451     -48.796 -20.727  28.834  1.00171.30           C  
ANISOU 2871  CE2 TYR A 451    15974  22344  26769  -2225   7038  -4662       C  
ATOM   2872  CZ  TYR A 451     -48.618 -20.520  30.192  1.00179.05           C  
ANISOU 2872  CZ  TYR A 451    17382  23100  27549  -2371   7424  -4498       C  
ATOM   2873  OH  TYR A 451     -48.673 -21.582  31.063  1.00181.46           O  
ANISOU 2873  OH  TYR A 451    18079  23104  27763  -2749   7973  -4492       O  
ATOM   2874  N   VAL A 452     -46.214 -15.303  29.242  1.00153.92           N  
ANISOU 2874  N   VAL A 452    14263  20476  23744   -842   5645  -3545       N  
ATOM   2875  CA  VAL A 452     -44.818 -14.876  29.407  1.00149.49           C  
ANISOU 2875  CA  VAL A 452    14175  19837  22786   -669   5398  -3074       C  
ATOM   2876  C   VAL A 452     -43.965 -16.106  29.744  1.00151.31           C  
ANISOU 2876  C   VAL A 452    14866  19866  22759   -877   5560  -2822       C  
ATOM   2877  O   VAL A 452     -44.283 -16.826  30.693  1.00152.98           O  
ANISOU 2877  O   VAL A 452    15285  19887  22953  -1174   6016  -2891       O  
ATOM   2878  CB  VAL A 452     -44.664 -13.745  30.468  1.00153.06           C  
ANISOU 2878  CB  VAL A 452    14834  20224  23096   -597   5503  -2959       C  
ATOM   2879  CG1 VAL A 452     -43.241 -13.190  30.486  1.00149.03           C  
ANISOU 2879  CG1 VAL A 452    14732  19676  22215   -392   5192  -2523       C  
ATOM   2880  CG2 VAL A 452     -45.672 -12.620  30.238  1.00154.67           C  
ANISOU 2880  CG2 VAL A 452    14575  20602  23590   -415   5414  -3258       C  
ATOM   2881  N   LYS A 453     -42.894 -16.348  28.964  1.00144.11           N  
ANISOU 2881  N   LYS A 453    14125  18985  21646   -716   5196  -2539       N  
ATOM   2882  CA  LYS A 453     -42.001 -17.497  29.153  1.00142.50           C  
ANISOU 2882  CA  LYS A 453    14345  18603  21194   -855   5281  -2293       C  
ATOM   2883  C   LYS A 453     -40.553 -17.090  29.421  1.00142.20           C  
ANISOU 2883  C   LYS A 453    14744  18509  20777   -675   5035  -1875       C  
ATOM   2884  O   LYS A 453     -40.036 -16.180  28.768  1.00139.43           O  
ANISOU 2884  O   LYS A 453    14293  18304  20378   -409   4650  -1755       O  
ATOM   2885  CB  LYS A 453     -42.059 -18.447  27.942  1.00144.97           C  
ANISOU 2885  CB  LYS A 453    14446  18994  21643   -872   5113  -2388       C  
ATOM   2886  CG  LYS A 453     -43.382 -19.196  27.784  1.00163.37           C  
ANISOU 2886  CG  LYS A 453    16407  21338  24328  -1123   5421  -2812       C  
ATOM   2887  CD  LYS A 453     -43.262 -20.404  26.854  1.00173.54           C  
ANISOU 2887  CD  LYS A 453    17635  22625  25678  -1213   5348  -2860       C  
ATOM   2888  CE  LYS A 453     -43.512 -20.074  25.400  1.00183.95           C  
ANISOU 2888  CE  LYS A 453    18498  24211  27183   -979   4905  -3012       C  
ATOM   2889  NZ  LYS A 453     -43.361 -21.271  24.532  1.00193.28           N  
ANISOU 2889  NZ  LYS A 453    19644  25384  28410  -1078   4848  -3061       N  
ATOM   2890  N   MET A 454     -39.895 -17.784  30.372  1.00138.20           N  
ANISOU 2890  N   MET A 454    14729  17782  19998   -820   5263  -1667       N  
ATOM   2891  CA  MET A 454     -38.490 -17.565  30.731  1.00135.04           C  
ANISOU 2891  CA  MET A 454    14757  17319  19231   -669   5053  -1299       C  
ATOM   2892  C   MET A 454     -37.796 -18.867  31.174  1.00138.43           C  
ANISOU 2892  C   MET A 454    15641  17535  19421   -802   5207  -1117       C  
ATOM   2893  O   MET A 454     -38.455 -19.783  31.671  1.00140.66           O  
ANISOU 2893  O   MET A 454    16028  17652  19765  -1053   5599  -1251       O  
ATOM   2894  CB  MET A 454     -38.318 -16.420  31.756  1.00137.16           C  
ANISOU 2894  CB  MET A 454    15196  17567  19353   -598   5104  -1216       C  
ATOM   2895  CG  MET A 454     -38.673 -16.782  33.182  1.00143.32           C  
ANISOU 2895  CG  MET A 454    16315  18130  20010   -823   5563  -1241       C  
ATOM   2896  SD  MET A 454     -38.109 -15.538  34.363  1.00146.75           S  
ANISOU 2896  SD  MET A 454    17049  18533  20177   -708   5550  -1075       S  
ATOM   2897  CE  MET A 454     -38.496 -16.351  35.890  1.00146.76           C  
ANISOU 2897  CE  MET A 454    17516  18246  19998   -993   6106  -1096       C  
ATOM   2898  N   SER A 455     -36.468 -18.943  30.973  1.00131.91           N  
ANISOU 2898  N   SER A 455    15082  16708  18329   -629   4905   -825       N  
ATOM   2899  CA  SER A 455     -35.643 -20.106  31.305  1.00131.49           C  
ANISOU 2899  CA  SER A 455    15468  16468  18024   -679   4965   -628       C  
ATOM   2900  C   SER A 455     -34.858 -19.932  32.607  1.00134.87           C  
ANISOU 2900  C   SER A 455    16404  16746  18096   -641   5044   -409       C  
ATOM   2901  O   SER A 455     -34.438 -18.821  32.939  1.00133.10           O  
ANISOU 2901  O   SER A 455    16184  16615  17772   -494   4874   -329       O  
ATOM   2902  CB  SER A 455     -34.690 -20.422  30.156  1.00132.43           C  
ANISOU 2902  CB  SER A 455    15522  16695  18100   -504   4569   -484       C  
ATOM   2903  OG  SER A 455     -33.949 -21.607  30.396  1.00141.37           O  
ANISOU 2903  OG  SER A 455    17049  17648  19016   -536   4619   -317       O  
ATOM   2904  N   LEU A 456     -34.649 -21.049  33.326  1.00132.78           N  
ANISOU 2904  N   LEU A 456    16585  16238  17629   -764   5296   -317       N  
ATOM   2905  CA  LEU A 456     -33.900 -21.123  34.581  1.00133.06           C  
ANISOU 2905  CA  LEU A 456    17173  16099  17286   -717   5376   -111       C  
ATOM   2906  C   LEU A 456     -32.843 -22.224  34.497  1.00136.09           C  
ANISOU 2906  C   LEU A 456    17938  16353  17418   -624   5242    103       C  
ATOM   2907  O   LEU A 456     -33.163 -23.353  34.123  1.00136.91           O  
ANISOU 2907  O   LEU A 456    18092  16328  17601   -757   5411     53       O  
ATOM   2908  CB  LEU A 456     -34.845 -21.383  35.770  1.00136.61           C  
ANISOU 2908  CB  LEU A 456    17878  16329  17699   -962   5897   -228       C  
ATOM   2909  CG  LEU A 456     -35.430 -20.154  36.462  1.00141.86           C  
ANISOU 2909  CG  LEU A 456    18414  17066  18418   -986   6018   -340       C  
ATOM   2910  CD1 LEU A 456     -36.705 -20.506  37.192  1.00145.67           C  
ANISOU 2910  CD1 LEU A 456    18948  17375  19027  -1284   6570   -561       C  
ATOM   2911  CD2 LEU A 456     -34.438 -19.545  37.441  1.00143.63           C  
ANISOU 2911  CD2 LEU A 456    19043  17259  18270   -814   5869   -121       C  
ATOM   2912  N   GLN A 457     -31.585 -21.890  34.832  1.00130.76           N  
ANISOU 2912  N   GLN A 457    17518  15713  16451   -393   4935    321       N  
ATOM   2913  CA  GLN A 457     -30.456 -22.823  34.802  1.00130.11           C  
ANISOU 2913  CA  GLN A 457    17793  15530  16114   -249   4752    521       C  
ATOM   2914  C   GLN A 457     -29.518 -22.572  35.985  1.00134.10           C  
ANISOU 2914  C   GLN A 457    18773  15954  16224    -85   4659    701       C  
ATOM   2915  O   GLN A 457     -29.193 -21.420  36.281  1.00132.38           O  
ANISOU 2915  O   GLN A 457    18450  15889  15960     21   4485    710       O  
ATOM   2916  CB  GLN A 457     -29.703 -22.716  33.458  1.00128.46           C  
ANISOU 2916  CB  GLN A 457    17239  15536  16033    -80   4329    560       C  
ATOM   2917  CG  GLN A 457     -28.586 -23.744  33.249  1.00144.02           C  
ANISOU 2917  CG  GLN A 457    19503  17420  17798     71   4134    731       C  
ATOM   2918  CD  GLN A 457     -29.099 -25.115  32.890  1.00165.67           C  
ANISOU 2918  CD  GLN A 457    22352  19972  20623    -84   4375    687       C  
ATOM   2919  OE1 GLN A 457     -29.405 -25.405  31.731  1.00160.48           O  
ANISOU 2919  OE1 GLN A 457    21341  19412  20221   -138   4306    586       O  
ATOM   2920  NE2 GLN A 457     -29.169 -25.998  33.874  1.00160.62           N  
ANISOU 2920  NE2 GLN A 457    22231  19047  19752   -152   4660    760       N  
ATOM   2921  N   LEU A 458     -29.087 -23.656  36.656  1.00132.49           N  
ANISOU 2921  N   LEU A 458    19103  15506  15731    -55   4772    834       N  
ATOM   2922  CA  LEU A 458     -28.181 -23.585  37.800  1.00133.26           C  
ANISOU 2922  CA  LEU A 458    19708  15509  15417    129   4668   1000       C  
ATOM   2923  C   LEU A 458     -26.744 -23.923  37.396  1.00135.31           C  
ANISOU 2923  C   LEU A 458    20057  15850  15505    417   4224   1152       C  
ATOM   2924  O   LEU A 458     -26.503 -24.935  36.736  1.00134.87           O  
ANISOU 2924  O   LEU A 458    20036  15720  15488    440   4180   1194       O  
ATOM   2925  CB  LEU A 458     -28.660 -24.502  38.942  1.00137.21           C  
ANISOU 2925  CB  LEU A 458    20811  15662  15661      2   5096   1046       C  
ATOM   2926  CG  LEU A 458     -28.049 -24.241  40.323  1.00143.78           C  
ANISOU 2926  CG  LEU A 458    22187  16384  16060    157   5069   1175       C  
ATOM   2927  CD1 LEU A 458     -28.854 -23.213  41.096  1.00144.78           C  
ANISOU 2927  CD1 LEU A 458    22254  16538  16219      7   5319   1061       C  
ATOM   2928  CD2 LEU A 458     -27.959 -25.520  41.127  1.00149.86           C  
ANISOU 2928  CD2 LEU A 458    23652  16796  16491    163   5320   1303       C  
ATOM   2929  N   TYR A 459     -25.799 -23.060  37.799  1.00130.55           N  
ANISOU 2929  N   TYR A 459    19476  15401  14725    627   3904   1212       N  
ATOM   2930  CA  TYR A 459     -24.363 -23.193  37.546  1.00129.07           C  
ANISOU 2930  CA  TYR A 459    19342  15324  14373    913   3466   1319       C  
ATOM   2931  C   TYR A 459     -23.595 -23.141  38.877  1.00134.70           C  
ANISOU 2931  C   TYR A 459    20569  15949  14664   1108   3367   1419       C  
ATOM   2932  O   TYR A 459     -24.200 -22.905  39.925  1.00136.35           O  
ANISOU 2932  O   TYR A 459    21068  16021  14716   1010   3639   1411       O  
ATOM   2933  CB  TYR A 459     -23.872 -22.049  36.637  1.00126.95           C  
ANISOU 2933  CB  TYR A 459    18529  15374  14331    984   3134   1249       C  
ATOM   2934  CG  TYR A 459     -24.517 -21.975  35.270  1.00126.62           C  
ANISOU 2934  CG  TYR A 459    17983  15451  14677    843   3162   1151       C  
ATOM   2935  CD1 TYR A 459     -24.024 -22.721  34.203  1.00127.45           C  
ANISOU 2935  CD1 TYR A 459    17945  15595  14886    911   2986   1179       C  
ATOM   2936  CD2 TYR A 459     -25.562 -21.091  35.019  1.00126.63           C  
ANISOU 2936  CD2 TYR A 459    17639  15540  14933    670   3330   1021       C  
ATOM   2937  CE1 TYR A 459     -24.591 -22.630  32.933  1.00126.47           C  
ANISOU 2937  CE1 TYR A 459    17372  15587  15093    798   2988   1083       C  
ATOM   2938  CE2 TYR A 459     -26.136 -20.989  33.752  1.00125.86           C  
ANISOU 2938  CE2 TYR A 459    17087  15564  15171    577   3315    921       C  
ATOM   2939  CZ  TYR A 459     -25.645 -21.758  32.710  1.00132.02           C  
ANISOU 2939  CZ  TYR A 459    17752  16378  16032    640   3141    954       C  
ATOM   2940  OH  TYR A 459     -26.211 -21.665  31.462  1.00131.35           O  
ANISOU 2940  OH  TYR A 459    17242  16413  16253    561   3114    850       O  
ATOM   2941  N   LEU A 460     -22.265 -23.348  38.832  1.00130.69           N  
ANISOU 2941  N   LEU A 460    20162  15523  13969   1390   2973   1494       N  
ATOM   2942  CA  LEU A 460     -21.396 -23.267  40.007  1.00132.43           C  
ANISOU 2942  CA  LEU A 460    20826  15704  13787   1627   2791   1564       C  
ATOM   2943  C   LEU A 460     -20.140 -22.447  39.695  1.00134.18           C  
ANISOU 2943  C   LEU A 460    20745  16220  14018   1847   2318   1514       C  
ATOM   2944  O   LEU A 460     -19.480 -22.686  38.681  1.00131.93           O  
ANISOU 2944  O   LEU A 460    20165  16068  13895   1939   2070   1502       O  
ATOM   2945  CB  LEU A 460     -21.089 -24.647  40.668  1.00135.76           C  
ANISOU 2945  CB  LEU A 460    21889  15833  13860   1782   2852   1703       C  
ATOM   2946  CG  LEU A 460     -20.235 -25.765  39.997  1.00140.54           C  
ANISOU 2946  CG  LEU A 460    22569  16397  14432   1989   2612   1778       C  
ATOM   2947  CD1 LEU A 460     -20.682 -26.127  38.595  1.00140.67           C  
ANISOU 2947  CD1 LEU A 460    22136  16468  14844   1813   2690   1730       C  
ATOM   2948  CD2 LEU A 460     -18.736 -25.558  40.159  1.00140.67           C  
ANISOU 2948  CD2 LEU A 460    22599  16595  14252   2349   2105   1783       C  
ATOM   2949  N   VAL A 461     -19.858 -21.436  40.536  1.00131.11           N  
ANISOU 2949  N   VAL A 461    20406  15934  13476   1905   2221   1464       N  
ATOM   2950  CA  VAL A 461     -18.715 -20.530  40.379  1.00129.51           C  
ANISOU 2950  CA  VAL A 461    19919  16006  13282   2078   1813   1380       C  
ATOM   2951  C   VAL A 461     -17.436 -21.215  40.880  1.00135.24           C  
ANISOU 2951  C   VAL A 461    20976  16726  13685   2413   1468   1423       C  
ATOM   2952  O   VAL A 461     -16.497 -21.399  40.104  1.00133.61           O  
ANISOU 2952  O   VAL A 461    20513  16671  13583   2561   1162   1387       O  
ATOM   2953  CB  VAL A 461     -18.951 -19.142  41.047  1.00133.23           C  
ANISOU 2953  CB  VAL A 461    20289  16591  13741   1992   1855   1284       C  
ATOM   2954  CG1 VAL A 461     -17.838 -18.157  40.692  1.00131.40           C  
ANISOU 2954  CG1 VAL A 461    19689  16646  13593   2114   1476   1167       C  
ATOM   2955  CG2 VAL A 461     -20.313 -18.562  40.670  1.00131.68           C  
ANISOU 2955  CG2 VAL A 461    19827  16367  13837   1689   2218   1239       C  
ATOM   2956  N   ASP A 462     -17.413 -21.596  42.172  1.00134.96           N  
ANISOU 2956  N   ASP A 462    21516  16511  13253   2541   1521   1490       N  
ATOM   2957  CA  ASP A 462     -16.288 -22.266  42.826  1.00137.35           C  
ANISOU 2957  CA  ASP A 462    22218  16780  13190   2898   1193   1530       C  
ATOM   2958  C   ASP A 462     -16.732 -23.615  43.424  1.00144.10           C  
ANISOU 2958  C   ASP A 462    23723  17277  13753   2960   1429   1697       C  
ATOM   2959  O   ASP A 462     -17.823 -24.092  43.101  1.00143.34           O  
ANISOU 2959  O   ASP A 462    23669  16987  13807   2703   1831   1761       O  
ATOM   2960  CB  ASP A 462     -15.675 -21.346  43.898  1.00140.67           C  
ANISOU 2960  CB  ASP A 462    22766  17334  13349   3050    970   1436       C  
ATOM   2961  N   ASN A 463     -15.881 -24.233  44.274  1.00143.74           N  
ANISOU 2961  N   ASN A 463    24184  17139  13291   3305   1178   1753       N  
ATOM   2962  CA  ASN A 463     -16.146 -25.517  44.934  1.00147.03           C  
ANISOU 2962  CA  ASN A 463    25310  17191  13361   3421   1367   1921       C  
ATOM   2963  C   ASN A 463     -17.370 -25.452  45.861  1.00152.43           C  
ANISOU 2963  C   ASN A 463    26428  17609  13879   3174   1867   1991       C  
ATOM   2964  O   ASN A 463     -18.188 -26.374  45.851  1.00153.33           O  
ANISOU 2964  O   ASN A 463    26868  17417  13974   3018   2258   2101       O  
ATOM   2965  CB  ASN A 463     -14.900 -25.995  45.698  1.00151.20           C  
ANISOU 2965  CB  ASN A 463    26277  17714  13458   3889    932   1943       C  
ATOM   2966  CG  ASN A 463     -15.037 -27.348  46.359  1.00177.73           C  
ANISOU 2966  CG  ASN A 463    30426  20680  16421   4069   1083   2128       C  
ATOM   2967  OD1 ASN A 463     -15.314 -28.367  45.714  1.00172.04           O  
ANISOU 2967  OD1 ASN A 463    29791  19764  15810   4015   1256   2225       O  
ATOM   2968  ND2 ASN A 463     -14.809 -27.393  47.663  1.00173.14           N  
ANISOU 2968  ND2 ASN A 463    30464  19967  15353   4301   1011   2177       N  
ATOM   2969  N   ARG A 464     -17.496 -24.361  46.641  1.00148.93           N  
ANISOU 2969  N   ARG A 464    25976  17279  13331   3124   1872   1910       N  
ATOM   2970  CA  ARG A 464     -18.605 -24.143  47.575  1.00150.48           C  
ANISOU 2970  CA  ARG A 464    26550  17254  13371   2891   2336   1946       C  
ATOM   2971  C   ARG A 464     -19.531 -22.987  47.142  1.00150.75           C  
ANISOU 2971  C   ARG A 464    26017  17452  13810   2523   2590   1819       C  
ATOM   2972  O   ARG A 464     -20.413 -22.587  47.908  1.00151.66           O  
ANISOU 2972  O   ARG A 464    26348  17441  13835   2328   2946   1806       O  
ATOM   2973  CB  ARG A 464     -18.068 -23.929  49.001  1.00154.48           C  
ANISOU 2973  CB  ARG A 464    27641  17701  13351   3156   2174   1965       C  
ATOM   2974  N   SER A 465     -19.344 -22.474  45.907  1.00142.97           N  
ANISOU 2974  N   SER A 465    24327  16734  13263   2438   2416   1725       N  
ATOM   2975  CA  SER A 465     -20.139 -21.378  45.348  1.00139.60           C  
ANISOU 2975  CA  SER A 465    23336  16473  13234   2137   2599   1604       C  
ATOM   2976  C   SER A 465     -21.064 -21.860  44.228  1.00140.88           C  
ANISOU 2976  C   SER A 465    23168  16570  13789   1875   2887   1607       C  
ATOM   2977  O   SER A 465     -20.635 -22.625  43.361  1.00139.50           O  
ANISOU 2977  O   SER A 465    22867  16407  13730   1959   2733   1650       O  
ATOM   2978  CB  SER A 465     -19.231 -20.262  44.839  1.00140.51           C  
ANISOU 2978  CB  SER A 465    22921  16943  13523   2242   2183   1477       C  
ATOM   2979  OG  SER A 465     -18.387 -19.767  45.866  1.00151.22           O  
ANISOU 2979  OG  SER A 465    24539  18381  14537   2472   1909   1435       O  
ATOM   2980  N   TYR A 466     -22.334 -21.412  44.255  1.00136.54           N  
ANISOU 2980  N   TYR A 466    22473  15959  13448   1564   3300   1542       N  
ATOM   2981  CA  TYR A 466     -23.358 -21.761  43.264  1.00134.64           C  
ANISOU 2981  CA  TYR A 466    21891  15672  13595   1296   3594   1500       C  
ATOM   2982  C   TYR A 466     -24.067 -20.518  42.717  1.00135.47           C  
ANISOU 2982  C   TYR A 466    21410  15985  14076   1093   3673   1352       C  
ATOM   2983  O   TYR A 466     -24.131 -19.494  43.401  1.00135.19           O  
ANISOU 2983  O   TYR A 466    21370  16030  13967   1082   3678   1291       O  
ATOM   2984  CB  TYR A 466     -24.364 -22.769  43.847  1.00138.90           C  
ANISOU 2984  CB  TYR A 466    22902  15859  14013   1108   4093   1551       C  
ATOM   2985  CG  TYR A 466     -23.808 -24.172  43.972  1.00142.72           C  
ANISOU 2985  CG  TYR A 466    23887  16113  14228   1280   4047   1700       C  
ATOM   2986  CD1 TYR A 466     -23.960 -25.097  42.945  1.00143.81           C  
ANISOU 2986  CD1 TYR A 466    23859  16190  14592   1213   4094   1717       C  
ATOM   2987  CD2 TYR A 466     -23.135 -24.577  45.122  1.00146.61           C  
ANISOU 2987  CD2 TYR A 466    25039  16440  14227   1525   3950   1819       C  
ATOM   2988  CE1 TYR A 466     -23.443 -26.388  43.051  1.00146.66           C  
ANISOU 2988  CE1 TYR A 466    24694  16322  14708   1381   4056   1853       C  
ATOM   2989  CE2 TYR A 466     -22.614 -25.865  45.239  1.00149.75           C  
ANISOU 2989  CE2 TYR A 466    25928  16609  14362   1717   3894   1960       C  
ATOM   2990  CZ  TYR A 466     -22.771 -26.768  44.201  1.00156.01           C  
ANISOU 2990  CZ  TYR A 466    26543  17334  15400   1640   3957   1979       C  
ATOM   2991  OH  TYR A 466     -22.266 -28.040  44.313  1.00159.15           O  
ANISOU 2991  OH  TYR A 466    27441  17488  15542   1834   3913   2117       O  
ATOM   2992  N   LEU A 467     -24.588 -20.609  41.480  1.00129.51           N  
ANISOU 2992  N   LEU A 467    20180  15314  13715    948   3723   1289       N  
ATOM   2993  CA  LEU A 467     -25.262 -19.507  40.792  1.00126.86           C  
ANISOU 2993  CA  LEU A 467    19278  15172  13749    792   3766   1150       C  
ATOM   2994  C   LEU A 467     -26.553 -19.955  40.100  1.00130.44           C  
ANISOU 2994  C   LEU A 467    19486  15544  14531    535   4111   1060       C  
ATOM   2995  O   LEU A 467     -26.628 -21.075  39.593  1.00130.40           O  
ANISOU 2995  O   LEU A 467    19555  15423  14567    504   4177   1102       O  
ATOM   2996  CB  LEU A 467     -24.295 -18.895  39.758  1.00123.77           C  
ANISOU 2996  CB  LEU A 467    18451  15056  13520    949   3325   1136       C  
ATOM   2997  N   LEU A 468     -27.553 -19.056  40.058  1.00126.51           N  
ANISOU 2997  N   LEU A 468    18674  15118  14275    361   4317    917       N  
ATOM   2998  CA  LEU A 468     -28.836 -19.261  39.385  1.00126.41           C  
ANISOU 2998  CA  LEU A 468    18331  15081  14618    127   4614    774       C  
ATOM   2999  C   LEU A 468     -28.963 -18.216  38.270  1.00127.39           C  
ANISOU 2999  C   LEU A 468    17848  15474  15080    155   4385    671       C  
ATOM   3000  O   LEU A 468     -28.770 -17.023  38.520  1.00125.93           O  
ANISOU 3000  O   LEU A 468    17536  15421  14890    222   4260    641       O  
ATOM   3001  CB  LEU A 468     -30.008 -19.159  40.382  1.00129.28           C  
ANISOU 3001  CB  LEU A 468    18879  15273  14970    -96   5095    666       C  
ATOM   3002  CG  LEU A 468     -31.413 -19.464  39.840  1.00134.90           C  
ANISOU 3002  CG  LEU A 468    19266  15941  16047   -359   5453    473       C  
ATOM   3003  CD1 LEU A 468     -31.666 -20.964  39.749  1.00137.03           C  
ANISOU 3003  CD1 LEU A 468    19801  15981  16283   -485   5697    501       C  
ATOM   3004  CD2 LEU A 468     -32.474 -18.827  40.708  1.00139.46           C  
ANISOU 3004  CD2 LEU A 468    19856  16451  16681   -543   5841    319       C  
ATOM   3005  N   ASP A 469     -29.265 -18.671  37.043  1.00122.90           N  
ANISOU 3005  N   ASP A 469    16936  14975  14787    111   4328    617       N  
ATOM   3006  CA  ASP A 469     -29.384 -17.807  35.868  1.00120.30           C  
ANISOU 3006  CA  ASP A 469    16072  14880  14757    158   4102    530       C  
ATOM   3007  C   ASP A 469     -30.815 -17.691  35.342  1.00125.11           C  
ANISOU 3007  C   ASP A 469    16308  15512  15715    -25   4352    325       C  
ATOM   3008  O   ASP A 469     -31.542 -18.686  35.292  1.00126.44           O  
ANISOU 3008  O   ASP A 469    16521  15547  15975   -190   4621    252       O  
ATOM   3009  CB  ASP A 469     -28.428 -18.284  34.759  1.00120.01           C  
ANISOU 3009  CB  ASP A 469    15910  14946  14743    303   3757    623       C  
ATOM   3010  CG  ASP A 469     -28.499 -17.488  33.472  1.00127.51           C  
ANISOU 3010  CG  ASP A 469    16366  16114  15969    358   3528    547       C  
ATOM   3011  OD1 ASP A 469     -28.061 -16.317  33.472  1.00126.65           O  
ANISOU 3011  OD1 ASP A 469    16136  16137  15850    460   3346    554       O  
ATOM   3012  OD2 ASP A 469     -28.998 -18.034  32.465  1.00133.15           O  
ANISOU 3012  OD2 ASP A 469    16832  16857  16902    299   3540    476       O  
ATOM   3013  N   PHE A 470     -31.199 -16.468  34.931  1.00120.64           N  
ANISOU 3013  N   PHE A 470    15372  15116  15349     14   4254    221       N  
ATOM   3014  CA  PHE A 470     -32.507 -16.146  34.362  1.00121.15           C  
ANISOU 3014  CA  PHE A 470    15024  15249  15760    -99   4415      2       C  
ATOM   3015  C   PHE A 470     -32.321 -15.732  32.898  1.00122.78           C  
ANISOU 3015  C   PHE A 470    14820  15656  16175     37   4078    -21       C  
ATOM   3016  O   PHE A 470     -31.578 -14.789  32.615  1.00120.44           O  
ANISOU 3016  O   PHE A 470    14461  15480  15820    202   3799     63       O  
ATOM   3017  CB  PHE A 470     -33.185 -15.013  35.155  1.00124.02           C  
ANISOU 3017  CB  PHE A 470    15326  15624  16170   -138   4591   -113       C  
ATOM   3018  CG  PHE A 470     -33.518 -15.317  36.596  1.00128.21           C  
ANISOU 3018  CG  PHE A 470    16252  15956  16508   -288   4963   -119       C  
ATOM   3019  CD1 PHE A 470     -32.584 -15.104  37.604  1.00131.34           C  
ANISOU 3019  CD1 PHE A 470    17071  16280  16552   -203   4900     48       C  
ATOM   3020  CD2 PHE A 470     -34.785 -15.762  36.953  1.00133.11           C  
ANISOU 3020  CD2 PHE A 470    16815  16463  17297   -514   5382   -313       C  
ATOM   3021  CE1 PHE A 470     -32.899 -15.370  38.939  1.00134.93           C  
ANISOU 3021  CE1 PHE A 470    17931  16542  16795   -329   5244     46       C  
ATOM   3022  CE2 PHE A 470     -35.102 -16.017  38.290  1.00138.61           C  
ANISOU 3022  CE2 PHE A 470    17909  16958  17799   -663   5760   -320       C  
ATOM   3023  CZ  PHE A 470     -34.157 -15.822  39.274  1.00136.66           C  
ANISOU 3023  CZ  PHE A 470    18121  16630  17172   -563   5685   -129       C  
ATOM   3024  N   LYS A 471     -32.976 -16.454  31.973  1.00119.76           N  
ANISOU 3024  N   LYS A 471    14182  15300  16022    -37   4115   -141       N  
ATOM   3025  CA  LYS A 471     -32.909 -16.200  30.531  1.00117.80           C  
ANISOU 3025  CA  LYS A 471    13568  15229  15962     87   3815   -177       C  
ATOM   3026  C   LYS A 471     -34.306 -15.869  29.993  1.00123.25           C  
ANISOU 3026  C   LYS A 471    13836  16007  16986     24   3927   -441       C  
ATOM   3027  O   LYS A 471     -35.279 -16.490  30.413  1.00125.17           O  
ANISOU 3027  O   LYS A 471    14045  16159  17356   -169   4250   -610       O  
ATOM   3028  CB  LYS A 471     -32.319 -17.425  29.806  1.00119.55           C  
ANISOU 3028  CB  LYS A 471    13866  15419  16138     87   3701    -90       C  
ATOM   3029  CG  LYS A 471     -31.960 -17.185  28.342  1.00131.07           C  
ANISOU 3029  CG  LYS A 471    15033  17052  17715    237   3360    -82       C  
ATOM   3030  CD  LYS A 471     -31.719 -18.495  27.605  1.00140.51           C  
ANISOU 3030  CD  LYS A 471    16248  18209  18930    193   3321    -62       C  
ATOM   3031  CE  LYS A 471     -32.092 -18.415  26.143  1.00149.68           C  
ANISOU 3031  CE  LYS A 471    17029  19530  20313    260   3118   -178       C  
ATOM   3032  NZ  LYS A 471     -33.566 -18.466  25.938  1.00160.18           N  
ANISOU 3032  NZ  LYS A 471    18046  20893  21923    137   3307   -447       N  
ATOM   3033  N   SER A 472     -34.402 -14.898  29.067  1.00118.82           N  
ANISOU 3033  N   SER A 472    12964  15618  16564    193   3664   -491       N  
ATOM   3034  CA  SER A 472     -35.673 -14.483  28.467  1.00120.16           C  
ANISOU 3034  CA  SER A 472    12714  15898  17044    199   3696   -751       C  
ATOM   3035  C   SER A 472     -35.956 -15.209  27.153  1.00124.22           C  
ANISOU 3035  C   SER A 472    12961  16507  17731    218   3541   -852       C  
ATOM   3036  O   SER A 472     -35.088 -15.263  26.279  1.00121.73           O  
ANISOU 3036  O   SER A 472    12675  16256  17322    355   3249   -704       O  
ATOM   3037  CB  SER A 472     -35.704 -12.972  28.258  1.00122.98           C  
ANISOU 3037  CB  SER A 472    12921  16367  17439    396   3506   -758       C  
ATOM   3038  OG  SER A 472     -34.626 -12.537  27.448  1.00129.42           O  
ANISOU 3038  OG  SER A 472    13791  17256  18125    583   3163   -570       O  
ATOM   3039  N   ILE A 473     -37.174 -15.768  27.019  1.00123.46           N  
ANISOU 3039  N   ILE A 473    12599  16421  17890     73   3748  -1124       N  
ATOM   3040  CA  ILE A 473     -37.611 -16.480  25.815  1.00123.85           C  
ANISOU 3040  CA  ILE A 473    12358  16568  18130     73   3623  -1278       C  
ATOM   3041  C   ILE A 473     -38.603 -15.603  25.043  1.00128.93           C  
ANISOU 3041  C   ILE A 473    12555  17399  19035    226   3463  -1527       C  
ATOM   3042  O   ILE A 473     -39.657 -15.243  25.575  1.00130.78           O  
ANISOU 3042  O   ILE A 473    12584  17645  19460    154   3676  -1763       O  
ATOM   3043  CB  ILE A 473     -38.148 -17.911  26.125  1.00129.14           C  
ANISOU 3043  CB  ILE A 473    13067  17109  18891   -208   3954  -1418       C  
ATOM   3044  CG1 ILE A 473     -37.057 -18.781  26.797  1.00128.57           C  
ANISOU 3044  CG1 ILE A 473    13487  16841  18521   -298   4056  -1142       C  
ATOM   3045  CG2 ILE A 473     -38.686 -18.594  24.852  1.00130.64           C  
ANISOU 3045  CG2 ILE A 473    12914  17417  19305   -214   3820  -1623       C  
ATOM   3046  CD1 ILE A 473     -37.577 -19.918  27.686  1.00138.82           C  
ANISOU 3046  CD1 ILE A 473    14988  17926  19831   -591   4504  -1234       C  
ATOM   3047  N   ASP A 474     -38.244 -15.250  23.796  1.00124.14           N  
ANISOU 3047  N   ASP A 474    11815  16931  18423    451   3086  -1474       N  
ATOM   3048  CA  ASP A 474     -39.041 -14.399  22.912  1.00124.98           C  
ANISOU 3048  CA  ASP A 474    11549  17214  18724    664   2856  -1675       C  
ATOM   3049  C   ASP A 474     -40.270 -15.129  22.370  1.00131.43           C  
ANISOU 3049  C   ASP A 474    11968  18127  19844    571   2926  -2036       C  
ATOM   3050  O   ASP A 474     -40.155 -16.263  21.898  1.00131.07           O  
ANISOU 3050  O   ASP A 474    11916  18066  19817    445   2943  -2064       O  
ATOM   3051  CB  ASP A 474     -38.178 -13.844  21.763  1.00124.59           C  
ANISOU 3051  CB  ASP A 474    11562  17252  18524    929   2451  -1482       C  
ATOM   3052  CG  ASP A 474     -36.917 -13.131  22.218  1.00132.40           C  
ANISOU 3052  CG  ASP A 474    12915  18155  19235   1005   2382  -1158       C  
ATOM   3053  OD1 ASP A 474     -37.034 -12.034  22.808  1.00133.12           O  
ANISOU 3053  OD1 ASP A 474    13044  18230  19306   1087   2417  -1140       O  
ATOM   3054  OD2 ASP A 474     -35.814 -13.665  21.975  1.00136.25           O  
ANISOU 3054  OD2 ASP A 474    13638  18597  19535    983   2293   -943       O  
ATOM   3055  N   ASP A 475     -41.444 -14.473  22.445  1.00130.34           N  
ANISOU 3055  N   ASP A 475    11484  18090  19951    635   2967  -2331       N  
ATOM   3056  CA  ASP A 475     -42.723 -15.015  21.983  1.00163.21           C  
ANISOU 3056  CA  ASP A 475    15198  22372  24442    560   3029  -2741       C  
ATOM   3057  C   ASP A 475     -42.801 -15.029  20.459  1.00188.04           C  
ANISOU 3057  C   ASP A 475    18110  25698  27640    796   2615  -2825       C  
ATOM   3058  O   ASP A 475     -42.634 -16.080  19.845  1.00147.82           O  
ANISOU 3058  O   ASP A 475    12997  20612  22555    688   2583  -2853       O  
ATOM   3059  CB  ASP A 475     -43.893 -14.213  22.571  1.00167.83           C  
ANISOU 3059  CB  ASP A 475    15480  23019  25270    587   3181  -3039       C  
ATOM   3060  N   LEU A 533     -50.351  -5.798  24.302  1.00149.00           N  
ANISOU 3060  N   LEU A 533    11132  21227  24254   2173   2954  -4753       N  
ATOM   3061  CA  LEU A 533     -50.502  -4.549  25.044  1.00149.35           C  
ANISOU 3061  CA  LEU A 533    11263  21196  24288   2331   3035  -4727       C  
ATOM   3062  C   LEU A 533     -49.266  -4.255  25.906  1.00149.42           C  
ANISOU 3062  C   LEU A 533    11860  20978  23937   2174   3211  -4260       C  
ATOM   3063  O   LEU A 533     -48.731  -3.146  25.848  1.00147.62           O  
ANISOU 3063  O   LEU A 533    11888  20681  23521   2432   3019  -4025       O  
ATOM   3064  CB  LEU A 533     -51.778  -4.586  25.906  1.00153.46           C  
ANISOU 3064  CB  LEU A 533    11365  21767  25177   2166   3411  -5190       C  
ATOM   3065  CG  LEU A 533     -52.031  -3.370  26.796  1.00159.86           C  
ANISOU 3065  CG  LEU A 533    12122  22551  26067   2400   3444  -5288       C  
ATOM   3066  CD1 LEU A 533     -52.226  -2.117  25.964  1.00164.06           C  
ANISOU 3066  CD1 LEU A 533    12109  23300  26924   2787   3142  -5724       C  
ATOM   3067  CD2 LEU A 533     -53.233  -3.594  27.689  1.00163.67           C  
ANISOU 3067  CD2 LEU A 533    12623  22913  26651   2034   4010  -5417       C  
ATOM   3068  N   GLY A 534     -48.838  -5.246  26.688  1.00144.57           N  
ANISOU 3068  N   GLY A 534    11456  20246  23229   1762   3571  -4146       N  
ATOM   3069  CA  GLY A 534     -47.688  -5.144  27.580  1.00141.13           C  
ANISOU 3069  CA  GLY A 534    11559  19608  22457   1586   3751  -3743       C  
ATOM   3070  C   GLY A 534     -46.362  -5.434  26.912  1.00140.83           C  
ANISOU 3070  C   GLY A 534    11890  19523  22097   1632   3480  -3338       C  
ATOM   3071  O   GLY A 534     -46.298  -6.203  25.947  1.00140.07           O  
ANISOU 3071  O   GLY A 534    11672  19519  22029   1649   3282  -3361       O  
ATOM   3072  N   SER A 535     -45.289  -4.821  27.438  1.00134.37           N  
ANISOU 3072  N   SER A 535    11514  18563  20976   1642   3480  -2985       N  
ATOM   3073  CA  SER A 535     -43.926  -4.971  26.935  1.00130.46           C  
ANISOU 3073  CA  SER A 535    11389  18011  20168   1676   3253  -2600       C  
ATOM   3074  C   SER A 535     -43.332  -6.326  27.312  1.00132.52           C  
ANISOU 3074  C   SER A 535    11848  18199  20304   1347   3452  -2471       C  
ATOM   3075  O   SER A 535     -43.370  -6.705  28.484  1.00132.53           O  
ANISOU 3075  O   SER A 535    12001  18088  20267   1082   3815  -2475       O  
ATOM   3076  CB  SER A 535     -43.044  -3.848  27.464  1.00132.12           C  
ANISOU 3076  CB  SER A 535    11968  18099  20132   1775   3221  -2325       C  
ATOM   3077  N   HIS A 536     -42.779  -7.046  26.314  1.00127.30           N  
ANISOU 3077  N   HIS A 536    11211  17590  19566   1375   3217  -2353       N  
ATOM   3078  CA  HIS A 536     -42.150  -8.362  26.483  1.00125.69           C  
ANISOU 3078  CA  HIS A 536    11203  17316  19236   1109   3351  -2218       C  
ATOM   3079  C   HIS A 536     -40.914  -8.288  27.388  1.00126.50           C  
ANISOU 3079  C   HIS A 536    11787  17261  19016    995   3456  -1882       C  
ATOM   3080  O   HIS A 536     -40.735  -9.161  28.240  1.00126.23           O  
ANISOU 3080  O   HIS A 536    11945  17116  18900    732   3742  -1839       O  
ATOM   3081  CB  HIS A 536     -41.805  -8.983  25.116  1.00125.37           C  
ANISOU 3081  CB  HIS A 536    11080  17375  19182   1215   3033  -2167       C  
ATOM   3082  CG  HIS A 536     -40.995 -10.241  25.204  1.00127.15           C  
ANISOU 3082  CG  HIS A 536    11549  17516  19247    987   3124  -1988       C  
ATOM   3083  ND1 HIS A 536     -39.628 -10.233  24.994  1.00125.87           N  
ANISOU 3083  ND1 HIS A 536    11733  17295  18796   1039   2949  -1648       N  
ATOM   3084  CD2 HIS A 536     -41.385 -11.502  25.501  1.00130.16           C  
ANISOU 3084  CD2 HIS A 536    11878  17853  19723    716   3384  -2117       C  
ATOM   3085  CE1 HIS A 536     -39.232 -11.484  25.158  1.00124.76           C  
ANISOU 3085  CE1 HIS A 536    11734  17084  18584    824   3082  -1579       C  
ATOM   3086  NE2 HIS A 536     -40.254 -12.284  25.465  1.00127.61           N  
ANISOU 3086  NE2 HIS A 536    11887  17439  19160    623   3351  -1843       N  
ATOM   3087  N   THR A 537     -40.076  -7.245  27.203  1.00120.57           N  
ANISOU 3087  N   THR A 537    11238  16495  18080   1197   3229  -1658       N  
ATOM   3088  CA  THR A 537     -38.865  -7.009  27.993  1.00117.95           C  
ANISOU 3088  CA  THR A 537    11325  16040  17450   1125   3279  -1370       C  
ATOM   3089  C   THR A 537     -39.208  -6.668  29.448  1.00122.46           C  
ANISOU 3089  C   THR A 537    12019  16507  18001    975   3618  -1431       C  
ATOM   3090  O   THR A 537     -38.499  -7.104  30.356  1.00121.20           O  
ANISOU 3090  O   THR A 537    12185  16238  17628    804   3779  -1273       O  
ATOM   3091  CB  THR A 537     -38.001  -5.931  27.338  1.00123.95           C  
ANISOU 3091  CB  THR A 537    12218  16816  18063   1368   2970  -1175       C  
ATOM   3092  N   MET A 538     -40.305  -5.910  29.661  1.00120.71           N  
ANISOU 3092  N   MET A 538    11545  16322  17998   1050   3720  -1672       N  
ATOM   3093  CA  MET A 538     -40.786  -5.507  30.987  1.00121.90           C  
ANISOU 3093  CA  MET A 538    11771  16381  18162    917   4058  -1774       C  
ATOM   3094  C   MET A 538     -41.431  -6.673  31.732  1.00127.13           C  
ANISOU 3094  C   MET A 538    12409  16985  18911    616   4437  -1933       C  
ATOM   3095  O   MET A 538     -41.206  -6.814  32.934  1.00126.98           O  
ANISOU 3095  O   MET A 538    12681  16834  18731    431   4722  -1866       O  
ATOM   3096  CB  MET A 538     -41.770  -4.329  30.889  1.00126.20           C  
ANISOU 3096  CB  MET A 538    12029  16988  18933   1115   4036  -2001       C  
ATOM   3097  CG  MET A 538     -41.117  -3.013  30.527  1.00128.27           C  
ANISOU 3097  CG  MET A 538    12429  17240  19066   1378   3765  -1830       C  
ATOM   3098  SD  MET A 538     -40.304  -2.228  31.930  1.00131.48           S  
ANISOU 3098  SD  MET A 538    13256  17493  19207   1276   3959  -1646       S  
ATOM   3099  CE  MET A 538     -38.620  -2.314  31.404  1.00124.60           C  
ANISOU 3099  CE  MET A 538    12725  16596  18022   1317   3671  -1287       C  
ATOM   3100  N   ASP A 539     -42.232  -7.503  31.022  1.00124.88           N  
ANISOU 3100  N   ASP A 539    11793  16786  18869    563   4450  -2153       N  
ATOM   3101  CA  ASP A 539     -42.919  -8.671  31.586  1.00126.82           C  
ANISOU 3101  CA  ASP A 539    11986  16966  19232    258   4831  -2340       C  
ATOM   3102  C   ASP A 539     -41.951  -9.728  32.116  1.00128.69           C  
ANISOU 3102  C   ASP A 539    12663  17053  19179     52   4958  -2082       C  
ATOM   3103  O   ASP A 539     -42.266 -10.396  33.102  1.00130.03           O  
ANISOU 3103  O   ASP A 539    13003  17085  19316   -209   5353  -2147       O  
ATOM   3104  CB  ASP A 539     -43.908  -9.284  30.581  1.00130.59           C  
ANISOU 3104  CB  ASP A 539    11993  17585  20039    262   4771  -2645       C  
ATOM   3105  CG  ASP A 539     -45.244  -8.564  30.488  1.00143.89           C  
ANISOU 3105  CG  ASP A 539    13212  19389  22069    365   4826  -3026       C  
ATOM   3106  OD1 ASP A 539     -45.846  -8.283  31.550  1.00146.44           O  
ANISOU 3106  OD1 ASP A 539    13536  19636  22467    224   5181  -3180       O  
ATOM   3107  OD2 ASP A 539     -45.718  -8.340  29.354  1.00150.62           O  
ANISOU 3107  OD2 ASP A 539    13696  20411  23121    586   4522  -3191       O  
ATOM   3108  N   PHE A 540     -40.771  -9.862  31.475  1.00121.89           N  
ANISOU 3108  N   PHE A 540    12001  16209  18101    178   4630  -1797       N  
ATOM   3109  CA  PHE A 540     -39.709 -10.781  31.889  1.00120.05           C  
ANISOU 3109  CA  PHE A 540    12190  15849  17576     48   4674  -1535       C  
ATOM   3110  C   PHE A 540     -39.096 -10.295  33.208  1.00123.48           C  
ANISOU 3110  C   PHE A 540    13031  16150  17735     -2   4833  -1369       C  
ATOM   3111  O   PHE A 540     -38.763 -11.115  34.065  1.00123.60           O  
ANISOU 3111  O   PHE A 540    13392  16015  17557   -183   5068  -1273       O  
ATOM   3112  CB  PHE A 540     -38.640 -10.913  30.783  1.00118.84           C  
ANISOU 3112  CB  PHE A 540    12085  15774  17297    223   4264  -1312       C  
ATOM   3113  CG  PHE A 540     -37.294 -11.457  31.211  1.00118.38           C  
ANISOU 3113  CG  PHE A 540    12467  15608  16903    183   4211  -1013       C  
ATOM   3114  CD1 PHE A 540     -37.150 -12.787  31.590  1.00122.13           C  
ANISOU 3114  CD1 PHE A 540    13159  15959  17284    -10   4411   -970       C  
ATOM   3115  CD2 PHE A 540     -36.167 -10.644  31.213  1.00118.18           C  
ANISOU 3115  CD2 PHE A 540    12637  15604  16663    347   3958   -790       C  
ATOM   3116  CE1 PHE A 540     -35.903 -13.290  31.977  1.00121.50           C  
ANISOU 3116  CE1 PHE A 540    13486  15787  16893     -7   4331   -706       C  
ATOM   3117  CE2 PHE A 540     -34.921 -11.148  31.598  1.00119.48           C  
ANISOU 3117  CE2 PHE A 540    13170  15692  16536    329   3887   -550       C  
ATOM   3118  CZ  PHE A 540     -34.798 -12.467  31.979  1.00118.33           C  
ANISOU 3118  CZ  PHE A 540    13235  15432  16293    168   4059   -508       C  
ATOM   3119  N   PHE A 541     -38.975  -8.961  33.369  1.00119.31           N  
ANISOU 3119  N   PHE A 541    12477  15671  17186    166   4708  -1344       N  
ATOM   3120  CA  PHE A 541     -38.447  -8.321  34.573  1.00118.97           C  
ANISOU 3120  CA  PHE A 541    12778  15524  16902    140   4832  -1221       C  
ATOM   3121  C   PHE A 541     -39.420  -8.464  35.746  1.00126.09           C  
ANISOU 3121  C   PHE A 541    13726  16316  17868    -71   5288  -1415       C  
ATOM   3122  O   PHE A 541     -38.976  -8.680  36.874  1.00126.09           O  
ANISOU 3122  O   PHE A 541    14123  16175  17608   -194   5489  -1300       O  
ATOM   3123  CB  PHE A 541     -38.125  -6.838  34.313  1.00119.42           C  
ANISOU 3123  CB  PHE A 541    12765  15657  16951    370   4583  -1172       C  
ATOM   3124  CG  PHE A 541     -36.939  -6.529  33.423  1.00117.97           C  
ANISOU 3124  CG  PHE A 541    12656  15539  16626    553   4187   -947       C  
ATOM   3125  CD1 PHE A 541     -35.828  -7.366  33.395  1.00119.31           C  
ANISOU 3125  CD1 PHE A 541    13093  15674  16565    504   4079   -735       C  
ATOM   3126  CD2 PHE A 541     -36.904  -5.365  32.665  1.00119.21           C  
ANISOU 3126  CD2 PHE A 541    12643  15779  16871    775   3940   -952       C  
ATOM   3127  CE1 PHE A 541     -34.726  -7.066  32.591  1.00117.73           C  
ANISOU 3127  CE1 PHE A 541    12947  15537  16250    656   3741   -555       C  
ATOM   3128  CE2 PHE A 541     -35.801  -5.066  31.861  1.00119.56           C  
ANISOU 3128  CE2 PHE A 541    12781  15865  16782    918   3619   -755       C  
ATOM   3129  CZ  PHE A 541     -34.719  -5.919  31.830  1.00116.01           C  
ANISOU 3129  CZ  PHE A 541    12558  15394  16125    847   3528   -567       C  
ATOM   3130  N   GLU A 542     -40.741  -8.356  35.475  1.00125.23           N  
ANISOU 3130  N   GLU A 542    13212  16271  18101   -108   5449  -1723       N  
ATOM   3131  CA  GLU A 542     -41.815  -8.500  36.469  1.00128.51           C  
ANISOU 3131  CA  GLU A 542    13593  16593  18642   -326   5917  -1967       C  
ATOM   3132  C   GLU A 542     -41.879  -9.950  36.968  1.00134.14           C  
ANISOU 3132  C   GLU A 542    14548  17155  19264   -609   6243  -1962       C  
ATOM   3133  O   GLU A 542     -42.129 -10.181  38.152  1.00135.72           O  
ANISOU 3133  O   GLU A 542    15028  17195  19346   -811   6638  -1997       O  
ATOM   3134  CB  GLU A 542     -43.177  -8.082  35.879  1.00132.12           C  
ANISOU 3134  CB  GLU A 542    13491  17185  19524   -273   5962  -2332       C  
ATOM   3135  CG  GLU A 542     -43.309  -6.603  35.551  1.00141.74           C  
ANISOU 3135  CG  GLU A 542    14497  18515  20841      9   5711  -2375       C  
ATOM   3136  CD  GLU A 542     -43.554  -5.685  36.732  1.00162.27           C  
ANISOU 3136  CD  GLU A 542    17242  21030  23383    -22   5963  -2429       C  
ATOM   3137  OE1 GLU A 542     -44.681  -5.704  37.278  1.00159.46           O  
ANISOU 3137  OE1 GLU A 542    16679  20656  23253   -160   6315  -2730       O  
ATOM   3138  OE2 GLU A 542     -42.631  -4.917  37.087  1.00153.49           O  
ANISOU 3138  OE2 GLU A 542    16431  19876  22014     92   5809  -2194       O  
ATOM   3139  N   MET A 543     -41.639 -10.915  36.055  1.00130.07           N  
ANISOU 3139  N   MET A 543    13954  16676  18791   -621   6083  -1913       N  
ATOM   3140  CA  MET A 543     -41.617 -12.356  36.316  1.00131.22           C  
ANISOU 3140  CA  MET A 543    14332  16670  18854   -864   6345  -1890       C  
ATOM   3141  C   MET A 543     -40.383 -12.718  37.155  1.00133.96           C  
ANISOU 3141  C   MET A 543    15289  16852  18756   -878   6342  -1553       C  
ATOM   3142  O   MET A 543     -40.468 -13.594  38.018  1.00135.44           O  
ANISOU 3142  O   MET A 543    15830  16841  18791  -1095   6701  -1535       O  
ATOM   3143  CB  MET A 543     -41.607 -13.122  34.982  1.00132.59           C  
ANISOU 3143  CB  MET A 543    14231  16953  19195   -820   6101  -1923       C  
ATOM   3144  CG  MET A 543     -42.020 -14.571  35.092  1.00138.42           C  
ANISOU 3144  CG  MET A 543    15056  17551  19987  -1100   6432  -2026       C  
ATOM   3145  SD  MET A 543     -42.123 -15.328  33.454  1.00141.70           S  
ANISOU 3145  SD  MET A 543    15081  18121  20636  -1036   6128  -2115       S  
ATOM   3146  CE  MET A 543     -42.377 -17.021  33.898  1.00140.92           C  
ANISOU 3146  CE  MET A 543    15252  17785  20508  -1392   6579  -2174       C  
ATOM   3147  N   CYS A 544     -39.243 -12.038  36.896  1.00127.68           N  
ANISOU 3147  N   CYS A 544    14622  16137  17754   -641   5939  -1303       N  
ATOM   3148  CA  CYS A 544     -37.979 -12.233  37.609  1.00126.28           C  
ANISOU 3148  CA  CYS A 544    14966  15848  17165   -598   5848  -1006       C  
ATOM   3149  C   CYS A 544     -38.064 -11.696  39.035  1.00131.82           C  
ANISOU 3149  C   CYS A 544    15992  16425  17668   -675   6126  -1004       C  
ATOM   3150  O   CYS A 544     -37.761 -12.432  39.975  1.00132.73           O  
ANISOU 3150  O   CYS A 544    16566  16356  17509   -799   6354   -900       O  
ATOM   3151  CB  CYS A 544     -36.816 -11.606  36.844  1.00123.22           C  
ANISOU 3151  CB  CYS A 544    14544  15604  16672   -340   5354   -802       C  
ATOM   3152  SG  CYS A 544     -36.137 -12.652  35.531  1.00125.05           S  
ANISOU 3152  SG  CYS A 544    14692  15899  16922   -269   5046   -676       S  
ATOM   3153  N   ALA A 545     -38.495 -10.421  39.191  1.00128.52           N  
ANISOU 3153  N   ALA A 545    15355  16098  17379   -592   6111  -1124       N  
ATOM   3154  CA  ALA A 545     -38.643  -9.728  40.475  1.00129.92           C  
ANISOU 3154  CA  ALA A 545    15784  16180  17400   -650   6359  -1152       C  
ATOM   3155  C   ALA A 545     -39.572 -10.465  41.440  1.00137.37           C  
ANISOU 3155  C   ALA A 545    16909  16938  18348   -929   6900  -1311       C  
ATOM   3156  O   ALA A 545     -39.269 -10.532  42.628  1.00138.19           O  
ANISOU 3156  O   ALA A 545    17478  16885  18143  -1009   7112  -1218       O  
ATOM   3157  CB  ALA A 545     -39.133  -8.306  40.254  1.00130.40           C  
ANISOU 3157  CB  ALA A 545    15493  16374  17682   -514   6263  -1300       C  
ATOM   3158  N   SER A 546     -40.674 -11.049  40.920  1.00135.80           N  
ANISOU 3158  N   SER A 546    16359  16752  18487  -1081   7126  -1558       N  
ATOM   3159  CA  SER A 546     -41.658 -11.811  41.696  1.00139.42           C  
ANISOU 3159  CA  SER A 546    16929  17031  19011  -1384   7685  -1758       C  
ATOM   3160  C   SER A 546     -41.074 -13.088  42.319  1.00144.05           C  
ANISOU 3160  C   SER A 546    18091  17386  19255  -1532   7878  -1560       C  
ATOM   3161  O   SER A 546     -41.567 -13.534  43.357  1.00146.79           O  
ANISOU 3161  O   SER A 546    18761  17524  19489  -1762   8357  -1635       O  
ATOM   3162  CB  SER A 546     -42.875 -12.145  40.840  1.00144.72           C  
ANISOU 3162  CB  SER A 546    17037  17800  20148  -1496   7821  -2089       C  
ATOM   3163  OG  SER A 546     -42.513 -12.890  39.689  1.00151.89           O  
ANISOU 3163  OG  SER A 546    17784  18790  21136  -1430   7531  -2015       O  
ATOM   3164  N   LEU A 547     -40.026 -13.666  41.695  1.00137.91           N  
ANISOU 3164  N   LEU A 547    17461  16633  18306  -1393   7516  -1311       N  
ATOM   3165  CA  LEU A 547     -39.355 -14.873  42.180  1.00138.36           C  
ANISOU 3165  CA  LEU A 547    18072  16475  18024  -1472   7624  -1101       C  
ATOM   3166  C   LEU A 547     -38.192 -14.545  43.129  1.00141.26           C  
ANISOU 3166  C   LEU A 547    18987  16766  17921  -1319   7464   -826       C  
ATOM   3167  O   LEU A 547     -37.995 -15.266  44.109  1.00143.00           O  
ANISOU 3167  O   LEU A 547    19764  16751  17820  -1424   7733   -722       O  
ATOM   3168  CB  LEU A 547     -38.886 -15.752  41.002  1.00136.50           C  
ANISOU 3168  CB  LEU A 547    17693  16301  17869  -1403   7338  -1009       C  
ATOM   3169  CG  LEU A 547     -38.479 -17.201  41.323  1.00142.55           C  
ANISOU 3169  CG  LEU A 547    18959  16826  18379  -1516   7512   -855       C  
ATOM   3170  CD1 LEU A 547     -39.690 -18.069  41.650  1.00146.63           C  
ANISOU 3170  CD1 LEU A 547    19507  17143  19064  -1856   8096  -1091       C  
ATOM   3171  CD2 LEU A 547     -37.726 -17.817  40.166  1.00142.44           C  
ANISOU 3171  CD2 LEU A 547    18812  16908  18402  -1375   7121   -722       C  
ATOM   3172  N   ILE A 548     -37.435 -13.461  42.843  1.00134.86           N  
ANISOU 3172  N   ILE A 548    18030  16145  17065  -1073   7033   -723       N  
ATOM   3173  CA  ILE A 548     -36.296 -13.010  43.658  1.00133.77           C  
ANISOU 3173  CA  ILE A 548    18328  15981  16518   -912   6825   -504       C  
ATOM   3174  C   ILE A 548     -36.778 -12.481  45.026  1.00140.17           C  
ANISOU 3174  C   ILE A 548    19435  16660  17163  -1027   7194   -587       C  
ATOM   3175  O   ILE A 548     -36.142 -12.770  46.041  1.00140.92           O  
ANISOU 3175  O   ILE A 548    20089  16606  16848  -1006   7249   -433       O  
ATOM   3176  CB  ILE A 548     -35.373 -12.008  42.887  1.00133.27           C  
ANISOU 3176  CB  ILE A 548    17992  16155  16491   -648   6291   -406       C  
ATOM   3177  CG1 ILE A 548     -34.834 -12.640  41.579  1.00131.28           C  
ANISOU 3177  CG1 ILE A 548    17515  16009  16358   -544   5955   -313       C  
ATOM   3178  CG2 ILE A 548     -34.202 -11.518  43.761  1.00133.48           C  
ANISOU 3178  CG2 ILE A 548    18434  16168  16113   -497   6083   -226       C  
ATOM   3179  CD1 ILE A 548     -34.469 -11.643  40.461  1.00135.73           C  
ANISOU 3179  CD1 ILE A 548    17629  16809  17132   -354   5545   -317       C  
ATOM   3180  N   THR A 549     -37.912 -11.745  45.052  1.00137.84           N  
ANISOU 3180  N   THR A 549    18775  16418  17181  -1139   7445   -839       N  
ATOM   3181  CA  THR A 549     -38.500 -11.198  46.285  1.00140.38           C  
ANISOU 3181  CA  THR A 549    19319  16621  17398  -1267   7832   -958       C  
ATOM   3182  C   THR A 549     -39.022 -12.296  47.218  1.00147.75           C  
ANISOU 3182  C   THR A 549    20715  17273  18149  -1524   8359   -987       C  
ATOM   3183  O   THR A 549     -38.887 -12.169  48.437  1.00149.39           O  
ANISOU 3183  O   THR A 549    21412  17325  18025  -1572   8585   -936       O  
ATOM   3184  CB  THR A 549     -39.572 -10.138  45.987  1.00149.18           C  
ANISOU 3184  CB  THR A 549    19888  17872  18922  -1297   7946  -1237       C  
ATOM   3185  OG1 THR A 549     -40.520 -10.661  45.053  1.00149.52           O  
ANISOU 3185  OG1 THR A 549    19463  17971  19376  -1409   8063  -1442       O  
ATOM   3186  CG2 THR A 549     -38.980  -8.831  45.471  1.00144.79           C  
ANISOU 3186  CG2 THR A 549    19060  17527  18427  -1038   7492  -1183       C  
ATOM   3187  N   THR A 550     -39.604 -13.372  46.647  1.00145.15           N  
ANISOU 3187  N   THR A 550    20256  16870  18024  -1692   8564  -1075       N  
ATOM   3188  CA  THR A 550     -40.130 -14.513  47.406  1.00148.63           C  
ANISOU 3188  CA  THR A 550    21136  17017  18320  -1962   9099  -1113       C  
ATOM   3189  C   THR A 550     -39.003 -15.377  47.977  1.00152.45           C  
ANISOU 3189  C   THR A 550    22325  17310  18287  -1866   8990   -796       C  
ATOM   3190  O   THR A 550     -39.088 -15.795  49.133  1.00155.22           O  
ANISOU 3190  O   THR A 550    23265  17405  18306  -1989   9363   -749       O  
ATOM   3191  CB  THR A 550     -41.135 -15.334  46.580  1.00157.68           C  
ANISOU 3191  CB  THR A 550    21884  18149  19878  -2185   9358  -1343       C  
ATOM   3192  OG1 THR A 550     -40.584 -15.623  45.295  1.00153.77           O  
ANISOU 3192  OG1 THR A 550    21068  17827  19530  -2015   8893  -1246       O  
ATOM   3193  CG2 THR A 550     -42.484 -14.640  46.438  1.00157.95           C  
ANISOU 3193  CG2 THR A 550    21352  18292  20371  -2343   9649  -1720       C  
ATOM   3194  N   LEU A 551     -37.948 -15.633  47.173  1.00145.62           N  
ANISOU 3194  N   LEU A 551    21413  16566  17348  -1634   8479   -589       N  
ATOM   3195  CA  LEU A 551     -36.789 -16.429  47.579  1.00145.33           C  
ANISOU 3195  CA  LEU A 551    21983  16387  16850  -1484   8288   -298       C  
ATOM   3196  C   LEU A 551     -35.894 -15.611  48.522  1.00148.81           C  
ANISOU 3196  C   LEU A 551    22790  16857  16893  -1279   8058   -151       C  
ATOM   3197  O   LEU A 551     -35.238 -14.663  48.084  1.00145.29           O  
ANISOU 3197  O   LEU A 551    22042  16655  16506  -1069   7612   -112       O  
ATOM   3198  CB  LEU A 551     -36.007 -16.913  46.340  1.00142.15           C  
ANISOU 3198  CB  LEU A 551    21331  16130  16552  -1306   7820   -168       C  
ATOM   3199  CG  LEU A 551     -35.010 -18.050  46.563  1.00147.36           C  
ANISOU 3199  CG  LEU A 551    22557  16614  16818  -1184   7685     88       C  
ATOM   3200  CD1 LEU A 551     -35.646 -19.401  46.283  1.00149.73           C  
ANISOU 3200  CD1 LEU A 551    22978  16691  17221  -1407   8053     40       C  
ATOM   3201  CD2 LEU A 551     -33.787 -17.874  45.688  1.00146.03           C  
ANISOU 3201  CD2 LEU A 551    22185  16668  16631   -890   7066    249       C  
ATOM   3202  N   ALA A 552     -35.895 -15.983  49.824  1.00148.83           N  
ANISOU 3202  N   ALA A 552    23460  16600  16487  -1351   8384    -83       N  
ATOM   3203  CA  ALA A 552     -35.143 -15.360  50.927  1.00181.33           C  
ANISOU 3203  CA  ALA A 552    28036  20697  20164  -1183   8244     36       C  
ATOM   3204  C   ALA A 552     -35.369 -13.852  51.050  1.00205.27           C  
ANISOU 3204  C   ALA A 552    30683  23939  23370  -1152   8152   -110       C  
ATOM   3205  O   ALA A 552     -36.506 -13.409  51.202  1.00171.02           O  
ANISOU 3205  O   ALA A 552    26099  19581  19299  -1365   8544   -331       O  
ATOM   3206  CB  ALA A 552     -33.655 -15.672  50.816  1.00180.32           C  
ANISOU 3206  CB  ALA A 552    28186  20631  19698   -868   7703    288       C  
TER    3207      ALA A 552                                                      
ATOM   3208  N   PHE B  59     -19.442  -5.350  -9.033  1.00186.04           N  
ANISOU 3208  N   PHE B  59    29574  22287  18824  -4151   1907  -1026       N  
ATOM   3209  CA  PHE B  59     -18.963  -6.710  -9.241  1.00183.39           C  
ANISOU 3209  CA  PHE B  59    28459  22314  18908  -4070   2039  -1152       C  
ATOM   3210  C   PHE B  59     -19.669  -7.678  -8.307  1.00184.24           C  
ANISOU 3210  C   PHE B  59    28072  22494  19438  -3532   1830   -973       C  
ATOM   3211  O   PHE B  59     -20.213  -8.693  -8.739  1.00182.06           O  
ANISOU 3211  O   PHE B  59    27283  22391  19499  -3338   1793   -991       O  
ATOM   3212  CB  PHE B  59     -17.453  -6.785  -9.015  1.00185.56           C  
ANISOU 3212  CB  PHE B  59    28520  22838  19146  -4443   2384  -1398       C  
ATOM   3213  N   VAL B  60     -19.663  -7.352  -7.021  1.00180.39           N  
ANISOU 3213  N   VAL B  60    27749  21869  18922  -3312   1705   -814       N  
ATOM   3214  CA  VAL B  60     -20.271  -8.208  -6.014  1.00177.73           C  
ANISOU 3214  CA  VAL B  60    27003  21587  18940  -2836   1524   -653       C  
ATOM   3215  C   VAL B  60     -21.765  -8.352  -6.260  1.00180.87           C  
ANISOU 3215  C   VAL B  60    27365  21867  19491  -2470   1228   -519       C  
ATOM   3216  O   VAL B  60     -22.327  -9.436  -6.115  1.00178.29           O  
ANISOU 3216  O   VAL B  60    26511  21694  19535  -2182   1165   -476       O  
ATOM   3217  CB  VAL B  60     -20.044  -7.656  -4.596  1.00181.81           C  
ANISOU 3217  CB  VAL B  60    27747  21986  19348  -2737   1481   -549       C  
ATOM   3218  N   SER B  61     -22.407  -7.258  -6.647  1.00179.46           N  
ANISOU 3218  N   SER B  61    27761  21412  19015  -2487   1044   -465       N  
ATOM   3219  CA  SER B  61     -23.842  -7.280  -6.861  1.00179.29           C  
ANISOU 3219  CA  SER B  61    27765  21267  19090  -2148    740   -373       C  
ATOM   3220  C   SER B  61     -24.158  -8.267  -7.964  1.00182.19           C  
ANISOU 3220  C   SER B  61    27780  21796  19648  -2199    790   -465       C  
ATOM   3221  O   SER B  61     -25.133  -9.011  -7.884  1.00180.81           O  
ANISOU 3221  O   SER B  61    27332  21644  19724  -1874    597   -413       O  
ATOM   3222  CB  SER B  61     -24.351  -5.894  -7.249  1.00185.78           C  
ANISOU 3222  CB  SER B  61    29346  21739  19503  -2161    519   -312       C  
ATOM   3223  OG  SER B  61     -25.601  -5.981  -7.912  1.00194.74           O  
ANISOU 3223  OG  SER B  61    30483  22764  20747  -1766    183   -240       O  
ATOM   3224  N   TRP B  62     -23.324  -8.273  -8.996  1.00179.14           N  
ANISOU 3224  N   TRP B  62    27385  21533  19148  -2613   1056   -625       N  
ATOM   3225  CA  TRP B  62     -23.551  -9.152 -10.129  1.00178.40           C  
ANISOU 3225  CA  TRP B  62    26968  21603  19212  -2719   1142   -749       C  
ATOM   3226  C   TRP B  62     -23.494 -10.607  -9.696  1.00179.21           C  
ANISOU 3226  C   TRP B  62    26343  21950  19800  -2448   1160   -744       C  
ATOM   3227  O   TRP B  62     -24.320 -11.418 -10.112  1.00178.16           O  
ANISOU 3227  O   TRP B  62    25953  21875  19867  -2326   1083   -764       O  
ATOM   3228  CB  TRP B  62     -22.508  -8.894 -11.216  1.00178.51           C  
ANISOU 3228  CB  TRP B  62    27097  21726  19004  -3233   1450   -961       C  
ATOM   3229  N   GLN B  63     -22.525 -10.939  -8.852  1.00174.08           N  
ANISOU 3229  N   GLN B  63    25390  21429  19323  -2360   1258   -718       N  
ATOM   3230  CA  GLN B  63     -22.405 -12.308  -8.379  1.00171.42           C  
ANISOU 3230  CA  GLN B  63    24428  21293  19409  -2107   1277   -696       C  
ATOM   3231  C   GLN B  63     -23.628 -12.701  -7.565  1.00173.99           C  
ANISOU 3231  C   GLN B  63    24634  21530  19943  -1690   1021   -533       C  
ATOM   3232  O   GLN B  63     -24.171 -13.791  -7.732  1.00172.22           O  
ANISOU 3232  O   GLN B  63    23981  21420  20035  -1513    997   -529       O  
ATOM   3233  CB  GLN B  63     -21.136 -12.479  -7.542  1.00171.84           C  
ANISOU 3233  CB  GLN B  63    24278  21485  19528  -2139   1435   -713       C  
ATOM   3234  N   GLN B  64     -24.073 -11.801  -6.696  1.00171.19           N  
ANISOU 3234  N   GLN B  64    24668  20972  19405  -1542    832   -420       N  
ATOM   3235  CA  GLN B  64     -25.242 -12.076  -5.874  1.00170.48           C  
ANISOU 3235  CA  GLN B  64    24505  20798  19473  -1151    573   -311       C  
ATOM   3236  C   GLN B  64     -26.462 -12.237  -6.768  1.00175.01           C  
ANISOU 3236  C   GLN B  64    25133  21304  20058  -1073    405   -349       C  
ATOM   3237  O   GLN B  64     -27.281 -13.130  -6.567  1.00173.87           O  
ANISOU 3237  O   GLN B  64    24697  21198  20169   -784    260   -324       O  
ATOM   3238  CB  GLN B  64     -25.424 -10.975  -4.805  1.00172.94           C  
ANISOU 3238  CB  GLN B  64    25248  20907  19554  -1028    412   -222       C  
ATOM   3239  CG  GLN B  64     -26.784 -10.286  -4.718  1.00185.38           C  
ANISOU 3239  CG  GLN B  64    26670  22443  21323   -606    168   -147       C  
ATOM   3240  CD  GLN B  64     -27.870 -11.204  -4.201  1.00200.30           C  
ANISOU 3240  CD  GLN B  64    28075  24511  23520   -447    265    -99       C  
ATOM   3241  OE1 GLN B  64     -28.895 -10.750  -3.695  1.00194.35           O  
ANISOU 3241  OE1 GLN B  64    27130  23894  22820   -615    493   -102       O  
ATOM   3242  NE2 GLN B  64     -27.650 -12.505  -4.325  1.00191.44           N  
ANISOU 3242  NE2 GLN B  64    26752  23393  22593   -117     89    -72       N  
ATOM   3243  N   ASP B  65     -26.538 -11.408  -7.800  1.00173.06           N  
ANISOU 3243  N   ASP B  65    25256  20970  19531  -1351    438   -425       N  
ATOM   3244  CA  ASP B  65     -27.673 -11.435  -8.707  1.00173.91           C  
ANISOU 3244  CA  ASP B  65    25475  21009  19595  -1325    290   -474       C  
ATOM   3245  C   ASP B  65     -27.781 -12.784  -9.402  1.00175.93           C  
ANISOU 3245  C   ASP B  65    25180  21468  20196  -1298    381   -548       C  
ATOM   3246  O   ASP B  65     -28.877 -13.313  -9.575  1.00175.95           O  
ANISOU 3246  O   ASP B  65    25140  21441  20270  -1160    221   -575       O  
ATOM   3247  CB  ASP B  65     -27.545 -10.323  -9.749  1.00178.13           C  
ANISOU 3247  CB  ASP B  65    26580  21397  19704  -1680    338   -539       C  
ATOM   3248  N   LEU B  66     -26.644 -13.346  -9.793  1.00170.64           N  
ANISOU 3248  N   LEU B  66    24107  20997  19733  -1420    624   -594       N  
ATOM   3249  CA  LEU B  66     -26.654 -14.589 -10.549  1.00169.03           C  
ANISOU 3249  CA  LEU B  66    23395  20969  19858  -1395    719   -665       C  
ATOM   3250  C   LEU B  66     -27.276 -15.721  -9.745  1.00171.30           C  
ANISOU 3250  C   LEU B  66    23311  21293  20481  -1037    589   -583       C  
ATOM   3251  O   LEU B  66     -28.063 -16.504 -10.269  1.00170.38           O  
ANISOU 3251  O   LEU B  66    22900  21247  20590   -971    578   -633       O  
ATOM   3252  CB  LEU B  66     -25.234 -14.966 -10.972  1.00168.11           C  
ANISOU 3252  CB  LEU B  66    23000  21034  19842  -1596    982   -750       C  
ATOM   3253  N   GLU B  67     -26.935 -15.796  -8.465  1.00167.23           N  
ANISOU 3253  N   GLU B  67    22815  20734  19992   -828    503   -473       N  
ATOM   3254  CA  GLU B  67     -27.502 -16.814  -7.592  1.00165.98           C  
ANISOU 3254  CA  GLU B  67    22326  20617  20121   -517    403   -414       C  
ATOM   3255  C   GLU B  67     -29.005 -16.612  -7.466  1.00170.75           C  
ANISOU 3255  C   GLU B  67    23065  21113  20698   -286    133   -430       C  
ATOM   3256  O   GLU B  67     -29.779 -17.569  -7.449  1.00169.81           O  
ANISOU 3256  O   GLU B  67    22660  21045  20815    -44     51   -425       O  
ATOM   3257  CB  GLU B  67     -26.842 -16.771  -6.214  1.00166.45           C  
ANISOU 3257  CB  GLU B  67    22326  20701  20218   -416    449   -317       C  
ATOM   3258  N   ASP B  68     -29.407 -15.351  -7.378  1.00168.90           N  
ANISOU 3258  N   ASP B  68    23269  20735  20171   -364     -5   -469       N  
ATOM   3259  CA  ASP B  68     -30.808 -14.991  -7.223  1.00170.27           C  
ANISOU 3259  CA  ASP B  68    23633  20791  20270   -134   -300   -508       C  
ATOM   3260  C   ASP B  68     -31.628 -15.444  -8.423  1.00173.46           C  
ANISOU 3260  C   ASP B  68    23675  21297  20935    -27   -351   -603       C  
ATOM   3261  O   ASP B  68     -32.760 -15.899  -8.277  1.00173.99           O  
ANISOU 3261  O   ASP B  68    23693  21342  21076    243   -579   -658       O  
ATOM   3262  CB  ASP B  68     -30.953 -13.481  -7.029  1.00174.38           C  
ANISOU 3262  CB  ASP B  68    24780  21108  20367   -272   -430   -515       C  
ATOM   3263  N   SER B  69     -31.048 -15.326  -9.611  1.00168.57           N  
ANISOU 3263  N   SER B  69    22806  20793  20451   -237   -144   -645       N  
ATOM   3264  CA  SER B  69     -31.773 -15.615 -10.839  1.00167.94           C  
ANISOU 3264  CA  SER B  69    22389  20808  20615   -193   -148   -739       C  
ATOM   3265  C   SER B  69     -32.241 -17.063 -10.850  1.00170.17           C  
ANISOU 3265  C   SER B  69    22228  21190  21238     47   -164   -747       C  
ATOM   3266  O   SER B  69     -33.343 -17.364 -11.306  1.00168.49           O  
ANISOU 3266  O   SER B  69    21836  21030  21151     88    -49   -667       O  
ATOM   3267  CB  SER B  69     -30.902 -15.325 -12.064  1.00170.63           C  
ANISOU 3267  CB  SER B  69    22557  21243  21030   -470     94   -783       C  
ATOM   3268  OG  SER B  69     -30.128 -16.455 -12.424  1.00177.76           O  
ANISOU 3268  OG  SER B  69    23228  22238  22076   -539    305   -722       O  
ATOM   3269  N   VAL B  70     -31.404 -17.959 -10.345  1.00 30.00           N  
ATOM   3270  CA  VAL B  70     -31.753 -19.370 -10.309  1.00 30.00           C  
ATOM   3271  C   VAL B  70     -32.978 -19.606  -9.431  1.00 30.00           C  
ATOM   3272  O   VAL B  70     -33.129 -18.991  -8.375  1.00 30.00           O  
ATOM   3273  CB  VAL B  70     -30.587 -20.224  -9.781  1.00 20.00           C  
ATOM   3274  N   LYS B  71     -33.846 -20.505  -9.884  1.00 30.00           N  
ATOM   3275  CA  LYS B  71     -35.056 -20.875  -9.157  1.00 30.00           C  
ATOM   3276  C   LYS B  71     -34.952 -22.338  -8.746  1.00 30.00           C  
ATOM   3277  O   LYS B  71     -34.598 -23.188  -9.572  1.00 30.00           O  
ATOM   3278  CB  LYS B  71     -36.292 -20.655 -10.028  1.00 20.00           C  
ATOM   3279  N   PRO B  72     -35.263 -22.625  -7.405  1.00162.09           N  
ANISOU 3279  N   PRO B  72    19938  20481  21167    332     61   -852       N  
ATOM   3280  CA  PRO B  72     -34.956 -24.020  -7.032  1.00160.26           C  
ANISOU 3280  CA  PRO B  72    19399  20314  21177    212    294   -818       C  
ATOM   3281  C   PRO B  72     -35.789 -25.058  -7.780  1.00163.25           C  
ANISOU 3281  C   PRO B  72    19480  20749  21797    229    314   -943       C  
ATOM   3282  O   PRO B  72     -37.007 -24.926  -7.886  1.00163.37           O  
ANISOU 3282  O   PRO B  72    19284  20818  21971    353    295  -1007       O  
ATOM   3283  CB  PRO B  72     -35.274 -24.075  -5.532  1.00161.21           C  
ANISOU 3283  CB  PRO B  72    19421  20460  21371    277    391   -708       C  
ATOM   3284  CG  PRO B  72     -36.373 -23.102  -5.353  1.00166.75           C  
ANISOU 3284  CG  PRO B  72    20247  21146  21965    474    199   -741       C  
ATOM   3285  CD  PRO B  72     -35.864 -21.949  -6.150  1.00163.85           C  
ANISOU 3285  CD  PRO B  72    20119  20719  21419    535    -29   -844       C  
ATOM   3286  N   THR B  73     -35.113 -26.083  -8.291  1.00158.63           N  
ANISOU 3286  N   THR B  73    18880  20161  21233     91    358  -1002       N  
ATOM   3287  CA  THR B  73     -35.761 -27.224  -8.929  1.00158.38           C  
ANISOU 3287  CA  THR B  73    18585  20173  21417     74    390  -1130       C  
ATOM   3288  C   THR B  73     -34.779 -28.390  -9.021  1.00159.97           C  
ANISOU 3288  C   THR B  73    18716  20366  21699   -114    550  -1126       C  
ATOM   3289  O   THR B  73     -33.577 -28.201  -8.852  1.00159.25           O  
ANISOU 3289  O   THR B  73    18825  20251  21433   -234    562  -1102       O  
ATOM   3290  CB  THR B  73     -36.303 -26.872 -10.324  1.00167.94           C  
ANISOU 3290  CB  THR B  73    19874  21395  22543    171    169  -1286       C  
ATOM   3291  OG1 THR B  73     -35.227 -26.423 -11.156  1.00168.32           O  
ANISOU 3291  OG1 THR B  73    20143  21412  22399    342    -35  -1281       O  
ATOM   3292  CG2 THR B  73     -37.345 -25.770 -10.224  1.00167.29           C  
ANISOU 3292  CG2 THR B  73    19463  21389  22712    225    179  -1445       C  
ATOM   3293  N   GLN B  74     -35.284 -29.589  -9.295  1.00155.19           N  
ANISOU 3293  N   GLN B  74    17833  19779  21352   -148    674  -1172       N  
ATOM   3294  CA  GLN B  74     -34.415 -30.744  -9.507  1.00153.93           C  
ANISOU 3294  CA  GLN B  74    17579  19602  21304   -294    809  -1194       C  
ATOM   3295  C   GLN B  74     -34.483 -31.165 -10.970  1.00157.04           C  
ANISOU 3295  C   GLN B  74    17977  20015  21676   -361    734  -1348       C  
ATOM   3296  O   GLN B  74     -35.565 -31.413 -11.497  1.00157.57           O  
ANISOU 3296  O   GLN B  74    17941  20114  21816   -290    647  -1458       O  
ATOM   3297  CB  GLN B  74     -34.841 -31.906  -8.608  1.00155.06           C  
ANISOU 3297  CB  GLN B  74    17480  19721  21714   -298    965  -1166       C  
ATOM   3298  CG  GLN B  74     -33.704 -32.818  -8.175  1.00167.79           C  
ANISOU 3298  CG  GLN B  74    19059  21287  23407   -393   1097  -1123       C  
ATOM   3299  CD  GLN B  74     -33.731 -33.114  -6.688  1.00185.30           C  
ANISOU 3299  CD  GLN B  74    21125  23439  25843   -381   1230  -1065       C  
ATOM   3300  OE1 GLN B  74     -33.183 -34.118  -6.231  1.00179.91           O  
ANISOU 3300  OE1 GLN B  74    20455  22738  25166   -319   1273   -949       O  
ATOM   3301  NE2 GLN B  74     -34.369 -32.237  -5.923  1.00177.78           N  
ANISOU 3301  NE2 GLN B  74    20051  22437  25061   -449   1301  -1144       N  
ATOM   3302  N   GLN B  75     -33.330 -31.251 -11.626  1.00152.10           N  
ANISOU 3302  N   GLN B  75    17463  19385  20943   -503    768  -1377       N  
ATOM   3303  CA  GLN B  75     -33.314 -31.571 -13.056  1.00152.15           C  
ANISOU 3303  CA  GLN B  75    17506  19412  20893   -600    712  -1521       C  
ATOM   3304  C   GLN B  75     -33.750 -33.006 -13.373  1.00154.80           C  
ANISOU 3304  C   GLN B  75    17564  19758  21495   -629    786  -1634       C  
ATOM   3305  O   GLN B  75     -34.629 -33.196 -14.215  1.00155.34           O  
ANISOU 3305  O   GLN B  75    17587  19855  21581   -603    689  -1755       O  
ATOM   3306  CB  GLN B  75     -31.939 -31.263 -13.669  1.00153.36           C  
ANISOU 3306  CB  GLN B  75    17842  19573  20857   -778    764  -1543       C  
ATOM   3307  N   ALA B  76     -33.141 -34.005 -12.703  1.00149.53           N  
ANISOU 3307  N   ALA B  76    16727  19059  21028   -674    946  -1602       N  
ATOM   3308  CA  ALA B  76     -33.443 -35.424 -12.909  1.00149.23           C  
ANISOU 3308  CA  ALA B  76    16457  18998  21245   -714   1034  -1698       C  
ATOM   3309  C   ALA B  76     -33.898 -36.113 -11.623  1.00151.33           C  
ANISOU 3309  C   ALA B  76    16573  19200  21724   -649   1142  -1611       C  
ATOM   3310  O   ALA B  76     -33.450 -35.743 -10.535  1.00150.04           O  
ANISOU 3310  O   ALA B  76    16472  19005  21531   -599   1185  -1469       O  
ATOM   3311  CB  ALA B  76     -32.230 -36.138 -13.485  1.00149.93           C  
ANISOU 3311  CB  ALA B  76    16519  19080  21368   -841   1114  -1777       C  
ATOM   3312  N   ARG B  77     -34.782 -37.123 -11.754  1.00147.64           N  
ANISOU 3312  N   ARG B  77    15924  18713  21458   -666   1194  -1704       N  
ATOM   3313  CA  ARG B  77     -35.313 -37.892 -10.626  1.00147.19           C  
ANISOU 3313  CA  ARG B  77    15751  18581  21593   -652   1321  -1645       C  
ATOM   3314  C   ARG B  77     -34.948 -39.397 -10.726  1.00150.18           C  
ANISOU 3314  C   ARG B  77    16027  18854  22181   -741   1444  -1698       C  
ATOM   3315  O   ARG B  77     -35.773 -40.208 -11.161  1.00150.77           O  
ANISOU 3315  O   ARG B  77    15964  18922  22399   -800   1489  -1824       O  
ATOM   3316  CB  ARG B  77     -36.821 -37.695 -10.515  1.00148.86           C  
ANISOU 3316  CB  ARG B  77    15850  18859  21850   -610   1293  -1727       C  
ATOM   3317  N   PRO B  78     -33.714 -39.793 -10.325  1.00145.16           N  
ANISOU 3317  N   PRO B  78    15456  18133  21564   -742   1492  -1621       N  
ATOM   3318  CA  PRO B  78     -33.331 -41.210 -10.426  1.00145.35           C  
ANISOU 3318  CA  PRO B  78    15410  18035  21781   -796   1580  -1682       C  
ATOM   3319  C   PRO B  78     -33.580 -42.025  -9.149  1.00148.69           C  
ANISOU 3319  C   PRO B  78    15861  18295  22340   -781   1695  -1566       C  
ATOM   3320  O   PRO B  78     -34.069 -41.486  -8.155  1.00147.99           O  
ANISOU 3320  O   PRO B  78    15827  18205  22196   -742   1722  -1443       O  
ATOM   3321  CB  PRO B  78     -31.840 -41.129 -10.772  1.00146.61           C  
ANISOU 3321  CB  PRO B  78    15624  18208  21872   -786   1538  -1706       C  
ATOM   3322  CG  PRO B  78     -31.378 -39.788 -10.221  1.00150.03           C  
ANISOU 3322  CG  PRO B  78    16185  18720  22098   -724   1480  -1585       C  
ATOM   3323  CD  PRO B  78     -32.589 -38.984  -9.815  1.00145.48           C  
ANISOU 3323  CD  PRO B  78    15633  18190  21452   -687   1456  -1507       C  
ATOM   3324  N   THR B  79     -33.235 -43.318  -9.183  1.00145.43           N  
ANISOU 3324  N   THR B  79    15430  17732  22092   -818   1762  -1613       N  
ATOM   3325  CA  THR B  79     -33.310 -44.208  -8.007  1.00145.86           C  
ANISOU 3325  CA  THR B  79    15576  17582  22261   -819   1867  -1508       C  
ATOM   3326  C   THR B  79     -32.102 -45.154  -7.805  1.00149.16           C  
ANISOU 3326  C   THR B  79    16076  17857  22742   -742   1832  -1502       C  
ATOM   3327  O   THR B  79     -31.638 -45.775  -8.758  1.00148.99           O  
ANISOU 3327  O   THR B  79    15968  17852  22787   -760   1792  -1655       O  
ATOM   3328  CB  THR B  79     -34.590 -45.043  -8.051  1.00155.03           C  
ANISOU 3328  CB  THR B  79    16658  18675  23569   -954   1990  -1600       C  
ATOM   3329  OG1 THR B  79     -35.720 -44.165  -8.028  1.00154.17           O  
ANISOU 3329  OG1 THR B  79    16421  18751  23407   -997   1979  -1681       O  
ATOM   3330  CG2 THR B  79     -34.650 -45.973  -6.861  1.00154.85           C  
ANISOU 3330  CG2 THR B  79    16782  18443  23611   -998   2124  -1476       C  
ATOM   3331  N   VAL B  80     -31.613 -45.265  -6.565  1.00145.17           N  
ANISOU 3331  N   VAL B  80    15733  17217  22208   -647   1833  -1342       N  
ATOM   3332  CA  VAL B  80     -30.355 -45.979  -6.251  1.00145.26           C  
ANISOU 3332  CA  VAL B  80    15836  17090  22265   -523   1763  -1341       C  
ATOM   3333  C   VAL B  80     -30.199 -47.502  -6.458  1.00150.15           C  
ANISOU 3333  C   VAL B  80    16483  17499  23069   -552   1797  -1435       C  
ATOM   3334  O   VAL B  80     -29.211 -47.941  -7.039  1.00149.90           O  
ANISOU 3334  O   VAL B  80    16347  17499  23109   -528   1733  -1604       O  
ATOM   3335  CB  VAL B  80     -29.917 -45.676  -4.804  1.00149.15           C  
ANISOU 3335  CB  VAL B  80    16518  17485  22667   -399   1739  -1148       C  
ATOM   3336  N   ILE B  81     -31.159 -48.307  -6.016  1.00147.59           N  
ANISOU 3336  N   ILE B  81    16309  16957  22812   -619   1907  -1338       N  
ATOM   3337  CA  ILE B  81     -31.118 -49.748  -6.303  1.00149.19           C  
ANISOU 3337  CA  ILE B  81    16605  16907  23174   -666   1958  -1400       C  
ATOM   3338  C   ILE B  81     -29.814 -50.533  -5.986  1.00153.26           C  
ANISOU 3338  C   ILE B  81    17216  17270  23746   -473   1812  -1447       C  
ATOM   3339  O   ILE B  81     -29.262 -51.170  -6.880  1.00152.78           O  
ANISOU 3339  O   ILE B  81    17002  17273  23775   -445   1743  -1639       O  
ATOM   3340  CB  ILE B  81     -31.537 -50.014  -7.763  1.00152.58           C  
ANISOU 3340  CB  ILE B  81    16836  17416  23720   -837   2040  -1588       C  
ATOM   3341  N   ARG B  82     -29.288 -50.479  -4.759  1.00150.24           N  
ANISOU 3341  N   ARG B  82    17084  16698  23303   -333   1755  -1288       N  
ATOM   3342  CA  ARG B  82     -27.980 -51.090  -4.497  1.00151.02           C  
ANISOU 3342  CA  ARG B  82    17297  16644  23442   -101   1582  -1335       C  
ATOM   3343  C   ARG B  82     -28.055 -52.387  -3.677  1.00157.08           C  
ANISOU 3343  C   ARG B  82    18407  17012  24263    -51   1580  -1238       C  
ATOM   3344  O   ARG B  82     -29.032 -52.610  -2.959  1.00157.44           O  
ANISOU 3344  O   ARG B  82    18654  16903  24262   -201   1727  -1078       O  
ATOM   3345  CB  ARG B  82     -27.018 -50.073  -3.848  1.00150.08           C  
ANISOU 3345  CB  ARG B  82    17170  16674  23180     79   1454  -1273       C  
ATOM   3346  CG  ARG B  82     -27.430 -49.584  -2.461  1.00160.43           C  
ANISOU 3346  CG  ARG B  82    18705  17908  24343     88   1500  -1018       C  
ATOM   3347  CD  ARG B  82     -26.431 -48.594  -1.901  1.00169.08           C  
ANISOU 3347  CD  ARG B  82    19770  19166  25307    265   1370   -985       C  
ATOM   3348  NE  ARG B  82     -26.399 -48.629  -0.439  1.00178.41           N  
ANISOU 3348  NE  ARG B  82    21246  20164  26377    366   1344   -768       N  
ATOM   3349  CZ  ARG B  82     -25.542 -49.351   0.277  1.00194.45           C  
ANISOU 3349  CZ  ARG B  82    23501  21971  28410    588   1186   -748       C  
ATOM   3350  NH1 ARG B  82     -24.631 -50.105  -0.326  1.00182.85           N  
ANISOU 3350  NH1 ARG B  82    21971  20440  27065    747   1036   -949       N  
ATOM   3351  NH2 ARG B  82     -25.588 -49.324   1.602  1.00182.27           N  
ANISOU 3351  NH2 ARG B  82    22251  20264  26739    663   1165   -539       N  
ATOM   3352  N   TRP B  83     -27.007 -53.231  -3.784  1.00154.94           N  
ANISOU 3352  N   TRP B  83    18215  16573  24081    157   1409  -1352       N  
ATOM   3353  CA  TRP B  83     -26.883 -54.511  -3.080  1.00157.61           C  
ANISOU 3353  CA  TRP B  83    18926  16497  24463    255   1352  -1281       C  
ATOM   3354  C   TRP B  83     -25.413 -54.882  -2.851  1.00162.29           C  
ANISOU 3354  C   TRP B  83    19586  16994  25082    600   1078  -1390       C  
ATOM   3355  O   TRP B  83     -24.610 -54.818  -3.783  1.00161.30           O  
ANISOU 3355  O   TRP B  83    19174  17057  25055    698    972  -1637       O  
ATOM   3356  CB  TRP B  83     -27.660 -55.621  -3.825  1.00157.90           C  
ANISOU 3356  CB  TRP B  83    18991  16352  24652     67   1481  -1377       C  
ATOM   3357  CG  TRP B  83     -27.251 -57.035  -3.521  1.00162.17           C  
ANISOU 3357  CG  TRP B  83    19869  16474  25275    203   1374  -1395       C  
ATOM   3358  CD1 TRP B  83     -26.766 -57.951  -4.408  1.00166.44           C  
ANISOU 3358  CD1 TRP B  83    20333  16917  25988    286   1281  -1617       C  
