CNRS Nantes University US2B US2B
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***  TRANSFERASE 29-SEP-21 7PUE  ***

elNémo ID: 23020112254464721

Job options:

ID        	=	 23020112254464721
JOBID     	=	 TRANSFERASE 29-SEP-21 7PUE
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    TRANSFERASE                             29-SEP-21   7PUE              
TITLE     HUMAN SERUM AND GLUCOCORTICOID-REGULATED KINASE 1 IN COMPLEX WITH     
TITLE    2 PYRAZOLOPYRIDINE INHIBITOR 3A                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE SGK1;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SERUM/GLUCOCORTICOID-REGULATED KINASE 1;                    
COMPND   5 EC: 2.7.11.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SGK1, SGK;                                                     
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    SERINE/THREONINE PROTEIN KINASE, ATP-COMPETITIVE INHIBITOR, DFG-LOOP, 
KEYWDS   2 HINGE-BINDER, OSTEOARTHRITIS, CARTILAGE DEGRADATION, PYRAZOLO-       
KEYWDS   3 PYRIDINE, TRANSFERASE                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.K.DREYER,N.HALLAND,M.NAZARE                                         
REVDAT   3   09-FEB-22 7PUE    1       JRNL                                     
REVDAT   2   02-FEB-22 7PUE    1       JRNL                                     
REVDAT   1   01-DEC-21 7PUE    0                                                
JRNL        AUTH   N.HALLAND,F.SCHMIDT,T.WEISS,Z.LI,J.CZECH,J.SAAS,             
JRNL        AUTH 2 D.DING-PFENNIGDORFF,M.K.DREYER,C.STRUBING,M.NAZARE           
JRNL        TITL   RATIONAL DESIGN OF HIGHLY POTENT, SELECTIVE, AND             
JRNL        TITL 2 BIOAVAILABLE SGK1 PROTEIN KINASE INHIBITORS FOR THE          
JRNL        TITL 3 TREATMENT OF OSTEOARTHRITIS.                                 
JRNL        REF    J.MED.CHEM.                   V.  65  1567 2022              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   34931844                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.1C01601                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.51 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.8                                        
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) : 2.51                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.73                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 70.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 10904                          
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)  : 0.216                          
REMARK   3   R VALUE            (WORKING SET)  : 0.214                          
REMARK   3   FREE R VALUE                      : 0.249                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : NULL                           
REMARK   3   FREE R VALUE TEST SET COUNT       : 767                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : NULL                     
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.51                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.71                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 9.19                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : NULL                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : NULL                     
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : NULL                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.3109                   
REMARK   3   BIN FREE R VALUE                        : 0.3479                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : NULL                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 23                       
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2155                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 47                                      
REMARK   3   SOLVENT ATOMS            : 24                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 86.98                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.75210                                              
REMARK   3    B22 (A**2) : 3.75210                                              
REMARK   3    B33 (A**2) : -7.50410                                             
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) : 0.370               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.686               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.316               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.634               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.316               
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      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2263   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 3074   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 741    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : 371    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2263   ; 10.000 ; 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   : 281    ; 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   : 1760   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.15                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.26                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 11.59                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   -26.636   26.2033     1.454           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0887 T22:   -0.3699                                    
REMARK   3     T33:   -0.3826 T12:    0.0509                                    
REMARK   3     T13:    0.0326 T23:    0.0637                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.2019 L22:    3.8399                                    
REMARK   3     L33:    5.1137 L12:   -0.5842                                    
REMARK   3     L13:    0.9468 L23:   -0.6138                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0681 S12:     -0.18 S13:   -0.9301                     
REMARK   3     S21:     -0.18 S22:     0.036 S23:   -0.1308                     
REMARK   3     S31:   -0.9301 S32:   -0.1308 S33:   -0.1041                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7PUE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-OCT-21.                  
REMARK 100 THE DEPOSITION ID IS D_1292118102.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-OCT-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
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          : AUTOPROC                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10904                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.510                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.730                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.9                               
REMARK 200  DATA REDUNDANCY                : 8.500                              
REMARK 200  R MERGE                    (I) : 0.07400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 19.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.51                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.77                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 69.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.38800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: BUSTER                                                
REMARK 200 STARTING MODEL: EARLIER IN-HOUSE STRUCTURE                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 25 MM HEPES, 100 MM    
REMARK 280  NACL,1 MM DTT, 5 MM MGCL2 PH 7.8; 3 MM AMPPNP; RESERVOIR            
REMARK 280  SOLUTION: 12% PEG3350, 200 MM NAF; SOAKING IN RES.SOL.+ 10 MM       
REMARK 280  CPD3A, 10% DMSO, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      114.68867            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       57.34433            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       86.01650            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       28.67217            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      143.36083            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      114.68867            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       57.34433            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       28.67217            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       86.01650            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      143.36083            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 450 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 13830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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     GLY A    57                                                      
REMARK 465     ALA A    58                                                      
REMARK 465     MET A    59                                                      
REMARK 465     ILE A    60                                                      
REMARK 465     SER A    61                                                      
REMARK 465     GLN A    62                                                      
REMARK 465     PRO A    63                                                      
REMARK 465     GLN A    64                                                      
REMARK 465     GLU A    65                                                      
REMARK 465     PRO A    66                                                      
REMARK 465     GLU A    67                                                      
REMARK 465     LEU A    68                                                      
REMARK 465     MET A    69                                                      
REMARK 465     ASN A    70                                                      
REMARK 465     ALA A    71                                                      
REMARK 465     ASN A    72                                                      
REMARK 465     PRO A    73                                                      
REMARK 465     SER A    74                                                      
REMARK 465     PRO A    75                                                      
REMARK 465     PRO A    76                                                      
REMARK 465     PRO A    77                                                      
REMARK 465     SER A    78                                                      
REMARK 465     PRO A    79                                                      
REMARK 465     SER A    80                                                      
REMARK 465     GLN A    81                                                      
REMARK 465     SER A   108                                                      
REMARK 465     PHE A   109                                                      