ATOM   3359  CD2 TRP B  83     -27.318 -57.703  -2.251  1.00164.64           C  
ANISOU 3359  CD2 TRP B  83    20677  16390  25487    269   1343  -1186       C  
ATOM   3360  NE1 TRP B  83     -26.527 -59.146  -3.772  1.00169.20           N  
ANISOU 3360  NE1 TRP B  83    21105  16824  26358    417   1181  -1560       N  
ATOM   3361  CE2 TRP B  83     -26.847 -59.020  -2.446  1.00171.51           C  
ANISOU 3361  CE2 TRP B  83    21774  16916  26474    408   1214  -1290       C  
ATOM   3362  CE3 TRP B  83     -27.716 -57.312  -0.961  1.00166.19           C  
ANISOU 3362  CE3 TRP B  83    21171  16481  25494    224   1408   -924       C  
ATOM   3363  CZ2 TRP B  83     -26.768 -59.950  -1.401  1.00174.15           C  
ANISOU 3363  CZ2 TRP B  83    22657  16785  26728    508   1136  -1130       C  
ATOM   3364  CZ3 TRP B  83     -27.637 -58.233   0.073  1.00170.91           C  
ANISOU 3364  CZ3 TRP B  83    22299  16633  26006    303   1347   -766       C  
ATOM   3365  CH2 TRP B  83     -27.167 -59.534  -0.151  1.00174.55           C  
ANISOU 3365  CH2 TRP B  83    23013  16737  26573    447   1207   -862       C  
ATOM   3366  N   SER B  84     -25.072 -55.267  -1.604  1.00160.45           N  
ANISOU 3366  N   SER B  84    19734  16476  24754    780    962  -1224       N  
ATOM   3367  CA  SER B  84     -23.717 -55.653  -1.201  1.00161.90           C  
ANISOU 3367  CA  SER B  84    20027  16541  24948   1148    669  -1325       C  
ATOM   3368  C   SER B  84     -23.564 -57.175  -1.096  1.00168.88           C  
ANISOU 3368  C   SER B  84    21254  16983  25931   1279    553  -1363       C  
ATOM   3369  O   SER B  84     -24.287 -57.818  -0.329  1.00170.32           O  
ANISOU 3369  O   SER B  84    21860  16817  26038   1180    637  -1147       O  
ATOM   3370  CB  SER B  84     -23.334 -54.980   0.115  1.00165.39           C  
ANISOU 3370  CB  SER B  84    20667  16975  25197   1307    571  -1132       C  
ATOM   3371  OG  SER B  84     -24.241 -55.312   1.154  1.00175.44           O  
ANISOU 3371  OG  SER B  84    22364  17951  26344   1176    693   -844       O  
ATOM   3372  N   GLU B  85     -22.627 -57.746  -1.883  1.00166.18           N  
ANISOU 3372  N   GLU B  85    20737  16654  25750   1487    365  -1653       N  
ATOM   3373  CA  GLU B  85     -22.333 -59.185  -1.932  1.00169.33           C  
ANISOU 3373  CA  GLU B  85    21424  16648  26266   1657    212  -1746       C  
ATOM   3374  C   GLU B  85     -20.907 -59.472  -2.427  1.00173.96           C  
ANISOU 3374  C   GLU B  85    21790  17324  26984   2015    -87  -2089       C  
ATOM   3375  O   GLU B  85     -20.181 -58.548  -2.800  1.00171.57           O  
ANISOU 3375  O   GLU B  85    21088  17419  26682   2084   -139  -2267       O  
ATOM   3376  CB  GLU B  85     -23.358 -59.915  -2.818  1.00170.92           C  
ANISOU 3376  CB  GLU B  85    21607  16739  26598   1351    439  -1779       C  
ATOM   3377  N   GLY B  86     -20.531 -60.753  -2.420  1.00173.61           N  
ANISOU 3377  N   GLY B  86    22017  16903  27044   2231   -275  -2194       N  
ATOM   3378  CA  GLY B  86     -19.230 -61.229  -2.878  1.00175.12           C  
ANISOU 3378  CA  GLY B  86    22027  17128  27383   2594   -577  -2557       C  
ATOM   3379  C   GLY B  86     -19.270 -61.942  -4.217  1.00178.81           C  
ANISOU 3379  C   GLY B  86    22239  17626  28075   2498   -523  -2839       C  
ATOM   3380  O   GLY B  86     -18.258 -62.500  -4.650  1.00180.37           O  
ANISOU 3380  O   GLY B  86    22301  17816  28417   2790   -767  -3169       O  
ATOM   3381  N   GLY B  87     -20.436 -61.919  -4.866  1.00173.17           N  
ANISOU 3381  N   GLY B  87    21449  16959  27390   2098   -210  -2730       N  
ATOM   3382  CA  GLY B  87     -20.666 -62.544  -6.165  1.00172.91           C  
ANISOU 3382  CA  GLY B  87    21175  16969  27554   1946   -113  -2967       C  
ATOM   3383  C   GLY B  87     -20.184 -61.695  -7.322  1.00173.62           C  
ANISOU 3383  C   GLY B  87    20672  17581  27716   1858    -57  -3256       C  
ATOM   3384  O   GLY B  87     -20.404 -60.482  -7.334  1.00170.07           O  
ANISOU 3384  O   GLY B  87    20002  17474  27142   1687     82  -3160       O  
ATOM   3385  N   LYS B  88     -19.528 -62.335  -8.308  1.00171.27           N  
ANISOU 3385  N   LYS B  88    20132  17335  27608   1963   -163  -3617       N  
ATOM   3386  CA  LYS B  88     -18.970 -61.673  -9.491  1.00169.09           C  
ANISOU 3386  CA  LYS B  88    19315  17533  27399   1871   -115  -3943       C  
ATOM   3387  C   LYS B  88     -20.029 -61.143 -10.464  1.00169.57           C  
ANISOU 3387  C   LYS B  88    19147  17839  27444   1441    199  -3878       C  
ATOM   3388  O   LYS B  88     -19.917 -59.997 -10.904  1.00166.47           O  
ANISOU 3388  O   LYS B  88    18445  17849  26956   1290    300  -3926       O  
ATOM   3389  CB  LYS B  88     -17.964 -62.586 -10.211  1.00174.41           C  
ANISOU 3389  CB  LYS B  88    19812  18176  28281   2112   -322  -4371       C  
ATOM   3390  N   GLU B  89     -21.047 -61.962 -10.798  1.00166.50           N  
ANISOU 3390  N   GLU B  89    18921  17205  27138   1247    346  -3783       N  
ATOM   3391  CA  GLU B  89     -22.115 -61.574 -11.723  1.00163.87           C  
ANISOU 3391  CA  GLU B  89    18382  17081  26799    863    621  -3744       C  
ATOM   3392  C   GLU B  89     -23.419 -61.260 -10.979  1.00166.32           C  
ANISOU 3392  C   GLU B  89    18953  17265  26977    640    817  -3367       C  
ATOM   3393  O   GLU B  89     -23.990 -62.141 -10.331  1.00167.89           O  
ANISOU 3393  O   GLU B  89    19525  17069  27195    634    843  -3201       O  
ATOM   3394  CB  GLU B  89     -22.321 -62.650 -12.804  1.00166.75           C  
ANISOU 3394  CB  GLU B  89    18651  17342  27364    773    664  -3979       C  
ATOM   3395  CG  GLU B  89     -22.925 -62.117 -14.092  1.00174.63           C  
ANISOU 3395  CG  GLU B  89    19289  18693  28370    451    871  -4096       C  
ATOM   3396  CD  GLU B  89     -23.018 -63.136 -15.210  1.00195.32           C  
ANISOU 3396  CD  GLU B  89    21777  21248  31186    371    903  -4362       C  
ATOM   3397  OE1 GLU B  89     -23.942 -63.979 -15.172  1.00190.02           O  
ANISOU 3397  OE1 GLU B  89    21318  20291  30588    240   1014  -4258       O  
ATOM   3398  OE2 GLU B  89     -22.171 -63.084 -16.131  1.00188.95           O  
ANISOU 3398  OE2 GLU B  89    20652  20685  30455    420    832  -4691       O  
ATOM   3399  N   VAL B  90     -23.865 -59.987 -11.051  1.00159.69           N  
ANISOU 3399  N   VAL B  90    17929  16757  25991    457    953  -3248       N  
ATOM   3400  CA  VAL B  90     -25.086 -59.491 -10.397  1.00158.14           C  
ANISOU 3400  CA  VAL B  90    17901  16521  25662    243   1141  -2935       C  
ATOM   3401  C   VAL B  90     -26.032 -58.876 -11.446  1.00159.58           C  
ANISOU 3401  C   VAL B  90    17793  17007  25834    -68   1345  -2982       C  
ATOM   3402  O   VAL B  90     -25.578 -58.138 -12.324  1.00157.45           O  
ANISOU 3402  O   VAL B  90    17206  17076  25540    -98   1325  -3155       O  
ATOM   3403  CB  VAL B  90     -24.800 -58.490  -9.232  1.00160.83           C  
ANISOU 3403  CB  VAL B  90    18363  16934  25813    362   1081  -2712       C  
ATOM   3404  CG1 VAL B  90     -26.095 -57.912  -8.669  1.00160.41           C  
ANISOU 3404  CG1 VAL B  90    18579  16722  25646    183   1252  -2399       C  
ATOM   3405  CG2 VAL B  90     -23.979 -59.130  -8.112  1.00162.66           C  
ANISOU 3405  CG2 VAL B  90    18780  16976  26048    721    822  -2751       C  
ATOM   3406  N   PHE B  91     -27.341 -59.179 -11.341  1.00156.31           N  
ANISOU 3406  N   PHE B  91    17500  16468  25423   -302   1536  -2845       N  
ATOM   3407  CA  PHE B  91     -28.392 -58.674 -12.233  1.00154.44           C  
ANISOU 3407  CA  PHE B  91    17017  16487  25175   -580   1715  -2890       C  
ATOM   3408  C   PHE B  91     -29.695 -58.413 -11.463  1.00157.99           C  
ANISOU 3408  C   PHE B  91    17626  16869  25534   -770   1894  -2658       C  
ATOM   3409  O   PHE B  91     -29.962 -59.090 -10.469  1.00159.42           O  
ANISOU 3409  O   PHE B  91    18139  16722  25710   -763   1933  -2503       O  
ATOM   3410  CB  PHE B  91     -28.638 -59.655 -13.389  1.00157.49           C  
ANISOU 3410  CB  PHE B  91    17270  16829  25741   -695   1768  -3128       C  
ATOM   3411  N   ILE B  92     -30.502 -57.432 -11.922  1.00152.44           N  
ANISOU 3411  N   ILE B  92    16701  16472  24748   -941   1998  -2652       N  
ATOM   3412  CA  ILE B  92     -31.771 -57.075 -11.281  1.00151.99           C  
ANISOU 3412  CA  ILE B  92    16725  16415  24611  -1123   2167  -2489       C  
ATOM   3413  C   ILE B  92     -32.909 -56.872 -12.283  1.00155.28           C  
ANISOU 3413  C   ILE B  92    16880  17057  25064  -1353   2300  -2633       C  
ATOM   3414  O   ILE B  92     -32.736 -56.170 -13.282  1.00153.16           O  
ANISOU 3414  O   ILE B  92    16350  17080  24763  -1347   2235  -2761       O  
ATOM   3415  CB  ILE B  92     -31.607 -55.855 -10.347  1.00153.37           C  
ANISOU 3415  CB  ILE B  92    16956  16718  24600  -1029   2121  -2284       C  
ATOM   3416  N   SER B  93     -34.074 -57.486 -11.999  1.00153.53           N  
ANISOU 3416  N   SER B  93    16743  16696  24894  -1561   2485  -2624       N  
ATOM   3417  CA  SER B  93     -35.289 -57.409 -12.814  1.00153.36           C  
ANISOU 3417  CA  SER B  93    16482  16871  24918  -1783   2620  -2784       C  
ATOM   3418  C   SER B  93     -36.492 -57.036 -11.945  1.00157.68           C  
ANISOU 3418  C   SER B  93    17086  17439  25387  -1947   2787  -2681       C  
ATOM   3419  O   SER B  93     -36.646 -57.569 -10.843  1.00158.79           O  
ANISOU 3419  O   SER B  93    17518  17308  25508  -2002   2887  -2536       O  
ATOM   3420  CB  SER B  93     -35.548 -58.736 -13.522  1.00159.05           C  
ANISOU 3420  CB  SER B  93    17194  17419  25820  -1915   2707  -2971       C  
ATOM   3421  OG  SER B  93     -34.482 -59.079 -14.392  1.00167.67           O  
ANISOU 3421  OG  SER B  93    18199  18516  26994  -1773   2558  -3104       O  
ATOM   3422  N   GLY B  94     -37.325 -56.128 -12.450  1.00153.15           N  
ANISOU 3422  N   GLY B  94    16247  17184  24759  -2022   2808  -2773       N  
ATOM   3423  CA  GLY B  94     -38.510 -55.652 -11.745  1.00153.39           C  
ANISOU 3423  CA  GLY B  94    16257  17301  24722  -2167   2953  -2738       C  
ATOM   3424  C   GLY B  94     -39.764 -55.579 -12.590  1.00157.89           C  
ANISOU 3424  C   GLY B  94    16532  18106  25353  -2343   3045  -2985       C  
ATOM   3425  O   GLY B  94     -39.991 -56.434 -13.450  1.00158.61           O  
ANISOU 3425  O   GLY B  94    16523  18164  25578  -2453   3098  -3176       O  
ATOM   3426  N   SER B  95     -40.596 -54.554 -12.328  1.00153.89           N  
ANISOU 3426  N   SER B  95    15880  17842  24749  -2360   3056  -3000       N  
ATOM   3427  CA  SER B  95     -41.859 -54.309 -13.030  1.00154.45           C  
ANISOU 3427  CA  SER B  95    15649  18176  24860  -2487   3111  -3258       C  
ATOM   3428  C   SER B  95     -41.757 -53.169 -14.056  1.00156.49           C  
ANISOU 3428  C   SER B  95    15683  18748  25030  -2313   2885  -3339       C  
ATOM   3429  O   SER B  95     -42.628 -53.053 -14.922  1.00156.59           O  
ANISOU 3429  O   SER B  95    15445  18973  25079  -2371   2869  -3580       O  
ATOM   3430  CB  SER B  95     -42.983 -54.039 -12.034  1.00159.25           C  
ANISOU 3430  CB  SER B  95    16241  18837  25429  -2637   3283  -3276       C  
ATOM   3431  OG  SER B  95     -42.705 -52.910 -11.223  1.00166.41           O  
ANISOU 3431  OG  SER B  95    17227  19818  26181  -2481   3189  -3077       O  
ATOM   3432  N   PHE B  96     -40.692 -52.340 -13.960  1.00151.18           N  
ANISOU 3432  N   PHE B  96    15118  18095  24227  -2105   2708  -3149       N  
ATOM   3433  CA  PHE B  96     -40.425 -51.210 -14.857  1.00149.34           C  
ANISOU 3433  CA  PHE B  96    14763  18112  23868  -1950   2494  -3187       C  
ATOM   3434  C   PHE B  96     -40.172 -51.679 -16.294  1.00153.74           C  
ANISOU 3434  C   PHE B  96    15188  18736  24490  -1972   2422  -3378       C  
ATOM   3435  O   PHE B  96     -40.690 -51.073 -17.233  1.00153.10           O  
ANISOU 3435  O   PHE B  96    14940  18885  24346  -1946   2310  -3534       O  
ATOM   3436  CB  PHE B  96     -39.242 -50.377 -14.342  1.00149.15           C  
ANISOU 3436  CB  PHE B  96    14918  18056  23696  -1771   2366  -2947       C  
ATOM   3437  N   ASN B  97     -39.393 -52.767 -16.453  1.00151.17           N  
ANISOU 3437  N   ASN B  97    14950  18202  24284  -2012   2476  -3376       N  
ATOM   3438  CA  ASN B  97     -39.070 -53.376 -17.746  1.00151.49           C  
ANISOU 3438  CA  ASN B  97    14876  18277  24407  -2050   2432  -3564       C  
ATOM   3439  C   ASN B  97     -39.972 -54.596 -18.022  1.00157.89           C  
ANISOU 3439  C   ASN B  97    15583  19002  25407  -2246   2603  -3761       C  
ATOM   3440  O   ASN B  97     -39.750 -55.317 -18.999  1.00158.08           O  
ANISOU 3440  O   ASN B  97    15520  19015  25530  -2299   2598  -3925       O  
ATOM   3441  CB  ASN B  97     -37.587 -53.762 -17.795  1.00151.62           C  
ANISOU 3441  CB  ASN B  97    15031  18139  24441  -1953   2369  -3477       C  
ATOM   3442  N   ASN B  98     -41.003 -54.801 -17.161  1.00156.04           N  
ANISOU 3442  N   ASN B  98    15355  18719  25214  -2371   2765  -3762       N  
ATOM   3443  CA  ASN B  98     -41.995 -55.888 -17.195  1.00158.43           C  
ANISOU 3443  CA  ASN B  98    15579  18940  25678  -2603   2972  -3953       C  
ATOM   3444  C   ASN B  98     -41.353 -57.292 -17.091  1.00163.92           C  
ANISOU 3444  C   ASN B  98    16463  19302  26519  -2688   3082  -3928       C  
ATOM   3445  O   ASN B  98     -41.881 -58.262 -17.645  1.00165.31           O  
ANISOU 3445  O   ASN B  98    16549  19424  26836  -2861   3204  -4133       O  
ATOM   3446  CB  ASN B  98     -42.932 -55.763 -18.410  1.00159.92           C  
ANISOU 3446  CB  ASN B  98    15454  19407  25902  -2668   2934  -4256       C  
ATOM   3447  N   TRP B  99     -40.222 -57.386 -16.344  1.00159.97           N  
ANISOU 3447  N   TRP B  99    16230  18570  25979  -2554   3027  -3688       N  
ATOM   3448  CA  TRP B  99     -39.421 -58.594 -16.083  1.00161.17           C  
ANISOU 3448  CA  TRP B  99    16622  18372  26242  -2557   3071  -3629       C  
ATOM   3449  C   TRP B  99     -38.946 -59.311 -17.372  1.00165.53           C  
ANISOU 3449  C   TRP B  99    17042  18930  26921  -2552   3008  -3832       C  
ATOM   3450  O   TRP B  99     -38.746 -60.529 -17.368  1.00167.02           O  
ANISOU 3450  O   TRP B  99    17371  18843  27247  -2624   3089  -3881       O  
ATOM   3451  CB  TRP B  99     -40.157 -59.556 -15.128  1.00162.50           C  
ANISOU 3451  CB  TRP B  99    17006  18260  26477  -2775   3310  -3601       C  
ATOM   3452  N   SER B 100     -38.733 -58.539 -18.458  1.00160.45           N  
ANISOU 3452  N   SER B 100    16159  18587  26219  -2467   2858  -3945       N  
ATOM   3453  CA  SER B 100     -38.286 -59.053 -19.754  1.00160.47           C  
ANISOU 3453  CA  SER B 100    16012  18648  26312  -2469   2793  -4151       C  
ATOM   3454  C   SER B 100     -36.760 -59.110 -19.867  1.00163.31           C  
ANISOU 3454  C   SER B 100    16474  18915  26663  -2283   2647  -4085       C  
ATOM   3455  O   SER B 100     -36.228 -60.070 -20.427  1.00163.96           O  
ANISOU 3455  O   SER B 100    16551  18865  26881  -2291   2645  -4220       O  
ATOM   3456  CB  SER B 100     -38.872 -58.223 -20.893  1.00163.13           C  
ANISOU 3456  CB  SER B 100    16071  19347  26564  -2491   2708  -4322       C  
ATOM   3457  OG  SER B 100     -38.446 -56.871 -20.826  1.00169.83           O  
ANISOU 3457  OG  SER B 100    16924  20388  27214  -2337   2550  -4189       O  
ATOM   3458  N   THR B 101     -36.064 -58.083 -19.342  1.00157.98           N  
ANISOU 3458  N   THR B 101    15874  18319  25831  -2119   2526  -3904       N  
ATOM   3459  CA  THR B 101     -34.602 -57.980 -19.381  1.00156.98           C  
ANISOU 3459  CA  THR B 101    15815  18153  25677  -1941   2386  -3868       C  
ATOM   3460  C   THR B 101     -33.988 -57.836 -17.978  1.00160.27           C  
ANISOU 3460  C   THR B 101    16486  18368  26042  -1793   2355  -3623       C  
ATOM   3461  O   THR B 101     -34.634 -57.309 -17.068  1.00159.43           O  
ANISOU 3461  O   THR B 101    16475  18252  25848  -1816   2413  -3449       O  
ATOM   3462  CB  THR B 101     -34.153 -56.866 -20.356  1.00163.78           C  
ANISOU 3462  CB  THR B 101    16504  19343  26383  -1899   2257  -3947       C  
ATOM   3463  OG1 THR B 101     -32.728 -56.881 -20.468  1.00163.27           O  
ANISOU 3463  OG1 THR B 101    16469  19257  26309  -1765   2150  -3976       O  
ATOM   3464  CG2 THR B 101     -34.640 -55.467 -19.949  1.00160.77           C  
ANISOU 3464  CG2 THR B 101    16131  19157  25797  -1869   2215  -3792       C  
ATOM   3465  N   LYS B 102     -32.734 -58.305 -17.820  1.00156.96           N  
ANISOU 3465  N   LYS B 102    16164  17798  25676  -1633   2253  -3632       N  
ATOM   3466  CA  LYS B 102     -31.981 -58.233 -16.569  1.00156.67           C  
ANISOU 3466  CA  LYS B 102    16367  17568  25591  -1454   2183  -3432       C  
ATOM   3467  C   LYS B 102     -30.930 -57.124 -16.656  1.00158.23           C  
ANISOU 3467  C   LYS B 102    16482  17994  25645  -1302   2036  -3414       C  
ATOM   3468  O   LYS B 102     -29.989 -57.222 -17.449  1.00157.76           O  
ANISOU 3468  O   LYS B 102    16290  18032  25620  -1240   1946  -3600       O  
ATOM   3469  CB  LYS B 102     -31.342 -59.591 -16.233  1.00161.54           C  
ANISOU 3469  CB  LYS B 102    17178  17830  26370  -1356   2152  -3475       C  
ATOM   3470  N   ILE B 103     -31.117 -56.054 -15.862  1.00153.04           N  
ANISOU 3470  N   ILE B 103    15894  17432  24822  -1265   2027  -3211       N  
ATOM   3471  CA  ILE B 103     -30.228 -54.888 -15.825  1.00150.93           C  
ANISOU 3471  CA  ILE B 103    15575  17378  24393  -1150   1912  -3174       C  
ATOM   3472  C   ILE B 103     -28.915 -55.235 -15.090  1.00155.17           C  
ANISOU 3472  C   ILE B 103    16242  17755  24960   -933   1793  -3151       C  
ATOM   3473  O   ILE B 103     -28.973 -55.707 -13.951  1.00155.70           O  
ANISOU 3473  O   ILE B 103    16540  17565  25055   -844   1796  -2985       O  
ATOM   3474  CB  ILE B 103     -30.951 -53.630 -15.237  1.00152.35           C  
ANISOU 3474  CB  ILE B 103    15788  17708  24389  -1185   1941  -2977       C  
ATOM   3475  CG1 ILE B 103     -32.311 -53.328 -15.951  1.00152.47           C  
ANISOU 3475  CG1 ILE B 103    15666  17882  24385  -1366   2028  -3038       C  
ATOM   3476  CG2 ILE B 103     -30.041 -52.389 -15.200  1.00151.36           C  
ANISOU 3476  CG2 ILE B 103    15635  17793  24082  -1088   1833  -2939       C  
ATOM   3477  CD1 ILE B 103     -32.291 -52.997 -17.512  1.00159.26           C  
ANISOU 3477  CD1 ILE B 103    16312  18993  25205  -1454   1982  -3258       C  
ATOM   3478  N   PRO B 104     -27.729 -55.024 -15.716  1.00151.27           N  
ANISOU 3478  N   PRO B 104    15609  17414  24454   -848   1687  -3335       N  
ATOM   3479  CA  PRO B 104     -26.474 -55.365 -15.026  1.00151.99           C  
ANISOU 3479  CA  PRO B 104    15789  17376  24584   -617   1554  -3363       C  
ATOM   3480  C   PRO B 104     -26.046 -54.344 -13.973  1.00154.39           C  
ANISOU 3480  C   PRO B 104    16197  17745  24720   -497   1494  -3172       C  
ATOM   3481  O   PRO B 104     -26.149 -53.136 -14.197  1.00152.02           O  
ANISOU 3481  O   PRO B 104    15809  17699  24252   -582   1519  -3128       O  
ATOM   3482  CB  PRO B 104     -25.460 -55.491 -16.165  1.00154.13           C  
ANISOU 3482  CB  PRO B 104    15826  17830  24907   -608   1488  -3684       C  
ATOM   3483  CG  PRO B 104     -25.987 -54.622 -17.246  1.00156.99           C  
ANISOU 3483  CG  PRO B 104    16015  18488  25145   -829   1573  -3746       C  
ATOM   3484  CD  PRO B 104     -27.475 -54.485 -17.070  1.00151.91           C  
ANISOU 3484  CD  PRO B 104    15454  17791  24475   -966   1685  -3549       C  
ATOM   3485  N   LEU B 105     -25.569 -54.846 -12.821  1.00152.12           N  
ANISOU 3485  N   LEU B 105    16121  17209  24468   -295   1406  -3062       N  
ATOM   3486  CA  LEU B 105     -25.098 -54.047 -11.687  1.00151.11           C  
ANISOU 3486  CA  LEU B 105    16117  17101  24197   -151   1334  -2884       C  
ATOM   3487  C   LEU B 105     -23.624 -53.688 -11.897  1.00154.96           C  
ANISOU 3487  C   LEU B 105    16450  17768  24661      7   1191  -3100       C  
ATOM   3488  O   LEU B 105     -22.825 -54.566 -12.235  1.00156.28           O  
ANISOU 3488  O   LEU B 105    16556  17853  24971    138   1088  -3329       O  
ATOM   3489  CB  LEU B 105     -25.267 -54.844 -10.367  1.00152.88           C  
ANISOU 3489  CB  LEU B 105    16672  16957  24459     -8   1295  -2680       C  
ATOM   3490  CG  LEU B 105     -26.612 -54.798  -9.587  1.00157.32           C  
ANISOU 3490  CG  LEU B 105    17446  17368  24961   -157   1448  -2402       C  
ATOM   3491  CD1 LEU B 105     -26.849 -53.461  -8.915  1.00157.69           C  
ANISOU 3491  CD1 LEU B 105    17500  17599  24815   -179   1479  -2209       C  
ATOM   3492  CD2 LEU B 105     -27.807 -55.263 -10.417  1.00157.59           C  
ANISOU 3492  CD2 LEU B 105    17394  17401  25084   -407   1615  -2458       C  
ATOM   3493  N   ILE B 106     -23.301 -52.405 -11.814  1.00149.80           N  
ANISOU 3493  N   ILE B 106    15726  17364  23828    -11   1188  -3052       N  
ATOM   3494  CA  ILE B 106     -21.915 -51.983 -11.833  1.00149.76           C  
ANISOU 3494  CA  ILE B 106    15557  17570  23773     95   1083  -3277       C  
ATOM   3495  C   ILE B 106     -21.344 -52.347 -10.479  1.00155.32           C  
ANISOU 3495  C   ILE B 106    16400  18093  24523    398    913  -3264       C  
ATOM   3496  O   ILE B 106     -22.071 -52.361  -9.488  1.00154.56           O  
ANISOU 3496  O   ILE B 106    16525  17854  24345    486    895  -2995       O  
ATOM   3497  CB  ILE B 106     -21.775 -50.479 -12.089  1.00150.67           C  
ANISOU 3497  CB  ILE B 106    15575  18006  23667    -61   1154  -3246       C  
ATOM   3498  CG1 ILE B 106     -22.604 -50.073 -13.307  1.00149.86           C  
ANISOU 3498  CG1 ILE B 106    15374  18060  23504   -336   1288  -3271       C  
ATOM   3499  CG2 ILE B 106     -20.315 -50.120 -12.304  1.00151.76           C  
ANISOU 3499  CG2 ILE B 106    15547  18375  23742     10   1075  -3505       C  
ATOM   3500  CD1 ILE B 106     -22.502 -51.041 -14.464  1.00158.12           C  
ANISOU 3500  CD1 ILE B 106    16223  19186  24670   -445   1309  -3585       C  
ATOM   3501  N   LYS B 107     -20.056 -52.657 -10.420  1.00153.92           N  
ANISOU 3501  N   LYS B 107    16090  17920  24474    565    777  -3574       N  
ATOM   3502  CA  LYS B 107     -19.493 -53.112  -9.162  1.00155.94           C  
ANISOU 3502  CA  LYS B 107    16453  18002  24797    898    566  -3644       C  
ATOM   3503  C   LYS B 107     -18.566 -52.105  -8.508  1.00159.26           C  
ANISOU 3503  C   LYS B 107    16855  18593  25063   1027    483  -3622       C  
ATOM   3504  O   LYS B 107     -17.543 -51.722  -9.067  1.00157.75           O  
ANISOU 3504  O   LYS B 107    16423  18739  24778    916    530  -3809       O  
ATOM   3505  CB  LYS B 107     -18.752 -54.435  -9.362  1.00160.88           C  
ANISOU 3505  CB  LYS B 107    16890  18626  25609   1041    436  -4042       C  
HETATM 3506  N   SEP B 108     -18.934 -51.702  -7.299  1.00156.82           N  
ANISOU 3506  N   SEP B 108    16823  18037  24722   1253    362  -3403       N  
HETATM 3507  CA  SEP B 108     -18.049 -50.987  -6.417  1.00156.57           C  
ANISOU 3507  CA  SEP B 108    16831  18100  24559   1432    249  -3359       C  
HETATM 3508  CB  SEP B 108     -18.811 -50.343  -5.270  1.00154.00           C  
ANISOU 3508  CB  SEP B 108    16580  17907  24025   1260    392  -3061       C  
HETATM 3509  OG  SEP B 108     -18.107 -49.185  -4.840  1.00153.68           O  
ANISOU 3509  OG  SEP B 108    16396  18130  23866   1349    321  -3192       O  
HETATM 3510  C   SEP B 108     -17.199 -52.100  -5.916  1.00163.02           C  
ANISOU 3510  C   SEP B 108    17940  18563  25436   1780     23  -3287       C  
HETATM 3511  O   SEP B 108     -17.589 -53.271  -6.107  1.00163.28           O  
ANISOU 3511  O   SEP B 108    18287  18254  25497   1775     49  -3031       O  
HETATM 3512  P   SEP B 108     -16.693 -49.342  -4.100  1.00153.43           P  
ANISOU 3512  P   SEP B 108    16609  17992  23694   1499    255  -2908       P  
HETATM 3513  O1P SEP B 108     -15.691 -49.056  -5.187  1.00152.91           O  
ANISOU 3513  O1P SEP B 108    16344  18249  23506   1543    210  -3088       O  
HETATM 3514  O2P SEP B 108     -16.699 -50.770  -3.616  1.00156.20           O  
ANISOU 3514  O2P SEP B 108    17222  18000  24128   1834     34  -2861       O  
HETATM 3515  O3P SEP B 108     -16.747 -48.308  -3.008  1.00151.22           O  
ANISOU 3515  O3P SEP B 108    16517  17646  23292   1280    441  -2521       O  
ATOM   3516  N   HIS B 109     -16.064 -51.809  -5.298  1.00161.22           N  
ANISOU 3516  N   HIS B 109    17618  18417  25220   2076   -202  -3533       N  
ATOM   3517  CA  HIS B 109     -15.180 -52.887  -4.903  1.00164.01           C  
ANISOU 3517  CA  HIS B 109    18232  18465  25618   2473   -485  -3538       C  
ATOM   3518  C   HIS B 109     -15.942 -53.798  -3.954  1.00167.73           C  
ANISOU 3518  C   HIS B 109    19183  18570  25978   2519   -486  -3090       C  
ATOM   3519  O   HIS B 109     -15.883 -55.019  -4.076  1.00170.03           O  
ANISOU 3519  O   HIS B 109    19798  18472  26332   2736   -649  -3029       O  
ATOM   3520  CB  HIS B 109     -13.950 -52.325  -4.196  1.00165.91           C  
ANISOU 3520  CB  HIS B 109    18265  18952  25820   2739   -691  -3831       C  
ATOM   3521  CG  HIS B 109     -14.232 -51.814  -2.818  1.00166.88           C  
ANISOU 3521  CG  HIS B 109    18324  19343  25741   2608   -578  -3681       C  
ATOM   3522  ND1 HIS B 109     -14.470 -52.652  -1.749  1.00168.64           N  
ANISOU 3522  ND1 HIS B 109    18859  19397  25820   2745   -651  -3367       N  
ATOM   3523  CD2 HIS B 109     -14.327 -50.553  -2.335  1.00166.35           C  
ANISOU 3523  CD2 HIS B 109    17940  19678  25586   2346   -399  -3809       C  
ATOM   3524  CE1 HIS B 109     -14.694 -51.929  -0.667  1.00165.69           C  
ANISOU 3524  CE1 HIS B 109    18327  19335  25294   2574   -517  -3320       C  
ATOM   3525  NE2 HIS B 109     -14.614 -50.653  -0.995  1.00164.64           N  
ANISOU 3525  NE2 HIS B 109    17832  19541  25183   2331   -364  -3575       N  
ATOM   3526  N   ASN B 110     -16.674 -53.204  -3.018  1.00161.39           N  
ANISOU 3526  N   ASN B 110    18441  17879  25000   2308   -305  -2793       N  
ATOM   3527  CA  ASN B 110     -17.527 -53.985  -2.137  1.00161.16           C  
ANISOU 3527  CA  ASN B 110    18836  17553  24844   2302   -267  -2385       C  
ATOM   3528  C   ASN B 110     -19.011 -53.967  -2.489  1.00163.56           C  
ANISOU 3528  C   ASN B 110    19296  17685  25166   1982    -15  -2137       C  
ATOM   3529  O   ASN B 110     -19.644 -55.013  -2.605  1.00165.19           O  
ANISOU 3529  O   ASN B 110    19859  17502  25402   2026    -42  -1986       O  
ATOM   3530  CB  ASN B 110     -17.337 -53.540  -0.687  1.00160.23           C  
ANISOU 3530  CB  ASN B 110    18709  17643  24529   2291   -238  -2226       C  
ATOM   3531  N   ASP B 111     -19.554 -52.767  -2.659  1.00156.85           N  
ANISOU 3531  N   ASP B 111    18192  17117  24288   1663    222  -2111       N  
ATOM   3532  CA  ASP B 111     -20.969 -52.593  -2.979  1.00155.42           C  
ANISOU 3532  CA  ASP B 111    18090  16840  24122   1356    462  -1922       C  
ATOM   3533  C   ASP B 111     -21.252 -52.756  -4.466  1.00156.94           C  
ANISOU 3533  C   ASP B 111    17932  17296  24402   1117    607  -2114       C  
ATOM   3534  O   ASP B 111     -20.363 -52.573  -5.296  1.00155.03           O  
ANISOU 3534  O   ASP B 111    17394  17386  24125   1092    598  -2299       O  
ATOM   3535  CB  ASP B 111     -21.476 -51.243  -2.470  1.00155.65           C  
ANISOU 3535  CB  ASP B 111    18286  16881  23974   1204    612  -1594       C  
ATOM   3536  CG  ASP B 111     -21.602 -51.199  -0.959  1.00163.57           C  
ANISOU 3536  CG  ASP B 111    19113  18206  24828   1225    600  -1584       C  
ATOM   3537  OD1 ASP B 111     -21.576 -52.273  -0.326  1.00162.23           O  
ANISOU 3537  OD1 ASP B 111    18624  18356  24658   1096    667  -1746       O  
ATOM   3538  OD2 ASP B 111     -21.724 -50.089  -0.403  1.00169.73           O  
ANISOU 3538  OD2 ASP B 111    20101  18910  25479   1353    532  -1407       O  
ATOM   3539  N   PHE B 112     -22.490 -53.104  -4.798  1.00153.37           N  
ANISOU 3539  N   PHE B 112    17533  16693  24048    926    746  -2075       N  
ATOM   3540  CA  PHE B 112     -22.938 -53.111  -6.183  1.00151.66           C  
ANISOU 3540  CA  PHE B 112    17026  16684  23912    697    879  -2244       C  
ATOM   3541  C   PHE B 112     -24.126 -52.178  -6.354  1.00152.40           C  
ANISOU 3541  C   PHE B 112    17072  16934  23898    422   1087  -2060       C  
ATOM   3542  O   PHE B 112     -25.084 -52.239  -5.586  1.00152.26           O  
ANISOU 3542  O   PHE B 112    17276  16729  23846    329   1193  -1833       O  
ATOM   3543  CB  PHE B 112     -23.341 -54.537  -6.539  1.00155.55           C  
ANISOU 3543  CB  PHE B 112    17582  16927  24593    675    886  -2360       C  
ATOM   3544  CG  PHE B 112     -22.205 -55.510  -6.495  1.00159.76           C  
ANISOU 3544  CG  PHE B 112    18161  17293  25249    968    659  -2574       C  
ATOM   3545  CD1 PHE B 112     -21.349 -55.643  -7.572  1.00163.07           C  
ANISOU 3545  CD1 PHE B 112    18258  17936  25765   1031    573  -2920       C  
ATOM   3546  CD2 PHE B 112     -21.991 -56.290  -5.374  1.00164.54           C  
ANISOU 3546  CD2 PHE B 112    19144  17510  25863   1182    523  -2446       C  
ATOM   3547  CE1 PHE B 112     -20.301 -56.540  -7.532  1.00166.67           C  
ANISOU 3547  CE1 PHE B 112    18726  18253  26346   1325    346  -3160       C  
ATOM   3548  CE2 PHE B 112     -20.945 -57.191  -5.327  1.00170.09           C  
ANISOU 3548  CE2 PHE B 112    19900  18048  26678   1495    275  -2664       C  
ATOM   3549  CZ  PHE B 112     -20.099 -57.315  -6.408  1.00168.29           C  
ANISOU 3549  CZ  PHE B 112    19307  18067  26567   1574    183  -3032       C  
ATOM   3550  N   VAL B 113     -24.069 -51.322  -7.367  1.00146.27           N  
ANISOU 3550  N   VAL B 113    16019  16497  23059    290   1142  -2176       N  
ATOM   3551  CA  VAL B 113     -25.151 -50.364  -7.605  1.00143.71           C  
ANISOU 3551  CA  VAL B 113    15634  16345  22625     67   1296  -2043       C  
ATOM   3552  C   VAL B 113     -25.375 -50.080  -9.088  1.00145.95           C  
ANISOU 3552  C   VAL B 113    15663  16858  22932   -114   1362  -2238       C  
ATOM   3553  O   VAL B 113     -24.411 -49.991  -9.851  1.00145.52           O  
ANISOU 3553  O   VAL B 113    15436  16962  22894    -84   1294  -2469       O  
ATOM   3554  CB  VAL B 113     -24.940 -49.058  -6.814  1.00145.98           C  
ANISOU 3554  CB  VAL B 113    15952  16793  22721    109   1280  -1893       C  
ATOM   3555  N   ALA B 114     -26.653 -49.928  -9.487  1.00141.37           N  
ANISOU 3555  N   ALA B 114    15063  16307  22346   -307   1492  -2163       N  
ATOM   3556  CA  ALA B 114     -27.069 -49.621 -10.858  1.00140.15           C  
ANISOU 3556  CA  ALA B 114    14705  16357  22188   -481   1547  -2321       C  
ATOM   3557  C   ALA B 114     -28.221 -48.616 -10.841  1.00141.85           C  
ANISOU 3557  C   ALA B 114    14918  16707  22274   -613   1629  -2182       C  
ATOM   3558  O   ALA B 114     -29.283 -48.898 -10.278  1.00141.75           O  
ANISOU 3558  O   ALA B 114    14994  16569  22296   -669   1715  -2050       O  
ATOM   3559  CB  ALA B 114     -27.476 -50.891 -11.592  1.00142.40           C  
ANISOU 3559  CB  ALA B 114    14942  16501  22664   -554   1593  -2462       C  
ATOM   3560  N   ILE B 115     -27.995 -47.435 -11.439  1.00136.54           N  
ANISOU 3560  N   ILE B 115    14154  16283  21440   -665   1600  -2228       N  
ATOM   3561  CA  ILE B 115     -28.962 -46.335 -11.492  1.00134.87           C  
ANISOU 3561  CA  ILE B 115    13949  16212  21083   -751   1633  -2122       C  
ATOM   3562  C   ILE B 115     -29.953 -46.518 -12.643  1.00138.60           C  
ANISOU 3562  C   ILE B 115    14306  16759  21598   -896   1674  -2244       C  
ATOM   3563  O   ILE B 115     -29.544 -46.771 -13.778  1.00138.51           O  
ANISOU 3563  O   ILE B 115    14188  16831  21610   -961   1652  -2435       O  
ATOM   3564  CB  ILE B 115     -28.245 -44.948 -11.528  1.00136.57           C  
ANISOU 3564  CB  ILE B 115    14182  16625  21081   -734   1570  -2103       C  
ATOM   3565  CG1 ILE B 115     -27.114 -44.832 -10.461  1.00136.99           C  
ANISOU 3565  CG1 ILE B 115    14316  16630  21104   -585   1520  -2034       C  
ATOM   3566  CG2 ILE B 115     -29.227 -43.770 -11.444  1.00136.10           C  
ANISOU 3566  CG2 ILE B 115    14173  16678  20863   -783   1575  -1979       C  
ATOM   3567  CD1 ILE B 115     -27.484 -45.029  -8.927  1.00144.60           C  
ANISOU 3567  CD1 ILE B 115    15436  17411  22094   -468   1536  -1802       C  
ATOM   3568  N   LEU B 116     -31.256 -46.384 -12.336  1.00134.81           N  
ANISOU 3568  N   LEU B 116    13835  16263  21123   -947   1733  -2156       N  
ATOM   3569  CA  LEU B 116     -32.347 -46.508 -13.301  1.00134.85           C  
ANISOU 3569  CA  LEU B 116    13720  16351  21166  -1064   1760  -2281       C  
ATOM   3570  C   LEU B 116     -33.436 -45.475 -12.997  1.00137.75           C  
ANISOU 3570  C   LEU B 116    14095  16833  21412  -1068   1751  -2195       C  
ATOM   3571  O   LEU B 116     -33.939 -45.424 -11.872  1.00137.46           O  
ANISOU 3571  O   LEU B 116    14125  16716  21388  -1039   1811  -2056       O  
ATOM   3572  CB  LEU B 116     -32.918 -47.942 -13.281  1.00136.52           C  
ANISOU 3572  CB  LEU B 116    13890  16384  21597  -1134   1864  -2350       C  
ATOM   3573  CG  LEU B 116     -33.875 -48.329 -14.414  1.00142.00           C  
ANISOU 3573  CG  LEU B 116    14426  17163  22366  -1261   1896  -2536       C  
ATOM   3574  CD1 LEU B 116     -33.116 -48.722 -15.675  1.00142.38           C  
ANISOU 3574  CD1 LEU B 116    14380  17273  22444  -1296   1843  -2726       C  
ATOM   3575  CD2 LEU B 116     -34.772 -49.472 -13.990  1.00146.12           C  
ANISOU 3575  CD2 LEU B 116    14939  17511  23070  -1353   2035  -2558       C  
ATOM   3576  N   ASP B 117     -33.779 -44.641 -13.998  1.00133.55           N  
ANISOU 3576  N   ASP B 117    13511  16483  20749  -1098   1665  -2290       N  
ATOM   3577  CA  ASP B 117     -34.805 -43.603 -13.875  1.00132.85           C  
ANISOU 3577  CA  ASP B 117    13428  16513  20538  -1069   1611  -2251       C  
ATOM   3578  C   ASP B 117     -36.205 -44.228 -13.908  1.00137.30           C  
ANISOU 3578  C   ASP B 117    13851  17072  21245  -1130   1682  -2353       C  
ATOM   3579  O   ASP B 117     -36.820 -44.346 -14.972  1.00137.57           O  
ANISOU 3579  O   ASP B 117    13770  17204  21294  -1180   1637  -2528       O  
ATOM   3580  CB  ASP B 117     -34.625 -42.514 -14.953  1.00134.19           C  
ANISOU 3580  CB  ASP B 117    13645  16847  20494  -1065   1469  -2320       C  
ATOM   3581  CG  ASP B 117     -33.417 -41.621 -14.742  1.00143.30           C  
ANISOU 3581  CG  ASP B 117    14963  18033  21451  -1017   1412  -2200       C  
ATOM   3582  OD1 ASP B 117     -32.856 -41.633 -13.623  1.00143.61           O  
ANISOU 3582  OD1 ASP B 117    15023  18026  21518  -1035   1451  -2202       O  
ATOM   3583  OD2 ASP B 117     -33.009 -40.938 -15.706  1.00148.67           O  
ANISOU 3583  OD2 ASP B 117    15749  18791  21949   -961   1323  -2130       O  
ATOM   3584  N   LEU B 118     -36.685 -44.660 -12.730  1.00133.83           N  
ANISOU 3584  N   LEU B 118    13425  16519  20905  -1142   1803  -2259       N  
ATOM   3585  CA  LEU B 118     -37.987 -45.301 -12.559  1.00134.91           C  
ANISOU 3585  CA  LEU B 118    13433  16647  21180  -1239   1916  -2368       C  
ATOM   3586  C   LEU B 118     -39.093 -44.280 -12.250  1.00138.47           C  
ANISOU 3586  C   LEU B 118    13816  17258  21540  -1191   1868  -2396       C  
ATOM   3587  O   LEU B 118     -38.848 -43.349 -11.478  1.00136.97           O  
ANISOU 3587  O   LEU B 118    13734  17087  21220  -1095   1821  -2241       O  
ATOM   3588  CB  LEU B 118     -37.914 -46.360 -11.451  1.00135.88           C  
ANISOU 3588  CB  LEU B 118    13645  16546  21437  -1312   2091  -2267       C  
ATOM   3589  N   PRO B 119     -40.314 -44.430 -12.825  1.00136.19           N  
ANISOU 3589  N   PRO B 119    13337  17091  21319  -1246   1872  -2612       N  
ATOM   3590  CA  PRO B 119     -41.387 -43.468 -12.516  1.00136.31           C  
ANISOU 3590  CA  PRO B 119    13262  17269  21259  -1173   1806  -2682       C  
ATOM   3591  C   PRO B 119     -41.989 -43.680 -11.125  1.00140.73           C  
ANISOU 3591  C   PRO B 119    13812  17772  21887  -1245   1984  -2625       C  
ATOM   3592  O   PRO B 119     -41.882 -44.778 -10.572  1.00141.07           O  
ANISOU 3592  O   PRO B 119    13895  17649  22058  -1391   2177  -2585       O  
ATOM   3593  CB  PRO B 119     -42.409 -43.704 -13.630  1.00139.54           C  
ANISOU 3593  CB  PRO B 119    13454  17831  21734  -1204   1746  -2971       C  
ATOM   3594  CG  PRO B 119     -42.215 -45.118 -14.027  1.00144.86           C  
ANISOU 3594  CG  PRO B 119    14073  18384  22583  -1368   1896  -3047       C  
ATOM   3595  CD  PRO B 119     -40.779 -45.477 -13.761  1.00139.11           C  
ANISOU 3595  CD  PRO B 119    13550  17465  21841  -1367   1930  -2827       C  
ATOM   3596  N   GLU B 120     -42.614 -42.624 -10.566  1.00137.12           N  
ANISOU 3596  N   GLU B 120    13323  17443  21332  -1148   1918  -2627       N  
ATOM   3597  CA  GLU B 120     -43.244 -42.618  -9.242  1.00137.68           C  
ANISOU 3597  CA  GLU B 120    13376  17500  21436  -1216   2079  -2594       C  
ATOM   3598  C   GLU B 120     -44.364 -43.654  -9.113  1.00143.83           C  
ANISOU 3598  C   GLU B 120    13965  18293  22389  -1426   2288  -2820       C  
ATOM   3599  O   GLU B 120     -45.293 -43.671  -9.924  1.00144.65           O  
ANISOU 3599  O   GLU B 120    13838  18568  22553  -1433   2235  -3097       O  
ATOM   3600  CB  GLU B 120     -43.751 -41.211  -8.886  1.00138.68           C  
ANISOU 3600  CB  GLU B 120    13469  17795  21427  -1051   1933  -2610       C  
ATOM   3601  N   GLY B 121     -44.238 -44.515  -8.106  1.00141.11           N  
ANISOU 3601  N   GLY B 121    13740  17764  22112  -1598   2521  -2708       N  
ATOM   3602  CA  GLY B 121     -45.184 -45.587  -7.816  1.00143.39           C  
ANISOU 3602  CA  GLY B 121    13919  18017  22545  -1854   2772  -2893       C  
ATOM   3603  C   GLY B 121     -44.540 -46.809  -7.188  1.00147.80           C  
ANISOU 3603  C   GLY B 121    14726  18270  23162  -2024   2971  -2718       C  
ATOM   3604  O   GLY B 121     -43.317 -46.857  -7.023  1.00145.81           O  
ANISOU 3604  O   GLY B 121    14705  17844  22852  -1915   2892  -2466       O  
ATOM   3605  N   GLU B 122     -45.368 -47.810  -6.834  1.00146.87           N  
ANISOU 3605  N   GLU B 122    14570  18082  23151  -2294   3226  -2869       N  
ATOM   3606  CA  GLU B 122     -44.913 -49.056  -6.215  1.00147.90           C  
ANISOU 3606  CA  GLU B 122    14980  17889  23327  -2481   3426  -2724       C  
ATOM   3607  C   GLU B 122     -44.404 -50.051  -7.262  1.00151.92           C  
ANISOU 3607  C   GLU B 122    15507  18264  23954  -2500   3393  -2774       C  
ATOM   3608  O   GLU B 122     -45.170 -50.491  -8.124  1.00152.74           O  
ANISOU 3608  O   GLU B 122    15380  18481  24171  -2618   3446  -3046       O  
ATOM   3609  CB  GLU B 122     -46.022 -49.674  -5.348  1.00152.19           C  
ANISOU 3609  CB  GLU B 122    15522  18397  23904  -2800   3737  -2866       C  
ATOM   3610  N   HIS B 123     -43.103 -50.385  -7.189  1.00147.33           N  
ANISOU 3610  N   HIS B 123    15182  17452  23346  -2374   3298  -2532       N  
ATOM   3611  CA  HIS B 123     -42.440 -51.317  -8.102  1.00147.28           C  
ANISOU 3611  CA  HIS B 123    15215  17298  23446  -2363   3249  -2565       C  
ATOM   3612  C   HIS B 123     -41.662 -52.381  -7.327  1.00152.37           C  
ANISOU 3612  C   HIS B 123    16224  17564  24104  -2417   3342  -2367       C  
ATOM   3613  O   HIS B 123     -40.851 -52.041  -6.461  1.00150.97           O  
ANISOU 3613  O   HIS B 123    16277  17266  23819  -2281   3272  -2123       O  
ATOM   3614  CB  HIS B 123     -41.516 -50.560  -9.070  1.00145.52           C  
ANISOU 3614  CB  HIS B 123    14900  17213  23176  -2108   2979  -2530       C  
ATOM   3615  N   GLN B 124     -41.923 -53.667  -7.629  1.00151.26           N  
ANISOU 3615  N   GLN B 124    16150  17232  24092  -2608   3490  -2481       N  
ATOM   3616  CA  GLN B 124     -41.273 -54.807  -6.977  1.00152.78           C  
ANISOU 3616  CA  GLN B 124    16724  17025  24300  -2662   3569  -2322       C  
ATOM   3617  C   GLN B 124     -40.141 -55.368  -7.837  1.00156.11           C  
ANISOU 3617  C   GLN B 124    17186  17320  24809  -2486   3392  -2314       C  
ATOM   3618  O   GLN B 124     -40.375 -55.766  -8.980  1.00155.81           O  
ANISOU 3618  O   GLN B 124    16934  17371  24894  -2539   3385  -2524       O  
ATOM   3619  CB  GLN B 124     -42.300 -55.898  -6.634  1.00157.42           C  
ANISOU 3619  CB  GLN B 124    17421  17439  24953  -3012   3866  -2452       C  
ATOM   3620  N   TYR B 125     -38.914 -55.384  -7.283  1.00152.25           N  
ANISOU 3620  N   TYR B 125    16955  16638  24255  -2274   3245  -2095       N  
ATOM   3621  CA  TYR B 125     -37.707 -55.872  -7.957  1.00151.71           C  
ANISOU 3621  CA  TYR B 125    16928  16453  24261  -2078   3063  -2099       C  
ATOM   3622  C   TYR B 125     -37.037 -57.022  -7.195  1.00158.08           C  
ANISOU 3622  C   TYR B 125    18151  16829  25084  -2046   3070  -1964       C  
ATOM   3623  O   TYR B 125     -37.196 -57.131  -5.977  1.00158.85           O  
ANISOU 3623  O   TYR B 125    18551  16729  25074  -2103   3159  -1787       O  
ATOM   3624  CB  TYR B 125     -36.713 -54.720  -8.173  1.00150.05           C  
ANISOU 3624  CB  TYR B 125    16596  16458  23960  -1807   2829  -2022       C  
ATOM   3625  N   LYS B 126     -36.284 -57.872  -7.921  1.00155.61           N  
ANISOU 3625  N   LYS B 126    17864  16365  24894  -1948   2965  -2057       N  
ATOM   3626  CA  LYS B 126     -35.568 -59.023  -7.363  1.00157.90           C  
ANISOU 3626  CA  LYS B 126    18551  16230  25214  -1867   2920  -1965       C  
ATOM   3627  C   LYS B 126     -34.168 -59.164  -7.962  1.00161.28           C  
ANISOU 3627  C   LYS B 126    18925  16642  25712  -1567   2660  -2022       C  
ATOM   3628  O   LYS B 126     -34.001 -59.021  -9.176  1.00159.62           O  
ANISOU 3628  O   LYS B 126    18390  16657  25601  -1545   2601  -2218       O  
ATOM   3629  CB  LYS B 126     -36.373 -60.313  -7.572  1.00163.41           C  
ANISOU 3629  CB  LYS B 126    19395  16672  26021  -2138   3125  -2081       C  
ATOM   3630  N   PHE B 127     -33.168 -59.451  -7.108  1.00159.02           N  
ANISOU 3630  N   PHE B 127    18958  16096  25366  -1338   2504  -1871       N  
ATOM   3631  CA  PHE B 127     -31.769 -59.623  -7.513  1.00158.70           C  
ANISOU 3631  CA  PHE B 127    18879  16030  25390  -1030   2246  -1952       C  
ATOM   3632  C   PHE B 127     -31.456 -61.073  -7.893  1.00165.60           C  
ANISOU 3632  C   PHE B 127    19940  16564  26418  -1000   2207  -2076       C  
ATOM   3633  O   PHE B 127     -32.099 -61.995  -7.389  1.00167.75           O  
ANISOU 3633  O   PHE B 127    20541  16502  26693  -1166   2347  -2008       O  
ATOM   3634  CB  PHE B 127     -30.810 -59.160  -6.400  1.00160.31           C  
ANISOU 3634  CB  PHE B 127    19306  16149  25455   -762   2065  -1765       C  
ATOM   3635  CG  PHE B 127     -30.972 -57.729  -5.943  1.00159.25           C  
ANISOU 3635  CG  PHE B 127    19019  16324  25164   -761   2081  -1637       C  
ATOM   3636  CD1 PHE B 127     -30.463 -56.679  -6.698  1.00159.65           C  
ANISOU 3636  CD1 PHE B 127    18700  16755  25205   -669   1983  -1745       C  
ATOM   3637  CD2 PHE B 127     -31.591 -57.434  -4.735  1.00161.87           C  
ANISOU 3637  CD2 PHE B 127    19605  16553  25347   -856   2194  -1413       C  
ATOM   3638  CE1 PHE B 127     -30.601 -55.356  -6.268  1.00158.34           C  
ANISOU 3638  CE1 PHE B 127    18426  16848  24887   -664   1991  -1626       C  
ATOM   3639  CE2 PHE B 127     -31.725 -56.111  -4.303  1.00162.38           C  
ANISOU 3639  CE2 PHE B 127    19527  16897  25272   -842   2201  -1306       C  
ATOM   3640  CZ  PHE B 127     -31.229 -55.081  -5.073  1.00157.78           C  
ANISOU 3640  CZ  PHE B 127    18586  16677  24688   -739   2094  -1409       C  
ATOM   3641  N   PHE B 128     -30.452 -61.263  -8.770  1.00162.04           N  
ANISOU 3641  N   PHE B 128    19290  16194  26084   -796   2020  -2271       N  
ATOM   3642  CA  PHE B 128     -29.981 -62.569  -9.233  1.00164.51           C  
ANISOU 3642  CA  PHE B 128    19733  16215  26557   -711   1936  -2429       C  
ATOM   3643  C   PHE B 128     -28.449 -62.603  -9.188  1.00168.88           C  
ANISOU 3643  C   PHE B 128    20284  16743  27140   -330   1636  -2516       C  
ATOM   3644  O   PHE B 128     -27.790 -61.951 -10.004  1.00166.47           O  
ANISOU 3644  O   PHE B 128    19602  16779  26871   -235   1539  -2692       O  
ATOM   3645  CB  PHE B 128     -30.516 -62.881 -10.642  1.00165.89           C  
ANISOU 3645  CB  PHE B 128    19572  16568  26890   -910   2055  -2677       C  
ATOM   3646  N   VAL B 129     -27.889 -63.326  -8.198  1.00168.27           N  
ANISOU 3646  N   VAL B 129    20640  16266  27027   -116   1486  -2403       N  
ATOM   3647  CA  VAL B 129     -26.441 -63.440  -7.984  1.00169.04           C  
ANISOU 3647  CA  VAL B 129    20774  16305  27149    284   1172  -2501       C  
ATOM   3648  C   VAL B 129     -25.963 -64.873  -8.258  1.00176.41           C  
ANISOU 3648  C   VAL B 129    21930  16857  28241    444   1029  -2666       C  
ATOM   3649  O   VAL B 129     -26.466 -65.819  -7.646  1.00178.73           O  
ANISOU 3649  O   VAL B 129    22686  16711  28513    378   1081  -2528       O  
ATOM   3650  CB  VAL B 129     -26.003 -62.930  -6.576  1.00173.19           C  
ANISOU 3650  CB  VAL B 129    21598  16723  27483    485   1042  -2258       C  
ATOM   3651  CG1 VAL B 129     -24.481 -62.904  -6.440  1.00173.78           C  
ANISOU 3651  CG1 VAL B 129    21620  16822  27587    908    707  -2414       C  
ATOM   3652  CG2 VAL B 129     -26.583 -61.550  -6.274  1.00169.76           C  
ANISOU 3652  CG2 VAL B 129    20967  16640  26895    307   1201  -2091       C  
ATOM   3653  N   ASP B 130     -24.982 -65.012  -9.181  1.00173.03           N  
ANISOU 3653  N   ASP B 130    21181  16598  27964    645    853  -2975       N  
ATOM   3654  CA  ASP B 130     -24.341 -66.265  -9.614  1.00176.00           C  
ANISOU 3654  CA  ASP B 130    21666  16688  28518    849    675  -3208       C  
ATOM   3655  C   ASP B 130     -25.353 -67.344 -10.066  1.00181.75           C  
ANISOU 3655  C   ASP B 130    22578  17127  29350    576    874  -3214       C  
ATOM   3656  O   ASP B 130     -25.210 -68.523  -9.728  1.00184.82           O  
ANISOU 3656  O   ASP B 130    23378  17051  29796    701    768  -3218       O  
ATOM   3657  CB  ASP B 130     -23.368 -66.799  -8.537  1.00180.85           C  
ANISOU 3657  CB  ASP B 130    22695  16936  29084   1263    358  -3158       C  
ATOM   3658  CG  ASP B 130     -22.289 -65.817  -8.119  1.00189.19           C  
ANISOU 3658  CG  ASP B 130    23546  18282  30055   1550    146  -3206       C  
ATOM   3659  OD1 ASP B 130     -21.476 -65.422  -8.984  1.00188.43           O  
ANISOU 3659  OD1 ASP B 130    22987  18546  30062   1654     55  -3511       O  
ATOM   3660  OD2 ASP B 130     -22.236 -65.471  -6.920  1.00195.32           O  
ANISOU 3660  OD2 ASP B 130    24636  18921  30656   1663     74  -2954       O  
ATOM   3661  N   GLY B 131     -26.352 -66.915 -10.838  1.00176.12           N  
ANISOU 3661  N   GLY B 131    21566  16696  28657    212   1151  -3230       N  
ATOM   3662  CA  GLY B 131     -27.407 -67.775 -11.363  1.00177.30           C  
ANISOU 3662  CA  GLY B 131    21799  16665  28902    -96   1378  -3267       C  
ATOM   3663  C   GLY B 131     -28.381 -68.268 -10.311  1.00183.19           C  
ANISOU 3663  C   GLY B 131    23057  17020  29528   -300   1552  -2989       C  
ATOM   3664  O   GLY B 131     -28.799 -69.428 -10.352  1.00185.70           O  
ANISOU 3664  O   GLY B 131    23682  16956  29920   -415   1629  -3017       O  
ATOM   3665  N   GLN B 132     -28.747 -67.386  -9.359  1.00178.38           N  
ANISOU 3665  N   GLN B 132    22552  16500  28724   -365   1627  -2730       N  
ATOM   3666  CA  GLN B 132     -29.677 -67.685  -8.268  1.00180.00           C  
ANISOU 3666  CA  GLN B 132    23231  16384  28777   -590   1816  -2464       C  
ATOM   3667  C   GLN B 132     -30.456 -66.421  -7.882  1.00180.87           C  
ANISOU 3667  C   GLN B 132    23138  16847  28736   -803   2008  -2301       C  
ATOM   3668  O   GLN B 132     -29.866 -65.463  -7.377  1.00178.52           O  
ANISOU 3668  O   GLN B 132    22756  16746  28327   -605   1870  -2196       O  
ATOM   3669  CB  GLN B 132     -28.922 -68.274  -7.059  1.00184.43           C  
ANISOU 3669  CB  GLN B 132    24378  16473  29226   -297   1587  -2290       C  
ATOM   3670  CG  GLN B 132     -29.806 -69.041  -6.084  1.00204.11           C  
ANISOU 3670  CG  GLN B 132    27483  18492  31578   -549   1778  -2065       C  
ATOM   3671  CD  GLN B 132     -28.993 -69.692  -4.995  1.00228.14           C  
ANISOU 3671  CD  GLN B 132    31144  21038  34502   -230   1511  -1911       C  
ATOM   3672  N   TRP B 133     -31.777 -66.419  -8.144  1.00177.18           N  
ANISOU 3672  N   TRP B 133    22577  16472  28272  -1202   2320  -2310       N  
ATOM   3673  CA  TRP B 133     -32.659 -65.289  -7.850  1.00174.56           C  
ANISOU 3673  CA  TRP B 133    22033  16476  27816  -1421   2511  -2201       C  
ATOM   3674  C   TRP B 133     -32.969 -65.183  -6.350  1.00179.80           C  
ANISOU 3674  C   TRP B 133    23155  16892  28270  -1482   2586  -1915       C  
ATOM   3675  O   TRP B 133     -33.852 -65.881  -5.844  1.00181.93           O  
ANISOU 3675  O   TRP B 133    23762  16878  28486  -1774   2814  -1848       O  
ATOM   3676  CB  TRP B 133     -33.941 -65.354  -8.700  1.00172.90           C  
ANISOU 3676  CB  TRP B 133    21527  16472  27695  -1799   2794  -2366       C  
ATOM   3677  N   VAL B 134     -32.206 -64.327  -5.638  1.00174.87           N  
ANISOU 3677  N   VAL B 134    22557  16369  27517  -1218   2399  -1760       N  
ATOM   3678  CA  VAL B 134     -32.341 -64.094  -4.192  1.00175.73           C  
ANISOU 3678  CA  VAL B 134    23084  16278  27409  -1229   2431  -1485       C  
ATOM   3679  C   VAL B 134     -32.576 -62.595  -3.927  1.00176.18           C  
ANISOU 3679  C   VAL B 134    22814  16771  27354  -1246   2472  -1399       C  
ATOM   3680  O   VAL B 134     -31.800 -61.760  -4.396  1.00173.05           O  
ANISOU 3680  O   VAL B 134    22072  16690  26990  -1009   2287  -1467       O  
ATOM   3681  CB  VAL B 134     -31.130 -64.655  -3.379  1.00181.92           C  
ANISOU 3681  CB  VAL B 134    24328  16673  28122   -858   2130  -1364       C  
ATOM   3682  CG1 VAL B 134     -31.303 -64.424  -1.878  1.00182.99           C  
ANISOU 3682  CG1 VAL B 134    24926  16591  28009   -885   2167  -1073       C  
ATOM   3683  CG2 VAL B 134     -30.901 -66.139  -3.661  1.00185.38           C  
ANISOU 3683  CG2 VAL B 134    25111  16655  28670   -817   2065  -1460       C  
ATOM   3684  N   HIS B 135     -33.644 -62.269  -3.173  1.00173.08           N  
ANISOU 3684  N   HIS B 135    22545  16392  26827  -1539   2723  -1268       N  
ATOM   3685  CA  HIS B 135     -34.013 -60.896  -2.815  1.00170.10           C  
ANISOU 3685  CA  HIS B 135    21904  16391  26334  -1580   2784  -1185       C  
ATOM   3686  C   HIS B 135     -33.170 -60.361  -1.640  1.00173.69           C  
ANISOU 3686  C   HIS B 135    22624  16759  26611  -1317   2599   -954       C  
ATOM   3687  O   HIS B 135     -32.458 -61.134  -0.992  1.00175.66           O  
ANISOU 3687  O   HIS B 135    23314  16623  26807  -1136   2447   -848       O  
ATOM   3688  CB  HIS B 135     -35.521 -60.810  -2.502  1.00171.64           C  
ANISOU 3688  CB  HIS B 135    22096  16649  26472  -2002   3130  -1188       C  
ATOM   3689  CG  HIS B 135     -35.906 -61.405  -1.182  1.00178.16           C  
ANISOU 3689  CG  HIS B 135    23485  17087  27123  -2179   3279   -991       C  
ATOM   3690  ND1 HIS B 135     -36.000 -62.774  -1.006  1.00183.63           N  
ANISOU 3690  ND1 HIS B 135    24632  17316  27824  -2308   3355   -983       N  
ATOM   3691  CD2 HIS B 135     -36.206 -60.793  -0.013  1.00179.92           C  
ANISOU 3691  CD2 HIS B 135    23896  17319  27147  -2254   3366   -804       C  
ATOM   3692  CE1 HIS B 135     -36.351 -62.950   0.257  1.00185.30           C  
ANISOU 3692  CE1 HIS B 135    25317  17263  27827  -2469   3488   -785       C  
ATOM   3693  NE2 HIS B 135     -36.487 -61.787   0.894  1.00183.51           N  
ANISOU 3693  NE2 HIS B 135    24937  17315  27472  -2445   3503   -675       N  
ATOM   3694  N   ASP B 136     -33.261 -59.043  -1.366  1.00167.50           N  
ANISOU 3694  N   ASP B 136    21583  16327  25732  -1288   2600   -887       N  
ATOM   3695  CA  ASP B 136     -32.542 -58.387  -0.272  1.00166.79           C  
ANISOU 3695  CA  ASP B 136    21688  16215  25469  -1061   2445   -682       C  
ATOM   3696  C   ASP B 136     -33.367 -58.438   1.031  1.00172.38           C  
ANISOU 3696  C   ASP B 136    22784  16730  25985  -1296   2652   -478       C  
ATOM   3697  O   ASP B 136     -34.502 -57.953   1.046  1.00171.24           O  
ANISOU 3697  O   ASP B 136    22456  16791  25814  -1592   2903   -509       O  
ATOM   3698  CB  ASP B 136     -32.170 -56.941  -0.648  1.00164.87           C  
ANISOU 3698  CB  ASP B 136    20992  16436  25214   -913   2340   -722       C  
ATOM   3699  CG  ASP B 136     -31.515 -56.161   0.474  1.00174.32           C  
ANISOU 3699  CG  ASP B 136    22348  17654  26232   -710   2206   -527       C  
ATOM   3700  OD1 ASP B 136     -32.221 -55.379   1.141  1.00174.03           O  
ANISOU 3700  OD1 ASP B 136    22300  17755  26068   -862   2354   -412       O  
ATOM   3701  OD2 ASP B 136     -30.304 -56.353   0.702  1.00180.69           O  
ANISOU 3701  OD2 ASP B 136    23285  18340  27027   -395   1951   -508       O  
ATOM   3702  N   PRO B 137     -32.838 -59.052   2.084  1.00171.44           N  
ANISOU 3702  N   PRO B 137    23200  16220  25717  -1169   2547   -286       N  
ATOM   3703  CA  PRO B 137     -33.520 -59.083   3.388  1.00173.27           C  
ANISOU 3703  CA  PRO B 137    23841  16254  25740  -1425   2761    -93       C  
ATOM   3704  C   PRO B 137     -33.654 -57.734   4.113  1.00174.91           C  
ANISOU 3704  C   PRO B 137    23945  16728  25786  -1380   2762     48       C  
ATOM   3705  O   PRO B 137     -34.714 -57.408   4.640  1.00175.32           O  
ANISOU 3705  O   PRO B 137    24130  16780  25703  -1680   3016    129       O  
ATOM   3706  CB  PRO B 137     -32.634 -60.017   4.218  1.00178.87           C  
ANISOU 3706  CB  PRO B 137    25209  16412  26342  -1285   2615     53       C  
ATOM   3707  CG  PRO B 137     -31.914 -60.854   3.217  1.00183.10           C  
ANISOU 3707  CG  PRO B 137    25627  16889  27051   -912   2298    -83       C  
ATOM   3708  CD  PRO B 137     -31.680 -59.957   2.041  1.00174.49           C  
ANISOU 3708  CD  PRO B 137    23867  16320  26113   -791   2226   -254       C  
ATOM   3709  N   SER B 138     -32.571 -56.966   4.114  1.00168.89           N  
ANISOU 3709  N   SER B 138    22948  16189  25032  -1024   2492     58       N  
ATOM   3710  CA  SER B 138     -32.427 -55.716   4.871  1.00166.58           C  
ANISOU 3710  CA  SER B 138    22552  16150  24593   -938   2458    184       C  
ATOM   3711  C   SER B 138     -33.480 -54.649   4.543  1.00167.77           C  
ANISOU 3711  C   SER B 138    22267  16714  24764  -1182   2679    103       C  
ATOM   3712  O   SER B 138     -33.870 -53.894   5.436  1.00166.86           O  
ANISOU 3712  O   SER B 138    22199  16706  24495  -1264   2774    224       O  
ATOM   3713  CB  SER B 138     -31.021 -55.146   4.714  1.00168.29           C  
ANISOU 3713  CB  SER B 138    22604  16508  24829   -517   2125    168       C  
ATOM   3714  OG  SER B 138     -30.716 -54.863   3.359  1.00174.73           O  
ANISOU 3714  OG  SER B 138    22944  17607  25840   -435   2048    -53       O  
ATOM   3715  N   GLU B 139     -33.934 -54.584   3.276  1.00162.75           N  
ANISOU 3715  N   GLU B 139    21217  16308  24312  -1283   2747   -112       N  
ATOM   3716  CA  GLU B 139     -34.940 -53.618   2.817  1.00160.34           C  
ANISOU 3716  CA  GLU B 139    20488  16393  24042  -1476   2915   -229       C  
ATOM   3717  C   GLU B 139     -36.356 -54.236   2.752  1.00165.96           C  
ANISOU 3717  C   GLU B 139    21222  17045  24790  -1878   3232   -336       C  
ATOM   3718  O   GLU B 139     -36.456 -55.459   2.621  1.00168.09           O  
ANISOU 3718  O   GLU B 139    21751  17002  25113  -1998   3305   -365       O  
ATOM   3719  CB  GLU B 139     -34.531 -52.996   1.466  1.00158.84           C  
ANISOU 3719  CB  GLU B 139    19824  16530  24000  -1316   2764   -408       C  
ATOM   3720  CG  GLU B 139     -33.358 -52.027   1.551  1.00166.95           C  
ANISOU 3720  CG  GLU B 139    20738  17730  24964   -996   2515   -341       C  
ATOM   3721  CD  GLU B 139     -33.559 -50.802   2.425  1.00185.27           C  
ANISOU 3721  CD  GLU B 139    23024  20247  27123   -986   2542   -211       C  
ATOM   3722  OE1 GLU B 139     -34.478 -50.002   2.134  1.00177.96           O  
ANISOU 3722  OE1 GLU B 139    21824  19592  26200  -1138   2667   -289       O  
ATOM   3723  OE2 GLU B 139     -32.787 -50.636   3.396  1.00179.19           O  
ANISOU 3723  OE2 GLU B 139    22498  19360  26224   -810   2422    -45       O  
ATOM   3724  N   PRO B 140     -37.455 -53.431   2.847  1.00161.47           N  
ANISOU 3724  N   PRO B 140    20390  16767  24195  -2091   3423   -417       N  
ATOM   3725  CA  PRO B 140     -38.811 -54.020   2.814  1.00163.48           C  
ANISOU 3725  CA  PRO B 140    20636  16994  24486  -2489   3738   -568       C  
ATOM   3726  C   PRO B 140     -39.154 -54.806   1.549  1.00167.56           C  
ANISOU 3726  C   PRO B 140    20953  17510  25203  -2593   3784   -796       C  
ATOM   3727  O   PRO B 140     -38.723 -54.440   0.455  1.00164.83           O  
ANISOU 3727  O   PRO B 140    20275  17371  24984  -2396   3605   -905       O  
ATOM   3728  CB  PRO B 140     -39.733 -52.808   2.993  1.00163.77           C  
ANISOU 3728  CB  PRO B 140    20325  17419  24481  -2596   3852   -661       C  
ATOM   3729  CG  PRO B 140     -38.913 -51.636   2.584  1.00164.72           C  
ANISOU 3729  CG  PRO B 140    20177  17803  24606  -2252   3578   -615       C  
ATOM   3730  CD  PRO B 140     -37.526 -51.966   3.032  1.00160.24           C  
ANISOU 3730  CD  PRO B 140    19943  16971  23970  -1983   3363   -398       C  
ATOM   3731  N   VAL B 141     -39.927 -55.896   1.716  1.00167.09           N  
ANISOU 3731  N   VAL B 141    21119  17211  25157  -2924   4037   -871       N  
ATOM   3732  CA  VAL B 141     -40.347 -56.789   0.634  1.00167.93           C  
ANISOU 3732  CA  VAL B 141    21088  17275  25444  -3075   4123  -1093       C  
ATOM   3733  C   VAL B 141     -41.853 -57.078   0.664  1.00173.72           C  
ANISOU 3733  C   VAL B 141    21705  18102  26199  -3516   4476  -1313       C  
ATOM   3734  O   VAL B 141     -42.474 -57.020   1.728  1.00175.03           O  
ANISOU 3734  O   VAL B 141    22080  18209  26216  -3758   4693  -1257       O  
ATOM   3735  CB  VAL B 141     -39.521 -58.094   0.646  1.00174.02           C  
ANISOU 3735  CB  VAL B 141    22301  17583  26237  -2998   4035   -989       C  
ATOM   3736  N   VAL B 142     -42.430 -57.398  -0.511  1.00170.16           N  
ANISOU 3736  N   VAL B 142    20913  17811  25930  -3628   4538  -1585       N  
ATOM   3737  CA  VAL B 142     -43.849 -57.719  -0.682  1.00172.13           C  
ANISOU 3737  CA  VAL B 142    20976  18190  26234  -4036   4859  -1866       C  
ATOM   3738  C   VAL B 142     -44.028 -59.029  -1.454  1.00178.12           C  
ANISOU 3738  C   VAL B 142    21817  18727  27134  -4219   4967  -2023       C  
ATOM   3739  O   VAL B 142     -43.298 -59.280  -2.415  1.00176.22           O  
ANISOU 3739  O   VAL B 142    21471  18462  27022  -3982   4751  -2039       O  
ATOM   3740  CB  VAL B 142     -44.617 -56.560  -1.351  1.00173.85           C  
ANISOU 3740  CB  VAL B 142    20596  18930  26530  -3995   4830  -2108       C  
ATOM   3741  N   THR B 143     -45.002 -59.857  -1.030  1.00178.30           N  
ANISOU 3741  N   THR B 143    22030  18591  27126  -4659   5314  -2156       N  
ATOM   3742  CA  THR B 143     -45.304 -61.151  -1.648  1.00180.75           C  
ANISOU 3742  CA  THR B 143    22458  18667  27553  -4900   5470  -2321       C  
ATOM   3743  C   THR B 143     -46.001 -60.991  -3.000  1.00183.45           C  
ANISOU 3743  C   THR B 143    22209  19389  28104  -4942   5482  -2678       C  
ATOM   3744  O   THR B 143     -47.006 -60.283  -3.097  1.00182.88           O  
ANISOU 3744  O   THR B 143    21732  19702  28051  -5086   5608  -2914       O  
ATOM   3745  CB  THR B 143     -46.094 -62.037  -0.682  1.00193.23           C  
ANISOU 3745  CB  THR B 143    24477  19943  29000  -5386   5855  -2342       C  
ATOM   3746  N   SER B 144     -45.454 -61.646  -4.041  1.00179.31           N  
ANISOU 3746  N   SER B 144    21639  18758  27733  -4802   5335  -2732       N  
ATOM   3747  CA  SER B 144     -45.979 -61.612  -5.409  1.00178.15           C  
ANISOU 3747  CA  SER B 144    20979  18930  27780  -4817   5314  -3057       C  
ATOM   3748  C   SER B 144     -46.976 -62.748  -5.670  1.00185.27           C  
ANISOU 3748  C   SER B 144    21911  19715  28766  -5262   5648  -3335       C  
ATOM   3749  O   SER B 144     -47.021 -63.716  -4.905  1.00187.84           O  
ANISOU 3749  O   SER B 144    22732  19632  29008  -5526   5860  -3238       O  
ATOM   3750  CB  SER B 144     -44.836 -61.665  -6.419  1.00179.29           C  
ANISOU 3750  CB  SER B 144    21036  19048  28037  -4440   4985  -2986       C  
ATOM   3751  N   GLN B 145     -47.770 -62.625  -6.755  1.00181.49           N  
ANISOU 3751  N   GLN B 145    20921  19593  28444  -5347   5689  -3689       N  
ATOM   3752  CA  GLN B 145     -48.776 -63.609  -7.170  1.00184.53           C  
ANISOU 3752  CA  GLN B 145    21229  19949  28933  -5765   5998  -4020       C  
ATOM   3753  C   GLN B 145     -48.161 -64.937  -7.631  1.00189.03           C  
ANISOU 3753  C   GLN B 145    22134  20098  29591  -5802   5998  -3968       C  
ATOM   3754  O   GLN B 145     -48.816 -65.977  -7.528  1.00191.77           O  
ANISOU 3754  O   GLN B 145    22670  20234  29961  -6204   6304  -4133       O  
ATOM   3755  CB  GLN B 145     -49.684 -63.026  -8.263  1.00185.08           C  
ANISOU 3755  CB  GLN B 145    20637  20539  29145  -5769   5975  -4415       C  
ATOM   3756  N   LEU B 146     -46.908 -64.899  -8.135  1.00183.00           N  
ANISOU 3756  N   LEU B 146    21442  19215  28874  -5393   5661  -3761       N  
ATOM   3757  CA  LEU B 146     -46.167 -66.072  -8.606  1.00183.91           C  
ANISOU 3757  CA  LEU B 146    21854  18941  29082  -5344   5595  -3709       C  
ATOM   3758  C   LEU B 146     -45.760 -66.999  -7.454  1.00189.84           C  
ANISOU 3758  C   LEU B 146    23316  19120  29695  -5478   5713  -3451       C  
ATOM   3759  O   LEU B 146     -45.899 -68.217  -7.578  1.00192.22           O  
ANISOU 3759  O   LEU B 146    23916  19073  30044  -5713   5876  -3528       O  
ATOM   3760  CB  LEU B 146     -44.936 -65.644  -9.417  1.00180.56           C  
ANISOU 3760  CB  LEU B 146    21268  18601  28737  -4863   5199  -3593       C  
ATOM   3761  N   GLY B 147     -45.277 -66.415  -6.354  1.00185.27           N  
ANISOU 3761  N   GLY B 147    23018  18441  28935  -5327   5624  -3154       N  
ATOM   3762  CA  GLY B 147     -44.858 -67.155  -5.168  1.00187.84           C  
ANISOU 3762  CA  GLY B 147    24053  18231  29087  -5415   5697  -2882       C  
ATOM   3763  C   GLY B 147     -43.828 -66.446  -4.313  1.00189.20           C  
ANISOU 3763  C   GLY B 147    24464  18317  29108  -5042   5426  -2533       C  
ATOM   3764  O   GLY B 147     -44.071 -66.204  -3.127  1.00189.94           O  
ANISOU 3764  O   GLY B 147    24868  18300  29001  -5184   5558  -2368       O  
ATOM   3765  N   THR B 148     -42.663 -66.123  -4.909  1.00182.41           N  
ANISOU 3765  N   THR B 148    23459  17513  28335  -4577   5055  -2438       N  
ATOM   3766  CA  THR B 148     -41.537 -65.463  -4.241  1.00179.94           C  
ANISOU 3766  CA  THR B 148    23324  17141  27903  -4178   4760  -2143       C  
ATOM   3767  C   THR B 148     -41.837 -64.023  -3.824  1.00180.24           C  
ANISOU 3767  C   THR B 148    23037  17602  27844  -4115   4745  -2091       C  
ATOM   3768  O   THR B 148     -42.471 -63.282  -4.577  1.00177.77           O  
ANISOU 3768  O   THR B 148    22183  17738  27626  -4159   4782  -2303       O  
ATOM   3769  CB  THR B 148     -40.281 -65.546  -5.109  1.00186.41           C  
ANISOU 3769  CB  THR B 148    24014  17951  28862  -3747   4402  -2135       C  
ATOM   3770  N   ILE B 149     -41.369 -63.635  -2.621  1.00176.27           N  
ANISOU 3770  N   ILE B 149    22886  16944  27146  -3998   4676  -1814       N  
ATOM   3771  CA  ILE B 149     -41.545 -62.293  -2.064  1.00173.30           C  
ANISOU 3771  CA  ILE B 149    22277  16912  26656  -3919   4650  -1730       C  
ATOM   3772  C   ILE B 149     -40.362 -61.399  -2.452  1.00172.46           C  
ANISOU 3772  C   ILE B 149    21939  17006  26582  -3439   4276  -1621       C  
ATOM   3773  O   ILE B 149     -39.277 -61.512  -1.875  1.00172.00           O  
ANISOU 3773  O   ILE B 149    22219  16697  26438  -3165   4063  -1396       O  
ATOM   3774  CB  ILE B 149     -41.781 -62.345  -0.534  1.00178.74           C  
ANISOU 3774  CB  ILE B 149    23464  17344  27103  -4105   4817  -1513       C  
ATOM   3775  N   ASN B 150     -40.576 -60.534  -3.459  1.00165.36           N  
ANISOU 3775  N   ASN B 150    20473  16555  25799  -3345   4196  -1802       N  
ATOM   3776  CA  ASN B 150     -39.565 -59.615  -3.995  1.00161.26           C  
ANISOU 3776  CA  ASN B 150    19687  16278  25308  -2950   3879  -1749       C  
ATOM   3777  C   ASN B 150     -39.526 -58.298  -3.218  1.00162.02           C  
ANISOU 3777  C   ASN B 150    19700  16609  25249  -2834   3820  -1599       C  
ATOM   3778  O   ASN B 150     -40.540 -57.895  -2.644  1.00162.21           O  
ANISOU 3778  O   ASN B 150    19675  16762  25196  -3071   4031  -1630       O  
ATOM   3779  CB  ASN B 150     -39.816 -59.342  -5.486  1.00160.27           C  
ANISOU 3779  CB  ASN B 150    19051  16491  25351  -2924   3821  -2012       C  
ATOM   3780  CG  ASN B 150     -40.118 -60.570  -6.314  1.00185.87           C  
ANISOU 3780  CG  ASN B 150    22301  19566  28755  -3099   3928  -2209       C  
ATOM   3781  OD1 ASN B 150     -39.321 -61.510  -6.408  1.00181.74           O  
ANISOU 3781  OD1 ASN B 150    22052  18714  28287  -2992   3831  -2158       O  
ATOM   3782  ND2 ASN B 150     -41.283 -60.581  -6.941  1.00178.36           N  
ANISOU 3782  ND2 ASN B 150    21038  18843  27886  -3360   4118  -2460       N  
ATOM   3783  N   ASN B 151     -38.355 -57.625  -3.215  1.00155.44           N  
ANISOU 3783  N   ASN B 151    18839  15845  24377  -2477   3540  -1462       N  
ATOM   3784  CA  ASN B 151     -38.142 -56.342  -2.538  1.00152.69           C  
ANISOU 3784  CA  ASN B 151    18416  15715  23885  -2329   3451  -1316       C  
ATOM   3785  C   ASN B 151     -38.927 -55.226  -3.233  1.00153.43           C  
ANISOU 3785  C   ASN B 151    18025  16261  24009  -2378   3479  -1485       C  
ATOM   3786  O   ASN B 151     -38.845 -55.085  -4.456  1.00151.70           O  
ANISOU 3786  O   ASN B 151    17492  16239  23907  -2307   3382  -1657       O  
ATOM   3787  CB  ASN B 151     -36.652 -56.003  -2.472  1.00151.77           C  
ANISOU 3787  CB  ASN B 151    18377  15557  23732  -1952   3151  -1173       C  
ATOM   3788  N   LEU B 152     -39.707 -54.457  -2.452  1.00149.06           N  
ANISOU 3788  N   LEU B 152    17430  15865  23343  -2498   3607  -1448       N  
ATOM   3789  CA  LEU B 152     -40.543 -53.371  -2.964  1.00146.85           C  
ANISOU 3789  CA  LEU B 152    16727  15994  23076  -2529   3621  -1616       C  
ATOM   3790  C   LEU B 152     -39.887 -51.999  -2.837  1.00146.76           C  
ANISOU 3790  C   LEU B 152    16594  16209  22961  -2251   3404  -1493       C  
ATOM   3791  O   LEU B 152     -39.391 -51.644  -1.765  1.00146.00           O  
ANISOU 3791  O   LEU B 152    16731  16013  22730  -2161   3372  -1277       O  
ATOM   3792  CB  LEU B 152     -41.915 -53.378  -2.276  1.00148.95           C  
ANISOU 3792  CB  LEU B 152    16968  16325  23302  -2848   3905  -1723       C  
ATOM   3793  N   ILE B 153     -39.893 -51.232  -3.941  1.00140.59           N  
ANISOU 3793  N   ILE B 153    15469  15722  22229  -2125   3257  -1634       N  
ATOM   3794  CA  ILE B 153     -39.346 -49.879  -4.016  1.00137.37           C  
ANISOU 3794  CA  ILE B 153    14935  15543  21717  -1888   3057  -1552       C  
ATOM   3795  C   ILE B 153     -40.479 -48.904  -4.339  1.00139.94           C  
ANISOU 3795  C   ILE B 153    14950  16194  22026  -1943   3082  -1724       C  
ATOM   3796  O   ILE B 153     -41.068 -48.975  -5.421  1.00139.64           O  
ANISOU 3796  O   ILE B 153    14660  16314  22083  -1993   3069  -1948       O  
ATOM   3797  CB  ILE B 153     -38.183 -49.798  -5.032  1.00138.77           C  
ANISOU 3797  CB  ILE B 153    15047  15750  21930  -1675   2835  -1559       C  
ATOM   3798  N   HIS B 154     -40.790 -48.024  -3.395  1.00135.54           N  
ANISOU 3798  N   HIS B 154    14418  15733  21349  -1928   3112  -1633       N  
ATOM   3799  CA  HIS B 154     -41.911 -47.106  -3.531  1.00134.84           C  
ANISOU 3799  CA  HIS B 154    14056  15943  21236  -1950   3120  -1801       C  
ATOM   3800  C   HIS B 154     -41.417 -45.670  -3.549  1.00135.35           C  
ANISOU 3800  C   HIS B 154    14060  16191  21174  -1695   2894  -1704       C  
ATOM   3801  O   HIS B 154     -40.980 -45.152  -2.526  1.00134.05           O  
ANISOU 3801  O   HIS B 154    14073  15969  20893  -1607   2868  -1496       O  
ATOM   3802  CB  HIS B 154     -42.871 -47.303  -2.360  1.00137.68           C  
ANISOU 3802  CB  HIS B 154    14466  16282  21564  -2175   3365  -1833       C  
ATOM   3803  CG  HIS B 154     -44.204 -46.651  -2.551  1.00141.68           C  
ANISOU 3803  CG  HIS B 154    14646  17096  22088  -2234   3404  -2094       C  
ATOM   3804  ND1 HIS B 154     -44.858 -45.987  -1.537  1.00142.88           N  
ANISOU 3804  ND1 HIS B 154    14751  17405  22130  -2163   3381  -2061       N  
ATOM   3805  CD2 HIS B 154     -45.008 -46.567  -3.636  1.00144.71           C  
ANISOU 3805  CD2 HIS B 154    14738  17656  22591  -2344   3451  -2409       C  
ATOM   3806  CE1 HIS B 154     -46.006 -45.518  -1.989  1.00143.33           C  
ANISOU 3806  CE1 HIS B 154    14487  17726  22246  -2217   3405  -2364       C  
ATOM   3807  NE2 HIS B 154     -46.122 -45.856  -3.261  1.00144.83           N  
ANISOU 3807  NE2 HIS B 154    14515  17942  22571  -2323   3443  -2586       N  
ATOM   3808  N   VAL B 155     -41.483 -45.026  -4.709  1.00130.22           N  
ANISOU 3808  N   VAL B 155    13187  15750  20539  -1584   2728  -1857       N  
ATOM   3809  CA  VAL B 155     -40.983 -43.664  -4.830  1.00127.61           C  
ANISOU 3809  CA  VAL B 155    12823  15586  20077  -1363   2509  -1793       C  
ATOM   3810  C   VAL B 155     -42.090 -42.659  -5.092  1.00131.21           C  
ANISOU 3810  C   VAL B 155    13063  16293  20498  -1333   2465  -1973       C  
ATOM   3811  O   VAL B 155     -42.820 -42.776  -6.072  1.00132.19           O  
ANISOU 3811  O   VAL B 155    12971  16536  20721  -1419   2499  -2227       O  
ATOM   3812  CB  VAL B 155     -39.968 -43.556  -5.978  1.00130.20           C  
ANISOU 3812  CB  VAL B 155    13132  15935  20403  -1251   2331  -1817       C  
ATOM   3813  N   LYS B 156     -42.205 -41.664  -4.220  1.00126.23           N  
ANISOU 3813  N   LYS B 156    12484  15746  19731  -1201   2380  -1861       N  
ATOM   3814  CA  LYS B 156     -43.189 -40.607  -4.406  1.00126.30           C  
ANISOU 3814  CA  LYS B 156    12309  15984  19697  -1128   2305  -2030       C  
ATOM   3815  C   LYS B 156     -42.567 -39.220  -4.519  1.00127.91           C  
ANISOU 3815  C   LYS B 156    12612  16262  19727   -907   2099  -1892       C  
ATOM   3816  O   LYS B 156     -42.838 -38.479  -5.460  1.00127.09           O  
ANISOU 3816  O   LYS B 156    12422  16304  19562   -765   1900  -2014       O  
ATOM   3817  CB  LYS B 156     -44.198 -40.624  -3.260  1.00130.73           C  
ANISOU 3817  CB  LYS B 156    12790  16575  20306  -1298   2528  -2121       C  
ATOM   3818  N   LYS B 157     -41.738 -38.871  -3.543  1.00123.26           N  
ANISOU 3818  N   LYS B 157    12224  15562  19046   -880   2141  -1643       N  
ATOM   3819  CA  LYS B 157     -41.122 -37.553  -3.514  1.00121.27           C  
ANISOU 3819  CA  LYS B 157    12090  15362  18625   -698   1977  -1500       C  
ATOM   3820  C   LYS B 157     -39.605 -37.633  -3.437  1.00123.15           C  
ANISOU 3820  C   LYS B 157    12542  15459  18792   -649   1930  -1278       C  
ATOM   3821  O   LYS B 157     -39.048 -38.338  -2.596  1.00122.70           O  
ANISOU 3821  O   LYS B 157    12608  15243  18769   -720   2056  -1134       O  
ATOM   3822  CB  LYS B 157     -41.659 -36.738  -2.338  1.00124.15           C  
ANISOU 3822  CB  LYS B 157    12462  15777  18933   -695   2058  -1451       C  
ATOM   3823  N   SER B 158     -38.944 -36.891  -4.315  1.00118.32           N  
ANISOU 3823  N   SER B 158    11980  14904  18073   -532   1744  -1272       N  
ATOM   3824  CA  SER B 158     -37.500 -36.797  -4.287  1.00116.63           C  
ANISOU 3824  CA  SER B 158    11930  14605  17780   -492   1689  -1123       C  
ATOM   3825  C   SER B 158     -37.096 -35.336  -4.375  1.00119.17           C  
ANISOU 3825  C   SER B 158    12367  15011  17900   -365   1534  -1054       C  
ATOM   3826  O   SER B 158     -36.496 -34.902  -5.355  1.00118.06           O  
ANISOU 3826  O   SER B 158    12292  14900  17666   -338   1416  -1083       O  
ATOM   3827  CB  SER B 158     -36.904 -37.573  -5.458  1.00120.14           C  
ANISOU 3827  CB  SER B 158    12332  15012  18302   -547   1663  -1224       C  
ATOM   3828  OG  SER B 158     -37.424 -37.101  -6.687  1.00128.41           O  
ANISOU 3828  OG  SER B 158    13309  16185  19297   -512   1523  -1380       O  
ATOM   3829  N   ASP B 159     -37.431 -34.583  -3.335  1.00115.56           N  
ANISOU 3829  N   ASP B 159    11948  14589  17368   -304   1545   -970       N  
ATOM   3830  CA  ASP B 159     -36.978 -33.210  -3.185  1.00114.34           C  
ANISOU 3830  CA  ASP B 159    11923  14499  17023   -189   1414   -897       C  
ATOM   3831  C   ASP B 159     -36.369 -33.083  -1.804  1.00117.00           C  
ANISOU 3831  C   ASP B 159    12381  14779  17294   -171   1487   -703       C  
ATOM   3832  O   ASP B 159     -36.956 -33.531  -0.822  1.00116.99           O  
ANISOU 3832  O   ASP B 159    12345  14760  17344   -192   1599   -654       O  
ATOM   3833  CB  ASP B 159     -38.133 -32.236  -3.367  1.00117.01           C  
ANISOU 3833  CB  ASP B 159    12186  14957  17318    -97   1309  -1022       C  
ATOM   3834  CG  ASP B 159     -38.697 -32.272  -4.767  1.00128.32           C  
ANISOU 3834  CG  ASP B 159    13583  16453  18719    -50   1144  -1196       C  
ATOM   3835  OD1 ASP B 159     -38.454 -33.271  -5.473  1.00129.63           O  
ANISOU 3835  OD1 ASP B 159    13616  16616  19020   -131   1188  -1320       O  
ATOM   3836  OD2 ASP B 159     -39.379 -31.306  -5.164  1.00134.53           O  
ANISOU 3836  OD2 ASP B 159    14494  17284  19338     68    966  -1213       O  
ATOM   3837  N   PHE B 160     -35.189 -32.485  -1.722  1.00112.22           N  
ANISOU 3837  N   PHE B 160    11918  14155  16565   -143   1428   -613       N  
ATOM   3838  CA  PHE B 160     -34.431 -32.551  -0.488  1.00111.06           C  
ANISOU 3838  CA  PHE B 160    11890  13971  16338   -113   1467   -453       C  
ATOM   3839  C   PHE B 160     -35.119 -31.907   0.708  1.00114.67           C  
ANISOU 3839  C   PHE B 160    12369  14446  16756    -65   1518   -355       C  
ATOM   3840  O   PHE B 160     -35.151 -32.495   1.787  1.00114.15           O  
ANISOU 3840  O   PHE B 160    12367  14317  16689    -64   1596   -228       O  
ATOM   3841  CB  PHE B 160     -33.060 -31.910  -0.689  1.00111.87           C  