REMARK 465     LEU A   135                                                      
REMARK 465     LYS A   136                                                      
REMARK 465     LYS A   137                                                      
REMARK 465     LYS A   138                                                      
REMARK 465     GLU A   139                                                      
REMARK 465     GLU A   140                                                      
REMARK 465     LYS A   141                                                      
REMARK 465     HIS A   142                                                      
REMARK 465     ILE A   143                                                      
REMARK 465     MET A   144                                                      
REMARK 465     SER A   145                                                      
REMARK 465     GLU A   146                                                      
REMARK 465     ARG A   147                                                      
REMARK 465     ASN A   148                                                      
REMARK 465     GLU A   246                                                      
REMARK 465     ASN A   247                                                      
REMARK 465     ILE A   248                                                      
REMARK 465     GLU A   249                                                      
REMARK 465     HIS A   250                                                      
REMARK 465     ASN A   251                                                      
REMARK 465     SER A   252                                                      
REMARK 465     THR A   253                                                      
REMARK 465     SER A   377                                                      
REMARK 465     GLY A   378                                                      
REMARK 465     PRO A   379                                                      
REMARK 465     ASN A   380                                                      
REMARK 465     ASP A   381                                                      
REMARK 465     LEU A   382                                                      
REMARK 465     ARG A   383                                                      
REMARK 465     HIS A   384                                                      
REMARK 465     PHE A   385                                                      
REMARK 465     ASP A   386                                                      
REMARK 465     PRO A   387                                                      
REMARK 465     GLU A   388                                                      
REMARK 465     PHE A   389                                                      
REMARK 465     THR A   390                                                      
REMARK 465     GLU A   391                                                      
REMARK 465     GLU A   392                                                      
REMARK 465     PRO A   393                                                      
REMARK 465     VAL A   394                                                      
REMARK 465     PRO A   395                                                      
REMARK 465     ASN A   396                                                      
REMARK 465     SER A   397                                                      
REMARK 465     ILE A   398                                                      
REMARK 465     GLY A   399                                                      
REMARK 465     LYS A   400                                                      
REMARK 465     SER A   401                                                      
REMARK 465     PRO A   402                                                      
REMARK 465     ASP A   403                                                      
REMARK 465     SER A   404                                                      
REMARK 465     VAL A   405                                                      
REMARK 465     LEU A   406                                                      
REMARK 465     VAL A   407                                                      
REMARK 465     THR A   408                                                      
REMARK 465     ALA A   409                                                      
REMARK 465     SER A   410                                                      
REMARK 465     VAL A   411                                                      
REMARK 465     LYS A   412                                                      
REMARK 465     GLU A   413                                                      
REMARK 465     ALA A   414                                                      
REMARK 465     ALA A   415                                                      
REMARK 465     GLU A   416                                                      
REMARK 465     ALA A   417                                                      
REMARK 465     PHE A   418                                                      
REMARK 465     LEU A   419                                                      
REMARK 465     GLY A   420                                                      
REMARK 465     PHE A   421                                                      
REMARK 465     ASP A   422                                                      
REMARK 465     TYR A   423                                                      
REMARK 465     ALA A   424                                                      
REMARK 465     PRO A   425                                                      
REMARK 465     PRO A   426                                                      
REMARK 465     THR A   427                                                      
REMARK 465     ASP A   428                                                      
REMARK 465     SER A   429                                                      
REMARK 465     PHE A   430                                                      
REMARK 465     LEU A   431                                                      
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     LYS A  94    CG   CD   CE   NZ                                   
REMARK 470     LYS A 106    CG   CD   CE   NZ                                   
REMARK 470     GLU A 120    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 121    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 131    CG   CD   CE   NZ                                   
REMARK 470     LYS A 132    CG   CD   CE   NZ                                   
REMARK 470     VAL A 149    CG1  CG2                                            
REMARK 470     LEU A 150    CG   CD1  CD2                                       
REMARK 470     GLN A 233    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 245    CG   CD   CE   NZ                                   
REMARK 470     LYS A 343    CG   CD   CE   NZ                                   
REMARK 470     ASN A 375    CG   OD1  ND2                                       
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    LEU A  85       13.29     59.05                                   
REMARK 500    LEU A 101      -74.56    -66.89                                   
REMARK 500    LYS A 118       43.74    -90.04                                   
REMARK 500    ALA A 119      125.71   -171.33                                   
REMARK 500    GLU A 121       48.11     24.31                                   
REMARK 500    LEU A 129      -63.86   -105.25                                   
REMARK 500    GLN A 130      111.66    108.62                                   
REMARK 500    LYS A 131      -55.41    -29.59                                   
REMARK 500    LYS A 132       83.70    -66.15                                   
REMARK 500    ALA A 133       34.97   -159.59                                   
REMARK 500    LEU A 151     -128.68     48.38                                   
REMARK 500    LYS A 152        8.43     56.62                                   
REMARK 500    ALA A 169       29.55    140.14                                   
REMARK 500    ASP A 170      -33.03   -177.92                                   
REMARK 500    ALA A 192      -47.92     70.64                                   
REMARK 500    ARG A 221      -47.28     67.78                                   
REMARK 500    ASP A 222       43.04   -104.20                                   
REMARK 500    PHE A 241       38.15    -96.18                                   
REMARK 500    CYS A 258      -99.42     61.89                                   
REMARK 500    HIS A 270       40.55    -99.97                                   
REMARK 500    LYS A 271       66.45     36.14                                   
REMARK 500    ASP A 275     -153.08   -140.72                                   
REMARK 500    LEU A 332       41.47    -95.94                                   
REMARK 500    ASP A 345     -132.14     45.54                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  7PUE A   60   431  UNP    O00141   SGK1_HUMAN      60    431             
SEQADV 7PUE GLY A   57  UNP  O00141              EXPRESSION TAG                 
SEQADV 7PUE ALA A   58  UNP  O00141              EXPRESSION TAG                 
SEQADV 7PUE MET A   59  UNP  O00141              EXPRESSION TAG                 
SEQADV 7PUE ALA A  192  UNP  O00141    ARG   192 ENGINEERED MUTATION            
SEQADV 7PUE ASP A  422  UNP  O00141    SER   422 ENGINEERED MUTATION            
SEQRES   1 A  375  GLY ALA MET ILE SER GLN PRO GLN GLU PRO GLU LEU MET          
SEQRES   2 A  375  ASN ALA ASN PRO SER PRO PRO PRO SER PRO SER GLN GLN          
SEQRES   3 A  375  ILE ASN LEU GLY PRO SER SER ASN PRO HIS ALA LYS PRO          
SEQRES   4 A  375  SER ASP PHE HIS PHE LEU LYS VAL ILE GLY LYS GLY SER          
SEQRES   5 A  375  PHE GLY LYS VAL LEU LEU ALA ARG HIS LYS ALA GLU GLU          
SEQRES   6 A  375  VAL PHE TYR ALA VAL LYS VAL LEU GLN LYS LYS ALA ILE          
SEQRES   7 A  375  LEU LYS LYS LYS GLU GLU LYS HIS ILE MET SER GLU ARG          
SEQRES   8 A  375  ASN VAL LEU LEU LYS ASN VAL LYS HIS PRO PHE LEU VAL          
SEQRES   9 A  375  GLY LEU HIS PHE SER PHE GLN THR ALA ASP LYS LEU TYR          
SEQRES  10 A  375  PHE VAL LEU ASP TYR ILE ASN GLY GLY GLU LEU PHE TYR          
SEQRES  11 A  375  HIS LEU GLN ARG GLU ALA CYS PHE LEU GLU PRO ARG ALA          
SEQRES  12 A  375  ARG PHE TYR ALA ALA GLU ILE ALA SER ALA LEU GLY TYR          
SEQRES  13 A  375  LEU HIS SER LEU ASN ILE VAL TYR ARG ASP LEU LYS PRO          
SEQRES  14 A  375  GLU ASN ILE LEU LEU ASP SER GLN GLY HIS ILE VAL LEU          
SEQRES  15 A  375  THR ASP PHE GLY LEU CYS LYS GLU ASN ILE GLU HIS ASN          
SEQRES  16 A  375  SER THR THR SER THR PHE CYS GLY THR PRO GLU TYR LEU          
SEQRES  17 A  375  ALA PRO GLU VAL LEU HIS LYS GLN PRO TYR ASP ARG THR          
SEQRES  18 A  375  VAL ASP TRP TRP CYS LEU GLY ALA VAL LEU TYR GLU MET          
SEQRES  19 A  375  LEU TYR GLY LEU PRO PRO PHE TYR SER ARG ASN THR ALA          
SEQRES  20 A  375  GLU MET TYR ASP ASN ILE LEU ASN LYS PRO LEU GLN LEU          
SEQRES  21 A  375  LYS PRO ASN ILE THR ASN SER ALA ARG HIS LEU LEU GLU          
SEQRES  22 A  375  GLY LEU LEU GLN LYS ASP ARG THR LYS ARG LEU GLY ALA          
SEQRES  23 A  375  LYS ASP ASP PHE MET GLU ILE LYS SER HIS VAL PHE PHE          
SEQRES  24 A  375  SER LEU ILE ASN TRP ASP ASP LEU ILE ASN LYS LYS ILE          
SEQRES  25 A  375  THR PRO PRO PHE ASN PRO ASN VAL SER GLY PRO ASN ASP          
SEQRES  26 A  375  LEU ARG HIS PHE ASP PRO GLU PHE THR GLU GLU PRO VAL          
SEQRES  27 A  375  PRO ASN SER ILE GLY LYS SER PRO ASP SER VAL LEU VAL          
SEQRES  28 A  375  THR ALA SER VAL LYS GLU ALA ALA GLU ALA PHE LEU GLY          
SEQRES  29 A  375  PHE ASP TYR ALA PRO PRO THR ASP SER PHE LEU                  
HET    GOL  A 501       6                                                       
HET    GOL  A 502       6                                                       
HET    86H  A 503      35                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     86H 6-[4-[[2,3-BIS(CHLORANYL)PHENYL]SULFONYLAMINO]PHENYL]-           
HETNAM   2 86H  ~{N}-[(3~{R})-PYRROLIDIN-3-YL]-2~{H}-PYRAZOLO[3,4-              
HETNAM   3 86H  B]PYRIDINE-4-CARBOXAMIDE                                        
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  GOL    2(C3 H8 O3)                                                  
FORMUL   4  86H    C23 H20 CL2 N6 O3 S                                          
FORMUL   5  HOH   *24(H2 O)                                                     
HELIX    1 AA1 LYS A   94  SER A   96  5                                   3    
HELIX    2 AA2 GLU A  183  ALA A  192  1                                  10    
HELIX    3 AA3 LEU A  195  LEU A  216  1                                  22    
HELIX    4 AA4 LYS A  224  GLU A  226  5                                   3    
HELIX    5 AA5 ALA A  265  HIS A  270  1                                   6    
HELIX    6 AA6 ARG A  276  GLY A  293  1                                  18    
HELIX    7 AA7 ASN A  301  LYS A  312  1                                  12    
HELIX    8 AA8 THR A  321  LEU A  332  1                                  12    
HELIX    9 AA9 ASP A  345  HIS A  352  1                                   8    
HELIX   10 AB1 VAL A  353  SER A  356  5                                   4    
HELIX   11 AB2 ASN A  359  ASN A  365  1                                   7    
SHEET    1 AA1 5 PHE A  98  GLY A 105  0                                        
SHEET    2 AA1 5 LYS A 111  HIS A 117 -1  O  LEU A 114   N  LYS A 102           
SHEET    3 AA1 5 PHE A 123  VAL A 128 -1  O  TYR A 124   N  ALA A 115           
SHEET    4 AA1 5 LEU A 172  ASP A 177 -1  O  LEU A 176   N  ALA A 125           
SHEET    5 AA1 5 LEU A 162  GLN A 167 -1  N  HIS A 163   O  VAL A 175           
SHEET    1 AA2 2 ILE A 228  LEU A 230  0                                        
SHEET    2 AA2 2 ILE A 236  LEU A 238 -1  O  VAL A 237   N  LEU A 229           
CRYST1   92.445   92.445  172.033  90.00  90.00 120.00 P 65 2 2     12          
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      0.010817  0.006245  0.000000        0.00000                         
SCALE2      0.000000  0.012491  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005813        0.00000                         
ATOM      1  N   GLN A  82     -31.606  56.423   2.991  1.00157.28           N  
ANISOU    1  N   GLN A  82    33283   6957  19520   4509  -1182    118       N  
ATOM      2  CA  GLN A  82     -32.596  56.194   1.942  1.00157.90           C  
ANISOU    2  CA  GLN A  82    33064   7287  19643   5013  -1189    450       C  
ATOM      3  C   GLN A  82     -31.956  55.590   0.683  1.00158.16           C  
ANISOU    3  C   GLN A  82    32782   7654  19656   4434  -1216    916       C  
ATOM      4  O   GLN A  82     -31.829  56.255  -0.344  1.00158.24           O  
ANISOU    4  O   GLN A  82    33182   7244  19698   4344  -1372   1285       O  
ATOM      5  CB  GLN A  82     -33.392  57.485   1.636  1.00159.63           C  
ANISOU    5  CB  GLN A  82    33770   6832  20049   5596  -1339    513       C  
ATOM      6  CG  GLN A  82     -34.592  57.330   0.684  1.00163.05           C  
ANISOU    6  CG  GLN A  82    33552   7686  20714   6141  -1330    814       C  
ATOM      7  CD  GLN A  82     -35.637  56.334   1.137  1.00167.62           C  
ANISOU    7  CD  GLN A  82    33383   9045  21259   6672  -1143    627       C  
ATOM      8  OE1 GLN A  82     -35.910  56.163   2.332  1.00169.24           O  
ANISOU    8  OE1 GLN A  82    33303   9482  21519   6846   -965    215       O  
ATOM      9  NE2 GLN A  82     -36.261  55.659   0.180  1.00168.10           N  
ANISOU    9  NE2 GLN A  82    33246   9474  21151   6991  -1199    932       N  
ATOM     10  N   ILE A  83     -31.529  54.326   0.776  1.00158.08           N  
ANISOU   10  N   ILE A  83    32088   8397  19578   4047  -1058    897       N  
ATOM     11  CA  ILE A  83     -30.934  53.616  -0.362  1.00158.41           C  
ANISOU   11  CA  ILE A  83    31760   8858  19571   3538  -1045   1285       C  
ATOM     12  C   ILE A  83     -32.041  53.235  -1.352  1.00158.35           C  
ANISOU   12  C   ILE A  83    31397   9209  19561   4079  -1071   1545       C  
ATOM     13  O   ILE A  83     -33.100  52.802  -0.917  1.00158.57           O  
ANISOU   13  O   ILE A  83    31019   9619  19614   4645   -991   1355       O  
ATOM     14  CB  ILE A  83     -30.074  52.401   0.082  1.00158.93           C  
ANISOU   14  CB  ILE A  83    31243   9576  19568   2988   -880   1144       C  
ATOM     15  CG1 ILE A  83     -30.728  51.615   1.246  1.00160.12           C  
ANISOU   15  CG1 ILE A  83    30913  10224  19701   3411   -722    763       C  
ATOM     16  CG2 ILE A  83     -28.665  52.855   0.436  1.00159.32           C  
ANISOU   16  CG2 ILE A  83    31663   9253  19617   2266   -923   1063       C  
ATOM     17  CD1 ILE A  83     -29.944  50.399   1.739  1.00161.62           C  
ANISOU   17  CD1 ILE A  83    30538  11049  19823   2956   -575    640       C  
ATOM     18  N   ASN A  84     -31.827  53.416  -2.672  1.00157.31           N  
ANISOU   18  N   ASN A  84    31420   8959  19391   3914  -1189   1983       N  
ATOM     19  CA  ASN A  84     -32.876  53.123  -3.662  1.00156.60           C  
ANISOU   19  CA  ASN A  84    31051   9170  19282   4428  -1268   2240       C  
ATOM     20  C   ASN A  84     -33.376  51.661  -3.663  1.00155.49           C  
ANISOU   20  C   ASN A  84    30052   9923  19103   4539  -1141   2161       C  
ATOM     21  O   ASN A  84     -34.472  51.415  -4.167  1.00155.82           O  
ANISOU   21  O   ASN A  84    29813  10225  19167   5087  -1215   2257       O  
ATOM     22  CB  ASN A  84     -32.497  53.563  -5.084  1.00157.87           C  
ANISOU   22  CB  ASN A  84    31538   9092  19355   4176  -1414   2735       C  
ATOM     23  CG  ASN A  84     -31.059  53.356  -5.486  1.00161.08           C  
ANISOU   23  CG  ASN A  84    31984   9558  19660   3312  -1336   2925       C  
ATOM     24  OD1 ASN A  84     -30.431  54.248  -6.070  1.00162.50           O  
ANISOU   24  OD1 ASN A  84    32727   9202  19813   2972  -1425   3212       O  
ATOM     25  ND2 ASN A  84     -30.506  52.181  -5.204  1.00161.45           N  
ANISOU   25  ND2 ASN A  84    31432  10261  19653   2940  -1164   2788       N  
ATOM     26  N   LEU A  85     -32.592  50.715  -3.104  1.00153.93           N  
ANISOU   26  N   LEU A  85    29454  10175  18859   4027   -973   1996       N  
ATOM     27  CA  LEU A  85     -32.942  49.296  -2.965  1.00153.24           C  
ANISOU   27  CA  LEU A  85    28597  10884  18745   4060   -849   1897       C  
ATOM     28  C   LEU A  85     -33.245  48.540  -4.274  1.00152.11           C  
ANISOU   28  C   LEU A  85    28098  11181  18514   4049   -927   2225       C  
ATOM     29  O   LEU A  85     -33.762  47.423  -4.223  1.00152.34           O  
ANISOU   29  O   LEU A  85    27521  11819  18544   4176   -871   2153       O  
ATOM     30  CB  LEU A  85     -34.114  49.108  -1.985  1.00153.48           C  
ANISOU   30  CB  LEU A  85    28326  11119  18870   4699   -777   1595       C  
ATOM     31  CG  LEU A  85     -33.756  48.735  -0.553  1.00155.00           C  
ANISOU   31  CG  LEU A  85    28360  11467  19068   4563   -589   1202       C  
ATOM     32  CD1 LEU A  85     -35.000  48.637   0.307  1.00155.54           C  
ANISOU   32  CD1 LEU A  85    28187  11705  19208   5246   -499    949       C  
ATOM     33  CD2 LEU A  85     -33.004  47.423  -0.504  1.00155.69           C  
ANISOU   33  CD2 LEU A  85    27904  12166  19087   4052   -469   1189       C  
ATOM     34  N   GLY A  86     -32.912  49.127  -5.415  1.00150.73           N  
ANISOU   34  N   GLY A  86    28316  10701  18255   3881  -1057   2579       N  
ATOM     35  CA  GLY A  86     -33.157  48.491  -6.701  1.00149.93           C  
ANISOU   35  CA  GLY A  86    27959  10984  18022   3870  -1148   2890       C  
ATOM     36  C   GLY A  86     -34.613  48.506  -7.123  1.00148.91           C  
ANISOU   36  C   GLY A  86    27659  10981  17939   4567  -1322   2972       C  
ATOM     37  O   GLY A  86     -35.421  49.263  -6.584  1.00148.82           O  
ANISOU   37  O   GLY A  86    27837  10645  18062   5099  -1384   2857       O  
ATOM     38  N   PRO A  87     -34.982  47.652  -8.089  1.00148.06           N  
ANISOU   38  N   PRO A  87    27176  11362  17718   4591  -1413   3162       N  
ATOM     39  CA  PRO A  87     -36.374  47.646  -8.570  1.00147.43           C  
ANISOU   39  CA  PRO A  87    26895  11437  17682   5231  -1623   3264       C  
ATOM     40  C   PRO A  87     -37.345  46.769  -7.778  1.00146.47           C  
ANISOU   40  C   PRO A  87    26113  11821  17718   5597  -1570   2986       C  
ATOM     41  O   PRO A  87     -38.550  46.857  -8.000  1.00146.73           O  
ANISOU   41  O   PRO A  87    25948  11968  17834   6162  -1736   3041       O  
ATOM     42  CB  PRO A  87     -36.247  47.196 -10.029  1.00148.27           C  
ANISOU   42  CB  PRO A  87    26958  11813  17566   5042  -1772   3599       C  
ATOM     43  CG  PRO A  87     -34.908  46.494 -10.118  1.00148.91           C  
ANISOU   43  CG  PRO A  87    26935  12134  17511   4340  -1570   3567       C  
ATOM     44  CD  PRO A  87     -34.143  46.698  -8.835  1.00147.47           C  
ANISOU   44  CD  PRO A  87    26870  11705  17457   4050  -1347   3295       C  
ATOM     45  N   SER A  88     -36.841  45.946  -6.848  1.00145.13           N  
ANISOU   45  N   SER A  88    25594  11959  17591   5281  -1344   2706       N  
ATOM     46  CA  SER A  88     -37.692  45.116  -5.993  1.00144.33           C  
ANISOU   46  CA  SER A  88    24877  12331  17632   5563  -1255   2454       C  