ANISOU 3841  CB  PHE B 160    12125  14118  16263    -90   1365   -442       C  
ATOM   3842  N   GLU B 161     -35.673 -30.712   0.537  1.00111.24           N  
ANISOU 3842  N   GLU B 161    11883  14098  16284    -17   1463   -428       N  
ATOM   3843  CA  GLU B 161     -36.310 -30.055   1.671  1.00111.00           C  
ANISOU 3843  CA  GLU B 161    11852  14109  16215     27   1507   -372       C  
ATOM   3844  C   GLU B 161     -37.557 -30.771   2.174  1.00115.88           C  
ANISOU 3844  C   GLU B 161    12306  14749  16974    -40   1628   -468       C  
ATOM   3845  O   GLU B 161     -37.711 -31.001   3.370  1.00115.72           O  
ANISOU 3845  O   GLU B 161    12302  14692  16973    -95   1766   -381       O  
ATOM   3846  CB  GLU B 161     -36.636 -28.604   1.328  1.00111.93           C  
ANISOU 3846  CB  GLU B 161    12045  14311  16172    144   1355   -398       C  
ATOM   3847  CG  GLU B 161     -35.423 -27.782   0.930  1.00120.71           C  
ANISOU 3847  CG  GLU B 161    13349  15402  17112    170   1273   -303       C  
ATOM   3848  CD  GLU B 161     -34.338 -27.791   1.988  1.00138.38           C  
ANISOU 3848  CD  GLU B 161    15678  17620  19281    174   1349   -143       C  
ATOM   3849  OE1 GLU B 161     -33.788 -26.714   2.288  1.00132.18           O  
ANISOU 3849  OE1 GLU B 161    14968  16877  18378    243   1309    -99       O  
ATOM   3850  OE2 GLU B 161     -34.030 -28.876   2.518  1.00130.98           O  
ANISOU 3850  OE2 GLU B 161    14741  16620  18403    121   1435    -74       O  
ATOM   3851  N   VAL B 162     -38.434 -31.146   1.252  1.00113.28           N  
ANISOU 3851  N   VAL B 162    11825  14485  16730    -47   1581   -664       N  
ATOM   3852  CA  VAL B 162     -39.644 -31.869   1.616  1.00114.69           C  
ANISOU 3852  CA  VAL B 162    11810  14720  17048   -132   1699   -824       C  
ATOM   3853  C   VAL B 162     -39.316 -33.257   2.138  1.00118.97           C  
ANISOU 3853  C   VAL B 162    12351  15136  17715   -307   1902   -772       C  
ATOM   3854  O   VAL B 162     -39.905 -33.729   3.104  1.00119.64           O  
ANISOU 3854  O   VAL B 162    12399  15212  17845   -418   2073   -779       O  
ATOM   3855  CB  VAL B 162     -40.639 -31.957   0.444  1.00119.63           C  
ANISOU 3855  CB  VAL B 162    12262  15463  17727    -74   1569  -1079       C  
ATOM   3856  CG1 VAL B 162     -41.809 -32.856   0.808  1.00121.41           C  
ANISOU 3856  CG1 VAL B 162    12252  15791  18086   -160   1695  -1292       C  
ATOM   3857  CG2 VAL B 162     -41.138 -30.570   0.072  1.00118.94           C  
ANISOU 3857  CG2 VAL B 162    12253  15451  17485    120   1332  -1112       C  
ATOM   3858  N   PHE B 163     -38.363 -33.905   1.484  1.00114.83           N  
ANISOU 3858  N   PHE B 163    11890  14507  17235   -338   1885   -725       N  
ATOM   3859  CA  PHE B 163     -38.024 -35.273   1.817  1.00115.33           C  
ANISOU 3859  CA  PHE B 163    11998  14414  17410   -477   2043   -671       C  
ATOM   3860  C   PHE B 163     -37.507 -35.335   3.235  1.00118.42           C  
ANISOU 3860  C   PHE B 163    12584  14679  17732   -484   2127   -452       C  
ATOM   3861  O   PHE B 163     -37.825 -36.252   3.984  1.00119.19           O  
ANISOU 3861  O   PHE B 163    12754  14641  17891   -609   2282   -405       O  
ATOM   3862  CB  PHE B 163     -36.965 -35.803   0.858  1.00116.78           C  
ANISOU 3862  CB  PHE B 163    12187  14529  17657   -480   1975   -704       C  
ATOM   3863  N   ASP B 164     -36.707 -34.349   3.605  1.00113.28           N  
ANISOU 3863  N   ASP B 164    12037  14065  16940   -355   2023   -326       N  
ATOM   3864  CA  ASP B 164     -36.134 -34.338   4.933  1.00112.74           C  
ANISOU 3864  CA  ASP B 164    12146  13904  16785   -329   2070   -131       C  
ATOM   3865  C   ASP B 164     -37.250 -34.252   5.957  1.00117.49           C  
ANISOU 3865  C   ASP B 164    12751  14531  17359   -408   2211   -110       C  
ATOM   3866  O   ASP B 164     -37.230 -34.944   6.974  1.00117.82           O  
ANISOU 3866  O   ASP B 164    12947  14443  17378   -473   2324     18       O  
ATOM   3867  CB  ASP B 164     -35.180 -33.156   5.089  1.00112.83           C  
ANISOU 3867  CB  ASP B 164    12236  13981  16654   -185   1925    -45       C  
ATOM   3868  N   ALA B 165     -38.244 -33.421   5.676  1.00114.23           N  
ANISOU 3868  N   ALA B 165    12176  14284  16943   -400   2197   -253       N  
ATOM   3869  CA  ALA B 165     -39.334 -33.252   6.618  1.00115.24           C  
ANISOU 3869  CA  ALA B 165    12248  14485  17054   -483   2332   -301       C  
ATOM   3870  C   ALA B 165     -40.067 -34.569   6.803  1.00121.14           C  
ANISOU 3870  C   ALA B 165    12960  15156  17910   -705   2548   -387       C  
ATOM   3871  O   ALA B 165     -40.376 -34.960   7.925  1.00121.86           O  
ANISOU 3871  O   ALA B 165    13130  15214  17958   -832   2717   -340       O  
ATOM   3872  CB  ALA B 165     -40.290 -32.176   6.134  1.00115.94           C  
ANISOU 3872  CB  ALA B 165    12147  14775  17132   -388   2225   -487       C  
ATOM   3873  N   LEU B 166     -40.319 -35.273   5.707  1.00118.31           N  
ANISOU 3873  N   LEU B 166    12502  14770  17683   -771   2554   -519       N  
ATOM   3874  CA  LEU B 166     -40.982 -36.561   5.806  1.00120.30           C  
ANISOU 3874  CA  LEU B 166    12729  14935  18043  -1003   2764   -620       C  
ATOM   3875  C   LEU B 166     -40.077 -37.490   6.588  1.00124.83           C  
ANISOU 3875  C   LEU B 166    13601  15249  18578  -1087   2866   -397       C  
ATOM   3876  O   LEU B 166     -40.525 -38.226   7.461  1.00126.39           O  
ANISOU 3876  O   LEU B 166    13903  15344  18778  -1299   3079   -399       O  
ATOM   3877  CB  LEU B 166     -41.264 -37.134   4.419  1.00120.64           C  
ANISOU 3877  CB  LEU B 166    12595  15014  18228  -1022   2712   -812       C  
ATOM   3878  N   LYS B 167     -38.788 -37.432   6.281  1.00119.96           N  
ANISOU 3878  N   LYS B 167    13136  14527  17916   -919   2707   -223       N  
ATOM   3879  CA  LYS B 167     -37.798 -38.180   7.032  1.00120.31           C  
ANISOU 3879  CA  LYS B 167    13471  14328  17914   -920   2731    -19       C  
ATOM   3880  C   LYS B 167     -37.784 -37.649   8.450  1.00124.64           C  
ANISOU 3880  C   LYS B 167    14200  14853  18305   -905   2779    149       C  
ATOM   3881  O   LYS B 167     -37.676 -38.401   9.415  1.00125.65           O  
ANISOU 3881  O   LYS B 167    14593  14776  18374   -986   2875    286       O  
ATOM   3882  CB  LYS B 167     -36.420 -38.036   6.394  1.00121.10           C  
ANISOU 3882  CB  LYS B 167    13610  14376  18028   -729   2531     46       C  
ATOM   3883  CG  LYS B 167     -36.110 -39.101   5.357  1.00134.46           C  
ANISOU 3883  CG  LYS B 167    15183  16036  19869   -767   2504    -98       C  
ATOM   3884  CD  LYS B 167     -36.622 -38.704   3.982  1.00142.02           C  
ANISOU 3884  CD  LYS B 167    16102  17029  20828   -591   2306    -98       C  
ATOM   3885  CE  LYS B 167     -36.731 -39.911   3.063  1.00151.55           C  
ANISOU 3885  CE  LYS B 167    17131  18288  22162   -628   2267   -278       C  
ATOM   3886  NZ  LYS B 167     -35.752 -39.860   1.942  1.00161.52           N  
ANISOU 3886  NZ  LYS B 167    18469  19349  23551   -730   2352   -307       N  
ATOM   3887  N   LEU B 168     -37.903 -36.334   8.562  1.00120.15           N  
ANISOU 3887  N   LEU B 168    13507  14486  17659   -802   2707    133       N  
ATOM   3888  CA  LEU B 168     -37.874 -35.670   9.853  1.00120.10           C  
ANISOU 3888  CA  LEU B 168    13627  14502  17503   -783   2747    265       C  
ATOM   3889  C   LEU B 168     -39.036 -36.121  10.724  1.00126.49           C  
ANISOU 3889  C   LEU B 168    14446  15319  18296  -1021   2988    196       C  
ATOM   3890  O   LEU B 168     -38.880 -36.314  11.927  1.00126.91           O  
ANISOU 3890  O   LEU B 168    14709  15291  18221  -1080   3080    337       O  
ATOM   3891  CB  LEU B 168     -37.916 -34.154   9.668  1.00118.22           C  
ANISOU 3891  CB  LEU B 168    13243  14475  17199   -611   2599    239       C  
ATOM   3892  N   ASP B 169     -40.202 -36.289  10.113  1.00124.41           N  
ANISOU 3892  N   ASP B 169    13954  15162  18153  -1167   3093    -40       N  
ATOM   3893  CA  ASP B 169     -41.398 -36.652  10.860  1.00126.75           C  
ANISOU 3893  CA  ASP B 169    14201  15504  18454  -1434   3349   -184       C  
ATOM   3894  C   ASP B 169     -41.210 -37.999  11.535  1.00133.08           C  
ANISOU 3894  C   ASP B 169    15315  16032  19215  -1662   3545    -67       C  
ATOM   3895  O   ASP B 169     -41.605 -38.188  12.682  1.00134.63           O  
ANISOU 3895  O   ASP B 169    15631  16202  19320  -1883   3762    -72       O  
ATOM   3896  CB  ASP B 169     -42.616 -36.695   9.937  1.00129.29           C  
ANISOU 3896  CB  ASP B 169    14177  16017  18931  -1510   3383   -504       C  
ATOM   3897  N   SER B 170     -40.590 -38.934  10.826  1.00129.68           N  
ANISOU 3897  N   SER B 170    15038  15392  18843  -1610   3464     30       N  
ATOM   3898  CA  SER B 170     -40.340 -40.246  11.392  1.00131.80           C  
ANISOU 3898  CA  SER B 170    15657  15350  19070  -1780   3598    155       C  
ATOM   3899  C   SER B 170     -39.398 -40.101  12.570  1.00136.01           C  
ANISOU 3899  C   SER B 170    16556  15708  19412  -1696   3555    429       C  
ATOM   3900  O   SER B 170     -38.489 -39.277  12.543  1.00133.37           O  
ANISOU 3900  O   SER B 170    16218  15425  19030  -1425   3338    552       O  
ATOM   3901  CB  SER B 170     -39.725 -41.177  10.354  1.00134.98           C  
ANISOU 3901  CB  SER B 170    16086  15598  19601  -1694   3480    156       C  
ATOM   3902  OG  SER B 170     -39.075 -42.267  10.983  1.00146.08           O  
ANISOU 3902  OG  SER B 170    17853  16680  20971  -1848   3596    262       O  
ATOM   3903  N   MET B 171     -39.629 -40.899  13.606  1.00135.54           N  
ANISOU 3903  N   MET B 171    16826  15441  19231  -1942   3767    511       N  
ATOM   3904  CA  MET B 171     -38.813 -40.858  14.813  1.00170.06           C  
ANISOU 3904  CA  MET B 171    21612  19611  23393  -1910   3756    764       C  
ATOM   3905  C   MET B 171     -39.205 -39.683  15.700  1.00197.71           C  
ANISOU 3905  C   MET B 171    25013  23329  26778  -1788   3700    819       C  
ATOM   3906  O   MET B 171     -40.315 -39.640  16.227  1.00158.87           O  
ANISOU 3906  O   MET B 171    19859  18641  21863  -1935   3849    659       O  
ATOM   3907  CB  MET B 171     -37.325 -40.785  14.462  1.00172.15           C  
ANISOU 3907  CB  MET B 171    22165  19604  23641  -1667   3526    958       C  
ATOM   3908  N   GLY B 190     -40.683 -31.999  28.302  1.00193.51           N  
ANISOU 3908  N   GLY B 190    25106  24006  24415  -2485   4684   1198       N  
ATOM   3909  CA  GLY B 190     -41.220 -33.355  28.217  1.00196.19           C  
ANISOU 3909  CA  GLY B 190    25693  24123  24728  -2802   4897   1180       C  
ATOM   3910  C   GLY B 190     -42.746 -33.362  28.077  1.00201.89           C  
ANISOU 3910  C   GLY B 190    26107  25054  25549  -3160   5213    824       C  
ATOM   3911  O   GLY B 190     -43.275 -34.097  27.242  1.00202.25           O  
ANISOU 3911  O   GLY B 190    26056  25049  25741  -3295   5298    684       O  
ATOM   3912  N   GLN B 191     -43.446 -32.544  28.890  1.00199.27           N  
ANISOU 3912  N   GLN B 191    25606  24967  25140  -3312   5385    654       N  
ATOM   3913  CA  GLN B 191     -44.904 -32.418  28.881  1.00201.20           C  
ANISOU 3913  CA  GLN B 191    25511  25463  25471  -3643   5684    260       C  
ATOM   3914  C   GLN B 191     -45.312 -30.953  28.726  1.00202.96           C  
ANISOU 3914  C   GLN B 191    25225  26057  25833  -3433   5579     18       C  
ATOM   3915  O   GLN B 191     -44.787 -30.090  29.434  1.00201.34           O  
ANISOU 3915  O   GLN B 191    25070  25918  25510  -3268   5474    145       O  
ATOM   3916  CB  GLN B 191     -45.512 -33.024  30.155  1.00206.67           C  
ANISOU 3916  CB  GLN B 191    26549  26075  25902  -4125   6061    238       C  
ATOM   3917  N   GLU B 192     -46.239 -30.676  27.788  1.00199.22           N  
ANISOU 3917  N   GLU B 192    24274  25816  25604  -3425   5590   -337       N  
ATOM   3918  CA  GLU B 192     -46.731 -29.329  27.491  1.00197.50           C  
ANISOU 3918  CA  GLU B 192    23570  25934  25537  -3201   5460   -608       C  
ATOM   3919  C   GLU B 192     -47.589 -28.752  28.621  1.00203.46           C  
ANISOU 3919  C   GLU B 192    24196  26926  26183  -3448   5713   -852       C  
ATOM   3920  O   GLU B 192     -48.654 -29.295  28.929  1.00206.33           O  
ANISOU 3920  O   GLU B 192    24473  27387  26534  -3846   6040  -1138       O  
ATOM   3921  CB  GLU B 192     -47.481 -29.302  26.149  1.00198.51           C  
ANISOU 3921  CB  GLU B 192    23263  26220  25942  -3110   5378   -928       C  
ATOM   3922  N   MET B 193     -47.100 -27.650  29.237  1.00198.25           N  
ANISOU 3922  N   MET B 193    23522  26364  25440  -3224   5570   -751       N  
ATOM   3923  CA  MET B 193     -47.720 -26.898  30.340  1.00199.74           C  
ANISOU 3923  CA  MET B 193    23587  26784  25520  -3384   5754   -951       C  
ATOM   3924  C   MET B 193     -48.112 -27.791  31.538  1.00207.14           C  
ANISOU 3924  C   MET B 193    24865  27628  26209  -3888   6150   -932       C  
ATOM   3925  O   MET B 193     -49.269 -27.789  31.971  1.00209.78           O  
ANISOU 3925  O   MET B 193    24981  28183  26545  -4226   6452  -1305       O  
ATOM   3926  CB  MET B 193     -48.904 -26.047  29.837  1.00202.75           C  
ANISOU 3926  CB  MET B 193    23385  27527  26125  -3324   5751  -1450       C  
ATOM   3927  N   TYR B 194     -47.134 -28.551  32.067  1.00203.50           N  
ANISOU 3927  N   TYR B 194    24956  26837  25527  -3937   6143   -512       N  
ATOM   3928  CA  TYR B 194     -47.339 -29.452  33.203  1.00206.89           C  
ANISOU 3928  CA  TYR B 194    25833  27103  25672  -4396   6482   -422       C  
ATOM   3929  C   TYR B 194     -46.287 -29.238  34.299  1.00209.99           C  
ANISOU 3929  C   TYR B 194    26678  27327  25783  -4297   6391    -40       C  
ATOM   3930  O   TYR B 194     -45.166 -29.745  34.197  1.00208.07           O  
ANISOU 3930  O   TYR B 194    26822  26784  25452  -4098   6182    337       O  
ATOM   3931  CB  TYR B 194     -47.390 -30.918  32.739  1.00209.85           C  
ANISOU 3931  CB  TYR B 194    26512  27189  26032  -4637   6610   -332       C  
ATOM   3932  N   ALA B 195     -46.654 -28.461  35.336  1.00207.83           N  
ANISOU 3932  N   ALA B 195    26330  27261  25374  -4424   6537   -165       N  
ATOM   3933  CA  ALA B 195     -45.784 -28.136  36.468  1.00207.49           C  
ANISOU 3933  CA  ALA B 195    26668  27112  25055  -4351   6472    142       C  
ATOM   3934  C   ALA B 195     -45.784 -29.256  37.512  1.00215.16           C  
ANISOU 3934  C   ALA B 195    28252  27815  25683  -4782   6754    324       C  
ATOM   3935  O   ALA B 195     -46.826 -29.552  38.104  1.00218.37           O  
ANISOU 3935  O   ALA B 195    28661  28328  25983  -5256   7138     66       O  
ATOM   3936  CB  ALA B 195     -46.212 -26.817  37.098  1.00207.96           C  
ANISOU 3936  CB  ALA B 195    26379  27515  25122  -4306   6510    -88       C  
ATOM   3937  N   PHE B 196     -44.613 -29.893  37.713  1.00211.15           N  
ANISOU 3937  N   PHE B 196    28277  26952  24997  -4618   6557    750       N  
ATOM   3938  CA  PHE B 196     -44.418 -30.994  38.662  1.00214.56           C  
ANISOU 3938  CA  PHE B 196    29399  27052  25074  -4952   6745    989       C  
ATOM   3939  C   PHE B 196     -42.966 -31.091  39.132  1.00217.44           C  
ANISOU 3939  C   PHE B 196    30241  27141  25237  -4610   6421   1430       C  
ATOM   3940  O   PHE B 196     -42.047 -30.835  38.351  1.00213.59           O  
ANISOU 3940  O   PHE B 196    29618  26610  24926  -4150   6058   1577       O  
ATOM   3941  CB  PHE B 196     -44.862 -32.331  38.048  1.00218.57           C  
ANISOU 3941  CB  PHE B 196    30115  27318  25615  -5235   6912    958       C  
ATOM   3942  N   ARG B 197     -42.768 -31.478  40.406  1.00217.49           N  
ANISOU 3942  N   ARG B 197    30811  26963  24861  -4845   6556   1620       N  
ATOM   3943  CA  ARG B 197     -41.448 -31.635  41.021  1.00217.22           C  
ANISOU 3943  CA  ARG B 197    31284  26664  24587  -4549   6261   2014       C  
ATOM   3944  C   ARG B 197     -40.741 -32.895  40.517  1.00222.23           C  
ANISOU 3944  C   ARG B 197    32379  26874  25185  -4429   6078   2276       C  
ATOM   3945  O   ARG B 197     -41.371 -33.948  40.395  1.00225.00           O  
ANISOU 3945  O   ARG B 197    32999  27020  25471  -4793   6319   2235       O  
ATOM   3946  CB  ARG B 197     -41.562 -31.658  42.553  1.00221.94           C  
ANISOU 3946  CB  ARG B 197    32357  27201  24769  -4861   6473   2110       C  
ATOM   3947  N   SER B 198     -39.433 -32.779  40.225  1.00216.37           N  
ANISOU 3947  N   SER B 198    31720  26008  24484  -3923   5655   2522       N  
ATOM   3948  CA  SER B 198     -38.603 -33.879  39.728  1.00216.72           C  
ANISOU 3948  CA  SER B 198    32165  25667  24514  -3718   5413   2759       C  
ATOM   3949  C   SER B 198     -37.674 -34.423  40.816  1.00222.67           C  
ANISOU 3949  C   SER B 198    33641  26086  24880  -3622   5245   3086       C  
ATOM   3950  O   SER B 198     -37.081 -33.646  41.568  1.00221.41           O  
ANISOU 3950  O   SER B 198    33496  26046  24582  -3422   5099   3174       O  
ATOM   3951  CB  SER B 198     -37.795 -33.431  38.513  1.00216.65           C  
ANISOU 3951  CB  SER B 198    31708  25764  24846  -3216   5050   2751       C  
ATOM   3952  OG  SER B 198     -37.092 -34.513  37.924  1.00226.91           O  
ANISOU 3952  OG  SER B 198    33327  26719  26170  -3032   4834   2924       O  
ATOM   3953  N   GLU B 199     -37.550 -35.762  40.889  1.00222.26           N  
ANISOU 3953  N   GLU B 199    34199  25605  24647  -3756   5253   3258       N  
ATOM   3954  CA  GLU B 199     -36.704 -36.457  41.862  1.00223.32           C  
ANISOU 3954  CA  GLU B 199    34749  25550  24551  -3540   4877   3610       C  
ATOM   3955  C   GLU B 199     -35.654 -37.327  41.169  1.00226.28           C  
ANISOU 3955  C   GLU B 199    35268  25654  25054  -3126   4443   3793       C  
ATOM   3956  O   GLU B 199     -35.992 -38.088  40.258  1.00225.95           O  
ANISOU 3956  O   GLU B 199    35186  25471  25193  -3215   4499   3731       O  
ATOM   3957  CB  GLU B 199     -37.559 -37.295  42.825  1.00225.33           C  
ANISOU 3957  CB  GLU B 199    34698  26053  24866  -3750   4774   3774       C  
ATOM   3958  N   GLU B 200     -34.381 -37.205  41.613  1.00224.27           N  
ANISOU 3958  N   GLU B 200    35628  25083  24500  -2775   4229   3961       N  
ATOM   3959  CA  GLU B 200     -33.196 -37.921  41.114  1.00246.56           C  
ANISOU 3959  CA  GLU B 200    36606  28764  28313  -1998   2917   4201       C  
ATOM   3960  C   GLU B 200     -32.976 -37.757  39.609  1.00261.44           C  
ANISOU 3960  C   GLU B 200    37116  31267  30953  -1707   2354   4056       C  
ATOM   3961  O   GLU B 200     -31.937 -37.253  39.189  1.00232.54           O  
ANISOU 3961  O   GLU B 200    36107  26083  26163  -1599   3348   3947       O  
ATOM   3962  CB  GLU B 200     -33.218 -39.407  41.513  1.00248.70           C  
ANISOU 3962  CB  GLU B 200    36717  29006  28773  -1987   2628   4436       C  
ATOM   3963  N   SER B 204     -24.394 -33.609  39.081  1.00150.28           N  
ANISOU 3963  N   SER B 204    24422  16625  16052   1178   1183   3752       N  
ATOM   3964  CA  SER B 204     -23.583 -32.405  39.238  1.00147.70           C  
ANISOU 3964  CA  SER B 204    23692  16654  15772   1421   1035   3625       C  
ATOM   3965  C   SER B 204     -24.025 -31.283  38.282  1.00147.14           C  
ANISOU 3965  C   SER B 204    22942  16952  16012   1285   1243   3443       C  
ATOM   3966  O   SER B 204     -24.314 -31.568  37.116  1.00145.09           O  
ANISOU 3966  O   SER B 204    22436  16682  16011   1231   1304   3357       O  
ATOM   3967  CB  SER B 204     -22.105 -32.725  39.036  1.00151.88           C  
ANISOU 3967  CB  SER B 204    24230  17147  16330   1914    592   3541       C  
ATOM   3968  OG  SER B 204     -21.625 -33.593  40.049  1.00164.85           O  
ANISOU 3968  OG  SER B 204    26509  18474  17654   2094    352   3697       O  
ATOM   3969  N   PRO B 205     -24.084 -30.008  38.744  1.00141.85           N  
ANISOU 3969  N   PRO B 205    21984  16598  15313   1235   1342   3379       N  
ATOM   3970  CA  PRO B 205     -24.503 -28.917  37.843  1.00137.79           C  
ANISOU 3970  CA  PRO B 205    20878  16402  15073   1123   1515   3209       C  
ATOM   3971  C   PRO B 205     -23.411 -28.519  36.842  1.00139.25           C  
ANISOU 3971  C   PRO B 205    20667  16759  15484   1432   1275   3030       C  
ATOM   3972  O   PRO B 205     -22.233 -28.744  37.131  1.00140.01           O  
ANISOU 3972  O   PRO B 205    20876  16826  15496   1751    976   3006       O  
ATOM   3973  CB  PRO B 205     -24.837 -27.761  38.803  1.00138.94           C  
ANISOU 3973  CB  PRO B 205    20931  16786  15075    993   1669   3208       C  
ATOM   3974  CG  PRO B 205     -24.679 -28.309  40.192  1.00146.97           C  
ANISOU 3974  CG  PRO B 205    22498  17606  15739    997   1608   3386       C  
ATOM   3975  CD  PRO B 205     -23.780 -29.488  40.090  1.00144.83           C  
ANISOU 3975  CD  PRO B 205    22578  17047  15404   1282   1295   3455       C  
ATOM   3976  N   PRO B 206     -23.753 -27.930  35.666  1.00132.68           N  
ANISOU 3976  N   PRO B 206    19378  16109  14925   1345   1393   2884       N  
ATOM   3977  CA  PRO B 206     -22.697 -27.552  34.708  1.00130.47           C  
ANISOU 3977  CA  PRO B 206    18748  15991  14834   1598   1189   2702       C  
ATOM   3978  C   PRO B 206     -21.904 -26.312  35.128  1.00132.93           C  
ANISOU 3978  C   PRO B 206    18825  16593  15090   1739   1102   2590       C  
ATOM   3979  O   PRO B 206     -22.459 -25.413  35.761  1.00131.76           O  
ANISOU 3979  O   PRO B 206    18617  16591  14854   1582   1272   2618       O  
ATOM   3980  CB  PRO B 206     -23.465 -27.335  33.406  1.00129.77           C  
ANISOU 3980  CB  PRO B 206    18325  15973  15009   1414   1368   2608       C  
ATOM   3981  CG  PRO B 206     -24.822 -26.919  33.833  1.00134.02           C  
ANISOU 3981  CG  PRO B 206    18872  16546  15502   1097   1668   2676       C  
ATOM   3982  CD  PRO B 206     -25.098 -27.600  35.144  1.00132.72           C  
ANISOU 3982  CD  PRO B 206    19179  16180  15069   1017   1706   2859       C  
ATOM   3983  N   ILE B 207     -20.604 -26.275  34.772  1.00129.34           N  
ANISOU 3983  N   ILE B 207    18229  16229  14687   2029    841   2440       N  
ATOM   3984  CA  ILE B 207     -19.678 -25.180  35.096  1.00128.22           C  
ANISOU 3984  CA  ILE B 207    17855  16366  14497   2177    739   2292       C  
ATOM   3985  C   ILE B 207     -20.033 -23.907  34.312  1.00128.91           C  
ANISOU 3985  C   ILE B 207    17527  16706  14747   2004    928   2163       C  
ATOM   3986  O   ILE B 207     -20.226 -23.965  33.096  1.00126.90           O  
ANISOU 3986  O   ILE B 207    17062  16455  14698   1938    981   2077       O  
ATOM   3987  CB  ILE B 207     -18.187 -25.619  34.936  1.00132.64           C  
ANISOU 3987  CB  ILE B 207    18381  16952  15065   2530    405   2126       C  
ATOM   3988  CG1 ILE B 207     -17.888 -26.886  35.775  1.00136.75           C  
ANISOU 3988  CG1 ILE B 207    19376  17184  15401   2730    184   2264       C  
ATOM   3989  CG2 ILE B 207     -17.213 -24.487  35.311  1.00132.62           C  
ANISOU 3989  CG2 ILE B 207    18130  17258  15003   2661    313   1941       C  
ATOM   3990  CD1 ILE B 207     -16.920 -27.878  35.138  1.00145.84           C  
ANISOU 3990  CD1 ILE B 207    20540  18221  16652   3028   -110   2125       C  
ATOM   3991  N   LEU B 208     -20.137 -22.770  35.032  1.00124.75           N  
ANISOU 3991  N   LEU B 208    16914  16372  14113   1934   1024   2153       N  
ATOM   3992  CA  LEU B 208     -20.481 -21.445  34.507  1.00121.91           C  
ANISOU 3992  CA  LEU B 208    16228  16234  13857   1782   1191   2043       C  
ATOM   3993  C   LEU B 208     -19.468 -20.933  33.464  1.00124.34           C  
ANISOU 3993  C   LEU B 208    16227  16710  14306   1888   1085   1813       C  
ATOM   3994  O   LEU B 208     -18.266 -20.927  33.743  1.00124.77           O  
ANISOU 3994  O   LEU B 208    16247  16863  14297   2094    893   1688       O  
ATOM   3995  CB  LEU B 208     -20.619 -20.436  35.672  1.00122.02           C  
ANISOU 3995  CB  LEU B 208    16267  16401  13695   1729   1272   2074       C  
ATOM   3996  CG  LEU B 208     -20.991 -18.987  35.321  1.00124.31           C  
ANISOU 3996  CG  LEU B 208    16273  16901  14057   1586   1432   1968       C  
ATOM   3997  CD1 LEU B 208     -22.498 -18.799  35.252  1.00123.82           C  
ANISOU 3997  CD1 LEU B 208    16214  16782  14049   1344   1669   2058       C  
ATOM   3998  CD2 LEU B 208     -20.399 -18.019  36.325  1.00126.93           C  
ANISOU 3998  CD2 LEU B 208    16579  17424  14225   1647   1402   1915       C  
ATOM   3999  N   PRO B 209     -19.935 -20.475  32.274  1.00118.89           N  
ANISOU 3999  N   PRO B 209    15315  16063  13795   1743   1208   1736       N  
ATOM   4000  CA  PRO B 209     -18.993 -19.935  31.277  1.00117.46           C  
ANISOU 4000  CA  PRO B 209    14870  16041  13719   1796   1137   1511       C  
ATOM   4001  C   PRO B 209     -18.487 -18.546  31.687  1.00120.56           C  
ANISOU 4001  C   PRO B 209    15120  16670  14018   1775   1172   1391       C  
ATOM   4002  O   PRO B 209     -19.278 -17.747  32.196  1.00119.42           O  
ANISOU 4002  O   PRO B 209    14996  16564  13813   1645   1318   1474       O  
ATOM   4003  CB  PRO B 209     -19.818 -19.884  29.981  1.00117.47           C  
ANISOU 4003  CB  PRO B 209    14750  15983  13900   1626   1269   1502       C  
ATOM   4004  CG  PRO B 209     -21.153 -20.504  30.307  1.00122.40           C  
ANISOU 4004  CG  PRO B 209    15550  16425  14532   1507   1392   1702       C  
ATOM   4005  CD  PRO B 209     -21.324 -20.401  31.782  1.00119.33           C  
ANISOU 4005  CD  PRO B 209    15353  16036  13951   1524   1411   1827       C  
ATOM   4006  N   PRO B 210     -17.183 -18.229  31.496  1.00117.46           N  
ANISOU 4006  N   PRO B 210    14575  16445  13611   1894   1045   1173       N  
ATOM   4007  CA  PRO B 210     -16.684 -16.907  31.923  1.00116.70           C  
ANISOU 4007  CA  PRO B 210    14354  16572  13415   1853   1093   1046       C  
ATOM   4008  C   PRO B 210     -17.105 -15.726  31.039  1.00118.37           C  
ANISOU 4008  C   PRO B 210    14420  16860  13695   1641   1264    971       C  
ATOM   4009  O   PRO B 210     -16.825 -14.578  31.393  1.00117.39           O  
ANISOU 4009  O   PRO B 210    14228  16893  13483   1580   1325    882       O  
ATOM   4010  CB  PRO B 210     -15.166 -17.096  31.968  1.00119.83           C  
ANISOU 4010  CB  PRO B 210    14630  17120  13779   2041    903    805       C  
ATOM   4011  CG  PRO B 210     -14.890 -18.174  30.996  1.00124.71           C  
ANISOU 4011  CG  PRO B 210    15213  17629  14541   2117    802    742       C  
ATOM   4012  CD  PRO B 210     -16.102 -19.060  30.926  1.00120.13           C  
ANISOU 4012  CD  PRO B 210    14837  16788  14021   2066    858   1005       C  
ATOM   4013  N   HIS B 211     -17.798 -16.000  29.914  1.00113.90           N  
ANISOU 4013  N   HIS B 211    13831  16172  13273   1533   1334   1008       N  
ATOM   4014  CA  HIS B 211     -18.288 -14.984  28.976  1.00112.04           C  
ANISOU 4014  CA  HIS B 211    13510  15963  13096   1350   1467    951       C  
ATOM   4015  C   HIS B 211     -19.462 -14.183  29.543  1.00115.11           C  
ANISOU 4015  C   HIS B 211    13972  16326  13438   1249   1599   1088       C  
ATOM   4016  O   HIS B 211     -19.722 -13.069  29.086  1.00113.51           O  
ANISOU 4016  O   HIS B 211    13727  16170  13231   1133   1683   1023       O  
ATOM   4017  CB  HIS B 211     -18.652 -15.620  27.626  1.00112.18           C  
ANISOU 4017  CB  HIS B 211    13493  15857  13273   1292   1473    942       C  
ATOM   4018  CG  HIS B 211     -17.493 -16.298  26.972  1.00116.30           C  
ANISOU 4018  CG  HIS B 211    13915  16424  13850   1376   1355    768       C  
ATOM   4019  ND1 HIS B 211     -16.506 -15.574  26.329  1.00117.85           N  
ANISOU 4019  ND1 HIS B 211    13973  16780  14023   1307   1362    528       N  
ATOM   4020  CD2 HIS B 211     -17.178 -17.612  26.918  1.00119.21           C  
ANISOU 4020  CD2 HIS B 211    14308  16700  14287   1517   1231    781       C  
ATOM   4021  CE1 HIS B 211     -15.630 -16.466  25.901  1.00118.26           C  
ANISOU 4021  CE1 HIS B 211    13937  16856  14142   1411   1245    385       C  
ATOM   4022  NE2 HIS B 211     -15.995 -17.707  26.227  1.00119.43           N  
ANISOU 4022  NE2 HIS B 211    14181  16846  14350   1555   1150    534       N  
ATOM   4023  N   LEU B 212     -20.160 -14.751  30.541  1.00112.61           N  
ANISOU 4023  N   LEU B 212    13780  15929  13076   1289   1615   1261       N  
ATOM   4024  CA  LEU B 212     -21.289 -14.117  31.218  1.00112.22           C  
ANISOU 4024  CA  LEU B 212    13784  15873  12982   1196   1743   1366       C  
ATOM   4025  C   LEU B 212     -20.812 -13.171  32.320  1.00116.70           C  
ANISOU 4025  C   LEU B 212    14356  16595  13390   1219   1755   1329       C  
ATOM   4026  O   LEU B 212     -21.472 -12.164  32.572  1.00115.62           O  
ANISOU 4026  O   LEU B 212    14200  16504  13225   1131   1858   1326       O  
ATOM   4027  CB  LEU B 212     -22.233 -15.175  31.810  1.00113.36           C  
ANISOU 4027  CB  LEU B 212    14067  15872  13131   1185   1785   1544       C  
ATOM   4028  CG  LEU B 212     -23.051 -16.009  30.823  1.00117.75           C  
ANISOU 4028  CG  LEU B 212    14619  16273  13848   1121   1819   1588       C  
ATOM   4029  CD1 LEU B 212     -23.508 -17.299  31.463  1.00119.60           C  
ANISOU 4029  CD1 LEU B 212    15031  16356  14055   1128   1826   1739       C  
ATOM   4030  CD2 LEU B 212     -24.251 -15.236  30.303  1.00119.09           C  
ANISOU 4030  CD2 LEU B 212    14702  16445  14102    992   1944   1562       C  
ATOM   4031  N   LEU B 213     -19.669 -13.498  32.973  1.00114.65           N  
ANISOU 4031  N   LEU B 213    14116  16418  13028   1352   1636   1282       N  
ATOM   4032  CA  LEU B 213     -19.060 -12.719  34.063  1.00115.13           C  
ANISOU 4032  CA  LEU B 213    14175  16641  12928   1395   1623   1227       C  
ATOM   4033  C   LEU B 213     -18.752 -11.271  33.675  1.00117.99           C  
ANISOU 4033  C   LEU B 213    14411  17143  13275   1295   1697   1066       C  
ATOM   4034  O   LEU B 213     -18.925 -10.374  34.503  1.00117.54           O  
ANISOU 4034  O   LEU B 213    14367  17179  13113   1259   1763   1066       O  
ATOM   4035  CB  LEU B 213     -17.805 -13.414  34.624  1.00116.83           C  
ANISOU 4035  CB  LEU B 213    14412  16922  13054   1585   1443   1160       C  
ATOM   4036  N   GLN B 214     -18.314 -11.044  32.420  1.00113.86           N  
ANISOU 4036  N   GLN B 214    13790  16625  12845   1236   1692    927       N  
ATOM   4037  CA  GLN B 214     -18.041  -9.703  31.898  1.00112.85           C  
ANISOU 4037  CA  GLN B 214    13600  16588  12690   1107   1771    776       C  
ATOM   4038  C   GLN B 214     -19.367  -9.030  31.526  1.00115.85           C  
ANISOU 4038  C   GLN B 214    14042  16854  13123    997   1880    869       C  
ATOM   4039  O   GLN B 214     -20.117  -9.552  30.698  1.00114.87           O  
ANISOU 4039  O   GLN B 214    13935  16591  13120    972   1885    939       O  
ATOM   4040  CB  GLN B 214     -17.033  -9.717  30.723  1.00114.04           C  
ANISOU 4040  CB  GLN B 214    13653  16788  12888   1058   1737    574       C  
ATOM   4041  CG  GLN B 214     -17.269 -10.789  29.649  1.00128.32           C  
ANISOU 4041  CG  GLN B 214    15452  18461  14844   1074   1689    611       C  
ATOM   4042  CD  GLN B 214     -16.494 -10.557  28.370  1.00146.68           C  
ANISOU 4042  CD  GLN B 214    17696  20830  17207    966   1699    405       C  
ATOM   4043  OE1 GLN B 214     -15.384 -10.010  28.357  1.00142.63           O  
ANISOU 4043  OE1 GLN B 214    17097  20482  16615    918   1705    189       O  
ATOM   4044  NE2 GLN B 214     -17.054 -11.009  27.258  1.00137.96           N  
ANISOU 4044  NE2 GLN B 214    16614  19586  16220    911   1709    451       N  
ATOM   4045  N   VAL B 215     -19.684  -7.911  32.195  1.00112.48           N  
ANISOU 4045  N   VAL B 215    13643  16488  12606    948   1953    861       N  
ATOM   4046  CA  VAL B 215     -20.932  -7.168  31.989  1.00111.70           C  
ANISOU 4046  CA  VAL B 215    13595  16297  12548    879   2032    915       C  
ATOM   4047  C   VAL B 215     -20.659  -5.907  31.167  1.00115.17           C  
ANISOU 4047  C   VAL B 215    14071  16734  12954    773   2063    775       C  
ATOM   4048  O   VAL B 215     -19.692  -5.193  31.444  1.00115.04           O  
ANISOU 4048  O   VAL B 215    14047  16838  12827    729   2080    651       O  
ATOM   4049  CB  VAL B 215     -21.653  -6.844  33.331  1.00116.16           C  
ANISOU 4049  CB  VAL B 215    14183  16911  13041    902   2092   1000       C  
ATOM   4050  CG1 VAL B 215     -23.067  -6.317  33.095  1.00115.60           C  
ANISOU 4050  CG1 VAL B 215    14131  16748  13045    859   2155   1029       C  
ATOM   4051  CG2 VAL B 215     -21.688  -8.059  34.257  1.00116.98           C  
ANISOU 4051  CG2 VAL B 215    14310  17016  13120    981   2066   1131       C  
ATOM   4052  N   ILE B 216     -21.519  -5.636  30.163  1.00111.26           N  
ANISOU 4052  N   ILE B 216    13634  16096  12543    728   2068    788       N  
ATOM   4053  CA  ILE B 216     -21.422  -4.460  29.287  1.00110.84           C  
ANISOU 4053  CA  ILE B 216    13691  15983  12442    626   2083    677       C  
ATOM   4054  C   ILE B 216     -21.716  -3.155  30.044  1.00115.01           C  
ANISOU 4054  C   ILE B 216    14289  16542  12868    610   2130    642       C  
ATOM   4055  O   ILE B 216     -21.220  -2.098  29.649  1.00114.66           O  
ANISOU 4055  O   ILE B 216    14359  16482  12725    511   2154    530       O  
ATOM   4056  CB  ILE B 216     -22.263  -4.593  27.986  1.00113.53           C  
ANISOU 4056  CB  ILE B 216    14103  16148  12887    610   2041    700       C  
ATOM   4057  CG1 ILE B 216     -23.729  -5.005  28.276  1.00113.99           C  
ANISOU 4057  CG1 ILE B 216    14116  16135  13061    705   2028    808       C  
ATOM   4058  CG2 ILE B 216     -21.583  -5.544  26.991  1.00114.09           C  
ANISOU 4058  CG2 ILE B 216    14132  16198  13017    573   2008    671       C  
ATOM   4059  CD1 ILE B 216     -24.743  -4.542  27.241  1.00121.44           C  
ANISOU 4059  CD1 ILE B 216    15148  16923  14070    713   1974    783       C  
ATOM   4060  N   LEU B 217     -22.504  -3.239  31.136  1.00111.93           N  
ANISOU 4060  N   LEU B 217    13843  16194  12493    691   2152    726       N  
ATOM   4061  CA  LEU B 217     -22.849  -2.095  31.985  1.00112.18           C  
ANISOU 4061  CA  LEU B 217    13914  16270  12441    691   2197    687       C  
ATOM   4062  C   LEU B 217     -21.730  -1.758  32.977  1.00116.81           C  
ANISOU 4062  C   LEU B 217    14466  17030  12889    664   2239    629       C  
ATOM   4063  O   LEU B 217     -21.664  -0.624  33.457  1.00116.67           O  
ANISOU 4063  O   LEU B 217    14503  17050  12777    629   2281    556       O  
ATOM   4064  CB  LEU B 217     -24.187  -2.320  32.703  1.00112.52           C  
ANISOU 4064  CB  LEU B 217    13894  16302  12556    767   2217    766       C  
ATOM   4065  CG  LEU B 217     -25.432  -2.162  31.831  1.00117.05           C  
ANISOU 4065  CG  LEU B 217    14497  16726  13250    803   2172    752       C  
ATOM   4066  CD1 LEU B 217     -26.526  -3.094  32.276  1.00117.58           C  
ANISOU 4066  CD1 LEU B 217    14443  16805  13427    848   2201    824       C  
ATOM   4067  CD2 LEU B 217     -25.922  -0.724  31.816  1.00119.76           C  
ANISOU 4067  CD2 LEU B 217    14942  17014  13546    821   2152    649       C  
ATOM   4068  N   ASN B 218     -20.847  -2.735  33.268  1.00113.89           N  
ANISOU 4068  N   ASN B 218    14006  16761  12505    694   2215    645       N  
ATOM   4069  CA  ASN B 218     -19.687  -2.557  34.144  1.00114.51           C  
ANISOU 4069  CA  ASN B 218    14030  17021  12456    694   2225    561       C  
ATOM   4070  C   ASN B 218     -18.526  -1.939  33.358  1.00118.81           C  
ANISOU 4070  C   ASN B 218    14593  17612  12938    575   2240    375       C  
ATOM   4071  O   ASN B 218     -17.696  -1.238  33.942  1.00118.89           O  
ANISOU 4071  O   ASN B 218    14580  17764  12827    525   2280    246       O  
ATOM   4072  CB  ASN B 218     -19.261  -3.888  34.771  1.00115.88           C  
ANISOU 4072  CB  ASN B 218    14122  17271  12638    807   2158    638       C  
ATOM   4073  CG  ASN B 218     -20.057  -4.303  35.988  1.00138.59           C  
ANISOU 4073  CG  ASN B 218    17009  20161  15487    883   2174    786       C  
ATOM   4074  OD1 ASN B 218     -20.578  -3.479  36.750  1.00132.82           O  
ANISOU 4074  OD1 ASN B 218    16298  19474  14693    859   2242    787       O  
ATOM   4075  ND2 ASN B 218     -20.120  -5.603  36.231  1.00130.89           N  
ANISOU 4075  ND2 ASN B 218    16038  19149  14546    966   2117    903       N  
ATOM   4076  N   LYS B 219     -18.480  -2.203  32.033  1.00115.31           N  
ANISOU 4076  N   LYS B 219    14191  17054  12566    511   2221    346       N  
ATOM   4077  CA  LYS B 219     -17.476  -1.694  31.095  1.00115.51           C  
ANISOU 4077  CA  LYS B 219    14258  17101  12530    354   2258    160       C  
ATOM   4078  C   LYS B 219     -17.632  -0.184  30.919  1.00120.04           C  
ANISOU 4078  C   LYS B 219    15011  17605  12995    216   2336     82       C  
ATOM   4079  O   LYS B 219     -18.754   0.305  30.759  1.00119.24           O  
ANISOU 4079  O   LYS B 219    15037  17344  12926    249   2322    182       O  
ATOM   4080  CB  LYS B 219     -17.611  -2.394  29.730  1.00117.54           C  
ANISOU 4080  CB  LYS B 219    14543  17228  12890    319   2220    175       C  
ATOM   4081  N   ASP B 220     -16.508   0.551  30.957  1.00117.79           N  
ANISOU 4081  N   ASP B 220    14738  17438  12577     65   2413   -116       N  
ATOM   4082  CA  ASP B 220     -16.498   2.006  30.806  1.00118.25           C  
ANISOU 4082  CA  ASP B 220    15004  17422  12504    -94   2498   -210       C  
ATOM   4083  C   ASP B 220     -16.125   2.421  29.387  1.00122.67           C  
ANISOU 4083  C   ASP B 220    15758  17848  13003   -305   2547   -321       C  
ATOM   4084  O   ASP B 220     -15.160   1.899  28.824  1.00122.61           O  
ANISOU 4084  O   ASP B 220    15654  17943  12988   -411   2578   -461       O  
ATOM   4085  CB  ASP B 220     -15.562   2.662  31.835  1.00121.00           C  
ANISOU 4085  CB  ASP B 220    15270  17981  12723   -158   2576   -368       C  
ATOM   4086  CG  ASP B 220     -15.982   2.444  33.275  1.00131.13           C  
ANISOU 4086  CG  ASP B 220    16417  19378  14027     30   2535   -257       C  
ATOM   4087  OD1 ASP B 220     -17.033   2.992  33.678  1.00131.31           O  
ANISOU 4087  OD1 ASP B 220    16538  19289  14063     95   2530   -138       O  
ATOM   4088  OD2 ASP B 220     -15.251   1.742  34.006  1.00137.59           O  
ANISOU 4088  OD2 ASP B 220    17039  20401  14840    113   2503   -306       O  
ATOM   4089  N   THR B 221     -16.903   3.354  28.812  1.00119.46           N  
ANISOU 4089  N   THR B 221    15636  17209  12546   -362   2546   -271       N  
ATOM   4090  CA  THR B 221     -16.697   3.882  27.458  1.00119.94           C  
ANISOU 4090  CA  THR B 221    15972  17090  12509   -571   2584   -352       C  
ATOM   4091  C   THR B 221     -15.926   5.211  27.490  1.00125.17           C  
ANISOU 4091  C   THR B 221    16853  17747  12960   -821   2719   -535       C  
ATOM   4092  O   THR B 221     -15.695   5.760  28.571  1.00125.06           O  
ANISOU 4092  O   THR B 221    16766  17857  12893   -803   2767   -584       O  
ATOM   4093  CB  THR B 221     -18.035   3.989  26.700  1.00127.72           C  
ANISOU 4093  CB  THR B 221    17173  17797  13559   -459   2466   -189       C  
ATOM   4094  OG1 THR B 221     -18.970   4.743  27.474  1.00127.37           O  
ANISOU 4094  OG1 THR B 221    17208  17672  13517   -316   2415   -109       O  
ATOM   4095  CG2 THR B 221     -18.619   2.629  26.340  1.00125.29           C  
ANISOU 4095  CG2 THR B 221    16674  17489  13443   -292   2366    -57       C  
ATOM   4096  N   ASN B 222     -15.521   5.715  26.303  1.00122.64           N  
ANISOU 4096  N   ASN B 222    16814  17279  12505  -1072   2788   -641       N  
ATOM   4097  CA  ASN B 222     -14.782   6.970  26.137  1.00124.03           C  
ANISOU 4097  CA  ASN B 222    17265  17408  12452  -1369   2939   -826       C  
ATOM   4098  C   ASN B 222     -15.571   8.187  26.625  1.00128.24           C  
ANISOU 4098  C   ASN B 222    18079  17744  12901  -1307   2903   -746       C  
ATOM   4099  O   ASN B 222     -16.800   8.199  26.549  1.00127.18           O  
ANISOU 4099  O   ASN B 222    18049  17418  12857  -1081   2749   -562       O  
ATOM   4100  CB  ASN B 222     -14.357   7.158  24.680  1.00125.99           C  
ANISOU 4100  CB  ASN B 222    17808  17498  12565  -1654   3013   -927       C  
ATOM   4101  CG  ASN B 222     -13.041   6.505  24.341  1.00150.43           C  
ANISOU 4101  CG  ASN B 222    20664  20848  15645  -1868   3148  -1162       C  
ATOM   4102  OD1 ASN B 222     -11.991   7.155  24.304  1.00146.86           O  
ANISOU 4102  OD1 ASN B 222    20277  20501  15020  -2174   3330  -1412       O  
ATOM   4103  ND2 ASN B 222     -13.064   5.207  24.075  1.00141.28           N  
ANISOU 4103  ND2 ASN B 222    19218  19798  14665  -1717   3063  -1112       N  
ATOM   4104  N   ILE B 223     -14.855   9.203  27.136  1.00126.02           N  
ANISOU 4104  N   ILE B 223    17904  17523  12454  -1504   3043   -910       N  
ATOM   4105  CA  ILE B 223     -15.440  10.448  27.651  1.00126.57           C  
ANISOU 4105  CA  ILE B 223    18248  17416  12425  -1471   3026   -874       C  
ATOM   4106  C   ILE B 223     -16.006  11.295  26.492  1.00131.44           C  
ANISOU 4106  C   ILE B 223    19408  17638  12895  -1575   2973   -827       C  
ATOM   4107  O   ILE B 223     -16.988  12.014  26.682  1.00131.22           O  
ANISOU 4107  O   ILE B 223    19612  17387  12860  -1405   2849   -722       O  
ATOM   4108  CB  ILE B 223     -14.426  11.240  28.538  1.00130.85           C  
ANISOU 4108  CB  ILE B 223    18738  18150  12827  -1671   3203  -1082       C  
ATOM   4109  CG1 ILE B 223     -14.080  10.474  29.840  1.00130.56           C  
ANISOU 4109  CG1 ILE B 223    18186  18517  12903  -1601   3248  -1176       C  
ATOM   4110  CG2 ILE B 223     -14.944  12.650  28.863  1.00132.03           C  
ANISOU 4110  CG2 ILE B 223    19065  18168  12930  -1557   3162  -1025       C  
ATOM   4111  CD1 ILE B 223     -12.905  11.046  30.636  1.00139.73           C  
ANISOU 4111  CD1 ILE B 223    19261  19916  13913  -1907   3453  -1483       C  
ATOM   4112  N   SER B 224     -15.401  11.176  25.293  1.00128.86           N  
ANISOU 4112  N   SER B 224    19284  17227  12449  -1841   3054   -914       N  
ATOM   4113  CA  SER B 224     -15.792  11.898  24.081  1.00130.16           C  
ANISOU 4113  CA  SER B 224    20010  17012  12434  -1978   3010   -879       C  
ATOM   4114  C   SER B 224     -17.139  11.471  23.493  1.00132.91           C  
ANISOU 4114  C   SER B 224    20451  17132  12916  -1665   2759   -660       C  
ATOM   4115  O   SER B 224     -17.887  12.331  23.024  1.00133.71           O  
ANISOU 4115  O   SER B 224    21005  16896  12903  -1609   2634   -593       O  
ATOM   4116  CB  SER B 224     -14.697  11.806  23.023  1.00135.19           C  
ANISOU 4116  CB  SER B 224    20806  17665  12897  -2382   3194  -1055       C  
ATOM   4117  OG  SER B 224     -14.431  10.460  22.662  1.00142.96           O  
ANISOU 4117  OG  SER B 224    21407  18859  14052  -2326   3182  -1054       O  
ATOM   4118  N   CYS B 225     -17.441  10.156  23.498  1.00127.37           N  
ANISOU 4118  N   CYS B 225    19341  16605  12450  -1462   2677   -566       N  
ATOM   4119  CA  CYS B 225     -18.690   9.623  22.943  1.00126.28           C  
ANISOU 4119  CA  CYS B 225    19230  16293  12457  -1178   2454   -388       C  
ATOM   4120  C   CYS B 225     -19.894   9.789  23.887  1.00128.70           C  
ANISOU 4120  C   CYS B 225    19400  16579  12921   -820   2291   -271       C  
ATOM   4121  O   CYS B 225     -19.719  10.033  25.083  1.00127.87           O  
ANISOU 4121  O   CYS B 225    19082  16651  12851   -771   2357   -305       O  
ATOM   4122  CB  CYS B 225     -18.519   8.176  22.483  1.00125.25           C  
ANISOU 4122  CB  CYS B 225    18758  16333  12497  -1141   2448   -351       C  
ATOM   4123  SG  CYS B 225     -18.107   7.012  23.808  1.00127.30           S  
ANISOU 4123  SG  CYS B 225    18374  17008  12987   -992   2509   -350       S  
ATOM   4124  N   ASP B 226     -21.115   9.673  23.318  1.00124.73           N  
ANISOU 4124  N   ASP B 226    19023  15866  12505   -579   2077   -159       N  
ATOM   4125  CA  ASP B 226     -22.420   9.802  23.977  1.00124.00           C  
ANISOU 4125  CA  ASP B 226    18817  15731  12567   -234   1900    -85       C  
ATOM   4126  C   ASP B 226     -22.578   8.862  25.192  1.00125.52           C  
ANISOU 4126  C   ASP B 226    18459  16249  12983    -78   1949    -40       C  
ATOM   4127  O   ASP B 226     -22.163   7.703  25.106  1.00123.80           O  
ANISOU 4127  O   ASP B 226    17948  16217  12874   -117   2014     -6       O  
ATOM   4128  CB  ASP B 226     -23.536   9.550  22.948  1.00126.17           C  
ANISOU 4128  CB  ASP B 226    19253  15777  12909    -33   1673    -13       C  
ATOM   4129  CG  ASP B 226     -24.917   9.958  23.405  1.00136.47           C  
ANISOU 4129  CG  ASP B 226    20537  16984  14331    307   1467      0       C  
ATOM   4130  OD1 ASP B 226     -25.654   9.087  23.907  1.00135.68           O  
ANISOU 4130  OD1 ASP B 226    20031  17059  14461    513   1420     43       O  
ATOM   4131  OD2 ASP B 226     -25.261  11.150  23.263  1.00144.25           O  
ANISOU 4131  OD2 ASP B 226    21920  17716  15172    362   1354    -49       O  
ATOM   4132  N   PRO B 227     -23.164   9.333  26.326  1.00121.73           N  
ANISOU 4132  N   PRO B 227    17855  15833  12565     93   1920    -47       N  
ATOM   4133  CA  PRO B 227     -23.305   8.455  27.504  1.00120.00           C  
ANISOU 4133  CA  PRO B 227    17163  15910  12523    212   1978     -1       C  
ATOM   4134  C   PRO B 227     -24.318   7.324  27.332  1.00122.41           C  
ANISOU 4134  C   PRO B 227    17211  16253  13045    421   1869     93       C  
ATOM   4135  O   PRO B 227     -24.089   6.230  27.851  1.00120.87           O  
ANISOU 4135  O   PRO B 227    16683  16278  12966    429   1943    150       O  
ATOM   4136  CB  PRO B 227     -23.717   9.416  28.630  1.00122.45           C  
ANISOU 4136  CB  PRO B 227    17475  16242  12809    313   1976    -54       C  
ATOM   4137  CG  PRO B 227     -23.511  10.794  28.085  1.00128.62           C  
ANISOU 4137  CG  PRO B 227    18728  16756  13385    208   1945   -135       C  
ATOM   4138  CD  PRO B 227     -23.692  10.680  26.612  1.00124.73           C  
ANISOU 4138  CD  PRO B 227    18532  16018  12843    177   1835   -104       C  
ATOM   4139  N   ALA B 228     -25.423   7.577  26.599  1.00119.19           N  
ANISOU 4139  N   ALA B 228    16972  15630  12685    589   1688     96       N  
ATOM   4140  CA  ALA B 228     -26.474   6.586  26.340  1.00118.22           C  
ANISOU 4140  CA  ALA B 228    16620  15533  12765    779   1580    150       C  
ATOM   4141  C   ALA B 228     -26.019   5.481  25.373  1.00120.57           C  
ANISOU 4141  C   ALA B 228    16864  15843  13106    675   1604    217       C  
ATOM   4142  O   ALA B 228     -26.664   4.435  25.298  1.00119.29           O  
ANISOU 4142  O   ALA B 228    16452  15754  13117    786   1566    269       O  
ATOM   4143  CB  ALA B 228     -27.728   7.271  25.816  1.00120.36           C  
ANISOU 4143  CB  ALA B 228    17088  15580  13063   1000   1361     89       C  
ATOM   4144  N   LEU B 229     -24.908   5.709  24.648  1.00117.08           N  
ANISOU 4144  N   LEU B 229    16648  15335  12501    447   1680    198       N  
ATOM   4145  CA  LEU B 229     -24.333   4.753  23.704  1.00116.12           C  
ANISOU 4145  CA  LEU B 229    16489  15231  12399    320   1716    230       C  
ATOM   4146  C   LEU B 229     -23.478   3.708  24.427  1.00118.50           C  
ANISOU 4146  C   LEU B 229    16430  15811  12782    242   1865    254       C  
ATOM   4147  O   LEU B 229     -22.724   4.051  25.340  1.00117.95           O  
ANISOU 4147  O   LEU B 229    16285  15890  12641    158   1981    208       O  
ATOM   4148  CB  LEU B 229     -23.501   5.492  22.641  1.00117.22           C  
ANISOU 4148  CB  LEU B 229    17035  15191  12312     82   1749    164       C  
ATOM   4149  CG  LEU B 229     -24.267   6.427  21.704  1.00122.69           C  
ANISOU 4149  CG  LEU B 229    18027  15627  12965    111   1596    183       C  
ATOM   4150  CD1 LEU B 229     -23.323   7.208  20.798  1.00124.36           C  
ANISOU 4150  CD1 LEU B 229    18552  15584  13115    303   1401    169       C  
ATOM   4151  CD2 LEU B 229     -25.237   5.647  20.847  1.00125.91           C  
ANISOU 4151  CD2 LEU B 229    18737  15941  13164   -197   1698    123       C  
ATOM   4152  N   LEU B 230     -23.602   2.434  24.010  1.00114.14           N  
ANISOU 4152  N   LEU B 230    15670  15323  12376    283   1848    316       N  
ATOM   4153  CA  LEU B 230     -22.874   1.293  24.575  1.00112.99           C  
ANISOU 4153  CA  LEU B 230    15210  15405  12317    249   1946    343       C  
ATOM   4154  C   LEU B 230     -22.105   0.505  23.491  1.00116.70           C  
ANISOU 4154  C   LEU B 230    15677  15874  12789    113   1971    315       C  
ATOM   4155  O   LEU B 230     -22.484   0.591  22.320  1.00116.56           O  
ANISOU 4155  O   LEU B 230    15855  15679  12754     87   1897    315       O  
ATOM   4156  CB  LEU B 230     -23.856   0.347  25.299  1.00112.39           C  
ANISOU 4156  CB  LEU B 230    14856  15413  12433    446   1904    446       C  
ATOM   4157  CG  LEU B 230     -24.283   0.706  26.725  1.00117.19           C  
ANISOU 4157  CG  LEU B 230    15338  16134  13053    546   1938    463       C  
ATOM   4158  CD1 LEU B 230     -25.353  -0.250  27.208  1.00117.06           C  
ANISOU 4158  CD1 LEU B 230    15096  16172  13212    694   1911    545       C  
ATOM   4159  CD2 LEU B 230     -23.105   0.663  27.698  1.00119.47           C  
ANISOU 4159  CD2 LEU B 230    15517  16620  13257    457   2054    436       C  
ATOM   4160  N   PRO B 231     -21.048  -0.284  23.834  1.00112.97           N  
ANISOU 4160  N   PRO B 231    14990  15597  12338     40   2059    277       N  
ATOM   4161  CA  PRO B 231     -20.356  -1.062  22.788  1.00112.75           C  
ANISOU 4161  CA  PRO B 231    14935  15579  12328    -78   2077    222       C  
ATOM   4162  C   PRO B 231     -21.158  -2.296  22.364  1.00116.05           C  
ANISOU 4162  C   PRO B 231    15205  15952  12936     67   1989    335       C  
ATOM   4163  O   PRO B 231     -22.076  -2.699  23.082  1.00115.09           O  
ANISOU 4163  O   PRO B 231    14949  15844  12936    242   1942    445       O  
ATOM   4164  CB  PRO B 231     -19.031  -1.441  23.451  1.00114.62           C  
ANISOU 4164  CB  PRO B 231    14965  16051  12533   -157   2175    112       C  
ATOM   4165  CG  PRO B 231     -19.342  -1.507  24.899  1.00118.74           C  
ANISOU 4165  CG  PRO B 231    15323  16689  13103      5   2167    192       C  
ATOM   4166  CD  PRO B 231     -20.448  -0.523  25.166  1.00114.36           C  
ANISOU 4166  CD  PRO B 231    14940  15992  12520     78   2127    266       C  
ATOM   4167  N   GLU B 232     -20.811  -2.895  21.201  1.00112.90           N  
ANISOU 4167  N   GLU B 232    14832  15506  12558    -27   1981    293       N  
ATOM   4168  CA  GLU B 232     -21.491  -4.076  20.656  1.00112.24           C  
ANISOU 4168  CA  GLU B 232    14622  15374  12650     83   1905    381       C  
ATOM   4169  C   GLU B 232     -21.363  -5.292  21.591  1.00115.69           C  
ANISOU 4169  C   GLU B 232    14762  15962  13232    209   1915    447       C  
ATOM   4170  O   GLU B 232     -20.242  -5.714  21.891  1.00115.42           O  
ANISOU 4170  O   GLU B 232    14603  16076  13177    157   1965    366       O  
ATOM   4171  CB  GLU B 232     -20.992  -4.407  19.241  1.00113.89           C  
ANISOU 4171  CB  GLU B 232    14926  15517  12830    -66   1908    300       C  
ATOM   4172  N   PRO B 233     -22.491  -5.843  22.095  1.00111.97           N  
ANISOU 4172  N   PRO B 233    14189  15458  12895    371   1865    576       N  
ATOM   4173  CA  PRO B 233     -22.392  -6.980  23.024  1.00111.62           C  
ANISOU 4173  CA  PRO B 233    13931  15525  12955    471   1878    651       C  
ATOM   4174  C   PRO B 233     -22.292  -8.348  22.352  1.00115.22           C  
ANISOU 4174  C   PRO B 233    14279  15959  13543    490   1846    674       C  
ATOM   4175  O   PRO B 233     -22.700  -8.510  21.199  1.00114.58           O  
ANISOU 4175  O   PRO B 233    14256  15767  13513    455   1808    661       O  
ATOM   4176  CB  PRO B 233     -23.660  -6.851  23.871  1.00113.40           C  
ANISOU 4176  CB  PRO B 233    14124  15723  13237    588   1869    754       C  
ATOM   4177  CG  PRO B 233     -24.643  -6.133  22.993  1.00117.91           C  
ANISOU 4177  CG  PRO B 233    14833  16147  13818    597   1807    731       C  
ATOM   4178  CD  PRO B 233     -23.900  -5.455  21.870  1.00113.56           C  
ANISOU 4178  CD  PRO B 233    14474  15525  13151    466   1793    634       C  
ATOM   4179  N   ASN B 234     -21.714  -9.300  23.069  1.00111.96           N  
ANISOU 4179  N   ASN B 234    13724  15641  13176    557   1849    706       N  
ATOM   4180  CA  ASN B 234     -21.590 -10.651  22.572  1.00111.84           C  
ANISOU 4180  CA  ASN B 234    13610  15597  13286    600   1810    731       C  
ATOM   4181  C   ASN B 234     -22.974 -11.242  22.464  1.00115.65           C  
ANISOU 4181  C   ASN B 234    14076  15968  13899    669   1798    866       C  
ATOM   4182  O   ASN B 234     -23.847 -10.930  23.263  1.00115.35           O  
ANISOU 4182  O   ASN B 234    14035  15938  13853    721   1828    949       O  
ATOM   4183  CB  ASN B 234     -20.731 -11.486  23.512  1.00113.28           C  
ANISOU 4183  CB  ASN B 234    13690  15897  13456    679   1789    716       C  
ATOM   4184  CG  ASN B 234     -20.328 -12.811  22.905  1.00136.87           C  
ANISOU 4184  CG  ASN B 234    16591  18864  16549    725   1729    685       C  
ATOM   4185  OD1 ASN B 234     -20.164 -12.927  21.690  1.00131.13           O  
ANISOU 4185  OD1 ASN B 234    15864  18027  15932    703   1715    713       O  
ATOM   4186  ND2 ASN B 234     -20.167 -13.821  23.748  1.00129.54           N  
ANISOU 4186  ND2 ASN B 234    15585  18043  15591    806   1679    615       N  
ATOM   4187  N   HIS B 235     -23.176 -12.097  21.473  1.00112.22           N  
ANISOU 4187  N   HIS B 235    13620  15441  13579    655   1766    865       N  
ATOM   4188  CA  HIS B 235     -24.493 -12.659  21.220  1.00112.14           C  
ANISOU 4188  CA  HIS B 235    13576  15331  13701    695   1762    951       C  
ATOM   4189  C   HIS B 235     -24.999 -13.490  22.391  1.00116.46           C  
ANISOU 4189  C   HIS B 235    14065  15882  14302    761   1796   1067       C  
ATOM   4190  O   HIS B 235     -26.181 -13.459  22.713  1.00116.35           O  
ANISOU 4190  O   HIS B 235    14030  15824  14353    768   1834   1123       O  
ATOM   4191  CB  HIS B 235     -24.496 -13.478  19.930  1.00112.76           C  
ANISOU 4191  CB  HIS B 235    13640  15324  13880    657   1721    907       C  
ATOM   4192  CG  HIS B 235     -23.855 -14.821  20.062  1.00116.43           C  
ANISOU 4192  CG  HIS B 235    14031  15800  14407    673   1703    898       C  
ATOM   4193  ND1 HIS B 235     -24.578 -15.993  20.063  1.00118.32           N  
ANISOU 4193  ND1 HIS B 235    14255  16125  14575    640   1687    786       N  
ATOM   4194  CD2 HIS B 235     -22.557 -15.177  20.209  1.00118.54           C  
ANISOU 4194  CD2 HIS B 235    14241  16002  14798    720   1696    968       C  
ATOM   4195  CE1 HIS B 235     -23.752 -17.015  20.200  1.00118.16           C  
ANISOU 4195  CE1 HIS B 235    14158  16092  14647    696   1650    785       C  
ATOM   4196  NE2 HIS B 235     -22.521 -16.547  20.291  1.00118.64           N  
ANISOU 4196  NE2 HIS B 235    14212  16047  14821    744   1653    906       N  
ATOM   4197  N   VAL B 236     -24.106 -14.236  23.023  1.00113.32           N  
ANISOU 4197  N   VAL B 236    13653  15535  13868    806   1778   1085       N  
ATOM   4198  CA  VAL B 236     -24.495 -15.095  24.133  1.00113.99           C  
ANISOU 4198  CA  VAL B 236    13750  15593  13966    868   1794   1204       C  
ATOM   4199  C   VAL B 236     -25.058 -14.314  25.318  1.00118.18           C  
ANISOU 4199  C   VAL B 236    14321  16187  14394    876   1856   1272       C  
ATOM   4200  O   VAL B 236     -26.002 -14.755  25.965  1.00118.54           O  
ANISOU 4200  O   VAL B 236    14402  16184  14455    872   1911   1374       O  
ATOM   4201  CB  VAL B 236     -23.319 -15.960  24.606  1.00118.59           C  
ANISOU 4201  CB  VAL B 236    14334  16185  14540    951   1713   1191       C  
ATOM   4202  CG1 VAL B 236     -23.720 -16.751  25.838  1.00118.36           C  
ANISOU 4202  CG1 VAL B 236    14265  16062  14646    946   1667   1153       C  
ATOM   4203  CG2 VAL B 236     -22.874 -16.897  23.498  1.00118.35           C  
ANISOU 4203  CG2 VAL B 236    14271  16301  14397    977   1669   1065       C  
ATOM   4204  N   MET B 237     -24.470 -13.159  25.604  1.00114.28           N  
ANISOU 4204  N   MET B 237    13833  15799  13789    870   1860   1205       N  
ATOM   4205  CA  MET B 237     -24.820 -12.391  26.794  1.00114.38           C  
ANISOU 4205  CA  MET B 237    13875  15888  13698    876   1918   1247       C  
ATOM   4206  C   MET B 237     -26.268 -11.920  26.837  1.00117.18           C  
ANISOU 4206  C   MET B 237    14218  16234  14071    830   1967   1208       C  
ATOM   4207  O   MET B 237     -26.896 -11.950  27.888  1.00116.67           O  
ANISOU 4207  O   MET B 237    14171  16246  13912    830   1998   1183       O  
ATOM   4208  CB  MET B 237     -23.896 -11.185  26.935  1.00116.93           C  
ANISOU 4208  CB  MET B 237    14207  16340  13879    911   1887   1186       C  
ATOM   4209  CG  MET B 237     -22.534 -11.519  27.511  1.00119.98           C  
ANISOU 4209  CG  MET B 237    14582  16775  14229    852   1868   1038       C  
ATOM   4210  SD  MET B 237     -21.630 -10.054  28.037  1.00124.52           S  
ANISOU 4210  SD  MET B 237    15168  17516  14627    842   1888    943       S  
ATOM   4211  CE  MET B 237     -22.980  -8.972  28.490  1.00121.01           C  
ANISOU 4211  CE  MET B 237    14778  17049  14151    815   1962    997       C  
ATOM   4212  N   LEU B 238     -26.805 -11.482  25.707  1.00113.23           N  
ANISOU 4212  N   LEU B 238    13685  15641  13695    807   1961   1190       N  
ATOM   4213  CA  LEU B 238     -28.150 -10.915  25.704  1.00112.81           C  
ANISOU 4213  CA  LEU B 238    13617  15569  13677    802   1965   1120       C  
ATOM   4214  C   LEU B 238     -29.208 -11.949  26.073  1.00117.32           C  
ANISOU 4214  C   LEU B 238    14125  16171  14283    794   2051   1138       C  
ATOM   4215  O   LEU B 238     -29.032 -13.137  25.837  1.00117.23           O  
ANISOU 4215  O   LEU B 238    14120  16241  14183    802   2093   1126       O  
ATOM   4216  CB  LEU B 238     -28.477 -10.242  24.367  1.00112.44           C  
ANISOU 4216  CB  LEU B 238    13564  15423  13736    795   1897   1061       C  
ATOM   4217  CG  LEU B 238     -28.500 -11.072  23.086  1.00117.00           C  
ANISOU 4217  CG  LEU B 238    14196  15962  14297    821   1831    959       C  
ATOM   4218  CD1 LEU B 238     -29.807 -11.834  22.958  1.00117.39           C  
ANISOU 4218  CD1 LEU B 238    14202  15925  14477    841   1775    907       C  
ATOM   4219  CD2 LEU B 238     -28.256 -10.209  21.863  1.00118.84           C  
ANISOU 4219  CD2 LEU B 238    14566  16182  14406    785   1782    911       C  
ATOM   4220  N   ASN B 239     -30.285 -11.482  26.695  1.00114.17           N  
ANISOU 4220  N   ASN B 239    13657  15715  14007    763   2088   1145       N  
ATOM   4221  CA  ASN B 239     -31.366 -12.343  27.159  1.00114.99           C  
ANISOU 4221  CA  ASN B 239    13676  15853  14162    715   2192   1115       C  
ATOM   4222  C   ASN B 239     -31.023 -12.983  28.484  1.00119.48           C  
ANISOU 4222  C   ASN B 239    14287  16487  14622    658   2309   1202       C  
ATOM   4223  O   ASN B 239     -31.755 -13.830  28.986  1.00120.11           O  
ANISOU 4223  O   ASN B 239    14301  16617  14720    587   2421   1153       O  
ATOM   4224  CB  ASN B 239     -31.703 -13.422  26.135  1.00116.28           C  
ANISOU 4224  CB  ASN B 239    13772  15940  14471    663   2219   1099       C  
ATOM   4225  CG  ASN B 239     -32.389 -12.862  24.915  1.00138.67           C  
ANISOU 4225  CG  ASN B 239    16540  18730  17418    716   2116    976       C  
ATOM   4226  OD1 ASN B 239     -32.990 -11.794  24.970  1.00131.87           O  
ANISOU 4226  OD1 ASN B 239    15733  17858  16514    791   2004    926       O  
ATOM   4227  ND2 ASN B 239     -32.309 -13.585  23.805  1.00131.57           N  
ANISOU 4227  ND2 ASN B 239    15544  17796  16651    671   2150    918       N  
ATOM   4228  N   HIS B 240     -29.905 -12.564  29.055  1.00115.65           N  
ANISOU 4228  N   HIS B 240    13910  16013  14018    685   2282   1308       N  
ATOM   4229  CA  HIS B 240     -29.487 -13.076  30.342  1.00116.43           C  
ANISOU 4229  CA  HIS B 240    14092  16162  13984    649   2364   1402       C  
ATOM   4230  C   HIS B 240     -29.669 -11.963  31.343  1.00120.26           C  
ANISOU 4230  C   HIS B 240    14547  16772  14374    652   2410   1340       C  
ATOM   4231  O   HIS B 240     -29.264 -10.831  31.096  1.00118.79           O  
ANISOU 4231  O   HIS B 240    14332  16628  14176    716   2338   1259       O  
ATOM   4232  CB  HIS B 240     -28.030 -13.512  30.295  1.00117.09           C  
ANISOU 4232  CB  HIS B 240    14294  16217  13976    716   2281   1505       C  
ATOM   4233  CG  HIS B 240     -27.839 -14.912  29.809  1.00120.56           C  
ANISOU 4233  CG  HIS B 240    14772  16530  14507    724   2231   1559       C  
ATOM   4234  ND1 HIS B 240     -28.853 -15.844  29.816  1.00123.73           N  
ANISOU 4234  ND1 HIS B 240    15295  16835  14884    677   2282   1671       N  
ATOM   4235  CD2 HIS B 240     -26.755 -15.540  29.299  1.00121.29           C  
ANISOU 4235  CD2 HIS B 240    14811  16569  14705    764   2140   1507       C  
ATOM   4236  CE1 HIS B 240     -28.402 -16.986  29.333  1.00122.91           C  
ANISOU 4236  CE1 HIS B 240    15197  16622  14882    706   2212   1682       C  
ATOM   4237  NE2 HIS B 240     -27.132 -16.829  29.011  1.00121.77           N  
ANISOU 4237  NE2 HIS B 240    14935  16509  14821    757   2128   1581       N  
ATOM   4238  N   LEU B 241     -30.309 -12.271  32.462  1.00118.14           N  
ANISOU 4238  N   LEU B 241    14305  16555  14028    566   2537   1372       N  
ATOM   4239  CA  LEU B 241     -30.633 -11.229  33.439  1.00118.34           C  
ANISOU 4239  CA  LEU B 241    14295  16709  13962    552   2603   1306       C  
ATOM   4240  C   LEU B 241     -29.454 -10.916  34.365  1.00122.22           C  
ANISOU 4240  C   LEU B 241    14900  17262  14275    600   2569   1393       C  
ATOM   4241  O   LEU B 241     -28.874 -11.823  34.966  1.00122.52           O  
ANISOU 4241  O   LEU B 241    15073  17262  14215    589   2572   1522       O  
ATOM   4242  CB  LEU B 241     -31.881 -11.624  34.253  1.00120.12           C  
ANISOU 4242  CB  LEU B 241    14477  16978  14184    406   2778   1264       C  
ATOM   4243  N   TYR B 242     -29.127  -9.618  34.484  1.00118.20           N  
ANISOU 4243  N   TYR B 242    14348  16843  13719    660   2528   1309       N  
ATOM   4244  CA  TYR B 242     -28.060  -9.089  35.331  1.00118.05           C  
ANISOU 4244  CA  TYR B 242    14401  16914  13539    706   2498   1344       C  
ATOM   4245  C   TYR B 242     -28.674  -8.140  36.358  1.00122.88           C  
ANISOU 4245  C   TYR B 242    14970  17645  14074    665   2594   1272       C  
ATOM   4246  O   TYR B 242     -29.347  -7.181  35.979  1.00122.06           O  
ANISOU 4246  O   TYR B 242    14770  17563  14046    679   2596   1141       O  
ATOM   4247  CB  TYR B 242     -27.006  -8.356  34.481  1.00117.85           C  
ANISOU 4247  CB  TYR B 242    14369  16889  13519    787   2377   1284       C  
ATOM   4248  CG  TYR B 242     -26.172  -9.268  33.608  1.00119.09           C  
ANISOU 4248  CG  TYR B 242    14559  16962  13726    826   2283   1332       C  
ATOM   4249  CD1 TYR B 242     -24.973  -9.802  34.070  1.00121.41           C  
ANISOU 4249  CD1 TYR B 242    14918  17292  13921    884   2219   1386       C  
ATOM   4250  CD2 TYR B 242     -26.563  -9.571  32.307  1.00119.16           C  
ANISOU 4250  CD2 TYR B 242    14526  16865  13883    820   2245   1300       C  
ATOM   4251  CE1 TYR B 242     -24.192 -10.629  33.266  1.00121.87           C  
ANISOU 4251  CE1 TYR B 242    14985  17285  14035    934   2123   1395       C  
ATOM   4252  CE2 TYR B 242     -25.794 -10.404  31.495  1.00119.67           C  
ANISOU 4252  CE2 TYR B 242    14610  16861  13997    851   2164   1327       C  
ATOM   4253  CZ  TYR B 242     -24.608 -10.932  31.980  1.00127.37           C  
ANISOU 4253  CZ  TYR B 242    15636  17877  14882    908   2105   1368       C  
ATOM   4254  OH  TYR B 242     -23.841 -11.750  31.187  1.00128.15           O  
ANISOU 4254  OH  TYR B 242    15734  17920  15039    952   2016   1361       O  
ATOM   4255  N   ALA B 243     -28.466  -8.419  37.653  1.00120.92           N  
ANISOU 4255  N   ALA B 243    14806  17466  13670    622   2663   1349       N  
ATOM   4256  CA  ALA B 243     -29.021  -7.601  38.731  1.00121.75           C  
ANISOU 4256  CA  ALA B 243    14873  17698  13689    566   2769   1278       C  
ATOM   4257  C   ALA B 243     -27.962  -7.108  39.708  1.00126.28           C  
ANISOU 4257  C   ALA B 243    15528  18375  14079    611   2738   1316       C  
ATOM   4258  O   ALA B 243     -27.026  -7.840  40.029  1.00126.19           O  
ANISOU 4258  O   ALA B 243    15639  18343  13966    654   2672   1431       O  
ATOM   4259  CB  ALA B 243     -30.100  -8.375  39.471  1.00124.26           C  
ANISOU 4259  CB  ALA B 243    15209  18021  13981    418   2929   1301       C  
ATOM   4260  N   LEU B 244     -28.122  -5.863  40.183  1.00123.24           N  
ANISOU 4260  N   LEU B 244    15071  18101  13652    614   2773   1203       N  
ATOM   4261  CA  LEU B 244     -27.232  -5.223  41.153  1.00123.53           C  
ANISOU 4261  CA  LEU B 244    15158  18260  13519    646   2760   1204       C  
ATOM   4262  C   LEU B 244     -27.855  -5.312  42.552  1.00129.72           C  
ANISOU 4262  C   LEU B 244    15978  19140  14169    544   2899   1223       C  
ATOM   4263  O   LEU B 244     -29.066  -5.119  42.692  1.00129.94           O  
ANISOU 4263  O   LEU B 244    15916  19191  14263    455   3016   1135       O  
ATOM   4264  CB  LEU B 244     -26.956  -3.758  40.731  1.00122.51           C  
ANISOU 4264  CB  LEU B 244    14952  18175  13422    700   2714   1060       C  
ATOM   4265  CG  LEU B 244     -26.456  -2.744  41.781  1.00127.65           C  
ANISOU 4265  CG  LEU B 244    15606  18972  13923    702   2744    997       C  
ATOM   4266  CD1 LEU B 244     -25.016  -3.017  42.193  1.00127.91           C  
ANISOU 4266  CD1 LEU B 244    15715  19072  13812    754   2667   1056       C  
ATOM   4267  CD2 LEU B 244     -26.570  -1.330  41.258  1.00129.33           C  
ANISOU 4267  CD2 LEU B 244    15767  19181  14194    731   2721    843       C  
ATOM   4268  N   SER B 245     -27.023  -5.623  43.575  1.00127.69           N  
ANISOU 4268  N   SER B 245    15853  18946  13716    557   2880   1319       N  
ATOM   4269  CA  SER B 245     -27.423  -5.752  44.982  1.00129.54           C  
ANISOU 4269  CA  SER B 245    16177  19271  13773    452   3003   1355       C  
ATOM   4270  C   SER B 245     -28.148  -4.501  45.483  1.00133.97           C  
ANISOU 4270  C   SER B 245    16594  19966  14343    394   3115   1192       C  
ATOM   4271  O   SER B 245     -27.721  -3.381  45.191  1.00132.35           O  
ANISOU 4271  O   SER B 245    16294  19815  14179    479   3052   1084       O  
ATOM   4272  CB  SER B 245     -26.216  -6.063  45.862  1.00133.94           C  
ANISOU 4272  CB  SER B 245    16899  19878  14115    529   2909   1458       C  
ATOM   4273  OG  SER B 245     -25.209  -5.073  45.737  1.00141.75           O  
ANISOU 4273  OG  SER B 245    17800  20965  15092    645   2807   1364       O  
ATOM   4274  N   ILE B 246     -29.228  -4.672  46.233  1.00132.50           N  
ANISOU 4274  N   ILE B 246    16396  19826  14120    239   3286   1155       N  
ATOM   4275  CA  ILE B 246     -30.054  -3.525  46.570  1.00133.03           C  
ANISOU 4275  CA  ILE B 246    16307  20028  14209    175   3404    967       C  
ATOM   4276  C   ILE B 246     -29.563  -2.795  47.809  1.00137.61           C  
ANISOU 4276  C   ILE B 246    16926  20754  14606    195   3409    948       C  
ATOM   4277  O   ILE B 246     -29.648  -3.303  48.924  1.00138.26           O  
ANISOU 4277  O   ILE B 246    17185  20866  14481    164   3412   1081       O  
ATOM   4278  CB  ILE B 246     -31.511  -3.948  46.802  1.00138.06           C  
ANISOU 4278  CB  ILE B 246    16893  20699  14865    -24   3606    889       C  
ATOM   4279  CG1 ILE B 246     -31.589  -4.934  47.966  1.00140.63           C  
ANISOU 4279  CG1 ILE B 246    17455  21024  14955   -192   3725   1045       C  
ATOM   4280  CG2 ILE B 246     -32.089  -4.561  45.538  1.00138.29           C  
ANISOU 4280  CG2 ILE B 246    16813  20613  15116    -27   3596    835       C  
ATOM   4281  CD1 ILE B 246     -32.999  -5.245  48.413  1.00150.60           C  
ANISOU 4281  CD1 ILE B 246    18672  22414  16136   -430   3969    912       C  
ATOM   4282  N   LYS B 247     -29.062  -1.584  47.592  1.00133.66           N  
ANISOU 4282  N   LYS B 247    16275  20332  14177    257   3395    776       N  
ATOM   4283  CA  LYS B 247     -28.634  -0.707  48.669  1.00133.89           C  
ANISOU 4283  CA  LYS B 247    16307  20508  14059    270   3412    717       C  
ATOM   4284  C   LYS B 247     -29.840  -0.340  49.513  1.00139.57           C  
ANISOU 4284  C   LYS B 247    16932  21357  14740    129   3595    576       C  
ATOM   4285  O   LYS B 247     -29.770  -0.273  50.738  1.00140.58           O  
ANISOU 4285  O   LYS B 247    17147  21602  14666     37   3685    610       O  
ATOM   4286  CB  LYS B 247     -27.980   0.552  48.097  1.00134.88           C  
ANISOU 4286  CB  LYS B 247    16354  20622  14274    404   3296    604       C  
ATOM   4287  CG  LYS B 247     -27.930   1.732  49.053  1.00150.25           C  
ANISOU 4287  CG  LYS B 247    18330  22705  16053    425   3288    567       C  
ATOM   4288  CD  LYS B 247     -27.620   3.024  48.316  1.00159.63           C  
ANISOU 4288  CD  LYS B 247    19451  23875  17326    509   3221    415       C  
ATOM   4289  N   ASP B 248     -30.952  -0.100  48.834  1.00136.20           N  
ANISOU 4289  N   ASP B 248    16329  20916  14505    116   3644    399       N  
ATOM   4290  CA  ASP B 248     -32.189   0.292  49.481  1.00137.84           C  
ANISOU 4290  CA  ASP B 248    16392  21259  14722    -14   3818    200       C  
ATOM   4291  C   ASP B 248     -33.298  -0.650  49.059  1.00142.53           C  
ANISOU 4291  C   ASP B 248    16937  21809  15409   -150   3929    177       C  
ATOM   4292  O   ASP B 248     -33.049  -1.656  48.405  1.00141.91           O  
ANISOU 4292  O   ASP B 248    17015  21615  15288   -192   3912    376       O  
ATOM   4293  CB  ASP B 248     -32.557   1.733  49.148  1.00139.32           C  
ANISOU 4293  CB  ASP B 248    16390  21482  15062    114   3757    -48       C  
ATOM   4294  CG  ASP B 248     -33.721   2.235  49.972  1.00151.55           C  
ANISOU 4294  CG  ASP B 248    17807  23221  16554     20   3907   -262       C  
ATOM   4295  OD1 ASP B 248     -34.662   1.443  50.190  1.00153.77           O  
ANISOU 4295  OD1 ASP B 248    17946  23582  16897   -108   4051   -423       O  
ATOM   4296  OD2 ASP B 248     -33.697   3.405  50.405  1.00157.49           O  
ANISOU 4296  OD2 ASP B 248    18586  24052  17203     64   3888   -290       O  
ATOM   4297  N   SER B 249     -34.523  -0.316  49.434  1.00140.22           N  
ANISOU 4297  N   SER B 249    16424  21611  15243   -218   4040    -86       N  
ATOM   4298  CA  SER B 249     -35.668  -1.166  49.175  1.00141.26           C  
ANISOU 4298  CA  SER B 249    16461  21733  15480   -362   4163   -177       C  
ATOM   4299  C   SER B 249     -35.794  -1.380  47.680  1.00143.15           C  
ANISOU 4299  C   SER B 249    16632  21811  15948   -198   3994   -178       C  
ATOM   4300  O   SER B 249     -36.189  -2.452  47.230  1.00143.38           O  
ANISOU 4300  O   SER B 249    16626  21793  16060   -300   4062   -191       O  
ATOM   4301  CB  SER B 249     -36.934  -0.500  49.692  1.00147.15           C  
ANISOU 4301  CB  SER B 249    16954  22671  16287   -479   4332   -515       C  
ATOM   4302  OG  SER B 249     -37.135   0.741  49.041  1.00155.48           O  
ANISOU 4302  OG  SER B 249    17803  23749  17525   -260   4188   -750       O  
ATOM   4303  N   VAL B 250     -35.475  -0.348  46.911  1.00137.47           N  
ANISOU 4303  N   VAL B 250    15912  21005  15317     37   3783   -171       N  
ATOM   4304  CA  VAL B 250     -35.588  -0.421  45.463  1.00135.63           C  
ANISOU 4304  CA  VAL B 250    15649  20609  15274    204   3602   -170       C  
ATOM   4305  C   VAL B 250     -34.688  -1.508  44.886  1.00137.50           C  
ANISOU 4305  C   VAL B 250    16076  20695  15471    194   3541    110       C  
ATOM   4306  O   VAL B 250     -33.567  -1.712  45.341  1.00136.23           O  
ANISOU 4306  O   VAL B 250    16093  20514  15157    205   3503    308       O  
ATOM   4307  CB  VAL B 250     -35.214   0.923  44.816  1.00138.41           C  
ANISOU 4307  CB  VAL B 250    15982  20902  15706    430   3411   -274       C  
ATOM   4308  CG1 VAL B 250     -36.000   2.051  45.464  1.00139.77           C  
ANISOU 4308  CG1 VAL B 250    15935  21172  16001    495   3417   -605       C  
ATOM   4309  CG2 VAL B 250     -33.722   1.177  44.949  1.00137.27           C  
ANISOU 4309  CG2 VAL B 250    15995  20774  15388    460   3374   -139       C  
ATOM   4310  N   MET B 251     -35.207  -2.205  43.882  1.00133.51           N  
ANISOU 4310  N   MET B 251    15520  20097  15111    181   3525    102       N  
ATOM   4311  CA  MET B 251     -34.519  -3.317  43.222  1.00132.00           C  
ANISOU 4311  CA  MET B 251    15483  19754  14915    178   3464    335       C  
ATOM   4312  C   MET B 251     -34.116  -2.947  41.794  1.00133.10           C  
ANISOU 4312  C   MET B 251    15619  19751  15202    369   3255    341       C  
ATOM   4313  O   MET B 251     -34.916  -2.372  41.052  1.00132.68           O  
ANISOU 4313  O   MET B 251    15422  19683  15309    463   3186    149       O  
ATOM   4314  CB  MET B 251     -35.377  -4.599  43.253  1.00135.86           C  
ANISOU 4314  CB  MET B 251    15955  20230  15435     -9   3616    339       C  
ATOM   4315  CG  MET B 251     -34.622  -5.851  42.839  1.00138.83           C  
ANISOU 4315  CG  MET B 251    16530  20449  15768    -30   3570    594       C  
ATOM   4316  SD  MET B 251     -35.587  -7.366  43.030  1.00145.18           S  
ANISOU 4316  SD  MET B 251    17379  21218  16566   -290   3777    613       S  
ATOM   4317  CE  MET B 251     -35.035  -7.888  44.627  1.00143.54           C  
ANISOU 4317  CE  MET B 251    17446  21047  16047   -461   3915    797       C  
ATOM   4318  N   VAL B 252     -32.869  -3.286  41.423  1.00127.58           N  
ANISOU 4318  N   VAL B 252    15087  18952  14437    427   3150    546       N  
ATOM   4319  CA  VAL B 252     -32.290  -3.016  40.105  1.00125.33           C  
ANISOU 4319  CA  VAL B 252    14841  18530  14250    569   2972    573       C  
ATOM   4320  C   VAL B 252     -31.918  -4.294  39.367  1.00127.80           C  
ANISOU 4320  C   VAL B 252    15230  18722  14605    547   2937    732       C  
ATOM   4321  O   VAL B 252     -31.155  -5.114  39.881  1.00127.51           O  
ANISOU 4321  O   VAL B 252    15320  18679  14449    496   2962    901       O  
ATOM   4322  CB  VAL B 252     -31.112  -2.013  40.136  1.00128.06           C  
ANISOU 4322  CB  VAL B 252    15285  18877  14496    660   2873    602       C  
ATOM   4323  CG1 VAL B 252     -30.487  -1.876  38.763  1.00127.94           C  
ANISOU 4323  CG1 VAL B 252    15205  18872  14533    751   2818    408       C  
ATOM   4324  CG2 VAL B 252     -31.534  -0.652  40.685  1.00128.34           C  
ANISOU 4324  CG2 VAL B 252    15406  19023  14334    598   2944    710       C  
ATOM   4325  N   LEU B 253     -32.469  -4.453  38.154  1.00123.19           N  
ANISOU 4325  N   LEU B 253    14578  18039  14190    599   2861    665       N  
ATOM   4326  CA  LEU B 253     -32.238  -5.598  37.270  1.00122.10           C  
ANISOU 4326  CA  LEU B 253    14491  17778  14124    587   2819    784       C  
ATOM   4327  C   LEU B 253     -32.394  -5.204  35.806  1.00124.30           C  
ANISOU 4327  C   LEU B 253    14734  17946  14550    701   2672    703       C  
ATOM   4328  O   LEU B 253     -33.352  -4.517  35.447  1.00124.32           O  
ANISOU 4328  O   LEU B 253    14625  17958  14651    761   2637    524       O  
ATOM   4329  CB  LEU B 253     -33.113  -6.816  37.632  1.00123.59           C  
ANISOU 4329  CB  LEU B 253    14642  17973  14343    439   2965    804       C  
ATOM   4330  CG  LEU B 253     -34.627  -6.648  37.540  1.00129.94           C  
ANISOU 4330  CG  LEU B 253    15269  18889  15215    354   3095    594       C  
ATOM   4331  CD1 LEU B 253     -35.098  -6.774  36.119  1.00130.36           C  
ANISOU 4331  CD1 LEU B 253    15179  18890  15462    366   3068    461       C  
ATOM   4332  CD2 LEU B 253     -35.332  -7.677  38.390  1.00134.21           C  
ANISOU 4332  CD2 LEU B 253    15863  19506  15623    150   3300    647       C  
ATOM   4333  N   SER B 254     -31.428  -5.622  34.973  1.00119.21           N  
ANISOU 4333  N   SER B 254    14191  17196  13906    738   2575    822       N  
ATOM   4334  CA  SER B 254     -31.361  -5.309  33.545  1.00117.82           C  
ANISOU 4334  CA  SER B 254    14034  16901  13832    825   2435    772       C  
ATOM   4335  C   SER B 254     -30.979  -6.517  32.683  1.00120.57           C  
ANISOU 4335  C   SER B 254    14415  17148  14246    800   2402    882       C  
ATOM   4336  O   SER B 254     -30.374  -7.467  33.181  1.00120.21           O  
ANISOU 4336  O   SER B 254    14421  17112  14142    743   2454   1016       O  
ATOM   4337  CB  SER B 254     -30.371  -4.172  33.309  1.00120.45           C  
ANISOU 4337  CB  SER B 254    14483  17213  14070    886   2344    758       C  
ATOM   4338  OG  SER B 254     -29.107  -4.468  33.878  1.00128.78           O  
ANISOU 4338  OG  SER B 254    15614  18320  14997    846   2370    875       O  
ATOM   4339  N   ALA B 255     -31.333  -6.466  31.381  1.00116.33           N  
ANISOU 4339  N   ALA B 255    13865  16508  13826    855   2300    818       N  
ATOM   4340  CA  ALA B 255     -31.043  -7.506  30.387  1.00115.42           C  
ANISOU 4340  CA  ALA B 255    13771  16293  13790    839   2256    893       C  
ATOM   4341  C   ALA B 255     -30.993  -6.918  28.976  1.00118.24           C  
ANISOU 4341  C   ALA B 255    14181  16542  14203    912   2115    819       C  
ATOM   4342  O   ALA B 255     -31.784  -6.030  28.648  1.00118.19           O  
ANISOU 4342  O   ALA B 255    14157  16515  14235    987   2047    686       O  
ATOM   4343  CB  ALA B 255     -32.087  -8.612  30.454  1.00117.14           C  
ANISOU 4343  CB  ALA B 255    13879  16509  14120    772   2345    886       C  
ATOM   4344  N   THR B 256     -30.064  -7.420  28.144  1.00113.76           N  
ANISOU 4344  N   THR B 256    13691  15900  13631    894   2061    893       N  
ATOM   4345  CA  THR B 256     -29.889  -6.975  26.758  1.00112.91           C  
ANISOU 4345  CA  THR B 256    13674  15681  13547    929   1940    836       C  
ATOM   4346  C   THR B 256     -30.810  -7.775  25.823  1.00116.90           C  
ANISOU 4346  C   THR B 256    14097  16113  14206    946   1901    802       C  
ATOM   4347  O   THR B 256     -30.905  -8.996  25.950  1.00116.55           O  
ANISOU 4347  O   THR B 256    13971  16077  14235    894   1968    872       O  
ATOM   4348  CB  THR B 256     -28.404  -7.035  26.350  1.00119.79           C  
ANISOU 4348  CB  THR B 256    14653  16536  14324    876   1921    891       C  
ATOM   4349  OG1 THR B 256     -27.597  -6.528  27.416  1.00119.14           O  
ANISOU 4349  OG1 THR B 256    14599  16557  14112    855   1976    912       O  
ATOM   4350  CG2 THR B 256     -28.111  -6.251  25.075  1.00118.05           C  
ANISOU 4350  CG2 THR B 256    14583  16206  14066    871   1820    818       C  
ATOM   4351  N   HIS B 257     -31.479  -7.087  24.911  1.00113.68           N  
ANISOU 4351  N   HIS B 257    13730  15624  13838   1025   1783    689       N  
ATOM   4352  CA  HIS B 257     -32.367  -7.746  23.969  1.00113.87           C  
ANISOU 4352  CA  HIS B 257    13674  15589  14004   1062   1720    621       C  
ATOM   4353  C   HIS B 257     -32.112  -7.226  22.567  1.00117.14           C  
ANISOU 4353  C   HIS B 257    14251  15865  14391   1102   1570    586       C  
ATOM   4354  O   HIS B 257     -31.702  -6.082  22.389  1.00116.69           O  
ANISOU 4354  O   HIS B 257    14377  15746  14212   1136   1491    555       O  
ATOM   4355  CB  HIS B 257     -33.821  -7.513  24.359  1.00116.03           C  
ANISOU 4355  CB  HIS B 257    13797  15921  14368   1144   1710    464       C  
ATOM   4356  CG  HIS B 257     -34.363  -8.537  25.303  1.00120.15           C  
ANISOU 4356  CG  HIS B 257    14131  16561  14960   1055   1878    474       C  
ATOM   4357  ND1 HIS B 257     -35.492  -9.278  25.030  1.00122.73           N  
ANISOU 4357  ND1 HIS B 257    14299  16904  15431   1022   1918    398       N  
ATOM   4358  CD2 HIS B 257     -33.929  -8.946  26.518  1.00122.07           C  
ANISOU 4358  CD2 HIS B 257    14349  16903  15129    977   2020    544       C  
ATOM   4359  CE1 HIS B 257     -35.731 -10.098  26.036  1.00122.87           C  
ANISOU 4359  CE1 HIS B 257    14217  17018  15449    905   2095    425       C  
ATOM   4360  NE2 HIS B 257     -34.798  -9.917  26.952  1.00122.86           N  
ANISOU 4360  NE2 HIS B 257    14301  17066  15313    880   2155    520       N  
ATOM   4361  N   ARG B 258     -32.356  -8.065  21.571  1.00113.44           N  
ANISOU 4361  N   ARG B 258    13737  15342  14025   1086   1537    588       N  
ATOM   4362  CA  ARG B 258     -32.100  -7.678  20.196  1.00113.06           C  
ANISOU 4362  CA  ARG B 258    13848  15162  13948   1107   1400    554       C  
ATOM   4363  C   ARG B 258     -33.398  -7.512  19.431  1.00117.98           C  
ANISOU 4363  C   ARG B 258    14441  15732  14655   1249   1253    403       C  
ATOM   4364  O   ARG B 258     -34.227  -8.415  19.397  1.00118.33           O  
ANISOU 4364  O   ARG B 258    14264  15855  14843   1284   1289    327       O  
ATOM   4365  CB  ARG B 258     -31.227  -8.727  19.507  1.00112.57           C  
ANISOU 4365  CB  ARG B 258    13754  15077  13939   1006   1445    635       C  
ATOM   4366  CG  ARG B 258     -31.199  -8.625  17.990  1.00122.36           C  
ANISOU 4366  CG  ARG B 258    15199  16200  15091    967   1348    622       C  
ATOM   4367  CD  ARG B 258     -30.707  -9.915  17.357  1.00131.29           C  
ANISOU 4367  CD  ARG B 258    16264  17324  16298    877   1392    671       C  
ATOM   4368  N   TYR B 259     -33.569  -6.349  18.816  1.00114.78           N  
ANISOU 4368  N   TYR B 259    14273  15193  14147   1326   1084    344       N  
ATOM   4369  CA  TYR B 259     -34.711  -6.117  17.950  1.00115.89           C  
ANISOU 4369  CA  TYR B 259    14435  15259  14339   1501    890    186       C  
ATOM   4370  C   TYR B 259     -34.235  -5.702  16.572  1.00119.42           C  
ANISOU 4370  C   TYR B 259    15159  15531  14684   1504    736    191       C  
ATOM   4371  O   TYR B 259     -33.442  -4.772  16.439  1.00119.22           O  
ANISOU 4371  O   TYR B 259    15446  15378  14475   1499    658    210       O  
ATOM   4372  CB  TYR B 259     -35.610  -5.029  18.533  1.00118.40           C  
ANISOU 4372  CB  TYR B 259    14792  15582  14615   1659    796     63       C  
ATOM   4373  N   LYS B 260     -34.716  -6.394  15.546  1.00115.56           N  
ANISOU 4373  N   LYS B 260    14572  15031  14304   1491    707    172       N  
ATOM   4374  CA  LYS B 260     -34.453  -5.992  14.173  1.00115.35           C  
ANISOU 4374  CA  LYS B 260    14774  14854  14198   1481    572    168       C  
ATOM   4375  C   LYS B 260     -32.963  -5.834  13.934  1.00117.70           C  
ANISOU 4375  C   LYS B 260    15370  15059  14292   1303    629    284       C  
ATOM   4376  O   LYS B 260     -32.531  -4.878  13.295  1.00118.10           O  
ANISOU 4376  O   LYS B 260    15752  14942  14177   1308    490    261       O  
ATOM   4377  CB  LYS B 260     -35.170  -4.681  13.853  1.00119.74           C  
ANISOU 4377  CB  LYS B 260    15483  15292  14721   1709    303      9       C  
ATOM   4378  N   LYS B 261     -32.174  -6.759  14.457  1.00112.29           N  
ANISOU 4378  N   LYS B 261    14569  14484  13611   1141    833    390       N  
ATOM   4379  CA  LYS B 261     -30.732  -6.643  14.337  1.00111.07           C  
ANISOU 4379  CA  LYS B 261    14599  14310  13293    950    935    461       C  
ATOM   4380  C   LYS B 261     -30.270  -5.354  14.997  1.00114.34           C  
ANISOU 4380  C   LYS B 261    15237  14680  13527    945    931    456       C  
ATOM   4381  O   LYS B 261     -29.343  -4.697  14.529  1.00114.29           O  
ANISOU 4381  O   LYS B 261    15547  14556  13321    833    909    447       O  
ATOM   4382  CB  LYS B 261     -30.321  -6.650  12.867  1.00113.84           C  
ANISOU 4382  CB  LYS B 261    15152  14548  13553    832    888    449       C  
ATOM   4383  N   LYS B 262     -30.933  -4.997  16.087  1.00110.15           N  
ANISOU 4383  N   LYS B 262    14544  14247  13061   1046    967    453       N  
ATOM   4384  CA  LYS B 262     -30.527  -3.865  16.900  1.00109.97           C  
ANISOU 4384  CA  LYS B 262    14670  14212  12903   1057    978    443       C  
ATOM   4385  C   LYS B 262     -30.475  -4.335  18.344  1.00112.51           C  
ANISOU 4385  C   LYS B 262    14698  14717  13335   1092   1105    472       C  
ATOM   4386  O   LYS B 262     -31.272  -5.176  18.752  1.00112.55           O  
ANISOU 4386  O   LYS B 262    14493  14782  13487   1224   1075    422       O  
ATOM   4387  CB  LYS B 262     -31.510  -2.710  16.742  1.00114.04           C  
ANISOU 4387  CB  LYS B 262    15436  14559  13335   1229    768    347       C  
ATOM   4388  N   TYR B 263     -29.536  -3.804  19.117  1.00107.62           N  
ANISOU 4388  N   TYR B 263    14061  14193  12637    961   1252    535       N  
ATOM   4389  CA  TYR B 263     -29.343  -4.261  20.485  1.00106.67           C  
ANISOU 4389  CA  TYR B 263    13709  14241  12580    969   1380    579       C  
ATOM   4390  C   TYR B 263     -29.741  -3.195  21.486  1.00110.18           C  
ANISOU 4390  C   TYR B 263    14209  14699  12954   1051   1362    529       C  
ATOM   4391  O   TYR B 263     -29.316  -2.050  21.376  1.00110.15           O  
ANISOU 4391  O   TYR B 263    14461  14598  12792   1025   1316    493       O  
ATOM   4392  CB  TYR B 263     -27.885  -4.647  20.706  1.00107.01           C  
ANISOU 4392  CB  TYR B 263    13700  14388  12570    819   1518    650       C  
ATOM   4393  CG  TYR B 263     -27.403  -5.763  19.814  1.00108.33           C  
ANISOU 4393  CG  TYR B 263    13852  14532  12778    728   1526    670       C  
ATOM   4394  CD1 TYR B 263     -28.282  -6.454  18.997  1.00110.04           C  
ANISOU 4394  CD1 TYR B 263    13862  14786  13160    761   1546    717       C  
ATOM   4395  CD2 TYR B 263     -26.068  -6.126  19.790  1.00109.14           C  
ANISOU 4395  CD2 TYR B 263    14150  14574  12745    592   1527    625       C  
ATOM   4396  CE1 TYR B 263     -27.843  -7.476  18.182  1.00110.54           C  
ANISOU 4396  CE1 TYR B 263    13905  14826  13268    685   1549    723       C  
ATOM   4397  CE2 TYR B 263     -25.620  -7.146  18.977  1.00109.76           C  
ANISOU 4397  CE2 TYR B 263    14196  14645  12862    502   1540    618       C  
ATOM   4398  CZ  TYR B 263     -26.512  -7.816  18.176  1.00116.93           C  
ANISOU 4398  CZ  TYR B 263    14887  15591  13951    562   1543    669       C  
ATOM   4399  OH  TYR B 263     -26.070  -8.832  17.365  1.00117.80           O  
ANISOU 4399  OH  TYR B 263    14960  15692  14106    482   1552    650       O  
ATOM   4400  N   VAL B 264     -30.558  -3.570  22.464  1.00106.19           N  
ANISOU 4400  N   VAL B 264    13475  14312  12560   1133   1411    516       N  
ATOM   4401  CA  VAL B 264     -31.026  -2.597  23.459  1.00106.33           C  
ANISOU 4401  CA  VAL B 264    13486  14376  12537   1214   1410    450       C  
ATOM   4402  C   VAL B 264     -30.868  -3.146  24.881  1.00108.89           C  
ANISOU 4402  C   VAL B 264    13594  14885  12893   1160   1577    512       C  
ATOM   4403  O   VAL B 264     -31.316  -4.258  25.168  1.00108.39           O  
ANISOU 4403  O   VAL B 264    13331  14902  12951   1143   1648    546       O  
ATOM   4404  CB  VAL B 264     -32.455  -2.035  23.194  1.00111.60           C  
ANISOU 4404  CB  VAL B 264    14137  14982  13285   1404   1256    299       C  
ATOM   4405  CG1 VAL B 264     -32.451  -1.033  22.045  1.00112.16           C  
ANISOU 4405  CG1 VAL B 264    14533  14840  13244   1479   1064    239       C  
ATOM   4406  CG2 VAL B 264     -33.481  -3.144  22.950  1.00111.74           C  
ANISOU 4406  CG2 VAL B 264    13902  15061  13494   1455   1253    250       C  
ATOM   4407  N   THR B 265     -30.205  -2.373  25.756  1.00104.63           N  
ANISOU 4407  N   THR B 265    13122  14404  12228   1120   1640    524       N  
ATOM   4408  CA  THR B 265     -29.976  -2.752  27.151  1.00103.92           C  
ANISOU 4408  CA  THR B 265    12874  14483  12128   1072   1783    581       C  
ATOM   4409  C   THR B 265     -30.920  -1.941  28.041  1.00107.89           C  
ANISOU 4409  C   THR B 265    13310  15044  12640   1161   1784    477       C  
ATOM   4410  O   THR B 265     -30.653  -0.771  28.334  1.00107.71           O  
ANISOU 4410  O   THR B 265    13418  14999  12509   1184   1757    424       O  
ATOM   4411  CB  THR B 265     -28.484  -2.634  27.520  1.00111.03           C  
ANISOU 4411  CB  THR B 265    13859  15438  12889    962   1856    653       C  
ATOM   4412  OG1 THR B 265     -27.687  -3.102  26.431  1.00109.81           O  
ANISOU 4412  OG1 THR B 265    13788  15210  12724    891   1825    684       O  
ATOM   4413  CG2 THR B 265     -28.132  -3.403  28.785  1.00109.54           C  
ANISOU 4413  CG2 THR B 265    13519  15409  12691    922   1978    737       C  
ATOM   4414  N   THR B 266     -32.048  -2.560  28.430  1.00104.50           N  
ANISOU 4414  N   THR B 266    12675  14689  12340   1201   1822    424       N  
ATOM   4415  CA  THR B 266     -33.085  -1.928  29.246  1.00105.21           C  
ANISOU 4415  CA  THR B 266    12647  14863  12466   1279   1833    280       C  
ATOM   4416  C   THR B 266     -32.877  -2.205  30.734  1.00107.97           C  
ANISOU 4416  C   THR B 266    12884  15382  12759   1182   2009    336       C  
ATOM   4417  O   THR B 266     -32.746  -3.360  31.136  1.00107.32           O  
ANISOU 4417  O   THR B 266    12714  15365  12699   1080   2125    442       O  
ATOM   4418  CB  THR B 266     -34.491  -2.321  28.748  1.00115.36           C  
ANISOU 4418  CB  THR B 266    13764  16148  13919   1368   1771    129       C  
ATOM   4419  OG1 THR B 266     -34.510  -2.346  27.318  1.00115.23           O  
ANISOU 4419  OG1 THR B 266    13868  15973  13942   1440   1612    119       O  
ATOM   4420  CG2 THR B 266     -35.576  -1.380  29.256  1.00115.65           C  
ANISOU 4420  CG2 THR B 266    13700  16245  13997   1498   1718    -92       C  
ATOM   4421  N   LEU B 267     -32.859  -1.133  31.540  1.00104.19           N  
ANISOU 4421  N   LEU B 267    12433  14959  12197   1216   2020    263       N  
ATOM   4422  CA  LEU B 267     -32.687  -1.153  32.993  1.00103.99           C  
ANISOU 4422  CA  LEU B 267    12325  15095  12093   1135   2173    293       C  
ATOM   4423  C   LEU B 267     -34.031  -0.934  33.674  1.00108.79           C  
ANISOU 4423  C   LEU B 267    12740  15812  12782   1171   2223    110       C  
ATOM   4424  O   LEU B 267     -34.839  -0.143  33.184  1.00109.17           O  
ANISOU 4424  O   LEU B 267    12766  15809  12904   1310   2098    -73       O  
ATOM   4425  CB  LEU B 267     -31.722  -0.032  33.423  1.00103.59           C  
ANISOU 4425  CB  LEU B 267    12427  15044  11888   1137   2160    309       C  
ATOM   4426  CG  LEU B 267     -30.228  -0.323  33.350  1.00107.01           C  
ANISOU 4426  CG  LEU B 267    12986  15469  12204   1047   2187    464       C  
ATOM   4427  CD1 LEU B 267     -29.665   0.013  31.978  1.00106.52           C  
ANISOU 4427  CD1 LEU B 267    13101  15241  12131   1064   2065    467       C  
ATOM   4428  CD2 LEU B 267     -29.483   0.483  34.388  1.00109.34           C  
ANISOU 4428  CD2 LEU B 267    13329  15863  12351   1010   2250    460       C  
ATOM   4429  N   LEU B 268     -34.269  -1.613  34.807  1.00105.52           N  
ANISOU 4429  N   LEU B 268    12200  15548  12344   1047   2400    140       N  
ATOM   4430  CA  LEU B 268     -35.511  -1.448  35.557  1.00106.85           C  
ANISOU 4430  CA  LEU B 268    12168  15854  12577   1036   2487    -61       C  
ATOM   4431  C   LEU B 268     -35.274  -1.119  37.024  1.00110.75           C  
ANISOU 4431  C   LEU B 268    12646  16498  12938    942   2634    -49       C  
ATOM   4432  O   LEU B 268     -34.529  -1.816  37.716  1.00109.92           O  
ANISOU 4432  O   LEU B 268    12616  16434  12714    814   2747    136       O  
ATOM   4433  CB  LEU B 268     -36.466  -2.653  35.403  1.00107.86           C  
ANISOU 4433  CB  LEU B 268    12128  16028  12826    940   2585   -115       C  
ATOM   4434  CG  LEU B 268     -37.840  -2.517  36.089  1.00114.73           C  
ANISOU 4434  CG  LEU B 268    12752  17065  13775    902   2693   -384       C  
ATOM   4435  CD1 LEU B 268     -38.819  -1.725  35.241  1.00115.82           C  
ANISOU 4435  CD1 LEU B 268    12763  17176  14066   1106   2512   -661       C  
ATOM   4436  CD2 LEU B 268     -38.416  -3.863  36.444  1.00118.24           C  
ANISOU 4436  CD2 LEU B 268    13088  17587  14252    694   2890   -373       C  
ATOM   4437  N   TYR B 269     -35.930  -0.047  37.483  1.00108.01           N  
ANISOU 4437  N   TYR B 269    12206  16226  12606   1022   2615   -261       N  
ATOM   4438  CA  TYR B 269     -35.920   0.425  38.859  1.00108.47           C  
ANISOU 4438  CA  TYR B 269    12218  16443  12554    946   2749   -309       C  
ATOM   4439  C   TYR B 269     -37.331   0.192  39.397  1.00114.12           C  
ANISOU 4439  C   TYR B 269    12680  17315  13365    882   2872   -552       C  
ATOM   4440  O   TYR B 269     -38.289   0.754  38.860  1.00114.70           O  
ANISOU 4440  O   TYR B 269    12613  17387  13581   1024   2763   -805       O  
ATOM   4441  CB  TYR B 269     -35.557   1.919  38.907  1.00109.39           C  
ANISOU 4441  CB  TYR B 269    12427  16518  12618   1089   2627   -396       C  
ATOM   4442  CG  TYR B 269     -34.073   2.208  38.901  1.00109.41           C  
ANISOU 4442  CG  TYR B 269    12654  16445  12470   1071   2594   -187       C  
ATOM   4443  CD1 TYR B 269     -33.333   2.136  37.724  1.00109.92           C  
ANISOU 4443  CD1 TYR B 269    12886  16338  12542   1122   2463    -69       C  
ATOM   4444  CD2 TYR B 269     -33.419   2.618  40.058  1.00110.25           C  
ANISOU 4444  CD2 TYR B 269    12798  16666  12424    998   2693   -141       C  
ATOM   4445  CE1 TYR B 269     -31.967   2.416  37.710  1.00109.42           C  
ANISOU 4445  CE1 TYR B 269    13001  16231  12341   1085   2448     74       C  
ATOM   4446  CE2 TYR B 269     -32.055   2.904  40.057  1.00109.88           C  
ANISOU 4446  CE2 TYR B 269    12929  16577  12243    979   2663      7       C  
ATOM   4447  CZ  TYR B 269     -31.333   2.807  38.878  1.00115.73           C  
ANISOU 4447  CZ  TYR B 269    13815  17158  13000   1018   2546    102       C  
ATOM   4448  OH  TYR B 269     -29.988   3.086  38.872  1.00115.52           O  
ANISOU 4448  OH  TYR B 269    13935  17115  12843    978   2533    203       O  
ATOM   4449  N   LYS B 270     -37.469  -0.695  40.397  1.00111.34           N  
ANISOU 4449  N   LYS B 270    12280  17092  12931    665   3093   -490       N  
ATOM   4450  CA  LYS B 270     -38.759  -1.033  41.005  1.00113.39           C  
ANISOU 4450  CA  LYS B 270    12305  17522  13254    533   3265   -731       C  
ATOM   4451  C   LYS B 270     -38.584  -1.399  42.487  1.00117.94           C  
ANISOU 4451  C   LYS B 270    12923  18245  13645    301   3502   -654       C  
ATOM   4452  O   LYS B 270     -37.785  -2.285  42.794  1.00116.82           O  
ANISOU 4452  O   LYS B 270    12973  18046  13366    177   3574   -381       O  
ATOM   4453  CB  LYS B 270     -39.458  -2.170  40.230  1.00116.50           C  
ANISOU 4453  CB  LYS B 270    12605  17879  13779    456   3302   -765       C  
ATOM   4454  N   PRO B 271     -39.326  -0.751  43.417  1.00116.10           N  
ANISOU 4454  N   PRO B 271    12521  18197  13394    245   3618   -902       N  
ATOM   4455  CA  PRO B 271     -39.175  -1.100  44.839  1.00117.04           C  
ANISOU 4455  CA  PRO B 271    12704  18454  13312      5   3852   -830       C  
ATOM   4456  C   PRO B 271     -39.838  -2.424  45.214  1.00122.54           C  
ANISOU 4456  C   PRO B 271    13381  19209  13970   -282   4088   -832       C  
ATOM   4457  O   PRO B 271     -40.825  -2.823  44.594  1.00123.13           O  
ANISOU 4457  O   PRO B 271    13268  19306  14209   -314   4118  -1031       O  
ATOM   4458  CB  PRO B 271     -39.798   0.090  45.568  1.00120.26           C  
ANISOU 4458  CB  PRO B 271    12921  19037  13734     48   3886  -1129       C  
ATOM   4459  CG  PRO B 271     -40.792   0.640  44.617  1.00125.35           C  
ANISOU 4459  CG  PRO B 271    13327  19681  14619    239   3741  -1441       C  
ATOM   4460  CD  PRO B 271     -40.320   0.326  43.225  1.00118.89           C  
ANISOU 4460  CD  PRO B 271    12630  18641  13903    404   3531  -1270       C  
ATOM   4461  N   ILE B 272     -39.278  -3.103  46.230  1.00119.56           N  
ANISOU 4461  N   ILE B 272    13221  18847  13362   -492   4251   -613       N  
ATOM   4462  CA  ILE B 272     -39.761  -4.386  46.746  1.00152.18           C  
ANISOU 4462  CA  ILE B 272    17436  22999  17389   -804   4494   -568       C  
ATOM   4463  C   ILE B 272     -41.037  -4.161  47.566  1.00182.60           C  
ANISOU 4463  C   ILE B 272    21052  27088  21241  -1026   4740   -920       C  
ATOM   4464  O   ILE B 272     -42.086  -4.715  47.241  1.00144.70           O  
ANISOU 4464  O   ILE B 272    16073  22348  16557  -1174   4870  -1139       O  
ATOM   4465  CB  ILE B 272     -38.642  -5.110  47.555  1.00155.06           C  
ANISOU 4465  CB  ILE B 272    18171  23268  17477   -914   4538   -205       C  
TER    4466      ILE B 272                                                      
ATOM   4467  N   ASN C  25     -38.926  18.473  -5.706  1.00197.19           N  
ANISOU 4467  N   ASN C  25    33921  26524  14479   5947  -3692   1211       N  
ATOM   4468  CA  ASN C  25     -37.594  18.631  -6.283  1.00197.03           C  
ANISOU 4468  CA  ASN C  25    34311  26360  14190   5774  -3065   1493       C  
ATOM   4469  C   ASN C  25     -36.805  19.765  -5.618  1.00198.66           C  
ANISOU 4469  C   ASN C  25    34621  26284  14575   5670  -2576   1878       C  
ATOM   4470  O   ASN C  25     -35.618  19.590  -5.335  1.00197.59           O  
ANISOU 4470  O   ASN C  25    34804  25932  14341   5646  -2026   1989       O  
ATOM   4471  CB  ASN C  25     -37.689  18.869  -7.791  1.00 20.00           C  
ATOM   4472  N   ASN C  26     -37.465  20.918  -5.371  1.00196.30           N  
ANISOU 4472  N   ASN C  26    34424  25873  14290   5912  -2809   2055       N  
ATOM   4473  CA  ASN C  26     -36.868  22.102  -4.743  1.00195.45           C  
ANISOU 4473  CA  ASN C  26    34582  25433  14250   5959  -2418   2399       C  
ATOM   4474  C   ASN C  26     -36.494  21.862  -3.277  1.00196.15           C  
ANISOU 4474  C   ASN C  26    34621  25309  14599   6067  -2225   2298       C  
ATOM   4475  O   ASN C  26     -35.490  22.403  -2.810  1.00195.25           O  
ANISOU 4475  O   ASN C  26    34816  24895  14474   6015  -1668   2552       O  
ATOM   4476  CB  ASN C  26     -37.814  23.299  -4.854  1.00 20.00           C  
ATOM   4477  N   SER C  27     -37.296  21.050  -2.561  1.00192.88           N  
ANISOU 4477  N   SER C  27    34170  24950  14166   6516  -2716   1903       N  
ATOM   4478  CA  SER C  27     -37.066  20.714  -1.158  1.00191.12           C  
ANISOU 4478  CA  SER C  27    34029  24535  14055   6815  -2632   1753       C  
ATOM   4479  C   SER C  27     -36.431  19.323  -1.027  1.00192.57           C  
ANISOU 4479  C   SER C  27    34141  24793  14234   6705  -2434   1521       C  
ATOM   4480  O   SER C  27     -37.126  18.305  -1.105  1.00192.38           O  
ANISOU 4480  O   SER C  27    33835  25008  14254   6807  -2903   1133       O  
ATOM   4481  CB  SER C  27     -38.362  20.820  -0.357  1.00193.46           C  
ANISOU 4481  CB  SER C  27    33710  25016  14781   6914  -3237   1499       C  
ATOM   4482  OG  SER C  27     -39.360  19.947  -0.860  1.00200.73           O  
ANISOU 4482  OG  SER C  27    33747  26395  16126   6443  -3693   1201       O  
ATOM   4483  N   VAL C  28     -35.095  19.292  -0.865  1.00189.12           N  
ANISOU 4483  N   VAL C  28    34307  24040  13510   6779  -1742   1750       N  
ATOM   4484  CA  VAL C  28     -34.305  18.060  -0.728  1.00188.20           C  
ANISOU 4484  CA  VAL C  28    34335  23898  13274   6800  -1430   1599       C  
ATOM   4485  C   VAL C  28     -34.185  17.611   0.740  1.00188.65           C  
ANISOU 4485  C   VAL C  28    34232  23867  13579   6981  -1365   1462       C  
ATOM   4486  O   VAL C  28     -33.889  16.442   0.999  1.00187.91           O  
ANISOU 4486  O   VAL C  28    34134  23820  13442   7092  -1317   1236       O  
ATOM   4487  CB  VAL C  28     -32.921  18.128  -1.436  1.00191.25           C  
ANISOU 4487  CB  VAL C  28    34812  24210  13645   6278   -661   1910       C  
ATOM   4488  CG1 VAL C  28     -33.073  18.121  -2.954  1.00192.58           C  
ANISOU 4488  CG1 VAL C  28    34917  24620  13634   6020   -803   1929       C  
ATOM   4489  CG2 VAL C  28     -32.096  19.328  -0.970  1.00190.75           C  
ANISOU 4489  CG2 VAL C  28    34988  23828  13662   6136    -60   2322       C  
ATOM   4490  N   TYR C  29     -34.415  18.540   1.689  1.00185.00           N  
ANISOU 4490  N   TYR C  29    34016  23177  13098   7348  -1374   1590       N  
ATOM   4491  CA  TYR C  29     -34.366  18.278   3.129  1.00183.24           C  
ANISOU 4491  CA  TYR C  29    33780  22857  12985   7692  -1329   1482       C  
ATOM   4492  C   TYR C  29     -35.569  17.442   3.575  1.00184.61           C  
ANISOU 4492  C   TYR C  29    33291  23406  13447   7861  -2143    967       C  
ATOM   4493  O   TYR C  29     -35.428  16.592   4.455  1.00181.22           O  
ANISOU 4493  O   TYR C  29    32433  23103  13319   7790  -2112    772       O  
ATOM   4494  CB  TYR C  29     -34.308  19.594   3.913  1.00183.68           C  
ANISOU 4494  CB  TYR C  29    33905  22679  13206   7678  -1094   1770       C  
ATOM   4495  N   THR C  30     -36.745  17.684   2.959  1.00182.39           N  
ANISOU 4495  N   THR C  30    32857  23317  13127   8030  -2839    749       N  
ATOM   4496  CA  THR C  30     -37.996  16.969   3.241  1.00182.17           C  
ANISOU 4496  CA  THR C  30    32227  23631  13358   8226  -3644    216       C  
ATOM   4497  C   THR C  30     -37.957  15.538   2.697  1.00184.66           C  
ANISOU 4497  C   THR C  30    32263  24160  13738   7983  -3762    -98       C  
ATOM   4498  O   THR C  30     -38.565  14.648   3.294  1.00184.09           O  
ANISOU 4498  O   THR C  30    31740  24300  13908   8153  -4218   -561       O  
ATOM   4499  CB  THR C  30     -39.212  17.736   2.700  1.00188.73           C  
ANISOU 4499  CB  THR C  30    32300  24716  14693   7696  -4055    247       C  
ATOM   4500  OG1 THR C  30     -39.052  17.954   1.298  1.00190.22           O  
ANISOU 4500  OG1 THR C  30    32720  24921  14634   7417  -3932    465       O  
ATOM   4501  CG2 THR C  30     -39.448  19.058   3.422  1.00188.00           C  
ANISOU 4501  CG2 THR C  30    32306  24452  14675   7915  -4039    468       C  
ATOM   4502  N   SER C  31     -37.250  15.322   1.564  1.00182.59           N  
ANISOU 4502  N   SER C  31    32544  23788  13044   7903  -3433     80       N  
ATOM   4503  CA  SER C  31     -37.102  14.011   0.924  1.00182.79           C  
ANISOU 4503  CA  SER C  31    32513  23953  12986   7782  -3502   -201       C  
ATOM   4504  C   SER C  31     -36.205  13.062   1.733  1.00184.13           C  
ANISOU 4504  C   SER C  31    32681  24035  13245   7780  -3083   -252       C  
ATOM   4505  O   SER C  31     -36.351  11.844   1.610  1.00184.29           O  
ANISOU 4505  O   SER C  31    32510  24197  13315   7786  -3310   -622       O  
ATOM   4506  CB  SER C  31     -36.602  14.153  -0.510  1.00185.84           C  
ANISOU 4506  CB  SER C  31    33013  24370  13227   7255  -3142     76       C  
ATOM   4507  OG  SER C  31     -35.315  14.745  -0.568  1.00189.41           O  
ANISOU 4507  OG  SER C  31    33464  24668  13837   6687  -2293    573       O  
ATOM   4508  N   PHE C  32     -35.293  13.622   2.568  1.00179.29           N  
ANISOU 4508  N   PHE C  32    32456  23144  12521   7954  -2493    100       N  
ATOM   4509  CA  PHE C  32     -34.398  12.871   3.459  1.00172.67           C  
ANISOU 4509  CA  PHE C  32    30933  22367  12308   7282  -1904    196       C  
ATOM   4510  C   PHE C  32     -35.238  12.171   4.532  1.00171.40           C  
ANISOU 4510  C   PHE C  32    29707  22526  12893   6966  -2344   -182       C  
ATOM   4511  O   PHE C  32     -34.946  11.032   4.903  1.00167.59           O  
ANISOU 4511  O   PHE C  32    28716  22164  12795   6588  -2198   -342       O  
ATOM   4512  CB  PHE C  32     -33.365  13.805   4.105  1.00171.52           C  
ANISOU 4512  CB  PHE C  32    30820  21996  12356   6952  -1138    696       C  
ATOM   4513  N   MET C  33     -36.301  12.857   5.000  1.00168.04           N  
ANISOU 4513  N   MET C  33    28985  22213  12650   7148  -2866   -327       N  
ATOM   4514  CA  MET C  33     -37.289  12.352   5.950  1.00164.99           C  
ANISOU 4514  CA  MET C  33    27645  22113  12930   6925  -3320   -712       C  
ATOM   4515  C   MET C  33     -38.420  11.696   5.136  1.00173.60           C  
ANISOU 4515  C   MET C  33    28754  23391  13817   7319  -4125  -1259       C  
ATOM   4516  O   MET C  33     -38.363  11.719   3.903  1.00178.77           O  
ANISOU 4516  O   MET C  33    30196  23946  13784   7775  -4314  -1293       O  
ATOM   4517  CB  MET C  33     -37.828  13.501   6.818  1.00165.84           C  
ANISOU 4517  CB  MET C  33    27461  22233  13318   6956  -3434   -593       C  
ATOM   4518  N   LYS C  34     -39.428  11.098   5.817  1.00168.35           N  
ANISOU 4518  N   LYS C  34    27231  22987  13749   7138  -4579  -1705       N  
ATOM   4519  CA  LYS C  34     -40.589  10.397   5.235  1.00172.46           C  
ANISOU 4519  CA  LYS C  34    27543  23719  14266   7409  -5366  -2322       C  
ATOM   4520  C   LYS C  34     -40.206   9.065   4.567  1.00176.25           C  
ANISOU 4520  C   LYS C  34    28158  24194  14617   7277  -5316  -2555       C  
ATOM   4521  O   LYS C  34     -40.805   8.037   4.885  1.00175.89           O  
ANISOU 4521  O   LYS C  34    27456  24312  15063   7006  -5574  -3005       O  
ATOM   4522  CB  LYS C  34     -41.422  11.288   4.292  1.00181.80           C  
ANISOU 4522  CB  LYS C  34    29294  24918  14862   8156  -6056  -2479       C  
ATOM   4523  N   SER C  35     -39.213   9.082   3.655  1.00173.27           N  
ANISOU 4523  N   SER C  35    28634  23606  13595   7456  -4949  -2255       N  
ATOM   4524  CA  SER C  35     -38.707   7.896   2.959  1.00174.12           C  
ANISOU 4524  CA  SER C  35    28988  23670  13500   7370  -4821  -2419       C  
ATOM   4525  C   SER C  35     -37.891   7.011   3.908  1.00171.65           C  
ANISOU 4525  C   SER C  35    28100  23333  13787   6701  -4171  -2273       C  
ATOM   4526  O   SER C  35     -37.896   5.789   3.756  1.00171.62           O  
ANISOU 4526  O   SER C  35    27890  23366  13951   6503  -4215  -2583       O  
ATOM   4527  CB  SER C  35     -37.863   8.301   1.755  1.00181.40           C  
ANISOU 4527  CB  SER C  35    31018  24357  13548   7774  -4541  -2100       C  
ATOM   4528  OG  SER C  35     -36.780   9.136   2.131  1.00185.72           O  
ANISOU 4528  OG  SER C  35    31761  24708  14097   7513  -3748  -1470       O  
ATOM   4529  N   HIS C  36     -37.198   7.634   4.886  1.00162.85           N  
ANISOU 4529  N   HIS C  36    26747  22146  12984   6377  -3591  -1816       N  
ATOM   4530  CA  HIS C  36     -36.382   6.950   5.890  1.00156.81           C  
ANISOU 4530  CA  HIS C  36    25452  21360  12769   5796  -2986  -1634       C  
ATOM   4531  C   HIS C  36     -37.181   6.721   7.176  1.00156.97           C  
ANISOU 4531  C   HIS C  36    24542  21552  13548   5439  -3167  -1845       C  
ATOM   4532  O   HIS C  36     -37.839   7.642   7.666  1.00156.28           O  
ANISOU 4532  O   HIS C  36    24232  21539  13607   5538  -3405  -1823       O  
ATOM   4533  CB  HIS C  36     -35.100   7.746   6.180  1.00154.58           C  
ANISOU 4533  CB  HIS C  36    25464  20898  12370   5664  -2255  -1050       C  
ATOM   4534  N   ARG C  37     -37.125   5.487   7.710  1.00151.04           N  
ANISOU 4534  N   ARG C  37    23286  20839  13263   5039  -3029  -2046       N  
ATOM   4535  CA  ARG C  37     -37.832   5.079   8.927  1.00147.86           C  
ANISOU 4535  CA  ARG C  37    22040  20557  13581   4660  -3105  -2252       C  
ATOM   4536  C   ARG C  37     -37.094   5.489  10.211  1.00145.67           C  
ANISOU 4536  C   ARG C  37    21436  20240  13672   4303  -2535  -1821       C  
ATOM   4537  O   ARG C  37     -35.921   5.867  10.154  1.00143.30           O  
ANISOU 4537  O   ARG C  37    21492  19818  13136   4284  -2049  -1403       O  
ATOM   4538  CB  ARG C  37     -38.096   3.564   8.908  1.00148.97           C  
ANISOU 4538  CB  ARG C  37    21868  20701  14031   4398  -3174  -2653       C  
ATOM   4539  N   CYS C  38     -37.790   5.411  11.367  1.00139.77           N  
ANISOU 4539  N   CYS C  38    20004  19593  13508   4026  -2594  -1950       N  
ATOM   4540  CA  CYS C  38     -37.260   5.750  12.693  1.00134.42           C  
ANISOU 4540  CA  CYS C  38    18972  18897  13203   3702  -2135  -1612       C  
ATOM   4541  C   CYS C  38     -36.174   4.787  13.176  1.00134.77           C  
ANISOU 4541  C   CYS C  38    18952  18840  13415   3369  -1596  -1421       C  
ATOM   4542  O   CYS C  38     -35.331   5.184  13.983  1.00130.66           O  
ANISOU 4542  O   CYS C  38    18362  18278  13004   3202  -1174  -1060       O  
ATOM   4543  CB  CYS C  38     -38.387   5.872  13.714  1.00134.03           C  
ANISOU 4543  CB  CYS C  38    18267  18973  13683   3538  -2351  -1839       C  
ATOM   4544  SG  CYS C  38     -39.424   7.340  13.503  1.00140.58           S  
ANISOU 4544  SG  CYS C  38    19122  19919  14373   3937  -2855  -1919       S  
ATOM   4545  N   TYR C  39     -36.204   3.526  12.691  1.00132.92           N  
ANISOU 4545  N   TYR C  39    18739  18560  13205   3292  -1634  -1688       N  
ATOM   4546  CA  TYR C  39     -35.262   2.455  13.032  1.00130.52           C  
ANISOU 4546  CA  TYR C  39    18406  18142  13044   3033  -1178  -1570       C  
ATOM   4547  C   TYR C  39     -33.792   2.821  12.770  1.00132.57           C  
ANISOU 4547  C   TYR C  39    19076  18317  12979   3105   -714  -1142       C  
ATOM   4548  O   TYR C  39     -32.924   2.441  13.558  1.00129.08           O  
ANISOU 4548  O   TYR C  39    18458  17826  12760   2881   -287   -919       O  
ATOM   4549  CB  TYR C  39     -35.652   1.141  12.319  1.00135.00           C  
ANISOU 4549  CB  TYR C  39    19034  18648  13611   3013  -1369  -1976       C  
ATOM   4550  CG  TYR C  39     -34.686  -0.003  12.548  1.00135.23           C  
ANISOU 4550  CG  TYR C  39    19107  18531  13742   2806   -916  -1869       C  
ATOM   4551  CD1 TYR C  39     -34.719  -0.744  13.726  1.00134.74           C  
ANISOU 4551  CD1 TYR C  39    18611  18409  14177   2466   -665  -1863       C  
ATOM   4552  CD2 TYR C  39     -33.734  -0.339  11.590  1.00137.38           C  
ANISOU 4552  CD2 TYR C  39    19888  18711  13598   2981   -720  -1768       C  
ATOM   4553  CE1 TYR C  39     -33.820  -1.785  13.950  1.00134.47           C  
ANISOU 4553  CE1 TYR C  39    18653  18225  14215   2330   -264  -1755       C  
ATOM   4554  CE2 TYR C  39     -32.827  -1.375  11.805  1.00137.13           C  
ANISOU 4554  CE2 TYR C  39    19888  18547  13667   2831   -306  -1676       C  
ATOM   4555  CZ  TYR C  39     -32.876  -2.098  12.985  1.00142.20           C  
ANISOU 4555  CZ  TYR C  39    20099  19131  14801   2519   -100  -1670       C  
ATOM   4556  OH  TYR C  39     -31.984  -3.118  13.196  1.00142.68           O  
ANISOU 4556  OH  TYR C  39    20227  19047  14940   2426    286  -1574       O  
ATOM   4557  N   ASP C  40     -33.524   3.554  11.670  1.00131.53           N  
ANISOU 4557  N   ASP C  40    19489  18158  12326   3428   -789  -1044       N  
ATOM   4558  CA  ASP C  40     -32.183   3.988  11.261  1.00130.83           C  
ANISOU 4558  CA  ASP C  40    19823  17970  11916   3504   -319   -670       C  
ATOM   4559  C   ASP C  40     -31.507   4.927  12.270  1.00130.67           C  
ANISOU 4559  C   ASP C  40    19580  17956  12112   3334     32   -299       C  
ATOM   4560  O   ASP C  40     -30.279   4.924  12.371  1.00128.93           O  
ANISOU 4560  O   ASP C  40    19443  17669  11876   3241    511    -35       O  
ATOM   4561  CB  ASP C  40     -32.223   4.625   9.864  1.00137.06           C  
ANISOU 4561  CB  ASP C  40    21298  18699  12080   3903   -482   -663       C  
ATOM   4562  N   LEU C  41     -32.307   5.716  13.015  1.00125.66           N  
ANISOU 4562  N   LEU C  41    18642  17404  11698   3297   -211   -311       N  
ATOM   4563  CA  LEU C  41     -31.829   6.654  14.037  1.00122.17           C  
ANISOU 4563  CA  LEU C  41    17973  16970  11477   3138     47    -14       C  
ATOM   4564  C   LEU C  41     -31.343   5.927  15.292  1.00121.93           C  
ANISOU 4564  C   LEU C  41    17448  16974  11906   2810    321     43       C  
ATOM   4565  O   LEU C  41     -30.428   6.415  15.959  1.00119.28           O  
ANISOU 4565  O   LEU C  41    17008  16623  11690   2678    657    307       O  
ATOM   4566  CB  LEU C  41     -32.937   7.644  14.424  1.00122.44           C  
ANISOU 4566  CB  LEU C  41    17853  17075  11593   3235   -327    -89       C  
ATOM   4567  CG  LEU C  41     -33.411   8.604  13.343  1.00130.90           C  
ANISOU 4567  CG  LEU C  41    19440  18097  12199   3613   -604    -86       C  
ATOM   4568  CD1 LEU C  41     -34.592   9.405  13.829  1.00133.13           C  
ANISOU 4568  CD1 LEU C  41    19519  18502  12562   3789  -1197   -432       C  
ATOM   4569  CD2 LEU C  41     -32.288   9.522  12.897  1.00132.65           C  
ANISOU 4569  CD2 LEU C  41    19878  18213  12310   3639   -336    265       C  
ATOM   4570  N   ILE C  42     -31.974   4.779  15.624  1.00117.94           N  
ANISOU 4570  N   ILE C  42    16654  16502  11656   2686    170   -220       N  
ATOM   4571  CA  ILE C  42     -31.657   3.955  16.797  1.00114.78           C  
ANISOU 4571  CA  ILE C  42    15856  16101  11654   2416    405   -187       C  
ATOM   4572  C   ILE C  42     -30.252   3.328  16.657  1.00117.48           C  
ANISOU 4572  C   ILE C  42    16341  16371  11926   2383    821     -5       C  
ATOM   4573  O   ILE C  42     -29.999   2.636  15.666  1.00119.20           O  
ANISOU 4573  O   ILE C  42    16853  16522  11916   2494    851   -108       O  
ATOM   4574  CB  ILE C  42     -32.766   2.892  17.084  1.00118.76           C  
ANISOU 4574  CB  ILE C  42    16077  16604  12441   2290    175   -530       C  
ATOM   4575  CG1 ILE C  42     -34.171   3.539  17.172  1.00120.41           C  
ANISOU 4575  CG1 ILE C  42    16083  16909  12759   2341   -242   -757       C  
ATOM   4576  CG2 ILE C  42     -32.453   2.076  18.355  1.00117.06           C  
ANISOU 4576  CG2 ILE C  42    15536  16343  12598   2035    459   -458       C  
ATOM   4577  CD1 ILE C  42     -35.344   2.603  16.834  1.00130.55           C  
ANISOU 4577  CD1 ILE C  42    17186  18192  14225   2287   -553  -1198       C  
ATOM   4578  N   PRO C  43     -29.334   3.556  17.634  1.00111.06           N  
ANISOU 4578  N   PRO C  43    15315  15575  11307   2253   1126    237       N  
ATOM   4579  CA  PRO C  43     -27.985   2.967  17.529  1.00110.61           C  
ANISOU 4579  CA  PRO C  43    15328  15472  11226   2251   1501    377       C  
ATOM   4580  C   PRO C  43     -27.962   1.443  17.686  1.00114.26           C  
ANISOU 4580  C   PRO C  43    15723  15865  11827   2201   1559    230       C  
ATOM   4581  O   PRO C  43     -28.914   0.866  18.217  1.00113.50           O  
ANISOU 4581  O   PRO C  43    15443  15747  11935   2094   1375     56       O  
ATOM   4582  CB  PRO C  43     -27.202   3.672  18.641  1.00109.96           C  
ANISOU 4582  CB  PRO C  43    14972  15452  11358   2137   1704    608       C  
ATOM   4583  CG  PRO C  43     -28.223   4.067  19.632  1.00112.74           C  
ANISOU 4583  CG  PRO C  43    15056  15858  11921   2035   1462    554       C  
ATOM   4584  CD  PRO C  43     -29.474   4.365  18.864  1.00110.02           C  
ANISOU 4584  CD  PRO C  43    14868  15513  11422   2129   1122    365       C  
ATOM   4585  N   THR C  44     -26.871   0.800  17.214  1.00111.43           N  
ANISOU 4585  N   THR C  44    15521  15451  11368   2278   1848    293       N  
ATOM   4586  CA  THR C  44     -26.656  -0.655  17.248  1.00111.84           C  
ANISOU 4586  CA  THR C  44    15586  15398  11509   2277   1957    175       C  
ATOM   4587  C   THR C  44     -26.710  -1.210  18.682  1.00113.15           C  
ANISOU 4587  C   THR C  44    15422  15547  12021   2139   2003    218       C  
ATOM   4588  O   THR C  44     -27.295  -2.270  18.897  1.00113.36           O  
ANISOU 4588  O   THR C  44    15441  15454  12175   2071   1950     53       O  
ATOM   4589  CB  THR C  44     -25.365  -1.028  16.495  1.00121.85           C  
ANISOU 4589  CB  THR C  44    17070  16628  12600   2423   2291    263       C  
ATOM   4590  OG1 THR C  44     -25.323  -0.330  15.249  1.00123.71           O  
ANISOU 4590  OG1 THR C  44    17660  16866  12480   2553   2292    265       O  
ATOM   4591  CG2 THR C  44     -25.239  -2.529  16.238  1.00122.19           C  
ANISOU 4591  CG2 THR C  44    17236  16530  12660   2474   2377    106       C  
ATOM   4592  N   SER C  45     -26.119  -0.488  19.650  1.00107.30           N  
ANISOU 4592  N   SER C  45    14442  14907  11422   2100   2106    427       N  
ATOM   4593  CA  SER C  45     -26.125  -0.862  21.065  1.00105.27           C  
ANISOU 4593  CA  SER C  45    13927  14641  11428   2017   2139    494       C  
ATOM   4594  C   SER C  45     -26.340   0.389  21.917  1.00106.64           C  
ANISOU 4594  C   SER C  45    13879  14942  11696   1934   2038    613       C  
ATOM   4595  O   SER C  45     -25.563   1.343  21.822  1.00105.77           O  
ANISOU 4595  O   SER C  45    13726  14929  11532   1967   2118    750       O  
ATOM   4596  CB  SER C  45     -24.835  -1.583  21.445  1.00109.16           C  
ANISOU 4596  CB  SER C  45    14384  15112  11978   2134   2395    606       C  
ATOM   4597  OG  SER C  45     -24.865  -2.023  22.793  1.00116.97           O  
ANISOU 4597  OG  SER C  45    15212  16070  13162   2108   2407    670       O  
ATOM   4598  N   SER C  46     -27.422   0.395  22.718  1.00101.99           N  
ANISOU 4598  N   SER C  46    13155  14336  11261   1814   1885    543       N  
ATOM   4599  CA  SER C  46     -27.796   1.536  23.556  1.00 99.97           C  
ANISOU 4599  CA  SER C  46    12709  14183  11093   1742   1777    625       C  
ATOM   4600  C   SER C  46     -28.154   1.169  25.002  1.00102.35           C  
ANISOU 4600  C   SER C  46    12840  14450  11597   1662   1812    656       C  
ATOM   4601  O   SER C  46     -28.376  -0.002  25.316  1.00102.71           O  
ANISOU 4601  O   SER C  46    12937  14362  11727   1638   1909    595       O  
ATOM   4602  CB  SER C  46     -28.937   2.316  22.907  1.00104.07           C  
ANISOU 4602  CB  SER C  46    13262  14736  11543   1714   1529    495       C  
ATOM   4603  OG  SER C  46     -30.074   1.496  22.693  1.00114.29           O  
ANISOU 4603  OG  SER C  46    14553  15949  12925   1646   1401    259       O  
ATOM   4604  N   LYS C  47     -28.205   2.194  25.874  1.00 97.08           N  
ANISOU 4604  N   LYS C  47    12018  13881  10989   1629   1755    754       N  
ATOM   4605  CA  LYS C  47     -28.534   2.106  27.295  1.00 95.90           C  
ANISOU 4605  CA  LYS C  47    11749  13713  10976   1579   1790    802       C  
ATOM   4606  C   LYS C  47     -29.842   2.864  27.545  1.00 99.23           C  
ANISOU 4606  C   LYS C  47    12056  14164  11484   1471   1642    703       C  
ATOM   4607  O   LYS C  47     -29.943   4.048  27.213  1.00 98.27           O  
ANISOU 4607  O   LYS C  47    11895  14141  11303   1486   1504    719       O  
ATOM   4608  CB  LYS C  47     -27.389   2.707  28.136  1.00 97.34           C  
ANISOU 4608  CB  LYS C  47    11843  13998  11143   1664   1832    971       C  
ATOM   4609  N   LEU C  48     -30.841   2.174  28.113  1.00 96.38           N  
ANISOU 4609  N   LEU C  48    11649  13698  11275   1366   1696    593       N  
ATOM   4610  CA  LEU C  48     -32.145   2.758  28.430  1.00 96.38           C  
ANISOU 4610  CA  LEU C  48    11484  13724  11412   1263   1592    462       C  
ATOM   4611  C   LEU C  48     -32.527   2.423  29.868  1.00100.24           C  
ANISOU 4611  C   LEU C  48    11924  14131  12032   1191   1783    510       C  
ATOM   4612  O   LEU C  48     -32.362   1.282  30.294  1.00100.84           O  
ANISOU 4612  O   LEU C  48    12118  14050  12145   1165   1994    537       O  
ATOM   4613  CB  LEU C  48     -33.219   2.256  27.450  1.00 98.37           C  
ANISOU 4613  CB  LEU C  48    11689  13925  11762   1180   1471    192       C  
ATOM   4614  CG  LEU C  48     -34.643   2.739  27.719  1.00103.72           C  
ANISOU 4614  CG  LEU C  48    12175  14704  12531   1163   1235     19       C  
ATOM   4615  CD1 LEU C  48     -34.739   4.240  27.590  1.00105.64           C  
ANISOU 4615  CD1 LEU C  48    12471  14984  12684   1234    971   -184       C  
ATOM   4616  CD2 LEU C  48     -35.638   2.073  26.795  1.00107.38           C  
ANISOU 4616  CD2 LEU C  48    12414  15098  13288    997   1346   -145       C  
ATOM   4617  N   VAL C  49     -33.026   3.422  30.615  1.00 95.92           N  
ANISOU 4617  N   VAL C  49    11248  13666  11531   1178   1732    528       N  
ATOM   4618  CA  VAL C  49     -33.437   3.267  32.016  1.00 95.98           C  
ANISOU 4618  CA  VAL C  49    11246  13599  11622   1130   1933    578       C  
ATOM   4619  C   VAL C  49     -34.966   3.399  32.115  1.00101.06           C  
ANISOU 4619  C   VAL C  49    11679  14216  12504    982   1954    361       C  
ATOM   4620  O   VAL C  49     -35.545   4.250  31.445  1.00100.64           O  
ANISOU 4620  O   VAL C  49    11459  14283  12497    995   1719    230       O  
ATOM   4621  CB  VAL C  49     -32.678   4.257  32.952  1.00 98.35           C  
ANISOU 4621  CB  VAL C  49    11583  14007  11780   1253   1890    761       C  
ATOM   4622  CG1 VAL C  49     -33.123   4.120  34.409  1.00 98.92           C  
ANISOU 4622  CG1 VAL C  49    11711  13995  11878   1241   2098    811       C  
ATOM   4623  CG2 VAL C  49     -31.166   4.067  32.844  1.00 97.37           C  
ANISOU 4623  CG2 VAL C  49    11588  13923  11487   1392   1862    918       C  
ATOM   4624  N   VAL C  50     -35.613   2.526  32.911  1.00 99.10           N  
ANISOU 4624  N   VAL C  50    11444  13796  12415    852   2251    312       N  
ATOM   4625  CA  VAL C  50     -37.066   2.524  33.125  1.00100.89           C  
ANISOU 4625  CA  VAL C  50    11422  13978  12936    678   2354     77       C  
ATOM   4626  C   VAL C  50     -37.354   2.574  34.632  1.00104.99           C  
ANISOU 4626  C   VAL C  50    12016  14402  13475    651   2678    189       C  
ATOM   4627  O   VAL C  50     -36.823   1.755  35.387  1.00105.07           O  
ANISOU 4627  O   VAL C  50    12311  14240  13372    672   2952    359       O  
ATOM   4628  CB  VAL C  50     -37.781   1.330  32.419  1.00107.47           C  
ANISOU 4628  CB  VAL C  50    12164  14653  14018    479   2453   -176       C  
ATOM   4629  CG1 VAL C  50     -39.256   1.251  32.800  1.00110.17           C  
ANISOU 4629  CG1 VAL C  50    12194  14935  14733    266   2624   -446       C  
ATOM   4630  CG2 VAL C  50     -37.634   1.408  30.903  1.00107.05           C  
ANISOU 4630  CG2 VAL C  50    12052  14712  13911    537   2090   -324       C  
ATOM   4631  N   PHE C  51     -38.190   3.539  35.059  1.00101.54           N  
ANISOU 4631  N   PHE C  51    11358  14066  13155    640   2648     93       N  
ATOM   4632  CA  PHE C  51     -38.582   3.710  36.457  1.00102.23           C  
ANISOU 4632  CA  PHE C  51    11518  14073  13252    626   2967    172       C  
ATOM   4633  C   PHE C  51     -40.022   3.266  36.688  1.00109.12           C  
ANISOU 4633  C   PHE C  51    12128  14827  14507    393   3269    -85       C  
ATOM   4634  O   PHE C  51     -40.905   3.605  35.895  1.00109.73           O  
ANISOU 4634  O   PHE C  51    11829  15016  14849    316   3069   -364       O  
ATOM   4635  CB  PHE C  51     -38.431   5.178  36.901  1.00102.30           C  
ANISOU 4635  CB  PHE C  51    11485  14269  13114    795   2759    248       C  
ATOM   4636  CG  PHE C  51     -37.044   5.771  36.827  1.00101.11           C  
ANISOU 4636  CG  PHE C  51    11544  14231  12642    991   2498    467       C  
ATOM   4637  CD1 PHE C  51     -36.008   5.260  37.599  1.00103.83           C  
ANISOU 4637  CD1 PHE C  51    12208  14497  12747   1096   2622    684       C  
ATOM   4638  CD2 PHE C  51     -36.793   6.893  36.048  1.00101.61           C  
ANISOU 4638  CD2 PHE C  51    11489  14469  12651   1083   2141    443       C  
ATOM   4639  CE1 PHE C  51     -34.731   5.820  37.544  1.00102.79           C  
ANISOU 4639  CE1 PHE C  51    12191  14485  12380   1262   2375    833       C  
ATOM   4640  CE2 PHE C  51     -35.518   7.466  36.009  1.00102.47           C  
ANISOU 4640  CE2 PHE C  51    11756  14659  12518   1218   1957    618       C  
ATOM   4641  CZ  PHE C  51     -34.494   6.920  36.750  1.00100.26           C  
ANISOU 4641  CZ  PHE C  51    11712  14326  12056   1295   2067    793       C  
ATOM   4642  N   ASP C  52     -40.263   2.526  37.786  1.00107.59           N  
ANISOU 4642  N   ASP C  52    12137  14400  14343    294   3757     -3       N  
ATOM   4643  CA  ASP C  52     -41.607   2.098  38.172  1.00111.10           C  
ANISOU 4643  CA  ASP C  52    12339  14695  15181     38   4159   -241       C  
ATOM   4644  C   ASP C  52     -42.201   3.222  39.019  1.00114.86           C  
ANISOU 4644  C   ASP C  52    12677  15291  15674    119   4228   -257       C  
ATOM   4645  O   ASP C  52     -41.563   3.676  39.971  1.00113.18           O  
ANISOU 4645  O   ASP C  52    12799  15077  15127    306   4299     -1       O  
ATOM   4646  CB  ASP C  52     -41.575   0.773  38.954  1.00115.71           C  
ANISOU 4646  CB  ASP C  52    13278  14917  15768   -109   4726   -124       C  
ATOM   4647  CG  ASP C  52     -42.911   0.060  39.013  1.00130.15           C  
ANISOU 4647  CG  ASP C  52    14818  16539  18094   -462   5168   -426       C  
ATOM   4648  OD1 ASP C  52     -43.789   0.505  39.784  1.00132.79           O  
ANISOU 4648  OD1 ASP C  52    14980  16863  18610   -540   5471   -518       O  
ATOM   4649  OD2 ASP C  52     -43.072  -0.957  38.305  1.00137.74           O  
ANISOU 4649  OD2 ASP C  52    15722  17336  19277   -668   5237   -585       O  
ATOM   4650  N   THR C  53     -43.412   3.682  38.661  1.00113.04           N  
ANISOU 4650  N   THR C  53    11950  15170  15830      4   4178   -583       N  
ATOM   4651  CA  THR C  53     -44.139   4.785  39.311  1.00113.51           C  
ANISOU 4651  CA  THR C  53    11797  15357  15975     88   4224   -665       C  
ATOM   4652  C   THR C  53     -44.209   4.709  40.856  1.00118.71           C  
ANISOU 4652  C   THR C  53    12779  15834  16491     94   4773   -478       C  
ATOM   4653  O   THR C  53     -44.388   5.743  41.501  1.00117.96           O  
ANISOU 4653  O   THR C  53    12677  15852  16292    253   4754   -445       O  
ATOM   4654  CB  THR C  53     -45.544   4.928  38.708  1.00124.99           C  
ANISOU 4654  CB  THR C  53    12630  16905  17955    -69   4179  -1100       C  
ATOM   4655  OG1 THR C  53     -46.180   3.649  38.658  1.00128.47           O  
ANISOU 4655  OG1 THR C  53    12929  17117  18767   -399   4589  -1298       O  
ATOM   4656  CG2 THR C  53     -45.527   5.566  37.324  1.00121.90           C  
ANISOU 4656  CG2 THR C  53    11962  16767  17587     77   3520  -1272       C  
ATOM   4657  N   SER C  54     -44.034   3.506  41.438  1.00117.03           N  
ANISOU 4657  N   SER C  54    12907  15324  16237    -51   5256   -347       N  
ATOM   4658  CA  SER C  54     -44.092   3.266  42.884  1.00119.06           C  
ANISOU 4658  CA  SER C  54    13576  15354  16308    -30   5828   -152       C  
ATOM   4659  C   SER C  54     -42.864   3.750  43.689  1.00119.71           C  
ANISOU 4659  C   SER C  54    14214  15476  15794    309   5668    208       C  
ATOM   4660  O   SER C  54     -42.985   3.908  44.907  1.00121.16           O  
ANISOU 4660  O   SER C  54    14725  15539  15772    403   6043    339       O  
ATOM   4661  CB  SER C  54     -44.367   1.792  43.172  1.00126.46           C  
ANISOU 4661  CB  SER C  54    14734  15913  17401   -291   6422   -140       C  
ATOM   4662  OG  SER C  54     -43.486   0.934  42.466  1.00133.55           O  
ANISOU 4662  OG  SER C  54    15855  16729  18160   -283   6214    -25       O  
ATOM   4663  N   LEU C  55     -41.702   3.990  43.038  1.00111.97           N  
ANISOU 4663  N   LEU C  55    13336  14663  14546    495   5129    343       N  
ATOM   4664  CA  LEU C  55     -40.496   4.444  43.749  1.00109.49           C  
ANISOU 4664  CA  LEU C  55    13472  14407  13723    804   4927    625       C  
ATOM   4665  C   LEU C  55     -40.450   5.968  43.958  1.00110.91           C  
ANISOU 4665  C   LEU C  55    13509  14837  13792    980   4591    591       C  
ATOM   4666  O   LEU C  55     -41.052   6.714  43.181  1.00109.61           O  
ANISOU 4666  O   LEU C  55    12900  14848  13897    914   4339    386       O  
ATOM   4667  CB  LEU C  55     -39.196   3.923  43.098  1.00107.03           C  
ANISOU 4667  CB  LEU C  55    13351  14124  13192    918   4588    782       C  
ATOM   4668  CG  LEU C  55     -38.879   4.343  41.663  1.00108.38           C  
ANISOU 4668  CG  LEU C  55    13179  14549  13451    930   4035    687       C  
ATOM   4669  CD1 LEU C  55     -38.289   5.736  41.626  1.00105.81           C  
ANISOU 4669  CD1 LEU C  55    13021  14403  12779   1190   3639    849       C  
ATOM   4670  CD2 LEU C  55     -37.881   3.408  41.051  1.00110.69           C  
ANISOU 4670  CD2 LEU C  55    13456  14756  13848    822   3991    667       C  
ATOM   4671  N   GLN C  56     -39.721   6.413  45.010  1.00106.70           N  
ANISOU 4671  N   GLN C  56    13388  14306  12847   1225   4570    781       N  
ATOM   4672  CA  GLN C  56     -39.540   7.819  45.395  1.00104.84           C  
ANISOU 4672  CA  GLN C  56    13122  14259  12454   1404   4281    762       C  
ATOM   4673  C   GLN C  56     -38.882   8.646  44.289  1.00104.42           C  
ANISOU 4673  C   GLN C  56    12798  14438  12440   1444   3701    716       C  
ATOM   4674  O   GLN C  56     -37.927   8.185  43.663  1.00102.12           O  
ANISOU 4674  O   GLN C  56    12566  14175  12058   1466   3467    810       O  
ATOM   4675  CB  GLN C  56     -38.741   7.928  46.702  1.00107.06           C  
ANISOU 4675  CB  GLN C  56    13944  14478  12256   1666   4332    957       C  
ATOM   4676  N   VAL C  57     -39.403   9.865  44.054  1.00 99.87           N  
ANISOU 4676  N   VAL C  57    11949  14004  11995   1466   3505    572       N  
ATOM   4677  CA  VAL C  57     -38.933  10.785  43.014  1.00 96.71           C  
ANISOU 4677  CA  VAL C  57    11332  13779  11634   1506   3017    527       C  
ATOM   4678  C   VAL C  57     -37.479  11.268  43.272  1.00 98.20           C  
ANISOU 4678  C   VAL C  57    11787  14033  11490   1664   2709    683       C  
ATOM   4679  O   VAL C  57     -36.746  11.481  42.307  1.00 95.69           O  
ANISOU 4679  O   VAL C  57    11369  13805  11184   1652   2393    705       O  
ATOM   4680  CB  VAL C  57     -39.942  11.946  42.772  1.00101.12           C  
ANISOU 4680  CB  VAL C  57    11585  14429  12408   1525   2922    335       C  
ATOM   4681  CG1 VAL C  57     -40.129  12.836  44.003  1.00101.38           C  
ANISOU 4681  CG1 VAL C  57    11812  14473  12233   1692   2916    356       C  
ATOM   4682  CG2 VAL C  57     -39.569  12.768  41.543  1.00 99.06           C  
ANISOU 4682  CG2 VAL C  57    11076  14291  12270   1525   2505    262       C  
ATOM   4683  N   LYS C  58     -37.062  11.388  44.556  1.00 95.56           N  
ANISOU 4683  N   LYS C  58    11793  13651  10867   1813   2812    773       N  
ATOM   4684  CA  LYS C  58     -35.712  11.812  44.952  1.00 94.19           C  
ANISOU 4684  CA  LYS C  58    11841  13545  10400   1973   2509    864       C  
ATOM   4685  C   LYS C  58     -34.660  10.772  44.568  1.00 96.67           C  
ANISOU 4685  C   LYS C  58    12255  13854  10622   1993   2420    988       C  
ATOM   4686  O   LYS C  58     -33.562  11.142  44.151  1.00 94.71           O  
ANISOU 4686  O   LYS C  58    11959  13712  10313   2040   2091   1006       O  
ATOM   4687  CB  LYS C  58     -35.648  12.106  46.458  1.00 98.90           C  
ANISOU 4687  CB  LYS C  58    12799  14088  10690   2160   2631    892       C  
ATOM   4688  N   LYS C  59     -35.006   9.476  44.696  1.00 94.29           N  
ANISOU 4688  N   LYS C  59    12084  13409  10331   1951   2741   1060       N  
ATOM   4689  CA  LYS C  59     -34.137   8.350  44.349  1.00 93.77           C  
ANISOU 4689  CA  LYS C  59    12144  13299  10186   1990   2712   1176       C  
ATOM   4690  C   LYS C  59     -34.010   8.194  42.831  1.00 95.23           C  
ANISOU 4690  C   LYS C  59    11998  13559  10627   1827   2538   1122       C  
ATOM   4691  O   LYS C  59     -32.986   7.703  42.355  1.00 93.96           O  
ANISOU 4691  O   LYS C  59    11868  13434  10399   1887   2373   1192       O  
ATOM   4692  CB  LYS C  59     -34.662   7.051  44.978  1.00 98.96           C  
ANISOU 4692  CB  LYS C  59    13099  13722  10780   1988   3164   1268       C  
ATOM   4693  N   ALA C  60     -35.051   8.614  42.079  1.00 91.09           N  
ANISOU 4693  N   ALA C  60    11168  13061  10382   1652   2565    983       N  
ATOM   4694  CA  ALA C  60     -35.105   8.549  40.617  1.00 89.29           C  
ANISOU 4694  CA  ALA C  60    10664  12899  10365   1524   2389    906       C  
ATOM   4695  C   ALA C  60     -34.145   9.537  39.949  1.00 90.85           C  
ANISOU 4695  C   ALA C  60    10775  13247  10498   1584   2018    922       C  
ATOM   4696  O   ALA C  60     -33.524   9.181  38.949  1.00 89.41           O  
ANISOU 4696  O   ALA C  60    10532  13099  10342   1554   1890    946       O  
ATOM   4697  CB  ALA C  60     -36.527   8.784  40.133  1.00 90.86           C  
ANISOU 4697  CB  ALA C  60    10579  13092  10853   1380   2483    723       C  
ATOM   4698  N   PHE C  61     -34.023  10.770  40.492  1.00 87.04           N  
ANISOU 4698  N   PHE C  61    10303  12831   9936   1658   1878    902       N  
ATOM   4699  CA  PHE C  61     -33.111  11.786  39.954  1.00 85.49           C  
ANISOU 4699  CA  PHE C  61    10046  12733   9703   1682   1581    907       C  
ATOM   4700  C   PHE C  61     -31.660  11.425  40.247  1.00 89.39           C  
ANISOU 4700  C   PHE C  61    10657  13268  10039   1768   1474    996       C  
ATOM   4701  O   PHE C  61     -30.787  11.679  39.417  1.00 88.15           O  
ANISOU 4701  O   PHE C  61    10402  13171   9919   1734   1312   1008       O  
ATOM   4702  CB  PHE C  61     -33.446  13.193  40.475  1.00 87.51           C  
ANISOU 4702  CB  PHE C  61    10297  13008   9943   1723   1484    836       C  
ATOM   4703  CG  PHE C  61     -34.827  13.698  40.125  1.00 89.49           C  
ANISOU 4703  CG  PHE C  61    10396  13240  10368   1687   1541    723       C  
ATOM   4704  CD1 PHE C  61     -35.270  13.710  38.807  1.00 92.08           C  
ANISOU 4704  CD1 PHE C  61    10549  13588  10851   1627   1443    669       C  
ATOM   4705  CD2 PHE C  61     -35.665  14.208  41.107  1.00 92.97           C  
ANISOU 4705  CD2 PHE C  61    10872  13649  10804   1746   1673    652       C  
ATOM   4706  CE1 PHE C  61     -36.547  14.179  38.486  1.00 93.99           C  
ANISOU 4706  CE1 PHE C  61    10620  13832  11259   1642   1440    529       C  
ATOM   4707  CE2 PHE C  61     -36.935  14.688  40.784  1.00 96.65           C  
ANISOU 4707  CE2 PHE C  61    11146  14114  11462   1741   1714    519       C  
ATOM   4708  CZ  PHE C  61     -37.372  14.662  39.477  1.00 94.39           C  
ANISOU 4708  CZ  PHE C  61    10654  13862  11347   1697   1577    450       C  
ATOM   4709  N   PHE C  62     -31.415  10.797  41.415  1.00 87.34           N  
ANISOU 4709  N   PHE C  62    10616  12968   9602   1898   1577   1052       N  
ATOM   4710  CA  PHE C  62     -30.102  10.317  41.849  1.00 87.84           C  
ANISOU 4710  CA  PHE C  62    10799  13077   9499   2049   1452   1114       C  
ATOM   4711  C   PHE C  62     -29.675   9.100  41.014  1.00 91.18           C  
ANISOU 4711  C   PHE C  62    11196  13471   9976   2034   1519   1184       C  
ATOM   4712  O   PHE C  62     -28.480   8.824  40.899  1.00 90.96           O  
ANISOU 4712  O   PHE C  62    11152  13515   9895   2138   1370   1208       O  
ATOM   4713  CB  PHE C  62     -30.134   9.968  43.348  1.00 91.86           C  
ANISOU 4713  CB  PHE C  62    11628  13526   9748   2249   1544   1155       C  
ATOM   4714  CG  PHE C  62     -29.728  11.085  44.285  1.00 94.41           C  
ANISOU 4714  CG  PHE C  62    12021  13926   9925   2362   1330   1071       C  
ATOM   4715  CD1 PHE C  62     -30.467  12.262  44.355  1.00 97.13           C  
ANISOU 4715  CD1 PHE C  62    12280  14272  10354   2262   1323    979       C  
ATOM   4716  CD2 PHE C  62     -28.637  10.941  45.133  1.00 98.43           C  
ANISOU 4716  CD2 PHE C  62    12696  14498  10204   2593   1121   1061       C  
ATOM   4717  CE1 PHE C  62     -30.095  13.290  45.227  1.00 99.19           C  
ANISOU 4717  CE1 PHE C  62    12629  14578  10479   2360   1130    879       C  
ATOM   4718  CE2 PHE C  62     -28.267  11.968  46.006  1.00102.54           C  
ANISOU 4718  CE2 PHE C  62    13280  15087  10592   2694    892    939       C  
ATOM   4719  CZ  PHE C  62     -28.999  13.135  46.049  1.00100.01           C  
ANISOU 4719  CZ  PHE C  62    12888  14748  10363   2562    912    850       C  
ATOM   4720  N   ALA C  63     -30.659   8.388  40.425  1.00 87.43           N  
ANISOU 4720  N   ALA C  63    10695  12893   9632   1905   1740   1188       N  
ATOM   4721  CA  ALA C  63     -30.457   7.219  39.569  1.00 87.11           C  
ANISOU 4721  CA  ALA C  63    10649  12791   9660   1867   1830   1227       C  
ATOM   4722  C   ALA C  63     -30.058   7.626  38.150  1.00 89.31           C  
ANISOU 4722  C   ALA C  63    10699  13164  10071   1764   1663   1180       C  
ATOM   4723  O   ALA C  63     -29.313   6.893  37.497  1.00 88.88           O  
ANISOU 4723  O   ALA C  63    10645  13110  10014   1796   1653   1217       O  
ATOM   4724  CB  ALA C  63     -31.719   6.382  39.531  1.00 88.81           C  
ANISOU 4724  CB  ALA C  63    10911  12843   9989   1742   2127   1200       C  
ATOM   4725  N   LEU C  64     -30.557   8.788  37.673  1.00 84.86           N  
ANISOU 4725  N   LEU C  64     9980  12660   9601   1665   1551   1104       N  
ATOM   4726  CA  LEU C  64     -30.243   9.333  36.348  1.00 83.68           C  
ANISOU 4726  CA  LEU C  64     9696  12569   9529   1591   1417   1076       C  
ATOM   4727  C   LEU C  64     -28.778   9.778  36.291  1.00 87.58           C  
ANISOU 4727  C   LEU C  64    10156  13149   9972   1644   1289   1117       C  
ATOM   4728  O   LEU C  64     -28.148   9.666  35.238  1.00 86.93           O  
ANISOU 4728  O   LEU C  64    10018  13089   9924   1611   1275   1131       O  
ATOM   4729  CB  LEU C  64     -31.168  10.514  36.000  1.00 83.38           C  
ANISOU 4729  CB  LEU C  64     9570  12542   9568   1527   1330    995       C  
ATOM   4730  CG  LEU C  64     -32.641  10.188  35.729  1.00 88.64           C  
ANISOU 4730  CG  LEU C  64    10165  13157  10357   1468   1412    892       C  
ATOM   4731  CD1 LEU C  64     -33.534  11.336  36.145  1.00 89.14           C  
ANISOU 4731  CD1 LEU C  64    10163  13235  10471   1484   1356    814       C  
ATOM   4732  CD2 LEU C  64     -32.878   9.851  34.265  1.00 91.09           C  
ANISOU 4732  CD2 LEU C  64    10415  13466  10728   1423   1339    831       C  
ATOM   4733  N   VAL C  65     -28.241  10.263  37.434  1.00 84.82           N  
ANISOU 4733  N   VAL C  65     9836  12846   9547   1727   1205   1113       N  
ATOM   4734  CA  VAL C  65     -26.856  10.722  37.594  1.00 85.32           C  
ANISOU 4734  CA  VAL C  65     9807  13002   9608   1772   1059   1092       C  
ATOM   4735  C   VAL C  65     -25.887   9.531  37.514  1.00 90.31           C  
ANISOU 4735  C   VAL C  65    10438  13669  10208   1897   1081   1133       C  
ATOM   4736  O   VAL C  65     -24.922   9.584  36.748  1.00 90.15           O  
ANISOU 4736  O   VAL C  65    10267  13707  10277   1867   1055   1115       O  
ATOM   4737  CB  VAL C  65     -26.652  11.556  38.894  1.00 90.13           C  
ANISOU 4737  CB  VAL C  65    10452  13651  10140   1845    919   1026       C  
ATOM   4738  CG1 VAL C  65     -25.211  12.045  39.025  1.00 91.17           C  
ANISOU 4738  CG1 VAL C  65    10422  13889  10329   1866    740    941       C  
ATOM   4739  CG2 VAL C  65     -27.617  12.735  38.960  1.00 89.35           C  
ANISOU 4739  CG2 VAL C  65    10371  13501  10077   1744    913    980       C  
ATOM   4740  N   THR C  66     -26.157   8.463  38.298  1.00 87.94           N  
ANISOU 4740  N   THR C  66    10325  13310   9778   2047   1159   1190       N  
ATOM   4741  CA  THR C  66     -25.344   7.240  38.367  1.00 89.10           C  
ANISOU 4741  CA  THR C  66    10541  13454   9858   2226   1182   1240       C  
ATOM   4742  C   THR C  66     -25.294   6.476  37.037  1.00 92.76           C  
ANISOU 4742  C   THR C  66    10954  13870  10422   2146   1315   1269       C  
ATOM   4743  O   THR C  66     -24.285   5.829  36.751  1.00 93.35           O  
ANISOU 4743  O   THR C  66    10981  13985  10501   2272   1297   1277       O  
ATOM   4744  CB  THR C  66     -25.786   6.337  39.531  1.00 98.49           C  
ANISOU 4744  CB  THR C  66    12039  14530  10851   2413   1281   1317       C  
ATOM   4745  OG1 THR C  66     -27.184   6.066  39.427  1.00 97.52           O  
ANISOU 4745  OG1 THR C  66    12036  14257  10760   2263   1518   1348       O  
ATOM   4746  CG2 THR C  66     -25.464   6.935  40.897  1.00 98.48           C  
ANISOU 4746  CG2 THR C  66    12142  14596  10681   2587   1106   1281       C  
ATOM   4747  N   ASN C  67     -26.370   6.559  36.229  1.00 88.38           N  
ANISOU 4747  N   ASN C  67    10401  13236   9942   1961   1428   1260       N  
ATOM   4748  CA  ASN C  67     -26.457   5.903  34.922  1.00 88.01           C  
ANISOU 4748  CA  ASN C  67    10341  13138   9961   1887   1528   1256       C  
ATOM   4749  C   ASN C  67     -26.024   6.815  33.761  1.00 91.72           C  
ANISOU 4749  C   ASN C  67    10658  13688  10505   1778   1464   1220       C  
ATOM   4750  O   ASN C  67     -25.688   6.317  32.683  1.00 91.47           O  
ANISOU 4750  O   ASN C  67    10629  13639  10487   1768   1536   1219       O  
ATOM   4751  CB  ASN C  67     -27.849   5.311  34.696  1.00 88.42           C  
ANISOU 4751  CB  ASN C  67    10494  13051  10049   1777   1666   1227       C  
ATOM   4752  CG  ASN C  67     -28.150   4.131  35.588  1.00110.88           C  
ANISOU 4752  CG  ASN C  67    13545  15751  12834   1864   1835   1278       C  
ATOM   4753  OD1 ASN C  67     -27.518   3.071  35.502  1.00105.26           O  
ANISOU 4753  OD1 ASN C  67    12954  14970  12071   1984   1911   1328       O  
ATOM   4754  ND2 ASN C  67     -29.133   4.283  36.460  1.00103.12           N  
ANISOU 4754  ND2 ASN C  67    12634  14696  11850   1814   1931   1270       N  
ATOM   4755  N   GLY C  68     -26.020   8.127  34.004  1.00 88.25           N  
ANISOU 4755  N   GLY C  68    10128  13308  10095   1708   1359   1194       N  
ATOM   4756  CA  GLY C  68     -25.602   9.142  33.042  1.00 88.13           C  
ANISOU 4756  CA  GLY C  68    10027  13321  10136   1602   1341   1178       C  
ATOM   4757  C   GLY C  68     -26.579   9.460  31.927  1.00 91.73           C  
ANISOU 4757  C   GLY C  68    10575  13706  10571   1516   1361   1169       C  
ATOM   4758  O   GLY C  68     -26.187  10.086  30.937  1.00 91.66           O  
ANISOU 4758  O   GLY C  68    10586  13684  10557   1462   1392   1182       O  
ATOM   4759  N   VAL C  69     -27.855   9.051  32.073  1.00 88.13           N  
ANISOU 4759  N   VAL C  69    10181  13198  10105   1512   1348   1131       N  
ATOM   4760  CA  VAL C  69     -28.887   9.308  31.064  1.00 88.06           C  
ANISOU 4760  CA  VAL C  69    10229  13145  10086   1472   1299   1072       C  
ATOM   4761  C   VAL C  69     -29.691  10.583  31.424  1.00 91.67           C  
ANISOU 4761  C   VAL C  69    10664  13602  10564   1456   1186   1038       C  
ATOM   4762  O   VAL C  69     -30.021  10.802  32.594  1.00 90.92           O  
ANISOU 4762  O   VAL C  69    10517  13520  10510   1459   1182   1025       O  
ATOM   4763  CB  VAL C  69     -29.767   8.056  30.764  1.00 92.44           C  
ANISOU 4763  CB  VAL C  69    10811  13643  10670   1465   1344    992       C  
ATOM   4764  CG1 VAL C  69     -30.733   7.727  31.903  1.00 92.34           C  
ANISOU 4764  CG1 VAL C  69    10743  13595  10748   1436   1393    941       C  
ATOM   4765  CG2 VAL C  69     -30.502   8.187  29.431  1.00 92.94           C  
ANISOU 4765  CG2 VAL C  69    10930  13684  10697   1464   1242    896       C  
ATOM   4766  N   ARG C  70     -29.949  11.434  30.412  1.00 88.65           N  
ANISOU 4766  N   ARG C  70    10366  13191  10128   1467   1106   1029       N  
ATOM   4767  CA  ARG C  70     -30.663  12.707  30.537  1.00 88.71           C  
ANISOU 4767  CA  ARG C  70    10399  13171  10136   1493    990   1001       C  
ATOM   4768  C   ARG C  70     -32.145  12.527  30.910  1.00 92.67           C  
ANISOU 4768  C   ARG C  70    10803  13687  10720   1532    904    873       C  
ATOM   4769  O   ARG C  70     -32.651  13.260  31.763  1.00 92.17           O  
ANISOU 4769  O   ARG C  70    10685  13625  10710   1549    871    844       O  
ATOM   4770  CB  ARG C  70     -30.501  13.534  29.246  1.00 90.20           C  
ANISOU 4770  CB  ARG C  70    10781  13288  10201   1540    947   1044       C  
ATOM   4771  CG  ARG C  70     -30.950  14.986  29.363  1.00101.83           C  
ANISOU 4771  CG  ARG C  70    12346  14690  11654   1587    854   1051       C  
ATOM   4772  CD  ARG C  70     -30.504  15.831  28.187  1.00113.95           C  
ANISOU 4772  CD  ARG C  70    14156  16102  13037   1630    886   1140       C  
ATOM   4773  NE  ARG C  70     -31.471  16.889  27.884  1.00124.50           N  
ANISOU 4773  NE  ARG C  70    15654  17355  14297   1779    724   1112       N  
ATOM   4774  CZ  ARG C  70     -31.416  18.126  28.367  1.00139.66           C  
ANISOU 4774  CZ  ARG C  70    17656  19169  16238   1774    730   1149       C  
ATOM   4775  NH1 ARG C  70     -30.435  18.485  29.184  1.00126.28           N  
ANISOU 4775  NH1 ARG C  70    15877  17450  14655   1601    876   1193       N  
ATOM   4776  NH2 ARG C  70     -32.342  19.016  28.034  1.00128.37           N  
ANISOU 4776  NH2 ARG C  70    16396  17655  14725   1959    570   1121       N  
ATOM   4777  N   ALA C  71     -32.830  11.561  30.268  1.00 89.75           N  
ANISOU 4777  N   ALA C  71    10394  13324  10382   1539    879    770       N  
ATOM   4778  CA  ALA C  71     -34.247  11.267  30.497  1.00 90.37           C  
ANISOU 4778  CA  ALA C  71    10312  13419  10606   1545    819    595       C  
ATOM   4779  C   ALA C  71     -34.529   9.761  30.490  1.00 94.25           C  
ANISOU 4779  C   ALA C  71    10722  13888  11201   1453    937    507       C  
ATOM   4780  O   ALA C  71     -33.776   8.997  29.883  1.00 93.56           O  
ANISOU 4780  O   ALA C  71    10742  13775  11032   1436    991    560       O  
ATOM   4781  CB  ALA C  71     -35.098  11.965  29.446  1.00 92.59           C  
ANISOU 4781  CB  ALA C  71    10618  13712  10849   1675    579    476       C  
ATOM   4782  N   ALA C  72     -35.615   9.338  31.168  1.00 91.49           N  
ANISOU 4782  N   ALA C  72    10189  13525  11046   1386   1013    364       N  
ATOM   4783  CA  ALA C  72     -36.003   7.929  31.258  1.00 92.17           C  
ANISOU 4783  CA  ALA C  72    10206  13540  11275   1262   1179    261       C  
ATOM   4784  C   ALA C  72     -37.531   7.737  31.322  1.00 97.86           C  
ANISOU 4784  C   ALA C  72    10658  14260  12266   1189   1170     -7       C  
ATOM   4785  O   ALA C  72     -38.187   8.414  32.119  1.00 97.78           O  
ANISOU 4785  O   ALA C  72    10514  14279  12360   1202   1213    -48       O  
ATOM   4786  CB  ALA C  72     -35.337   7.283  32.462  1.00 92.18           C  
ANISOU 4786  CB  ALA C  72    10313  13465  11247   1208   1455    421       C  
ATOM   4787  N   PRO C  73     -38.116   6.824  30.498  1.00 96.04           N  
ANISOU 4787  N   PRO C  73    10323  13995  12172   1110   1117   -222       N  
ATOM   4788  CA  PRO C  73     -39.578   6.628  30.536  1.00 98.56           C  
ANISOU 4788  CA  PRO C  73    10308  14325  12817   1019   1100   -537       C  
ATOM   4789  C   PRO C  73     -40.092   5.994  31.827  1.00103.36           C  
ANISOU 4789  C   PRO C  73    10798  14814  13659    828   1503   -559       C  
ATOM   4790  O   PRO C  73     -39.357   5.264  32.495  1.00102.01           O  
ANISOU 4790  O   PRO C  73    10850  14513  13393    756   1789   -361       O  
ATOM   4791  CB  PRO C  73     -39.847   5.733  29.324  1.00102.16           C  
ANISOU 4791  CB  PRO C  73    10722  14757  13337    970    938   -766       C  
ATOM   4792  CG  PRO C  73     -38.580   4.995  29.114  1.00104.84           C  
ANISOU 4792  CG  PRO C  73    11382  15002  13448    956   1070   -542       C  
ATOM   4793  CD  PRO C  73     -37.488   5.955  29.480  1.00 97.58           C  
ANISOU 4793  CD  PRO C  73    10681  14144  12253   1102   1065   -224       C  
ATOM   4794  N   LEU C  74     -41.360   6.280  32.170  1.00102.15           N  
ANISOU 4794  N   LEU C  74    10308  14698  13806    771   1537   -803       N  
ATOM   4795  CA  LEU C  74     -42.017   5.774  33.376  1.00103.67           C  
ANISOU 4795  CA  LEU C  74    10375  14764  14249    583   1976   -852       C  
ATOM   4796  C   LEU C  74     -42.956   4.607  33.075  1.00110.92           C  
ANISOU 4796  C   LEU C  74    11023  15566  15556    328   2146  -1175       C  
ATOM   4797  O   LEU C  74     -43.673   4.631  32.073  1.00112.43           O  
ANISOU 4797  O   LEU C  74    10918  15859  15942    331   1833  -1494       O  
ATOM   4798  CB  LEU C  74     -42.770   6.902  34.099  1.00104.40           C  
ANISOU 4798  CB  LEU C  74    10262  14958  14446    676   1987   -912       C  
ATOM   4799  CG  LEU C  74     -41.906   8.026  34.670  1.00106.19           C  
ANISOU 4799  CG  LEU C  74    10777  15238  14334    869   1942   -604       C  
ATOM   4800  CD1 LEU C  74     -42.763   9.143  35.225  1.00106.64           C  
ANISOU 4800  CD1 LEU C  74    10654  15448  14414   1066   1651   -711       C  
ATOM   4801  CD2 LEU C  74     -40.946   7.505  35.726  1.00108.82           C  
ANISOU 4801  CD2 LEU C  74    11298  15437  14611    795   2388   -428       C  
ATOM   4802  N   TRP C  75     -42.945   3.590  33.953  1.00108.67           N  
ANISOU 4802  N   TRP C  75    10862  15051  15375    115   2639  -1101       N  
ATOM   4803  CA  TRP C  75     -43.762   2.379  33.847  1.00112.30           C  
ANISOU 4803  CA  TRP C  75    11117  15321  16230   -189   2925  -1385       C  
ATOM   4804  C   TRP C  75     -44.720   2.265  35.033  1.00119.42           C  
ANISOU 4804  C   TRP C  75    11829  16094  17451   -382   3435  -1481       C  
ATOM   4805  O   TRP C  75     -44.340   2.569  36.165  1.00117.81           O  
ANISOU 4805  O   TRP C  75    11899  15828  17034   -303   3724  -1195       O  
ATOM   4806  CB  TRP C  75     -42.853   1.137  33.761  1.00110.40           C  
ANISOU 4806  CB  TRP C  75    11277  14846  15824   -278   3132  -1201       C  
ATOM   4807  CG  TRP C  75     -43.569  -0.184  33.717  1.00115.39           C  