ATOM     47  C   SER A  88     -38.514  45.942  -4.973  1.00143.92           C  
ANISOU   47  C   SER A  88    24927  12008  17748   6116  -1187   2240       C  
ATOM     48  O   SER A  88     -39.337  45.379  -4.258  1.00144.05           O  
ANISOU   48  O   SER A  88    24447  12407  17879   6387  -1082   2043       O  
ATOM     49  CB  SER A  88     -36.834  44.103  -5.241  1.00144.86           C  
ANISOU   49  CB  SER A  88    24620  12749  17670   5048  -1033   2242       C  
ATOM     50  OG  SER A  88     -35.743  44.725  -4.580  1.00146.12           O  
ANISOU   50  OG  SER A  88    25201  12517  17801   4692   -886   2117       O  
ATOM     51  N   SER A  89     -38.286  47.263  -4.909  1.00143.25           N  
ANISOU   51  N   SER A  89    25494  11264  17670   6278  -1240   2280       N  
ATOM     52  CA  SER A  89     -38.895  48.201  -3.982  1.00143.11           C  
ANISOU   52  CA  SER A  89    25715  10881  17779   6799  -1177   2061       C  
ATOM     53  C   SER A  89     -40.388  48.378  -4.103  1.00142.88           C  
ANISOU   53  C   SER A  89    25399  11010  17881   7571  -1289   2094       C  
ATOM     54  O   SER A  89     -40.903  48.644  -5.184  1.00142.95           O  
ANISOU   54  O   SER A  89    25453  10985  17878   7816  -1534   2384       O  
ATOM     55  CB  SER A  89     -38.221  49.562  -4.096  1.00144.43           C  
ANISOU   55  CB  SER A  89    26719  10245  17913   6714  -1248   2126       C  
ATOM     56  OG  SER A  89     -36.811  49.434  -4.038  1.00146.79           O  
ANISOU   56  OG  SER A  89    27254  10416  18102   5964  -1165   2140       O  
ATOM     57  N   ASN A  90     -41.075  48.282  -2.967  1.00142.56           N  
ANISOU   57  N   ASN A  90    25072  11141  17953   7969  -1107   1801       N  
ATOM     58  CA  ASN A  90     -42.507  48.502  -2.872  1.00142.69           C  
ANISOU   58  CA  ASN A  90    24767  11335  18116   8747  -1160   1790       C  
ATOM     59  C   ASN A  90     -42.654  49.788  -2.089  1.00142.71           C  
ANISOU   59  C   ASN A  90    25333  10727  18165   9222  -1086   1584       C  
ATOM     60  O   ASN A  90     -42.580  49.784  -0.864  1.00142.71           O  
ANISOU   60  O   ASN A  90    25300  10755  18169   9286   -834   1254       O  
ATOM     61  CB  ASN A  90     -43.186  47.350  -2.134  1.00143.81           C  
ANISOU   61  CB  ASN A  90    24088  12215  18340   8823   -965   1617       C  
ATOM     62  CG  ASN A  90     -44.694  47.419  -2.145  1.00146.71           C  
ANISOU   62  CG  ASN A  90    23970  12902  18873   9569  -1018   1649       C  
ATOM     63  OD1 ASN A  90     -45.291  48.428  -2.535  1.00147.95           O  
ANISOU   63  OD1 ASN A  90    24416  12704  19093  10139  -1186   1754       O  
ATOM     64  ND2 ASN A  90     -45.348  46.356  -1.694  1.00147.18           N  
ANISOU   64  ND2 ASN A  90    23264  13640  19016   9586   -879   1571       N  
ATOM     65  N   PRO A  91     -42.838  50.916  -2.783  1.00142.76           N  
ANISOU   65  N   PRO A  91    25907  10148  18187   9563  -1314   1774       N  
ATOM     66  CA  PRO A  91     -42.961  52.202  -2.074  1.00143.04           C  
ANISOU   66  CA  PRO A  91    26568   9514  18268  10033  -1271   1568       C  
ATOM     67  C   PRO A  91     -44.214  52.351  -1.200  1.00143.61           C  
ANISOU   67  C   PRO A  91    26283   9816  18467  10859  -1123   1322       C  
ATOM     68  O   PRO A  91     -44.377  53.368  -0.519  1.00143.94           O  
ANISOU   68  O   PRO A  91    26822   9339  18529  11300  -1055   1093       O  
ATOM     69  CB  PRO A  91     -42.911  53.240  -3.204  1.00143.48           C  
ANISOU   69  CB  PRO A  91    27270   8934  18314  10180  -1586   1903       C  
ATOM     70  CG  PRO A  91     -42.458  52.490  -4.428  1.00143.76           C  
ANISOU   70  CG  PRO A  91    27104   9278  18241   9605  -1744   2258       C  
ATOM     71  CD  PRO A  91     -42.935  51.094  -4.241  1.00142.24           C  
ANISOU   71  CD  PRO A  91    25997   9969  18079   9537  -1629   2185       C  
ATOM     72  N   HIS A  92     -45.098  51.346  -1.211  1.00143.54           N  
ANISOU   72  N   HIS A  92    25415  10582  18540  11066  -1068   1365       N  
ATOM     73  CA  HIS A  92     -46.313  51.368  -0.402  1.00143.82           C  
ANISOU   73  CA  HIS A  92    24986  10959  18701  11817   -890   1162       C  
ATOM     74  C   HIS A  92     -46.162  50.494   0.849  1.00143.64           C  
ANISOU   74  C   HIS A  92    24528  11421  18629  11577   -518    842       C  
ATOM     75  O   HIS A  92     -46.824  50.753   1.848  1.00144.24           O  
ANISOU   75  O   HIS A  92    24463  11602  18738  12131   -282    582       O  
ATOM     76  CB  HIS A  92     -47.538  50.912  -1.217  1.00144.50           C  
ANISOU   76  CB  HIS A  92    24353  11617  18933  12236  -1071   1426       C  
ATOM     77  CG  HIS A  92     -47.584  51.468  -2.605  1.00146.56           C  
ANISOU   77  CG  HIS A  92    24937  11550  19200  12335  -1471   1798       C  
ATOM     78  ND1 HIS A  92     -47.083  50.753  -3.683  1.00148.49           N  
ANISOU   78  ND1 HIS A  92    25011  12044  19366  11759  -1686   2090       N  
ATOM     79  CD2 HIS A  92     -48.035  52.666  -3.042  1.00147.35           C  
ANISOU   79  CD2 HIS A  92    25546  11089  19352  12952  -1685   1918       C  
ATOM     80  CE1 HIS A  92     -47.259  51.532  -4.738  1.00148.97           C  
ANISOU   80  CE1 HIS A  92    25472  11714  19415  12032  -2017   2387       C  
ATOM     81  NE2 HIS A  92     -47.831  52.693  -4.402  1.00148.53           N  
ANISOU   81  NE2 HIS A  92    25834  11154  19447  12745  -2037   2308       N  
ATOM     82  N   ALA A  93     -45.312  49.466   0.800  1.00142.81           N  
ANISOU   82  N   ALA A  93    24205  11625  18432  10790   -458    868       N  
ATOM     83  CA  ALA A  93     -45.122  48.572   1.925  1.00142.53           C  
ANISOU   83  CA  ALA A  93    23756  12060  18337  10525   -134    611       C  
ATOM     84  C   ALA A  93     -44.504  49.251   3.144  1.00142.05           C  
ANISOU   84  C   ALA A  93    24257  11569  18146  10518     90    241       C  
ATOM     85  O   ALA A  93     -43.623  50.101   3.032  1.00141.97           O  
ANISOU   85  O   ALA A  93    25004  10881  18057  10291    -25    197       O  
ATOM     86  CB  ALA A  93     -44.298  47.369   1.509  1.00142.57           C  
ANISOU   86  CB  ALA A  93    23428  12461  18283   9716   -164    747       C  
ATOM     87  N   LYS A  94     -45.020  48.880   4.307  1.00141.56           N  
ANISOU   87  N   LYS A  94    23811  11921  18054  10770    406    -17       N  
ATOM     88  CA  LYS A  94     -44.599  49.321   5.632  1.00141.66           C  
ANISOU   88  CA  LYS A  94    24230  11689  17907  10816    658   -406       C  
ATOM     89  C   LYS A  94     -44.718  48.095   6.561  1.00141.28           C  
ANISOU   89  C   LYS A  94    23516  12380  17786  10604    972   -531       C  
ATOM     90  O   LYS A  94     -45.559  47.228   6.305  1.00141.27           O  
ANISOU   90  O   LYS A  94    22751  13019  17906  10732   1028   -356       O  
ATOM     91  CB  LYS A  94     -45.496  50.474   6.123  1.00143.78           C  
ANISOU   91  CB  LYS A  94    24835  11595  18199  11714    733   -612       C  
ATOM     92  N   PRO A  95     -43.892  47.967   7.626  1.00140.85           N  
ANISOU   92  N   PRO A  95    23728  12256  17533  10258   1161   -814       N  
ATOM     93  CA  PRO A  95     -43.988  46.765   8.486  1.00140.87           C  
ANISOU   93  CA  PRO A  95    23120  12954  17449  10038   1449   -893       C  
ATOM     94  C   PRO A  95     -45.370  46.503   9.090  1.00141.25           C  
ANISOU   94  C   PRO A  95    22545  13568  17554  10706   1730   -933       C  
ATOM     95  O   PRO A  95     -45.652  45.379   9.496  1.00141.21           O  
ANISOU   95  O   PRO A  95    21879  14223  17552  10511   1918   -860       O  
ATOM     96  CB  PRO A  95     -42.912  46.981   9.559  1.00141.26           C  
ANISOU   96  CB  PRO A  95    23712  12712  17250   9710   1572  -1225       C  
ATOM     97  CG  PRO A  95     -42.512  48.399   9.452  1.00141.57           C  
ANISOU   97  CG  PRO A  95    24617  11914  17260   9880   1386  -1368       C  
ATOM     98  CD  PRO A  95     -42.815  48.870   8.068  1.00140.11           C  
ANISOU   98  CD  PRO A  95    24495  11455  17284  10004   1090  -1050       C  
ATOM     99  N   SER A  96     -46.245  47.521   9.087  1.00141.32           N  
ANISOU   99  N   SER A  96    22745  13325  17625  11492   1751  -1022       N  
ATOM    100  CA  SER A  96     -47.627  47.450   9.562  1.00141.80           C  
ANISOU  100  CA  SER A  96    22220  13896  17760  12229   2014  -1049       C  
ATOM    101  C   SER A  96     -48.466  46.437   8.741  1.00142.35           C  
ANISOU  101  C   SER A  96    21378  14635  18073  12164   1931   -679       C  
ATOM    102  O   SER A  96     -49.454  45.919   9.257  1.00142.88           O  
ANISOU  102  O   SER A  96    20754  15340  18195  12491   2200   -661       O  
ATOM    103  CB  SER A  96     -48.278  48.833   9.506  1.00142.52           C  
ANISOU  103  CB  SER A  96    22761  13488  17901  13080   1967  -1180       C  
ATOM    104  OG  SER A  96     -47.424  49.858   9.991  1.00144.03           O  
ANISOU  104  OG  SER A  96    23911  12905  17910  13070   1917  -1481       O  
ATOM    105  N   ASP A  97     -48.066  46.144   7.479  1.00141.99           N  
ANISOU  105  N   ASP A  97    21332  14458  18160  11727   1563   -386       N  
ATOM    106  CA  ASP A  97     -48.740  45.189   6.581  1.00142.13           C  
ANISOU  106  CA  ASP A  97    20572  15039  18392  11595   1406    -45       C  
ATOM    107  C   ASP A  97     -48.542  43.713   6.975  1.00141.77           C  
ANISOU  107  C   ASP A  97    19919  15625  18323  10984   1565     22       C  
ATOM    108  O   ASP A  97     -48.987  42.835   6.236  1.00141.95           O  
ANISOU  108  O   ASP A  97    19358  16065  18511  10750   1399    291       O  
ATOM    109  CB  ASP A  97     -48.200  45.338   5.144  1.00144.05           C  
ANISOU  109  CB  ASP A  97    21115  14906  18711  11253    966    215       C  
ATOM    110  CG  ASP A  97     -48.525  46.639   4.446  1.00148.75           C  
ANISOU  110  CG  ASP A  97    22168  14964  19387  11839    724    282       C  
ATOM    111  OD1 ASP A  97     -49.371  47.397   4.968  1.00149.68           O  
ANISOU  111  OD1 ASP A  97    22288  15038  19546  12598    877    137       O  
ATOM    112  OD2 ASP A  97     -47.945  46.893   3.364  1.00150.74           O  
ANISOU  112  OD2 ASP A  97    22776  14846  19652  11559    386    490       O  
ATOM    113  N   PHE A  98     -47.833  43.431   8.075  1.00140.95           N  
ANISOU  113  N   PHE A  98    19988  15556  18009  10701   1847   -212       N  
ATOM    114  CA  PHE A  98     -47.544  42.060   8.467  1.00140.64           C  
ANISOU  114  CA  PHE A  98    19464  16041  17931  10108   1981   -141       C  