ANISOU 4807  CG  TRP C  75    11789  15211  16843   -614   3489  -1461       C  
ATOM   4808  CD1 TRP C  75     -43.849  -0.999  34.773  1.00120.81           C  
ANISOU 4808  CD1 TRP C  75    12622  15595  17685   -835   4100  -1395       C  
ATOM   4809  CD2 TRP C  75     -44.051  -0.860  32.548  1.00117.66           C  
ANISOU 4809  CD2 TRP C  75    11834  15478  17394   -769   3272  -1832       C  
ATOM   4810  NE1 TRP C  75     -44.498  -2.131  34.340  1.00124.18           N  
ANISOU 4810  NE1 TRP C  75    12887  15795  18500  -1153   4310  -1707       N  
ATOM   4811  CE2 TRP C  75     -44.633  -2.074  32.977  1.00125.58           C  
ANISOU 4811  CE2 TRP C  75    12805  16151  18758  -1122   3785  -1997       C  
ATOM   4812  CE3 TRP C  75     -44.060  -0.553  31.177  1.00118.51           C  
ANISOU 4812  CE3 TRP C  75    11780  15797  17450   -635   2696  -2051       C  
ATOM   4813  CZ2 TRP C  75     -45.215  -2.982  32.084  1.00128.44           C  
ANISOU 4813  CZ2 TRP C  75    12934  16397  19470  -1369   3719  -2403       C  
ATOM   4814  CZ3 TRP C  75     -44.634  -1.455  30.293  1.00123.47           C  
ANISOU 4814  CZ3 TRP C  75    12203  16331  18378   -840   2601  -2448       C  
ATOM   4815  CH2 TRP C  75     -45.205  -2.652  30.747  1.00128.00           C  
ANISOU 4815  CH2 TRP C  75    12701  16585  19349  -1216   3096  -2636       C  
ATOM   4816  N   ASP C  76     -45.956   1.808  34.767  1.00120.50           N  
ANISOU 4816  N   ASP C  76    11497  16185  18101   -635   3555  -1904       N  
ATOM   4817  CA  ASP C  76     -46.983   1.599  35.785  1.00124.28           C  
ANISOU 4817  CA  ASP C  76    11729  16520  18974   -873   4110  -2059       C  
ATOM   4818  C   ASP C  76     -47.295   0.106  35.865  1.00131.85           C  
ANISOU 4818  C   ASP C  76    12714  17135  20249  -1254   4596  -2206       C  
ATOM   4819  O   ASP C  76     -47.721  -0.487  34.870  1.00133.66           O  
ANISOU 4819  O   ASP C  76    12645  17358  20781  -1422   4386  -2561       O  
ATOM   4820  CB  ASP C  76     -48.244   2.418  35.467  1.00128.99           C  
ANISOU 4820  CB  ASP C  76    11668  17357  19987   -855   3873  -2483       C  
ATOM   4821  CG  ASP C  76     -49.218   2.510  36.621  1.00142.96           C  
ANISOU 4821  CG  ASP C  76    13180  19027  22112  -1030   4451  -2602       C  
ATOM   4822  OD1 ASP C  76     -50.036   1.580  36.782  1.00148.30           O  
ANISOU 4822  OD1 ASP C  76    13577  19496  23276  -1396   4897  -2892       O  
ATOM   4823  OD2 ASP C  76     -49.172   3.519  37.356  1.00147.35           O  
ANISOU 4823  OD2 ASP C  76    13814  19699  22473   -812   4481  -2422       O  
ATOM   4824  N   SER C  77     -47.043  -0.504  37.037  1.00129.36           N  
ANISOU 4824  N   SER C  77    12810  16511  19830  -1372   5236  -1928       N  
ATOM   4825  CA  SER C  77     -47.257  -1.933  37.283  1.00133.07           C  
ANISOU 4825  CA  SER C  77    13438  16571  20549  -1725   5806  -1994       C  
ATOM   4826  C   SER C  77     -48.737  -2.326  37.272  1.00143.05           C  
ANISOU 4826  C   SER C  77    14092  17730  22531  -2130   6160  -2500       C  
ATOM   4827  O   SER C  77     -49.066  -3.428  36.830  1.00146.08           O  
ANISOU 4827  O   SER C  77    14381  17863  23259  -2457   6362  -2753       O  
ATOM   4828  CB  SER C  77     -46.602  -2.357  38.593  1.00136.43           C  
ANISOU 4828  CB  SER C  77    14532  16693  20614  -1672   6389  -1538       C  
ATOM   4829  OG  SER C  77     -46.551  -3.769  38.710  1.00148.51           O  
ANISOU 4829  OG  SER C  77    16369  17793  22267  -1942   6880  -1523       O  
ATOM   4830  N   LYS C  78     -49.620  -1.429  37.755  1.00141.30           N  
ANISOU 4830  N   LYS C  78    13439  17691  22558  -2111   6241  -2672       N  
ATOM   4831  CA  LYS C  78     -51.067  -1.651  37.809  1.00147.39           C  
ANISOU 4831  CA  LYS C  78    13530  18410  24061  -2472   6579  -3190       C  
ATOM   4832  C   LYS C  78     -51.713  -1.599  36.420  1.00153.00           C  
ANISOU 4832  C   LYS C  78    13571  19375  25187  -2531   5945  -3738       C  
ATOM   4833  O   LYS C  78     -52.587  -2.418  36.126  1.00158.02           O  
ANISOU 4833  O   LYS C  78    13764  19847  26427  -2928   6187  -4196       O  
ATOM   4834  CB  LYS C  78     -51.736  -0.644  38.757  1.00151.14           C  
ANISOU 4834  CB  LYS C  78    13765  19025  24635  -2369   6837  -3194       C  
ATOM   4835  N   LYS C  79     -51.283  -0.642  35.574  1.00145.43           N  
ANISOU 4835  N   LYS C  79    12560  18797  23899  -2132   5145  -3704       N  
ATOM   4836  CA  LYS C  79     -51.792  -0.455  34.213  1.00146.75           C  
ANISOU 4836  CA  LYS C  79    12200  19237  24320  -2068   4442  -4181       C  
ATOM   4837  C   LYS C  79     -51.112  -1.375  33.189  1.00149.58           C  
ANISOU 4837  C   LYS C  79    12843  19483  24509  -2127   4151  -4198       C  
ATOM   4838  O   LYS C  79     -51.698  -1.644  32.138  1.00152.30           O  
ANISOU 4838  O   LYS C  79    12751  19936  25179  -2207   3732  -4688       O  
ATOM   4839  CB  LYS C  79     -51.662   1.016  33.788  1.00145.90           C  
ANISOU 4839  CB  LYS C  79    11994  19544  23897  -1585   3764  -4115       C  
ATOM   4840  N   GLN C  80     -49.883  -1.856  33.506  1.00142.13           N  
ANISOU 4840  N   GLN C  80    12625  18324  23056  -2064   4360  -3688       N  
ATOM   4841  CA  GLN C  80     -49.038  -2.738  32.682  1.00140.47           C  
ANISOU 4841  CA  GLN C  80    12802  17971  22597  -2076   4168  -3606       C  
ATOM   4842  C   GLN C  80     -48.720  -2.131  31.298  1.00141.95           C  
ANISOU 4842  C   GLN C  80    12909  18498  22526  -1750   3321  -3736       C  
ATOM   4843  O   GLN C  80     -48.738  -2.830  30.279  1.00143.26           O  
ANISOU 4843  O   GLN C  80    13024  18622  22786  -1839   3046  -4019       O  
ATOM   4844  CB  GLN C  80     -49.615  -4.167  32.583  1.00147.25           C  
ANISOU 4844  CB  GLN C  80    13529  18458  23962  -2557   4604  -3952       C  
ATOM   4845  CG  GLN C  80     -49.378  -5.022  33.828  1.00164.00           C  
ANISOU 4845  CG  GLN C  80    16103  20126  26084  -2809   5471  -3631       C  
ATOM   4846  CD  GLN C  80     -47.947  -5.483  33.968  1.00179.12           C  
ANISOU 4846  CD  GLN C  80    18812  21863  27381  -2596   5525  -3093       C  
ATOM   4847  OE1 GLN C  80     -47.444  -6.291  33.179  1.00174.62           O  
ANISOU 4847  OE1 GLN C  80    18463  21161  26724  -2630   5358  -3140       O  
ATOM   4848  NE2 GLN C  80     -47.266  -4.995  34.993  1.00168.08           N  
ANISOU 4848  NE2 GLN C  80    17854  20457  25553  -2358   5760  -2596       N  
ATOM   4849  N   SER C  81     -48.413  -0.816  31.287  1.00134.81           N  
ANISOU 4849  N   SER C  81    12046  17905  21272  -1363   2936  -3517       N  
ATOM   4850  CA  SER C  81     -48.063  -0.016  30.107  1.00132.32           C  
ANISOU 4850  CA  SER C  81    11753  17897  20626   -992   2191  -3550       C  
ATOM   4851  C   SER C  81     -47.351   1.276  30.528  1.00131.23           C  
ANISOU 4851  C   SER C  81    11899  17947  20016   -627   2043  -3111       C  
ATOM   4852  O   SER C  81     -47.557   1.748  31.650  1.00130.33           O  
ANISOU 4852  O   SER C  81    11747  17812  19962   -647   2397  -2950       O  
ATOM   4853  CB  SER C  81     -49.308   0.318  29.288  1.00140.48           C  
ANISOU 4853  CB  SER C  81    12138  19159  22078   -970   1725  -4146       C  
ATOM   4854  OG  SER C  81     -50.274   1.012  30.061  1.00151.70           O  
ANISOU 4854  OG  SER C  81    13092  20691  23858   -992   1892  -4309       O  
ATOM   4855  N   PHE C  82     -46.520   1.846  29.628  1.00124.53           N  
ANISOU 4855  N   PHE C  82    11348  17262  18704   -304   1547  -2931       N  
ATOM   4856  CA  PHE C  82     -45.791   3.094  29.877  1.00120.13           C  
ANISOU 4856  CA  PHE C  82    11068  16863  17714     24   1377  -2547       C  
ATOM   4857  C   PHE C  82     -46.768   4.272  29.928  1.00125.62           C  
ANISOU 4857  C   PHE C  82    11357  17786  18588    208   1110  -2765       C  
ATOM   4858  O   PHE C  82     -47.568   4.445  29.005  1.00128.31           O  
ANISOU 4858  O   PHE C  82    11357  18282  19114    310    672  -3162       O  
ATOM   4859  CB  PHE C  82     -44.700   3.324  28.816  1.00118.96           C  
ANISOU 4859  CB  PHE C  82    11331  16791  17076    281    978  -2338       C  
ATOM   4860  CG  PHE C  82     -43.553   2.342  28.867  1.00118.36           C  
ANISOU 4860  CG  PHE C  82    11693  16514  16766    175   1247  -2055       C  
ATOM   4861  CD1 PHE C  82     -42.485   2.540  29.734  1.00117.85           C  
ANISOU 4861  CD1 PHE C  82    11993  16381  16404    237   1520  -1605       C  
ATOM   4862  CD2 PHE C  82     -43.528   1.233  28.030  1.00122.45           C  
ANISOU 4862  CD2 PHE C  82    12256  16913  17355     44   1193  -2263       C  
ATOM   4863  CE1 PHE C  82     -41.420   1.635  29.776  1.00117.22           C  
ANISOU 4863  CE1 PHE C  82    12293  16130  16117    190   1735  -1366       C  
ATOM   4864  CE2 PHE C  82     -42.459   0.332  28.068  1.00123.53           C  
ANISOU 4864  CE2 PHE C  82    12806  16858  17273    -14   1439  -2006       C  
ATOM   4865  CZ  PHE C  82     -41.416   0.535  28.945  1.00118.15           C  
ANISOU 4865  CZ  PHE C  82    12459  16121  16310     71   1707  -1557       C  
ATOM   4866  N   VAL C  83     -46.727   5.050  31.025  1.00120.52           N  
ANISOU 4866  N   VAL C  83    10751  17154  17888    271   1366  -2530       N  
ATOM   4867  CA  VAL C  83     -47.631   6.182  31.246  1.00121.99           C  
ANISOU 4867  CA  VAL C  83    10577  17527  18246    457   1188  -2709       C  
ATOM   4868  C   VAL C  83     -46.955   7.528  30.935  1.00122.51           C  
ANISOU 4868  C   VAL C  83    10957  17739  17852    845    803  -2429       C  
ATOM   4869  O   VAL C  83     -47.479   8.296  30.126  1.00123.60           O  
ANISOU 4869  O   VAL C  83    10921  18053  17988   1115    321  -2639       O  
ATOM   4870  CB  VAL C  83     -48.278   6.139  32.664  1.00127.62           C  
ANISOU 4870  CB  VAL C  83    11071  18140  19278    256   1764  -2723       C  
ATOM   4871  CG1 VAL C  83     -49.059   7.416  32.976  1.00128.70           C  
ANISOU 4871  CG1 VAL C  83    10901  18466  19532    498   1604  -2853       C  
ATOM   4872  CG2 VAL C  83     -49.179   4.917  32.817  1.00132.07           C  
ANISOU 4872  CG2 VAL C  83    11240  18553  20389   -137   2135  -3092       C  
ATOM   4873  N   GLY C  84     -45.821   7.800  31.579  1.00115.19           N  
ANISOU 4873  N   GLY C  84    10489  16725  16551    878   1013  -1980       N  
ATOM   4874  CA  GLY C  84     -45.105   9.059  31.406  1.00112.19           C  
ANISOU 4874  CA  GLY C  84    10420  16435  15773   1182    738  -1707       C  
ATOM   4875  C   GLY C  84     -43.657   8.966  30.974  1.00112.58           C  
ANISOU 4875  C   GLY C  84    10964  16425  15386   1232    676  -1357       C  
ATOM   4876  O   GLY C  84     -43.191   7.917  30.517  1.00111.79           O  
ANISOU 4876  O   GLY C  84    10984  16242  15249   1093    736  -1345       O  
ATOM   4877  N   MET C  85     -42.946  10.097  31.115  1.00106.91           N  
ANISOU 4877  N   MET C  85    10522  15739  14359   1432    566  -1089       N  
ATOM   4878  CA  MET C  85     -41.540  10.281  30.764  1.00103.71           C  
ANISOU 4878  CA  MET C  85    10545  15290  13568   1496    519   -764       C  
ATOM   4879  C   MET C  85     -40.896  11.197  31.814  1.00105.38           C  
ANISOU 4879  C   MET C  85    10944  15476  13620   1546    676   -497       C  
ATOM   4880  O   MET C  85     -41.344  12.335  31.989  1.00105.47           O  
ANISOU 4880  O   MET C  85    10906  15537  13631   1710    541   -530       O  
ATOM   4881  CB  MET C  85     -41.434  10.903  29.356  1.00106.65           C  
ANISOU 4881  CB  MET C  85    11066  15732  13724   1736     91   -804       C  
ATOM   4882  CG  MET C  85     -40.026  10.969  28.816  1.00107.90           C  
ANISOU 4882  CG  MET C  85    11637  15833  13528   1771     91   -511       C  
ATOM   4883  SD  MET C  85     -39.530   9.432  28.020  1.00112.28           S  
ANISOU 4883  SD  MET C  85    12278  16332  14051   1622    152   -558       S  
ATOM   4884  CE  MET C  85     -37.789   9.545  28.200  1.00105.77           C  
ANISOU 4884  CE  MET C  85    11825  15438  12926   1601    355   -169       C  
ATOM   4885  N   LEU C  86     -39.866  10.698  32.522  1.00 99.91           N  
ANISOU 4885  N   LEU C  86    10466  14702  12795   1425    939   -259       N  
ATOM   4886  CA  LEU C  86     -39.173  11.482  33.545  1.00 98.05           C  
ANISOU 4886  CA  LEU C  86    10410  14445  12400   1469   1055    -42       C  
ATOM   4887  C   LEU C  86     -37.958  12.209  32.968  1.00100.12           C  
ANISOU 4887  C   LEU C  86    10944  14712  12386   1567    881    162       C  
ATOM   4888  O   LEU C  86     -37.030  11.574  32.462  1.00 98.69           O  
ANISOU 4888  O   LEU C  86    10907  14507  12085   1518    900    272       O  
ATOM   4889  CB  LEU C  86     -38.799  10.628  34.772  1.00 97.67           C  
ANISOU 4889  CB  LEU C  86    10445  14311  12356   1332   1415     72       C  
ATOM   4890  CG  LEU C  86     -38.396  11.402  36.036  1.00101.55           C  
ANISOU 4890  CG  LEU C  86    11083  14789  12711   1396   1528    217       C  
ATOM   4891  CD1 LEU C  86     -39.615  11.793  36.863  1.00103.63           C  
ANISOU 4891  CD1 LEU C  86    11163  15051  13159   1406   1684     66       C  
ATOM   4892  CD2 LEU C  86     -37.441  10.593  36.882  1.00103.22           C  
ANISOU 4892  CD2 LEU C  86    11524  14926  12769   1347   1747    399       C  
ATOM   4893  N   THR C  87     -37.987  13.549  33.036  1.00 96.65           N  
ANISOU 4893  N   THR C  87    10572  14284  11868   1703    739    197       N  
ATOM   4894  CA  THR C  87     -36.935  14.441  32.537  1.00 95.40           C  
ANISOU 4894  CA  THR C  87    10669  14090  11489   1773    621    369       C  
ATOM   4895  C   THR C  87     -36.394  15.315  33.679  1.00 98.47           C  
ANISOU 4895  C   THR C  87    11153  14442  11820   1767    712    479       C  
ATOM   4896  O   THR C  87     -36.929  15.270  34.791  1.00 98.28           O  
ANISOU 4896  O   THR C  87    11027  14427  11888   1751    843    421       O  
ATOM   4897  CB  THR C  87     -37.479  15.316  31.385  1.00105.18           C  
ANISOU 4897  CB  THR C  87    11974  15324  12665   1962    348    295       C  
ATOM   4898  OG1 THR C  87     -38.616  16.052  31.840  1.00106.13           O  
ANISOU 4898  OG1 THR C  87    11940  15468  12917   2088    267    149       O  
ATOM   4899  CG2 THR C  87     -37.837  14.510  30.139  1.00105.16           C  
ANISOU 4899  CG2 THR C  87    11939  15360  12656   2000    197    176       C  
ATOM   4900  N   ILE C  88     -35.348  16.129  33.397  1.00 94.50           N  
ANISOU 4900  N   ILE C  88    10853  13882  11169   1775    659    617       N  
ATOM   4901  CA  ILE C  88     -34.756  17.062  34.370  1.00 93.96           C  
ANISOU 4901  CA  ILE C  88    10879  13765  11055   1758    701    681       C  
ATOM   4902  C   ILE C  88     -35.732  18.229  34.623  1.00 98.91           C  
ANISOU 4902  C   ILE C  88    11513  14347  11722   1897    609    590       C  
ATOM   4903  O   ILE C  88     -35.649  18.883  35.664  1.00 98.47           O  
ANISOU 4903  O   ILE C  88    11497  14256  11660   1901    658    582       O  
ATOM   4904  CB  ILE C  88     -33.332  17.563  33.980  1.00 96.61           C  
ANISOU 4904  CB  ILE C  88    11380  14038  11289   1681    702    811       C  
ATOM   4905  CG1 ILE C  88     -32.278  16.432  33.988  1.00 96.48           C  
ANISOU 4905  CG1 ILE C  88    11366  14058  11234   1609    755    882       C  
ATOM   4906  CG2 ILE C  88     -32.901  18.736  34.878  1.00 97.04           C  
ANISOU 4906  CG2 ILE C  88    11448  14087  11338   1612    757    827       C  
ATOM   4907  CD1 ILE C  88     -30.948  16.816  33.365  1.00104.71           C  
ANISOU 4907  CD1 ILE C  88    12569  15015  12200   1560    776    982       C  
ATOM   4908  N   THR C  89     -36.675  18.458  33.674  1.00 96.77           N  
ANISOU 4908  N   THR C  89    11208  14077  11482   2041    455    501       N  
ATOM   4909  CA  THR C  89     -37.731  19.476  33.739  1.00 98.31           C  
ANISOU 4909  CA  THR C  89    11385  14239  11728   2236    331    388       C  
ATOM   4910  C   THR C  89     -38.591  19.238  34.989  1.00102.55           C  
ANISOU 4910  C   THR C  89    11690  14844  12430   2228    472    257       C  
ATOM   4911  O   THR C  89     -38.979  20.201  35.651  1.00103.09           O  
ANISOU 4911  O   THR C  89    11796  14861  12512   2334    474    211       O  
ATOM   4912  CB  THR C  89     -38.569  19.464  32.443  1.00108.31           C  
ANISOU 4912  CB  THR C  89    12624  15534  12994   2426     98    285       C  
ATOM   4913  OG1 THR C  89     -37.700  19.408  31.310  1.00107.58           O  
ANISOU 4913  OG1 THR C  89    12786  15376  12713   2413     38    424       O  
ATOM   4914  CG2 THR C  89     -39.494  20.674  32.324  1.00109.30           C  
ANISOU 4914  CG2 THR C  89    12794  15606  13130   2698    -84    187       C  
ATOM   4915  N   ASP C  90     -38.846  17.952  35.324  1.00 98.60           N  
ANISOU 4915  N   ASP C  90    10989  14430  12044   2098    629    201       N  
ATOM   4916  CA  ASP C  90     -39.604  17.524  36.502  1.00 99.13           C  
ANISOU 4916  CA  ASP C  90    10874  14532  12260   2055    859     95       C  
ATOM   4917  C   ASP C  90     -38.875  17.932  37.786  1.00101.53           C  
ANISOU 4917  C   ASP C  90    11374  14780  12423   2017   1011    208       C  
ATOM   4918  O   ASP C  90     -39.521  18.395  38.726  1.00102.27           O  
ANISOU 4918  O   ASP C  90    11434  14860  12563   2087   1132    126       O  
ATOM   4919  CB  ASP C  90     -39.852  16.005  36.475  1.00101.17           C  
ANISOU 4919  CB  ASP C  90    10958  14834  12649   1895   1035     43       C  
ATOM   4920  CG  ASP C  90     -40.614  15.506  35.259  1.00113.27           C  
ANISOU 4920  CG  ASP C  90    12268  16427  14341   1918    865   -127       C  
ATOM   4921  OD1 ASP C  90     -41.696  16.064  34.961  1.00115.75           O  
ANISOU 4921  OD1 ASP C  90    12376  16791  14812   2065    722   -323       O  
ATOM   4922  OD2 ASP C  90     -40.146  14.541  34.624  1.00119.14           O  
ANISOU 4922  OD2 ASP C  90    13039  17172  15056   1808    861    -87       O  
ATOM   4923  N   PHE C  91     -37.528  17.800  37.802  1.00 95.99           N  
ANISOU 4923  N   PHE C  91    10870  14052  11551   1926    988    370       N  
ATOM   4924  CA  PHE C  91     -36.665  18.184  38.925  1.00 95.20           C  
ANISOU 4924  CA  PHE C  91    10954  13914  11303   1905   1050    445       C  
ATOM   4925  C   PHE C  91     -36.672  19.704  39.117  1.00 99.12           C  
ANISOU 4925  C   PHE C  91    11575  14329  11758   2003    927    410       C  
ATOM   4926  O   PHE C  91     -36.614  20.172  40.253  1.00 99.37           O  
ANISOU 4926  O   PHE C  91    11710  14329  11716   2039    994    376       O  
ATOM   4927  CB  PHE C  91     -35.237  17.636  38.726  1.00 95.65           C  
ANISOU 4927  CB  PHE C  91    11111  13985  11246   1798   1014    577       C  
ATOM   4928  CG  PHE C  91     -34.213  17.969  39.790  1.00 97.26           C  
ANISOU 4928  CG  PHE C  91    11468  14178  11310   1791   1003    612       C  
ATOM   4929  CD1 PHE C  91     -34.361  17.505  41.093  1.00101.16           C  
ANISOU 4929  CD1 PHE C  91    12043  14686  11708   1843   1144    596       C  
ATOM   4930  CD2 PHE C  91     -33.064  18.681  39.471  1.00 99.17           C  
ANISOU 4930  CD2 PHE C  91    11779  14387  11513   1732    859    646       C  
ATOM   4931  CE1 PHE C  91     -33.402  17.793  42.069  1.00102.61           C  
ANISOU 4931  CE1 PHE C  91    12384  14873  11729   1879   1071    597       C  
ATOM   4932  CE2 PHE C  91     -32.103  18.966  40.446  1.00102.58           C  
ANISOU 4932  CE2 PHE C  91    12300  14826  11848   1725    801    621       C  
ATOM   4933  CZ  PHE C  91     -32.277  18.517  41.738  1.00101.45           C  
ANISOU 4933  CZ  PHE C  91    12245  14720  11581   1817    874    590       C  
ATOM   4934  N   ILE C  92     -36.784  20.464  38.005  1.00 95.37           N  
ANISOU 4934  N   ILE C  92    11131  13797  11308   2065    755    413       N  
ATOM   4935  CA  ILE C  92     -36.872  21.928  37.997  1.00 96.04           C  
ANISOU 4935  CA  ILE C  92    11377  13753  11360   2175    648    387       C  
ATOM   4936  C   ILE C  92     -38.244  22.337  38.563  1.00101.05           C  
ANISOU 4936  C   ILE C  92    11899  14400  12094   2353    688    236       C  
ATOM   4937  O   ILE C  92     -38.310  23.219  39.421  1.00101.55           O  
ANISOU 4937  O   ILE C  92    12084  14383  12116   2420    719    187       O  
ATOM   4938  CB  ILE C  92     -36.616  22.497  36.567  1.00 99.46           C  
ANISOU 4938  CB  ILE C  92    11945  14090  11754   2220    489    460       C  
ATOM   4939  CG1 ILE C  92     -35.168  22.220  36.106  1.00 98.72           C  
ANISOU 4939  CG1 ILE C  92    11960  13964  11583   2028    516    598       C  
ATOM   4940  CG2 ILE C  92     -36.947  23.997  36.478  1.00101.93           C  
ANISOU 4940  CG2 ILE C  92    12466  14227  12038   2381    396    432       C  
ATOM   4941  CD1 ILE C  92     -34.978  22.058  34.602  1.00106.47           C  
ANISOU 4941  CD1 ILE C  92    13031  14911  12513   2047    448    684       C  
ATOM   4942  N   ASN C  93     -39.324  21.665  38.098  1.00 97.93           N  
ANISOU 4942  N   ASN C  93    11250  14108  11850   2422    695    134       N  
ATOM   4943  CA  ASN C  93     -40.710  21.899  38.519  1.00 99.66           C  
ANISOU 4943  CA  ASN C  93    11259  14370  12237   2585    754    -51       C  
ATOM   4944  C   ASN C  93     -40.945  21.628  40.009  1.00103.50           C  
ANISOU 4944  C   ASN C  93    11717  14873  12735   2532   1045    -99       C  
ATOM   4945  O   ASN C  93     -41.793  22.287  40.612  1.00105.02           O  
ANISOU 4945  O   ASN C  93    11854  15046  13004   2683   1121   -229       O  
ATOM   4946  CB  ASN C  93     -41.690  21.100  37.653  1.00101.52           C  
ANISOU 4946  CB  ASN C  93    11171  14725  12675   2625    688   -190       C  
ATOM   4947  CG  ASN C  93     -41.814  21.601  36.231  1.00125.10           C  
ANISOU 4947  CG  ASN C  93    14217  17693  15623   2796    363   -198       C  
ATOM   4948  OD1 ASN C  93     -42.047  22.788  35.972  1.00121.19           O  
ANISOU 4948  OD1 ASN C  93    13877  17104  15066   3019    198   -210       O  
ATOM   4949  ND2 ASN C  93     -41.706  20.693  35.272  1.00116.23           N  
ANISOU 4949  ND2 ASN C  93    13007  16641  14514   2723    268   -197       N  
ATOM   4950  N   ILE C  94     -40.291  20.606  40.535  1.00 98.28           N  
ANISOU 4950  N   ILE C  94    11130  14236  11975   2353   1212      6       N  
ATOM   4951  CA  ILE C  94     -40.438  20.276  41.935  1.00 98.73           C  
ANISOU 4951  CA  ILE C  94    11268  14284  11960   2329   1498     -6       C  
ATOM   4952  C   ILE C  94     -39.876  21.376  42.812  1.00102.62           C  
ANISOU 4952  C   ILE C  94    12057  14687  12248   2405   1428     17       C  
ATOM   4953  O   ILE C  94     -40.494  21.780  43.791  1.00104.00           O  
ANISOU 4953  O   ILE C  94    12282  14825  12406   2520   1578    -82       O  
ATOM   4954  CB  ILE C  94     -39.706  18.969  42.284  1.00100.85           C  
ANISOU 4954  CB  ILE C  94    11572  14585  12160   2166   1681    101       C  
ATOM   4955  CG1 ILE C  94     -40.350  17.768  41.585  1.00102.07           C  
ANISOU 4955  CG1 ILE C  94    11422  14792  12568   2080   1837     14       C  
ATOM   4956  CG2 ILE C  94     -39.698  18.762  43.785  1.00102.59           C  
ANISOU 4956  CG2 ILE C  94    12034  14761  12184   2191   1931    136       C  
ATOM   4957  CD1 ILE C  94     -39.531  16.495  41.669  1.00108.04           C  
ANISOU 4957  CD1 ILE C  94    12207  15553  13290   1918   1914    127       C  
ATOM   4958  N   LEU C  95     -38.697  21.861  42.452  1.00 97.62           N  
ANISOU 4958  N   LEU C  95    11602  14010  11481   2333   1214    120       N  
ATOM   4959  CA  LEU C  95     -38.001  22.825  43.287  1.00 97.85           C  
ANISOU 4959  CA  LEU C  95    11887  13940  11352   2359   1111    107       C  
ATOM   4960  C   LEU C  95     -38.697  24.165  43.422  1.00103.43           C  
ANISOU 4960  C   LEU C  95    12657  14527  12113   2512   1034      4       C  
ATOM   4961  O   LEU C  95     -38.789  24.710  44.518  1.00104.42           O  
ANISOU 4961  O   LEU C  95    12943  14587  12145   2602   1095    -86       O  
ATOM   4962  CB  LEU C  95     -36.574  23.022  42.794  1.00 96.47           C  
ANISOU 4962  CB  LEU C  95    11805  13743  11107   2209    924    204       C  
ATOM   4963  CG  LEU C  95     -35.715  21.770  42.923  1.00100.06           C  
ANISOU 4963  CG  LEU C  95    12243  14301  11472   2101    959    292       C  
ATOM   4964  CD1 LEU C  95     -34.356  21.992  42.281  1.00 99.02           C  
ANISOU 4964  CD1 LEU C  95    12084  14167  11374   1960    802    372       C  
ATOM   4965  CD2 LEU C  95     -35.567  21.381  44.382  1.00103.79           C  
ANISOU 4965  CD2 LEU C  95    12906  14785  11743   2154    988    243       C  
ATOM   4966  N   HIS C  96     -39.198  24.700  42.316  1.00100.23           N  
ANISOU 4966  N   HIS C  96    12161  14085  11835   2578    899     10       N  
ATOM   4967  CA  HIS C  96     -39.843  25.996  42.384  1.00101.94           C  
ANISOU 4967  CA  HIS C  96    12472  14165  12095   2776    804    -74       C  
ATOM   4968  C   HIS C  96     -41.069  25.885  43.265  1.00108.13           C  
ANISOU 4968  C   HIS C  96    13078  15003  13002   2985    946   -237       C  
ATOM   4969  O   HIS C  96     -41.326  26.739  44.108  1.00109.59           O  
ANISOU 4969  O   HIS C  96    13282  15101  13256   3205    851   -323       O  
ATOM   4970  CB  HIS C  96     -40.240  26.478  40.991  1.00102.59           C  
ANISOU 4970  CB  HIS C  96    12587  14174  12219   2826    601      0       C  
ATOM   4971  N   ARG C  97     -41.826  24.815  43.068  1.00104.97           N  
ANISOU 4971  N   ARG C  97    12524  14728  12631   2929   1200   -283       N  
ATOM   4972  CA  ARG C  97     -43.031  24.598  43.847  1.00107.27           C  
ANISOU 4972  CA  ARG C  97    12607  15074  13076   3083   1426   -450       C  
ATOM   4973  C   ARG C  97     -42.780  24.357  45.327  1.00112.23           C  
ANISOU 4973  C   ARG C  97    13350  15713  13579   3036   1758   -471       C  
ATOM   4974  O   ARG C  97     -43.488  24.893  46.170  1.00114.21           O  
ANISOU 4974  O   ARG C  97    13609  15929  13856   3196   1946   -605       O  
ATOM   4975  CB  ARG C  97     -43.833  23.433  43.268  1.00108.08           C  
ANISOU 4975  CB  ARG C  97    12296  15318  13452   3081   1451   -532       C  
ATOM   4976  N   TYR C  98     -41.781  23.542  45.646  1.00107.50           N  
ANISOU 4976  N   TYR C  98    12866  15154  12827   2852   1841   -339       N  
ATOM   4977  CA  TYR C  98     -41.622  23.080  47.021  1.00108.63           C  
ANISOU 4977  CA  TYR C  98    13200  15290  12784   2841   2153   -329       C  
ATOM   4978  C   TYR C  98     -40.483  23.665  47.845  1.00112.39           C  
ANISOU 4978  C   TYR C  98    14088  15689  12925   2867   2028   -289       C  
ATOM   4979  O   TYR C  98     -40.506  23.585  49.069  1.00113.71           O  
ANISOU 4979  O   TYR C  98    14491  15830  12885   2945   2260   -316       O  
ATOM   4980  CB  TYR C  98     -41.535  21.558  47.049  1.00109.22           C  
ANISOU 4980  CB  TYR C  98    13175  15436  12889   2676   2365   -229       C  
ATOM   4981  CG  TYR C  98     -42.801  20.879  46.599  1.00112.30           C  
ANISOU 4981  CG  TYR C  98    13155  15888  13625   2628   2578   -331       C  
ATOM   4982  CD1 TYR C  98     -43.821  20.612  47.498  1.00112.76           C  
ANISOU 4982  CD1 TYR C  98    12965  16016  13862   2489   2440   -295       C  
ATOM   4983  CD2 TYR C  98     -42.975  20.502  45.278  1.00116.20           C  
ANISOU 4983  CD2 TYR C  98    13495  16373  14284   2714   2931   -493       C  
ATOM   4984  CE1 TYR C  98     -44.984  19.992  47.090  1.00115.20           C  
ANISOU 4984  CE1 TYR C  98    12870  16385  14515   2430   2605   -440       C  
ATOM   4985  CE2 TYR C  98     -44.133  19.881  44.862  1.00118.82           C  
ANISOU 4985  CE2 TYR C  98    13383  16770  14994   2643   3130   -639       C  
ATOM   4986  CZ  TYR C  98     -45.133  19.629  45.772  1.00124.76           C  
ANISOU 4986  CZ  TYR C  98    13881  17593  15929   2497   2945   -624       C  
ATOM   4987  OH  TYR C  98     -46.285  19.009  45.356  1.00127.88           O  
ANISOU 4987  OH  TYR C  98    13811  18054  16723   2417   3104   -818       O  
ATOM   4988  N   TYR C  99     -39.487  24.250  47.198  1.00107.37           N  
ANISOU 4988  N   TYR C  99    13546  15012  12238   2802   1677   -245       N  
ATOM   4989  CA  TYR C  99     -38.359  24.797  47.965  1.00107.50           C  
ANISOU 4989  CA  TYR C  99    13883  14963  11998   2798   1505   -264       C  
ATOM   4990  C   TYR C  99     -38.773  25.966  48.859  1.00113.87           C  
ANISOU 4990  C   TYR C  99    14914  15650  12700   2969   1541   -422       C  
ATOM   4991  O   TYR C  99     -39.313  26.962  48.371  1.00114.03           O  
ANISOU 4991  O   TYR C  99    14881  15575  12871   3049   1473   -498       O  
ATOM   4992  CB  TYR C  99     -37.179  25.169  47.046  1.00106.86           C  
ANISOU 4992  CB  TYR C  99    13783  14853  11967   2642   1179   -205       C  
ATOM   4993  CG  TYR C  99     -36.009  25.829  47.746  1.00109.43           C  
ANISOU 4993  CG  TYR C  99    14357  15109  12111   2606    971   -288       C  
ATOM   4994  CD1 TYR C  99     -35.096  25.079  48.480  1.00111.53           C  
ANISOU 4994  CD1 TYR C  99    14734  15468  12174   2582    910   -274       C  
ATOM   4995  CD2 TYR C  99     -35.780  27.196  47.624  1.00111.22           C  
ANISOU 4995  CD2 TYR C  99    14705  15168  12387   2599    812   -398       C  
ATOM   4996  CE1 TYR C  99     -34.011  25.679  49.114  1.00113.63           C  
ANISOU 4996  CE1 TYR C  99    15178  15695  12302   2559    664   -405       C  
ATOM   4997  CE2 TYR C  99     -34.697  27.808  48.253  1.00113.37           C  
ANISOU 4997  CE2 TYR C  99    15165  15369  12540   2531    610   -525       C  
ATOM   4998  CZ  TYR C  99     -33.812  27.045  48.995  1.00120.85           C  
ANISOU 4998  CZ  TYR C  99    16169  16446  13304   2511    517   -545       C  
ATOM   4999  OH  TYR C  99     -32.740  27.641  49.613  1.00123.47           O  
ANISOU 4999  OH  TYR C  99    16639  16730  13546   2455    266   -722       O  
ATOM   5000  N   LYS C 100     -38.515  25.828  50.171  1.00112.23           N  
ANISOU 5000  N   LYS C 100    14999  15437  12206   3056   1643   -475       N  
ATOM   5001  CA  LYS C 100     -38.839  26.834  51.179  1.00114.85           C  
ANISOU 5001  CA  LYS C 100    15607  15654  12375   3234   1696   -640       C  
ATOM   5002  C   LYS C 100     -37.630  27.717  51.491  1.00119.28           C  
ANISOU 5002  C   LYS C 100    16416  16123  12781   3189   1343   -744       C  
ATOM   5003  O   LYS C 100     -37.702  28.928  51.289  1.00119.71           O  
ANISOU 5003  O   LYS C 100    16531  16028  12927   3213   1217   -859       O  
ATOM   5004  CB  LYS C 100     -39.395  26.173  52.451  1.00119.76           C  
ANISOU 5004  CB  LYS C 100    16451  16306  12748   3384   2059   -654       C  
ATOM   5005  N   SER C 101     -36.521  27.109  51.975  1.00115.77           N  
ANISOU 5005  N   SER C 101    16110  15757  12120   3131   1179   -724       N  
ATOM   5006  CA  SER C 101     -35.271  27.794  52.331  1.00116.63           C  
ANISOU 5006  CA  SER C 101    16389  15812  12112   3068    816   -873       C  
ATOM   5007  C   SER C 101     -34.112  26.800  52.497  1.00120.15           C  
ANISOU 5007  C   SER C 101    16825  16408  12419   3004    626   -816       C  
ATOM   5008  O   SER C 101     -34.320  25.588  52.405  1.00118.53           O  
ANISOU 5008  O   SER C 101    16548  16320  12169   3028    802   -643       O  
ATOM   5009  CB  SER C 101     -35.448  28.598  53.618  1.00123.44           C  
ANISOU 5009  CB  SER C 101    17631  16570  12699   3264    816  -1085       C  
ATOM   5010  OG  SER C 101     -34.348  29.464  53.842  1.00133.34           O  
ANISOU 5010  OG  SER C 101    19000  17739  13924   3173    446  -1289       O  
ATOM   5011  N   ALA C 102     -32.895  27.319  52.753  1.00118.19           N  
ANISOU 5011  N   ALA C 102    16639  16145  12121   2930    264   -987       N  
ATOM   5012  CA  ALA C 102     -31.688  26.519  52.973  1.00118.31           C  
ANISOU 5012  CA  ALA C 102    16622  16312  12018   2911     10   -997       C  
ATOM   5013  C   ALA C 102     -31.702  25.834  54.346  1.00125.01           C  
ANISOU 5013  C   ALA C 102    17845  17242  12413   3204     29  -1029       C  
ATOM   5014  O   ALA C 102     -30.992  24.845  54.547  1.00124.71           O  
ANISOU 5014  O   ALA C 102    17821  17340  12223   3277    -98   -968       O  
ATOM   5015  CB  ALA C 102     -30.452  27.395  52.835  1.00120.34           C  
ANISOU 5015  CB  ALA C 102    16777  16524  12424   2733   -376  -1230       C  
ATOM   5016  N   LEU C 103     -32.517  26.360  55.280  1.00124.16           N  
ANISOU 5016  N   LEU C 103    18072  17033  12069   3399    204  -1122       N  
ATOM   5017  CA  LEU C 103     -32.663  25.866  56.651  1.00127.21           C  
ANISOU 5017  CA  LEU C 103    18922  17447  11963   3713    285  -1155       C  
ATOM   5018  C   LEU C 103     -33.730  24.772  56.749  1.00130.96           C  
ANISOU 5018  C   LEU C 103    19484  17932  12341   3819    796   -893       C  
ATOM   5019  O   LEU C 103     -33.500  23.756  57.408  1.00131.93           O  
ANISOU 5019  O   LEU C 103    19885  18112  12129   4004    864   -792       O  
ATOM   5020  CB  LEU C 103     -33.002  27.026  57.613  1.00130.53           C  
ANISOU 5020  CB  LEU C 103    19692  17732  12170   3870    254  -1405       C  
ATOM   5021  CG  LEU C 103     -32.247  28.348  57.418  1.00136.09           C  
ANISOU 5021  CG  LEU C 103    20294  18345  13069   3707   -148  -1692       C  
ATOM   5022  CD1 LEU C 103     -33.023  29.506  57.994  1.00138.53           C  
ANISOU 5022  CD1 LEU C 103    20872  18467  13298   3816    -15  -1869       C  
ATOM   5023  CD2 LEU C 103     -30.848  28.289  58.002  1.00141.10           C  
ANISOU 5023  CD2 LEU C 103    21015  19081  13514   3753   -659  -1925       C  
ATOM   5024  N   VAL C 104     -34.892  24.984  56.101  1.00126.34           N  
ANISOU 5024  N   VAL C 104    18668  17279  12057   3709   1154   -801       N  
ATOM   5025  CA  VAL C 104     -36.016  24.043  56.098  1.00126.17           C  
ANISOU 5025  CA  VAL C 104    18631  17251  12057   3747   1676   -605       C  
ATOM   5026  C   VAL C 104     -35.817  23.007  54.986  1.00127.30           C  
ANISOU 5026  C   VAL C 104    18405  17486  12475   3545   1693   -402       C  
ATOM   5027  O   VAL C 104     -35.650  23.376  53.822  1.00124.09           O  
ANISOU 5027  O   VAL C 104    17611  17106  12432   3337   1515   -397       O  
ATOM   5028  CB  VAL C 104     -37.393  24.766  55.994  1.00130.71           C  
ANISOU 5028  CB  VAL C 104    19092  17728  12844   3759   2029   -664       C  
ATOM   5029  CG1 VAL C 104     -38.555  23.775  56.060  1.00131.08           C  
ANISOU 5029  CG1 VAL C 104    19073  17768  12961   3773   2596   -515       C  
ATOM   5030  CG2 VAL C 104     -37.544  25.833  57.076  1.00133.93           C  
ANISOU 5030  CG2 VAL C 104    19886  18028  12971   3970   2009   -879       C  
ATOM   5031  N   GLN C 105     -35.830  21.713  55.356  1.00125.02           N  
ANISOU 5031  N   GLN C 105    18290  17222  11989   3623   1925   -234       N  
ATOM   5032  CA  GLN C 105     -35.676  20.589  54.428  1.00122.56           C  
ANISOU 5032  CA  GLN C 105    17699  16974  11894   3459   1987    -46       C  
ATOM   5033  C   GLN C 105     -36.890  20.487  53.508  1.00125.29           C  
ANISOU 5033  C   GLN C 105    17652  17294  12658   3275   2321      6       C  
ATOM   5034  O   GLN C 105     -38.013  20.741  53.950  1.00126.67           O  
ANISOU 5034  O   GLN C 105    17873  17395  12862   3337   2690    -46       O  
ATOM   5035  CB  GLN C 105     -35.518  19.266  55.196  1.00125.91           C  
ANISOU 5035  CB  GLN C 105    18498  17370  11970   3623   2218    115       C  
ATOM   5036  CG  GLN C 105     -34.183  19.096  55.908  1.00144.79           C  
ANISOU 5036  CG  GLN C 105    21227  19824  13964   3839   1804     76       C  
ATOM   5037  N   ILE C 106     -36.671  20.109  52.237  1.00119.26           N  
ANISOU 5037  N   ILE C 106    16498  16599  12217   3069   2190     85       N  
ATOM   5038  CA  ILE C 106     -37.760  19.935  51.272  1.00118.00           C  
ANISOU 5038  CA  ILE C 106    15945  16437  12452   2914   2426    104       C  
ATOM   5039  C   ILE C 106     -38.390  18.561  51.558  1.00123.66           C  
ANISOU 5039  C   ILE C 106    16721  17110  13155   2890   2884    226       C  
ATOM   5040  O   ILE C 106     -38.012  17.555  50.950  1.00121.70           O  
ANISOU 5040  O   ILE C 106    16365  16889  12988   2776   2872    347       O  
ATOM   5041  CB  ILE C 106     -37.302  20.129  49.789  1.00117.88           C  
ANISOU 5041  CB  ILE C 106    15550  16494  12743   2729   2102    125       C  
ATOM   5042  CG1 ILE C 106     -36.866  21.587  49.509  1.00117.69           C  
ANISOU 5042  CG1 ILE C 106    15558  16465  12694   2730   1691     24       C  
ATOM   5043  CG2 ILE C 106     -38.403  19.690  48.809  1.00117.99           C  
ANISOU 5043  CG2 ILE C 106    15184  16514  13132   2635   2270     89       C  
ATOM   5044  CD1 ILE C 106     -36.162  21.799  48.171  1.00122.46           C  
ANISOU 5044  CD1 ILE C 106    15996  17131  13403   2577   1370     86       C  
ATOM   5045  N   TYR C 107     -39.324  18.529  52.535  1.00123.89           N  
ANISOU 5045  N   TYR C 107    16957  17044  13071   2999   3322    188       N  
ATOM   5046  CA  TYR C 107     -40.028  17.324  52.998  1.00126.20           C  
ANISOU 5046  CA  TYR C 107    17375  17234  13343   2969   3872    288       C  
ATOM   5047  C   TYR C 107     -40.847  16.640  51.902  1.00129.16           C  
ANISOU 5047  C   TYR C 107    17253  17623  14197   2722   4074    280       C  
ATOM   5048  O   TYR C 107     -41.156  15.452  52.021  1.00130.09           O  
ANISOU 5048  O   TYR C 107    17436  17644  14350   2627   4461    376       O  
ATOM   5049  CB  TYR C 107     -40.919  17.633  54.219  1.00131.55           C  
ANISOU 5049  CB  TYR C 107    18348  17795  13839   3125   4343    218       C  
ATOM   5050  CG  TYR C 107     -40.217  18.354  55.351  1.00135.23           C  
ANISOU 5050  CG  TYR C 107    19336  18239  13807   3395   4142    183       C  
ATOM   5051  CD1 TYR C 107     -39.249  17.714  56.121  1.00138.47           C  
ANISOU 5051  CD1 TYR C 107    20260  18611  13741   3568   4042    311       C  
ATOM   5052  CD2 TYR C 107     -40.560  19.660  55.688  1.00137.01           C  
ANISOU 5052  CD2 TYR C 107    19564  18471  14023   3507   4050      2       C  
ATOM   5053  CE1 TYR C 107     -38.607  18.371  57.169  1.00141.44           C  
ANISOU 5053  CE1 TYR C 107    21115  18980  13647   3840   3805    235       C  
ATOM   5054  CE2 TYR C 107     -39.927  20.327  56.737  1.00139.92           C  
ANISOU 5054  CE2 TYR C 107    20421  18809  13932   3751   3849    -69       C  
ATOM   5055  CZ  TYR C 107     -38.952  19.678  57.477  1.00148.72           C  
ANISOU 5055  CZ  TYR C 107    22022  19908  14578   3916   3713     37       C  
ATOM   5056  OH  TYR C 107     -38.328  20.328  58.514  1.00152.21           O  
ANISOU 5056  OH  TYR C 107    22942  20333  14556   4178   3463    -74       O  
ATOM   5057  N   GLU C 108     -41.187  17.387  50.838  1.00123.76           N  
ANISOU 5057  N   GLU C 108    16109  17044  13870   2630   3802    155       N  
ATOM   5058  CA  GLU C 108     -41.958  16.890  49.704  1.00122.82           C  
ANISOU 5058  CA  GLU C 108    15492  16969  14204   2433   3879     92       C  
ATOM   5059  C   GLU C 108     -41.115  15.991  48.801  1.00123.98           C  
ANISOU 5059  C   GLU C 108    15573  17154  14379   2294   3646    225       C  
ATOM   5060  O   GLU C 108     -41.539  14.874  48.523  1.00124.21           O  
ANISOU 5060  O   GLU C 108    15480  17129  14584   2142   3928    251       O  
ATOM   5061  CB  GLU C 108     -42.601  18.044  48.916  1.00123.59           C  
ANISOU 5061  CB  GLU C 108    15197  17157  14603   2462   3631    -89       C  
ATOM   5062  CG  GLU C 108     -43.646  18.816  49.709  1.00137.36           C  
ANISOU 5062  CG  GLU C 108    16939  18861  16389   2608   3908   -248       C  
ATOM   5063  CD  GLU C 108     -43.107  19.924  50.594  1.00158.17           C  
ANISOU 5063  CD  GLU C 108    19894  21475  18729   2810   3659   -272       C  
ATOM   5064  OE1 GLU C 108     -41.869  20.095  50.664  1.00152.24           O  
ANISOU 5064  OE1 GLU C 108    19570  20687  17589   2871   3541   -157       O  
ATOM   5065  OE2 GLU C 108     -43.930  20.602  51.251  1.00153.44           O  
ANISOU 5065  OE2 GLU C 108    19119  20887  18292   2924   3578   -429       O  
ATOM   5066  N   LEU C 109     -39.912  16.454  48.384  1.00117.98           N  
ANISOU 5066  N   LEU C 109    14902  16469  13456   2338   3169    293       N  
ATOM   5067  CA  LEU C 109     -38.983  15.725  47.507  1.00115.41           C  
ANISOU 5067  CA  LEU C 109    14517  16191  13143   2234   2925    410       C  
ATOM   5068  C   LEU C 109     -38.654  14.302  47.995  1.00120.34           C  
ANISOU 5068  C   LEU C 109    15398  16724  13603   2215   3196    559       C  
ATOM   5069  O   LEU C 109     -38.695  13.366  47.194  1.00119.04           O  
ANISOU 5069  O   LEU C 109    15061  16547  13620   2069   3248    600       O  
ATOM   5070  CB  LEU C 109     -37.695  16.548  47.269  1.00113.46           C  
ANISOU 5070  CB  LEU C 109    14363  16018  12728   2297   2449    437       C  
ATOM   5071  CG  LEU C 109     -36.614  15.951  46.346  1.00115.87           C  
ANISOU 5071  CG  LEU C 109    14590  16384  13051   2207   2191    541       C  
ATOM   5072  CD1 LEU C 109     -37.021  16.020  44.880  1.00114.34           C  
ANISOU 5072  CD1 LEU C 109    14033  16237  13175   2064   2079    501       C  
ATOM   5073  CD2 LEU C 109     -35.296  16.662  46.532  1.00117.66           C  
ANISOU 5073  CD2 LEU C 109    14951  16662  13091   2275   1825    544       C  
ATOM   5074  N   GLU C 110     -38.353  14.146  49.298  1.00119.14           N  
ANISOU 5074  N   GLU C 110    15693  16488  13086   2386   3366    633       N  
ATOM   5075  CA  GLU C 110     -38.018  12.856  49.906  1.00120.65           C  
ANISOU 5075  CA  GLU C 110    16247  16553  13042   2439   3635    796       C  
ATOM   5076  C   GLU C 110     -39.220  11.909  50.021  1.00126.83           C  
ANISOU 5076  C   GLU C 110    16983  17169  14035   2284   4231    799       C  
ATOM   5077  O   GLU C 110     -39.095  10.730  49.684  1.00126.56           O  
ANISOU 5077  O   GLU C 110    16986  17038  14063   2180   4393    898       O  
ATOM   5078  CB  GLU C 110     -37.344  13.054  51.275  1.00124.24           C  
ANISOU 5078  CB  GLU C 110    17251  16964  12991   2724   3599    860       C  
ATOM   5079  CG  GLU C 110     -35.828  13.179  51.215  1.00133.58           C  
ANISOU 5079  CG  GLU C 110    18555  18265  13937   2869   3068    901       C  
ATOM   5080  CD  GLU C 110     -35.251  14.427  50.568  1.00152.00           C  
ANISOU 5080  CD  GLU C 110    20574  20764  16416   2817   2574    764       C  
ATOM   5081  OE1 GLU C 110     -34.192  14.311  49.911  1.00144.97           O  
ANISOU 5081  OE1 GLU C 110    19548  19972  15561   2792   2215    785       O  
ATOM   5082  OE2 GLU C 110     -35.841  15.520  50.729  1.00146.51           O  
ANISOU 5082  OE2 GLU C 110    19786  20079  15802   2805   2571    633       O  
ATOM   5083  N   GLU C 111     -40.375  12.424  50.488  1.00125.50           N  
ANISOU 5083  N   GLU C 111    16721  16958  14007   2260   4574    671       N  
ATOM   5084  CA  GLU C 111     -41.603  11.649  50.684  1.00128.42           C  
ANISOU 5084  CA  GLU C 111    16991  17163  14638   2086   5201    622       C  
ATOM   5085  C   GLU C 111     -42.335  11.279  49.391  1.00131.07           C  
ANISOU 5085  C   GLU C 111    16723  17553  15523   1806   5195    471       C  
ATOM   5086  O   GLU C 111     -42.865  10.169  49.302  1.00132.59           O  
ANISOU 5086  O   GLU C 111    16872  17589  15918   1612   5614    473       O  
ATOM   5087  CB  GLU C 111     -42.553  12.370  51.651  1.00133.01           C  
ANISOU 5087  CB  GLU C 111    17646  17693  15199   2172   5581    509       C  
ATOM   5088  N   HIS C 112     -42.385  12.203  48.405  1.00124.94           N  
ANISOU 5088  N   HIS C 112    15516  16978  14976   1794   4730    327       N  
ATOM   5089  CA  HIS C 112     -43.073  12.007  47.123  1.00124.03           C  
ANISOU 5089  CA  HIS C 112    14842  16946  15339   1594   4619    150       C  
ATOM   5090  C   HIS C 112     -42.519  10.864  46.284  1.00126.13           C  
ANISOU 5090  C   HIS C 112    15086  17172  15664   1441   4525    236       C  
ATOM   5091  O   HIS C 112     -41.303  10.711  46.155  1.00123.26           O  
ANISOU 5091  O   HIS C 112    14994  16832  15005   1532   4230    416       O  
ATOM   5092  CB  HIS C 112     -43.092  13.296  46.282  1.00122.59           C  
ANISOU 5092  CB  HIS C 112    14342  16960  15275   1690   4102     20       C  
ATOM   5093  CG  HIS C 112     -44.283  14.172  46.518  1.00128.33           C  
ANISOU 5093  CG  HIS C 112    14778  17732  16248   1752   4242   -201       C  
ATOM   5094  ND1 HIS C 112     -45.532  13.839  46.025  1.00132.57           N  
ANISOU 5094  ND1 HIS C 112    14822  18290  17260   1609   4455   -443       N  
ATOM   5095  CD2 HIS C 112     -44.367  15.365  47.149  1.00130.50           C  
ANISOU 5095  CD2 HIS C 112    15170  18040  16374   1953   4168   -239       C  
ATOM   5096  CE1 HIS C 112     -46.337  14.822  46.393  1.00133.88           C  
ANISOU 5096  CE1 HIS C 112    14810  18510  17550   1747   4515   -612       C  
ATOM   5097  NE2 HIS C 112     -45.680  15.764  47.071  1.00132.99           N  
ANISOU 5097  NE2 HIS C 112    15075  18394  17060   1958   4357   -487       N  
ATOM   5098  N   LYS C 113     -43.434  10.076  45.707  1.00124.35           N  
ANISOU 5098  N   LYS C 113    14510  16888  15849   1207   4775     75       N  
ATOM   5099  CA  LYS C 113     -43.147   8.967  44.803  1.00123.32           C  
ANISOU 5099  CA  LYS C 113    14296  16705  15856   1032   4717     90       C  
ATOM   5100  C   LYS C 113     -43.324   9.477  43.366  1.00125.19           C  
ANISOU 5100  C   LYS C 113    14069  17145  16353   1005   4214    -94       C  
ATOM   5101  O   LYS C 113     -43.798  10.601  43.175  1.00124.48           O  
ANISOU 5101  O   LYS C 113    13732  17204  16362   1116   3988   -232       O  
ATOM   5102  CB  LYS C 113     -44.096   7.790  45.086  1.00129.81           C  
ANISOU 5102  CB  LYS C 113    15031  17304  16988    772   5326    -15       C  
ATOM   5103  N   ILE C 114     -42.935   8.667  42.362  1.00120.73           N  
ANISOU 5103  N   ILE C 114    13434  16573  15867    889   4038    -93       N  
ATOM   5104  CA  ILE C 114     -43.055   9.029  40.946  1.00119.14           C  
ANISOU 5104  CA  ILE C 114    12875  16542  15851    888   3567   -257       C  
ATOM   5105  C   ILE C 114     -44.519   9.167  40.499  1.00126.09           C  
ANISOU 5105  C   ILE C 114    13216  17486  17205    782   3618   -613       C  
ATOM   5106  O   ILE C 114     -44.818  10.022  39.663  1.00125.09           O  
ANISOU 5106  O   ILE C 114    12822  17535  17172    910   3202   -763       O  
ATOM   5107  CB  ILE C 114     -42.259   8.056  40.049  1.00120.68           C  
ANISOU 5107  CB  ILE C 114    13178  16696  15981    804   3410   -174       C  
ATOM   5108  N   GLU C 115     -45.423   8.347  41.076  1.00126.32           N  
ANISOU 5108  N   GLU C 115    13097  17362  17537    565   4137   -757       N  
ATOM   5109  CA  GLU C 115     -46.857   8.351  40.775  1.00129.94           C  
ANISOU 5109  CA  GLU C 115    12976  17872  18524    430   4255  -1147       C  
ATOM   5110  C   GLU C 115     -47.600   9.499  41.458  1.00135.43           C  
ANISOU 5110  C   GLU C 115    13487  18667  19302    591   4334  -1256       C  
ATOM   5111  O   GLU C 115     -48.482  10.096  40.837  1.00136.61           O  
ANISOU 5111  O   GLU C 115    13146  18986  19773    660   4078  -1562       O  
ATOM   5112  CB  GLU C 115     -47.500   7.009  41.156  1.00135.22           C  
ANISOU 5112  CB  GLU C 115    13552  18301  19525     91   4853  -1272       C  
ATOM   5113  N   THR C 116     -47.262   9.790  42.736  1.00132.01           N  
ANISOU 5113  N   THR C 116    13459  18128  18569    679   4677  -1026       N  
ATOM   5114  CA  THR C 116     -47.892  10.844  43.547  1.00133.56           C  
ANISOU 5114  CA  THR C 116    13574  18384  18789    844   4825  -1104       C  
ATOM   5115  C   THR C 116     -47.700  12.240  42.957  1.00135.15           C  
ANISOU 5115  C   THR C 116    13682  18800  18867   1135   4224  -1134       C  
ATOM   5116  O   THR C 116     -48.657  13.015  42.921  1.00136.97           O  
ANISOU 5116  O   THR C 116    13537  19140  19366   1249   4181  -1381       O  
ATOM   5117  CB  THR C 116     -47.442  10.779  45.014  1.00142.23           C  
ANISOU 5117  CB  THR C 116    15228  19304  19509    898   5291   -837       C  
ATOM   5118  OG1 THR C 116     -46.023  10.904  45.078  1.00138.11           O  
ANISOU 5118  OG1 THR C 116    15220  18783  18474   1050   4967   -518       O  
ATOM   5119  CG2 THR C 116     -47.900   9.507  45.722  1.00144.57           C  
ANISOU 5119  CG2 THR C 116    15633  19339  19956    632   6006   -831       C  
ATOM   5120  N   TRP C 117     -46.475  12.558  42.491  1.00127.71           N  
ANISOU 5120  N   TRP C 117    13082  17902  17541   1259   3785   -891       N  
ATOM   5121  CA  TRP C 117     -46.173  13.853  41.883  1.00125.52           C  
ANISOU 5121  CA  TRP C 117    12800  17771  17121   1511   3254   -885       C  
ATOM   5122  C   TRP C 117     -46.769  13.969  40.473  1.00130.12           C  
ANISOU 5122  C   TRP C 117    12949  18496  17996   1548   2840  -1133       C  
ATOM   5123  O   TRP C 117     -47.106  15.076  40.047  1.00129.97           O  
ANISOU 5123  O   TRP C 117    12798  18583  18000   1783   2506  -1239       O  
ATOM   5124  CB  TRP C 117     -44.663  14.141  41.885  1.00120.34           C  
ANISOU 5124  CB  TRP C 117    12632  17092  16000   1596   2988   -569       C  
ATOM   5125  CG  TRP C 117     -44.324  15.521  41.405  1.00119.69           C  
ANISOU 5125  CG  TRP C 117    12608  17097  15770   1824   2541   -548       C  
ATOM   5126  CD1 TRP C 117     -44.408  16.682  42.117  1.00123.04           C  
ANISOU 5126  CD1 TRP C 117    13161  17515  16075   2007   2532   -545       C  
ATOM   5127  CD2 TRP C 117     -43.931  15.890  40.079  1.00117.81           C  
ANISOU 5127  CD2 TRP C 117    12325  16936  15500   1898   2075   -542       C  
ATOM   5128  NE1 TRP C 117     -44.071  17.751  41.320  1.00121.12           N  
ANISOU 5128  NE1 TRP C 117    12962  17318  15740   2175   2096   -530       N  
ATOM   5129  CE2 TRP C 117     -43.771  17.294  40.063  1.00121.24           C  
ANISOU 5129  CE2 TRP C 117    12888  17383  15795   2117   1822   -517       C  
ATOM   5130  CE3 TRP C 117     -43.688  15.169  38.898  1.00118.19           C  
ANISOU 5130  CE3 TRP C 117    12281  17022  15603   1809   1866   -554       C  
ATOM   5131  CZ2 TRP C 117     -43.363  17.988  38.919  1.00119.36           C  
ANISOU 5131  CZ2 TRP C 117    12719  17172  15460   2244   1403   -479       C  
ATOM   5132  CZ3 TRP C 117     -43.293  15.858  37.764  1.00118.44           C  
ANISOU 5132  CZ3 TRP C 117    12375  17106  15521   1951   1437   -525       C  
ATOM   5133  CH2 TRP C 117     -43.121  17.249  37.783  1.00118.74           C  
ANISOU 5133  CH2 TRP C 117    12571  17134  15410   2163   1226   -475       C  
ATOM   5134  N   ARG C 118     -46.922  12.825  39.767  1.00127.44           N  
ANISOU 5134  N   ARG C 118    12418  18141  17862   1340   2859  -1237       N  
ATOM   5135  CA  ARG C 118     -47.506  12.751  38.422  1.00128.54           C  
ANISOU 5135  CA  ARG C 118    12162  18412  18267   1371   2458  -1510       C  
ATOM   5136  C   ARG C 118     -48.981  13.178  38.425  1.00136.80           C  
ANISOU 5136  C   ARG C 118    12643  19568  19765   1446   2480  -1904       C  
ATOM   5137  O   ARG C 118     -49.451  13.747  37.439  1.00137.49           O  
ANISOU 5137  O   ARG C 118    12465  19807  19966   1654   2008  -2118       O  
ATOM   5138  CB  ARG C 118     -47.356  11.339  37.840  1.00129.17           C  
ANISOU 5138  CB  ARG C 118    12185  18419  18474   1103   2540  -1560       C  
ATOM   5139  N   GLU C 119     -49.697  12.912  39.537  1.00136.19           N  
ANISOU 5139  N   GLU C 119    12401  19411  19934   1303   3035  -2004       N  
ATOM   5140  CA  GLU C 119     -51.100  13.286  39.728  1.00140.67           C  
ANISOU 5140  CA  GLU C 119    12395  20075  20977   1357   3164  -2391       C  
ATOM   5141  C   GLU C 119     -51.227  14.794  39.972  1.00144.06           C  
ANISOU 5141  C   GLU C 119    12890  20603  21244   1732   2922  -2366       C  
ATOM   5142  O   GLU C 119     -52.225  15.395  39.572  1.00146.86           O  
ANISOU 5142  O   GLU C 119    12774  21107  21920   1930   2699  -2696       O  
ATOM   5143  CB  GLU C 119     -51.711  12.502  40.899  1.00145.41           C  
ANISOU 5143  CB  GLU C 119    12877  20515  21855   1065   3933  -2464       C  
ATOM   5144  N   VAL C 120     -50.211  15.397  40.627  1.00136.96           N  
ANISOU 5144  N   VAL C 120    12569  19612  19857   1840   2949  -1997       N  
ATOM   5145  CA  VAL C 120     -50.146  16.830  40.940  1.00136.10           C  
ANISOU 5145  CA  VAL C 120    12638  19538  19535   2170   2749  -1931       C  
ATOM   5146  C   VAL C 120     -49.798  17.626  39.667  1.00138.14           C  
ANISOU 5146  C   VAL C 120    12958  19894  19636   2434   2074  -1916       C  
ATOM   5147  O   VAL C 120     -50.484  18.599  39.349  1.00139.80           O  
ANISOU 5147  O   VAL C 120    12963  20192  19962   2735   1804  -2102       O  
ATOM   5148  CB  VAL C 120     -49.165  17.128  42.116  1.00137.37           C  
ANISOU 5148  CB  VAL C 120    13394  19551  19248   2163   3017  -1585       C  
ATOM   5149  CG1 VAL C 120     -49.129  18.617  42.457  1.00136.97           C  
ANISOU 5149  CG1 VAL C 120    13529  19508  19005   2482   2824  -1554       C  
ATOM   5150  CG2 VAL C 120     -49.518  16.310  43.357  1.00139.44           C  
ANISOU 5150  CG2 VAL C 120    13689  19689  19602   1944   3702  -1580       C  
ATOM   5151  N   TYR C 121     -48.743  17.199  38.944  1.00131.21           N  
ANISOU 5151  N   TYR C 121    12386  18984  18484   2341   1830  -1694       N  
ATOM   5152  CA  TYR C 121     -48.268  17.834  37.715  1.00129.41           C  
ANISOU 5152  CA  TYR C 121    12318  18804  18046   2560   1267  -1630       C  
ATOM   5153  C   TYR C 121     -49.188  17.511  36.532  1.00135.89           C  
ANISOU 5153  C   TYR C 121    12684  19771  19176   2651    924  -1966       C  
ATOM   5154  O   TYR C 121     -49.208  16.373  36.054  1.00135.63           O  
ANISOU 5154  O   TYR C 121    12487  19759  19288   2423    955  -2056       O  
ATOM   5155  CB  TYR C 121     -46.810  17.423  37.435  1.00126.50           C  
ANISOU 5155  CB  TYR C 121    12419  18346  17299   2410   1208  -1289       C  
ATOM   5156  CG  TYR C 121     -46.131  18.202  36.328  1.00126.75           C  
ANISOU 5156  CG  TYR C 121    12736  18374  17048   2617    739  -1156       C  
ATOM   5157  CD1 TYR C 121     -45.672  19.499  36.542  1.00127.84           C  
ANISOU 5157  CD1 TYR C 121    13201  18433  16941   2821    614  -1001       C  
ATOM   5158  CD2 TYR C 121     -45.872  17.614  35.094  1.00127.10           C  
ANISOU 5158  CD2 TYR C 121    12785  18460  17047   2591    466  -1169       C  
ATOM   5159  CE1 TYR C 121     -45.023  20.212  35.535  1.00127.63           C  
ANISOU 5159  CE1 TYR C 121    13487  18351  16653   2987    261   -860       C  
ATOM   5160  CE2 TYR C 121     -45.216  18.314  34.082  1.00126.90           C  
ANISOU 5160  CE2 TYR C 121    13089  18400  16728   2781    103  -1023       C  
ATOM   5161  CZ  TYR C 121     -44.792  19.613  34.307  1.00133.70           C  
ANISOU 5161  CZ  TYR C 121    14270  19163  17365   2970     22   -861       C  
ATOM   5162  OH  TYR C 121     -44.145  20.308  33.313  1.00134.12           O  
ANISOU 5162  OH  TYR C 121    14687  19136  17134   3137   -265   -706       O  
ATOM   5163  N   LEU C 122     -49.960  18.527  36.078  1.00134.93           N  
ANISOU 5163  N   LEU C 122    12372  19743  19152   3011    579  -2172       N  
ATOM   5164  CA  LEU C 122     -50.928  18.476  34.972  1.00167.61           C  
ANISOU 5164  CA  LEU C 122    16076  24045  23561   3220    148  -2541       C  
ATOM   5165  C   LEU C 122     -51.998  17.399  35.148  1.00193.93           C  
ANISOU 5165  C   LEU C 122    18754  27483  27447   2976    388  -2937       C  
ATOM   5166  O   LEU C 122     -52.872  17.531  36.002  1.00155.75           O  
ANISOU 5166  O   LEU C 122    13542  22680  22957   2957    716  -3146       O  
ATOM   5167  CB  LEU C 122     -50.233  18.344  33.607  1.00166.05           C  
ANISOU 5167  CB  LEU C 122    16183  23852  23056   3317   -323  -2427       C  
ATOM   5168  N   PRO C 128     -52.246  11.497  28.181  1.00150.23           N  
ANISOU 5168  N   PRO C 128    12474  22281  22324   2382  -1531  -4293       N  
ATOM   5169  CA  PRO C 128     -51.933  10.441  27.208  1.00150.46           C  
ANISOU 5169  CA  PRO C 128    12607  22279  22282   2233  -1730  -4421       C  
ATOM   5170  C   PRO C 128     -50.436  10.301  26.939  1.00148.54           C  
ANISOU 5170  C   PRO C 128    13118  21874  21447   2199  -1627  -3889       C  
ATOM   5171  O   PRO C 128     -49.692  11.276  27.069  1.00144.71           O  
ANISOU 5171  O   PRO C 128    13096  21352  20533   2430  -1645  -3482       O  
ATOM   5172  CB  PRO C 128     -52.701  10.871  25.957  1.00156.97           C  
ANISOU 5172  CB  PRO C 128    13220  23319  23101   2670  -2500  -4850       C  
ATOM   5173  CG  PRO C 128     -52.824  12.350  26.076  1.00161.19           C  
ANISOU 5173  CG  PRO C 128    13911  23937  23395   3142  -2740  -4688       C  
ATOM   5174  CD  PRO C 128     -52.852  12.681  27.543  1.00154.54           C  
ANISOU 5174  CD  PRO C 128    12948  23010  22761   2927  -2128  -4468       C  
ATOM   5175  N   LEU C 129     -50.001   9.086  26.556  1.00144.41           N  
ANISOU 5175  N   LEU C 129    12699  21244  20928   1906  -1508  -3917       N  
ATOM   5176  CA  LEU C 129     -48.602   8.783  26.254  1.00139.56           C  
ANISOU 5176  CA  LEU C 129    12731  20482  19813   1857  -1389  -3470       C  
ATOM   5177  C   LEU C 129     -48.210   9.330  24.877  1.00143.34           C  
ANISOU 5177  C   LEU C 129    13613  21040  19808   2265  -1966  -3432       C  
ATOM   5178  O   LEU C 129     -48.867   9.022  23.879  1.00146.98           O  
ANISOU 5178  O   LEU C 129    13888  21610  20348   2408  -2425  -3840       O  
ATOM   5179  CB  LEU C 129     -48.341   7.262  26.350  1.00139.61           C  
ANISOU 5179  CB  LEU C 129    12704  20326  20015   1425  -1039  -3537       C  
ATOM   5180  CG  LEU C 129     -46.906   6.769  26.099  1.00140.10           C  
ANISOU 5180  CG  LEU C 129    13373  20232  19625   1354   -868  -3114       C  
ATOM   5181  CD1 LEU C 129     -46.015   6.985  27.317  1.00135.83           C  
ANISOU 5181  CD1 LEU C 129    13111  19564  18933   1226   -358  -2632       C  
ATOM   5182  CD2 LEU C 129     -46.900   5.303  25.720  1.00144.27           C  
ANISOU 5182  CD2 LEU C 129    13844  20630  20342   1049   -743  -3330       C  
ATOM   5183  N   VAL C 130     -47.143  10.148  24.838  1.00135.69           N  
ANISOU 5183  N   VAL C 130    13210  20004  18341   2451  -1927  -2955       N  
ATOM   5184  CA  VAL C 130     -46.619  10.751  23.609  1.00135.48           C  
ANISOU 5184  CA  VAL C 130    13686  19996  17795   2830  -2352  -2828       C  
ATOM   5185  C   VAL C 130     -45.382   9.951  23.174  1.00135.96           C  
ANISOU 5185  C   VAL C 130    14198  19917  17542   2652  -2144  -2556       C  
ATOM   5186  O   VAL C 130     -44.335  10.024  23.824  1.00131.35           O  
ANISOU 5186  O   VAL C 130    13890  19213  16803   2490  -1738  -2144       O  
ATOM   5187  CB  VAL C 130     -46.338  12.277  23.757  1.00138.08           C  
ANISOU 5187  CB  VAL C 130    14337  20315  17811   3167  -2442  -2525       C  
ATOM   5188  CG1 VAL C 130     -45.861  12.884  22.440  1.00138.91           C  
ANISOU 5188  CG1 VAL C 130    15012  20396  17371   3566  -2838  -2401       C  
ATOM   5189  CG2 VAL C 130     -47.570  13.022  24.269  1.00140.89           C  
ANISOU 5189  CG2 VAL C 130    14226  20802  18504   3353  -2614  -2805       C  
ATOM   5190  N   CYS C 131     -45.529   9.156  22.097  1.00134.73           N  
ANISOU 5190  N   CYS C 131    14090  19784  17317   2691  -2430  -2821       N  
ATOM   5191  CA  CYS C 131     -44.470   8.299  21.555  1.00132.46           C  
ANISOU 5191  CA  CYS C 131    14205  19370  16752   2554  -2263  -2635       C  
ATOM   5192  C   CYS C 131     -44.578   8.121  20.031  1.00139.05           C  
ANISOU 5192  C   CYS C 131    15320  20253  17262   2849  -2757  -2862       C  
ATOM   5193  O   CYS C 131     -45.519   8.627  19.415  1.00142.65           O  
ANISOU 5193  O   CYS C 131    15640  20848  17713   3172  -3268  -3185       O  
ATOM   5194  CB  CYS C 131     -44.447   6.954  22.280  1.00131.98           C  
ANISOU 5194  CB  CYS C 131    13860  19206  17079   2093  -1844  -2723       C  
ATOM   5195  SG  CYS C 131     -45.957   5.973  22.077  1.00141.48           S  
ANISOU 5195  SG  CYS C 131    14416  20482  18857   1913  -2071  -3406       S  
ATOM   5196  N   ILE C 132     -43.606   7.403  19.432  1.00133.82           N  
ANISOU 5196  N   ILE C 132    15062  19475  16309   2770  -2613  -2702       N  
ATOM   5197  CA  ILE C 132     -43.548   7.121  17.996  1.00136.55           C  
ANISOU 5197  CA  ILE C 132    15769  19835  16280   3036  -3010  -2884       C  
ATOM   5198  C   ILE C 132     -43.213   5.633  17.733  1.00140.17           C  
ANISOU 5198  C   ILE C 132    16226  20188  16842   2739  -2831  -3035       C  
ATOM   5199  O   ILE C 132     -42.719   4.947  18.630  1.00136.68           O  
ANISOU 5199  O   ILE C 132    15650  19631  16650   2369  -2341  -2864       O  
ATOM   5200  CB  ILE C 132     -42.595   8.128  17.275  1.00138.48           C  
ANISOU 5200  CB  ILE C 132    16705  20018  15894   3385  -3038  -2473       C  
ATOM   5201  CG1 ILE C 132     -43.014   9.598  17.501  1.00143.75           C  
ANISOU 5201  CG1 ILE C 132    17753  20741  16126   3839  -3605  -2713       C  
ATOM   5202  CG2 ILE C 132     -42.406   7.813  15.790  1.00135.05           C  
ANISOU 5202  CG2 ILE C 132    16644  19422  15247   3173  -2511  -2034       C  
ATOM   5203  CD1 ILE C 132     -44.426   9.948  17.025  1.00154.86           C  
ANISOU 5203  CD1 ILE C 132    19066  22284  17488   4263  -4131  -2920       C  
ATOM   5204  N   SER C 133     -43.505   5.144  16.514  1.00140.37           N  
ANISOU 5204  N   SER C 133    16427  20244  16663   2929  -3245  -3367       N  
ATOM   5205  CA  SER C 133     -43.263   3.764  16.085  1.00141.13           C  
ANISOU 5205  CA  SER C 133    16574  20229  16819   2702  -3150  -3569       C  
ATOM   5206  C   SER C 133     -41.938   3.654  15.296  1.00142.76           C  
ANISOU 5206  C   SER C 133    17479  20315  16449   2848  -2973  -3214       C  
ATOM   5207  O   SER C 133     -41.621   4.582  14.548  1.00142.97           O  
ANISOU 5207  O   SER C 133    17964  20378  15979   3232  -3178  -3032       O  
ATOM   5208  CB  SER C 133     -44.429   3.278  15.227  1.00150.81           C  
ANISOU 5208  CB  SER C 133    17544  21563  18193   2820  -3738  -4215       C  
ATOM   5209  OG  SER C 133     -44.321   1.905  14.887  1.00161.19           O  
ANISOU 5209  OG  SER C 133    18853  22749  19643   2556  -3646  -4475       O  
ATOM   5210  N   PRO C 134     -41.153   2.548  15.424  1.00137.21           N  
ANISOU 5210  N   PRO C 134    16891  19450  15793   2569  -2573  -3114       N  
ATOM   5211  CA  PRO C 134     -39.901   2.446  14.645  1.00135.77           C  
ANISOU 5211  CA  PRO C 134    17336  19164  15086   2724  -2386  -2806       C  
ATOM   5212  C   PRO C 134     -40.139   2.270  13.144  1.00143.96           C  
ANISOU 5212  C   PRO C 134    18777  20227  15696   3061  -2850  -3105       C  
ATOM   5213  O   PRO C 134     -39.304   2.687  12.340  1.00143.59           O  
ANISOU 5213  O   PRO C 134    19317  20135  15106   3333  -2796  -2843       O  
ATOM   5214  CB  PRO C 134     -39.189   1.241  15.263  1.00135.13           C  
ANISOU 5214  CB  PRO C 134    17185  18914  15246   2357  -1884  -2696       C  
ATOM   5215  CG  PRO C 134     -40.271   0.413  15.836  1.00141.54           C  
ANISOU 5215  CG  PRO C 134    17453  19706  16622   2052  -1953  -3112       C  
ATOM   5216  CD  PRO C 134     -41.359   1.352  16.268  1.00138.12           C  
ANISOU 5216  CD  PRO C 134    16604  19447  16429   2122  -2248  -3270       C  
ATOM   5217  N   ASN C 135     -41.289   1.671  12.774  1.00144.60           N  
ANISOU 5217  N   ASN C 135    18541  20375  16025   3044  -3300  -3674       N  
ATOM   5218  CA  ASN C 135     -41.707   1.451  11.388  1.00149.62           C  
ANISOU 5218  CA  ASN C 135    19501  21058  16291   3380  -3848  -4066       C  
ATOM   5219  C   ASN C 135     -42.170   2.767  10.752  1.00155.50           C  
ANISOU 5219  C   ASN C 135    20491  21959  16634   3889  -4344  -4063       C  
ATOM   5220  O   ASN C 135     -42.095   2.910   9.530  1.00158.81           O  
ANISOU 5220  O   ASN C 135    21457  22386  16497   4293  -4701  -4169       O  
ATOM   5221  CB  ASN C 135     -42.828   0.408  11.320  1.00154.83           C  
ANISOU 5221  CB  ASN C 135    19650  21743  17437   3159  -4180  -4725       C  
ATOM   5222  CG  ASN C 135     -42.478  -0.930  11.928  1.00176.50           C  
ANISOU 5222  CG  ASN C 135    22188  24283  20589   2664  -3693  -4758       C  
ATOM   5223  OD1 ASN C 135     -41.550  -1.623  11.494  1.00170.28           O  
ANISOU 5223  OD1 ASN C 135    21841  23333  19525   2638  -3419  -4599       O  
ATOM   5224  ND2 ASN C 135     -43.239  -1.338  12.932  1.00168.32           N  
ANISOU 5224  ND2 ASN C 135    20500  23233  20221   2275  -3557  -4979       N  
ATOM   5225  N   ALA C 136     -42.652   3.719  11.585  1.00149.94           N  
ANISOU 5225  N   ALA C 136    19423  21359  16186   3893  -4360  -3942       N  
ATOM   5226  CA  ALA C 136     -43.131   5.038  11.163  1.00151.79           C  
ANISOU 5226  CA  ALA C 136    19857  21718  16098   4376  -4793  -3910       C  
ATOM   5227  C   ALA C 136     -42.004   5.912  10.604  1.00153.50           C  
ANISOU 5227  C   ALA C 136    20872  21813  15636   4678  -4555  -3366       C  
ATOM   5228  O   ALA C 136     -40.839   5.736  10.966  1.00148.74           O  
ANISOU 5228  O   ALA C 136    20475  21065  14973   4433  -3955  -2938       O  
ATOM   5229  CB  ALA C 136     -43.825   5.743  12.320  1.00150.73           C  
ANISOU 5229  CB  ALA C 136    19123  21691  16457   4249  -4759  -3893       C  
ATOM   5230  N   SER C 137     -42.366   6.842   9.707  1.00153.67           N  
ANISOU 5230  N   SER C 137    21347  21884  15158   5224  -5025  -3404       N  
ATOM   5231  CA  SER C 137     -41.462   7.763   9.019  1.00153.31           C  
ANISOU 5231  CA  SER C 137    22134  21693  14424   5573  -4842  -2937       C  
ATOM   5232  C   SER C 137     -40.800   8.797   9.937  1.00151.84           C  
ANISOU 5232  C   SER C 137    21957  21413  14321   5431  -4335  -2399       C  
ATOM   5233  O   SER C 137     -41.322   9.090  11.016  1.00149.02           O  
ANISOU 5233  O   SER C 137    21002  21147  14471   5224  -4310  -2432       O  
ATOM   5234  CB  SER C 137     -42.209   8.471   7.895  1.00163.17           C  
ANISOU 5234  CB  SER C 137    23850  23007  15142   6226  -5529  -3164       C  
ATOM   5235  OG  SER C 137     -42.639   7.552   6.904  1.00176.76           O  
ANISOU 5235  OG  SER C 137    25702  24791  16666   6402  -5993  -3641       O  
ATOM   5236  N   LEU C 138     -39.650   9.353   9.491  1.00147.04           N  
ANISOU 5236  N   LEU C 138    22037  20614  13219   5540  -3917  -1925       N  
ATOM   5237  CA  LEU C 138     -38.886  10.388  10.197  1.00142.95           C  
ANISOU 5237  CA  LEU C 138    21628  19969  12717   5421  -3425  -1422       C  
ATOM   5238  C   LEU C 138     -39.664  11.713  10.203  1.00148.76           C  
ANISOU 5238  C   LEU C 138    22481  20723  13319   5811  -3793  -1403       C  
ATOM   5239  O   LEU C 138     -39.633  12.428  11.207  1.00145.15           O  
ANISOU 5239  O   LEU C 138    21726  20252  13171   5638  -3577  -1200       O  
ATOM   5240  CB  LEU C 138     -37.480  10.553   9.566  1.00142.53           C  
ANISOU 5240  CB  LEU C 138    22275  19692  12187   5431  -2878   -993       C  
ATOM   5241  CG  LEU C 138     -36.584  11.733  10.012  1.00144.83           C  
ANISOU 5241  CG  LEU C 138    22830  19803  12396   5357  -2364   -484       C  
ATOM   5242  CD1 LEU C 138     -36.230  11.660  11.491  1.00139.33           C  
ANISOU 5242  CD1 LEU C 138    21461  19158  12320   4860  -1992   -347       C  
ATOM   5243  CD2 LEU C 138     -35.313  11.787   9.195  1.00148.33           C  
ANISOU 5243  CD2 LEU C 138    23957  20029  12372   5393  -1855   -155       C  
ATOM   5244  N   PHE C 139     -40.386  12.015   9.099  1.00150.93           N  
ANISOU 5244  N   PHE C 139    23194  21026  13126   6363  -4377  -1638       N  
ATOM   5245  CA  PHE C 139     -41.216  13.215   8.940  1.00154.05           C  
ANISOU 5245  CA  PHE C 139    23767  21437  13329   6848  -4826  -1673       C  
ATOM   5246  C   PHE C 139     -42.341  13.263   9.982  1.00156.59           C  
ANISOU 5246  C   PHE C 139    23199  21983  14314   6715  -5139  -1999       C  
ATOM   5247  O   PHE C 139     -42.702  14.348  10.441  1.00156.22           O  
ANISOU 5247  O   PHE C 139    23121  21914  14320   6895  -5208  -1871       O  
ATOM   5248  CB  PHE C 139     -41.797  13.290   7.521  1.00162.93           C  
ANISOU 5248  CB  PHE C 139    25510  22578  13820   7494  -5460  -1937       C  
ATOM   5249  N   ASP C 140     -42.875  12.084  10.359  1.00152.23           N  
ANISOU 5249  N   ASP C 140    21944  21621  14274   6388  -5279  -2417       N  
ATOM   5250  CA  ASP C 140     -43.923  11.934  11.370  1.00151.21           C  
ANISOU 5250  CA  ASP C 140    20919  21695  14838   6181  -5478  -2760       C  
ATOM   5251  C   ASP C 140     -43.349  12.044  12.791  1.00148.29           C  
ANISOU 5251  C   ASP C 140    20145  21264  14935   5655  -4829  -2422       C  
ATOM   5252  O   ASP C 140     -44.089  12.377  13.719  1.00147.05           O  
ANISOU 5252  O   ASP C 140    19411  21217  15244   5560  -4890  -2554       O  
ATOM   5253  CB  ASP C 140     -44.668  10.603  11.186  1.00155.43           C  
ANISOU 5253  CB  ASP C 140    20909  22405  15742   6000  -5810  -3340       C  
ATOM   5254  CG  ASP C 140     -45.526  10.557   9.940  1.00172.31           C  
ANISOU 5254  CG  ASP C 140    23270  24668  17533   6550  -6600  -3811       C  
ATOM   5255  OD1 ASP C 140     -45.055  10.022   8.915  1.00174.88           O  
ANISOU 5255  OD1 ASP C 140    24143  24917  17385   6695  -6683  -3840       O  
ATOM   5256  OD2 ASP C 140     -46.671  11.056   9.990  1.00181.93           O  
ANISOU 5256  OD2 ASP C 140    24115  26064  18945   6859  -7148  -4168       O  
ATOM   5257  N   ALA C 141     -42.036  11.771  12.956  1.00140.49           N  
ANISOU 5257  N   ALA C 141    19463  20104  13814   5341  -4222  -2005       N  
ATOM   5258  CA  ALA C 141     -41.332  11.833  14.240  1.00134.51           C  
ANISOU 5258  CA  ALA C 141    18402  19281  13425   4876  -3623  -1677       C  
ATOM   5259  C   ALA C 141     -40.902  13.256  14.604  1.00136.75           C  
ANISOU 5259  C   ALA C 141    18999  19432  13528   5013  -3414  -1272       C  
ATOM   5260  O   ALA C 141     -41.023  13.640  15.769  1.00133.39           O  
ANISOU 5260  O   ALA C 141    18161  19033  13489   4792  -3217  -1188       O  
ATOM   5261  CB  ALA C 141     -40.128  10.907  14.228  1.00132.16           C  
ANISOU 5261  CB  ALA C 141    18258  18875  13082   4525  -3121  -1462       C  
ATOM   5262  N   VAL C 142     -40.391  14.027  13.616  1.00135.55           N  
ANISOU 5262  N   VAL C 142    19608  19112  12782   5372  -3429  -1025       N  
ATOM   5263  CA  VAL C 142     -39.950  15.418  13.797  1.00134.89           C  
ANISOU 5263  CA  VAL C 142    19935  18839  12477   5521  -3212   -641       C  
ATOM   5264  C   VAL C 142     -41.170  16.305  14.092  1.00141.17           C  
ANISOU 5264  C   VAL C 142    20517  19724  13397   5859  -3676   -837       C  
ATOM   5265  O   VAL C 142     -41.100  17.164  14.974  1.00138.59           O  
ANISOU 5265  O   VAL C 142    20068  19326  13263   5766  -3465   -642       O  
ATOM   5266  CB  VAL C 142     -39.095  15.939  12.602  1.00141.45           C  
ANISOU 5266  CB  VAL C 142    21688  19422  12633   5806  -3043   -330       C  
ATOM   5267  CG1 VAL C 142     -38.661  17.389  12.811  1.00141.28           C  
ANISOU 5267  CG1 VAL C 142    22100  19156  12426   5921  -2774     55       C  
ATOM   5268  CG2 VAL C 142     -37.872  15.055  12.371  1.00138.95           C  
ANISOU 5268  CG2 VAL C 142    21513  19030  12252   5462  -2542   -155       C  
ATOM   5269  N   SER C 143     -42.297  16.055  13.386  1.00142.47           N  
ANISOU 5269  N   SER C 143    20592  20056  13482   6248  -4320  -1261       N  
ATOM   5270  CA  SER C 143     -43.564  16.771  13.560  1.00145.62           C  
ANISOU 5270  CA  SER C 143    20719  20585  14025   6631  -4844  -1538       C  
ATOM   5271  C   SER C 143     -44.138  16.568  14.966  1.00146.39           C  
ANISOU 5271  C   SER C 143    19933  20848  14842   6248  -4718  -1711       C  
ATOM   5272  O   SER C 143     -44.719  17.501  15.519  1.00146.57           O  
ANISOU 5272  O   SER C 143    19797  20881  15011   6432  -4831  -1714       O  
ATOM   5273  CB  SER C 143     -44.579  16.336  12.506  1.00155.16           C  
ANISOU 5273  CB  SER C 143    21930  21973  15050   7087  -5575  -2025       C  
ATOM   5274  OG  SER C 143     -44.899  14.960  12.625  1.00163.33           O  
ANISOU 5274  OG  SER C 143    22363  23204  16490   6739  -5655  -2415       O  
ATOM   5275  N   SER C 144     -43.951  15.359  15.543  1.00139.96           N  
ANISOU 5275  N   SER C 144    18596  20134  14447   5732  -4450  -1837       N  
ATOM   5276  CA  SER C 144     -44.400  14.992  16.890  1.00136.95           C  
ANISOU 5276  CA  SER C 144    17438  19876  14722   5321  -4233  -1978       C  
ATOM   5277  C   SER C 144     -43.685  15.810  17.970  1.00136.68           C  
ANISOU 5277  C   SER C 144    17466  19697  14770   5099  -3724  -1551       C  
ATOM   5278  O   SER C 144     -44.307  16.168  18.969  1.00135.48           O  
ANISOU 5278  O   SER C 144    16849  19621  15008   5019  -3686  -1645       O  
ATOM   5279  CB  SER C 144     -44.193  13.501  17.138  1.00138.46           C  
ANISOU 5279  CB  SER C 144    17244  20131  15233   4850  -4006  -2143       C  
ATOM   5280  OG  SER C 144     -44.998  12.717  16.273  1.00151.60           O  
ANISOU 5280  OG  SER C 144    18738  21937  16924   5010  -4496  -2620       O  
ATOM   5281  N   LEU C 145     -42.387  16.113  17.762  1.00131.02           N  
ANISOU 5281  N   LEU C 145    17315  18770  13697   5001  -3332  -1111       N  
ATOM   5282  CA  LEU C 145     -41.572  16.906  18.686  1.00127.24           C  
ANISOU 5282  CA  LEU C 145    16941  18135  13269   4784  -2864   -725       C  
ATOM   5283  C   LEU C 145     -41.952  18.392  18.645  1.00133.54           C  
ANISOU 5283  C   LEU C 145    18047  18817  13873   5175  -3039   -613       C  
ATOM   5284  O   LEU C 145     -41.892  19.065  19.677  1.00130.94           O  
ANISOU 5284  O   LEU C 145    17548  18436  13767   5038  -2813   -482       O  
ATOM   5285  CB  LEU C 145     -40.081  16.729  18.373  1.00124.85           C  
ANISOU 5285  CB  LEU C 145    17096  17652  12689   4560  -2408   -354       C  
ATOM   5286  N   ILE C 146     -42.344  18.896  17.456  1.00134.90           N  
ANISOU 5286  N   ILE C 146    18713  18934  13608   5687  -3446   -670       N  
ATOM   5287  CA  ILE C 146     -42.743  20.290  17.231  1.00137.92           C  
ANISOU 5287  CA  ILE C 146    19503  19170  13730   6152  -3658   -566       C  
ATOM   5288  C   ILE C 146     -44.171  20.549  17.748  1.00144.37           C  
ANISOU 5288  C   ILE C 146    19747  20197  14909   6397  -4097   -947       C  
ATOM   5289  O   ILE C 146     -44.380  21.511  18.489  1.00143.48           O  
ANISOU 5289  O   ILE C 146    19584  20004  14929   6463  -4007   -847       O  
ATOM   5290  CB  ILE C 146     -42.548  20.707  15.732  1.00145.64           C  
ANISOU 5290  CB  ILE C 146    21330  19972  14033   6647  -3898   -451       C  
ATOM   5291  CG1 ILE C 146     -41.074  20.521  15.243  1.00144.15           C  
ANISOU 5291  CG1 ILE C 146    21715  19548  13507   6384  -3362    -57       C  
ATOM   5292  CG2 ILE C 146     -43.068  22.126  15.433  1.00150.51           C  
ANISOU 5292  CG2 ILE C 146    22429  20414  14344   7210  -4169   -362       C  
ATOM   5293  CD1 ILE C 146     -39.931  21.392  15.927  1.00148.57           C  
ANISOU 5293  CD1 ILE C 146    22536  19822  14091   6068  -2731    388       C  
ATOM   5294  N   ARG C 147     -45.139  19.690  17.357  1.00143.99           N  
ANISOU 5294  N   ARG C 147    19253  20413  15042   6524  -4557  -1406       N  
ATOM   5295  CA  ARG C 147     -46.558  19.784  17.724  1.00147.06           C  
ANISOU 5295  CA  ARG C 147    19007  21040  15830   6758  -5001  -1856       C  
ATOM   5296  C   ARG C 147     -46.810  19.629  19.232  1.00147.61           C  
ANISOU 5296  C   ARG C 147    18362  21203  16518   6314  -4636  -1913       C  
ATOM   5297  O   ARG C 147     -47.527  20.449  19.809  1.00148.61           O  
ANISOU 5297  O   ARG C 147    18262  21362  16842   6528  -4747  -2005       O  
ATOM   5298  CB  ARG C 147     -47.389  18.772  16.910  1.00151.39           C  
ANISOU 5298  CB  ARG C 147    19225  21836  16461   6912  -5531  -2362       C  
ATOM   5299  CG  ARG C 147     -48.904  18.891  17.067  1.00166.40           C  
ANISOU 5299  CG  ARG C 147    20462  23998  18765   7226  -6074  -2901       C  
ATOM   5300  CD  ARG C 147     -49.647  17.790  16.325  1.00179.93           C  
ANISOU 5300  CD  ARG C 147    21775  25955  20637   7281  -6564  -3447       C  
ATOM   5301  NE  ARG C 147     -49.522  16.486  16.982  1.00184.50           N  
ANISOU 5301  NE  ARG C 147    21756  26619  21726   6617  -6181  -3596       N  
ATOM   5302  CZ  ARG C 147     -48.739  15.498  16.557  1.00196.02           C  
ANISOU 5302  CZ  ARG C 147    23442  28009  23026   6304  -5972  -3502       C  
ATOM   5303  NH1 ARG C 147     -47.999  15.649  15.465  1.00183.88           N  
ANISOU 5303  NH1 ARG C 147    22699  26330  20836   6576  -6088  -3265       N  
ATOM   5304  NH2 ARG C 147     -48.689  14.351  17.221  1.00180.10           N  
ANISOU 5304  NH2 ARG C 147    20896  26042  21490   5730  -5617  -3638       N  
ATOM   5305  N   ASN C 148     -46.231  18.586  19.861  1.00140.11           N  
ANISOU 5305  N   ASN C 148    17101  20285  15847   5736  -4199  -1859       N  
ATOM   5306  CA  ASN C 148     -46.394  18.315  21.294  1.00136.80           C  
ANISOU 5306  CA  ASN C 148    16086  19933  15959   5308  -3807  -1891       C  
ATOM   5307  C   ASN C 148     -45.508  19.199  22.188  1.00136.92           C  
ANISOU 5307  C   ASN C 148    16393  19744  15887   5141  -3341  -1452       C  
ATOM   5308  O   ASN C 148     -45.696  19.209  23.408  1.00134.41           O  
ANISOU 5308  O   ASN C 148    15667  19465  15939   4883  -3054  -1467       O  
ATOM   5309  CB  ASN C 148     -46.195  16.826  21.601  1.00135.53           C  
ANISOU 5309  CB  ASN C 148    15525  19863  16108   4808  -3550  -2024       C  
ATOM   5310  CG  ASN C 148     -47.205  15.927  20.931  1.00163.60           C  
ANISOU 5310  CG  ASN C 148    18657  23619  19884   4898  -3980  -2538       C  
ATOM   5311  OD1 ASN C 148     -48.380  15.872  21.312  1.00161.14           O  
ANISOU 5311  OD1 ASN C 148    17737  23479  20010   4957  -4183  -2939       O  
ATOM   5312  ND2 ASN C 148     -46.764  15.186  19.926  1.00156.41           N  
ANISOU 5312  ND2 ASN C 148    18039  22690  18701   4897  -4116  -2566       N  
ATOM   5313  N   LYS C 149     -44.563  19.951  21.572  1.00133.15           N  
ANISOU 5313  N   LYS C 149    16631  19037  14922   5293  -3262  -1082       N  
ATOM   5314  CA  LYS C 149     -43.615  20.882  22.209  1.00130.15           C  
ANISOU 5314  CA  LYS C 149    16612  18424  14416   5153  -2854   -680       C  
ATOM   5315  C   LYS C 149     -42.716  20.179  23.249  1.00129.13           C  
ANISOU 5315  C   LYS C 149    16237  18295  14533   4583  -2338   -517       C  
ATOM   5316  O   LYS C 149     -42.669  20.577  24.418  1.00126.66           O  
ANISOU 5316  O   LYS C 149    15713  17959  14453   4403  -2089   -451       O  
ATOM   5317  CB  LYS C 149     -44.328  22.133  22.790  1.00134.48           C  
ANISOU 5317  CB  LYS C 149    17125  18916  15053   5446  -2972   -714       C  
ATOM   5318  N   ILE C 150     -42.012  19.119  22.806  1.00124.18           N  
ANISOU 5318  N   ILE C 150    15661  17691  13831   4337  -2198   -465       N  
ATOM   5319  CA  ILE C 150     -41.107  18.309  23.635  1.00119.83           C  
ANISOU 5319  CA  ILE C 150    14922  17144  13465   3857  -1758   -320       C  
ATOM   5320  C   ILE C 150     -39.748  18.086  22.962  1.00122.22           C  
ANISOU 5320  C   ILE C 150    15682  17305  13453   3728  -1521    -35       C  
ATOM   5321  O   ILE C 150     -39.661  18.093  21.732  1.00124.17           O  
ANISOU 5321  O   ILE C 150    16313  17497  13367   3965  -1706    -24       O  
ATOM   5322  CB  ILE C 150     -41.749  16.969  24.102  1.00122.51           C  
ANISOU 5322  CB  ILE C 150    14684  17678  14187   3617  -1751   -612       C  
ATOM   5323  CG1 ILE C 150     -42.141  16.059  22.910  1.00126.12           C  
ANISOU 5323  CG1 ILE C 150    15092  18245  14582   3791  -2124   -906       C  
ATOM   5324  CG2 ILE C 150     -42.929  17.215  25.050  1.00123.65           C  
ANISOU 5324  CG2 ILE C 150    14333  17921  14726   3579  -1727   -806       C  
ATOM   5325  CD1 ILE C 150     -42.570  14.662  23.294  1.00132.25           C  
ANISOU 5325  CD1 ILE C 150    15596  19091  15561   3455  -1965  -1034       C  
ATOM   5326  N   HIS C 151     -38.695  17.878  23.776  1.00115.33           N  
ANISOU 5326  N   HIS C 151    14762  16377  12682   3374  -1113    176       N  
ATOM   5327  CA  HIS C 151     -37.328  17.635  23.304  1.00113.86           C  
ANISOU 5327  CA  HIS C 151    14905  16073  12283   3209   -828    425       C  
ATOM   5328  C   HIS C 151     -37.012  16.139  23.236  1.00115.85           C  
ANISOU 5328  C   HIS C 151    14934  16439  12643   2984   -724    341       C  
ATOM   5329  O   HIS C 151     -36.297  15.709  22.329  1.00115.77           O  
ANISOU 5329  O   HIS C 151    15209  16375  12404   2987   -643    430       O  
ATOM   5330  CB  HIS C 151     -36.303  18.361  24.189  1.00112.53           C  
ANISOU 5330  CB  HIS C 151    14808  15776  12173   2987   -482    670       C  
ATOM   5331  CG  HIS C 151     -36.527  19.838  24.284  1.00117.59           C  
ANISOU 5331  CG  HIS C 151    15708  16254  12715   3178   -539    759       C  
ATOM   5332  ND1 HIS C 151     -37.134  20.405  25.390  1.00118.79           N  
ANISOU 5332  ND1 HIS C 151    15603  16438  13094   3174   -575    680       N  
ATOM   5333  CD2 HIS C 151     -36.233  20.816  23.396  1.00121.86           C  
ANISOU 5333  CD2 HIS C 151    16779  16577  12945   3386   -540    919       C  
ATOM   5334  CE1 HIS C 151     -37.183  21.704  25.146  1.00120.19           C  
ANISOU 5334  CE1 HIS C 151    16143  16419  13106   3379   -618    784       C  
ATOM   5335  NE2 HIS C 151     -36.655  21.999  23.957  1.00122.50           N  
ANISOU 5335  NE2 HIS C 151    16928  16543  13072   3510   -591    938       N  
ATOM   5336  N   ARG C 152     -37.541  15.354  24.197  1.00110.78           N  
ANISOU 5336  N   ARG C 152    13820  15931  12342   2797   -690    175       N  
ATOM   5337  CA  ARG C 152     -37.340  13.908  24.283  1.00109.35           C  
ANISOU 5337  CA  ARG C 152    13426  15822  12301   2578   -567     86       C  
ATOM   5338  C   ARG C 152     -38.614  13.127  23.951  1.00115.29           C  
ANISOU 5338  C   ARG C 152    13883  16693  13229   2644   -845   -266       C  
ATOM   5339  O   ARG C 152     -39.614  13.237  24.665  1.00115.49           O  
ANISOU 5339  O   ARG C 152    13550  16796  13535   2635   -924   -454       O  
ATOM   5340  CB  ARG C 152     -36.791  13.514  25.666  1.00106.42           C  
ANISOU 5340  CB  ARG C 152    12813  15459  12164   2290   -240    193       C  
ATOM   5341  CG  ARG C 152     -35.271  13.536  25.752  1.00113.42           C  
ANISOU 5341  CG  ARG C 152    13914  16264  12916   2154     43    462       C  
ATOM   5342  CD  ARG C 152     -34.737  14.807  26.375  1.00120.56           C  
ANISOU 5342  CD  ARG C 152    14925  17092  13790   2146    146    638       C  
ATOM   5343  NE  ARG C 152     -33.279  14.799  26.419  1.00126.49           N  
ANISOU 5343  NE  ARG C 152    15809  17781  14472   1999    405    838       N  
ATOM   5344  N   LEU C 153     -38.568  12.345  22.857  1.00113.33           N  
ANISOU 5344  N   LEU C 153    13778  16453  12830   2705   -983   -380       N  
ATOM   5345  CA  LEU C 153     -39.678  11.517  22.379  1.00115.86           C  
ANISOU 5345  CA  LEU C 153    13831  16875  13315   2750  -1274   -762       C  
ATOM   5346  C   LEU C 153     -39.243  10.037  22.332  1.00118.66           C  
ANISOU 5346  C   LEU C 153    14109  17205  13773   2489  -1071   -821       C  
ATOM   5347  O   LEU C 153     -38.329   9.702  21.577  1.00117.89           O  
ANISOU 5347  O   LEU C 153    14360  17038  13396   2513   -987   -680       O  
ATOM   5348  CB  LEU C 153     -40.157  12.014  20.994  1.00119.65           C  
ANISOU 5348  CB  LEU C 153    14611  17378  13474   3139  -1720   -906       C  
ATOM   5349  CG  LEU C 153     -41.260  11.213  20.286  1.00128.16           C  
ANISOU 5349  CG  LEU C 153    15441  18573  14681   3236  -2117  -1358       C  
ATOM   5350  CD1 LEU C 153     -42.643  11.624  20.765  1.00130.71           C  
ANISOU 5350  CD1 LEU C 153    15288  19032  15346   3343  -2399  -1676       C  
ATOM   5351  CD2 LEU C 153     -41.176  11.395  18.786  1.00133.88           C  
ANISOU 5351  CD2 LEU C 153    16653  19278  14939   3594  -2464  -1410       C  
ATOM   5352  N   PRO C 154     -39.863   9.137  23.131  1.00115.01           N  
ANISOU 5352  N   PRO C 154    13222  16770  13706   2241   -949  -1022       N  
ATOM   5353  CA  PRO C 154     -39.441   7.727  23.095  1.00114.31           C  
ANISOU 5353  CA  PRO C 154    13116  16609  13707   2005   -733  -1066       C  
ATOM   5354  C   PRO C 154     -40.046   6.931  21.940  1.00121.45           C  
ANISOU 5354  C   PRO C 154    14012  17536  14598   2073  -1039  -1418       C  
ATOM   5355  O   PRO C 154     -41.174   7.204  21.527  1.00124.16           O  
ANISOU 5355  O   PRO C 154    14138  17981  15056   2218  -1412  -1746       O  
ATOM   5356  CB  PRO C 154     -39.886   7.190  24.456  1.00115.18           C  
ANISOU 5356  CB  PRO C 154    12845  16694  14225   1725   -438  -1118       C  
ATOM   5357  CG  PRO C 154     -41.044   8.045  24.846  1.00121.25           C  
ANISOU 5357  CG  PRO C 154    13299  17567  15203   1822   -629  -1305       C  
ATOM   5358  CD  PRO C 154     -40.959   9.351  24.101  1.00117.28           C  
ANISOU 5358  CD  PRO C 154    13057  17126  14376   2164   -952  -1212       C  
ATOM   5359  N   VAL C 155     -39.293   5.941  21.423  1.00117.66           N  
ANISOU 5359  N   VAL C 155    13760  16963  13984   1984   -898  -1376       N  
ATOM   5360  CA  VAL C 155     -39.746   5.070  20.336  1.00120.80           C  
ANISOU 5360  CA  VAL C 155    14196  17354  14347   2028  -1162  -1717       C  
ATOM   5361  C   VAL C 155     -40.052   3.664  20.893  1.00125.09           C  
ANISOU 5361  C   VAL C 155    14451  17794  15284   1683   -923  -1922       C  
ATOM   5362  O   VAL C 155     -39.197   3.045  21.533  1.00122.11           O  
ANISOU 5362  O   VAL C 155    14170  17292  14935   1498   -514  -1676       O  
ATOM   5363  CB  VAL C 155     -38.817   5.084  19.080  1.00125.17           C  
ANISOU 5363  CB  VAL C 155    15293  17865  14401   2252  -1240  -1579       C  
ATOM   5364  CG1 VAL C 155     -37.413   4.559  19.371  1.00121.90           C  
ANISOU 5364  CG1 VAL C 155    15115  17329  13872   2107   -782  -1235       C  
ATOM   5365  CG2 VAL C 155     -39.447   4.343  17.906  1.00129.17           C  
ANISOU 5365  CG2 VAL C 155    15864  18385  14830   2361  -1609  -1986       C  
ATOM   5366  N   ILE C 156     -41.305   3.205  20.703  1.00125.30           N  
ANISOU 5366  N   ILE C 156    14107  17861  15638   1605  -1173  -2385       N  
ATOM   5367  CA  ILE C 156     -41.790   1.908  21.191  1.00126.63           C  
ANISOU 5367  CA  ILE C 156    13978  17896  16241   1249   -939  -2643       C  
ATOM   5368  C   ILE C 156     -42.237   1.028  20.017  1.00134.53           C  
ANISOU 5368  C   ILE C 156    14998  18869  17249   1258  -1258  -3078       C  
ATOM   5369  O   ILE C 156     -43.030   1.473  19.184  1.00137.44           O  
ANISOU 5369  O   ILE C 156    15257  19391  17573   1481  -1767  -3413       O  
ATOM   5370  CB  ILE C 156     -42.916   2.066  22.264  1.00130.95           C  
ANISOU 5370  CB  ILE C 156    13976  18477  17301   1043   -825  -2840       C  
ATOM   5371  CG1 ILE C 156     -42.553   3.120  23.342  1.00127.77           C  
ANISOU 5371  CG1 ILE C 156    13587  18127  16833   1102   -594  -2446       C  
ATOM   5372  CG2 ILE C 156     -43.264   0.714  22.907  1.00133.20           C  
ANISOU 5372  CG2 ILE C 156    14033  18552  18025    631   -431  -3025       C  
ATOM   5373  CD1 ILE C 156     -43.734   3.703  24.136  1.00136.85           C  
ANISOU 5373  CD1 ILE C 156    14246  19377  18374   1050   -612  -2651       C  
ATOM   5374  N   ASP C 157     -41.737  -0.224  19.972  1.00131.12           N  
ANISOU 5374  N   ASP C 157    14719  18234  16869   1038   -976  -3088       N  
ATOM   5375  CA  ASP C 157     -42.069  -1.213  18.944  1.00134.87           C  
ANISOU 5375  CA  ASP C 157    15244  18632  17368    999  -1214  -3506       C  
ATOM   5376  C   ASP C 157     -43.518  -1.700  19.108  1.00143.29           C  
ANISOU 5376  C   ASP C 157    15732  19701  19010    749  -1373  -4074       C  
ATOM   5377  O   ASP C 157     -43.905  -2.046  20.225  1.00142.54           O  
ANISOU 5377  O   ASP C 157    15309  19493  19357    423   -976  -4070       O  
ATOM   5378  CB  ASP C 157     -41.095  -2.398  19.001  1.00135.39           C  
ANISOU 5378  CB  ASP C 157    15638  18445  17360    826   -800  -3330       C  
ATOM   5379  N   PRO C 158     -44.344  -1.720  18.033  1.00144.56           N  
ANISOU 5379  N   PRO C 158    15752  19988  19185    900  -1942  -4583       N  
ATOM   5380  CA  PRO C 158     -45.738  -2.175  18.199  1.00149.34           C  
ANISOU 5380  CA  PRO C 158    15717  20611  20413    640  -2100  -5184       C  
ATOM   5381  C   PRO C 158     -45.889  -3.687  18.387  1.00155.37           C  
ANISOU 5381  C   PRO C 158    16366  21080  21586    186  -1756  -5459       C  
ATOM   5382  O   PRO C 158     -46.735  -4.113  19.175  1.00157.23           O  
ANISOU 5382  O   PRO C 158    16094  21219  22426   -187  -1493  -5719       O  
ATOM   5383  CB  PRO C 158     -46.441  -1.660  16.941  1.00155.60           C  
ANISOU 5383  CB  PRO C 158    16449  21648  21022   1017  -2877  -5632       C  
ATOM   5384  CG  PRO C 158     -45.369  -1.528  15.926  1.00158.40           C  
ANISOU 5384  CG  PRO C 158    17521  21996  20669   1366  -3041  -5350       C  
ATOM   5385  CD  PRO C 158     -44.059  -1.329  16.635  1.00147.68           C  
ANISOU 5385  CD  PRO C 158    16567  20511  19033   1324  -2462  -4657       C  
ATOM   5386  N   GLU C 159     -45.067  -4.488  17.680  1.00151.51           N  
ANISOU 5386  N   GLU C 159    16368  20423  20775    215  -1716  -5396       N  
ATOM   5387  CA  GLU C 159     -45.080  -5.951  17.752  1.00153.66           C  
ANISOU 5387  CA  GLU C 159    16650  20370  21365   -177  -1389  -5630       C  
ATOM   5388  C   GLU C 159     -44.499  -6.465  19.071  1.00153.79           C  
ANISOU 5388  C   GLU C 159    16759  20112  21563   -482   -629  -5188       C  
ATOM   5389  O   GLU C 159     -45.021  -7.433  19.627  1.00156.14           O  
ANISOU 5389  O   GLU C 159    16822  20140  22365   -902   -265  -5425       O  
ATOM   5390  CB  GLU C 159     -44.332  -6.561  16.558  1.00155.93           C  
ANISOU 5390  CB  GLU C 159    17485  20569  21192     16  -1594  -5680       C  
ATOM   5391  N   SER C 160     -43.423  -5.820  19.567  1.00144.58           N  
ANISOU 5391  N   SER C 160    15949  18999  19985   -265   -392  -4564       N  
ATOM   5392  CA  SER C 160     -42.755  -6.188  20.816  1.00140.95           C  
ANISOU 5392  CA  SER C 160    15641  18317  19597   -452    257  -4108       C  
ATOM   5393  C   SER C 160     -43.462  -5.591  22.039  1.00143.88           C  
ANISOU 5393  C   SER C 160    15590  18746  20332   -617    494  -4042       C  
ATOM   5394  O   SER C 160     -43.815  -6.332  22.958  1.00144.84           O  
ANISOU 5394  O   SER C 160    15572  18608  20852   -968    980  -4078       O  
ATOM   5395  CB  SER C 160     -41.285  -5.779  20.783  1.00139.50           C  
ANISOU 5395  CB  SER C 160    15978  18181  18844   -141    365  -3536       C  
ATOM   5396  N   GLY C 161     -43.665  -4.273  22.027  1.00138.52           N  
ANISOU 5396  N   GLY C 161    14750  18381  19502   -355    178  -3949       N  
ATOM   5397  CA  GLY C 161     -44.321  -3.542  23.108  1.00137.68           C  
ANISOU 5397  CA  GLY C 161    14260  18367  19685   -444    354  -3888       C  
ATOM   5398  C   GLY C 161     -43.382  -2.785  24.029  1.00135.94           C  
ANISOU 5398  C   GLY C 161    14316  18189  19147   -284    634  -3290       C  
ATOM   5399  O   GLY C 161     -43.844  -1.981  24.844  1.00134.73           O  
ANISOU 5399  O   GLY C 161    13904  18147  19139   -281    717  -3212       O  
ATOM   5400  N   ASN C 162     -42.061  -3.038  23.912  1.00128.93           N  
ANISOU 5400  N   ASN C 162    13934  17212  17840   -146    776  -2892       N  
ATOM   5401  CA  ASN C 162     -41.021  -2.420  24.741  1.00123.94           C  
ANISOU 5401  CA  ASN C 162    13574  16613  16906      6   1020  -2354       C  
ATOM   5402  C   ASN C 162     -40.331  -1.219  24.093  1.00124.64           C  
ANISOU 5402  C   ASN C 162    13859  16953  16547    368    663  -2128       C  
ATOM   5403  O   ASN C 162     -40.267  -1.130  22.864  1.00125.39           O  
ANISOU 5403  O   ASN C 162    14081  17136  16426    542    296  -2287       O  
ATOM   5404  CB  ASN C 162     -39.990  -3.466  25.166  1.00123.36           C  
ANISOU 5404  CB  ASN C 162    13884  16274  16711    -69   1440  -2074       C  
ATOM   5405  N   THR C 163     -39.806  -0.301  24.935  1.00117.59           N  
ANISOU 5405  N   THR C 163    13023  16149  15505    479    795  -1760       N  
ATOM   5406  CA  THR C 163     -39.080   0.908  24.522  1.00114.64           C  
ANISOU 5406  CA  THR C 163    12847  15965  14745    776    559  -1504       C  
ATOM   5407  C   THR C 163     -37.739   0.537  23.894  1.00116.49           C  
ANISOU 5407  C   THR C 163    13497  16143  14620    904    623  -1265       C  
ATOM   5408  O   THR C 163     -37.080  -0.396  24.360  1.00115.34           O  
ANISOU 5408  O   THR C 163    13498  15831  14495    800    948  -1122       O  
ATOM   5409  CB  THR C 163     -38.865   1.861  25.708  1.00120.17           C  
ANISOU 5409  CB  THR C 163    13487  16735  15439    807    730  -1212       C  
ATOM   5410  OG1 THR C 163     -38.301   1.138  26.804  1.00118.71           O  
ANISOU 5410  OG1 THR C 163    13404  16383  15317    660   1160   -991       O  
ATOM   5411  CG2 THR C 163     -40.141   2.567  26.140  1.00120.35           C  
ANISOU 5411  CG2 THR C 163    13119  16863  15744    773    606  -1434       C  
ATOM   5412  N   LEU C 164     -37.336   1.271  22.845  1.00112.56           N  
ANISOU 5412  N   LEU C 164    13206  15772  13790   1150    336  -1221       N  
ATOM   5413  CA  LEU C 164     -36.083   1.016  22.133  1.00111.25           C  
ANISOU 5413  CA  LEU C 164    13420  15564  13284   1285    417  -1018       C  
ATOM   5414  C   LEU C 164     -35.066   2.143  22.303  1.00112.04           C  
ANISOU 5414  C   LEU C 164    13687  15761  13124   1446    486   -654       C  
ATOM   5415  O   LEU C 164     -33.925   1.877  22.679  1.00109.78           O  
ANISOU 5415  O   LEU C 164    13538  15422  12753   1442    759   -399       O  
ATOM   5416  CB  LEU C 164     -36.341   0.740  20.639  1.00114.22           C  
ANISOU 5416  CB  LEU C 164    13988  15952  13457   1425    107  -1282       C  
ATOM   5417  CG  LEU C 164     -37.202  -0.479  20.297  1.00122.24           C  
ANISOU 5417  CG  LEU C 164    14870  16853  14725   1256     23  -1692       C  
ATOM   5418  CD1 LEU C 164     -37.894  -0.294  18.967  1.00125.89           C  
ANISOU 5418  CD1 LEU C 164    15404  17408  15022   1439   -452  -2039       C  
ATOM   5419  CD2 LEU C 164     -36.382  -1.761  20.304  1.00124.61           C  
ANISOU 5419  CD2 LEU C 164    15388  16947  15012   1151    345  -1621       C  
ATOM   5420  N   TYR C 165     -35.476   3.395  22.031  1.00108.50           N  
ANISOU 5420  N   TYR C 165    13220  15439  12565   1593    236   -648       N  
ATOM   5421  CA  TYR C 165     -34.605   4.568  22.114  1.00106.25           C  
ANISOU 5421  CA  TYR C 165    13103  15212  12054   1722    301   -338       C  
ATOM   5422  C   TYR C 165     -35.393   5.845  22.436  1.00109.77           C  
ANISOU 5422  C   TYR C 165    13407  15754  12545   1805     90   -356       C  
ATOM   5423  O   TYR C 165     -36.599   5.906  22.194  1.00111.44           O  
ANISOU 5423  O   TYR C 165    13442  16019  12880   1846   -188   -636       O  
ATOM   5424  CB  TYR C 165     -33.811   4.717  20.792  1.00108.57           C  
ANISOU 5424  CB  TYR C 165    13792  15487  11971   1910    265   -260       C  
ATOM   5425  CG  TYR C 165     -32.832   5.871  20.756  1.00109.09           C  
ANISOU 5425  CG  TYR C 165    14055  15569  11825   2006    400     45       C  
ATOM   5426  CD1 TYR C 165     -31.641   5.824  21.474  1.00108.94           C  
ANISOU 5426  CD1 TYR C 165    13998  15529  11864   1905    728    290       C  
ATOM   5427  CD2 TYR C 165     -33.091   7.006  19.993  1.00111.30           C  
ANISOU 5427  CD2 TYR C 165    14567  15867  11854   2206    201     71       C  
ATOM   5428  CE1 TYR C 165     -30.738   6.886  21.448  1.00109.14           C  
ANISOU 5428  CE1 TYR C 165    14156  15558  11757   1950    869    525       C  
ATOM   5429  CE2 TYR C 165     -32.193   8.071  19.954  1.00111.49           C  
ANISOU 5429  CE2 TYR C 165    14792  15857  11712   2257    380    344       C  
ATOM   5430  CZ  TYR C 165     -31.018   8.008  20.685  1.00117.04           C  
ANISOU 5430  CZ  TYR C 165    15397  16543  12529   2103    723    556       C  
ATOM   5431  OH  TYR C 165     -30.133   9.057  20.659  1.00118.08           O  
ANISOU 5431  OH  TYR C 165    15678  16630  12558   2110    915    780       O  
ATOM   5432  N   ILE C 166     -34.710   6.854  23.001  1.00104.05           N  
ANISOU 5432  N   ILE C 166    12741  15049  11745   1832    220    -85       N  
ATOM   5433  CA  ILE C 166     -35.308   8.149  23.323  1.00103.73           C  
ANISOU 5433  CA  ILE C 166    12626  15068  11719   1930     56    -67       C  
ATOM   5434  C   ILE C 166     -34.746   9.181  22.334  1.00108.07           C  
ANISOU 5434  C   ILE C 166    13553  15592  11918   2140    -27     87       C  
ATOM   5435  O   ILE C 166     -33.603   9.627  22.479  1.00106.21           O  
ANISOU 5435  O   ILE C 166    13477  15305  11572   2104    213    343       O  
ATOM   5436  CB  ILE C 166     -35.111   8.537  24.818  1.00104.50           C  
ANISOU 5436  CB  ILE C 166    12513  15175  12018   1789    267     82       C  
ATOM   5437  CG1 ILE C 166     -35.667   7.445  25.761  1.00104.79           C  
ANISOU 5437  CG1 ILE C 166    12265  15193  12358   1594    413    -50       C  
ATOM   5438  CG2 ILE C 166     -35.758   9.890  25.115  1.00105.50           C  
ANISOU 5438  CG2 ILE C 166    12584  15346  12156   1906     99     81       C  
ATOM   5439  CD1 ILE C 166     -34.845   7.214  27.022  1.00110.06           C  
ANISOU 5439  CD1 ILE C 166    12902  15822  13094   1470    719    162       C  
ATOM   5440  N   LEU C 167     -35.546   9.516  21.303  1.00107.18           N  
ANISOU 5440  N   LEU C 167    13593  15500  11631   2368   -362    -87       N  
ATOM   5441  CA  LEU C 167     -35.184  10.453  20.236  1.00108.56           C  
ANISOU 5441  CA  LEU C 167    14221  15611  11416   2619   -453     44       C  
ATOM   5442  C   LEU C 167     -35.024  11.888  20.720  1.00111.27           C  
ANISOU 5442  C   LEU C 167    14651  15907  11720   2680   -400    250       C  
ATOM   5443  O   LEU C 167     -35.839  12.377  21.505  1.00110.48           O  
ANISOU 5443  O   LEU C 167    14281  15864  11833   2683   -535    162       O  
ATOM   5444  CB  LEU C 167     -36.184  10.389  19.069  1.00112.40           C  
ANISOU 5444  CB  LEU C 167    14868  16137  11703   2901   -886   -228       C  
ATOM   5445  CG  LEU C 167     -36.131   9.137  18.192  1.00118.86           C  
ANISOU 5445  CG  LEU C 167    15786  16955  12420   2901   -951   -418       C  
ATOM   5446  CD1 LEU C 167     -37.471   8.870  17.551  1.00122.70           C  
ANISOU 5446  CD1 LEU C 167    16165  17536  12920   3096  -1451   -821       C  
ATOM   5447  CD2 LEU C 167     -35.055   9.252  17.125  1.00122.39           C  
ANISOU 5447  CD2 LEU C 167    16783  17289  12430   3036   -770   -208       C  
ATOM   5448  N   THR C 168     -33.959  12.553  20.245  1.00107.63           N  
ANISOU 5448  N   THR C 168    14572  15321  11001   2717   -171    511       N  
ATOM   5449  CA  THR C 168     -33.611  13.938  20.579  1.00107.09           C  
ANISOU 5449  CA  THR C 168    14666  15147  10876   2747    -58    721       C  
ATOM   5450  C   THR C 168     -33.362  14.752  19.309  1.00113.68           C  
ANISOU 5450  C   THR C 168    16088  15819  11285   3006    -69    851       C  
ATOM   5451  O   THR C 168     -33.027  14.177  18.270  1.00114.87           O  
ANISOU 5451  O   THR C 168    16531  15937  11177   3100    -35    844       O  
ATOM   5452  CB  THR C 168     -32.371  13.979  21.493  1.00112.52           C  
ANISOU 5452  CB  THR C 168    15201  15802  11750   2457    340    921       C  
ATOM   5453  OG1 THR C 168     -31.323  13.197  20.914  1.00111.80           O  
ANISOU 5453  OG1 THR C 168    15235  15684  11560   2372    596    999       O  
ATOM   5454  CG2 THR C 168     -32.663  13.511  22.915  1.00108.73           C  
ANISOU 5454  CG2 THR C 168    14236  15443  11632   2260    346    836       C  
ATOM   5455  N   HIS C 169     -33.498  16.095  19.403  1.00111.07           N  
ANISOU 5455  N   HIS C 169    15979  15360  10862   3129    -85    978       N  
ATOM   5456  CA  HIS C 169     -33.262  17.036  18.300  1.00114.15           C  
ANISOU 5456  CA  HIS C 169    17008  15534  10830   3387    -39   1145       C  
ATOM   5457  C   HIS C 169     -31.804  16.996  17.826  1.00117.72           C  
ANISOU 5457  C   HIS C 169    17751  15829  11149   3207    460   1381       C  
ATOM   5458  O   HIS C 169     -31.539  17.227  16.645  1.00120.50           O  
ANISOU 5458  O   HIS C 169    18663  16022  11099   3411    550   1485       O  
ATOM   5459  CB  HIS C 169     -33.643  18.464  18.713  1.00115.86           C  
ANISOU 5459  CB  HIS C 169    17369  15610  11043   3509   -100   1241       C  
ATOM   5460  CG  HIS C 169     -35.118  18.715  18.730  1.00120.85           C  
ANISOU 5460  CG  HIS C 169    17893  16350  11675   3829   -610   1015       C  
ATOM   5461  ND1 HIS C 169     -35.757  19.323  17.665  1.00126.82           N  
ANISOU 5461  ND1 HIS C 169    19156  17000  12031   4277   -908    997       N  
ATOM   5462  CD2 HIS C 169     -36.033  18.434  19.686  1.00120.95           C  
ANISOU 5462  CD2 HIS C 169    17348  16562  12045   3774   -849    791       C  
ATOM   5463  CE1 HIS C 169     -37.034  19.392  18.005  1.00126.98           C  
ANISOU 5463  CE1 HIS C 169    18856  17182  12209   4485  -1352    739       C  
ATOM   5464  NE2 HIS C 169     -37.248  18.869  19.212  1.00123.88           N  
ANISOU 5464  NE2 HIS C 169    17812  16972  12286   4176  -1304    607       N  
ATOM   5465  N   LYS C 170     -30.869  16.691  18.752  1.00110.85           N  
ANISOU 5465  N   LYS C 170    16499  15006  10612   2846    784   1449       N  
ATOM   5466  CA  LYS C 170     -29.434  16.575  18.490  1.00110.60           C  
ANISOU 5466  CA  LYS C 170    16578  14869  10575   2633   1270   1620       C  
ATOM   5467  C   LYS C 170     -29.120  15.342  17.642  1.00114.46           C  
ANISOU 5467  C   LYS C 170    17154  15432  10905   2680   1329   1556       C  
ATOM   5468  O   LYS C 170     -28.263  15.418  16.762  1.00116.26           O  
ANISOU 5468  O   LYS C 170    17756  15513  10905   2693   1670   1693       O  
ATOM   5469  CB  LYS C 170     -28.647  16.534  19.808  1.00110.11           C  
ANISOU 5469  CB  LYS C 170    16012  14885  10940   2288   1485   1642       C  
ATOM   5470  N   ARG C 171     -29.819  14.216  17.900  1.00108.97           N  
ANISOU 5470  N   ARG C 171    16130  14938  10334   2699   1031   1340       N  
ATOM   5471  CA  ARG C 171     -29.643  12.951  17.181  1.00109.21           C  
ANISOU 5471  CA  ARG C 171    16216  15035  10245   2741   1043   1233       C  
ATOM   5472  C   ARG C 171     -30.199  13.007  15.751  1.00116.54           C  
ANISOU 5472  C   ARG C 171    17700  15882  10699   3084    836   1174       C  
ATOM   5473  O   ARG C 171     -29.610  12.400  14.855  1.00117.83           O  
ANISOU 5473  O   ARG C 171    18151  15994  10626   3140   1026   1193       O  
ATOM   5474  CB  ARG C 171     -30.257  11.781  17.978  1.00106.85           C  
ANISOU 5474  CB  ARG C 171    15410  14928  10259   2626    815   1011       C  
ATOM   5475  CG  ARG C 171     -29.828  10.377  17.526  1.00116.33           C  
ANISOU 5475  CG  ARG C 171    16588  16172  11439   2586    920    915       C  
ATOM   5476  CD  ARG C 171     -28.413  10.011  17.950  1.00122.91           C  
ANISOU 5476  CD  ARG C 171    17267  16994  12440   2376   1360   1070       C  
ATOM   5477  NE  ARG C 171     -28.170   8.570  17.856  1.00129.22           N  
ANISOU 5477  NE  ARG C 171    17942  17848  13308   2336   1412    950       N  
ATOM   5478  CZ  ARG C 171     -27.680   7.956  16.783  1.00144.78           C  
ANISOU 5478  CZ  ARG C 171    20221  19759  15032   2442   1560    933       C  
ATOM   5479  NH1 ARG C 171     -27.375   8.648  15.693  1.00134.85           N  
ANISOU 5479  NH1 ARG C 171    19438  18385  13416   2598   1691   1040       N  
ATOM   5480  NH2 ARG C 171     -27.496   6.643  16.791  1.00130.87           N  
ANISOU 5480  NH2 ARG C 171    18337  18029  13359   2406   1601    814       N  
ATOM   5481  N   ILE C 172     -31.323  13.728  15.541  1.00114.50           N  
ANISOU 5481  N   ILE C 172    17606  15613  10286   3344    437   1090       N  
ATOM   5482  CA  ILE C 172     -31.968  13.880  14.229  1.00118.40           C  
ANISOU 5482  CA  ILE C 172    18653  16040  10293   3746    142   1008       C  
ATOM   5483  C   ILE C 172     -31.084  14.710  13.278  1.00124.98           C  
ANISOU 5483  C   ILE C 172    20184  16607  10694   3877    529   1296       C  
ATOM   5484  O   ILE C 172     -30.865  14.287  12.141  1.00127.52           O  
ANISOU 5484  O   ILE C 172    20977  16861  10616   4074    580   1289       O  
ATOM   5485  CB  ILE C 172     -33.433  14.410  14.345  1.00122.85           C  
ANISOU 5485  CB  ILE C 172    19137  16689  10852   4023   -430    804       C  
ATOM   5486  CG1 ILE C 172     -34.306  13.453  15.197  1.00120.92           C  
ANISOU 5486  CG1 ILE C 172    18199  16690  11056   3861   -737    488       C  
ATOM   5487  CG2 ILE C 172     -34.071  14.633  12.958  1.00128.64           C  
ANISOU 5487  CG2 ILE C 172    20487  17355  11035   4508   -793    706       C  
ATOM   5488  CD1 ILE C 172     -35.500  14.107  15.921  1.00128.35           C  
ANISOU 5488  CD1 ILE C 172    18807  17726  12233   3958  -1103    338       C  
ATOM   5489  N   LEU C 173     -30.554  15.860  13.753  1.00120.87           N  
ANISOU 5489  N   LEU C 173    19743  15919  10263   3750    838   1540       N  
ATOM   5490  CA  LEU C 173     -29.679  16.734  12.963  1.00123.87           C  
ANISOU 5490  CA  LEU C 173    20768  15995  10300   3809   1302   1827       C  
ATOM   5491  C   LEU C 173     -28.319  16.080  12.665  1.00127.52           C  
ANISOU 5491  C   LEU C 173    21233  16412  10807   3552   1872   1936       C  
ATOM   5492  O   LEU C 173     -27.750  16.334  11.601  1.00130.90           O  
ANISOU 5492  O   LEU C 173    22281  16619  10837   3683   2221   2099       O  
ATOM   5493  CB  LEU C 173     -29.501  18.107  13.630  1.00123.74           C  
ANISOU 5493  CB  LEU C 173    20788  15791  10438   3697   1487   2017       C  
ATOM   5494  CG  LEU C 173     -28.545  19.067  12.916  1.00133.21           C  
ANISOU 5494  CG  LEU C 173    22808  16612  11193   3885   1829   2286       C  
ATOM   5495  CD1 LEU C 173     -29.051  19.424  11.532  1.00136.33           C  
ANISOU 5495  CD1 LEU C 173    23660  16908  11230   4353   1356   2266       C  
ATOM   5496  CD2 LEU C 173     -28.324  20.319  13.729  1.00135.22           C  
ANISOU 5496  CD2 LEU C 173    22977  16652  11749   3504   2393   2494       C  
ATOM   5497  N   LYS C 174     -27.815  15.231  13.589  1.00120.12           N  
ANISOU 5497  N   LYS C 174    19630  15674  10336   3219   1974   1844       N  
ATOM   5498  CA  LYS C 174     -26.558  14.493  13.418  1.00119.77           C  
ANISOU 5498  CA  LYS C 174    19477  15631  10398   3000   2461   1900       C  
ATOM   5499  C   LYS C 174     -26.731  13.416  12.343  1.00125.59           C  
ANISOU 5499  C   LYS C 174    20516  16416  10785   3231   2356   1774       C  
ATOM   5500  O   LYS C 174     -25.801  13.158  11.578  1.00127.52           O  
ANISOU 5500  O   LYS C 174    21065  16547  10841   3225   2801   1873       O  
ATOM   5501  CB  LYS C 174     -26.104  13.861  14.742  1.00117.99           C  
ANISOU 5501  CB  LYS C 174    18485  15611  10734   2663   2502   1817       C  
ATOM   5502  N   PHE C 175     -27.937  12.809  12.281  1.00121.61           N  
ANISOU 5502  N   PHE C 175    19924  16072  10209   3432   1777   1531       N  
ATOM   5503  CA  PHE C 175     -28.322  11.795  11.298  1.00123.59           C  
ANISOU 5503  CA  PHE C 175    20448  16376  10136   3669   1555   1339       C  
ATOM   5504  C   PHE C 175     -28.469  12.445   9.917  1.00132.69           C  
ANISOU 5504  C   PHE C 175    22454  17321  10641   4054   1562   1436       C  
ATOM   5505  O   PHE C 175     -28.150  11.812   8.909  1.00134.95           O  
ANISOU 5505  O   PHE C 175    23150  17555  10570   4215   1685   1396       O  
ATOM   5506  CB  PHE C 175     -29.636  11.111  11.723  1.00123.86           C  
ANISOU 5506  CB  PHE C 175    20089  16623  10350   3736    925   1015       C  
ATOM   5507  CG  PHE C 175     -30.135  10.022  10.801  1.00127.81           C  
ANISOU 5507  CG  PHE C 175    20794  17184  10584   3947    629    745       C  
ATOM   5508  CD1 PHE C 175     -29.667   8.719  10.919  1.00129.51           C  
ANISOU 5508  CD1 PHE C 175    20740  17472  10995   3765    779    624       C  
ATOM   5509  CD2 PHE C 175     -31.099  10.293   9.837  1.00133.98           C  
ANISOU 5509  CD2 PHE C 175    22040  17945  10921   4350    167    586       C  
ATOM   5510  CE1 PHE C 175     -30.133   7.712  10.069  1.00132.92           C  
ANISOU 5510  CE1 PHE C 175    21375  17935  11192   3945    506    347       C  
ATOM   5511  CE2 PHE C 175     -31.562   9.286   8.986  1.00139.44           C  
ANISOU 5511  CE2 PHE C 175    22916  18695  11371   4544   -144    290       C  
ATOM   5512  CZ  PHE C 175     -31.077   8.003   9.108  1.00136.00           C  
ANISOU 5512  CZ  PHE C 175    22212  18314  11148   4321     39    169       C  
ATOM   5513  N   LEU C 176     -28.962  13.704   9.880  1.00131.05           N  
ANISOU 5513  N   LEU C 176    22554  16980  10259   4229   1434   1564       N  
ATOM   5514  CA  LEU C 176     -29.148  14.483   8.655  1.00136.35           C  
ANISOU 5514  CA  LEU C 176    24112  17413  10280   4642   1435   1694       C  
ATOM   5515  C   LEU C 176     -27.807  14.874   8.043  1.00143.30           C  
ANISOU 5515  C   LEU C 176    25485  18017  10945   4535   2209   2002       C  
ATOM   5516  O   LEU C 176     -27.633  14.709   6.838  1.00147.25           O  
ANISOU 5516  O   LEU C 176    26677  18376  10896   4821   2343   2044       O  
ATOM   5517  CB  LEU C 176     -30.010  15.733   8.912  1.00137.37           C  
ANISOU 5517  CB  LEU C 176    24409  17455  10333   4857   1108   1756       C  
ATOM   5518  CG  LEU C 176     -31.522  15.514   8.984  1.00142.30           C  
ANISOU 5518  CG  LEU C 176    24831  18297  10939   5164    294   1429       C  
ATOM   5519  CD1 LEU C 176     -32.175  16.539   9.886  1.00140.98           C  
ANISOU 5519  CD1 LEU C 176    24393  18130  11042   5160     72   1463       C  
ATOM   5520  CD2 LEU C 176     -32.156  15.550   7.599  1.00150.49           C  
ANISOU 5520  CD2 LEU C 176    26643  19256  11282   5732    -83   1330       C  
ATOM   5521  N   LYS C 177     -26.847  15.340   8.877  1.00138.01           N  
ANISOU 5521  N   LYS C 177    24440  17276  10720   4119   2726   2188       N  
ATOM   5522  CA  LYS C 177     -25.493  15.740   8.466  1.00140.61           C  
ANISOU 5522  CA  LYS C 177    25074  17351  10999   3924   3528   2446       C  
ATOM   5523  C   LYS C 177     -24.694  14.586   7.838  1.00146.36           C  
ANISOU 5523  C   LYS C 177    25827  18139  11643   3882   3864   2384       C  
ATOM   5524  O   LYS C 177     -23.741  14.834   7.098  1.00149.56           O  
ANISOU 5524  O   LYS C 177    26687  18311  11828   3854   4508   2571       O  
ATOM   5525  CB  LYS C 177     -24.727  16.347   9.651  1.00140.18           C  
ANISOU 5525  CB  LYS C 177    24433  17277  11553   3460   3889   2554       C  
ATOM   5526  N   LEU C 178     -25.096  13.334   8.129  1.00140.82           N  
ANISOU 5526  N   LEU C 178    24658  17727  11120   3880   3457   2117       N  
ATOM   5527  CA  LEU C 178     -24.495  12.106   7.610  1.00141.67           C  
ANISOU 5527  CA  LEU C 178    24749  17914  11167   3875   3671   2007       C  
ATOM   5528  C   LEU C 178     -24.946  11.840   6.161  1.00151.85           C  
ANISOU 5528  C   LEU C 178    26876  19089  11731   4326   3526   1951       C  
ATOM   5529  O   LEU C 178     -24.109  11.518   5.315  1.00154.62           O  
ANISOU 5529  O   LEU C 178    27639  19306  11805   4379   4033   2033       O  
ATOM   5530  CB  LEU C 178     -24.869  10.923   8.534  1.00136.90           C  
ANISOU 5530  CB  LEU C 178    23372  17615  11026   3711   3263   1740       C  
ATOM   5531  CG  LEU C 178     -24.474   9.510   8.091  1.00141.84           C  
ANISOU 5531  CG  LEU C 178    23949  18333  11611   3740   3346   1570       C  
ATOM   5532  CD1 LEU C 178     -23.050   9.180   8.500  1.00141.06           C  
ANISOU 5532  CD1 LEU C 178    23475  18237  11885   3443   3978   1677       C  
ATOM   5533  CD2 LEU C 178     -25.425   8.482   8.666  1.00140.98           C  
ANISOU 5533  CD2 LEU C 178    23373  18451  11741   3732   2745   1269       C  
ATOM   5534  N   PHE C 179     -26.261  11.971   5.887  1.00150.46           N  
ANISOU 5534  N   PHE C 179    26938  18974  11255   4665   2828   1787       N  
ATOM   5535  CA  PHE C 179     -26.866  11.725   4.574  1.00155.76           C  
ANISOU 5535  CA  PHE C 179    28382  19575  11224   5150   2521   1667       C  
ATOM   5536  C   PHE C 179     -26.870  12.936   3.628  1.00166.41           C  
ANISOU 5536  C   PHE C 179    30693  20605  11930   5502   2720   1930       C  
ATOM   5537  O   PHE C 179     -26.859  12.743   2.410  1.00170.90           O  
ANISOU 5537  O   PHE C 179    32047  21039  11849   5873   2766   1925       O  
ATOM   5538  CB  PHE C 179     -28.287  11.165   4.734  1.00156.50           C  
ANISOU 5538  CB  PHE C 179    28197  19915  11352   5354   1629   1291       C  
ATOM   5539  N   ILE C 180     -26.891  14.171   4.177  1.00163.57           N  
ANISOU 5539  N   ILE C 180    30324  20102  11722   5408   2842   2158       N  
ATOM   5540  CA  ILE C 180     -26.915  15.414   3.393  1.00169.31           C  
ANISOU 5540  CA  ILE C 180    31984  20476  11872   5730   3058   2438       C  
ATOM   5541  C   ILE C 180     -25.600  15.701   2.651  1.00178.63           C  
ANISOU 5541  C   ILE C 180    33764  21323  12785   5628   4008   2746       C  
ATOM   5542  O   ILE C 180     -25.616  16.476   1.694  1.00181.10           O  
ANISOU 5542  O   ILE C 180    34479  21543  12788   5612   4024   2883       O  
ATOM   5543  CB  ILE C 180     -27.352  16.625   4.248  1.00170.72           C  
ANISOU 5543  CB  ILE C 180    31962  20576  12329   5646   2913   2570       C  
ATOM   5544  N   THR C 181     -24.475  15.086   3.083  1.00173.68           N  
ANISOU 5544  N   THR C 181    32572  20770  12649   5167   4586   2762       N  
ATOM   5545  CA  THR C 181     -23.147  15.255   2.467  1.00177.87           C  
ANISOU 5545  CA  THR C 181    33506  21021  13057   5005   5548   3006       C  
ATOM   5546  C   THR C 181     -23.104  14.801   1.003  1.00183.71           C  
ANISOU 5546  C   THR C 181    34293  22011  13499   4896   5299   2868       C  
ATOM   5547  O   THR C 181     -22.406  15.417   0.196  1.00184.40           O  
ANISOU 5547  O   THR C 181    34310  22137  13617   4508   5608   3004       O  
ATOM   5548  CB  THR C 181     -22.046  14.584   3.304  1.00183.44           C  
ANISOU 5548  CB  THR C 181    33291  21905  14504   4469   6006   2944       C  
ATOM   5549  OG1 THR C 181     -22.468  13.279   3.708  1.00179.07           O  
ANISOU 5549  OG1 THR C 181    32128  21721  14190   4468   5458   2628       O  
ATOM   5550  CG2 THR C 181     -21.643  15.411   4.516  1.00178.49           C  
ANISOU 5550  CG2 THR C 181    32005  21266  14549   4017   6206   3047       C  
ATOM   5551  N   GLU C 182     -23.856  13.735   0.668  1.00181.86           N  
ANISOU 5551  N   GLU C 182    34286  21903  12908   5326   4786   2605       N  
ATOM   5552  CA  GLU C 182     -23.944  13.179  -0.683  1.00183.05           C  
ANISOU 5552  CA  GLU C 182    34431  22320  12801   5230   4479   2420       C  
ATOM   5553  C   GLU C 182     -24.892  13.981  -1.590  1.00187.28           C  
ANISOU 5553  C   GLU C 182    34771  23133  13256   5054   3732   2366       C  
ATOM   5554  O   GLU C 182     -24.805  13.862  -2.815  1.00188.05           O  
ANISOU 5554  O   GLU C 182    34856  23436  13159   4886   3627   2311       O  
ATOM   5555  CB  GLU C 182     -24.370  11.704  -0.628  1.00183.72           C  
ANISOU 5555  CB  GLU C 182    34425  22567  12813   5487   4099   2078       C  
ATOM   5556  N   PHE C 183     -25.788  14.796  -0.992  1.00185.10           N  
ANISOU 5556  N   PHE C 183    34731  22702  12896   5364   3374   2438       N  
ATOM   5557  CA  PHE C 183     -26.769  15.613  -1.712  1.00186.07           C  
ANISOU 5557  CA  PHE C 183    34874  22969  12855   5391   2750   2433       C  
ATOM   5558  C   PHE C 183     -26.329  17.083  -1.867  1.00190.22           C  
ANISOU 5558  C   PHE C 183    35156  23467  13652   4918   3012   2757       C  
ATOM   5559  O   PHE C 183     -25.796  17.652  -0.912  1.00189.17           O  
ANISOU 5559  O   PHE C 183    35069  23063  13742   4859   3476   2951       O  
ATOM   5560  CB  PHE C 183     -28.139  15.533  -1.022  1.00186.69           C  
ANISOU 5560  CB  PHE C 183    34826  23131  12976   5750   1967   2201       C  
ATOM   5561  N   PRO C 184     -26.555  17.728  -3.041  1.00189.94           N  
ANISOU 5561  N   PRO C 184    35266  23540  13363   4842   2838   2862       N  
ATOM   5562  CA  PRO C 184     -26.153  19.138  -3.190  1.00190.62           C  
ANISOU 5562  CA  PRO C 184    35346  23507  13572   4556   3121   3194       C  
ATOM   5563  C   PRO C 184     -27.126  20.090  -2.492  1.00193.51           C  
ANISOU 5563  C   PRO C 184    35523  23836  14168   4624   2642   3238       C  
ATOM   5564  O   PRO C 184     -28.334  20.029  -2.737  1.00193.37           O  
ANISOU 5564  O   PRO C 184    35507  23965  14000   4900   1959   3079       O  
ATOM   5565  CB  PRO C 184     -26.115  19.352  -4.713  1.00193.29           C  
ANISOU 5565  CB  PRO C 184    35490  24181  13771   4257   2950   3233       C  
ATOM   5566  CG  PRO C 184     -26.479  18.021  -5.334  1.00196.53           C  
ANISOU 5566  CG  PRO C 184    35594  24957  14122   4236   2557   2888       C  
ATOM   5567  CD  PRO C 184     -27.171  17.224  -4.283  1.00192.19           C  
ANISOU 5567  CD  PRO C 184    35382  24192  13449   4793   2314   2660       C  
ATOM   5568  N   LYS C 185     -26.594  20.953  -1.603  1.00191.10           N  
ANISOU 5568  N   LYS C 185    35435  23162  14011   4606   3132   3478       N  
ATOM   5569  CA  LYS C 185     -27.367  21.921  -0.819  1.00190.73           C  
ANISOU 5569  CA  LYS C 185    35450  22939  14081   4791   2846   3559       C  
ATOM   5570  C   LYS C 185     -27.949  23.062  -1.674  1.00194.73           C  
ANISOU 5570  C   LYS C 185    35659  23647  14683   4540   2416   3697       C  
ATOM   5571  O   LYS C 185     -27.231  23.613  -2.512  1.00195.56           O  
ANISOU 5571  O   LYS C 185    35725  23793  14784   4194   2732   3907       O  
ATOM   5572  CB  LYS C 185     -26.522  22.483   0.334  1.00191.89           C  
ANISOU 5572  CB  LYS C 185    35454  22813  14641   4516   3438   3722       C  
ATOM   5573  N   PRO C 186     -29.233  23.450  -1.464  1.00192.20           N  
ANISOU 5573  N   PRO C 186    35517  23292  14219   4970   1814   3629       N  
ATOM   5574  CA  PRO C 186     -29.818  24.535  -2.272  1.00193.18           C  
ANISOU 5574  CA  PRO C 186    35567  23509  14323   4879   1488   3801       C  
ATOM   5575  C   PRO C 186     -29.404  25.943  -1.827  1.00196.10           C  
ANISOU 5575  C   PRO C 186    35718  23701  15091   4514   1763   4088       C  
ATOM   5576  O   PRO C 186     -28.563  26.088  -0.936  1.00195.14           O  
ANISOU 5576  O   PRO C 186    35685  23306  15152   4393   2298   4168       O  
ATOM   5577  CB  PRO C 186     -31.335  24.302  -2.146  1.00194.22           C  
ANISOU 5577  CB  PRO C 186    35479  23856  14460   5210    666   3548       C  
ATOM   5578  CG  PRO C 186     -31.504  23.080  -1.272  1.00196.12           C  
ANISOU 5578  CG  PRO C 186    35470  24201  14846   5330    517   3216       C  
ATOM   5579  CD  PRO C 186     -30.229  22.906  -0.523  1.00192.25           C  
ANISOU 5579  CD  PRO C 186    35411  23346  14291   5353   1299   3351       C  
ATOM   5580  N   GLU C 187     -29.992  26.981  -2.465  1.00194.72           N  
ANISOU 5580  N   GLU C 187    35666  23508  14810   4581   1499   4275       N  
ATOM   5581  CA  GLU C 187     -29.725  28.401  -2.207  1.00195.08           C  
ANISOU 5581  CA  GLU C 187    35720  23311  15090   4379   1722   4566       C  
ATOM   5582  C   GLU C 187     -30.071  28.862  -0.787  1.00196.89           C  
ANISOU 5582  C   GLU C 187    35781  23340  15689   4444   1652   4510       C  
ATOM   5583  O   GLU C 187     -29.331  29.672  -0.224  1.00196.56           O  
ANISOU 5583  O   GLU C 187    35803  23010  15873   4214   2114   4698       O  
ATOM   5584  CB  GLU C 187     -30.430  29.283  -3.247  1.00197.37           C  
ANISOU 5584  CB  GLU C 187    35796  23810  15384   4279   1296   4728       C  
ATOM   5585  N   PHE C 188     -31.184  28.356  -0.211  1.00193.88           N  
ANISOU 5585  N   PHE C 188    35584  22951  15129   4996   1166   4273       N  
ATOM   5586  CA  PHE C 188     -31.621  28.717   1.143  1.00192.93           C  
ANISOU 5586  CA  PHE C 188    35513  22596  15194   5249   1086   4203       C  
ATOM   5587  C   PHE C 188     -30.736  28.110   2.245  1.00194.43           C  
ANISOU 5587  C   PHE C 188    35594  22666  15615   5070   1573   4117       C  
ATOM   5588  O   PHE C 188     -30.730  28.620   3.368  1.00193.50           O  
ANISOU 5588  O   PHE C 188    35549  22288  15684   5147   1725   4142       O  
ATOM   5589  CB  PHE C 188     -33.113  28.400   1.368  1.00193.97           C  
ANISOU 5589  CB  PHE C 188    35376  22980  15343   5637    285   3929       C  
ATOM   5590  CG  PHE C 188     -33.521  26.951   1.240  1.00194.64           C  
ANISOU 5590  CG  PHE C 188    35285  23378  15293   5820    -62   3593       C  
ATOM   5591  CD1 PHE C 188     -33.546  26.117   2.352  1.00195.58           C  
ANISOU 5591  CD1 PHE C 188    35245  23518  15550   5965    -90   3347       C  
ATOM   5592  CD2 PHE C 188     -33.941  26.436   0.019  1.00197.11           C  
ANISOU 5592  CD2 PHE C 188    35330  24055  15506   5685   -410   3503       C  
ATOM   5593  CE1 PHE C 188     -33.942  24.781   2.237  1.00195.90           C  
ANISOU 5593  CE1 PHE C 188    35112  23838  15483   6142   -433   3022       C  
ATOM   5594  CE2 PHE C 188     -34.342  25.101  -0.095  1.00198.76           C  
ANISOU 5594  CE2 PHE C 188    35263  24569  15686   5754   -743   3167       C  
ATOM   5595  CZ  PHE C 188     -34.338  24.283   1.014  1.00196.21           C  
ANISOU 5595  CZ  PHE C 188    35067  24154  15331   6102   -753   2927       C  
ATOM   5596  N   MET C 189     -29.983  27.038   1.919  1.00191.89           N  
ANISOU 5596  N   MET C 189    35516  22360  15034   5086   1938   4059       N  
ATOM   5597  CA  MET C 189     -29.061  26.366   2.839  1.00190.90           C  
ANISOU 5597  CA  MET C 189    35473  22053  15006   5018   2522   4019       C  
ATOM   5598  C   MET C 189     -27.784  27.193   3.051  1.00194.10           C  
ANISOU 5598  C   MET C 189    35626  22287  15837   4371   3206   4256       C  
ATOM   5599  O   MET C 189     -27.108  27.022   4.067  1.00193.17           O  
ANISOU 5599  O   MET C 189    35539  21940  15918   4279   3722   4258       O  
ATOM   5600  CB  MET C 189     -28.714  24.961   2.327  1.00192.31           C  
ANISOU 5600  CB  MET C 189    35497  22511  15062   4971   2543   3831       C  
ATOM   5601  N   SER C 190     -27.460  28.083   2.090  1.00192.90           N  
ANISOU 5601  N   SER C 190    35600  22082  15611   4153   3341   4492       N  
ATOM   5602  CA  SER C 190     -26.294  28.968   2.128  1.00193.44           C  
ANISOU 5602  CA  SER C 190    35559  21955  15986   3634   3957   4725       C  
ATOM   5603  C   SER C 190     -26.716  30.438   2.368  1.00196.66           C  
ANISOU 5603  C   SER C 190    35719  22283  16719   3456   3690   4870       C  
ATOM   5604  O   SER C 190     -26.009  31.366   1.961  1.00197.39           O  
ANISOU 5604  O   SER C 190    35704  22299  16997   3065   3972   5087       O  
ATOM   5605  CB  SER C 190     -25.479  28.823   0.845  1.00196.91           C  
ANISOU 5605  CB  SER C 190    35635  22731  16451   3182   4078   4804       C  
ATOM   5606  OG  SER C 190     -24.260  29.545   0.917  1.00203.56           O  
ANISOU 5606  OG  SER C 190    35731  23724  17887   2428   4390   4914       O  
ATOM   5607  N   LYS C 191     -27.863  30.636   3.050  1.00193.62           N  
ANISOU 5607  N   LYS C 191    35656  21726  16186   3975   3299   4790       N  
ATOM   5608  CA  LYS C 191     -28.415  31.954   3.374  1.00193.97           C  
ANISOU 5608  CA  LYS C 191    35704  21582  16413   4000   3085   4918       C  
ATOM   5609  C   LYS C 191     -28.007  32.411   4.774  1.00196.08           C  
ANISOU 5609  C   LYS C 191    35753  21613  17135   3764   3389   4882       C  
ATOM   5610  O   LYS C 191     -27.950  31.596   5.698  1.00194.58           O  
ANISOU 5610  O   LYS C 191    35649  21354  16928   3942   3552   4713       O  
ATOM   5611  CB  LYS C 191     -29.943  31.950   3.235  1.00195.57           C  
ANISOU 5611  CB  LYS C 191    35768  22024  16514   4416   2256   4772       C  
ATOM   5612  N   SER C 192     -27.735  33.721   4.924  1.00194.67           N  
ANISOU 5612  N   SER C 192    35719  21109  17138   3580   3624   5092       N  
ATOM   5613  CA  SER C 192     -27.325  34.351   6.184  1.00194.34           C  
ANISOU 5613  CA  SER C 192    35664  20721  17456   3393   3997   5090       C  
ATOM   5614  C   SER C 192     -28.467  34.408   7.209  1.00196.12           C  
ANISOU 5614  C   SER C 192    35793  20963  17761   3764   3497   4902       C  
ATOM   5615  O   SER C 192     -29.638  34.307   6.835  1.00195.72           O  
ANISOU 5615  O   SER C 192    35814  21091  17460   4213   2882   4835       O  
ATOM   5616  CB  SER C 192     -26.779  35.752   5.919  1.00198.22           C  
ANISOU 5616  CB  SER C 192    35779  21154  18383   2859   4071   5291       C  
ATOM   5617  OG  SER C 192     -26.259  36.344   7.099  1.00204.19           O  
ANISOU 5617  OG  SER C 192    35915  21878  19792   2378   4176   5195       O  
ATOM   5618  N   LEU C 193     -28.114  34.575   8.502  1.00193.17           N  
ANISOU 5618  N   LEU C 193    35642  20213  17542   3761   3946   4855       N  
ATOM   5619  CA  LEU C 193     -29.056  34.665   9.623  1.00192.22           C  
ANISOU 5619  CA  LEU C 193    35629  19994  17412   4187   3637   4700       C  
ATOM   5620  C   LEU C 193     -29.937  35.917   9.545  1.00195.39           C  
ANISOU 5620  C   LEU C 193    35778  20429  18034   4211   3088   4746       C  
ATOM   5621  O   LEU C 193     -31.095  35.871   9.965  1.00194.66           O  
ANISOU 5621  O   LEU C 193    35743  20414  17805   4714   2571   4606       O  
ATOM   5622  CB  LEU C 193     -28.305  34.628  10.960  1.00191.77           C  
ANISOU 5622  CB  LEU C 193    35528  19662  17675   3923   4220   4627       C  
ATOM   5623  N   GLU C 194     -29.387  37.027   9.007  1.00193.99           N  
ANISOU 5623  N   GLU C 194    35714  20005  17990   3886   3360   4985       N  
ATOM   5624  CA  GLU C 194     -30.087  38.303   8.835  1.00194.66           C  
ANISOU 5624  CA  GLU C 194    35755  19990  18216   3955   2997   5099       C  
ATOM   5625  C   GLU C 194     -31.180  38.205   7.764  1.00197.20           C  
ANISOU 5625  C   GLU C 194    35812  20728  18386   4212   2276   5103       C  
ATOM   5626  O   GLU C 194     -32.259  38.773   7.944  1.00197.14           O  
ANISOU 5626  O   GLU C 194    35785  20715  18404   4544   1816   5069       O  
ATOM   5627  CB  GLU C 194     -29.094  39.423   8.491  1.00197.00           C  
ANISOU 5627  CB  GLU C 194    35818  20125  18907   3336   3344   5317       C  
ATOM   5628  N   GLU C 195     -30.900  37.479   6.662  1.00194.47           N  
ANISOU 5628  N   GLU C 195    35676  20544  17670   4261   2342   5178       N  
ATOM   5629  CA  GLU C 195     -31.834  37.269   5.553  1.00194.45           C  
ANISOU 5629  CA  GLU C 195    35625  20856  17402   4551   1780   5193       C  
ATOM   5630  C   GLU C 195     -32.917  36.245   5.915  1.00195.26           C  
ANISOU 5630  C   GLU C 195    35515  21287  17388   4972   1221   4885       C  
ATOM   5631  O   GLU C 195     -34.087  36.460   5.591  1.00195.31           O  
ANISOU 5631  O   GLU C 195    35397  21463  17347   5289    648   4833       O  
ATOM   5632  CB  GLU C 195     -31.084  36.844   4.281  1.00196.04           C  
ANISOU 5632  CB  GLU C 195    35710  21295  17479   4212   1953   5325       C  
ATOM   5633  N   LEU C 196     -32.526  35.139   6.585  1.00190.96           N  
ANISOU 5633  N   LEU C 196    35319  20660  16577   5208   1498   4718       N  
ATOM   5634  CA  LEU C 196     -33.433  34.072   7.016  1.00189.48           C  
ANISOU 5634  CA  LEU C 196    35120  20709  16165   5735   1030   4420       C  
ATOM   5635  C   LEU C 196     -34.268  34.495   8.233  1.00191.08           C  
ANISOU 5635  C   LEU C 196    35080  20884  16636   5963    707   4250       C  
ATOM   5636  O   LEU C 196     -33.907  35.449   8.926  1.00190.88           O  
ANISOU 5636  O   LEU C 196    35155  20527  16842   5789   1028   4367       O  
ATOM   5637  CB  LEU C 196     -32.644  32.791   7.321  1.00188.51           C  
ANISOU 5637  CB  LEU C 196    35105  20634  15886   5702   1400   4301       C  
ATOM   5638  N   GLN C 197     -35.386  33.785   8.484  1.00187.91           N  
ANISOU 5638  N   GLN C 197    34752  20687  15958   6623    129   3981       N  
ATOM   5639  CA  GLN C 197     -36.302  34.064   9.594  1.00187.24           C  
ANISOU 5639  CA  GLN C 197    34538  20601  16005   7024   -239   3780       C  
ATOM   5640  C   GLN C 197     -36.198  33.059  10.762  1.00188.21           C  
ANISOU 5640  C   GLN C 197    34499  20856  16158   7186   -207   3517       C  
ATOM   5641  O   GLN C 197     -36.979  33.149  11.715  1.00187.55           O  
ANISOU 5641  O   GLN C 197    34240  20848  16174   7552   -551   3305       O  
ATOM   5642  CB  GLN C 197     -37.747  34.169   9.077  1.00188.74           C  
ANISOU 5642  CB  GLN C 197    34275  21146  16293   7290  -1028   3620       C  
ATOM   5643  N   ILE C 198     -35.223  32.128  10.700  1.00184.62           N  
ANISOU 5643  N   ILE C 198    34476  20299  15372   7206    275   3559       N  
ATOM   5644  CA  ILE C 198     -34.997  31.102  11.723  1.00181.82           C  
ANISOU 5644  CA  ILE C 198    33906  20103  15073   7300    369   3354       C  
ATOM   5645  C   ILE C 198     -34.442  31.684  13.025  1.00180.88           C  
ANISOU 5645  C   ILE C 198    33279  19876  15574   6712    774   3391       C  
ATOM   5646  O   ILE C 198     -33.466  32.437  13.000  1.00182.14           O  
ANISOU 5646  O   ILE C 198    33881  19582  15743   6390   1449   3663       O  
ATOM   5647  CB  ILE C 198     -34.109  29.961  11.176  1.00183.37           C  
ANISOU 5647  CB  ILE C 198    33990  20459  15224   6961    700   3371       C  
ATOM   5648  N   GLY C 199     -35.079  31.327  14.140  1.00172.02           N  
ANISOU 5648  N   GLY C 199    31244  19159  14959   6578    365   3099       N  
ATOM   5649  CA  GLY C 199     -34.698  31.771  15.477  1.00167.70           C  
ANISOU 5649  CA  GLY C 199    30141  18587  14992   6072    627   3068       C  
ATOM   5650  C   GLY C 199     -35.535  32.919  16.004  1.00172.49           C  
ANISOU 5650  C   GLY C 199    30908  19003  15628   6404    369   3042       C  
ATOM   5651  O   GLY C 199     -35.784  33.888  15.280  1.00177.69           O  
ANISOU 5651  O   GLY C 199    32443  19239  15834   6862    385   3238       O  
ATOM   5652  N   THR C 200     -35.967  32.817  17.279  1.00163.98           N  
ANISOU 5652  N   THR C 200    29020  18216  15067   6194    151   2804       N  
ATOM   5653  CA  THR C 200     -36.778  33.835  17.958  1.00164.66           C  
ANISOU 5653  CA  THR C 200    29127  18173  15264   6471    -89   2733       C  
ATOM   5654  C   THR C 200     -35.888  35.034  18.318  1.00169.16           C  
ANISOU 5654  C   THR C 200    30161  18196  15917   6153    503   2973       C  
ATOM   5655  O   THR C 200     -35.140  34.980  19.296  1.00165.00           O  
ANISOU 5655  O   THR C 200    29136  17707  15850   5558    833   2925       O  
ATOM   5656  CB  THR C 200     -37.529  33.228  19.164  1.00167.63           C  
ANISOU 5656  CB  THR C 200    28496  19052  16144   6346   -473   2389       C  
ATOM   5657  OG1 THR C 200     -38.102  31.972  18.791  1.00165.52           O  
ANISOU 5657  OG1 THR C 200    27774  19255  15860   6485   -885   2169       O  
ATOM   5658  CG2 THR C 200     -38.616  34.149  19.708  1.00168.22           C  
ANISOU 5658  CG2 THR C 200    28573  19064  16280   6776   -825   2262       C  
ATOM   5659  N   TYR C 201     -35.966  36.101  17.503  1.00170.92           N  
ANISOU 5659  N   TYR C 201    31365  17894  15682   6561    632   3219       N  
ATOM   5660  CA  TYR C 201     -35.171  37.323  17.647  1.00173.18           C  
ANISOU 5660  CA  TYR C 201    32252  17561  15987   6309   1229   3464       C  
ATOM   5661  C   TYR C 201     -35.561  38.212  18.833  1.00175.41           C  
ANISOU 5661  C   TYR C 201    32286  17732  16630   6253   1153   3338       C  
ATOM   5662  O   TYR C 201     -34.689  38.877  19.393  1.00175.13           O  
ANISOU 5662  O   TYR C 201    32329  17346  16867   5759   1670   3420       O  
ATOM   5663  CB  TYR C 201     -35.193  38.136  16.345  1.00181.36           C  
ANISOU 5663  CB  TYR C 201    34503  18038  16366   6816   1401   3782       C  
ATOM   5664  N   ALA C 202     -36.857  38.240  19.202  1.00170.92           N  
ANISOU 5664  N   ALA C 202    31420  17447  16075   6757    524   3118       N  
ATOM   5665  CA  ALA C 202     -37.366  39.083  20.289  1.00170.21           C  
ANISOU 5665  CA  ALA C 202    31128  17262  16282   6800    417   2982       C  
ATOM   5666  C   ALA C 202     -37.819  38.323  21.543  1.00167.64           C  
ANISOU 5666  C   ALA C 202    29708  17516  16472   6552    115   2639       C  
ATOM   5667  O   ALA C 202     -38.100  37.124  21.476  1.00163.84           O  
ANISOU 5667  O   ALA C 202    28631  17549  16072   6521   -165   2475       O  
ATOM   5668  CB  ALA C 202     -38.491  39.970  19.773  1.00176.50           C  
ANISOU 5668  CB  ALA C 202    32564  17815  16684   7625     16   3017       C  
ATOM   5669  N   ASN C 203     -37.894  39.051  22.686  1.00163.07           N  
ANISOU 5669  N   ASN C 203    28923  16815  16222   6386    200   2532       N  
ATOM   5670  CA  ASN C 203     -38.317  38.600  24.021  1.00158.12           C  
ANISOU 5670  CA  ASN C 203    27400  16624  16056   6174     -3   2229       C  
ATOM   5671  C   ASN C 203     -37.496  37.409  24.556  1.00155.71           C  
ANISOU 5671  C   ASN C 203    26375  16712  16077   5531    179   2140       C  
ATOM   5672  O   ASN C 203     -38.064  36.419  25.028  1.00151.72           O  
ANISOU 5672  O   ASN C 203    25157  16720  15772   5526   -122   1917       O  
ATOM   5673  CB  ASN C 203     -39.832  38.317  24.066  1.00159.85           C  
ANISOU 5673  CB  ASN C 203    27265  17222  16248   6785   -620   1988       C  
ATOM   5674  CG  ASN C 203     -40.696  39.526  23.799  1.00189.52           C  
ANISOU 5674  CG  ASN C 203    31616  20632  19762   7443   -843   2018       C  
ATOM   5675  OD1 ASN C 203     -40.684  40.514  24.543  1.00185.41           O  
ANISOU 5675  OD1 ASN C 203    31266  19802  19379   7409   -676   2012       O  
ATOM   5676  ND2 ASN C 203     -41.495  39.458  22.745  1.00185.37           N  
ANISOU 5676  ND2 ASN C 203    31410  20157  18863   8092  -1258   2025       N  
ATOM   5677  N   ILE C 204     -36.156  37.526  24.505  1.00151.34           N  
ANISOU 5677  N   ILE C 204    26006  15898  15597   4992    689   2300       N  
ATOM   5678  CA  ILE C 204     -35.255  36.476  24.990  1.00146.17           C  
ANISOU 5678  CA  ILE C 204    24722  15574  15243   4408    877   2223       C  
ATOM   5679  C   ILE C 204     -35.040  36.577  26.500  1.00146.16           C  
ANISOU 5679  C   ILE C 204    24161  15705  15670   4032    922   2015       C  
ATOM   5680  O   ILE C 204     -34.686  37.642  27.011  1.00147.73           O  
ANISOU 5680  O   ILE C 204    24627  15526  15976   3883   1146   2024       O  
ATOM   5681  CB  ILE C 204     -33.918  36.362  24.206  1.00150.42           C  
ANISOU 5681  CB  ILE C 204    25591  15859  15701   4014   1375   2440       C  
ATOM   5682  CG1 ILE C 204     -33.233  37.737  23.990  1.00155.59           C  
ANISOU 5682  CG1 ILE C 204    26966  15851  16301   3875   1843   2627       C  
ATOM   5683  CG2 ILE C 204     -34.135  35.615  22.889  1.00152.14           C  
ANISOU 5683  CG2 ILE C 204    26066  16202  15537   4320   1252   2567       C  
ATOM   5684  CD1 ILE C 204     -31.698  37.695  23.929  1.00163.26           C  
ANISOU 5684  CD1 ILE C 204    27917  16621  17493   3224   2429   2706       C  
ATOM   5685  N   ALA C 205     -35.281  35.460  27.207  1.00137.61           N  
ANISOU 5685  N   ALA C 205    22338  15141  14807   3900    708   1821       N  
ATOM   5686  CA  ALA C 205     -35.127  35.346  28.657  1.00134.10           C  
ANISOU 5686  CA  ALA C 205    21350  14889  14713   3588    714   1615       C  
ATOM   5687  C   ALA C 205     -33.681  34.998  29.009  1.00135.30           C  
ANISOU 5687  C   ALA C 205    21286  15037  15082   2989   1059   1628       C  
ATOM   5688  O   ALA C 205     -33.082  34.129  28.367  1.00133.57           O  
ANISOU 5688  O   ALA C 205    20961  14967  14822   2824   1163   1713       O  
ATOM   5689  CB  ALA C 205     -36.074  34.288  29.197  1.00131.59           C  
ANISOU 5689  CB  ALA C 205    20407  15090  14501   3749    369   1419       C  
ATOM   5690  N   MET C 206     -33.114  35.693  30.013  1.00131.53           N  
ANISOU 5690  N   MET C 206    20748  14387  14842   2682   1222   1519       N  
ATOM   5691  CA  MET C 206     -31.723  35.503  30.440  1.00130.19           C  
ANISOU 5691  CA  MET C 206    20340  14201  14924   2127   1510   1469       C  
ATOM   5692  C   MET C 206     -31.495  35.742  31.941  1.00131.97           C  
ANISOU 5692  C   MET C 206    20209  14512  15423   1892   1452   1223       C  
ATOM   5693  O   MET C 206     -32.338  36.340  32.613  1.00132.03           O  
ANISOU 5693  O   MET C 206    20286  14467  15414   2132   1280   1120       O  
ATOM   5694  CB  MET C 206     -30.777  36.384  29.594  1.00136.65           C  
ANISOU 5694  CB  MET C 206    21703  14505  15714   1903   1936   1639       C  
ATOM   5695  N   VAL C 207     -30.329  35.295  32.443  1.00126.79           N  
ANISOU 5695  N   VAL C 207    19190  13979  15005   1445   1591   1117       N  
ATOM   5696  CA  VAL C 207     -29.894  35.450  33.836  1.00125.70           C  
ANISOU 5696  CA  VAL C 207    18722  13932  15107   1196   1524    862       C  
ATOM   5697  C   VAL C 207     -28.586  36.247  33.931  1.00132.09           C  
ANISOU 5697  C   VAL C 207    19630  14394  16165    737   1826    775       C  
ATOM   5698  O   VAL C 207     -27.881  36.394  32.930  1.00133.74           O  
ANISOU 5698  O   VAL C 207    20055  14366  16395    552   2137    922       O  
ATOM   5699  CB  VAL C 207     -29.817  34.109  34.618  1.00125.64           C  
ANISOU 5699  CB  VAL C 207    18121  14449  15167   1143   1316    739       C  
ATOM   5700  CG1 VAL C 207     -31.192  33.468  34.752  1.00123.21           C  
ANISOU 5700  CG1 VAL C 207    17689  14419  14706   1540   1039    719       C  
ATOM   5701  CG2 VAL C 207     -28.808  33.138  34.002  1.00123.96           C  
ANISOU 5701  CG2 VAL C 207    17688  14437  14976    973   1431    850       C  
ATOM   5702  N   ARG C 208     -28.271  36.761  35.133  1.00128.92           N  
ANISOU 5702  N   ARG C 208    19071  13953  15958    551   1748    514       N  
ATOM   5703  CA  ARG C 208     -27.050  37.525  35.400  1.00131.90           C  
ANISOU 5703  CA  ARG C 208    19453  14025  16639     86   1985    340       C  
ATOM   5704  C   ARG C 208     -26.118  36.746  36.339  1.00133.44           C  
ANISOU 5704  C   ARG C 208    19039  14594  17069   -201   1835     77       C  
ATOM   5705  O   ARG C 208     -26.554  35.772  36.954  1.00129.45           O  
ANISOU 5705  O   ARG C 208    18210  14526  16447      2   1546     38       O  
ATOM   5706  CB  ARG C 208     -27.381  38.928  35.955  1.00135.72           C  
ANISOU 5706  CB  ARG C 208    20330  14075  17160    106   2011    212       C  
ATOM   5707  CG  ARG C 208     -27.872  39.923  34.899  1.00149.78           C  
ANISOU 5707  CG  ARG C 208    22797  15339  18774    288   2267    461       C  
ATOM   5708  CD  ARG C 208     -29.385  39.919  34.740  1.00158.83           C  
ANISOU 5708  CD  ARG C 208    24190  16573  19586    878   2014    610       C  
ATOM   5709  NE  ARG C 208     -29.810  40.617  33.525  1.00170.97           N  
ANISOU 5709  NE  ARG C 208    26378  17684  20900   1128   2214    887       N  
ATOM   5710  CZ  ARG C 208     -31.030  40.538  33.000  1.00184.81           C  
ANISOU 5710  CZ  ARG C 208    28370  19505  22346   1670   2009   1053       C  
ATOM   5711  NH1 ARG C 208     -31.960  39.783  33.573  1.00168.77           N  
ANISOU 5711  NH1 ARG C 208    25939  17945  20242   1972   1643    962       N  
ATOM   5712  NH2 ARG C 208     -31.326  41.207  31.895  1.00174.94           N  
ANISOU 5712  NH2 ARG C 208    27764  17844  20863   1922   2174   1297       N  
ATOM   5713  N   THR C 209     -24.838  37.164  36.438  1.00132.51           N  
ANISOU 5713  N   THR C 209    18770  14292  17286   -661   2038   -113       N  
ATOM   5714  CA  THR C 209     -23.803  36.528  37.273  1.00131.68           C  
ANISOU 5714  CA  THR C 209    18081  14512  17440   -933   1878   -406       C  
ATOM   5715  C   THR C 209     -24.167  36.443  38.768  1.00133.35           C  
ANISOU 5715  C   THR C 209    18102  14976  17590   -778   1465   -673       C  
ATOM   5716  O   THR C 209     -23.711  35.524  39.452  1.00131.22           O  
ANISOU 5716  O   THR C 209    17390  15109  17357   -787   1224   -827       O  
ATOM   5717  CB  THR C 209     -22.438  37.207  37.072  1.00144.67           C  
ANISOU 5717  CB  THR C 209    19610  15848  19509  -1459   2186   -613       C  
ATOM   5718  OG1 THR C 209     -22.580  38.623  37.205  1.00148.25           O  
ANISOU 5718  OG1 THR C 209    20495  15782  20050  -1586   2347   -701       O  
ATOM   5719  CG2 THR C 209     -21.804  36.865  35.730  1.00144.21           C  
ANISOU 5719  CG2 THR C 209    19564  15692  19538  -1645   2601   -389       C  
ATOM   5720  N   THR C 210     -24.989  37.389  39.262  1.00130.32           N  
ANISOU 5720  N   THR C 210    18088  14343  17085   -606   1395   -720       N  
ATOM   5721  CA  THR C 210     -25.431  37.456  40.661  1.00129.23           C  
ANISOU 5721  CA  THR C 210    17877  14381  16845   -430   1057   -965       C  
ATOM   5722  C   THR C 210     -26.822  36.833  40.892  1.00128.38           C  
ANISOU 5722  C   THR C 210    17852  14543  16383     55    880   -780       C  
ATOM   5723  O   THR C 210     -27.232  36.689  42.047  1.00127.18           O  
ANISOU 5723  O   THR C 210    17631  14584  16106    231    638   -950       O  
ATOM   5724  CB  THR C 210     -25.356  38.902  41.186  1.00141.71           C  
ANISOU 5724  CB  THR C 210    19776  15511  18556   -578   1104  -1201       C  
ATOM   5725  OG1 THR C 210     -26.052  39.772  40.291  1.00142.65           O  
ANISOU 5725  OG1 THR C 210    20419  15197  18584   -454   1368   -956       O  
ATOM   5726  CG2 THR C 210     -23.923  39.383  41.385  1.00144.54           C  
ANISOU 5726  CG2 THR C 210    19902  15693  19322  -1092   1187  -1526       C  
ATOM   5727  N   THR C 211     -27.535  36.458  39.803  1.00122.34           N  
ANISOU 5727  N   THR C 211    17232  13789  15461    270   1008   -454       N  
ATOM   5728  CA  THR C 211     -28.878  35.862  39.854  1.00118.81           C  
ANISOU 5728  CA  THR C 211    16814  13584  14745    702    870   -298       C  
ATOM   5729  C   THR C 211     -28.866  34.480  40.539  1.00118.75           C  
ANISOU 5729  C   THR C 211    16386  14073  14661    779    676   -342       C  
ATOM   5730  O   THR C 211     -28.121  33.597  40.105  1.00116.93           O  
ANISOU 5730  O   THR C 211    15886  14040  14503    620    707   -280       O  
ATOM   5731  CB  THR C 211     -29.528  35.841  38.452  1.00125.92           C  
ANISOU 5731  CB  THR C 211    17962  14360  15521    896   1018     11       C  
ATOM   5732  OG1 THR C 211     -29.463  37.147  37.882  1.00129.04           O  
ANISOU 5732  OG1 THR C 211    18821  14251  15958    841   1217     60       O  
ATOM   5733  CG2 THR C 211     -30.981  35.371  38.474  1.00122.11           C  
ANISOU 5733  CG2 THR C 211    17482  14094  14819   1341    861    112       C  
ATOM   5734  N   PRO C 212     -29.691  34.276  41.599  1.00113.89           N  
ANISOU 5734  N   PRO C 212    15743  13641  13889   1034    509   -442       N  
ATOM   5735  CA  PRO C 212     -29.712  32.970  42.281  1.00110.93           C  
ANISOU 5735  CA  PRO C 212    15053  13685  13412   1121    373   -463       C  
ATOM   5736  C   PRO C 212     -30.344  31.857  41.446  1.00111.30           C  
ANISOU 5736  C   PRO C 212    14959  13958  13373   1279    427   -218       C  
ATOM   5737  O   PRO C 212     -31.035  32.140  40.464  1.00110.66           O  
ANISOU 5737  O   PRO C 212    15037  13741  13266   1408    516    -54       O  
ATOM   5738  CB  PRO C 212     -30.523  33.243  43.557  1.00113.29           C  
ANISOU 5738  CB  PRO C 212    15464  14029  13551   1359    267   -620       C  
ATOM   5739  CG  PRO C 212     -30.643  34.734  43.653  1.00120.91           C  
ANISOU 5739  CG  PRO C 212    16757  14605  14578   1335    306   -741       C  
ATOM   5740  CD  PRO C 212     -30.622  35.219  42.246  1.00116.99           C  
ANISOU 5740  CD  PRO C 212    16418  13846  14186   1261    474   -541       C  
ATOM   5741  N   VAL C 213     -30.101  30.589  41.843  1.00105.61           N  
ANISOU 5741  N   VAL C 213    13962  13567  12599   1285    357   -210       N  
ATOM   5742  CA  VAL C 213     -30.612  29.391  41.162  1.00102.64           C  
ANISOU 5742  CA  VAL C 213    13424  13413  12160   1400    404    -17       C  
ATOM   5743  C   VAL C 213     -32.150  29.349  41.195  1.00105.61           C  
ANISOU 5743  C   VAL C 213    13871  13825  12431   1699    424     37       C  
ATOM   5744  O   VAL C 213     -32.753  29.041  40.169  1.00104.29           O  
ANISOU 5744  O   VAL C 213    13687  13674  12265   1798    466    180       O  
ATOM   5745  CB  VAL C 213     -29.961  28.064  41.658  1.00104.98           C  
ANISOU 5745  CB  VAL C 213    13454  14010  12424   1346    341    -30       C  
ATOM   5746  CG1 VAL C 213     -30.336  26.889  40.755  1.00102.38           C  
ANISOU 5746  CG1 VAL C 213    12982  13848  12070   1407    417    163       C  
ATOM   5747  CG2 VAL C 213     -28.441  28.187  41.744  1.00106.20           C  
ANISOU 5747  CG2 VAL C 213    13481  14150  12721   1081    283   -148       C  
ATOM   5748  N   TYR C 214     -32.778  29.705  42.341  1.00102.93           N  
ANISOU 5748  N   TYR C 214    13608  13491  12009   1851    395   -102       N  
ATOM   5749  CA  TYR C 214     -34.240  29.724  42.494  1.00102.69           C  
ANISOU 5749  CA  TYR C 214    13595  13497  11927   2133    446    -98       C  
ATOM   5750  C   TYR C 214     -34.928  30.661  41.493  1.00107.76           C  
ANISOU 5750  C   TYR C 214    14406  13918  12621   2277    449    -35       C  
ATOM   5751  O   TYR C 214     -35.979  30.305  40.957  1.00106.95           O  
ANISOU 5751  O   TYR C 214    14201  13906  12529   2483    454     20       O  
ATOM   5752  CB  TYR C 214     -34.658  30.057  43.940  1.00105.21           C  
ANISOU 5752  CB  TYR C 214    14011  13825  12140   2262    457   -273       C  
ATOM   5753  CG  TYR C 214     -36.132  29.838  44.210  1.00107.08           C  
ANISOU 5753  CG  TYR C 214    14178  14150  12355   2533    570   -288       C  
ATOM   5754  CD1 TYR C 214     -36.634  28.565  44.467  1.00107.71           C  
ANISOU 5754  CD1 TYR C 214    14039  14473  12412   2575    682   -242       C  
ATOM   5755  CD2 TYR C 214     -37.028  30.904  44.206  1.00109.79           C  
ANISOU 5755  CD2 TYR C 214    14667  14320  12729   2746    587   -364       C  
ATOM   5756  CE1 TYR C 214     -37.991  28.357  44.709  1.00109.27           C  
ANISOU 5756  CE1 TYR C 214    14119  14745  12652   2786    831   -290       C  
ATOM   5757  CE2 TYR C 214     -38.389  30.706  44.440  1.00111.37           C  
ANISOU 5757  CE2 TYR C 214    14736  14619  12962   2999    701   -415       C  
ATOM   5758  CZ  TYR C 214     -38.866  29.430  44.691  1.00117.53           C  
ANISOU 5758  CZ  TYR C 214    15252  15648  13755   2999    834   -387       C  
ATOM   5759  OH  TYR C 214     -40.203  29.228  44.936  1.00119.63           O  
ANISOU 5759  OH  TYR C 214    15339  16006  14111   3211    990   -471       O  
ATOM   5760  N   VAL C 215     -34.329  31.843  41.239  1.00106.22           N  
ANISOU 5760  N   VAL C 215    14477  13420  12463   2176    441    -58       N  
ATOM   5761  CA  VAL C 215     -34.836  32.838  40.285  1.00107.81           C  
ANISOU 5761  CA  VAL C 215    14947  13341  12673   2331    453     21       C  
ATOM   5762  C   VAL C 215     -34.663  32.292  38.856  1.00110.50           C  
ANISOU 5762  C   VAL C 215    15260  13712  13011   2301    467    221       C  
ATOM   5763  O   VAL C 215     -35.586  32.404  38.045  1.00110.58           O  
ANISOU 5763  O   VAL C 215    15349  13694  12971   2570    416    299       O  
ATOM   5764  CB  VAL C 215     -34.177  34.236  40.483  1.00114.59           C  
ANISOU 5764  CB  VAL C 215    16150  13816  13575   2199    494    -62       C  
ATOM   5765  CG1 VAL C 215     -34.712  35.260  39.482  1.00116.73           C  
ANISOU 5765  CG1 VAL C 215    16784  13752  13815   2401    529     49       C  
ATOM   5766  CG2 VAL C 215     -34.376  34.742  41.909  1.00115.67           C  
ANISOU 5766  CG2 VAL C 215    16334  13930  13683   2253    457   -287       C  
ATOM   5767  N   ALA C 216     -33.498  31.665  38.576  1.00105.84           N  
ANISOU 5767  N   ALA C 216    14549  13197  12469   2002    522    281       N  
ATOM   5768  CA  ALA C 216     -33.163  31.057  37.285  1.00104.77           C  
ANISOU 5768  CA  ALA C 216    14394  13098  12316   1943    569    459       C  
ATOM   5769  C   ALA C 216     -34.105  29.898  36.943  1.00106.76           C  
ANISOU 5769  C   ALA C 216    14403  13647  12513   2146    482    506       C  
ATOM   5770  O   ALA C 216     -34.567  29.818  35.805  1.00106.72           O  
ANISOU 5770  O   ALA C 216    14501  13608  12438   2305    446    617       O  
ATOM   5771  CB  ALA C 216     -31.718  30.581  37.288  1.00104.83           C  
ANISOU 5771  CB  ALA C 216    14254  13158  12419   1590    658    463       C  