ATOM    115  C   PHE A  98     -47.845  41.778   9.937  1.00140.49           C  
ANISOU  115  C   PHE A  98    19252  16384  17743  10278   2426   -356       C  
ATOM    116  O   PHE A  98     -47.960  42.698  10.752  1.00140.67           O  
ANISOU  116  O   PHE A  98    19682  16156  17611  10759   2628   -629       O  
ATOM    117  CB  PHE A  98     -46.051  41.756   8.210  1.00140.37           C  
ANISOU  117  CB  PHE A  98    19907  15658  17768   9344   1800   -153       C  
ATOM    118  CG  PHE A  98     -45.595  41.830   6.774  1.00140.74           C  
ANISOU  118  CG  PHE A  98    20123  15422  17930   9040   1398     81       C  
ATOM    119  CD1 PHE A  98     -45.753  40.750   5.924  1.00141.34           C  
ANISOU  119  CD1 PHE A  98    19689  15885  18127   8622   1229    336       C  
ATOM    120  CD2 PHE A  98     -44.958  42.959   6.290  1.00141.37           C  
ANISOU  120  CD2 PHE A  98    20912  14832  17969   9137   1191     43       C  
ATOM    121  CE1 PHE A  98     -45.321  40.814   4.607  1.00141.94           C  
ANISOU  121  CE1 PHE A  98    19950  15720  18259   8355    875    539       C  
ATOM    122  CE2 PHE A  98     -44.522  43.017   4.974  1.00141.93           C  
ANISOU  122  CE2 PHE A  98    21152  14668  18109   8844    848    279       C  
ATOM    123  CZ  PHE A  98     -44.711  41.948   4.141  1.00141.71           C  
ANISOU  123  CZ  PHE A  98    20604  15065  18174   8472    700    519       C  
ATOM    124  N   HIS A  99     -47.927  40.487  10.281  1.00139.83           N  
ANISOU  124  N   HIS A  99    18587  16873  17669   9861   2572   -233       N  
ATOM    125  CA  HIS A  99     -48.076  40.027  11.650  1.00139.46           C  
ANISOU  125  CA  HIS A  99    18352  17208  17427   9884   2988   -385       C  
ATOM    126  C   HIS A  99     -46.811  39.198  11.874  1.00137.91           C  
ANISOU  126  C   HIS A  99    18388  16932  17078   9099   2921   -399       C  
ATOM    127  O   HIS A  99     -46.672  38.146  11.267  1.00137.71           O  
ANISOU  127  O   HIS A  99    17994  17136  17192   8597   2747   -161       O  
ATOM    128  CB  HIS A  99     -49.332  39.155  11.810  1.00140.96           C  
ANISOU  128  CB  HIS A  99    17610  18161  17787  10031   3202   -165       C  
ATOM    129  CG  HIS A  99     -50.555  39.909  12.230  1.00144.39           C  
ANISOU  129  CG  HIS A  99    17762  18816  18281  10867   3445   -226       C  
ATOM    130  ND1 HIS A  99     -51.774  39.718  11.597  1.00146.64           N  
ANISOU  130  ND1 HIS A  99    17337  19508  18872  11166   3362     28       N  
ATOM    131  CD2 HIS A  99     -50.715  40.824  13.217  1.00146.00           C  
ANISOU  131  CD2 HIS A  99    18293  18908  18272  11461   3764   -518       C  
ATOM    132  CE1 HIS A  99     -52.633  40.521  12.214  1.00147.27           C  
ANISOU  132  CE1 HIS A  99    17302  19726  18928  11946   3646   -105       C  
ATOM    133  NE2 HIS A  99     -52.045  41.211  13.193  1.00147.11           N  
ANISOU  133  NE2 HIS A  99    17911  19394  18591  12165   3903   -442       N  
ATOM    134  N   PHE A 100     -45.864  39.704  12.674  1.00136.60           N  
ANISOU  134  N   PHE A 100    18858  16411  16633   9000   3017   -681       N  
ATOM    135  CA  PHE A 100     -44.592  39.022  12.917  1.00135.77           C  
ANISOU  135  CA  PHE A 100    18997  16213  16377   8291   2935   -709       C  
ATOM    136  C   PHE A 100     -44.666  37.995  14.052  1.00134.17           C  
ANISOU  136  C   PHE A 100    18429  16542  16009   8092   3254   -711       C  
ATOM    137  O   PHE A 100     -44.548  38.342  15.228  1.00134.36           O  
ANISOU  137  O   PHE A 100    18702  16585  15762   8317   3529   -954       O  
ATOM    138  CB  PHE A 100     -43.473  40.036  13.189  1.00136.01           C  
ANISOU  138  CB  PHE A 100    19885  15591  16200   8210   2822   -993       C  
ATOM    139  CG  PHE A 100     -43.350  41.131  12.158  1.00136.99           C  
ANISOU  139  CG  PHE A 100    20449  15139  16463   8416   2532   -987       C  
ATOM    140  CD1 PHE A 100     -42.609  40.941  11.007  1.00137.71           C  
ANISOU  140  CD1 PHE A 100    20604  15014  16704   7970   2195   -776       C  
ATOM    141  CD2 PHE A 100     -43.955  42.362  12.356  1.00138.09           C  
ANISOU  141  CD2 PHE A 100    20958  14945  16565   9074   2603  -1186       C  
ATOM    142  CE1 PHE A 100     -42.490  41.952  10.066  1.00138.51           C  
ANISOU  142  CE1 PHE A 100    21125  14591  16912   8150   1937   -736       C  
ATOM    143  CE2 PHE A 100     -43.838  43.370  11.410  1.00138.82           C  
ANISOU  143  CE2 PHE A 100    21485  14474  16785   9263   2324  -1153       C  
ATOM    144  CZ  PHE A 100     -43.113  43.156  10.267  1.00138.51           C  
ANISOU  144  CZ  PHE A 100    21498  14240  16890   8786   1994   -913       C  
ATOM    145  N   LEU A 101     -44.820  36.725  13.687  1.00132.37           N  
ANISOU  145  N   LEU A 101    17650  16719  15928   7656   3201   -441       N  
ATOM    146  CA  LEU A 101     -44.917  35.613  14.620  1.00131.09           C  
ANISOU  146  CA  LEU A 101    17102  17059  15645   7403   3468   -369       C  
ATOM    147  C   LEU A 101     -43.615  35.332  15.416  1.00129.02           C  
ANISOU  147  C   LEU A 101    17309  16623  15088   6960   3484   -536       C  
ATOM    148  O   LEU A 101     -43.548  35.666  16.598  1.00128.97           O  
ANISOU  148  O   LEU A 101    17541  16669  14793   7171   3756   -750       O  
ATOM    149  CB  LEU A 101     -45.399  34.336  13.883  1.00131.71           C  
ANISOU  149  CB  LEU A 101    16489  17553  16000   7041   3351    -20       C  
ATOM    150  CG  LEU A 101     -46.861  34.264  13.441  1.00133.70           C  
ANISOU  150  CG  LEU A 101    16078  18197  16525   7428   3408    181       C  
ATOM    151  CD1 LEU A 101     -47.051  34.842  12.052  1.00134.19           C  
ANISOU  151  CD1 LEU A 101    16214  17949  16824   7587   3044    252       C  
ATOM    152  CD2 LEU A 101     -47.336  32.820  13.421  1.00134.71           C  
ANISOU  152  CD2 LEU A 101    15520  18842  16821   7016   3431    477       C  
ATOM    153  N   LYS A 102     -42.586  34.735  14.772  1.00127.12           N  
ANISOU  153  N   LYS A 102    17202  16192  14906   6373   3190   -446       N  
ATOM    154  CA  LYS A 102     -41.356  34.311  15.434  1.00125.73           C  
ANISOU  154  CA  LYS A 102    17368  15914  14491   5923   3169   -560       C  
ATOM    155  C   LYS A 102     -40.095  34.798  14.746  1.00123.64           C  
ANISOU  155  C   LYS A 102    17630  15120  14228   5597   2838   -654       C  
ATOM    156  O   LYS A 102     -40.049  34.801  13.524  1.00124.01           O  
ANISOU  156  O   LYS A 102    17608  15006  14502   5478   2586   -506       O  
ATOM    157  CB  LYS A 102     -41.321  32.765  15.423  1.00127.78           C  
ANISOU  157  CB  LYS A 102    17135  16591  14825   5459   3178   -301       C  
ATOM    158  CG  LYS A 102     -40.120  32.133  16.126  1.00131.96           C  
ANISOU  158  CG  LYS A 102    17928  17088  15123   5002   3153   -371       C  
ATOM    159  CD  LYS A 102     -39.758  30.772  15.550  1.00136.26           C  
ANISOU  159  CD  LYS A 102    18140  17807  15827   4482   2981   -118       C  
ATOM    160  CE  LYS A 102     -38.811  30.018  16.457  1.00140.05           C  
ANISOU  160  CE  LYS A 102    18786  18356  16070   4115   3012   -155       C  
ATOM    161  NZ  LYS A 102     -37.692  30.874  16.941  1.00142.19           N  
ANISOU  161  NZ  LYS A 102    19670  18248  16109   4067   2912   -435       N  
ATOM    162  N   VAL A 103     -39.044  35.130  15.517  1.00121.35           N  
ANISOU  162  N   VAL A 103    17837  14592  13677   5412   2829   -883       N  
ATOM    163  CA  VAL A 103     -37.736  35.460  14.947  1.00119.64           C  
ANISOU  163  CA  VAL A 103    18058  13937  13465   5011   2526   -946       C  
ATOM    164  C   VAL A 103     -37.045  34.104  14.633  1.00117.81           C  
ANISOU  164  C   VAL A 103    17517  13948  13297   4454   2406   -740       C  
ATOM    165  O   VAL A 103     -36.641  33.387  15.545  1.00117.90           O  
ANISOU  165  O   VAL A 103    17473  14194  13131   4248   2513   -766       O  
ATOM    166  CB  VAL A 103     -36.885  36.430  15.824  1.00120.00           C  
ANISOU  166  CB  VAL A 103    18755  13606  13236   5019   2515  -1276       C  
ATOM    167  CG1 VAL A 103     -37.058  36.167  17.316  1.00120.48           C  
ANISOU  167  CG1 VAL A 103    18828  13963  12986   5157   2793  -1438       C  
ATOM    168  CG2 VAL A 103     -35.414  36.404  15.430  1.00120.30           C  
ANISOU  168  CG2 VAL A 103    19098  13343  13267   4465   2229  -1294       C  
ATOM    169  N   ILE A 104     -37.013  33.713  13.344  1.00115.99           N  
ANISOU  169  N   ILE A 104    17070  13686  13315   4257   2194   -527       N  
ATOM    170  CA  ILE A 104     -36.507  32.414  12.896  1.00114.62           C  
ANISOU  170  CA  ILE A 104    16589  13732  13230   3798   2074   -332       C  
ATOM    171  C   ILE A 104     -35.008  32.352  12.604  1.00113.39           C  
ANISOU  171  C   ILE A 104    16748  13320  13014   3346   1858   -380       C  
ATOM    172  O   ILE A 104     -34.477  31.256  12.453  1.00113.35           O  
ANISOU  172  O   ILE A 104    16530  13497  13040   2993   1782   -258       O  
ATOM    173  CB  ILE A 104     -37.312  31.938  11.674  1.00114.91           C  
ANISOU  173  CB  ILE A 104    16201  13920  13540   3835   1961    -86       C  
ATOM    174  CG1 ILE A 104     -37.054  32.853  10.459  1.00115.77           C  
ANISOU  174  CG1 ILE A 104    16580  13643  13764   3877   1724    -70       C  
ATOM    175  CG2 ILE A 104     -38.795  31.857  12.022  1.00115.33           C  
ANISOU  175  CG2 ILE A 104    15844  14303  13674   4244   2177    -12       C  
ATOM    176  CD1 ILE A 104     -37.769  32.471   9.165  1.00116.80           C  
ANISOU  176  CD1 ILE A 104    16354  13894  14130   3914   1560    159       C  
ATOM    177  N   GLY A 105     -34.353  33.503  12.523  1.00112.36           N  
ANISOU  177  N   GLY A 105    17105  12777  12811   3359   1761   -550       N  
ATOM    178  CA  GLY A 105     -32.916  33.615  12.277  1.00112.05           C  
ANISOU  178  CA  GLY A 105    17359  12495  12720   2932   1567   -599       C  
ATOM    179  C   GLY A 105     -32.365  34.884  12.897  1.00111.67           C  
ANISOU  179  C   GLY A 105    17861  12057  12512   2987   1544   -856       C  
ATOM    180  O   GLY A 105     -33.096  35.872  12.983  1.00111.81           O  
ANISOU  180  O   GLY A 105    18098  11856  12529   3377   1608   -960       O  
ATOM    181  N   LYS A 106     -31.094  34.892  13.346  1.00111.29           N  
ANISOU  181  N   LYS A 106    18045  11908  12331   2612   1438   -969       N  
ATOM    182  CA  LYS A 106     -30.543  36.093  13.989  1.00111.64           C  
ANISOU  182  CA  LYS A 106    18633  11565  12222   2614   1378  -1232       C  
ATOM    183  C   LYS A 106     -29.049  36.309  13.778  1.00112.03           C  
ANISOU  183  C   LYS A 106    18911  11393  12262   2108   1152  -1260       C  
ATOM    184  O   LYS A 106     -28.297  35.355  13.621  1.00112.37           O  
ANISOU  184  O   LYS A 106    18681  11684  12329   1764   1087  -1137       O  
ATOM    185  CB  LYS A 106     -30.869  36.106  15.494  1.00113.34           C  
ANISOU  185  CB  LYS A 106    18957  11936  12170   2830   1554  -1457       C  
ATOM    186  N   GLY A 107     -28.640  37.571  13.800  1.00112.08           N  
ANISOU  186  N   GLY A 107    19412  10932  12240   2073   1034  -1421       N  
ATOM    187  CA  GLY A 107     -27.251  37.983  13.650  1.00112.74           C  
ANISOU  187  CA  GLY A 107    19738  10771  12328   1580    817  -1454       C  
ATOM    188  C   GLY A 107     -26.954  39.255  14.426  1.00113.33           C  
ANISOU  188  C   GLY A 107    20410  10370  12282   1588    715  -1735       C  
ATOM    189  O   GLY A 107     -27.455  39.456  15.541  1.00113.42           O  
ANISOU  189  O   GLY A 107    20627  10378  12089   1857    804  -1984       O  
ATOM    190  N   GLY A 110     -29.485  42.565  12.654  1.00105.65           N  
ANISOU  190  N   GLY A 110    20413   8105  11624   2795    740  -1740       N  
ATOM    191  CA  GLY A 110     -29.734  41.853  11.403  1.00106.04           C  
ANISOU  191  CA  GLY A 110    20003   8425  11862   2762    754  -1395       C  
ATOM    192  C   GLY A 110     -30.326  40.467  11.593  1.00105.78           C  
ANISOU  192  C   GLY A 110    19348   9031  11811   2878    931  -1300       C  
ATOM    193  O   GLY A 110     -29.587  39.488  11.702  1.00105.90           O  
ANISOU  193  O   GLY A 110    19087   9370  11778   2499    920  -1255       O  
ATOM    194  N   LYS A 111     -31.671  40.371  11.606  1.00105.13           N  
ANISOU  194  N   LYS A 111    19031   9132  11782   3400   1086  -1253       N  
ATOM    195  CA  LYS A 111     -32.378  39.112  11.829  1.00104.92           C  
ANISOU  195  CA  LYS A 111    18415   9692  11758   3521   1260  -1149       C  
ATOM    196  C   LYS A 111     -33.471  38.795  10.789  1.00103.98           C  
ANISOU  196  C   LYS A 111    17904   9767  11838   3818   1285   -902       C  
ATOM    197  O   LYS A 111     -33.843  39.649   9.996  1.00103.87           O  
ANISOU  197  O   LYS A 111    18094   9440  11932   4078   1204   -843       O  
ATOM    198  CB  LYS A 111     -32.951  39.085  13.257  1.00107.36           C  
ANISOU  198  CB  LYS A 111    18746  10184  11861   3842   1480  -1394       C  
ATOM    199  CG  LYS A 111     -34.012  40.141  13.518  1.00112.23           C  
ANISOU  199  CG  LYS A 111    19632  10554  12455   4451   1592  -1554       C  
ATOM    200  CD  LYS A 111     -33.822  40.817  14.886  1.00117.74           C  
ANISOU  200  CD  LYS A 111    20787  11074  12877   4593   1679  -1916       C  
ATOM    201  CE  LYS A 111     -33.824  39.857  16.064  1.00122.13           C  
ANISOU  201  CE  LYS A 111    21068  12126  13210   4526   1872  -1994       C  
ATOM    202  NZ  LYS A 111     -33.766  40.576  17.375  1.00124.64           N  
ANISOU  202  NZ  LYS A 111    21859  12281  13216   4734   1962  -2361       N  
ATOM    203  N   VAL A 112     -33.956  37.547  10.787  1.00103.21           N  
ANISOU  203  N   VAL A 112    17251  10175  11788   3766   1375   -751       N  
ATOM    204  CA  VAL A 112     -34.987  37.027   9.892  1.00103.03           C  
ANISOU  204  CA  VAL A 112    16784  10412  11952   3984   1376   -519       C  
ATOM    205  C   VAL A 112     -36.224  36.700  10.731  1.00103.89           C  
ANISOU  205  C   VAL A 112    16557  10878  12040   4415   1623   -568       C  
ATOM    206  O   VAL A 112     -36.093  36.160  11.823  1.00103.84           O  
ANISOU  206  O   VAL A 112    16476  11103  11876   4355   1792   -686       O  
ATOM    207  CB  VAL A 112     -34.466  35.774   9.138  1.00102.64           C  
ANISOU  207  CB  VAL A 112    16366  10649  11983   3548   1267   -307       C  
ATOM    208  CG1 VAL A 112     -35.492  35.249   8.142  1.00102.77           C  
ANISOU  208  CG1 VAL A 112    15954  10907  12187   3731   1214    -79       C  
ATOM    209  CG2 VAL A 112     -33.140  36.062   8.447  1.00102.76           C  
ANISOU  209  CG2 VAL A 112    16693  10367  11983   3119   1075   -271       C  
ATOM    210  N   LEU A 113     -37.416  37.040  10.245  1.00104.80           N  
ANISOU  210  N   LEU A 113    16466  11052  12302   4854   1648   -468       N  
ATOM    211  CA  LEU A 113     -38.655  36.804  10.988  1.00106.31           C  
ANISOU  211  CA  LEU A 113    16287  11614  12494   5290   1902   -492       C  
ATOM    212  C   LEU A 113     -39.694  36.038  10.167  1.00108.01           C  
ANISOU  212  C   LEU A 113    15892  12208  12939   5395   1865   -226       C  
ATOM    213  O   LEU A 113     -39.658  36.077   8.944  1.00107.97           O  
ANISOU  213  O   LEU A 113    15869  12072  13085   5314   1626    -63       O  
ATOM    214  CB  LEU A 113     -39.266  38.160  11.376  1.00106.36           C  
ANISOU  214  CB  LEU A 113    16650  11315  12448   5865   1998   -686       C  
ATOM    215  CG  LEU A 113     -38.833  38.770  12.689  1.00107.80           C  
ANISOU  215  CG  LEU A 113    17306  11289  12364   5945   2148  -1006       C  
ATOM    216  CD1 LEU A 113     -37.485  39.433  12.570  1.00108.31           C  
ANISOU  216  CD1 LEU A 113    18009  10782  12361   5628   1918  -1131       C  
ATOM    217  CD2 LEU A 113     -39.822  39.811  13.122  1.00108.66           C  
ANISOU  217  CD2 LEU A 113    17521  11341  12425   6636   2349  -1175       C  
ATOM    218  N   LEU A 114     -40.653  35.386  10.833  1.00109.31           N  
ANISOU  218  N   LEU A 114    15566  12845  13123   5581   2096   -178       N  
ATOM    219  CA  LEU A 114     -41.762  34.739  10.143  1.00111.06           C  
ANISOU  219  CA  LEU A 114    15179  13440  13580   5703   2058     65       C  
ATOM    220  C   LEU A 114     -42.919  35.725  10.246  1.00113.37           C  
ANISOU  220  C   LEU A 114    15415  13719  13940   6369   2170     17       C  
ATOM    221  O   LEU A 114     -43.236  36.175  11.347  1.00113.55           O  
ANISOU  221  O   LEU A 114    15539  13794  13813   6710   2451   -167       O  
ATOM    222  CB  LEU A 114     -42.154  33.408  10.796  1.00111.03           C  
ANISOU  222  CB  LEU A 114    14633  13968  13584   5498   2248    180       C  
ATOM    223  CG  LEU A 114     -43.454  32.783  10.276  1.00112.16           C  
ANISOU  223  CG  LEU A 114    14098  14539  13980   5650   2243    417       C  
ATOM    224  CD1 LEU A 114     -43.355  32.437   8.820  1.00112.48           C  
ANISOU  224  CD1 LEU A 114    14025  14494  14217   5408   1878    599       C  
ATOM    225  CD2 LEU A 114     -43.829  31.570  11.067  1.00112.96           C  
ANISOU  225  CD2 LEU A 114    13717  15128  14073   5444   2467    530       C  
ATOM    226  N   ALA A 115     -43.534  36.079   9.114  1.00114.75           N  
ANISOU  226  N   ALA A 115    15449  13828  14322   6580   1951    173       N  
ATOM    227  CA  ALA A 115     -44.637  37.023   9.118  1.00116.53           C  
ANISOU  227  CA  ALA A 115    15605  14037  14636   7251   2024    144       C  
ATOM    228  C   ALA A 115     -45.716  36.631   8.124  1.00118.81           C  
ANISOU  228  C   ALA A 115    15314  14635  15195   7407   1848    407       C  
ATOM    229  O   ALA A 115     -45.410  36.074   7.073  1.00118.57           O  
ANISOU  229  O   ALA A 115    15196  14590  15265   7031   1558    582       O  
ATOM    230  CB  ALA A 115     -44.128  38.422   8.825  1.00116.56           C  
ANISOU  230  CB  ALA A 115    16320  13405  14561   7488   1890    -10       C  
ATOM    231  N   ARG A 116     -46.988  36.908   8.458  1.00120.81           N  
ANISOU  231  N   ARG A 116    15158  15187  15557   7970   2019    430       N  
ATOM    232  CA  ARG A 116     -48.088  36.599   7.546  1.00122.99           C  
ANISOU  232  CA  ARG A 116    14845  15782  16105   8155   1829    678       C  
ATOM    233  C   ARG A 116     -48.678  37.877   6.958  1.00124.96           C  
ANISOU  233  C   ARG A 116    15306  15736  16438   8789   1688    666       C  
ATOM    234  O   ARG A 116     -48.926  38.846   7.683  1.00125.19           O  
ANISOU  234  O   ARG A 116    15612  15584  16370   9310   1907    469       O  
ATOM    235  CB  ARG A 116     -49.153  35.669   8.176  1.00124.41           C  
ANISOU  235  CB  ARG A 116    14211  16647  16412   8208   2075    804       C  
ATOM    236  CG  ARG A 116     -50.026  36.281   9.257  1.00127.24           C  
ANISOU  236  CG  ARG A 116    14399  17237  16710   8819   2485    670       C  
ATOM    237  CD  ARG A 116     -51.281  35.453   9.473  1.00130.59           C  
ANISOU  237  CD  ARG A 116    13912  18367  17340   8912   2652    881       C  
ATOM    238  NE  ARG A 116     -52.290  36.172  10.260  1.00133.90           N  
ANISOU  238  NE  ARG A 116    14091  19038  17748   9637   3005    789       N  
ATOM    239  CZ  ARG A 116     -52.559  35.928  11.540  1.00136.18           C  
ANISOU  239  CZ  ARG A 116    14167  19695  17883   9751   3468    710       C  
ATOM    240  NH1 ARG A 116     -51.904  34.975  12.195  1.00136.23           N  
ANISOU  240  NH1 ARG A 116    14174  19847  17739   9174   3615    729       N  
ATOM    241  NH2 ARG A 116     -53.496  36.627  12.172  1.00135.44           N  
ANISOU  241  NH2 ARG A 116    13857  19835  17768  10464   3792    619       N  
ATOM    242  N   HIS A 117     -48.832  37.906   5.632  1.00126.22           N  
ANISOU  242  N   HIS A 117    15398  15807  16752   8748   1304    867       N  
ATOM    243  CA  HIS A 117     -49.347  39.086   4.955  1.00127.98           C  
ANISOU  243  CA  HIS A 117    15847  15724  17056   9330   1115    898       C  
ATOM    244  C   HIS A 117     -50.830  39.312   5.251  1.00129.33           C  
ANISOU  244  C   HIS A 117    15404  16328  17407   9998   1264    948       C  
ATOM    245  O   HIS A 117     -51.597  38.361   5.375  1.00129.59           O  
ANISOU  245  O   HIS A 117    14688  16962  17587   9893   1350   1084       O  
ATOM    246  CB  HIS A 117     -49.059  39.025   3.445  1.00129.14           C  
ANISOU  246  CB  HIS A 117    16111  15678  17276   9081    654   1117       C  
ATOM    247  CG  HIS A 117     -49.210  40.344   2.751  1.00131.56           C  
ANISOU  247  CG  HIS A 117    16902  15495  17592   9572    436   1143       C  
ATOM    248  ND1 HIS A 117     -49.559  40.419   1.417  1.00133.49           N  
ANISOU  248  ND1 HIS A 117    17063  15713  17942   9631     37   1384       N  
ATOM    249  CD2 HIS A 117     -49.059  41.602   3.235  1.00132.83           C  
ANISOU  249  CD2 HIS A 117    17651  15164  17656  10013    554    961       C  
ATOM    250  CE1 HIS A 117     -49.616  41.712   1.132  1.00134.25           C  
ANISOU  250  CE1 HIS A 117    17689  15310  18010  10112    -67   1365       C  
ATOM    251  NE2 HIS A 117     -49.331  42.463   2.197  1.00134.14           N  