ATOM   5772  N   LEU C 217     -34.417  29.032  37.938  1.00101.82           N  
ANISOU 5772  N   LEU C 217    13487  13290  11911   2153    455    408       N  
ATOM   5773  CA  LEU C 217     -35.317  27.878  37.801  1.00100.19           C  
ANISOU 5773  CA  LEU C 217    13015  13348  11705   2291    421    412       C  
ATOM   5774  C   LEU C 217     -36.760  28.296  37.521  1.00105.71           C  
ANISOU 5774  C   LEU C 217    13724  14028  12410   2616    337    353       C  
ATOM   5775  O   LEU C 217     -37.484  27.565  36.842  1.00104.91           O  
ANISOU 5775  O   LEU C 217    13449  14077  12332   2741    271    359       O  
ATOM   5776  CB  LEU C 217     -35.267  26.970  39.046  1.00 98.90           C  
ANISOU 5776  CB  LEU C 217    12619  13404  11553   2214    477    326       C  
ATOM   5777  CG  LEU C 217     -33.983  26.167  39.289  1.00102.22           C  
ANISOU 5777  CG  LEU C 217    12944  13930  11964   1968    510    369       C  
ATOM   5778  CD1 LEU C 217     -33.968  25.587  40.684  1.00102.08           C  
ANISOU 5778  CD1 LEU C 217    12834  14059  11893   1969    545    277       C  
ATOM   5779  CD2 LEU C 217     -33.805  25.063  38.266  1.00103.16           C  
ANISOU 5779  CD2 LEU C 217    12922  14176  12097   1913    526    488       C  
ATOM   5780  N   GLY C 218     -37.155  29.456  38.050  1.00104.37           N  
ANISOU 5780  N   GLY C 218    13744  13677  12236   2759    326    270       N  
ATOM   5781  CA  GLY C 218     -38.481  30.034  37.864  1.00106.26           C  
ANISOU 5781  CA  GLY C 218    14002  13877  12497   3110    235    188       C  
ATOM   5782  C   GLY C 218     -38.755  30.406  36.420  1.00111.58           C  
ANISOU 5782  C   GLY C 218    14873  14423  13098   3309     95    291       C  
ATOM   5783  O   GLY C 218     -39.883  30.254  35.946  1.00112.33           O  
ANISOU 5783  O   GLY C 218    14830  14625  13225   3606    -49    217       O  
ATOM   5784  N   ILE C 219     -37.707  30.871  35.710  1.00108.47           N  
ANISOU 5784  N   ILE C 219    14806  13801  12607   3151    144    448       N  
ATOM   5785  CA  ILE C 219     -37.741  31.261  34.296  1.00110.06           C  
ANISOU 5785  CA  ILE C 219    15325  13823  12669   3323     63    589       C  
ATOM   5786  C   ILE C 219     -37.941  30.018  33.402  1.00112.79           C  
ANISOU 5786  C   ILE C 219    15446  14426  12983   3346    -34    629       C  
ATOM   5787  O   ILE C 219     -38.672  30.095  32.411  1.00114.08           O  
ANISOU 5787  O   ILE C 219    15725  14579  13040   3660   -219    641       O  
ATOM   5788  CB  ILE C 219     -36.484  32.110  33.928  1.00114.29           C  
ANISOU 5788  CB  ILE C 219    16284  14006  13135   3088    244    738       C  
ATOM   5789  CG1 ILE C 219     -36.424  33.406  34.776  1.00116.75           C  
ANISOU 5789  CG1 ILE C 219    16840  14027  13491   3091    315    658       C  
ATOM   5790  CG2 ILE C 219     -36.433  32.443  32.431  1.00117.15           C  
ANISOU 5790  CG2 ILE C 219    17058  14154  13301   3259    228    921       C  
ATOM   5791  CD1 ILE C 219     -35.022  33.956  35.044  1.00124.51           C  
ANISOU 5791  CD1 ILE C 219    18008  14756  14543   2688    533    688       C  
ATOM   5792  N   PHE C 220     -37.331  28.868  33.786  1.00106.85           N  
ANISOU 5792  N   PHE C 220    14383  13902  12314   3047     67    627       N  
ATOM   5793  CA  PHE C 220     -37.444  27.581  33.083  1.00105.41           C  
ANISOU 5793  CA  PHE C 220    13968  13956  12125   3021      5    643       C  
ATOM   5794  C   PHE C 220     -38.894  27.064  33.061  1.00110.51           C  
ANISOU 5794  C   PHE C 220    14303  14821  12865   3291   -181    467       C  
ATOM   5795  O   PHE C 220     -39.264  26.328  32.145  1.00110.28           O  
ANISOU 5795  O   PHE C 220    14178  14919  12804   3386   -317    446       O  
ATOM   5796  CB  PHE C 220     -36.541  26.517  33.735  1.00104.34           C  
ANISOU 5796  CB  PHE C 220    13574  13994  12076   2674    165    658       C  
ATOM   5797  CG  PHE C 220     -35.073  26.555  33.379  1.00105.26           C  
ANISOU 5797  CG  PHE C 220    13864  13989  12142   2399    319    802       C  
ATOM   5798  CD1 PHE C 220     -34.613  25.989  32.196  1.00108.15           C  
ANISOU 5798  CD1 PHE C 220    14318  14362  12413   2361    342    919       C  
ATOM   5799  CD2 PHE C 220     -34.140  27.077  34.265  1.00107.27           C  
ANISOU 5799  CD2 PHE C 220    14151  14142  12464   2172    444    787       C  
ATOM   5800  CE1 PHE C 220     -33.251  26.002  31.878  1.00108.89           C  
ANISOU 5800  CE1 PHE C 220    14526  14350  12497   2099    532   1032       C  
ATOM   5801  CE2 PHE C 220     -32.779  27.089  33.948  1.00110.05           C  
ANISOU 5801  CE2 PHE C 220    14580  14400  12834   1902    594    873       C  
ATOM   5802  CZ  PHE C 220     -32.343  26.548  32.758  1.00108.02           C  
ANISOU 5802  CZ  PHE C 220    14395  14146  12503   1863    659   1001       C  
ATOM   5803  N   VAL C 221     -39.695  27.437  34.079  1.00108.20           N  
ANISOU 5803  N   VAL C 221    13837  14571  12704   3403   -173    314       N  
ATOM   5804  CA  VAL C 221     -41.103  27.053  34.233  1.00109.52           C  
ANISOU 5804  CA  VAL C 221    13642  14937  13034   3636   -294    101       C  
ATOM   5805  C   VAL C 221     -42.017  28.137  33.620  1.00117.46           C  
ANISOU 5805  C   VAL C 221    14826  15816  13988   4070   -533     29       C  
ATOM   5806  O   VAL C 221     -43.045  27.804  33.027  1.00118.94           O  
ANISOU 5806  O   VAL C 221    14779  16156  14256   4330   -755   -131       O  
ATOM   5807  CB  VAL C 221     -41.465  26.746  35.719  1.00112.65           C  
ANISOU 5807  CB  VAL C 221    13741  15456  13606   3517    -88    -30       C  
ATOM   5808  CG1 VAL C 221     -42.858  26.130  35.843  1.00114.01           C  
ANISOU 5808  CG1 VAL C 221    13464  15846  14010   3678   -129   -266       C  
ATOM   5809  CG2 VAL C 221     -40.426  25.834  36.371  1.00109.53           C  
ANISOU 5809  CG2 VAL C 221    13291  15133  13192   3147    125     69       C  
ATOM   5810  N   GLN C 222     -41.630  29.423  33.757  1.00115.70           N  
ANISOU 5810  N   GLN C 222    15019  15303  13637   4158   -499    129       N  
ATOM   5811  CA  GLN C 222     -42.379  30.577  33.247  1.00119.34           C  
ANISOU 5811  CA  GLN C 222    15754  15578  14010   4599   -703     92       C  
ATOM   5812  C   GLN C 222     -42.335  30.666  31.712  1.00125.31           C  
ANISOU 5812  C   GLN C 222    16837  16238  14537   4831   -928    209       C  
ATOM   5813  O   GLN C 222     -43.374  30.520  31.066  1.00127.17           O  
ANISOU 5813  O   GLN C 222    16926  16611  14783   5200  -1224     60       O  
ATOM   5814  CB  GLN C 222     -41.866  31.879  33.896  1.00121.65           C  
ANISOU 5814  CB  GLN C 222    16447  15540  14233   4575   -551    172       C  
ATOM   5815  CG  GLN C 222     -42.784  33.089  33.725  1.00141.89           C  
ANISOU 5815  CG  GLN C 222    19257  17907  16749   5057   -722     96       C  
ATOM   5816  CD  GLN C 222     -42.088  34.388  34.061  1.00163.34           C  
ANISOU 5816  CD  GLN C 222    22497  20211  19353   5006   -565    215       C  
ATOM   5817  OE1 GLN C 222     -42.007  35.317  33.248  1.00157.64           O  
ANISOU 5817  OE1 GLN C 222    21739  19437  18718   4720   -353    180       O  
ATOM   5818  NE2 GLN C 222     -41.544  34.471  35.266  1.00158.93           N  
ANISOU 5818  NE2 GLN C 222    22468  19331  18588   5299   -668    345       N  
ATOM   5819  N   HIS C 223     -41.138  30.907  31.140  1.00121.58           N  
ANISOU 5819  N   HIS C 223    16804  15530  13860   4624   -782    454       N  
ATOM   5820  CA  HIS C 223     -40.924  31.061  29.698  1.00123.61           C  
ANISOU 5820  CA  HIS C 223    17499  15634  13834   4825   -912    610       C  
ATOM   5821  C   HIS C 223     -40.865  29.733  28.933  1.00126.37           C  
ANISOU 5821  C   HIS C 223    17607  16252  14155   4735  -1013    589       C  
ATOM   5822  O   HIS C 223     -41.133  29.720  27.729  1.00128.36           O  
ANISOU 5822  O   HIS C 223    18128  16467  14174   5035  -1235    625       O  
ATOM   5823  CB  HIS C 223     -39.679  31.920  29.425  1.00124.92           C  
ANISOU 5823  CB  HIS C 223    18244  15400  13821   4619   -634    870       C  
ATOM   5824  CG  HIS C 223     -39.796  33.319  29.947  1.00130.73           C  
ANISOU 5824  CG  HIS C 223    19321  15802  14548   4762   -565    885       C  
ATOM   5825  ND1 HIS C 223     -40.251  34.351  29.148  1.00136.73           N  
ANISOU 5825  ND1 HIS C 223    20630  16255  15068   5208   -702    969       N  
ATOM   5826  CD2 HIS C 223     -39.534  33.806  31.182  1.00131.46           C  
ANISOU 5826  CD2 HIS C 223    19303  15821  14826   4540   -388    812       C  
ATOM   5827  CE1 HIS C 223     -40.241  35.430  29.914  1.00137.47           C  
ANISOU 5827  CE1 HIS C 223    20921  16081  15231   5223   -582    951       C  
ATOM   5828  NE2 HIS C 223     -39.816  35.151  31.146  1.00134.74           N  
ANISOU 5828  NE2 HIS C 223    20184  15869  15140   4821   -398    846       N  
ATOM   5829  N   ARG C 224     -40.526  28.625  29.635  1.00119.60           N  
ANISOU 5829  N   ARG C 224    16285  15647  13510   4351   -858    525       N  
ATOM   5830  CA  ARG C 224     -40.418  27.248  29.123  1.00117.78           C  
ANISOU 5830  CA  ARG C 224    15778  15668  13306   4201   -901    485       C  
ATOM   5831  C   ARG C 224     -39.388  27.116  27.983  1.00121.52           C  
ANISOU 5831  C   ARG C 224    16677  15989  13505   4111   -815    710       C  
ATOM   5832  O   ARG C 224     -39.747  26.843  26.832  1.00122.96           O  
ANISOU 5832  O   ARG C 224    17023  16202  13493   4365  -1038    696       O  
ATOM   5833  CB  ARG C 224     -41.794  26.654  28.741  1.00120.39           C  
ANISOU 5833  CB  ARG C 224    15741  16256  13745   4510  -1241    217       C  
ATOM   5834  CG  ARG C 224     -42.767  26.555  29.909  1.00132.20           C  
ANISOU 5834  CG  ARG C 224    16726  17931  15571   4526  -1233    -25       C  
ATOM   5835  CD  ARG C 224     -43.493  25.225  29.940  1.00143.92           C  
ANISOU 5835  CD  ARG C 224    17650  19728  17306   4435  -1308   -266       C  
ATOM   5836  NE  ARG C 224     -44.314  25.085  31.145  1.00154.76           N  
ANISOU 5836  NE  ARG C 224    18550  21242  19008   4383  -1180   -476       N  
ATOM   5837  CZ  ARG C 224     -43.892  24.551  32.289  1.00167.44           C  
ANISOU 5837  CZ  ARG C 224    19971  22894  20757   4025   -838   -436       C  
ATOM   5838  NH1 ARG C 224     -42.649  24.098  32.400  1.00151.93           N  
ANISOU 5838  NH1 ARG C 224    18202  20866  18660   3699   -633   -215       N  
ATOM   5839  NH2 ARG C 224     -44.709  24.469  33.330  1.00155.52           N  
ANISOU 5839  NH2 ARG C 224    18090  21489  19513   4017   -694   -626       N  
ATOM   5840  N   VAL C 225     -38.102  27.325  28.320  1.00116.29           N  
ANISOU 5840  N   VAL C 225    16189  15163  12834   3756   -487    894       N  
ATOM   5841  CA  VAL C 225     -36.970  27.237  27.386  1.00116.24           C  
ANISOU 5841  CA  VAL C 225    16551  14993  12623   3601   -294   1107       C  
ATOM   5842  C   VAL C 225     -35.848  26.357  27.955  1.00116.67           C  
ANISOU 5842  C   VAL C 225    16315  15171  12842   3143    -26   1146       C  
ATOM   5843  O   VAL C 225     -35.625  26.361  29.166  1.00114.37           O  
ANISOU 5843  O   VAL C 225    15744  14946  12765   2928     76   1079       O  
ATOM   5844  CB  VAL C 225     -36.452  28.616  26.889  1.00123.12           C  
ANISOU 5844  CB  VAL C 225    18048  15445  13287   3688   -138   1303       C  
ATOM   5845  CG1 VAL C 225     -37.451  29.269  25.937  1.00126.84           C  
ANISOU 5845  CG1 VAL C 225    18925  15784  13484   4220   -431   1307       C  
ATOM   5846  CG2 VAL C 225     -36.104  29.552  28.047  1.00122.62           C  
ANISOU 5846  CG2 VAL C 225    17973  15208  13410   3497     41   1294       C  
ATOM   5847  N   SER C 226     -35.156  25.601  27.079  1.00112.75           N  
ANISOU 5847  N   SER C 226    15907  14706  12225   3033     74   1243       N  
ATOM   5848  CA  SER C 226     -34.080  24.677  27.456  1.00109.84           C  
ANISOU 5848  CA  SER C 226    15273  14465  11997   2660    303   1274       C  
ATOM   5849  C   SER C 226     -32.812  25.349  27.992  1.00113.36           C  
ANISOU 5849  C   SER C 226    15804  14721  12546   2346    611   1374       C  
ATOM   5850  O   SER C 226     -32.220  24.837  28.944  1.00110.77           O  
ANISOU 5850  O   SER C 226    15129  14537  12421   2089    701   1312       O  
ATOM   5851  CB  SER C 226     -33.734  23.747  26.298  1.00113.58           C  
ANISOU 5851  CB  SER C 226    15847  15004  12304   2672    330   1336       C  
ATOM   5852  N   ALA C 227     -32.387  26.474  27.382  1.00112.43           N  
ANISOU 5852  N   ALA C 227    16155  14271  12294   2371    772   1512       N  
ATOM   5853  CA  ALA C 227     -31.173  27.187  27.788  1.00112.80           C  
ANISOU 5853  CA  ALA C 227    16279  14099  12483   2041   1088   1571       C  
ATOM   5854  C   ALA C 227     -31.414  28.629  28.233  1.00118.32           C  
ANISOU 5854  C   ALA C 227    17257  14498  13202   2096   1110   1570       C  
ATOM   5855  O   ALA C 227     -32.295  29.308  27.701  1.00119.96           O  
ANISOU 5855  O   ALA C 227    17827  14542  13211   2434    970   1618       O  
ATOM   5856  CB  ALA C 227     -30.143  27.145  26.671  1.00115.37           C  
ANISOU 5856  CB  ALA C 227    16896  14245  12693   1899   1405   1735       C  
ATOM   5857  N   LEU C 228     -30.614  29.086  29.213  1.00114.39           N  
ANISOU 5857  N   LEU C 228    16593  13925  12944   1781   1266   1493       N  
ATOM   5858  CA  LEU C 228     -30.654  30.433  29.781  1.00116.26           C  
ANISOU 5858  CA  LEU C 228    17064  13858  13251   1755   1322   1455       C  
ATOM   5859  C   LEU C 228     -29.235  31.029  29.754  1.00122.06           C  
ANISOU 5859  C   LEU C 228    17895  14322  14160   1345   1690   1478       C  
ATOM   5860  O   LEU C 228     -28.341  30.474  30.397  1.00120.18           O  
ANISOU 5860  O   LEU C 228    17242  14270  14151   1040   1752   1362       O  
ATOM   5861  CB  LEU C 228     -31.197  30.383  31.223  1.00114.31           C  
ANISOU 5861  CB  LEU C 228    16453  13818  13161   1775   1102   1254       C  
ATOM   5862  CG  LEU C 228     -32.671  30.732  31.434  1.00119.28           C  
ANISOU 5862  CG  LEU C 228    17160  14479  13682   2177    836   1199       C  
ATOM   5863  CD1 LEU C 228     -33.590  29.599  30.988  1.00117.67           C  
ANISOU 5863  CD1 LEU C 228    16728  14599  13382   2425    613   1186       C  
ATOM   5864  CD2 LEU C 228     -32.939  31.022  32.889  1.00120.89           C  
ANISOU 5864  CD2 LEU C 228    17125  14763  14044   2133    749   1013       C  
ATOM   5865  N   PRO C 229     -28.980  32.124  29.002  1.00122.36           N  
ANISOU 5865  N   PRO C 229    18471  13912  14106   1332   1953   1614       N  
ATOM   5866  CA  PRO C 229     -27.612  32.663  28.950  1.00124.69           C  
ANISOU 5866  CA  PRO C 229    18815  13932  14629    890   2362   1607       C  
ATOM   5867  C   PRO C 229     -27.250  33.589  30.108  1.00129.74           C  
ANISOU 5867  C   PRO C 229    19345  14401  15547    640   2384   1407       C  
ATOM   5868  O   PRO C 229     -27.981  34.538  30.399  1.00130.72           O  
ANISOU 5868  O   PRO C 229    19785  14291  15593    832   2289   1397       O  
ATOM   5869  CB  PRO C 229     -27.551  33.372  27.589  1.00130.47           C  
ANISOU 5869  CB  PRO C 229    20234  14226  15112    994   2683   1856       C  
ATOM   5870  CG  PRO C 229     -28.980  33.455  27.095  1.00134.80           C  
ANISOU 5870  CG  PRO C 229    21135  14792  15292   1548   2355   1965       C  
ATOM   5871  CD  PRO C 229     -29.892  32.908  28.149  1.00126.62           C  
ANISOU 5871  CD  PRO C 229    19613  14159  14337   1724   1907   1774       C  
ATOM   5872  N   VAL C 230     -26.110  33.305  30.768  1.00126.11           N  
ANISOU 5872  N   VAL C 230    18434  14065  15417    233   2489   1223       N  
ATOM   5873  CA  VAL C 230     -25.581  34.102  31.881  1.00127.59           C  
ANISOU 5873  CA  VAL C 230    18463  14115  15899    -49   2491    975       C  
ATOM   5874  C   VAL C 230     -24.889  35.323  31.262  1.00136.53           C  
ANISOU 5874  C   VAL C 230    20030  14686  17159   -330   2943   1028       C  
ATOM   5875  O   VAL C 230     -23.837  35.192  30.630  1.00138.11           O  
ANISOU 5875  O   VAL C 230    20165  14781  17531   -648   3308   1056       O  
ATOM   5876  CB  VAL C 230     -24.648  33.287  32.825  1.00129.86           C  
ANISOU 5876  CB  VAL C 230    18092  14775  16475   -324   2364    723       C  
ATOM   5877  CG1 VAL C 230     -24.166  34.138  33.999  1.00131.81           C  
ANISOU 5877  CG1 VAL C 230    18197  14890  16996   -574   2297    424       C  
ATOM   5878  CG2 VAL C 230     -25.337  32.022  33.331  1.00125.08           C  
ANISOU 5878  CG2 VAL C 230    17152  14666  15707    -37   1993    718       C  
ATOM   5879  N   VAL C 231     -25.523  36.498  31.400  1.00135.48           N  
ANISOU 5879  N   VAL C 231    20367  14173  16936   -194   2949   1050       N  
ATOM   5880  CA  VAL C 231     -25.052  37.757  30.817  1.00140.63           C  
ANISOU 5880  CA  VAL C 231    21559  14209  17666   -410   3395   1127       C  
ATOM   5881  C   VAL C 231     -24.600  38.750  31.899  1.00146.98           C  
ANISOU 5881  C   VAL C 231    22275  14765  18804   -729   3416    829       C  
ATOM   5882  O   VAL C 231     -25.294  38.934  32.899  1.00144.84           O  
ANISOU 5882  O   VAL C 231    21906  14632  18496   -535   3050    673       O  
ATOM   5883  CB  VAL C 231     -26.127  38.374  29.868  1.00146.30           C  
ANISOU 5883  CB  VAL C 231    23034  14593  17959     54   3431   1431       C  
ATOM   5884  CG1 VAL C 231     -25.608  39.624  29.165  1.00152.11           C  
ANISOU 5884  CG1 VAL C 231    24431  14637  18728   -151   3961   1560       C  
ATOM   5885  CG2 VAL C 231     -26.619  37.356  28.838  1.00143.78           C  
ANISOU 5885  CG2 VAL C 231    22779  14555  17297    398   3331   1671       C  
ATOM   5886  N   ASP C 232     -23.443  39.400  31.670  1.00148.02           N  
ANISOU 5886  N   ASP C 232    22456  14514  19271  -1226   3870    735       N  
ATOM   5887  CA  ASP C 232     -22.851  40.429  32.529  1.00151.52           C  
ANISOU 5887  CA  ASP C 232    22849  14636  20087  -1611   3965    422       C  
ATOM   5888  C   ASP C 232     -23.705  41.709  32.455  1.00157.91           C  
ANISOU 5888  C   ASP C 232    24394  14910  20696  -1378   4034    535       C  
ATOM   5889  O   ASP C 232     -24.431  41.905  31.476  1.00158.00           O  
ANISOU 5889  O   ASP C 232    25000  14698  20337  -1015   4157    878       O  
ATOM   5890  CB  ASP C 232     -21.401  40.709  32.083  1.00158.12           C  
ANISOU 5890  CB  ASP C 232    23533  15184  21361  -2218   4505    304       C  
ATOM   5891  CG  ASP C 232     -20.614  41.642  32.984  1.00172.93           C  
ANISOU 5891  CG  ASP C 232    25218  16770  23715  -2701   4594   -102       C  
ATOM   5892  OD1 ASP C 232     -20.312  41.245  34.131  1.00171.79           O  
ANISOU 5892  OD1 ASP C 232    24466  17021  23783  -2797   4182   -459       O  
ATOM   5893  OD2 ASP C 232     -20.278  42.757  32.533  1.00184.44           O  
ANISOU 5893  OD2 ASP C 232    27156  17593  25332  -2983   5083    -75       O  
ATOM   5894  N   GLU C 233     -23.611  42.573  33.489  1.00156.37           N  
ANISOU 5894  N   GLU C 233    24175  14507  20731  -1556   3934    232       N  
ATOM   5895  CA  GLU C 233     -24.358  43.834  33.614  1.00159.10           C  
ANISOU 5895  CA  GLU C 233    25180  14334  20937  -1352   3978    274       C  
ATOM   5896  C   GLU C 233     -24.167  44.797  32.430  1.00168.04           C  
ANISOU 5896  C   GLU C 233    27090  14751  22008  -1443   4566    549       C  
ATOM   5897  O   GLU C 233     -25.086  45.555  32.115  1.00169.26           O  
ANISOU 5897  O   GLU C 233    27920  14539  21850  -1042   4571    751       O  
ATOM   5898  CB  GLU C 233     -24.051  44.541  34.951  1.00162.39           C  
ANISOU 5898  CB  GLU C 233    25382  14649  21672  -1623   3808   -159       C  
ATOM   5899  CG  GLU C 233     -24.163  43.665  36.196  1.00168.33           C  
ANISOU 5899  CG  GLU C 233    25448  16055  22456  -1533   3258   -444       C  
ATOM   5900  CD  GLU C 233     -25.408  42.808  36.337  1.00182.11           C  
ANISOU 5900  CD  GLU C 233    27123  18288  23783   -937   2843   -255       C  
ATOM   5901  OE1 GLU C 233     -26.528  43.369  36.329  1.00176.66           O  
ANISOU 5901  OE1 GLU C 233    26890  17417  22816   -510   2743   -123       O  
ATOM   5902  OE2 GLU C 233     -25.261  41.572  36.471  1.00170.91           O  
ANISOU 5902  OE2 GLU C 233    25178  17424  22337   -898   2627   -258       O  
ATOM   5903  N   LYS C 234     -22.991  44.753  31.773  1.00167.46           N  
ANISOU 5903  N   LYS C 234    26934  14474  22219  -1942   5074    560       N  
ATOM   5904  CA  LYS C 234     -22.674  45.577  30.603  1.00172.89           C  
ANISOU 5904  CA  LYS C 234    28372  14465  22852  -2081   5734    836       C  
ATOM   5905  C   LYS C 234     -23.414  45.076  29.354  1.00174.79           C  
ANISOU 5905  C   LYS C 234    29112  14762  22540  -1550   5770   1305       C  
ATOM   5906  O   LYS C 234     -23.781  45.881  28.497  1.00178.45           O  
ANISOU 5906  O   LYS C 234    30439  14650  22713  -1335   6107   1604       O  
ATOM   5907  CB  LYS C 234     -21.160  45.606  30.354  1.00179.52           C  
ANISOU 5907  CB  LYS C 234    28879  15113  24219  -2810   6295    658       C  
ATOM   5908  N   GLY C 235     -23.618  43.759  29.274  1.00165.60           N  
ANISOU 5908  N   GLY C 235    27428  14269  21224  -1333   5414   1350       N  
ATOM   5909  CA  GLY C 235     -24.308  43.101  28.169  1.00163.40           C  
ANISOU 5909  CA  GLY C 235    27493  14150  20441   -834   5350   1723       C  
ATOM   5910  C   GLY C 235     -23.524  41.989  27.496  1.00165.43           C  
ANISOU 5910  C   GLY C 235    27364  14737  20754  -1043   5553   1795       C  
ATOM   5911  O   GLY C 235     -23.932  41.506  26.436  1.00164.42           O  
ANISOU 5911  O   GLY C 235    27600  14659  20213   -689   5597   2101       O  
ATOM   5912  N   ARG C 236     -22.411  41.553  28.122  1.00161.28           N  
ANISOU 5912  N   ARG C 236    26089  14458  20730  -1583   5640   1489       N  
ATOM   5913  CA  ARG C 236     -21.526  40.504  27.610  1.00159.91           C  
ANISOU 5913  CA  ARG C 236    25453  14608  20698  -1826   5848   1496       C  
ATOM   5914  C   ARG C 236     -21.913  39.107  28.100  1.00156.77           C  
ANISOU 5914  C   ARG C 236    24388  14976  20201  -1560   5258   1413       C  
ATOM   5915  O   ARG C 236     -22.107  38.911  29.299  1.00153.31           O  
ANISOU 5915  O   ARG C 236    23451  14873  19929  -1558   4800   1142       O  
ATOM   5916  CB  ARG C 236     -20.066  40.815  27.977  1.00164.21           C  
ANISOU 5916  CB  ARG C 236    25530  14984  21877  -2541   6279   1182       C  
ATOM   5917  N   VAL C 237     -22.004  38.133  27.174  1.00151.14           N  
ANISOU 5917  N   VAL C 237    23705  14514  19209  -1341   5295   1642       N  
ATOM   5918  CA  VAL C 237     -22.344  36.741  27.497  1.00144.91           C  
ANISOU 5918  CA  VAL C 237    22341  14401  18319  -1102   4806   1587       C  
ATOM   5919  C   VAL C 237     -21.077  36.031  27.999  1.00147.80           C  
ANISOU 5919  C   VAL C 237    21922  15081  19155  -1556   4896   1314       C  
ATOM   5920  O   VAL C 237     -20.087  35.948  27.267  1.00150.40           O  
ANISOU 5920  O   VAL C 237    22228  15255  19663  -1869   5400   1352       O  
ATOM   5921  CB  VAL C 237     -23.027  35.993  26.313  1.00147.22           C  
ANISOU 5921  CB  VAL C 237    23003  14823  18112   -656   4761   1908       C  
ATOM   5922  N   VAL C 238     -21.109  35.544  29.254  1.00140.66           N  
ANISOU 5922  N   VAL C 238    20396  14606  18444  -1569   4416   1032       N  
ATOM   5923  CA  VAL C 238     -19.977  34.863  29.893  1.00140.00           C  
ANISOU 5923  CA  VAL C 238    19545  14861  18786  -1917   4380    732       C  
ATOM   5924  C   VAL C 238     -20.220  33.336  30.001  1.00138.28           C  
ANISOU 5924  C   VAL C 238    18903  15239  18397  -1636   4009    765       C  
ATOM   5925  O   VAL C 238     -19.330  32.560  29.646  1.00138.14           O  
ANISOU 5925  O   VAL C 238    18514  15417  18556  -1806   4190    722       O  
ATOM   5926  CB  VAL C 238     -19.565  35.531  31.246  1.00145.42           C  
ANISOU 5926  CB  VAL C 238    19870  15526  19857  -2195   4169    339       C  
ATOM   5927  CG1 VAL C 238     -20.705  35.550  32.268  1.00141.55           C  
ANISOU 5927  CG1 VAL C 238    19422  15239  19120  -1825   3606    286       C  
ATOM   5928  CG2 VAL C 238     -18.300  34.907  31.833  1.00146.03           C  
ANISOU 5928  CG2 VAL C 238    19165  15929  20391  -2538   4124     -5       C  
ATOM   5929  N   ASP C 239     -21.416  32.917  30.463  1.00130.21           N  
ANISOU 5929  N   ASP C 239    17945  14478  17052  -1215   3533    835       N  
ATOM   5930  CA  ASP C 239     -21.780  31.507  30.624  1.00125.18           C  
ANISOU 5930  CA  ASP C 239    16963  14353  16247   -947   3193    866       C  
ATOM   5931  C   ASP C 239     -23.185  31.187  30.096  1.00125.75           C  
ANISOU 5931  C   ASP C 239    17427  14486  15864   -478   2980   1118       C  
ATOM   5932  O   ASP C 239     -23.882  32.081  29.613  1.00126.98           O  
ANISOU 5932  O   ASP C 239    18126  14304  15816   -317   3060   1269       O  
ATOM   5933  CB  ASP C 239     -21.624  31.067  32.093  1.00124.85           C  
ANISOU 5933  CB  ASP C 239    16374  14675  16389   -971   2776    574       C  
ATOM   5934  CG  ASP C 239     -20.242  30.554  32.442  1.00136.31           C  
ANISOU 5934  CG  ASP C 239    17246  16326  18220  -1287   2845    331       C  
ATOM   5935  OD1 ASP C 239     -19.850  29.491  31.912  1.00135.45           O  
ANISOU 5935  OD1 ASP C 239    16916  16455  18092  -1247   2919    410       O  
ATOM   5936  OD2 ASP C 239     -19.570  31.191  33.281  1.00145.11           O  
ANISOU 5936  OD2 ASP C 239    18108  17375  19652  -1550   2790     36       O  
ATOM   5937  N   ILE C 240     -23.580  29.900  30.165  1.00118.15           N  
ANISOU 5937  N   ILE C 240    16186  13945  14760   -254   2709   1145       N  
ATOM   5938  CA  ILE C 240     -24.890  29.407  29.737  1.00115.22           C  
ANISOU 5938  CA  ILE C 240    16049  13704  14025    166   2461   1311       C  
ATOM   5939  C   ILE C 240     -25.381  28.312  30.700  1.00114.80           C  
ANISOU 5939  C   ILE C 240    15551  14098  13971    317   2073   1189       C  
ATOM   5940  O   ILE C 240     -24.691  27.311  30.913  1.00112.96           O  
ANISOU 5940  O   ILE C 240    14927  14134  13860    208   2061   1119       O  
ATOM   5941  CB  ILE C 240     -24.938  29.001  28.227  1.00119.17           C  
ANISOU 5941  CB  ILE C 240    16893  14118  14267    300   2681   1549       C  
ATOM   5942  CG1 ILE C 240     -26.365  28.586  27.791  1.00117.61           C  
ANISOU 5942  CG1 ILE C 240    16924  14048  13713    751   2362   1662       C  
ATOM   5943  CG2 ILE C 240     -23.884  27.938  27.854  1.00119.39           C  
ANISOU 5943  CG2 ILE C 240    16579  14357  14426    109   2873   1533       C  
ATOM   5944  CD1 ILE C 240     -26.729  28.917  26.348  1.00127.63           C  
ANISOU 5944  CD1 ILE C 240    18798  15053  14641    979   2523   1889       C  
ATOM   5945  N   TYR C 241     -26.556  28.539  31.310  1.00109.79           N  
ANISOU 5945  N   TYR C 241    14992  13515  13209    573   1785   1158       N  
ATOM   5946  CA  TYR C 241     -27.182  27.615  32.252  1.00106.30           C  
ANISOU 5946  CA  TYR C 241    14209  13433  12746    728   1477   1055       C  
ATOM   5947  C   TYR C 241     -28.356  26.900  31.580  1.00108.35           C  
ANISOU 5947  C   TYR C 241    14567  13834  12768   1050   1327   1173       C  
ATOM   5948  O   TYR C 241     -29.431  27.482  31.407  1.00108.53           O  
ANISOU 5948  O   TYR C 241    14840  13746  12650   1298   1207   1206       O  
ATOM   5949  CB  TYR C 241     -27.610  28.347  33.540  1.00107.58           C  
ANISOU 5949  CB  TYR C 241    14336  13564  12977    756   1302    891       C  
ATOM   5950  CG  TYR C 241     -27.976  27.424  34.684  1.00106.67           C  
ANISOU 5950  CG  TYR C 241    13880  13788  12860    854   1066    771       C  
ATOM   5951  CD1 TYR C 241     -26.996  26.881  35.508  1.00108.31           C  
ANISOU 5951  CD1 TYR C 241    13760  14178  13213    676   1025    631       C  
ATOM   5952  CD2 TYR C 241     -29.305  27.121  34.964  1.00105.85           C  
ANISOU 5952  CD2 TYR C 241    13796  13808  12614   1137    897    783       C  
ATOM   5953  CE1 TYR C 241     -27.326  26.044  36.573  1.00107.23           C  
ANISOU 5953  CE1 TYR C 241    13405  14313  13023    799    833    543       C  
ATOM   5954  CE2 TYR C 241     -29.648  26.282  36.023  1.00104.88           C  
ANISOU 5954  CE2 TYR C 241    13415  13952  12484   1212    757    686       C  
ATOM   5955  CZ  TYR C 241     -28.654  25.743  36.824  1.00111.96           C  
ANISOU 5955  CZ  TYR C 241    14071  15000  13470   1053    732    585       C  
ATOM   5956  OH  TYR C 241     -28.982  24.915  37.871  1.00111.52           O  
ANISOU 5956  OH  TYR C 241    13849  15170  13354   1160    617    515       O  
ATOM   5957  N   SER C 242     -28.124  25.647  31.163  1.00103.13           N  
ANISOU 5957  N   SER C 242    13702  13406  12076   1050   1329   1212       N  
ATOM   5958  CA  SER C 242     -29.112  24.800  30.495  1.00101.53           C  
ANISOU 5958  CA  SER C 242    13534  13355  11689   1308   1185   1276       C  
ATOM   5959  C   SER C 242     -29.816  23.885  31.508  1.00102.71           C  
ANISOU 5959  C   SER C 242    13345  13792  11888   1398    972   1158       C  
ATOM   5960  O   SER C 242     -29.452  23.884  32.688  1.00101.54           O  
ANISOU 5960  O   SER C 242    12985  13726  11871   1284    945   1053       O  
ATOM   5961  CB  SER C 242     -28.435  23.973  29.403  1.00105.24           C  
ANISOU 5961  CB  SER C 242    14029  13868  12089   1248   1347   1378       C  
ATOM   5962  OG  SER C 242     -29.377  23.239  28.638  1.00113.57           O  
ANISOU 5962  OG  SER C 242    15166  15031  12952   1496   1193   1415       O  
ATOM   5963  N   LYS C 243     -30.822  23.108  31.045  1.00 98.30           N  
ANISOU 5963  N   LYS C 243    12754  13372  11224   1604    832   1161       N  
ATOM   5964  CA  LYS C 243     -31.578  22.153  31.865  1.00 96.22           C  
ANISOU 5964  CA  LYS C 243    12194  13344  11021   1673    701   1055       C  
ATOM   5965  C   LYS C 243     -30.678  21.036  32.407  1.00 98.61           C  
ANISOU 5965  C   LYS C 243    12243  13816  11409   1502    785   1044       C  
ATOM   5966  O   LYS C 243     -30.968  20.480  33.467  1.00 97.03           O  
ANISOU 5966  O   LYS C 243    11850  13751  11266   1507    742    966       O  
ATOM   5967  CB  LYS C 243     -32.761  21.563  31.080  1.00 98.73           C  
ANISOU 5967  CB  LYS C 243    12511  13749  11255   1889    553   1026       C  
ATOM   5968  CG  LYS C 243     -33.955  22.504  30.980  1.00113.48           C  
ANISOU 5968  CG  LYS C 243    14509  15529  13080   2135    388    965       C  
ATOM   5969  CD  LYS C 243     -35.235  21.762  30.613  1.00122.68           C  
ANISOU 5969  CD  LYS C 243    15499  16854  14260   2331    200    839       C  
ATOM   5970  CE  LYS C 243     -36.478  22.574  30.897  1.00133.61           C  
ANISOU 5970  CE  LYS C 243    16867  18213  15686   2577     32    717       C  
ATOM   5971  NZ  LYS C 243     -36.697  23.645  29.888  1.00144.64           N  
ANISOU 5971  NZ  LYS C 243    18644  19417  16897   2826    -99    782       N  
ATOM   5972  N   PHE C 244     -29.580  20.728  31.685  1.00 95.65           N  
ANISOU 5972  N   PHE C 244    11897  13417  11030   1373    925   1122       N  
ATOM   5973  CA  PHE C 244     -28.589  19.720  32.061  1.00 94.63           C  
ANISOU 5973  CA  PHE C 244    11539  13433  10982   1247   1000   1109       C  
ATOM   5974  C   PHE C 244     -27.763  20.178  33.264  1.00 99.21           C  
ANISOU 5974  C   PHE C 244    11975  14028  11693   1119    995   1022       C  
ATOM   5975  O   PHE C 244     -27.368  19.344  34.074  1.00 98.09           O  
ANISOU 5975  O   PHE C 244    11636  14043  11591   1114    953    970       O  
ATOM   5976  CB  PHE C 244     -27.665  19.394  30.874  1.00 97.21           C  
ANISOU 5976  CB  PHE C 244    11936  13717  11284   1167   1175   1199       C  
ATOM   5977  CG  PHE C 244     -26.674  18.285  31.140  1.00 98.13           C  
ANISOU 5977  CG  PHE C 244    11808  13989  11488   1086   1245   1177       C  
ATOM   5978  CD1 PHE C 244     -27.047  16.953  31.014  1.00 99.91           C  
ANISOU 5978  CD1 PHE C 244    11955  14350  11657   1183   1205   1182       C  
ATOM   5979  CD2 PHE C 244     -25.370  18.574  31.523  1.00101.46           C  
ANISOU 5979  CD2 PHE C 244    12069  14412  12071    923   1345   1128       C  
ATOM   5980  CE1 PHE C 244     -26.133  15.930  31.272  1.00100.59           C  
ANISOU 5980  CE1 PHE C 244    11853  14558  11810   1152   1266   1168       C  
ATOM   5981  CE2 PHE C 244     -24.457  17.551  31.781  1.00104.18           C  
ANISOU 5981  CE2 PHE C 244    12170  14913  12500    903   1375   1088       C  
ATOM   5982  CZ  PHE C 244     -24.844  16.236  31.655  1.00100.85           C  
ANISOU 5982  CZ  PHE C 244    11722  14612  11986   1035   1337   1123       C  
ATOM   5983  N   ASP C 245     -27.491  21.491  33.373  1.00 97.53           N  
ANISOU 5983  N   ASP C 245    11886  13637  11536   1030   1027    994       N  
ATOM   5984  CA  ASP C 245     -26.705  22.068  34.469  1.00 98.42           C  
ANISOU 5984  CA  ASP C 245    11867  13743  11785    896    990    862       C  
ATOM   5985  C   ASP C 245     -27.419  21.997  35.833  1.00101.35           C  
ANISOU 5985  C   ASP C 245    12184  14218  12106   1022    812    763       C  
ATOM   5986  O   ASP C 245     -26.773  22.150  36.872  1.00101.62           O  
ANISOU 5986  O   ASP C 245    12098  14309  12203    965    727    633       O  
ATOM   5987  CB  ASP C 245     -26.267  23.501  34.126  1.00102.73           C  
ANISOU 5987  CB  ASP C 245    12589  14021  12422    739   1108    845       C  
ATOM   5988  CG  ASP C 245     -25.423  23.586  32.870  1.00114.52           C  
ANISOU 5988  CG  ASP C 245    14159  15386  13968    590   1362    943       C  
ATOM   5989  OD1 ASP C 245     -24.214  23.276  32.945  1.00116.15           O  
ANISOU 5989  OD1 ASP C 245    14121  15659  14350    410   1463    869       O  
ATOM   5990  OD2 ASP C 245     -25.974  23.948  31.809  1.00120.90           O  
ANISOU 5990  OD2 ASP C 245    15277  16027  14631    678   1461   1085       O  
ATOM   5991  N   VAL C 246     -28.741  21.732  35.819  1.00 96.74           N  
ANISOU 5991  N   VAL C 246    11683  13663  11411   1202    762    804       N  
ATOM   5992  CA  VAL C 246     -29.585  21.594  37.011  1.00 96.03           C  
ANISOU 5992  CA  VAL C 246    11565  13655  11266   1331    672    725       C  
ATOM   5993  C   VAL C 246     -29.292  20.256  37.722  1.00 98.94           C  
ANISOU 5993  C   VAL C 246    11779  14217  11597   1364    665    718       C  
ATOM   5994  O   VAL C 246     -29.339  20.208  38.953  1.00 98.91           O  
ANISOU 5994  O   VAL C 246    11775  14268  11536   1425    609    637       O  
ATOM   5995  CB  VAL C 246     -31.099  21.759  36.686  1.00 99.64           C  
ANISOU 5995  CB  VAL C 246    12105  14080  11674   1502    655    742       C  
ATOM   5996  CG1 VAL C 246     -31.935  21.841  37.961  1.00 99.57           C  
ANISOU 5996  CG1 VAL C 246    12076  14118  11637   1616    630    643       C  
ATOM   5997  CG2 VAL C 246     -31.354  22.983  35.807  1.00100.80           C  
ANISOU 5997  CG2 VAL C 246    12463  14020  11816   1533    646    777       C  
ATOM   5998  N   ILE C 247     -28.962  19.187  36.952  1.00 94.61           N  
ANISOU 5998  N   ILE C 247    11145  13748  11053   1344    728    802       N  
ATOM   5999  CA  ILE C 247     -28.660  17.845  37.477  1.00 93.77           C  
ANISOU 5999  CA  ILE C 247    10941  13785  10903   1396    743    817       C  
ATOM   6000  C   ILE C 247     -27.438  17.847  38.431  1.00 98.76           C  
ANISOU 6000  C   ILE C 247    11495  14489  11539   1382    649    735       C  
ATOM   6001  O   ILE C 247     -27.288  16.914  39.224  1.00 98.33           O  
ANISOU 6001  O   ILE C 247    11434  14533  11394   1495    623    733       O  
ATOM   6002  CB  ILE C 247     -28.544  16.783  36.339  1.00 96.05           C  
ANISOU 6002  CB  ILE C 247    11181  14111  11202   1381    832    910       C  
ATOM   6003  CG1 ILE C 247     -29.826  16.726  35.494  1.00 95.81           C  
ANISOU 6003  CG1 ILE C 247    11132  14158  11113   1473    888    933       C  
ATOM   6004  CG2 ILE C 247     -28.150  15.389  36.845  1.00 97.45           C  
ANISOU 6004  CG2 ILE C 247    11268  14307  11450   1281    867    927       C  
ATOM   6005  CD1 ILE C 247     -31.063  16.393  36.255  1.00102.55           C  
ANISOU 6005  CD1 ILE C 247    11999  14983  11980   1499    948    939       C  
ATOM   6006  N   ASN C 248     -26.597  18.906  38.368  1.00 96.77           N  
ANISOU 6006  N   ASN C 248    11200  14174  11395   1255    594    649       N  
ATOM   6007  CA  ASN C 248     -25.420  19.089  39.221  1.00 98.40           C  
ANISOU 6007  CA  ASN C 248    11279  14454  11656   1228    453    502       C  
ATOM   6008  C   ASN C 248     -25.819  19.313  40.687  1.00103.00           C  
ANISOU 6008  C   ASN C 248    11977  15068  12091   1370    306    397       C  
ATOM   6009  O   ASN C 248     -25.050  18.962  41.584  1.00104.00           O  
ANISOU 6009  O   ASN C 248    12042  15308  12164   1462    145    288       O  
ATOM   6010  CB  ASN C 248     -24.553  20.239  38.713  1.00101.29           C  
ANISOU 6010  CB  ASN C 248    11555  14704  12226   1007    476    407       C  
ATOM   6011  CG  ASN C 248     -23.169  20.258  39.313  1.00127.44           C  
ANISOU 6011  CG  ASN C 248    14623  18120  15679    946    334    214       C  
ATOM   6012  OD1 ASN C 248     -22.300  19.452  38.962  1.00122.34           O  
ANISOU 6012  OD1 ASN C 248    13772  17596  15117    949    352    211       O  
ATOM   6013  ND2 ASN C 248     -22.937  21.177  40.238  1.00121.42           N  
ANISOU 6013  ND2 ASN C 248    13863  17317  14953    906    171     19       N  
ATOM   6014  N   LEU C 249     -27.026  19.881  40.923  1.00 98.94           N  
ANISOU 6014  N   LEU C 249    11641  14456  11497   1420    357    420       N  
ATOM   6015  CA  LEU C 249     -27.582  20.117  42.260  1.00 99.58           C  
ANISOU 6015  CA  LEU C 249    11881  14543  11412   1568    283    334       C  
ATOM   6016  C   LEU C 249     -27.937  18.786  42.929  1.00103.01           C  
ANISOU 6016  C   LEU C 249    12393  15085  11660   1754    339    414       C  
ATOM   6017  O   LEU C 249     -27.859  18.680  44.152  1.00103.96           O  
ANISOU 6017  O   LEU C 249    12658  15246  11595   1908    254    340       O  
ATOM   6018  CB  LEU C 249     -28.826  21.022  42.195  1.00 99.36           C  
ANISOU 6018  CB  LEU C 249    11993  14378  11380   1584    370    339       C  
ATOM   6019  CG  LEU C 249     -28.591  22.495  41.852  1.00105.23           C  
ANISOU 6019  CG  LEU C 249    12776  14955  12252   1449    321    250       C  
ATOM   6020  CD1 LEU C 249     -29.779  23.073  41.114  1.00104.77           C  
ANISOU 6020  CD1 LEU C 249    12817  14765  12224   1485    432    331       C  
ATOM   6021  CD2 LEU C 249     -28.292  23.317  43.098  1.00109.80           C  
ANISOU 6021  CD2 LEU C 249    13461  15494  12764   1481    174     55       C  
ATOM   6022  N   ALA C 250     -28.324  17.778  42.119  1.00 98.08           N  
ANISOU 6022  N   ALA C 250    11713  14483  11070   1744    494    560       N  
ATOM   6023  CA  ALA C 250     -28.660  16.427  42.570  1.00 97.77           C  
ANISOU 6023  CA  ALA C 250    11764  14493  10892   1882    610    652       C  
ATOM   6024  C   ALA C 250     -27.398  15.559  42.655  1.00102.49           C  
ANISOU 6024  C   ALA C 250    12300  15192  11449   1953    499    662       C  
ATOM   6025  O   ALA C 250     -27.327  14.670  43.506  1.00103.10           O  
ANISOU 6025  O   ALA C 250    12540  15298  11336   2138    512    698       O  
ATOM   6026  CB  ALA C 250     -29.665  15.794  41.621  1.00 96.96           C  
ANISOU 6026  CB  ALA C 250    11611  14347  10883   1818    811    758       C  
ATOM   6027  N   ALA C 251     -26.406  15.825  41.775  1.00 98.97           N  
ANISOU 6027  N   ALA C 251    11637  14786  11179   1824    411    627       N  
ATOM   6028  CA  ALA C 251     -25.125  15.115  41.709  1.00 99.79           C  
ANISOU 6028  CA  ALA C 251    11601  15002  11311   1888    301    600       C  
ATOM   6029  C   ALA C 251     -24.234  15.423  42.918  1.00106.25           C  
ANISOU 6029  C   ALA C 251    12418  15913  12038   2032     29    427       C  
ATOM   6030  O   ALA C 251     -23.586  14.517  43.446  1.00107.16           O  
ANISOU 6030  O   ALA C 251    12557  16125  12034   2243    -85    418       O  
ATOM   6031  CB  ALA C 251     -24.398  15.469  40.420  1.00100.15           C  
ANISOU 6031  CB  ALA C 251    11406  15047  11601   1686    343    590       C  
ATOM   6032  N   GLU C 252     -24.202  16.701  43.346  1.00103.86           N  
ANISOU 6032  N   GLU C 252    12106  15573  11783   1940    -95    273       N  
ATOM   6033  CA  GLU C 252     -23.410  17.178  44.482  1.00106.56           C  
ANISOU 6033  CA  GLU C 252    12441  15996  12050   2058   -397     49       C  
ATOM   6034  C   GLU C 252     -24.238  17.273  45.772  1.00111.10           C  
ANISOU 6034  C   GLU C 252    13373  16533  12308   2267   -432     40       C  
ATOM   6035  O   GLU C 252     -23.675  17.563  46.833  1.00113.40           O  
ANISOU 6035  O   GLU C 252    13741  16892  12454   2429   -707   -148       O  
ATOM   6036  CB  GLU C 252     -22.772  18.542  44.156  1.00109.24           C  
ANISOU 6036  CB  GLU C 252    12554  16289  12663   1800   -498   -154       C  
ATOM   6037  N   LYS C 253     -25.568  17.019  45.677  1.00105.64           N  
ANISOU 6037  N   LYS C 253    12891  15734  11515   2272   -152    220       N  
ATOM   6038  CA  LYS C 253     -26.556  17.090  46.767  1.00106.20           C  
ANISOU 6038  CA  LYS C 253    13301  15737  11315   2439    -60    238       C  
ATOM   6039  C   LYS C 253     -26.657  18.518  47.352  1.00111.41           C  
ANISOU 6039  C   LYS C 253    14018  16341  11973   2390   -202     44       C  
ATOM   6040  O   LYS C 253     -26.888  18.696  48.551  1.00112.97           O  
ANISOU 6040  O   LYS C 253    14498  16528  11899   2587   -270    -38       O  
ATOM   6041  CB  LYS C 253     -26.313  16.011  47.844  1.00110.77           C  
ANISOU 6041  CB  LYS C 253    14166  16367  11555   2759   -110    282       C  
ATOM   6042  N   THR C 254     -26.500  19.531  46.473  1.00107.17           N  
ANISOU 6042  N   THR C 254    13257  15741  11721   2135   -221    -24       N  
ATOM   6043  CA  THR C 254     -26.547  20.959  46.810  1.00108.34           C  
ANISOU 6043  CA  THR C 254    13447  15787  11930   2042   -329   -209       C  
ATOM   6044  C   THR C 254     -27.914  21.595  46.489  1.00110.81           C  
ANISOU 6044  C   THR C 254    13880  15949  12275   1992    -89   -119       C  
ATOM   6045  O   THR C 254     -28.038  22.823  46.504  1.00111.16           O  
ANISOU 6045  O   THR C 254    13960  15866  12408   1899   -134   -241       O  
ATOM   6046  CB  THR C 254     -25.371  21.713  46.153  1.00117.64           C  
ANISOU 6046  CB  THR C 254    14338  16952  13407   1799   -491   -367       C  
ATOM   6047  OG1 THR C 254     -25.344  21.432  44.752  1.00115.04           O  
ANISOU 6047  OG1 THR C 254    13817  16594  13300   1619   -299   -199       O  
ATOM   6048  CG2 THR C 254     -24.026  21.377  46.788  1.00119.11           C  
ANISOU 6048  CG2 THR C 254    14376  17300  13581   1882   -806   -571       C  
ATOM   6049  N   TYR C 255     -28.941  20.752  46.233  1.00105.83           N  
ANISOU 6049  N   TYR C 255    13302  15324  11584   2067    161     69       N  
ATOM   6050  CA  TYR C 255     -30.315  21.167  45.915  1.00104.74           C  
ANISOU 6050  CA  TYR C 255    13214  15082  11503   2060    380    132       C  
ATOM   6051  C   TYR C 255     -31.005  21.929  47.053  1.00110.45           C  
ANISOU 6051  C   TYR C 255    14176  15730  12061   2201    410     12       C  
ATOM   6052  O   TYR C 255     -31.916  22.717  46.791  1.00109.86           O  
ANISOU 6052  O   TYR C 255    14112  15551  12080   2191    514     -7       O  
ATOM   6053  CB  TYR C 255     -31.172  19.968  45.454  1.00104.40           C  
ANISOU 6053  CB  TYR C 255    13117  15077  11473   2091    627    303       C  
ATOM   6054  CG  TYR C 255     -31.244  18.825  46.446  1.00107.17           C  
ANISOU 6054  CG  TYR C 255    13649  15483  11587   2257    742    361       C  
ATOM   6055  CD1 TYR C 255     -32.205  18.807  47.453  1.00110.63           C  
ANISOU 6055  CD1 TYR C 255    14310  15867  11855   2400    947    344       C  
ATOM   6056  CD2 TYR C 255     -30.380  17.737  46.350  1.00107.76           C  
ANISOU 6056  CD2 TYR C 255    13702  15640  11601   2289    683    440       C  
ATOM   6057  CE1 TYR C 255     -32.274  17.759  48.370  1.00112.86           C  
ANISOU 6057  CE1 TYR C 255    14840  16154  11887   2561   1108    420       C  
ATOM   6058  CE2 TYR C 255     -30.446  16.678  47.255  1.00110.00           C  
ANISOU 6058  CE2 TYR C 255    14229  15933  11635   2475    804    514       C  
ATOM   6059  CZ  TYR C 255     -31.398  16.692  48.262  1.00119.06           C  
ANISOU 6059  CZ  TYR C 255    15644  17001  12592   2605   1030    513       C  
ATOM   6060  OH  TYR C 255     -31.472  15.650  49.155  1.00121.86           O  
ANISOU 6060  OH  TYR C 255    16313  17319  12668   2795   1204    609       O  
ATOM   6061  N   ASN C 256     -30.567  21.694  48.308  1.00109.13           N  
ANISOU 6061  N   ASN C 256    14223  15614  11627   2365    309    -76       N  
ATOM   6062  CA  ASN C 256     -31.109  22.336  49.508  1.00111.22           C  
ANISOU 6062  CA  ASN C 256    14778  15812  11670   2533    338   -202       C  
ATOM   6063  C   ASN C 256     -30.758  23.832  49.608  1.00116.17           C  
ANISOU 6063  C   ASN C 256    15424  16330  12384   2450    129   -412       C  
ATOM   6064  O   ASN C 256     -31.388  24.545  50.387  1.00117.39           O  
ANISOU 6064  O   ASN C 256    15805  16395  12404   2570    184   -521       O  
ATOM   6065  CB  ASN C 256     -30.687  21.576  50.771  1.00114.87           C  
ANISOU 6065  CB  ASN C 256    15530  16352  11764   2771    277   -225       C  
ATOM   6066  CG  ASN C 256     -31.587  21.825  51.958  1.00143.07           C  
ANISOU 6066  CG  ASN C 256    19464  19846  15050   2982    470   -275       C  
ATOM   6067  OD1 ASN C 256     -32.749  21.403  51.994  1.00137.46           O  
ANISOU 6067  OD1 ASN C 256    18809  19083  14338   3020    848   -153       O  
ATOM   6068  ND2 ASN C 256     -31.067  22.518  52.960  1.00138.60           N  
ANISOU 6068  ND2 ASN C 256    19145  19268  14249   3121    225   -481       N  
ATOM   6069  N   ASN C 257     -29.770  24.307  48.822  1.00112.14           N  
ANISOU 6069  N   ASN C 257    14693  15805  12111   2238    -72   -475       N  
ATOM   6070  CA  ASN C 257     -29.375  25.716  48.802  1.00113.47           C  
ANISOU 6070  CA  ASN C 257    14878  15822  12416   2105   -229   -676       C  
ATOM   6071  C   ASN C 257     -29.459  26.280  47.381  1.00115.53           C  
ANISOU 6071  C   ASN C 257    14955  15950  12989   1880   -129   -577       C  
ATOM   6072  O   ASN C 257     -28.523  26.130  46.589  1.00114.57           O  
ANISOU 6072  O   ASN C 257    14622  15854  13058   1688   -196   -558       O  
ATOM   6073  CB  ASN C 257     -27.982  25.920  49.421  1.00116.90           C  
ANISOU 6073  CB  ASN C 257    15269  16320  12828   2059   -569   -919       C  
ATOM   6074  CG  ASN C 257     -27.668  27.355  49.785  1.00142.24           C  
ANISOU 6074  CG  ASN C 257    18568  19350  16128   1948   -727  -1190       C  
ATOM   6075  OD1 ASN C 257     -27.583  28.246  48.932  1.00136.05           O  
ANISOU 6075  OD1 ASN C 257    17689  18382  15621   1716   -660  -1203       O  
ATOM   6076  ND2 ASN C 257     -27.443  27.603  51.066  1.00137.24           N  
ANISOU 6076  ND2 ASN C 257    18155  18746  15245   2118   -941  -1423       N  
ATOM   6077  N   LEU C 258     -30.602  26.909  47.058  1.00111.58           N  
ANISOU 6077  N   LEU C 258    14558  15310  12528   1934     45   -515       N  
ATOM   6078  CA  LEU C 258     -30.852  27.527  45.752  1.00110.46           C  
ANISOU 6078  CA  LEU C 258    14345  15013  12612   1802    133   -413       C  
ATOM   6079  C   LEU C 258     -30.685  29.055  45.827  1.00116.83           C  
ANISOU 6079  C   LEU C 258    15325  15556  13509   1720     72   -574       C  
ATOM   6080  O   LEU C 258     -30.834  29.747  44.816  1.00116.33           O  
ANISOU 6080  O   LEU C 258    15297  15302  13600   1633    149   -497       O  
ATOM   6081  CB  LEU C 258     -32.249  27.145  45.211  1.00108.87           C  
ANISOU 6081  CB  LEU C 258    14121  14835  12411   1957    330   -250       C  
ATOM   6082  CG  LEU C 258     -32.542  25.652  44.987  1.00111.49           C  
ANISOU 6082  CG  LEU C 258    14284  15376  12702   2002    436    -99       C  
ATOM   6083  CD1 LEU C 258     -34.018  25.422  44.764  1.00111.15           C  
ANISOU 6083  CD1 LEU C 258    14199  15347  12684   2157    618    -37       C  
ATOM   6084  CD2 LEU C 258     -31.753  25.087  43.811  1.00112.31           C  
ANISOU 6084  CD2 LEU C 258    14206  15530  12938   1831    403     26       C  
ATOM   6085  N   ASP C 259     -30.345  29.565  47.028  1.00116.00           N  
ANISOU 6085  N   ASP C 259    15366  15420  13287   1759    -69   -803       N  
ATOM   6086  CA  ASP C 259     -30.124  30.984  47.313  1.00118.70           C  
ANISOU 6086  CA  ASP C 259    15899  15497  13704   1675   -142  -1009       C  
ATOM   6087  C   ASP C 259     -28.830  31.508  46.676  1.00123.93           C  
ANISOU 6087  C   ASP C 259    16433  16026  14631   1343   -225  -1104       C  
ATOM   6088  O   ASP C 259     -28.735  32.704  46.393  1.00125.46           O  
ANISOU 6088  O   ASP C 259    16778  15919  14970   1209   -184  -1195       O  
ATOM   6089  CB  ASP C 259     -30.105  31.231  48.835  1.00123.05           C  
ANISOU 6089  CB  ASP C 259    16649  16082  14021   1829   -291  -1255       C  
ATOM   6090  CG  ASP C 259     -31.355  30.805  49.594  1.00133.13           C  
ANISOU 6090  CG  ASP C 259    18093  17454  15036   2146   -139  -1189       C  
ATOM   6091  OD1 ASP C 259     -32.451  30.802  48.988  1.00132.29           O  
ANISOU 6091  OD1 ASP C 259    17968  17308  14989   2247     76  -1019       O  
ATOM   6092  OD2 ASP C 259     -31.242  30.517  50.805  1.00140.61           O  
ANISOU 6092  OD2 ASP C 259    19201  18506  15720   2303   -231  -1326       O  
ATOM   6093  N   VAL C 260     -27.836  30.617  46.466  1.00119.88           N  
ANISOU 6093  N   VAL C 260    15644  15715  14191   1213   -314  -1093       N  
ATOM   6094  CA  VAL C 260     -26.534  30.935  45.861  1.00121.27           C  
ANISOU 6094  CA  VAL C 260    15610  15807  14659    883   -353  -1200       C  
ATOM   6095  C   VAL C 260     -26.660  31.292  44.374  1.00124.23           C  
ANISOU 6095  C   VAL C 260    16000  15973  15228    717    -90   -978       C  
ATOM   6096  O   VAL C 260     -27.563  30.794  43.701  1.00121.12           O  
ANISOU 6096  O   VAL C 260    15659  15629  14730    879     51   -717       O  
ATOM   6097  CB  VAL C 260     -25.454  29.844  46.103  1.00125.12           C  
ANISOU 6097  CB  VAL C 260    15776  16592  15172    843   -530  -1273       C  
ATOM   6098  CG1 VAL C 260     -24.929  29.892  47.535  1.00127.70           C  
ANISOU 6098  CG1 VAL C 260    16120  17041  15358    949   -856  -1593       C  
ATOM   6099  CG2 VAL C 260     -25.958  28.445  45.744  1.00121.47           C  
ANISOU 6099  CG2 VAL C 260    15233  16375  14547   1037   -437   -991       C  
ATOM   6100  N   SER C 261     -25.744  32.146  43.873  1.00123.54           N  
ANISOU 6100  N   SER C 261    15877  15641  15420    397    -19  -1098       N  
ATOM   6101  CA  SER C 261     -25.697  32.623  42.486  1.00123.59           C  
ANISOU 6101  CA  SER C 261    15981  15384  15592    223    267   -902       C  
ATOM   6102  C   SER C 261     -25.472  31.510  41.451  1.00125.06           C  
ANISOU 6102  C   SER C 261    15962  15765  15792    210    392   -658       C  
ATOM   6103  O   SER C 261     -24.988  30.430  41.796  1.00123.27           O  
ANISOU 6103  O   SER C 261    15443  15854  15541    246    258   -692       O  
ATOM   6104  CB  SER C 261     -24.640  33.713  42.333  1.00131.26           C  
ANISOU 6104  CB  SER C 261    16949  16040  16882   -158    360  -1122       C  
ATOM   6105  OG  SER C 261     -23.342  33.225  42.631  1.00141.51           O  
ANISOU 6105  OG  SER C 261    17836  17533  18399   -385    237  -1346       O  
ATOM   6106  N   VAL C 262     -25.822  31.794  40.179  1.00121.55           N  
ANISOU 6106  N   VAL C 262    15712  15110  15360    188    642   -417       N  
ATOM   6107  CA  VAL C 262     -25.686  30.877  39.041  1.00119.57           C  
ANISOU 6107  CA  VAL C 262    15352  14984  15096    187    790   -181       C  
ATOM   6108  C   VAL C 262     -24.198  30.573  38.722  1.00125.57           C  
ANISOU 6108  C   VAL C 262    15793  15792  16124   -137    889   -284       C  
ATOM   6109  O   VAL C 262     -23.894  29.485  38.228  1.00123.30           O  
ANISOU 6109  O   VAL C 262    15292  15736  15821   -110    920   -171       O  
ATOM   6110  CB  VAL C 262     -26.499  31.377  37.809  1.00123.42           C  
ANISOU 6110  CB  VAL C 262    16210  15211  15474    302    998     78       C  
ATOM   6111  CG1 VAL C 262     -25.825  32.553  37.104  1.00126.88           C  
ANISOU 6111  CG1 VAL C 262    16895  15223  16092     29   1270     77       C  
ATOM   6112  CG2 VAL C 262     -26.797  30.248  36.829  1.00120.64           C  
ANISOU 6112  CG2 VAL C 262    15784  15058  14994    436   1054    311       C  
ATOM   6113  N   THR C 263     -23.286  31.524  39.038  1.00126.33           N  
ANISOU 6113  N   THR C 263    15838  15670  16491   -442    939   -528       N  
ATOM   6114  CA  THR C 263     -21.837  31.406  38.833  1.00128.94           C  
ANISOU 6114  CA  THR C 263    15804  16026  17162   -784   1041   -706       C  
ATOM   6115  C   THR C 263     -21.262  30.306  39.742  1.00132.37           C  
ANISOU 6115  C   THR C 263    15801  16892  17600   -687    717   -890       C  
ATOM   6116  O   THR C 263     -20.388  29.550  39.311  1.00132.18           O  
ANISOU 6116  O   THR C 263    15444  17043  17735   -790    782   -901       O  
ATOM   6117  CB  THR C 263     -21.151  32.774  39.031  1.00141.62           C  
ANISOU 6117  CB  THR C 263    17466  17262  19083  -1141   1168   -966       C  
ATOM   6118  OG1 THR C 263     -21.902  33.787  38.357  1.00141.78           O  
ANISOU 6118  OG1 THR C 263    18002  16862  19006  -1127   1426   -769       O  
ATOM   6119  CG2 THR C 263     -19.710  32.792  38.526  1.00143.73           C  
ANISOU 6119  CG2 THR C 263    17365  17476  19771  -1549   1400  -1132       C  
ATOM   6120  N   LYS C 264     -21.777  30.209  40.987  1.00128.51           N  
ANISOU 6120  N   LYS C 264    15355  16562  16911   -455    383  -1023       N  
ATOM   6121  CA  LYS C 264     -21.383  29.201  41.976  1.00127.93           C  
ANISOU 6121  CA  LYS C 264    14995  16867  16744   -276     49  -1178       C  
ATOM   6122  C   LYS C 264     -21.902  27.818  41.571  1.00128.40           C  
ANISOU 6122  C   LYS C 264    15032  17184  16568    -15     78   -886       C  
ATOM   6123  O   LYS C 264     -21.246  26.813  41.849  1.00127.74           O  
ANISOU 6123  O   LYS C 264    14666  17377  16492     65    -70   -946       O  
ATOM   6124  CB  LYS C 264     -21.902  29.576  43.374  1.00131.12           C  
ANISOU 6124  CB  LYS C 264    15576  17309  16937    -76   -254  -1371       C  
ATOM   6125  N   ALA C 265     -23.075  27.775  40.909  1.00122.77           N  
ANISOU 6125  N   ALA C 265    14616  16372  15660    126    257   -592       N  
ATOM   6126  CA  ALA C 265     -23.711  26.549  40.423  1.00119.46           C  
ANISOU 6126  CA  ALA C 265    14202  16147  15042    343    310   -331       C  
ATOM   6127  C   ALA C 265     -22.974  25.973  39.206  1.00123.78           C  
ANISOU 6127  C   ALA C 265    14568  16722  15742    196    518   -207       C  
ATOM   6128  O   ALA C 265     -23.052  24.768  38.963  1.00121.28           O  
ANISOU 6128  O   ALA C 265    14149  16614  15317    340    512    -75       O  
ATOM   6129  CB  ALA C 265     -25.166  26.820  40.073  1.00118.26           C  
ANISOU 6129  CB  ALA C 265    14375  15869  14690    523    406   -129       C  
ATOM   6130  N   LEU C 266     -22.264  26.835  38.449  1.00123.33           N  
ANISOU 6130  N   LEU C 266    14499  16427  15934    -95    738   -250       N  
ATOM   6131  CA  LEU C 266     -21.498  26.461  37.255  1.00123.96           C  
ANISOU 6131  CA  LEU C 266    14442  16483  16173   -264   1011   -146       C  
ATOM   6132  C   LEU C 266     -19.976  26.458  37.514  1.00131.64           C  
ANISOU 6132  C   LEU C 266    14981  17536  17500   -519   1005   -421       C  
ATOM   6133  O   LEU C 266     -19.187  26.394  36.567  1.00132.79           O  
ANISOU 6133  O   LEU C 266    14988  17610  17855   -726   1297   -390       O  
ATOM   6134  CB  LEU C 266     -21.852  27.392  36.074  1.00125.02           C  
ANISOU 6134  CB  LEU C 266    14939  16256  16308   -388   1345     39       C  
ATOM   6135  CG  LEU C 266     -23.286  27.326  35.540  1.00127.13           C  
ANISOU 6135  CG  LEU C 266    15596  16457  16252   -108   1343    297       C  
ATOM   6136  CD1 LEU C 266     -23.522  28.390  34.491  1.00129.47           C  
ANISOU 6136  CD1 LEU C 266    16309  16348  16534   -180   1558    390       C  
ATOM   6137  CD2 LEU C 266     -23.610  25.954  34.977  1.00127.30           C  
ANISOU 6137  CD2 LEU C 266    15605  16642  16123     35   1424    509       C  
ATOM   6138  N   GLN C 267     -19.572  26.496  38.801  1.00130.03           N  
ANISOU 6138  N   GLN C 267    14557  17491  17357   -482    669   -709       N  
ATOM   6139  CA  GLN C 267     -18.170  26.500  39.231  1.00133.75           C  
ANISOU 6139  CA  GLN C 267    14559  18082  18177   -676    556  -1049       C  
ATOM   6140  C   GLN C 267     -17.477  25.142  39.023  1.00137.53           C  
ANISOU 6140  C   GLN C 267    14687  18878  18688   -542    503  -1031       C  
ATOM   6141  O   GLN C 267     -16.245  25.088  38.992  1.00140.44           O  
ANISOU 6141  O   GLN C 267    14617  19337  19406   -719    505  -1282       O  
ATOM   6142  CB  GLN C 267     -18.066  26.943  40.699  1.00136.97           C  
ANISOU 6142  CB  GLN C 267    14904  18571  18569   -604    145  -1376       C  
ATOM   6143  CG  GLN C 267     -16.829  27.781  41.002  1.00157.83           C  
ANISOU 6143  CG  GLN C 267    17177  21131  21660   -946     94  -1796       C  
ATOM   6144  CD  GLN C 267     -16.757  28.202  42.450  1.00179.96           C  
ANISOU 6144  CD  GLN C 267    19954  24019  24403   -842   -360  -2144       C  
ATOM   6145  OE1 GLN C 267     -17.647  28.880  42.979  1.00174.70           O  
ANISOU 6145  OE1 GLN C 267    19677  23192  23508   -754   -432  -2113       O  
ATOM   6146  NE2 GLN C 267     -15.673  27.839  43.117  1.00175.89           N  
ANISOU 6146  NE2 GLN C 267    18979  23755  24095   -833   -686  -2510       N  
ATOM   6147  N   HIS C 268     -18.265  24.056  38.880  1.00130.61           N  
ANISOU 6147  N   HIS C 268    13990  18159  17475   -233    464   -757       N  
ATOM   6148  CA  HIS C 268     -17.769  22.691  38.683  1.00129.72           C  
ANISOU 6148  CA  HIS C 268    13637  18316  17335    -56    422   -702       C  
ATOM   6149  C   HIS C 268     -17.115  22.463  37.311  1.00134.83           C  
ANISOU 6149  C   HIS C 268    14132  18897  18200   -251    811   -597       C  
ATOM   6150  O   HIS C 268     -16.139  21.716  37.225  1.00135.96           O  
ANISOU 6150  O   HIS C 268    13901  19236  18522   -225    790   -714       O  
ATOM   6151  CB  HIS C 268     -18.886  21.663  38.939  1.00126.48           C  
ANISOU 6151  CB  HIS C 268    13512  18030  16516    294    312   -450       C  
ATOM   6152  CG  HIS C 268     -20.022  21.739  37.965  1.00126.93           C  
ANISOU 6152  CG  HIS C 268    13925  17910  16393    294    576   -143       C  
ATOM   6153  ND1 HIS C 268     -20.983  22.730  38.052  1.00128.03           N  
ANISOU 6153  ND1 HIS C 268    14377  17841  16429    260    606    -87       N  
ATOM   6154  CD2 HIS C 268     -20.305  20.947  36.905  1.00126.69           C  
ANISOU 6154  CD2 HIS C 268    13974  17889  16272    350    786     88       C  
ATOM   6155  CE1 HIS C 268     -21.817  22.508  37.049  1.00125.25           C  
ANISOU 6155  CE1 HIS C 268    14263  17395  15931    313    805    168       C  
ATOM   6156  NE2 HIS C 268     -21.452  21.445  36.334  1.00124.72           N  
ANISOU 6156  NE2 HIS C 268    14074  17453  15860    360    913    275       N  
ATOM   6157  N   ARG C 269     -17.654  23.097  36.249  1.00131.03           N  
ANISOU 6157  N   ARG C 269    13965  18138  17683   -410   1163   -380       N  
ATOM   6158  CA  ARG C 269     -17.158  22.962  34.874  1.00131.98           C  
ANISOU 6158  CA  ARG C 269    14066  18146  17934   -577   1587   -244       C  
ATOM   6159  C   ARG C 269     -15.992  23.909  34.536  1.00141.46           C  
ANISOU 6159  C   ARG C 269    15005  19162  19579   -975   1875   -464       C  
ATOM   6160  O   ARG C 269     -15.341  23.708  33.511  1.00142.68           O  
ANISOU 6160  O   ARG C 269    15059  19257  19894  -1123   2252   -403       O  
ATOM   6161  CB  ARG C 269     -18.308  23.100  33.852  1.00129.24           C  
ANISOU 6161  CB  ARG C 269    14237  17590  17281   -498   1812     96       C  
ATOM   6162  CG  ARG C 269     -19.070  24.424  33.909  1.00139.08           C  
ANISOU 6162  CG  ARG C 269    15848  18499  18496   -635   1918    138       C  
ATOM   6163  CD  ARG C 269     -20.113  24.519  32.816  1.00143.41           C  
ANISOU 6163  CD  ARG C 269    16839  18990  18661   -369   1824    384       C  
ATOM   6164  NE  ARG C 269     -20.822  25.800  32.823  1.00149.03           N  
ANISOU 6164  NE  ARG C 269    17865  19557  19203   -324   2113    640       N  
ATOM   6165  CZ  ARG C 269     -21.822  26.110  32.003  1.00162.92           C  
ANISOU 6165  CZ  ARG C 269    20052  20989  20861   -367   2328    783       C  
ATOM   6166  NH1 ARG C 269     -22.246  25.235  31.099  1.00151.13           N  
ANISOU 6166  NH1 ARG C 269    18715  19261  19448   -477   2313    698       N  
ATOM   6167  NH2 ARG C 269     -22.403  27.300  32.077  1.00149.31           N  
ANISOU 6167  NH2 ARG C 269    18644  19157  18929   -272   2550   1006       N  
ATOM   6168  N   SER C 270     -15.725  24.918  35.400  1.00141.24           N  
ANISOU 6168  N   SER C 270    14869  19036  19761  -1157   1719   -735       N  
ATOM   6169  CA  SER C 270     -14.675  25.940  35.251  1.00146.53           C  
ANISOU 6169  CA  SER C 270    15275  19493  20905  -1585   1975  -1006       C  
ATOM   6170  C   SER C 270     -13.303  25.410  34.807  1.00154.44           C  
ANISOU 6170  C   SER C 270    15721  20645  22314  -1757   2183  -1197       C  
ATOM   6171  O   SER C 270     -12.639  26.054  33.994  1.00157.67           O  
ANISOU 6171  O   SER C 270    16062  20797  23048  -2121   2667  -1240       O  
ATOM   6172  CB  SER C 270     -14.529  26.751  36.535  1.00152.32           C  
ANISOU 6172  CB  SER C 270    15862  20219  21791  -1671   1611  -1356       C  
ATOM   6173  OG  SER C 270     -14.056  25.949  37.605  1.00161.28           O  
ANISOU 6173  OG  SER C 270    16588  21745  22944  -1443   1126  -1612       O  
ATOM   6174  N   HIS C 271     -12.890  24.244  35.339  1.00150.69           N  
ANISOU 6174  N   HIS C 271    14870  20565  21820  -1484   1846  -1311       N  
ATOM   6175  CA  HIS C 271     -11.613  23.604  35.021  1.00154.01           C  
ANISOU 6175  CA  HIS C 271    14715  21186  22618  -1560   1972  -1517       C  
ATOM   6176  C   HIS C 271     -11.605  22.916  33.652  1.00157.22           C  
ANISOU 6176  C   HIS C 271    15273  21542  22923  -1532   2444  -1204       C  
ATOM   6177  O   HIS C 271     -10.566  22.913  32.988  1.00160.64           O  
ANISOU 6177  O   HIS C 271    15343  21951  23743  -1768   2823  -1338       O  
ATOM   6178  CB  HIS C 271     -11.220  22.608  36.122  1.00154.63           C  
ANISOU 6178  CB  HIS C 271    14404  21687  22660  -1204   1402  -1744       C  
ATOM   6179  N   TYR C 272     -12.747  22.325  33.237  1.00149.29           N  
ANISOU 6179  N   TYR C 272    14785  20524  21414  -1247   2425   -818       N  
ATOM   6180  CA  TYR C 272     -12.864  21.604  31.965  1.00147.93           C  
ANISOU 6180  CA  TYR C 272    14826  20312  21069  -1167   2805   -526       C  
ATOM   6181  C   TYR C 272     -14.002  22.149  31.079  1.00149.43           C  
ANISOU 6181  C   TYR C 272    15699  20182  20895  -1177   3065   -168       C  
ATOM   6182  O   TYR C 272     -15.048  21.509  30.928  1.00144.84           O  
ANISOU 6182  O   TYR C 272    15473  19663  19897   -882   2898     79       O  
ATOM   6183  CB  TYR C 272     -12.979  20.079  32.201  1.00146.39           C  
ANISOU 6183  CB  TYR C 272    14520  20454  20647   -765   2513   -456       C  
ATOM   6184  CG  TYR C 272     -11.901  19.512  33.102  1.00150.96           C  
ANISOU 6184  CG  TYR C 272    14477  21351  21530   -665   2199   -802       C  
ATOM   6185  CD1 TYR C 272     -10.649  19.171  32.597  1.00156.89           C  
ANISOU 6185  CD1 TYR C 272    14737  22203  22672   -774   2458   -989       C  
ATOM   6186  CD2 TYR C 272     -12.132  19.315  34.461  1.00150.80           C  
ANISOU 6186  CD2 TYR C 272    14372  21529  21394   -430   1641   -954       C  
ATOM   6187  CE1 TYR C 272      -9.650  18.659  33.424  1.00160.70           C  
ANISOU 6187  CE1 TYR C 272    14617  22995  23447   -635   2121  -1340       C  
ATOM   6188  CE2 TYR C 272     -11.140  18.804  35.298  1.00154.67           C  
ANISOU 6188  CE2 TYR C 272    14331  22314  22123   -277   1299  -1285       C  
ATOM   6189  CZ  TYR C 272      -9.901  18.475  34.774  1.00166.10           C  
ANISOU 6189  CZ  TYR C 272    15255  23876  23979   -370   1515  -1487       C  
ATOM   6190  OH  TYR C 272      -8.921  17.965  35.593  1.00170.42           O  
ANISOU 6190  OH  TYR C 272    15250  24732  24770   -170   1132  -1841       O  
ATOM   6191  N   PHE C 273     -13.787  23.351  30.507  1.00149.16           N  
ANISOU 6191  N   PHE C 273    15847  19791  21035  -1514   3471   -163       N  
ATOM   6192  CA  PHE C 273     -14.735  24.047  29.630  1.00148.03           C  
ANISOU 6192  CA  PHE C 273    16380  19298  20569  -1519   3737    151       C  
ATOM   6193  C   PHE C 273     -13.982  24.923  28.626  1.00156.58           C  
ANISOU 6193  C   PHE C 273    17584  20009  21899  -1890   4386    169       C  
ATOM   6194  O   PHE C 273     -13.161  25.752  29.028  1.00160.20           O  
ANISOU 6194  O   PHE C 273    17739  20332  22798  -2244   4537    -97       O  
ATOM   6195  CB  PHE C 273     -15.739  24.873  30.460  1.00148.06           C  
ANISOU 6195  CB  PHE C 273    16669  19186  20400  -1451   3397    157       C  
ATOM   6196  CG  PHE C 273     -16.849  25.561  29.698  1.00148.70           C  
ANISOU 6196  CG  PHE C 273    17441  18940  20119  -1361   3557    460       C  
ATOM   6197  CD1 PHE C 273     -17.012  26.939  29.770  1.00154.36           C  
ANISOU 6197  CD1 PHE C 273    18448  19285  20917  -1565   3710    440       C  
ATOM   6198  CD2 PHE C 273     -17.755  24.827  28.941  1.00147.82           C  
ANISOU 6198  CD2 PHE C 273    17694  18888  19584  -1045   3519    742       C  
ATOM   6199  CE1 PHE C 273     -18.051  27.573  29.083  1.00154.77           C  
ANISOU 6199  CE1 PHE C 273    19161  19034  20611  -1416   3819    717       C  
ATOM   6200  CE2 PHE C 273     -18.784  25.464  28.242  1.00150.30           C  
ANISOU 6200  CE2 PHE C 273    18629  18921  19558   -909   3605    988       C  
ATOM   6201  CZ  PHE C 273     -18.931  26.831  28.326  1.00150.93           C  
ANISOU 6201  CZ  PHE C 273    19005  18639  19701  -1073   3745    983       C  
ATOM   6202  N   GLU C 274     -14.251  24.721  27.321  1.00153.02           N  
ANISOU 6202  N   GLU C 274    17591  19384  21164  -1810   4782    469       N  
ATOM   6203  CA  GLU C 274     -13.593  25.441  26.226  1.00157.66           C  
ANISOU 6203  CA  GLU C 274    18416  19589  21899  -2117   5484    549       C  
ATOM   6204  C   GLU C 274     -14.389  26.663  25.716  1.00162.25           C  
ANISOU 6204  C   GLU C 274    19742  19695  22209  -2157   5703    786       C  
ATOM   6205  O   GLU C 274     -14.443  26.916  24.508  1.00164.04           O  
ANISOU 6205  O   GLU C 274    20505  19616  22208  -2159   6193   1038       O  
ATOM   6206  CB  GLU C 274     -13.244  24.470  25.082  1.00159.45           C  
ANISOU 6206  CB  GLU C 274    18719  19894  21969  -1991   5836    713       C  
ATOM   6207  N   GLY C 275     -14.970  27.419  26.648  1.00157.37           N  
ANISOU 6207  N   GLY C 275    19179  19009  21607  -2164   5345    695       N  
ATOM   6208  CA  GLY C 275     -15.736  28.627  26.351  1.00158.29           C  
ANISOU 6208  CA  GLY C 275    19966  18680  21497  -2169   5483    881       C  
ATOM   6209  C   GLY C 275     -17.128  28.398  25.795  1.00158.20           C  
ANISOU 6209  C   GLY C 275    20583  18650  20873  -1710   5248   1210       C  
ATOM   6210  O   GLY C 275     -17.462  27.289  25.366  1.00154.73           O  
ANISOU 6210  O   GLY C 275    20137  18490  20165  -1425   5092   1330       O  
ATOM   6211  N   VAL C 276     -17.953  29.461  25.809  1.00155.18           N  
ANISOU 6211  N   VAL C 276    20740  17934  20288  -1630   5207   1331       N  
ATOM   6212  CA  VAL C 276     -19.337  29.440  25.317  1.00152.37           C  
ANISOU 6212  CA  VAL C 276    20980  17530  19384  -1177   4949   1601       C  
ATOM   6213  C   VAL C 276     -19.409  29.549  23.795  1.00158.97           C  
ANISOU 6213  C   VAL C 276    22482  18058  19860  -1052   5398   1904       C  
ATOM   6214  O   VAL C 276     -18.650  30.312  23.191  1.00163.48           O  
ANISOU 6214  O   VAL C 276    23328  18222  20564  -1340   5990   1963       O  
ATOM   6215  CB  VAL C 276     -20.270  30.468  26.011  1.00155.80           C  
ANISOU 6215  CB  VAL C 276    21696  17771  19731  -1062   4658   1587       C  
ATOM   6216  CG1 VAL C 276     -19.645  31.856  26.013  1.00151.48           C  
ANISOU 6216  CG1 VAL C 276    20612  17628  19316   -977   4082   1355       C  
ATOM   6217  CG2 VAL C 276     -21.665  30.496  25.385  1.00160.76           C  
ANISOU 6217  CG2 VAL C 276    22554  17893  20633  -1434   5089   1527       C  
ATOM   6218  N   LEU C 277     -20.331  28.788  23.184  1.00152.78           N  
ANISOU 6218  N   LEU C 277    21976  17457  18615   -621   5123   2082       N  
ATOM   6219  CA  LEU C 277     -20.537  28.769  21.738  1.00155.17           C  
ANISOU 6219  CA  LEU C 277    22960  17519  18479   -401   5440   2359       C  
ATOM   6220  C   LEU C 277     -21.375  29.959  21.282  1.00162.24           C  
ANISOU 6220  C   LEU C 277    24647  17971  19027   -175   5475   2562       C  
ATOM   6221  O   LEU C 277     -22.528  30.104  21.698  1.00159.21           O  
ANISOU 6221  O   LEU C 277    24367  17685  18441    152   4963   2561       O  
ATOM   6222  CB  LEU C 277     -21.177  27.436  21.288  1.00151.53           C  
ANISOU 6222  CB  LEU C 277    22449  17444  17682    -26   5081   2413       C  
ATOM   6223  N   LYS C 278     -20.779  30.822  20.442  1.00164.94           N  
ANISOU 6223  N   LYS C 278    25549  17807  19312   -347   6109   2728       N  
ATOM   6224  CA  LYS C 278     -21.433  32.013  19.902  1.00168.70           C  
ANISOU 6224  CA  LYS C 278    26888  17775  19435   -127   6241   2952       C  
ATOM   6225  C   LYS C 278     -21.081  32.260  18.434  1.00178.62           C  
ANISOU 6225  C   LYS C 278    28945  18615  20308    -46   6853   3242       C  
ATOM   6226  O   LYS C 278     -19.904  32.231  18.064  1.00181.58           O  
ANISOU 6226  O   LYS C 278    29219  18833  20941   -445   7491   3236       O  
ATOM   6227  CB  LYS C 278     -21.186  33.264  20.776  1.00173.32           C  
ANISOU 6227  CB  LYS C 278    27432  18023  20398   -455   6379   2832       C  
ATOM   6228  CG  LYS C 278     -19.721  33.590  21.075  1.00189.98           C  
ANISOU 6228  CG  LYS C 278    29124  19961  23100  -1101   6966   2655       C  
ATOM   6229  CD  LYS C 278     -19.587  34.898  21.840  1.00202.18           C  
ANISOU 6229  CD  LYS C 278    30750  21103  24965  -1396   7097   2535       C  
ATOM   6230  N   CYS C 279     -22.112  32.478  17.598  1.00176.73           N  
ANISOU 6230  N   CYS C 279    29498  18207  19444    496   6652   3480       N  
ATOM   6231  CA  CYS C 279     -21.960  32.742  16.165  1.00182.08           C  
ANISOU 6231  CA  CYS C 279    31097  18469  19618    697   7163   3784       C  
ATOM   6232  C   CYS C 279     -22.412  34.165  15.805  1.00191.06           C  
ANISOU 6232  C   CYS C 279    33167  18975  20451    888   7376   4011       C  
ATOM   6233  O   CYS C 279     -22.964  34.869  16.655  1.00189.40           O  
ANISOU 6233  O   CYS C 279    32856  18703  20405    915   7047   3919       O  
ATOM   6234  CB  CYS C 279     -22.680  31.684  15.331  1.00180.53           C  
ANISOU 6234  CB  CYS C 279    31113  18601  18878   1221   6757   3863       C  
ATOM   6235  SG  CYS C 279     -24.487  31.763  15.420  1.00181.88           S  
ANISOU 6235  SG  CYS C 279    31569  18955  18582   1932   5830   3864       S  
ATOM   6236  N   TYR C 280     -22.170  34.587  14.552  1.00191.47           N  
ANISOU 6236  N   TYR C 280    33796  18790  20162    940   7644   4264       N  
ATOM   6237  CA  TYR C 280     -22.520  35.923  14.072  1.00192.34           C  
ANISOU 6237  CA  TYR C 280    34059  18796  20223    921   7267   4419       C  
ATOM   6238  C   TYR C 280     -23.702  35.935  13.097  1.00194.96           C  
ANISOU 6238  C   TYR C 280    34664  19395  20017   1481   6503   4564       C  
ATOM   6239  O   TYR C 280     -24.023  34.904  12.502  1.00194.08           O  
ANISOU 6239  O   TYR C 280    34750  19495  19496   1839   6390   4580       O  
ATOM   6240  CB  TYR C 280     -21.285  36.618  13.477  1.00194.53           C  
ANISOU 6240  CB  TYR C 280    33821  19171  20921    258   7446   4491       C  
ATOM   6241  CG  TYR C 280     -20.348  37.170  14.530  1.00196.20           C  
ANISOU 6241  CG  TYR C 280    33422  19290  21834   -360   7713   4291       C  
ATOM   6242  CD1 TYR C 280     -20.416  38.503  14.922  1.00198.56           C  
ANISOU 6242  CD1 TYR C 280    33570  19445  22427   -567   7432   4304       C  
ATOM   6243  CD2 TYR C 280     -19.399  36.357  15.144  1.00196.36           C  
ANISOU 6243  CD2 TYR C 280    32910  19429  22268   -737   8147   4058       C  
ATOM   6244  CE1 TYR C 280     -19.564  39.015  15.899  1.00199.76           C  
ANISOU 6244  CE1 TYR C 280    33177  19513  23207  -1111   7621   4093       C  
ATOM   6245  CE2 TYR C 280     -18.544  36.856  16.126  1.00197.71           C  
ANISOU 6245  CE2 TYR C 280    32473  19543  23103  -1297   8330   3826       C  
ATOM   6246  CZ  TYR C 280     -18.629  38.188  16.499  1.00203.83           C  
ANISOU 6246  CZ  TYR C 280    32865  20413  24168  -1505   7697   3827       C  
ATOM   6247  OH  TYR C 280     -17.786  38.689  17.461  1.00204.54           O  
ANISOU 6247  OH  TYR C 280    32313  20521  24883  -2022   7721   3588       O  
ATOM   6248  N   LEU C 281     -24.356  37.108  12.954  1.00193.22           N  
ANISOU 6248  N   LEU C 281    34797  18928  19690   1667   6236   4694       N  
ATOM   6249  CA  LEU C 281     -25.506  37.321  12.067  1.00193.04           C  
ANISOU 6249  CA  LEU C 281    35100  19043  19205   2201   5602   4825       C  
ATOM   6250  C   LEU C 281     -25.140  37.226  10.582  1.00196.19           C  
ANISOU 6250  C   LEU C 281    35217  19811  19515   2006   5398   4981       C  
ATOM   6251  O   LEU C 281     -25.998  36.876   9.768  1.00195.56           O  
ANISOU 6251  O   LEU C 281    35364  19931  19009   2448   4950   5031       O  
ATOM   6252  CB  LEU C 281     -26.181  38.671  12.365  1.00193.86           C  
ANISOU 6252  CB  LEU C 281    35262  18944  19450   2284   5252   4878       C  
ATOM   6253  CG  LEU C 281     -27.125  38.705  13.565  1.00196.34           C  
ANISOU 6253  CG  LEU C 281    35464  19285  19851   2587   4864   4670       C  
ATOM   6254  CD1 LEU C 281     -27.105  40.063  14.230  1.00197.47           C  