ANISOU  251  NE2 HIS A 117    18095  14985  17886  10355    233   1109       N  
ATOM    252  N   LYS A 118     -51.225  40.575   5.390  1.00129.97           N  
ANISOU  252  N   LYS A 118    15801  16099  17483  10687   1300    840       N  
ATOM    253  CA  LYS A 118     -52.600  40.939   5.684  1.00130.96           C  
ANISOU  253  CA  LYS A 118    15381  16606  17773  11417   1453    869       C  
ATOM    254  C   LYS A 118     -53.396  41.142   4.394  1.00132.34           C  
ANISOU  254  C   LYS A 118    15238  16858  18185  11690   1040   1133       C  
ATOM    255  O   LYS A 118     -54.157  42.097   4.272  1.00132.87           O  
ANISOU  255  O   LYS A 118    15317  16823  18343  12419   1001   1129       O  
ATOM    256  CB  LYS A 118     -52.623  42.193   6.562  1.00132.21           C  
ANISOU  256  CB  LYS A 118    16066  16384  17784  12071   1723    583       C  
ATOM    257  CG  LYS A 118     -51.871  42.001   7.869  1.00135.73           C  
ANISOU  257  CG  LYS A 118    16811  16795  17967  11815   2113    312       C  
ATOM    258  CD  LYS A 118     -51.833  43.274   8.691  1.00139.78           C  
ANISOU  258  CD  LYS A 118    17939  16869  18304  12439   2337     -7       C  
ATOM    259  CE  LYS A 118     -51.244  43.037  10.060  1.00143.32           C  
ANISOU  259  CE  LYS A 118    18594  17389  18473  12243   2735   -278       C  
ATOM    260  NZ  LYS A 118     -51.259  44.266  10.903  1.00145.51           N  
ANISOU  260  NZ  LYS A 118    19489  17243  18553  12875   2949   -625       N  
ATOM    261  N   ALA A 119     -53.206  40.228   3.437  1.00132.82           N  
ANISOU  261  N   ALA A 119    15034  17100  18333  11112    720   1354       N  
ATOM    262  CA  ALA A 119     -53.833  40.139   2.108  1.00133.80           C  
ANISOU  262  CA  ALA A 119    14835  17357  18647  11181    264   1624       C  
ATOM    263  C   ALA A 119     -53.381  38.767   1.576  1.00134.75           C  
ANISOU  263  C   ALA A 119    14668  17749  18783  10361     81   1761       C  
ATOM    264  O   ALA A 119     -52.176  38.457   1.613  1.00135.06           O  
ANISOU  264  O   ALA A 119    15204  17482  18632   9799     99   1673       O  
ATOM    265  CB  ALA A 119     -53.331  41.254   1.190  1.00133.77           C  
ANISOU  265  CB  ALA A 119    15594  16682  18551  11388    -65   1655       C  
ATOM    266  N   GLU A 120     -54.344  37.911   1.169  1.00134.69           N  
ANISOU  266  N   GLU A 120    13842  18328  19006  10291    -76   1962       N  
ATOM    267  CA  GLU A 120     -54.052  36.528   0.741  1.00134.74           C  
ANISOU  267  CA  GLU A 120    13519  18622  19055   9545   -253   2081       C  
ATOM    268  C   GLU A 120     -53.483  35.650   1.879  1.00134.00           C  
ANISOU  268  C   GLU A 120    13323  18714  18875   9059    141   1961       C  
ATOM    269  O   GLU A 120     -53.013  34.546   1.593  1.00134.07           O  
ANISOU  269  O   GLU A 120    13200  18852  18887   8418     11   2030       O  
ATOM    270  CB  GLU A 120     -53.136  36.464  -0.502  1.00137.00           C  
ANISOU  270  CB  GLU A 120    14358  18495  19200   9127   -670   2147       C  
ATOM    271  N   GLU A 121     -53.531  36.155   3.158  1.00132.93           N  
ANISOU  271  N   GLU A 121    13280  18580  18649   9387    609   1779       N  
ATOM    272  CA  GLU A 121     -53.054  35.565   4.423  1.00132.26           C  
ANISOU  272  CA  GLU A 121    13158  18659  18437   9058   1032   1652       C  
ATOM    273  C   GLU A 121     -51.946  34.541   4.225  1.00131.15           C  
ANISOU  273  C   GLU A 121    13288  18368  18175   8265    916   1651       C  
ATOM    274  O   GLU A 121     -52.002  33.439   4.765  1.00131.61           O  
ANISOU  274  O   GLU A 121    12971  18774  18262   7841   1075   1701       O  
ATOM    275  CB  GLU A 121     -54.220  34.988   5.240  1.00134.44           C  
ANISOU  275  CB  GLU A 121    12546  19634  18901   9187   1311   1765       C  
ATOM    276  N   VAL A 122     -50.945  34.919   3.428  1.00129.45           N  
ANISOU  276  N   VAL A 122    13727  17634  17826   8082    640   1608       N  
ATOM    277  CA  VAL A 122     -49.833  34.072   3.016  1.00128.14           C  
ANISOU  277  CA  VAL A 122    13872  17277  17538   7398    479   1607       C  
ATOM    278  C   VAL A 122     -48.624  34.235   3.949  1.00126.18           C  
ANISOU  278  C   VAL A 122    14187  16716  17039   7180    771   1388       C  
ATOM    279  O   VAL A 122     -48.363  35.330   4.447  1.00126.32           O  
ANISOU  279  O   VAL A 122    14612  16448  16936   7565    966   1220       O  
ATOM    280  CB  VAL A 122     -49.504  34.311   1.505  1.00129.02           C  
ANISOU  280  CB  VAL A 122    14317  17069  17637   7327     19   1713       C  
ATOM    281  CG1 VAL A 122     -49.462  35.800   1.149  1.00129.90           C  
ANISOU  281  CG1 VAL A 122    14955  16728  17675   7867    -35   1658       C  
ATOM    282  CG2 VAL A 122     -48.227  33.600   1.064  1.00129.28           C  
ANISOU  282  CG2 VAL A 122    14739  16873  17509   6683   -121   1691       C  
ATOM    283  N   PHE A 123     -47.922  33.129   4.231  1.00124.11           N  
ANISOU  283  N   PHE A 123    13938  16517  16701   6576    793   1383       N  
ATOM    284  CA  PHE A 123     -46.753  33.165   5.099  1.00122.39           C  
ANISOU  284  CA  PHE A 123    14204  16049  16251   6328   1027   1191       C  
ATOM    285  C   PHE A 123     -45.470  33.486   4.328  1.00119.78           C  
ANISOU  285  C   PHE A 123    14517  15227  15768   6021    805   1136       C  
ATOM    286  O   PHE A 123     -45.159  32.877   3.300  1.00119.43           O  
ANISOU  286  O   PHE A 123    14450  15169  15758   5676    520   1256       O  
ATOM    287  CB  PHE A 123     -46.636  31.886   5.944  1.00122.57           C  
ANISOU  287  CB  PHE A 123    13874  16434  16263   5915   1235   1214       C  
ATOM    288  CG  PHE A 123     -47.485  31.959   7.190  1.00123.56           C  
ANISOU  288  CG  PHE A 123    13643  16908  16395   6259   1626   1176       C  
ATOM    289  CD1 PHE A 123     -48.867  31.896   7.113  1.00124.47           C  
ANISOU  289  CD1 PHE A 123    13114  17447  16734   6584   1659   1328       C  
ATOM    290  CD2 PHE A 123     -46.907  32.143   8.434  1.00124.57           C  
ANISOU  290  CD2 PHE A 123    14086  16953  16291   6289   1960    984       C  
ATOM    291  CE1 PHE A 123     -49.650  32.003   8.258  1.00125.25           C  
ANISOU  291  CE1 PHE A 123    12870  17898  16820   6935   2059   1299       C  
ATOM    292  CE2 PHE A 123     -47.693  32.247   9.577  1.00125.31           C  
ANISOU  292  CE2 PHE A 123    13883  17383  16346   6644   2345    942       C  
ATOM    293  CZ  PHE A 123     -49.058  32.180   9.482  1.00125.07           C  
ANISOU  293  CZ  PHE A 123    13196  17789  16536   6971   2412   1103       C  
ATOM    294  N   TYR A 124     -44.757  34.491   4.831  1.00117.77           N  
ANISOU  294  N   TYR A 124    14838  14572  15337   6159    943    949       N  
ATOM    295  CA  TYR A 124     -43.516  35.021   4.286  1.00116.33           C  
ANISOU  295  CA  TYR A 124    15292  13904  15005   5900    790    887       C  
ATOM    296  C   TYR A 124     -42.406  35.033   5.353  1.00114.30           C  
ANISOU  296  C   TYR A 124    15407  13475  14546   5642   1017    679       C  
ATOM    297  O   TYR A 124     -42.690  35.018   6.547  1.00114.19           O  
ANISOU  297  O   TYR A 124    15285  13628  14473   5809   1301    550       O  
ATOM    298  CB  TYR A 124     -43.744  36.472   3.824  1.00116.47           C  
ANISOU  298  CB  TYR A 124    15727  13504  15023   6355    675    874       C  
ATOM    299  CG  TYR A 124     -44.476  36.631   2.511  1.00117.43           C  
ANISOU  299  CG  TYR A 124    15647  13678  15293   6561    364   1092       C  
ATOM    300  CD1 TYR A 124     -44.001  36.035   1.353  1.00118.35           C  
ANISOU  300  CD1 TYR A 124    15748  13814  15405   6165     81   1249       C  
ATOM    301  CD2 TYR A 124     -45.570  37.479   2.402  1.00118.52           C  
ANISOU  301  CD2 TYR A 124    15673  13809  15548   7181    338   1131       C  
ATOM    302  CE1 TYR A 124     -44.637  36.219   0.133  1.00119.38           C  
ANISOU  302  CE1 TYR A 124    15741  13986  15632   6355   -232   1443       C  
ATOM    303  CE2 TYR A 124     -46.211  37.678   1.185  1.00119.56           C  
ANISOU  303  CE2 TYR A 124    15643  13982  15802   7386     17   1339       C  
ATOM    304  CZ  TYR A 124     -45.742  37.045   0.049  1.00120.48           C  
ANISOU  304  CZ  TYR A 124    15749  14132  15896   6959   -276   1496       C  
ATOM    305  OH  TYR A 124     -46.375  37.232  -1.159  1.00122.07           O  
ANISOU  305  OH  TYR A 124    15815  14385  16183   7160   -619   1698       O  
ATOM    306  N   ALA A 125     -41.147  35.118   4.918  1.00112.61           N  
ANISOU  306  N   ALA A 125    15639  12936  14213   5252    888    648       N  
ATOM    307  CA  ALA A 125     -40.015  35.230   5.822  1.00111.77           C  
ANISOU  307  CA  ALA A 125    15912  12635  13921   4996   1042    455       C  
ATOM    308  C   ALA A 125     -39.400  36.580   5.533  1.00110.95           C  
ANISOU  308  C   ALA A 125    16435  11981  13738   5115    952    368       C  
ATOM    309  O   ALA A 125     -38.937  36.774   4.426  1.00111.06           O  
ANISOU  309  O   ALA A 125    16649  11778  13771   4947    728    498       O  
ATOM    310  CB  ALA A 125     -39.009  34.135   5.532  1.00111.92           C  
ANISOU  310  CB  ALA A 125    15885  12752  13888   4415    955    507       C  
ATOM    311  N   VAL A 126     -39.425  37.529   6.479  1.00110.28           N  
ANISOU  311  N   VAL A 126    16679  11661  13560   5414   1119    158       N  
ATOM    312  CA  VAL A 126     -38.907  38.878   6.227  1.00110.45           C  
ANISOU  312  CA  VAL A 126    17338  11102  13525   5530   1016     73       C  
ATOM    313  C   VAL A 126     -37.557  39.124   6.918  1.00110.85           C  
ANISOU  313  C   VAL A 126    17848  10871  13400   5132   1056   -118       C  
ATOM    314  O   VAL A 126     -37.449  39.084   8.141  1.00111.02           O  
ANISOU  314  O   VAL A 126    17919  10968  13294   5175   1251   -332       O  
ATOM    315  CB  VAL A 126     -39.953  40.003   6.527  1.00110.88           C  
ANISOU  315  CB  VAL A 126    17535  10970  13624   6214   1093    -20       C  
ATOM    316  CG1 VAL A 126     -40.761  39.719   7.786  1.00111.48           C  
ANISOU  316  CG1 VAL A 126    17307  11403  13649   6541   1400   -188       C  
ATOM    317  CG2 VAL A 126     -39.317  41.393   6.576  1.00111.08           C  
ANISOU  317  CG2 VAL A 126    18306  10331  13570   6301   1006   -157       C  
ATOM    318  N   LYS A 127     -36.532  39.398   6.114  1.00111.07           N  
ANISOU  318  N   LYS A 127    18199  10591  13410   4740    866    -30       N  
ATOM    319  CA  LYS A 127     -35.192  39.663   6.605  1.00112.16           C  
ANISOU  319  CA  LYS A 127    18740  10464  13413   4310    857   -174       C  