ANISOU 6254  CD1 LEU C 281    35497  19139  20394   2342   4859   4667       C  
ATOM   6255  CD2 LEU C 281     -28.548  38.338  13.162  1.00197.32           C  
ANISOU 6255  CD2 LEU C 281    35668  19718  19587   3232   4115   4633       C  
ATOM   6256  N   HIS C 282     -23.872  37.526  10.233  1.00194.67           N  
ANISOU 6256  N   HIS C 282    34916  19491  19557   1486   5958   5091       N  
ATOM   6257  CA  HIS C 282     -23.360  37.473   8.860  1.00195.33           C  
ANISOU 6257  CA  HIS C 282    34913  19811  19493   1318   5961   5273       C  
ATOM   6258  C   HIS C 282     -22.789  36.085   8.483  1.00197.16           C  
ANISOU 6258  C   HIS C 282    34906  20389  19616   1241   6138   5166       C  
ATOM   6259  O   HIS C 282     -21.933  35.985   7.599  1.00197.69           O  
ANISOU 6259  O   HIS C 282    34775  20636  19702    932   6345   5271       O  
ATOM   6260  CB  HIS C 282     -22.348  38.609   8.606  1.00197.49           C  
ANISOU 6260  CB  HIS C 282    34782  20040  20216    719   6134   5419       C  
ATOM   6261  CG  HIS C 282     -21.156  38.586   9.513  1.00200.02           C  
ANISOU 6261  CG  HIS C 282    34504  20379  21118    138   6516   5254       C  
ATOM   6262  ND1 HIS C 282     -21.118  39.339  10.673  1.00201.41           N  
ANISOU 6262  ND1 HIS C 282    34465  20332  21727    -64   6509   5131       N  
ATOM   6263  CD2 HIS C 282     -19.990  37.910   9.393  1.00201.37           C  
ANISOU 6263  CD2 HIS C 282    34221  20791  21500   -263   6864   5179       C  
ATOM   6264  CE1 HIS C 282     -19.938  39.096  11.220  1.00201.29           C  
ANISOU 6264  CE1 HIS C 282    34043  20314  22124   -550   6979   4996       C  
ATOM   6265  NE2 HIS C 282     -19.226  38.240  10.487  1.00201.52           N  
ANISOU 6265  NE2 HIS C 282    33880  20639  22052   -683   7189   5019       N  
ATOM   6266  N   GLU C 283     -23.291  35.019   9.139  1.00193.15           N  
ANISOU 6266  N   GLU C 283    34822  19748  18819   1686   6298   5015       N  
ATOM   6267  CA  GLU C 283     -22.880  33.634   8.900  1.00192.20           C  
ANISOU 6267  CA  GLU C 283    34690  19816  18521   1751   6566   4921       C  
ATOM   6268  C   GLU C 283     -23.984  32.843   8.200  1.00193.81           C  
ANISOU 6268  C   GLU C 283    35071  20351  18216   2305   5911   4879       C  
ATOM   6269  O   GLU C 283     -25.162  32.997   8.534  1.00192.96           O  
ANISOU 6269  O   GLU C 283    35246  20191  17881   2793   5434   4836       O  
ATOM   6270  CB  GLU C 283     -22.477  32.949  10.213  1.00192.19           C  
ANISOU 6270  CB  GLU C 283    34449  19721  18854   1624   6969   4710       C  
ATOM   6271  N   THR C 284     -23.595  31.996   7.228  1.00191.18           N  
ANISOU 6271  N   THR C 284    34931  20153  17557   2375   6109   4922       N  
ATOM   6272  CA  THR C 284     -24.506  31.155   6.441  1.00190.37           C  
ANISOU 6272  CA  THR C 284    35110  20303  16918   2903   5599   4871       C  
ATOM   6273  C   THR C 284     -25.119  30.034   7.286  1.00190.90           C  
ANISOU 6273  C   THR C 284    35141  20492  16900   3288   5372   4639       C  
ATOM   6274  O   THR C 284     -24.494  29.582   8.248  1.00190.02           O  
ANISOU 6274  O   THR C 284    34920  20229  17048   3141   5888   4564       O  
ATOM   6275  CB  THR C 284     -23.800  30.599   5.191  1.00196.85           C  
ANISOU 6275  CB  THR C 284    35328  21656  17810   2486   5480   4857       C  
ATOM   6276  OG1 THR C 284     -22.638  29.868   5.587  1.00196.31           O  
ANISOU 6276  OG1 THR C 284    35046  21568  17976   2175   6122   4782       O  
ATOM   6277  CG2 THR C 284     -23.425  31.687   4.189  1.00197.45           C  
ANISOU 6277  CG2 THR C 284    35365  21745  17911   2187   5491   5095       C  
ATOM   6278  N   LEU C 285     -26.339  29.586   6.911  1.00187.39           N  
ANISOU 6278  N   LEU C 285    35136  20139  15924   3962   4787   4573       N  
ATOM   6279  CA  LEU C 285     -27.101  28.522   7.581  1.00185.67           C  
ANISOU 6279  CA  LEU C 285    35054  20023  15469   4519   4482   4366       C  
ATOM   6280  C   LEU C 285     -26.331  27.195   7.649  1.00186.98           C  
ANISOU 6280  C   LEU C 285    34939  20379  15728   4352   4833   4252       C  
ATOM   6281  O   LEU C 285     -26.421  26.496   8.660  1.00183.98           O  
ANISOU 6281  O   LEU C 285    34249  20104  15551   4429   4815   4097       O  
ATOM   6282  CB  LEU C 285     -28.465  28.328   6.889  1.00185.75           C  
ANISOU 6282  CB  LEU C 285    35162  20325  15088   5046   3578   4239       C  
ATOM   6283  CG  LEU C 285     -29.526  27.533   7.656  1.00187.90           C  
ANISOU 6283  CG  LEU C 285    35173  20884  15338   5496   2933   3946       C  
ATOM   6284  CD1 LEU C 285     -30.413  28.451   8.483  1.00187.76           C  
ANISOU 6284  CD1 LEU C 285    35136  20764  15443   5740   2554   3913       C  
ATOM   6285  CD2 LEU C 285     -30.380  26.720   6.705  1.00189.87           C  
ANISOU 6285  CD2 LEU C 285    35233  21565  15345   5741   2211   3735       C  
ATOM   6286  N   GLU C 286     -25.566  26.865   6.584  1.00184.80           N  
ANISOU 6286  N   GLU C 286    34783  20137  15295   4148   5177   4340       N  
ATOM   6287  CA  GLU C 286     -24.745  25.653   6.487  1.00184.11           C  
ANISOU 6287  CA  GLU C 286    34582  20146  15225   4044   5630   4267       C  
ATOM   6288  C   GLU C 286     -23.627  25.638   7.537  1.00186.35           C  
ANISOU 6288  C   GLU C 286    34378  20300  16125   3526   6335   4264       C  
ATOM   6289  O   GLU C 286     -23.314  24.575   8.076  1.00183.00           O  
ANISOU 6289  O   GLU C 286    33435  20125  15971   3427   6383   4095       O  
ATOM   6290  CB  GLU C 286     -24.158  25.510   5.075  1.00186.03           C  
ANISOU 6290  CB  GLU C 286    34664  20643  15376   3716   5653   4312       C  
ATOM   6291  N   THR C 287     -23.044  26.818   7.834  1.00184.14           N  
ANISOU 6291  N   THR C 287    34122  19694  16147   3142   6794   4415       N  
ATOM   6292  CA  THR C 287     -21.981  26.999   8.828  1.00184.08           C  
ANISOU 6292  CA  THR C 287    33808  19420  16714   2677   7589   4413       C  
ATOM   6293  C   THR C 287     -22.557  26.875  10.252  1.00180.49           C  
ANISOU 6293  C   THR C 287    32413  19363  16803   2530   6901   4156       C  
ATOM   6294  O   THR C 287     -21.897  26.309  11.127  1.00176.14           O  
ANISOU 6294  O   THR C 287    30945  19113  16867   2091   6954   3958       O  
ATOM   6295  CB  THR C 287     -21.237  28.330   8.585  1.00189.48           C  
ANISOU 6295  CB  THR C 287    33705  20321  17967   1875   7413   4436       C  
ATOM   6296  OG1 THR C 287     -20.937  28.458   7.193  1.00190.39           O  
ANISOU 6296  OG1 THR C 287    33847  20653  17841   1758   7294   4548       O  
ATOM   6297  CG2 THR C 287     -19.946  28.444   9.392  1.00189.53           C  
ANISOU 6297  CG2 THR C 287    33244  20158  18610   1306   8174   4367       C  
ATOM   6298  N   ILE C 288     -23.788  27.395  10.468  1.00175.77           N  
ANISOU 6298  N   ILE C 288    32064  18763  15958   2931   6260   4155       N  
ATOM   6299  CA  ILE C 288     -24.513  27.358  11.747  1.00169.78           C  
ANISOU 6299  CA  ILE C 288    30541  18344  15624   2874   5601   3928       C  
ATOM   6300  C   ILE C 288     -24.848  25.904  12.133  1.00167.47           C  
ANISOU 6300  C   ILE C 288    29481  18646  15505   2906   5059   3661       C  
ATOM   6301  O   ILE C 288     -24.606  25.509  13.276  1.00162.33           O  
ANISOU 6301  O   ILE C 288    27960  18295  15423   2556   4917   3469       O  
ATOM   6302  CB  ILE C 288     -25.761  28.300  11.723  1.00174.48           C  
ANISOU 6302  CB  ILE C 288    31676  18753  15864   3355   5107   3998       C  
ATOM   6303  N   ILE C 289     -25.370  25.113  11.168  1.00164.47           N  
ANISOU 6303  N   ILE C 289    29464  18405  14621   3327   4780   3646       N  
ATOM   6304  CA  ILE C 289     -25.724  23.696  11.338  1.00159.75           C  
ANISOU 6304  CA  ILE C 289    28272  18305  14120   3387   4305   3398       C  
ATOM   6305  C   ILE C 289     -24.463  22.857  11.633  1.00161.11           C  
ANISOU 6305  C   ILE C 289    27852  18638  14724   2914   4780   3333       C  
ATOM   6306  O   ILE C 289     -24.497  22.000  12.520  1.00155.73           O  
ANISOU 6306  O   ILE C 289    26367  18341  14462   2727   4479   3118       O  
ATOM   6307  CB  ILE C 289     -26.565  23.179  10.126  1.00165.58           C  
ANISOU 6307  CB  ILE C 289    29643  19089  14181   3967   3910   3380       C  
ATOM   6308  CG1 ILE C 289     -27.972  23.829  10.120  1.00166.96           C  
ANISOU 6308  CG1 ILE C 289    30124  19246  14067   4455   3238   3334       C  
ATOM   6309  CG2 ILE C 289     -26.676  21.642  10.096  1.00163.01           C  
ANISOU 6309  CG2 ILE C 289    28797  19196  13944   3965   3595   3133       C  
ATOM   6310  CD1 ILE C 289     -28.665  23.912   8.748  1.00179.09           C  
ANISOU 6310  CD1 ILE C 289    32603  20627  14815   5095   2977   3401       C  
ATOM   6311  N   ASN C 290     -23.348  23.148  10.925  1.00161.54           N  
ANISOU 6311  N   ASN C 290    28307  18380  14691   2727   5545   3517       N  
ATOM   6312  CA  ASN C 290     -22.053  22.477  11.095  1.00160.56           C  
ANISOU 6312  CA  ASN C 290    27661  18364  14980   2300   6076   3456       C  
ATOM   6313  C   ASN C 290     -21.427  22.765  12.468  1.00161.05           C  
ANISOU 6313  C   ASN C 290    26875  18538  15778   1801   6167   3329       C  
ATOM   6314  O   ASN C 290     -20.699  21.921  12.994  1.00158.04           O  
ANISOU 6314  O   ASN C 290    25788  18439  15819   1530   6248   3168       O  
ATOM   6315  CB  ASN C 290     -21.089  22.871   9.979  1.00167.28           C  
ANISOU 6315  CB  ASN C 290    29188  18810  15561   2232   6919   3679       C  
ATOM   6316  N   ARG C 291     -21.716  23.951  13.040  1.00158.00           N  
ANISOU 6316  N   ARG C 291    26585  17926  15524   1713   6127   3388       N  
ATOM   6317  CA  ARG C 291     -21.224  24.391  14.347  1.00155.39           C  
ANISOU 6317  CA  ARG C 291    25543  17660  15837   1277   6160   3253       C  
ATOM   6318  C   ARG C 291     -21.904  23.618  15.488  1.00152.83           C  
ANISOU 6318  C   ARG C 291    24474  17811  15782   1320   5446   3017       C  
ATOM   6319  O   ARG C 291     -21.227  23.232  16.441  1.00149.78           O  
ANISOU 6319  O   ARG C 291    23346  17652  15909    989   5469   2847       O  
ATOM   6320  CB  ARG C 291     -21.436  25.909  14.515  1.00158.69           C  
ANISOU 6320  CB  ARG C 291    26408  17647  16239   1222   6321   3388       C  
ATOM   6321  N   LEU C 292     -23.234  23.398  15.384  1.00147.42           N  
ANISOU 6321  N   LEU C 292    23996  17266  14752   1739   4827   2996       N  
ATOM   6322  CA  LEU C 292     -24.048  22.695  16.383  1.00141.97           C  
ANISOU 6322  CA  LEU C 292    22690  16981  14271   1810   4182   2785       C  
ATOM   6323  C   LEU C 292     -23.718  21.206  16.519  1.00142.86           C  
ANISOU 6323  C   LEU C 292    22279  17464  14536   1747   4081   2632       C  
ATOM   6324  O   LEU C 292     -23.696  20.698  17.642  1.00138.51           O  
ANISOU 6324  O   LEU C 292    21063  17192  14373   1580   3838   2468       O  
ATOM   6325  CB  LEU C 292     -25.549  22.893  16.112  1.00141.84           C  
ANISOU 6325  CB  LEU C 292    23037  16987  13868   2273   3604   2778       C  
ATOM   6326  N   VAL C 293     -23.474  20.509  15.388  1.00141.55           N  
ANISOU 6326  N   VAL C 293    22459  17281  14042   1906   4269   2688       N  
ATOM   6327  CA  VAL C 293     -23.141  19.077  15.378  1.00139.19           C  
ANISOU 6327  CA  VAL C 293    21754  17286  13846   1879   4211   2550       C  
ATOM   6328  C   VAL C 293     -21.737  18.812  15.944  1.00142.80           C  
ANISOU 6328  C   VAL C 293    21662  17810  14786   1480   4659   2501       C  
ATOM   6329  O   VAL C 293     -21.535  17.797  16.612  1.00139.19           O  
ANISOU 6329  O   VAL C 293    20629  17651  14604   1401   4475   2344       O  
ATOM   6330  CB  VAL C 293     -23.357  18.372  14.008  1.00145.56           C  
ANISOU 6330  CB  VAL C 293    23105  18062  14140   2197   4236   2589       C  
ATOM   6331  CG1 VAL C 293     -24.839  18.157  13.724  1.00144.63           C  
ANISOU 6331  CG1 VAL C 293    23240  18047  13668   2600   3587   2501       C  
ATOM   6332  CG2 VAL C 293     -22.677  19.116  12.859  1.00150.87           C  
ANISOU 6332  CG2 VAL C 293    24491  18354  14477   2226   4846   2813       C  
ATOM   6333  N   GLU C 294     -20.782  19.729  15.683  1.00143.14           N  
ANISOU 6333  N   GLU C 294    21882  17563  14943   1238   5245   2619       N  
ATOM   6334  CA  GLU C 294     -19.399  19.637  16.158  1.00143.83           C  
ANISOU 6334  CA  GLU C 294    21428  17689  15530    849   5698   2535       C  
ATOM   6335  C   GLU C 294     -19.300  19.904  17.663  1.00144.69           C  
ANISOU 6335  C   GLU C 294    20858  17973  16145    607   5418   2371       C  
ATOM   6336  O   GLU C 294     -18.514  19.246  18.347  1.00142.95           O  
ANISOU 6336  O   GLU C 294    20002  17990  16321    426   5440   2208       O  
ATOM   6337  CB  GLU C 294     -18.495  20.604  15.379  1.00150.82           C  
ANISOU 6337  CB  GLU C 294    22731  18173  16402    644   6441   2689       C  
ATOM   6338  N   ALA C 295     -20.098  20.865  18.171  1.00140.49           N  
ANISOU 6338  N   ALA C 295    20487  17319  15575    639   5141   2405       N  
ATOM   6339  CA  ALA C 295     -20.137  21.249  19.584  1.00137.74           C  
ANISOU 6339  CA  ALA C 295    19605  17099  15631    448   4856   2254       C  
ATOM   6340  C   ALA C 295     -21.049  20.347  20.422  1.00136.64           C  
ANISOU 6340  C   ALA C 295    19111  17317  15489    645   4230   2129       C  
ATOM   6341  O   ALA C 295     -20.891  20.300  21.643  1.00133.94           O  
ANISOU 6341  O   ALA C 295    18252  17153  15487    500   4015   1979       O  
ATOM   6342  CB  ALA C 295     -20.569  22.699  19.718  1.00140.30           C  
ANISOU 6342  CB  ALA C 295    20304  17097  15905    404   4891   2344       C  
ATOM   6343  N   GLU C 296     -22.009  19.648  19.764  1.00132.03           N  
ANISOU 6343  N   GLU C 296    18825  16819  14520    974   3949   2176       N  
ATOM   6344  CA  GLU C 296     -22.990  18.718  20.355  1.00127.92           C  
ANISOU 6344  CA  GLU C 296    18039  16594  13972   1163   3414   2057       C  
ATOM   6345  C   GLU C 296     -23.981  19.408  21.329  1.00129.83           C  
ANISOU 6345  C   GLU C 296    18188  16856  14285   1212   3022   2005       C  
ATOM   6346  O   GLU C 296     -24.614  18.734  22.147  1.00126.21           O  
ANISOU 6346  O   GLU C 296    17390  16637  13928   1276   2657   1884       O  
ATOM   6347  CB  GLU C 296     -22.300  17.495  21.008  1.00127.10           C  
ANISOU 6347  CB  GLU C 296    17362  16774  14157   1049   3395   1921       C  
ATOM   6348  CG  GLU C 296     -21.511  16.634  20.032  1.00139.11           C  
ANISOU 6348  CG  GLU C 296    18966  18307  15583   1071   3722   1947       C  
ATOM   6349  CD  GLU C 296     -20.197  16.096  20.567  1.00158.00           C  
ANISOU 6349  CD  GLU C 296    20833  20840  18360    860   3965   1846       C  
ATOM   6350  OE1 GLU C 296     -19.283  16.909  20.836  1.00153.26           O  
ANISOU 6350  OE1 GLU C 296    20061  20133  18038    609   4271   1831       O  
ATOM   6351  OE2 GLU C 296     -20.067  14.856  20.677  1.00149.53           O  
ANISOU 6351  OE2 GLU C 296    19524  19971  17319    955   3856   1766       O  
ATOM   6352  N   VAL C 297     -24.142  20.742  21.201  1.00128.68           N  
ANISOU 6352  N   VAL C 297    18388  16433  14071   1195   3130   2102       N  
ATOM   6353  CA  VAL C 297     -25.043  21.556  22.023  1.00127.38           C  
ANISOU 6353  CA  VAL C 297    18207  16236  13954   1262   2814   2061       C  
ATOM   6354  C   VAL C 297     -26.412  21.730  21.353  1.00132.06           C  
ANISOU 6354  C   VAL C 297    19234  16778  14165   1648   2485   2106       C  
ATOM   6355  O   VAL C 297     -26.510  21.630  20.128  1.00134.07           O  
ANISOU 6355  O   VAL C 297    19959  16910  14074   1844   2582   2211       O  
ATOM   6356  CB  VAL C 297     -24.402  22.917  22.369  1.00133.61           C  
ANISOU 6356  CB  VAL C 297    19099  16737  14931   1020   3109   2107       C  
ATOM   6357  N   HIS C 298     -27.463  21.989  22.157  1.00127.00           N  
ANISOU 6357  N   HIS C 298    18432  16237  13586   1777   2092   2007       N  
ATOM   6358  CA  HIS C 298     -28.834  22.170  21.668  1.00127.69           C  
ANISOU 6358  CA  HIS C 298    18813  16319  13385   2160   1717   1988       C  
ATOM   6359  C   HIS C 298     -29.102  23.605  21.200  1.00135.09           C  
ANISOU 6359  C   HIS C 298    20317  16907  14105   2327   1788   2127       C  
ATOM   6360  O   HIS C 298     -29.461  23.805  20.040  1.00137.56           O  
ANISOU 6360  O   HIS C 298    21173  17064  14028   2622   1762   2227       O  
ATOM   6361  CB  HIS C 298     -29.857  21.724  22.727  1.00125.45           C  
ANISOU 6361  CB  HIS C 298    18061  16304  13298   2225   1308   1797       C  
ATOM   6362  CG  HIS C 298     -31.231  21.478  22.185  1.00129.60           C  
ANISOU 6362  CG  HIS C 298    18707  16925  13609   2595    897   1695       C  
ATOM   6363  ND1 HIS C 298     -32.137  22.510  22.019  1.00133.49           N  
ANISOU 6363  ND1 HIS C 298    19496  17275  13949   2884    678   1700       N  
ATOM   6364  CD2 HIS C 298     -31.818  20.317  21.814  1.00130.56           C  
ANISOU 6364  CD2 HIS C 298    18656  17269  13681   2715    658   1555       C  
ATOM   6365  CE1 HIS C 298     -33.236  21.949  21.541  1.00133.49           C  
ANISOU 6365  CE1 HIS C 298    19460  17441  13820   3181    293   1547       C  
ATOM   6366  NE2 HIS C 298     -33.091  20.631  21.402  1.00132.15           N  
ANISOU 6366  NE2 HIS C 298    19008  17486  13716   3071    273   1447       N  
ATOM   6367  N   ARG C 299     -28.925  24.595  22.096  1.00131.82           N  
ANISOU 6367  N   ARG C 299    19821  16350  13916   2161   1874   2129       N  
ATOM   6368  CA  ARG C 299     -29.150  26.008  21.785  1.00135.13           C  
ANISOU 6368  CA  ARG C 299    20785  16393  14165   2299   1968   2258       C  
ATOM   6369  C   ARG C 299     -27.849  26.733  21.453  1.00141.97           C  
ANISOU 6369  C   ARG C 299    21938  16911  15092   1987   2541   2413       C  
ATOM   6370  O   ARG C 299     -26.840  26.538  22.134  1.00140.23           O  
ANISOU 6370  O   ARG C 299    21291  16760  15232   1588   2784   2342       O  
ATOM   6371  CB  ARG C 299     -29.887  26.709  22.934  1.00134.26           C  
ANISOU 6371  CB  ARG C 299    20457  16303  14252   2341   1704   2141       C  
ATOM   6372  N   LEU C 300     -27.880  27.571  20.402  1.00143.04           N  
ANISOU 6372  N   LEU C 300    22808  16663  14879   2180   2760   2612       N  
ATOM   6373  CA  LEU C 300     -26.730  28.346  19.938  1.00146.77           C  
ANISOU 6373  CA  LEU C 300    23659  16727  15381   1894   3382   2777       C  
ATOM   6374  C   LEU C 300     -26.984  29.852  20.081  1.00154.54           C  
ANISOU 6374  C   LEU C 300    25133  17270  16317   1949   3496   2877       C  
ATOM   6375  O   LEU C 300     -27.941  30.383  19.513  1.00156.30           O  
ANISOU 6375  O   LEU C 300    25923  17317  16146   2398   3271   2983       O  
ATOM   6376  CB  LEU C 300     -26.376  27.962  18.485  1.00149.89           C  
ANISOU 6376  CB  LEU C 300    24592  16985  15375   2043   3681   2958       C  
ATOM   6377  CG  LEU C 300     -25.027  28.434  17.926  1.00158.54           C  
ANISOU 6377  CG  LEU C 300    25990  17707  16542   1689   4433   3112       C  
ATOM   6378  CD1 LEU C 300     -23.859  27.706  18.581  1.00156.41           C  
ANISOU 6378  CD1 LEU C 300    24965  17681  16784   1197   4689   2953       C  
ATOM   6379  CD2 LEU C 300     -24.963  28.207  16.434  1.00164.69           C  
ANISOU 6379  CD2 LEU C 300    27475  18303  16796   1964   4686   3316       C  
ATOM   6380  N   VAL C 301     -26.124  30.523  20.864  1.00152.26           N  
ANISOU 6380  N   VAL C 301    24612  16803  16439   1505   3822   2816       N  
ATOM   6381  CA  VAL C 301     -26.180  31.961  21.155  1.00155.60           C  
ANISOU 6381  CA  VAL C 301    25434  16774  16914   1450   3997   2874       C  
ATOM   6382  C   VAL C 301     -25.679  32.761  19.940  1.00166.65           C  
ANISOU 6382  C   VAL C 301    27684  17617  18019   1462   4574   3146       C  
ATOM   6383  O   VAL C 301     -24.675  32.386  19.335  1.00167.95           O  
ANISOU 6383  O   VAL C 301    27866  17712  18234   1191   5057   3214       O  
ATOM   6384  CB  VAL C 301     -25.379  32.291  22.454  1.00158.12           C  
ANISOU 6384  CB  VAL C 301    25151  17121  17807    936   4126   2658       C  
ATOM   6385  CG1 VAL C 301     -25.312  33.794  22.722  1.00161.62           C  
ANISOU 6385  CG1 VAL C 301    26014  17059  18335    835   4340   2689       C  
ATOM   6386  CG2 VAL C 301     -25.958  31.562  23.664  1.00152.49           C  
ANISOU 6386  CG2 VAL C 301    23705  16925  17309    975   3579   2416       C  
ATOM   6387  N   VAL C 302     -26.332  33.877  19.631  1.00167.75           N  
ANISOU 6387  N   VAL C 302    28551  17344  17841   1797   4544   3302       N  
ATOM   6388  CA  VAL C 302     -25.867  34.751  18.555  1.00174.41           C  
ANISOU 6388  CA  VAL C 302    30335  17580  18352   1858   5109   3589       C  
ATOM   6389  C   VAL C 302     -25.547  36.164  19.047  1.00182.46           C  
ANISOU 6389  C   VAL C 302    31566  18076  19684   1485   5553   3597       C  
ATOM   6390  O   VAL C 302     -26.314  36.745  19.806  1.00180.19           O  
ANISOU 6390  O   VAL C 302    30996  17830  19636   1471   5232   3433       O  
ATOM   6391  CB  VAL C 302     -26.852  34.784  17.365  1.00181.37           C  
ANISOU 6391  CB  VAL C 302    32065  18307  18538   2573   4819   3803       C  
ATOM   6392  CG1 VAL C 302     -26.389  35.795  16.331  1.00179.33           C  
ANISOU 6392  CG1 VAL C 302    31713  18462  17962   2854   4550   3800       C  
ATOM   6393  CG2 VAL C 302     -27.023  33.409  16.732  1.00180.13           C  
ANISOU 6393  CG2 VAL C 302    31933  18208  18300   3006   4202   3713       C  
ATOM   6394  N   VAL C 303     -24.409  36.699  18.616  1.00185.18           N  
ANISOU 6394  N   VAL C 303    32403  17915  20041   1167   6320   3770       N  
ATOM   6395  CA  VAL C 303     -24.015  38.062  18.959  1.00189.85           C  
ANISOU 6395  CA  VAL C 303    33228  17939  20967    737   6856   3768       C  
ATOM   6396  C   VAL C 303     -23.463  38.794  17.737  1.00197.11           C  
ANISOU 6396  C   VAL C 303    34311  18765  21815    585   6837   4017       C  
ATOM   6397  O   VAL C 303     -22.971  38.166  16.801  1.00196.99           O  
ANISOU 6397  O   VAL C 303    34429  18945  21475    746   6789   4187       O  
ATOM   6398  CB  VAL C 303     -22.967  38.078  20.083  1.00192.23           C  
ANISOU 6398  CB  VAL C 303    32589  18444  22007      8   7114   3463       C  
ATOM   6399  CG1 VAL C 303     -21.825  37.133  19.752  1.00195.41           C  
ANISOU 6399  CG1 VAL C 303    32975  18717  22555   -401   7845   3530       C  
ATOM   6400  CG2 VAL C 303     -22.454  39.491  20.315  1.00194.06           C  
ANISOU 6400  CG2 VAL C 303    32728  18327  22678   -360   7244   3290       C  
ATOM   6401  N   ASP C 304     -23.553  40.122  17.741  1.00196.24           N  
ANISOU 6401  N   ASP C 304    34172  18378  22012    289   6839   4037       N  
ATOM   6402  CA  ASP C 304     -23.105  40.911  16.595  1.00197.56           C  
ANISOU 6402  CA  ASP C 304    34232  18590  22242     83   6646   4271       C  
ATOM   6403  C   ASP C 304     -22.017  41.940  16.912  1.00201.44           C  
ANISOU 6403  C   ASP C 304    33994  19112  23433   -598   6578   4170       C  
ATOM   6404  O   ASP C 304     -22.125  42.703  17.871  1.00201.30           O  
ANISOU 6404  O   ASP C 304    33964  18854  23668   -659   6522   4009       O  
ATOM   6405  CB  ASP C 304     -24.298  41.604  15.931  1.00199.01           C  
ANISOU 6405  CB  ASP C 304    34722  18819  22075    601   5998   4457       C  
ATOM   6406  N   GLU C 305     -20.962  41.937  16.101  1.00200.08           N  
ANISOU 6406  N   GLU C 305    33605  18981  23436  -1022   6873   4295       N  
ATOM   6407  CA  GLU C 305     -19.936  42.977  16.131  1.00201.67           C  
ANISOU 6407  CA  GLU C 305    33284  19132  24210  -1635   6952   4254       C  
ATOM   6408  C   GLU C 305     -19.090  42.887  17.389  1.00204.74           C  
ANISOU 6408  C   GLU C 305    33031  19627  25135  -2040   7036   3875       C  
ATOM   6409  O   GLU C 305     -17.873  42.721  17.336  1.00204.53           O  
ANISOU 6409  O   GLU C 305    32574  19790  25350  -2402   7366   3757       O  
ATOM   6410  CB  GLU C 305     -20.573  44.363  16.027  1.00203.93           C  
ANISOU 6410  CB  GLU C 305    33613  19255  24616  -1615   6497   4422       C  
ATOM   6411  N   ASN C 306     -19.764  43.002  18.524  1.00202.47           N  
ANISOU 6411  N   ASN C 306    33008  18957  24962  -1955   7093   3675       N  
ATOM   6412  CA  ASN C 306     -19.150  42.847  19.827  1.00202.44           C  
ANISOU 6412  CA  ASN C 306    32599  18894  25426  -2307   7319   3276       C  
ATOM   6413  C   ASN C 306     -20.105  41.986  20.615  1.00203.05           C  
ANISOU 6413  C   ASN C 306    32870  19042  25238  -1880   7236   3107       C  
ATOM   6414  O   ASN C 306     -21.289  41.932  20.284  1.00201.69           O  
ANISOU 6414  O   ASN C 306    33282  18840  24511  -1300   7063   3315       O  
ATOM   6415  CB  ASN C 306     -18.969  44.199  20.510  1.00205.69           C  
ANISOU 6415  CB  ASN C 306    32766  19109  26276  -2600   7028   3163       C  
ATOM   6416  CG  ASN C 306     -18.220  44.091  21.823  1.00223.81           C  
ANISOU 6416  CG  ASN C 306    33513  22295  29229  -3009   5964   2838       C  
ATOM   6417  OD1 ASN C 306     -17.719  43.024  22.178  1.00219.63           O  
ANISOU 6417  OD1 ASN C 306    32903  21737  28811  -3193   6564   2576       O  
ATOM   6418  ND2 ASN C 306     -18.139  45.197  22.551  1.00219.98           N  
ANISOU 6418  ND2 ASN C 306    33166  21329  29089  -3302   6122   2732       N  
ATOM   6419  N   ASP C 307     -19.616  41.304  21.644  1.00200.16           N  
ANISOU 6419  N   ASP C 307    32292  18534  25225  -2162   7678   2722       N  
ATOM   6420  CA  ASP C 307     -20.494  40.403  22.367  1.00198.32           C  
ANISOU 6420  CA  ASP C 307    32321  18260  24772  -1807   7787   2552       C  
ATOM   6421  C   ASP C 307     -21.624  41.249  22.917  1.00200.79           C  
ANISOU 6421  C   ASP C 307    33104  18415  24774  -1334   7308   2613       C  
ATOM   6422  O   ASP C 307     -21.397  42.288  23.534  1.00200.44           O  
ANISOU 6422  O   ASP C 307    32842  18258  25058  -1541   7158   2360       O  
ATOM   6423  CB  ASP C 307     -19.742  39.713  23.503  1.00197.12           C  
ANISOU 6423  CB  ASP C 307    31047  18609  25239  -2261   7537   2110       C  
ATOM   6424  N   VAL C 308     -22.848  40.800  22.678  1.00196.78           N  
ANISOU 6424  N   VAL C 308    33280  17866  23621   -681   7095   2941       N  
ATOM   6425  CA  VAL C 308     -24.028  41.544  23.074  1.00196.26           C  
ANISOU 6425  CA  VAL C 308    33741  17656  23174   -103   6644   3044       C  
ATOM   6426  C   VAL C 308     -25.222  40.615  23.113  1.00193.38           C  
ANISOU 6426  C   VAL C 308    33137  17927  22412    506   5931   3090       C  
ATOM   6427  O   VAL C 308     -25.190  39.534  22.530  1.00191.27           O  
ANISOU 6427  O   VAL C 308    32792  17941  21939    605   5958   3207       O  
ATOM   6428  CB  VAL C 308     -24.328  42.682  22.086  1.00201.76           C  
ANISOU 6428  CB  VAL C 308    34580  18281  23799    -14   6279   3325       C  
ATOM   6429  CG1 VAL C 308     -25.345  43.643  22.679  1.00201.65           C  
ANISOU 6429  CG1 VAL C 308    34989  18134  23496    557   5804   3385       C  
ATOM   6430  CG2 VAL C 308     -23.047  43.411  21.709  1.00203.54           C  
ANISOU 6430  CG2 VAL C 308    34318  18393  24624   -692   6378   3267       C  
ATOM   6431  N   VAL C 309     -26.285  41.036  23.781  1.00186.82           N  
ANISOU 6431  N   VAL C 309    32181  17305  21498    896   5323   2975       N  
ATOM   6432  CA  VAL C 309     -27.506  40.257  23.753  1.00181.71           C  
ANISOU 6432  CA  VAL C 309    31259  17233  20550   1451   4642   2963       C  
ATOM   6433  C   VAL C 309     -28.027  40.238  22.325  1.00187.25           C  
ANISOU 6433  C   VAL C 309    32736  17786  20625   2065   4574   3275       C  
ATOM   6434  O   VAL C 309     -28.058  41.262  21.650  1.00192.24           O  
ANISOU 6434  O   VAL C 309    34248  17834  20960   2317   4813   3492       O  
ATOM   6435  CB  VAL C 309     -28.582  40.863  24.669  1.00182.91           C  
ANISOU 6435  CB  VAL C 309    31059  17619  20819   1683   4081   2735       C  
ATOM   6436  N   LYS C 310     -28.434  39.063  21.869  1.00179.40           N  
ANISOU 6436  N   LYS C 310    31436  17307  19419   2315   4242   3285       N  
ATOM   6437  CA  LYS C 310     -29.046  38.916  20.560  1.00180.85           C  
ANISOU 6437  CA  LYS C 310    32251  17462  19003   2920   4069   3517       C  
ATOM   6438  C   LYS C 310     -29.887  37.657  20.593  1.00178.35           C  
ANISOU 6438  C   LYS C 310    31337  17838  18589   3237   3435   3368       C  
ATOM   6439  O   LYS C 310     -29.680  36.798  21.444  1.00172.95           O  
ANISOU 6439  O   LYS C 310    29825  17618  18270   2880   3336   3167       O  
ATOM   6440  CB  LYS C 310     -27.989  38.838  19.464  1.00187.84           C  
ANISOU 6440  CB  LYS C 310    33747  17967  19657   2748   4720   3784       C  
ATOM   6441  N   GLY C 311     -30.825  37.526  19.668  1.00175.72           N  
ANISOU 6441  N   GLY C 311    31447  17545  17772   3911   3013   3454       N  
ATOM   6442  CA  GLY C 311     -31.753  36.420  19.746  1.00171.60           C  
ANISOU 6442  CA  GLY C 311    30460  17611  17128   4288   2381   3294       C  
ATOM   6443  C   GLY C 311     -31.038  35.087  19.692  1.00171.09           C  
ANISOU 6443  C   GLY C 311    29898  17974  17133   4032   2412   3236       C  
ATOM   6444  O   GLY C 311     -30.125  34.883  18.903  1.00173.03           O  
ANISOU 6444  O   GLY C 311    30610  18142  16990   4214   2539   3399       O  
ATOM   6445  N   ILE C 312     -31.465  34.176  20.553  1.00161.58           N  
ANISOU 6445  N   ILE C 312    27778  17223  16393   3660   2268   2996       N  
ATOM   6446  CA  ILE C 312     -30.948  32.795  20.574  1.00157.15           C  
ANISOU 6446  CA  ILE C 312    26611  17102  15996   3376   2271   2895       C  
ATOM   6447  C   ILE C 312     -31.643  31.869  19.561  1.00160.29           C  
ANISOU 6447  C   ILE C 312    27139  17763  16001   3813   1918   2900       C  
ATOM   6448  O   ILE C 312     -32.873  31.871  19.466  1.00160.14           O  
ANISOU 6448  O   ILE C 312    27154  17895  15796   4302   1394   2801       O  
ATOM   6449  CB  ILE C 312     -31.006  32.192  22.021  1.00154.91           C  
ANISOU 6449  CB  ILE C 312    25401  17252  16208   3071   2037   2624       C  
ATOM   6450  N   VAL C 313     -30.844  31.075  18.820  1.00156.33           N  
ANISOU 6450  N   VAL C 313    26680  17321  15398   3631   2203   2983       N  
ATOM   6451  CA  VAL C 313     -31.328  30.100  17.839  1.00156.17           C  
ANISOU 6451  CA  VAL C 313    26776  17545  15016   3979   1915   2963       C  
ATOM   6452  C   VAL C 313     -31.088  28.669  18.366  1.00154.33           C  
ANISOU 6452  C   VAL C 313    25714  17813  15110   3681   1788   2759       C  
ATOM   6453  O   VAL C 313     -29.952  28.298  18.667  1.00152.26           O  
ANISOU 6453  O   VAL C 313    25151  17576  15125   3210   2200   2779       O  
ATOM   6454  CB  VAL C 313     -30.799  30.348  16.389  1.00165.21           C  
ANISOU 6454  CB  VAL C 313    28806  18316  15650   4152   2303   3233       C  
ATOM   6455  CG1 VAL C 313     -29.270  30.337  16.310  1.00165.53           C  
ANISOU 6455  CG1 VAL C 313    28846  18145  15901   3587   3046   3370       C  
ATOM   6456  CG2 VAL C 313     -31.411  29.371  15.387  1.00165.67           C  
ANISOU 6456  CG2 VAL C 313    29020  18635  15293   4572   1922   3172       C  
ATOM   6457  N   SER C 314     -32.174  27.897  18.518  1.00148.29           N  
ANISOU 6457  N   SER C 314    24568  17434  14340   3961   1219   2544       N  
ATOM   6458  CA  SER C 314     -32.136  26.521  19.020  1.00143.43           C  
ANISOU 6458  CA  SER C 314    23221  17266  14010   3735   1063   2343       C  
ATOM   6459  C   SER C 314     -32.447  25.516  17.904  1.00147.66           C  
ANISOU 6459  C   SER C 314    23924  17970  14211   4003    854   2296       C  
ATOM   6460  O   SER C 314     -32.913  25.919  16.835  1.00151.32           O  
ANISOU 6460  O   SER C 314    25031  18254  14210   4438    709   2378       O  
ATOM   6461  CB  SER C 314     -33.117  26.358  20.178  1.00144.00           C  
ANISOU 6461  CB  SER C 314    22679  17631  14405   3774    642   2104       C  
ATOM   6462  OG  SER C 314     -32.980  25.093  20.805  1.00148.83           O  
ANISOU 6462  OG  SER C 314    22618  18609  15320   3502    583   1937       O  
ATOM   6463  N   LEU C 315     -32.196  24.208  18.156  1.00140.35           N  
ANISOU 6463  N   LEU C 315    22453  17373  13500   3769    825   2153       N  
ATOM   6464  CA  LEU C 315     -32.449  23.113  17.208  1.00140.61           C  
ANISOU 6464  CA  LEU C 315    22563  17586  13276   3966    627   2059       C  
ATOM   6465  C   LEU C 315     -33.922  23.003  16.810  1.00145.70           C  
ANISOU 6465  C   LEU C 315    23252  18386  13720   4455     -3   1849       C  
ATOM   6466  O   LEU C 315     -34.218  22.577  15.693  1.00148.05           O  
ANISOU 6466  O   LEU C 315    23919  18700  13632   4770   -203   1806       O  
ATOM   6467  CB  LEU C 315     -31.948  21.766  17.756  1.00136.59           C  
ANISOU 6467  CB  LEU C 315    21414  17379  13104   3605    713   1927       C  
ATOM   6468  CG  LEU C 315     -30.436  21.531  17.750  1.00140.55           C  
ANISOU 6468  CG  LEU C 315    21895  17782  13726   3211   1288   2086       C  
ATOM   6469  CD1 LEU C 315     -30.077  20.337  18.598  1.00136.59           C  
ANISOU 6469  CD1 LEU C 315    20704  17584  13611   2901   1295   1938       C  
ATOM   6470  CD2 LEU C 315     -29.904  21.334  16.342  1.00146.52           C  
ANISOU 6470  CD2 LEU C 315    23251  18368  14050   3358   1540   2225       C  
ATOM   6471  N   SER C 316     -34.835  23.405  17.717  1.00140.71           N  
ANISOU 6471  N   SER C 316    22241  17868  13352   4531   -317   1697       N  
ATOM   6472  CA  SER C 316     -36.283  23.408  17.499  1.00142.36           C  
ANISOU 6472  CA  SER C 316    22373  18242  13474   4985   -921   1450       C  
ATOM   6473  C   SER C 316     -36.701  24.388  16.392  1.00151.21           C  
ANISOU 6473  C   SER C 316    24300  19093  14061   5534  -1113   1566       C  
ATOM   6474  O   SER C 316     -37.712  24.150  15.733  1.00153.64           O  
ANISOU 6474  O   SER C 316    24686  19541  14150   5984  -1636   1354       O  
ATOM   6475  CB  SER C 316     -37.023  23.710  18.799  1.00143.70           C  
ANISOU 6475  CB  SER C 316    21959  18560  14079   4905  -1097   1285       C  
ATOM   6476  OG  SER C 316     -36.533  24.885  19.424  1.00152.39           O  
ANISOU 6476  OG  SER C 316    23251  19393  15256   4775   -790   1489       O  
ATOM   6477  N   ASP C 317     -35.918  25.471  16.181  1.00149.30           N  
ANISOU 6477  N   ASP C 317    24669  18449  13609   5504   -689   1886       N  
ATOM   6478  CA  ASP C 317     -36.160  26.474  15.136  1.00154.61           C  
ANISOU 6478  CA  ASP C 317    26244  18776  13726   6017   -761   2063       C  
ATOM   6479  C   ASP C 317     -35.689  25.943  13.782  1.00160.79           C  
ANISOU 6479  C   ASP C 317    27617  19471  14006   6184   -651   2170       C  
ATOM   6480  O   ASP C 317     -36.378  26.135  12.778  1.00165.03           O  
ANISOU 6480  O   ASP C 317    28717  19945  14043   6759  -1035   2135       O  
ATOM   6481  CB  ASP C 317     -35.429  27.793  15.446  1.00157.71           C  
ANISOU 6481  CB  ASP C 317    27088  18718  14115   5857   -256   2370       C  
ATOM   6482  CG  ASP C 317     -35.708  28.368  16.815  1.00164.83           C  
ANISOU 6482  CG  ASP C 317    27466  19664  15500   5644   -281   2282       C  
ATOM   6483  OD1 ASP C 317     -36.772  29.001  16.986  1.00167.24           O  
ANISOU 6483  OD1 ASP C 317    27817  19967  15760   6059   -695   2172       O  
ATOM   6484  OD2 ASP C 317     -34.848  28.214  17.705  1.00166.95           O  
ANISOU 6484  OD2 ASP C 317    27302  19958  16173   5090    111   2316       O  
ATOM   6485  N   ILE C 318     -34.505  25.291  13.760  1.00154.54           N  
ANISOU 6485  N   ILE C 318    26710  18672  13334   5708   -132   2288       N  
ATOM   6486  CA  ILE C 318     -33.879  24.712  12.567  1.00156.65           C  
ANISOU 6486  CA  ILE C 318    27492  18853  13173   5781     95   2397       C  
ATOM   6487  C   ILE C 318     -34.714  23.543  12.027  1.00160.62           C  
ANISOU 6487  C   ILE C 318    27772  19720  13537   6067   -486   2080       C  
ATOM   6488  O   ILE C 318     -35.036  23.539  10.839  1.00164.87           O  
ANISOU 6488  O   ILE C 318    28974  20165  13504   6544   -709   2085       O  
ATOM   6489  CB  ILE C 318     -32.382  24.354  12.825  1.00157.10           C  
ANISOU 6489  CB  ILE C 318    27372  18827  13492   5178    820   2572       C  
ATOM   6490  CG1 ILE C 318     -31.562  25.621  13.153  1.00158.87           C  
ANISOU 6490  CG1 ILE C 318    27933  18628  13801   4933   1399   2861       C  
ATOM   6491  CG2 ILE C 318     -31.752  23.602  11.642  1.00160.10           C  
ANISOU 6491  CG2 ILE C 318    28191  19164  13474   5240   1067   2645       C  
ATOM   6492  CD1 ILE C 318     -30.651  25.487  14.337  1.00161.76           C  
ANISOU 6492  CD1 ILE C 318    27597  19077  14787   4303   1785   2848       C  
ATOM   6493  N   LEU C 319     -35.095  22.585  12.905  1.00152.57           N  
ANISOU 6493  N   LEU C 319    25854  19090  13027   5793   -736   1793       N  
ATOM   6494  CA  LEU C 319     -35.911  21.420  12.544  1.00152.47           C  
ANISOU 6494  CA  LEU C 319    25510  19419  13003   5974  -1266   1441       C  
ATOM   6495  C   LEU C 319     -37.310  21.798  12.038  1.00160.60           C  
ANISOU 6495  C   LEU C 319    26722  20530  13769   6594  -1981   1203       C  
ATOM   6496  O   LEU C 319     -37.833  21.116  11.157  1.00163.08           O  
ANISOU 6496  O   LEU C 319    27176  20989  13796   6911  -2399    971       O  
ATOM   6497  CB  LEU C 319     -36.005  20.405  13.706  1.00147.03           C  
ANISOU 6497  CB  LEU C 319    23846  19065  12954   5511  -1293   1211       C  
ATOM   6498  CG  LEU C 319     -35.001  19.221  13.751  1.00148.67           C  
ANISOU 6498  CG  LEU C 319    23798  19367  13324   5080   -906   1233       C  
ATOM   6499  CD1 LEU C 319     -35.000  18.401  12.459  1.00151.96           C  
ANISOU 6499  CD1 LEU C 319    24623  19810  13304   5331  -1053   1131       C  
ATOM   6500  CD2 LEU C 319     -33.599  19.665  14.137  1.00149.22           C  
ANISOU 6500  CD2 LEU C 319    23974  19217  13506   4684   -218   1565       C  
ATOM   6501  N   GLN C 320     -37.899  22.888  12.580  1.00157.88           N  
ANISOU 6501  N   GLN C 320    26377  20091  13520   6784  -2138   1237       N  
ATOM   6502  CA  GLN C 320     -39.213  23.404  12.176  1.00162.15           C  
ANISOU 6502  CA  GLN C 320    27076  20695  13839   7418  -2817   1014       C  
ATOM   6503  C   GLN C 320     -39.127  23.997  10.764  1.00172.34           C  
ANISOU 6503  C   GLN C 320    29448  21687  14347   7994  -2905   1200       C  
ATOM   6504  O   GLN C 320     -40.062  23.837   9.976  1.00176.19           O  
ANISOU 6504  O   GLN C 320    30132  22307  14504   8555  -3542    938       O  
ATOM   6505  CB  GLN C 320     -39.707  24.468  13.171  1.00162.70           C  
ANISOU 6505  CB  GLN C 320    26907  20695  14216   7453  -2860   1044       C  
ATOM   6506  N   ALA C 321     -38.000  24.671  10.452  1.00170.10           N  
ANISOU 6506  N   ALA C 321    29865  20993  13773   7852  -2253   1635       N  
ATOM   6507  CA  ALA C 321     -37.728  25.281   9.150  1.00176.30           C  
ANISOU 6507  CA  ALA C 321    31791  21409  13788   8336  -2153   1893       C  
ATOM   6508  C   ALA C 321     -37.480  24.215   8.080  1.00182.46           C  
ANISOU 6508  C   ALA C 321    32847  22305  14176   8445  -2227   1793       C  
ATOM   6509  O   ALA C 321     -37.825  24.434   6.918  1.00183.84           O  
ANISOU 6509  O   ALA C 321    33089  22527  14233   8346  -2446   1847       O  
ATOM   6510  CB  ALA C 321     -36.531  26.213   9.250  1.00177.15           C  
ANISOU 6510  CB  ALA C 321    32453  21039  13818   8024  -1322   2362       C  
ATOM   6511  N   LEU C 322     -36.891  23.065   8.474  1.00174.61           N  
ANISOU 6511  N   LEU C 322    31208  21550  13586   7888  -1969   1687       N  
ATOM   6512  CA  LEU C 322     -36.599  21.937   7.582  1.00175.68           C  
ANISOU 6512  CA  LEU C 322    31508  21809  13435   7916  -1998   1564       C  
ATOM   6513  C   LEU C 322     -37.873  21.206   7.140  1.00182.52           C  
ANISOU 6513  C   LEU C 322    32122  23026  14202   8356  -2879   1080       C  
ATOM   6514  O   LEU C 322     -37.905  20.663   6.035  1.00184.70           O  
ANISOU 6514  O   LEU C 322    32630  23366  14180   8397  -3031   1007       O  
ATOM   6515  CB  LEU C 322     -35.616  20.947   8.237  1.00169.81           C  
ANISOU 6515  CB  LEU C 322    30111  21208  13203   7206  -1475   1580       C  
ATOM   6516  CG  LEU C 322     -34.167  21.418   8.420  1.00173.04           C  
ANISOU 6516  CG  LEU C 322    30788  21294  13665   6765   -577   2001       C  
ATOM   6517  CD1 LEU C 322     -33.512  20.714   9.588  1.00167.00           C  
ANISOU 6517  CD1 LEU C 322    29108  20737  13608   6092   -243   1952       C  
ATOM   6518  CD2 LEU C 322     -33.344  21.215   7.159  1.00179.12           C  
ANISOU 6518  CD2 LEU C 322    32395  21823  13838   6909   -165   2201       C  
ATOM   6519  N   VAL C 323     -38.915  21.194   8.000  1.00177.27           N  
ANISOU 6519  N   VAL C 323    30669  22645  14040   8360  -3387    762       N  
ATOM   6520  CA  VAL C 323     -40.205  20.546   7.729  1.00179.73           C  
ANISOU 6520  CA  VAL C 323    30574  23310  14404   8722  -4231    237       C  
ATOM   6521  C   VAL C 323     -41.015  21.358   6.706  1.00185.42           C  
ANISOU 6521  C   VAL C 323    31269  24042  15141   8594  -4532    359       C  
ATOM   6522  O   VAL C 323     -41.392  20.816   5.665  1.00186.37           O  
ANISOU 6522  O   VAL C 323    31274  24333  15205   8434  -4786    244       O  
ATOM   6523  CB  VAL C 323     -41.001  20.238   9.034  1.00179.50           C  
ANISOU 6523  CB  VAL C 323    29409  23607  15184   8398  -4476    -84       C  
ATOM   6524  CG1 VAL C 323     -42.437  19.804   8.739  1.00183.31           C  
ANISOU 6524  CG1 VAL C 323    29478  24421  15750   8824  -5358   -650       C  
ATOM   6525  CG2 VAL C 323     -40.292  19.181   9.874  1.00172.86           C  
ANISOU 6525  CG2 VAL C 323    27868  22905  14904   7655  -3998    -86       C  
ATOM   6526  N   LEU C 324     -41.273  22.649   7.001  1.00182.82           N  
ANISOU 6526  N   LEU C 324    31137  23521  14807   8774  -4513    581       N  
ATOM   6527  CA  LEU C 324     -42.044  23.536   6.128  1.00183.68           C  
ANISOU 6527  CA  LEU C 324    31133  23649  15007   8605  -4741    756       C  
ATOM   6528  C   LEU C 324     -41.140  24.378   5.222  1.00186.39           C  
ANISOU 6528  C   LEU C 324    31926  23713  15180   8147  -4143   1309       C  
ATOM   6529  O   LEU C 324     -40.450  25.285   5.696  1.00185.59           O  
ANISOU 6529  O   LEU C 324    32225  23280  15012   8151  -3688   1619       O  
ATOM   6530  CB  LEU C 324     -43.009  24.422   6.944  1.00183.75           C  
ANISOU 6530  CB  LEU C 324    30728  23697  15391   8773  -5048    679       C  
TER    6531      LEU C 324                                                      
HETATM 6532  C1  GLC D   1     -41.736 -72.105  -8.704  1.00213.07           C  
HETATM 6533  C2  GLC D   1     -41.208 -72.079  -7.266  1.00213.03           C  
HETATM 6534  C3  GLC D   1     -40.353 -70.837  -7.033  1.00213.04           C  
HETATM 6535  C4  GLC D   1     -39.235 -70.668  -8.069  1.00213.03           C  
HETATM 6536  C5  GLC D   1     -39.551 -71.280  -9.437  1.00213.02           C  
HETATM 6537  C6  GLC D   1     -38.999 -72.695  -9.548  1.00212.97           C  
HETATM 6538  O2  GLC D   1     -42.306 -72.088  -6.347  1.00212.98           O  
HETATM 6539  O3  GLC D   1     -39.775 -70.902  -5.723  1.00213.02           O  
HETATM 6540  O4  GLC D   1     -38.998 -69.269  -8.215  1.00212.98           O  
HETATM 6541  O5  GLC D   1     -40.971 -71.301  -9.622  1.00213.05           O  
HETATM 6542  O6  GLC D   1     -37.576 -72.666  -9.391  1.00212.92           O  
HETATM 6543  C1  GLC D   2     -37.674 -68.973  -8.653  1.00212.83           C  
HETATM 6544  C2  GLC D   2     -37.173 -67.743  -7.909  1.00212.73           C  
HETATM 6545  C3  GLC D   2     -38.090 -66.561  -8.186  1.00212.70           C  
HETATM 6546  C4  GLC D   2     -38.274 -66.365  -9.686  1.00212.72           C  
HETATM 6547  C5  GLC D   2     -38.634 -67.676 -10.383  1.00212.64           C  
HETATM 6548  C6  GLC D   2     -38.670 -67.504 -11.897  1.00212.47           C  
HETATM 6549  O2  GLC D   2     -37.140 -68.009  -6.502  1.00212.66           O  
HETATM 6550  O3  GLC D   2     -37.527 -65.374  -7.614  1.00212.66           O  
HETATM 6551  O4  GLC D   2     -39.297 -65.397  -9.915  1.00212.78           O  
HETATM 6552  O5  GLC D   2     -37.688 -68.693 -10.050  1.00212.74           O  
HETATM 6553  O6  GLC D   2     -39.820 -66.736 -12.266  1.00212.35           O  
HETATM 6554  C1  GLC D   3     -38.789 -64.211 -10.525  1.00212.78           C  
HETATM 6555  C2  GLC D   3     -39.293 -62.991  -9.761  1.00212.79           C  
HETATM 6556  C3  GLC D   3     -40.810 -62.885  -9.851  1.00212.78           C  
HETATM 6557  C4  GLC D   3     -41.265 -62.964 -11.302  1.00212.78           C  
HETATM 6558  C5  GLC D   3     -40.651 -64.177 -11.992  1.00212.73           C  
HETATM 6559  C6  GLC D   3     -41.036 -64.221 -13.466  1.00212.70           C  
HETATM 6560  O2  GLC D   3     -38.899 -63.087  -8.387  1.00212.79           O  
HETATM 6561  O3  GLC D   3     -41.237 -61.642  -9.282  1.00212.79           O  
HETATM 6562  O4  GLC D   3     -42.687 -63.060 -11.357  1.00212.84           O  
HETATM 6563  O5  GLC D   3     -39.229 -64.135 -11.880  1.00212.76           O  
HETATM 6564  O6  GLC D   3     -40.435 -65.366 -14.082  1.00212.67           O  
HETATM 6565  C1  GLC D   4     -43.218 -62.412 -12.513  1.00212.92           C  
HETATM 6566  C2  GLC D   4     -44.383 -61.509 -12.117  1.00212.98           C  
HETATM 6567  C3  GLC D   4     -45.583 -62.327 -11.665  1.00213.03           C  
HETATM 6568  C4  GLC D   4     -45.925 -63.365 -12.723  1.00213.04           C  
HETATM 6569  C5  GLC D   4     -44.706 -64.225 -13.034  1.00212.97           C  
HETATM 6570  C6  GLC D   4     -45.007 -65.242 -14.128  1.00212.93           C  
HETATM 6571  O2  GLC D   4     -43.966 -60.652 -11.049  1.00212.96           O  
HETATM 6572  O3  GLC D   4     -46.706 -61.462 -11.459  1.00213.05           O  
HETATM 6573  O4  GLC D   4     -47.014 -64.175 -12.277  1.00213.09           O  
HETATM 6574  O5  GLC D   4     -43.615 -63.407 -13.460  1.00212.92           O  
HETATM 6575  O6  GLC D   4     -45.406 -64.557 -15.320  1.00212.91           O  
HETATM 6576  C1  GLC D   5     -48.044 -64.280 -13.260  1.00213.12           C  
HETATM 6577  C2  GLC D   5     -49.377 -64.617 -12.602  1.00213.16           C  
HETATM 6578  C3  GLC D   5     -49.339 -65.988 -11.934  1.00213.20           C  
HETATM 6579  C4  GLC D   5     -48.753 -67.052 -12.855  1.00213.17           C  
HETATM 6580  C5  GLC D   5     -47.465 -66.548 -13.492  1.00213.12           C  
HETATM 6581  C6  GLC D   5     -46.908 -67.571 -14.475  1.00213.09           C  
HETATM 6582  O2  GLC D   5     -49.699 -63.618 -11.627  1.00213.16           O  
HETATM 6583  O3  GLC D   5     -50.667 -66.368 -11.555  1.00213.26           O  
HETATM 6584  O4  GLC D   5     -48.454 -68.213 -12.085  1.00213.15           O  
HETATM 6585  O5  GLC D   5     -47.710 -65.320 -14.175  1.00213.11           O  
HETATM 6586  O6  GLC D   5     -46.621 -68.791 -13.782  1.00213.07           O  
HETATM 6587  C1  GLC D   6     -49.617 -68.883 -11.597  1.00213.04           C  
HETATM 6588  C2  GLC D   6     -49.755 -68.796 -10.084  1.00212.96           C  
HETATM 6589  C3  GLC D   6     -48.571 -69.470  -9.420  1.00212.90           C  
HETATM 6590  C4  GLC D   6     -48.412 -70.901  -9.912  1.00212.94           C  
HETATM 6591  C5  GLC D   6     -48.532 -71.044 -11.432  1.00212.91           C  
HETATM 6592  C6  GLC D   6     -48.782 -72.501 -11.809  1.00212.83           C  
HETATM 6593  O2  GLC D   6     -49.802 -67.421  -9.688  1.00212.95           O  
HETATM 6594  O3  GLC D   6     -48.762 -69.473  -8.000  1.00212.85           O  
HETATM 6595  O4  GLC D   6     -47.116 -71.322  -9.491  1.00213.01           O  
HETATM 6596  O5  GLC D   6     -49.557 -70.241 -12.037  1.00212.97           O  
HETATM 6597  O6  GLC D   6     -48.901 -72.613 -13.232  1.00212.78           O  
HETATM 6598  C1  GLC D   7     -46.841 -72.701  -9.724  1.00213.07           C  
HETATM 6599  C2  GLC D   7     -46.326 -73.342  -8.445  1.00213.06           C  
HETATM 6600  C3  GLC D   7     -45.078 -72.610  -7.979  1.00213.04           C  
HETATM 6601  C4  GLC D   7     -44.053 -72.507  -9.102  1.00213.07           C  
HETATM 6602  C5  GLC D   7     -44.674 -72.030 -10.412  1.00213.07           C  
HETATM 6603  C6  GLC D   7     -43.656 -72.151 -11.540  1.00213.04           C  
HETATM 6604  O2  GLC D   7     -47.336 -73.255  -7.435  1.00213.06           O  
HETATM 6605  O3  GLC D   7     -44.502 -73.310  -6.870  1.00213.00           O  
HETATM 6606  O4  GLC D   7     -43.057 -71.570  -8.700  1.00213.08           O  
HETATM 6607  O5  GLC D   7     -45.844 -72.783 -10.741  1.00213.10           O  
HETATM 6608  O6  GLC D   7     -44.288 -71.851 -12.789  1.00213.01           O  
HETATM 6609  O4  STU A 601     -12.242 -37.188   1.630  1.00 88.99           O  
HETATM 6610  C25 STU A 601     -10.968 -36.702   1.184  1.00 88.99           C  
HETATM 6611  C24 STU A 601     -10.079 -36.140   2.292  1.00 89.34           C  
HETATM 6612  C23 STU A 601     -10.658 -36.396   3.671  1.00 89.51           C  
HETATM 6613  C22 STU A 601     -12.077 -35.858   3.723  1.00 89.17           C  
HETATM 6614  C21 STU A 601     -12.965 -36.460   2.630  1.00 89.04           C  
HETATM 6615  C26 STU A 601     -13.885 -37.488   3.283  1.00 89.13           C  
HETATM 6616  N2  STU A 601     -13.784 -35.377   1.995  1.00 88.85           N  
HETATM 6617  C18 STU A 601     -13.425 -34.705   0.875  1.00 88.57           C  
HETATM 6618  C19 STU A 601     -12.225 -34.845   0.001  1.00 88.53           C  
HETATM 6619  C6  STU A 601     -12.086 -33.984  -1.174  1.00 88.54           C  
HETATM 6620  C7  STU A 601     -13.166 -32.999  -1.443  1.00 88.45           C  
HETATM 6621  C10 STU A 601     -14.358 -32.828  -0.618  1.00 88.38           C  
HETATM 6622  C11 STU A 601     -14.480 -33.716   0.576  1.00 88.45           C  
HETATM 6623  C12 STU A 601     -15.469 -33.884   1.642  1.00 88.48           C  
HETATM 6624  C17 STU A 601     -14.972 -34.960   2.535  1.00 88.73           C  
HETATM 6625  C16 STU A 601     -15.752 -35.305   3.629  1.00 88.76           C  
HETATM 6626  C15 STU A 601     -16.953 -34.623   3.835  1.00 88.72           C  
HETATM 6627  C14 STU A 601     -17.399 -33.609   2.979  1.00 88.54           C  
HETATM 6628  C13 STU A 601     -16.662 -33.219   1.862  1.00 88.40           C  
HETATM 6629  C9  STU A 601     -15.208 -31.780  -1.164  1.00 88.32           C  
HETATM 6630  N1  STU A 601     -14.488 -31.299  -2.378  1.00 88.34           N  
HETATM 6631  C8  STU A 601     -13.335 -32.004  -2.517  1.00 88.43           C  
HETATM 6632  O5  STU A 601     -12.491 -31.824  -3.469  1.00 88.43           O  
HETATM 6633  C5  STU A 601     -10.826 -34.384  -1.777  1.00 88.53           C  
HETATM 6634  C20 STU A 601     -10.289 -35.468  -0.916  1.00 88.52           C  
HETATM 6635  C1  STU A 601      -9.074 -36.021  -1.292  1.00 88.53           C  
HETATM 6636  C2  STU A 601      -8.433 -35.541  -2.437  1.00 88.62           C  
HETATM 6637  C3  STU A 601      -8.967 -34.518  -3.227  1.00 88.63           C  
HETATM 6638  C4  STU A 601     -10.182 -33.917  -2.909  1.00 88.57           C  
HETATM 6639  N3  STU A 601     -11.168 -35.686   0.120  1.00 88.63           N  
HETATM 6640  O6  STU A 601     -12.027 -34.434   3.625  1.00 89.13           O  
HETATM 6641  C27 STU A 601     -11.834 -33.822   4.899  1.00 89.22           C  
HETATM 6642  N4  STU A 601      -9.842 -35.756   4.684  1.00 90.01           N  
HETATM 6643  C28 STU A 601      -8.722 -36.466   5.269  1.00 90.17           C  
HETATM 6644  OAB CG7 A 602     -20.968 -48.573   4.202  1.00137.91           O  
HETATM 6645  CAV CG7 A 602     -22.005 -47.971   4.557  1.00137.75           C  
HETATM 6646  OAC CG7 A 602     -22.657 -48.376   5.544  1.00137.79           O  
HETATM 6647  CBD CG7 A 602     -22.444 -46.853   3.847  1.00137.48           C  
HETATM 6648  CAP CG7 A 602     -23.398 -47.053   2.843  1.00137.25           C  
HETATM 6649  CAW CG7 A 602     -21.975 -45.548   4.108  1.00137.42           C  
HETATM 6650  CAA CG7 A 602     -21.022 -45.271   5.093  1.00137.46           C  
HETATM 6651  CAI CG7 A 602     -22.466 -44.473   3.357  1.00137.28           C  
HETATM 6652  CAK CG7 A 602     -23.422 -44.681   2.360  1.00137.15           C  
HETATM 6653  CAZ CG7 A 602     -23.874 -45.978   2.086  1.00137.11           C  
HETATM 6654  OAU CG7 A 602     -24.823 -46.207   1.129  1.00136.98           O  
HETATM 6655  CBC CG7 A 602     -24.419 -46.019  -0.163  1.00136.81           C  
HETATM 6656  NAR CG7 A 602     -25.105 -45.316  -1.053  1.00136.65           N  
HETATM 6657  NAT CG7 A 602     -23.359 -46.575  -0.743  1.00136.78           N  
HETATM 6658  CBH CG7 A 602     -23.354 -46.167  -2.012  1.00136.70           C  
HETATM 6659  NAS CG7 A 602     -22.498 -46.417  -3.029  1.00136.71           N  
HETATM 6660  CBG CG7 A 602     -24.437 -45.392  -2.200  1.00136.62           C  
HETATM 6661  CAQ CG7 A 602     -24.692 -44.864  -3.401  1.00136.59           C  
HETATM 6662  CAY CG7 A 602     -23.819 -45.077  -4.466  1.00136.72           C  
HETATM 6663 CL1  CG7 A 602     -24.198 -44.337  -5.997  1.00136.87          CL  
HETATM 6664  CBF CG7 A 602     -22.697 -45.901  -4.264  1.00136.73           C  
HETATM 6665  CBB CG7 A 602     -21.766 -46.164  -5.278  1.00136.76           C  
HETATM 6666  CAO CG7 A 602     -22.162 -46.753  -6.487  1.00136.73           C  
HETATM 6667  CAM CG7 A 602     -21.232 -46.992  -7.500  1.00136.82           C  
HETATM 6668  CAN CG7 A 602     -20.410 -45.860  -5.080  1.00136.86           C  
HETATM 6669  CAL CG7 A 602     -19.469 -46.136  -6.079  1.00136.87           C  
HETATM 6670  CBA CG7 A 602     -19.877 -46.691  -7.302  1.00136.91           C  
HETATM 6671  CBE CG7 A 602     -18.955 -46.954  -8.325  1.00137.08           C  
HETATM 6672  CAJ CG7 A 602     -18.789 -48.269  -8.784  1.00137.10           C  
HETATM 6673  CAG CG7 A 602     -17.891 -48.556  -9.817  1.00137.21           C  
HETATM 6674  CAF CG7 A 602     -17.147 -47.536 -10.415  1.00137.31           C  
HETATM 6675  CAH CG7 A 602     -17.306 -46.219  -9.978  1.00137.32           C  
HETATM 6676  CAX CG7 A 602     -18.209 -45.934  -8.948  1.00137.28           C  
HETATM 6677  OAD CG7 A 602     -18.374 -44.657  -8.504  1.00137.39           O  
HETATM 6678  P   AMP C 400     -28.236  20.943  26.216  1.00134.38           P  
HETATM 6679  O1P AMP C 400     -28.190  19.940  25.087  1.00134.39           O  
HETATM 6680  O2P AMP C 400     -28.666  22.331  25.806  1.00134.33           O  
HETATM 6681  O3P AMP C 400     -28.916  20.440  27.468  1.00134.45           O  
HETATM 6682  O5' AMP C 400     -26.688  21.143  26.619  1.00134.30           O  
HETATM 6683  C5' AMP C 400     -25.919  20.120  27.257  1.00134.30           C  
HETATM 6684  C4' AMP C 400     -24.646  20.719  27.857  1.00134.41           C  
HETATM 6685  O4' AMP C 400     -24.000  21.576  26.908  1.00134.52           O  
HETATM 6686  C3' AMP C 400     -24.914  21.543  29.113  1.00134.49           C  
HETATM 6687  O3' AMP C 400     -23.988  21.130  30.126  1.00134.48           O  
HETATM 6688  C2' AMP C 400     -24.645  22.987  28.709  1.00134.56           C  
HETATM 6689  O2' AMP C 400     -23.955  23.711  29.735  1.00134.56           O  
HETATM 6690  C1' AMP C 400     -23.791  22.883  27.450  1.00134.66           C  
HETATM 6691  N9  AMP C 400     -24.135  23.926  26.444  1.00134.81           N  
HETATM 6692  C8  AMP C 400     -25.316  24.065  25.805  1.00134.90           C  
HETATM 6693  N7  AMP C 400     -25.293  25.113  24.942  1.00134.91           N  
HETATM 6694  C5  AMP C 400     -24.061  25.647  24.992  1.00134.88           C  
HETATM 6695  C6  AMP C 400     -23.348  26.775  24.333  1.00135.00           C  
HETATM 6696  N6  AMP C 400     -23.972  27.552  23.414  1.00135.09           N  
HETATM 6697  N1  AMP C 400     -22.054  27.003  24.678  1.00134.99           N  
HETATM 6698  C2  AMP C 400     -21.412  26.240  25.592  1.00134.91           C  
HETATM 6699  N3  AMP C 400     -22.000  25.203  26.229  1.00134.86           N  
HETATM 6700  C4  AMP C 400     -23.296  24.858  25.979  1.00134.83           C  
HETATM 6701  P   AMP C 401     -35.631  25.184  23.244  1.00143.15           P  
HETATM 6702  O1P AMP C 401     -35.757  24.227  22.081  1.00143.09           O  
HETATM 6703  O2P AMP C 401     -36.412  24.779  24.472  1.00143.17           O  
HETATM 6704  O3P AMP C 401     -34.214  25.628  23.523  1.00143.03           O  
HETATM 6705  O5' AMP C 401     -36.352  26.540  22.757  1.00143.26           O  
HETATM 6706  C5' AMP C 401     -37.691  26.568  22.254  1.00143.28           C  
HETATM 6707  C4' AMP C 401     -37.980  27.926  21.611  1.00143.27           C  
HETATM 6708  O4' AMP C 401     -37.581  28.991  22.483  1.00143.29           O  
HETATM 6709  C3' AMP C 401     -37.240  28.111  20.291  1.00143.22           C  
HETATM 6710  O3' AMP C 401     -38.177  28.514  19.284  1.00143.16           O  
HETATM 6711  C2' AMP C 401     -36.201  29.194  20.554  1.00143.26           C  
HETATM 6712  O2' AMP C 401     -36.144  30.164  19.501  1.00143.27           O  
HETATM 6713  C1' AMP C 401     -36.607  29.843  21.871  1.00143.29           C  
HETATM 6714  N9  AMP C 401     -35.463  30.043  22.808  1.00143.30           N  
HETATM 6715  C8  AMP C 401     -34.348  29.287  22.920  1.00143.29           C  
HETATM 6716  N7  AMP C 401     -33.525  29.751  23.894  1.00143.35           N  
HETATM 6717  C5  AMP C 401     -34.124  30.819  24.449  1.00143.40           C  
HETATM 6718  C6  AMP C 401     -33.815  31.787  25.539  1.00143.44           C  
HETATM 6719  N6  AMP C 401     -32.664  31.697  26.249  1.00143.46           N  
HETATM 6720  N1  AMP C 401     -34.721  32.765  25.800  1.00143.45           N  
HETATM 6721  C2  AMP C 401     -35.878  32.869  25.109  1.00143.45           C  
HETATM 6722  N3  AMP C 401     -36.219  32.031  24.106  1.00143.42           N  
HETATM 6723  C4  AMP C 401     -35.397  31.013  23.725  1.00143.38           C  
CONECT 1203 1206                                                                
CONECT 1206 1203 1207                                                           
CONECT 1207 1206 1208 1215                                                      
CONECT 1208 1207 1209 1210                                                      
CONECT 1209 1208                                                                
CONECT 1210 1208 1211                                                           
CONECT 1211 1210 1212 1213 1214                                                 
CONECT 1212 1211                                                                
CONECT 1213 1211                                                                
CONECT 1214 1211                                                                
CONECT 1215 1207 1216 1217                                                      
CONECT 1216 1215                                                                
CONECT 1217 1215                                                                
CONECT 3503 3506                                                                
CONECT 3506 3503 3507                                                           
CONECT 3507 3506 3508 3510                                                      
CONECT 3508 3507 3509                                                           
CONECT 3509 3508 3512                                                           
CONECT 3510 3507 3511 3516                                                      
CONECT 3511 3510                                                                
CONECT 3512 3509 3513 3514 3515                                                 
CONECT 3513 3512                                                                
CONECT 3514 3512                                                                
CONECT 3515 3512                                                                
CONECT 3516 3510                                                                
CONECT 6532 6533 6541 6606                                                      
CONECT 6533 6532 6534 6538                                                      
CONECT 6534 6533 6535 6539                                                      
CONECT 6535 6534 6536 6540                                                      
CONECT 6536 6535 6537 6541                                                      
CONECT 6537 6536 6542                                                           
CONECT 6538 6533                                                                
CONECT 6539 6534                                                                
CONECT 6540 6535 6543                                                           
CONECT 6541 6532 6536                                                           
CONECT 6542 6537                                                                
CONECT 6543 6540 6544 6552                                                      
CONECT 6544 6543 6545 6549                                                      
CONECT 6545 6544 6546 6550                                                      
CONECT 6546 6545 6547 6551                                                      
CONECT 6547 6546 6548 6552                                                      
CONECT 6548 6547 6553                                                           
CONECT 6549 6544                                                                
CONECT 6550 6545                                                                
CONECT 6551 6546 6554                                                           
CONECT 6552 6543 6547                                                           
CONECT 6553 6548                                                                
CONECT 6554 6551 6555 6563                                                      
CONECT 6555 6554 6556 6560                                                      
CONECT 6556 6555 6557 6561                                                      
CONECT 6557 6556 6558 6562                                                      
CONECT 6558 6557 6559 6563                                                      
CONECT 6559 6558 6564                                                           
CONECT 6560 6555                                                                
CONECT 6561 6556                                                                
CONECT 6562 6557 6565                                                           
CONECT 6563 6554 6558                                                           
CONECT 6564 6559                                                                
CONECT 6565 6562 6566 6574                                                      
CONECT 6566 6565 6567 6571                                                      
CONECT 6567 6566 6568 6572                                                      
CONECT 6568 6567 6569 6573                                                      
CONECT 6569 6568 6570 6574                                                      
CONECT 6570 6569 6575                                                           
CONECT 6571 6566                                                                
CONECT 6572 6567                                                                
CONECT 6573 6568 6576                                                           
CONECT 6574 6565 6569                                                           
CONECT 6575 6570                                                                
CONECT 6576 6573 6577 6585                                                      
CONECT 6577 6576 6578 6582                                                      
CONECT 6578 6577 6579 6583                                                      
CONECT 6579 6578 6580 6584                                                      
CONECT 6580 6579 6581 6585                                                      
CONECT 6581 6580 6586                                                           
CONECT 6582 6577                                                                
CONECT 6583 6578                                                                
CONECT 6584 6579 6587                                                           
CONECT 6585 6576 6580                                                           
CONECT 6586 6581                                                                
CONECT 6587 6584 6588 6596                                                      
CONECT 6588 6587 6589 6593                                                      
CONECT 6589 6588 6590 6594                                                      
CONECT 6590 6589 6591 6595                                                      
CONECT 6591 6590 6592 6596                                                      
CONECT 6592 6591 6597                                                           
CONECT 6593 6588                                                                
CONECT 6594 6589                                                                
CONECT 6595 6590 6598                                                           
CONECT 6596 6587 6591                                                           
CONECT 6597 6592                                                                
CONECT 6598 6595 6599 6607                                                      
CONECT 6599 6598 6600 6604                                                      
CONECT 6600 6599 6601 6605                                                      
CONECT 6601 6600 6602 6606                                                      
CONECT 6602 6601 6603 6607                                                      
CONECT 6603 6602 6608                                                           
CONECT 6604 6599                                                                
CONECT 6605 6600                                                                
CONECT 6606 6532 6601                                                           
CONECT 6607 6598 6602                                                           
CONECT 6608 6603                                                                
CONECT 6609 6610 6614                                                           
CONECT 6610 6609 6611 6639                                                      
CONECT 6611 6610 6612                                                           
CONECT 6612 6611 6613 6642                                                      
CONECT 6613 6612 6614 6640                                                      
CONECT 6614 6609 6613 6615 6616                                                 
CONECT 6615 6614                                                                
CONECT 6616 6614 6617 6624                                                      
CONECT 6617 6616 6618 6622                                                      
CONECT 6618 6617 6619 6639                                                      
CONECT 6619 6618 6620 6633                                                      
CONECT 6620 6619 6621 6631                                                      
CONECT 6621 6620 6622 6629                                                      
CONECT 6622 6617 6621 6623                                                      
CONECT 6623 6622 6624 6628                                                      
CONECT 6624 6616 6623 6625                                                      
CONECT 6625 6624 6626                                                           
CONECT 6626 6625 6627                                                           
CONECT 6627 6626 6628                                                           
CONECT 6628 6623 6627                                                           
CONECT 6629 6621 6630                                                           
CONECT 6630 6629 6631                                                           
CONECT 6631 6620 6630 6632                                                      
CONECT 6632 6631                                                                
CONECT 6633 6619 6634 6638                                                      
CONECT 6634 6633 6635 6639                                                      
CONECT 6635 6634 6636                                                           
CONECT 6636 6635 6637                                                           
CONECT 6637 6636 6638                                                           
CONECT 6638 6633 6637                                                           
CONECT 6639 6610 6618 6634                                                      
CONECT 6640 6613 6641                                                           
CONECT 6641 6640                                                                
CONECT 6642 6612 6643                                                           
CONECT 6643 6642                                                                
CONECT 6644 6645                                                                
CONECT 6645 6644 6646 6647                                                      
CONECT 6646 6645                                                                
CONECT 6647 6645 6648 6649                                                      
CONECT 6648 6647 6653                                                           
CONECT 6649 6647 6650 6651                                                      
CONECT 6650 6649                                                                
CONECT 6651 6649 6652                                                           
CONECT 6652 6651 6653                                                           
CONECT 6653 6648 6652 6654                                                      
CONECT 6654 6653 6655                                                           
CONECT 6655 6654 6656 6657                                                      
CONECT 6656 6655 6660                                                           
CONECT 6657 6655 6658                                                           
CONECT 6658 6657 6659 6660                                                      
CONECT 6659 6658 6664                                                           
CONECT 6660 6656 6658 6661                                                      
CONECT 6661 6660 6662                                                           
CONECT 6662 6661 6663 6664                                                      
CONECT 6663 6662                                                                
CONECT 6664 6659 6662 6665                                                      
CONECT 6665 6664 6666 6668                                                      
CONECT 6666 6665 6667                                                           
CONECT 6667 6666 6670                                                           
CONECT 6668 6665 6669                                                           
CONECT 6669 6668 6670                                                           
CONECT 6670 6667 6669 6671                                                      
CONECT 6671 6670 6672 6676                                                      
CONECT 6672 6671 6673                                                           
CONECT 6673 6672 6674                                                           
CONECT 6674 6673 6675                                                           
CONECT 6675 6674 6676                                                           
CONECT 6676 6671 6675 6677                                                      
CONECT 6677 6676                                                                
CONECT 6678 6679 6680 6681 6682                                                 
CONECT 6679 6678                                                                
CONECT 6680 6678                                                                
CONECT 6681 6678                                                                
CONECT 6682 6678 6683                                                           
CONECT 6683 6682 6684                                                           
CONECT 6684 6683 6685 6686                                                      
CONECT 6685 6684 6690                                                           
CONECT 6686 6684 6687 6688                                                      
CONECT 6687 6686                                                                
CONECT 6688 6686 6689 6690                                                      
CONECT 6689 6688                                                                
CONECT 6690 6685 6688 6691                                                      
CONECT 6691 6690 6692 6700                                                      
CONECT 6692 6691 6693                                                           
CONECT 6693 6692 6694                                                           
CONECT 6694 6693 6695 6700                                                      
CONECT 6695 6694 6696 6697                                                      
CONECT 6696 6695                                                                
CONECT 6697 6695 6698                                                           
CONECT 6698 6697 6699                                                           
CONECT 6699 6698 6700                                                           
CONECT 6700 6691 6694 6699                                                      
CONECT 6701 6702 6703 6704 6705                                                 
CONECT 6702 6701                                                                
CONECT 6703 6701                                                                
CONECT 6704 6701                                                                
CONECT 6705 6701 6706                                                           
CONECT 6706 6705 6707                                                           
CONECT 6707 6706 6708 6709                                                      
CONECT 6708 6707 6713                                                           
CONECT 6709 6707 6710 6711                                                      
CONECT 6710 6709                                                                
CONECT 6711 6709 6712 6713                                                      
CONECT 6712 6711                                                                
CONECT 6713 6708 6711 6714                                                      
CONECT 6714 6713 6715 6723                                                      
CONECT 6715 6714 6716                                                           
CONECT 6716 6715 6717                                                           
CONECT 6717 6716 6718 6723                                                      
CONECT 6718 6717 6719 6720                                                      
CONECT 6719 6718                                                                
CONECT 6720 6718 6721                                                           
CONECT 6721 6720 6722                                                           
CONECT 6722 6721 6723                                                           
CONECT 6723 6714 6717 6722                                                      
MASTER      827    0   13   36   37    0    0    6 6720    3  217   91          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 25th, 2023.