ATOM    320  C   LYS A 127     -35.013  41.144   6.897  1.00114.40           C  
ANISOU  320  C   LYS A 127    19660  10156  13650   4505    814   -329       C  
ATOM    321  O   LYS A 127     -34.873  41.938   5.969  1.00114.43           O  
ANISOU  321  O   LYS A 127    19975   9783  13719   4532    647   -191       O  
ATOM    322  CB  LYS A 127     -34.159  39.200   5.570  1.00112.73           C  
ANISOU  322  CB  LYS A 127    18800  10536  13496   3778    694     16       C  
ATOM    323  CG  LYS A 127     -32.716  39.461   5.967  1.00114.75           C  
ANISOU  323  CG  LYS A 127    19421  10539  13640   3300    661    -95       C  
ATOM    324  CD  LYS A 127     -31.777  39.040   4.866  1.00117.30           C  
ANISOU  324  CD  LYS A 127    19697  10894  13976   2840    530    115       C  
ATOM    325  CE  LYS A 127     -30.336  39.192   5.259  1.00119.82           C  
ANISOU  325  CE  LYS A 127    20274  11044  14207   2343    504     25       C  
ATOM    326  NZ  LYS A 127     -29.457  38.356   4.402  1.00121.47           N  
ANISOU  326  NZ  LYS A 127    20263  11478  14413   1912    445    209       N  
ATOM    327  N   VAL A 128     -35.034  41.519   8.187  1.00116.16           N  
ANISOU  327  N   VAL A 128    20107  10284  13746   4643    957   -616       N  
ATOM    328  CA  VAL A 128     -34.833  42.904   8.654  1.00118.13           C  
ANISOU  328  CA  VAL A 128    21017   9937  13929   4818    911   -825       C  
ATOM    329  C   VAL A 128     -33.344  43.077   8.990  1.00120.56           C  
ANISOU  329  C   VAL A 128    21689   9986  14133   4210    804   -926       C  
ATOM    330  O   VAL A 128     -32.793  42.235   9.697  1.00120.94           O  
ANISOU  330  O   VAL A 128    21490  10377  14084   3878    874   -994       O  
ATOM    331  CB  VAL A 128     -35.824  43.412   9.765  1.00118.53           C  
ANISOU  331  CB  VAL A 128    21184   9961  13893   5433   1106  -1099       C  
ATOM    332  CG1 VAL A 128     -36.700  42.299  10.340  1.00119.06           C  
ANISOU  332  CG1 VAL A 128    20587  10662  13987   5773   1327  -1043       C  
ATOM    333  CG2 VAL A 128     -35.127  44.195  10.878  1.00118.94           C  
ANISOU  333  CG2 VAL A 128    21676   9785  13729   5292   1160  -1441       C  
ATOM    334  N   LEU A 129     -32.680  44.113   8.442  1.00122.12           N  
ANISOU  334  N   LEU A 129    22441   9596  14361   4042    623   -909       N  
ATOM    335  CA  LEU A 129     -31.244  44.271   8.662  1.00124.29           C  
ANISOU  335  CA  LEU A 129    23003   9651  14569   3416    504   -967       C  
ATOM    336  C   LEU A 129     -30.863  45.380   9.646  1.00126.84           C  
ANISOU  336  C   LEU A 129    23958   9449  14785   3419    445  -1284       C  
ATOM    337  O   LEU A 129     -30.290  45.071  10.689  1.00127.11           O  
ANISOU  337  O   LEU A 129    24028   9585  14684   3107    453  -1487       O  
ATOM    338  CB  LEU A 129     -30.487  44.439   7.334  1.00124.40           C  
ANISOU  338  CB  LEU A 129    23100   9471  14694   3005    333   -657       C  
ATOM    339  CG  LEU A 129     -30.217  43.164   6.548  1.00125.78           C  
ANISOU  339  CG  LEU A 129    22706  10175  14910   2712    353   -400       C  
ATOM    340  CD1 LEU A 129     -29.543  43.477   5.245  1.00126.25           C  
ANISOU  340  CD1 LEU A 129    22927  10010  15032   2351    209   -116       C  
ATOM    341  CD2 LEU A 129     -29.348  42.209   7.335  1.00126.56           C  
ANISOU  341  CD2 LEU A 129    22510  10663  14913   2313    419   -519       C  
ATOM    342  N   GLN A 130     -31.169  46.646   9.309  1.00128.60           N  
ANISOU  342  N   GLN A 130    24698   9099  15064   3761    361  -1324       N  
ATOM    343  CA  GLN A 130     -30.845  47.877  10.045  1.00130.79           C  
ANISOU  343  CA  GLN A 130    25688   8745  15262   3792    259  -1620       C  
ATOM    344  C   GLN A 130     -29.764  48.659   9.288  1.00132.49           C  
ANISOU  344  C   GLN A 130    26355   8413  15573   3238     15  -1461       C  
ATOM    345  O   GLN A 130     -28.632  48.186   9.163  1.00132.66           O  
ANISOU  345  O   GLN A 130    26214   8599  15590   2596    -54  -1363       O  
ATOM    346  CB  GLN A 130     -30.493  47.655  11.530  1.00132.92           C  
ANISOU  346  CB  GLN A 130    26017   9172  15313   3720    341  -1995       C  
ATOM    347  CG  GLN A 130     -31.656  47.949  12.480  1.00137.38           C  
ANISOU  347  CG  GLN A 130    26650   9801  15747   4451    540  -2280       C  
ATOM    348  CD  GLN A 130     -31.830  46.917  13.579  1.00143.07           C  
ANISOU  348  CD  GLN A 130    26898  11181  16282   4501    763  -2419       C  
ATOM    349  OE1 GLN A 130     -31.530  45.719  13.415  1.00144.80           O  
ANISOU  349  OE1 GLN A 130    26555  11934  16528   4160    812  -2217       O  
ATOM    350  NE2 GLN A 130     -32.344  47.361  14.724  1.00143.87           N  
ANISOU  350  NE2 GLN A 130    27241  11249  16175   4953    908  -2765       N  
ATOM    351  N   LYS A 131     -30.158  49.833   8.740  1.00133.51           N  
ANISOU  351  N   LYS A 131    27027   7905  15795   3511   -107  -1411       N  
ATOM    352  CA  LYS A 131     -29.379  50.755   7.904  1.00135.04           C  
ANISOU  352  CA  LYS A 131    27728   7485  16098   3089   -331  -1211       C  
ATOM    353  C   LYS A 131     -27.866  50.765   8.171  1.00136.66           C  
ANISOU  353  C   LYS A 131    28069   7584  16272   2271   -461  -1251       C  
ATOM    354  O   LYS A 131     -27.103  50.542   7.231  1.00136.97           O  
ANISOU  354  O   LYS A 131    27984   7660  16397   1751   -533   -928       O  
ATOM    355  CB  LYS A 131     -29.945  52.184   7.975  1.00136.51           C  
ANISOU  355  CB  LYS A 131    28658   6884  16324   3543   -449  -1344       C  
ATOM    356  N   LYS A 132     -27.434  51.010   9.433  1.00137.34           N  
ANISOU  356  N   LYS A 132    28391   7566  16224   2159   -492  -1639       N  
ATOM    357  CA  LYS A 132     -26.015  51.058   9.805  1.00138.12           C  
ANISOU  357  CA  LYS A 132    28603   7581  16295   1395   -648  -1708       C  
ATOM    358  C   LYS A 132     -25.295  49.701   9.675  1.00138.82           C  
ANISOU  358  C   LYS A 132    27964   8418  16364    952   -555  -1541       C  
ATOM    359  O   LYS A 132     -25.150  48.974  10.657  1.00138.83           O  
ANISOU  359  O   LYS A 132    27683   8842  16222    927   -484  -1768       O  
ATOM    360  CB  LYS A 132     -25.836  51.655  11.208  1.00139.56           C  
ANISOU  360  CB  LYS A 132    29261   7452  16315   1445   -738  -2188       C  
ATOM    361  N   ALA A 133     -24.840  49.380   8.451  1.00139.23           N  
ANISOU  361  N   ALA A 133    27741   8617  16544    624   -557  -1139       N  
ATOM    362  CA  ALA A 133     -24.124  48.150   8.100  1.00140.12           C  
ANISOU  362  CA  ALA A 133    27200   9381  16658    216   -476   -935       C  
ATOM    363  C   ALA A 133     -23.333  48.344   6.788  1.00141.04           C  
ANISOU  363  C   ALA A 133    27324   9366  16900   -289   -548   -539       C  
ATOM    364  O   ALA A 133     -23.208  47.399   6.001  1.00140.90           O  
ANISOU  364  O   ALA A 133    26798   9839  16899   -397   -441   -275       O  
ATOM    365  CB  ALA A 133     -25.102  46.995   7.954  1.00140.09           C  
ANISOU  365  CB  ALA A 133    26622   9982  16624    695   -269   -858       C  
ATOM    366  N   ILE A 134     -22.793  49.574   6.565  1.00141.54           N  
ANISOU  366  N   ILE A 134    27984   8755  17038   -604   -727   -500       N  
ATOM    367  CA  ILE A 134     -22.014  49.935   5.376  1.00142.42           C  
ANISOU  367  CA  ILE A 134    28191   8665  17257  -1117   -791   -113       C  
ATOM    368  C   ILE A 134     -20.568  49.463   5.487  1.00142.90           C  
ANISOU  368  C   ILE A 134    27981   8985  17332  -1878   -839    -73       C  
ATOM    369  O   ILE A 134     -20.069  48.798   4.581  1.00143.13           O  
ANISOU  369  O   ILE A 134    27584   9416  17381  -2191   -744    235       O  
ATOM    370  CB  ILE A 134     -22.080  51.458   5.108  1.00143.26           C  
ANISOU  370  CB  ILE A 134    29086   7897  17451  -1104   -965    -64       C  
ATOM    371  CG1 ILE A 134     -21.360  51.833   3.794  1.00144.36           C  
ANISOU  371  CG1 ILE A 134    29329   7838  17684  -1604  -1001    401       C  
ATOM    372  CG2 ILE A 134     -21.512  52.242   6.285  1.00143.81           C  
ANISOU  372  CG2 ILE A 134    29654   7474  17512  -1347  -1156   -433       C  
ATOM    373  CD1 ILE A 134     -21.923  51.172   2.556  1.00145.63           C  
ANISOU  373  CD1 ILE A 134    29089   8428  17816  -1355   -841    765       C  
ATOM    374  N   VAL A 149     -25.349  47.688  -6.350  1.00121.31           N  
ANISOU  374  N   VAL A 149    24348   7678  14067      2   -398   3085       N  
ATOM    375  CA  VAL A 149     -25.376  46.232  -6.538  1.00122.02           C  
ANISOU  375  CA  VAL A 149    23801   8492  14068     77   -296   2993       C  
ATOM    376  C   VAL A 149     -26.812  45.697  -6.683  1.00122.04           C  
ANISOU  376  C   VAL A 149    23604   8684  14083    743   -396   2904       C  
ATOM    377  O   VAL A 149     -27.175  44.708  -6.029  1.00121.72           O  
ANISOU  377  O   VAL A 149    23110   9042  14097    929   -349   2634       O  
ATOM    378  CB  VAL A 149     -24.595  45.484  -5.427  1.00123.00           C  
ANISOU  378  CB  VAL A 149    23524   8946  14263   -233   -170   2679       C  
ATOM    379  N   LEU A 150     -27.616  46.356  -7.569  1.00121.94           N  
ANISOU  379  N   LEU A 150    23923   8389  14019   1090   -545   3157       N  
ATOM    380  CA  LEU A 150     -29.030  46.061  -7.879  1.00121.88           C  
ANISOU  380  CA  LEU A 150    23766   8514  14030   1733   -685   3139       C  
ATOM    381  C   LEU A 150     -29.395  44.564  -7.747  1.00121.33           C  
ANISOU  381  C   LEU A 150    23033   9132  13935   1856   -633   2967       C  
ATOM    382  O   LEU A 150     -30.074  44.211  -6.776  1.00121.33           O  
ANISOU  382  O   LEU A 150    22759   9267  14076   2179   -629   2692       O  
ATOM    383  CB  LEU A 150     -29.426  46.626  -9.261  1.00122.14           C  
ANISOU  383  CB  LEU A 150    24157   8326  13923   1928   -845   3530       C  
ATOM    384  N   LEU A 151     -28.862  43.693  -8.665  1.00120.43           N  
ANISOU  384  N   LEU A 151    22682   9440  13637   1566   -576   3119       N  
ATOM    385  CA  LEU A 151     -29.028  42.224  -8.706  1.00119.58           C  
ANISOU  385  CA  LEU A 151    22001   9954  13479   1590   -534   2982       C  
ATOM    386  C   LEU A 151     -30.530  41.802  -8.555  1.00118.30           C  
ANISOU  386  C   LEU A 151    21555   9977  13415   2159   -690   2871       C  
ATOM    387  O   LEU A 151     -31.371  42.334  -9.301  1.00118.35           O  
ANISOU  387  O   LEU A 151    21756   9831  13380   2509   -873   3065       O  
ATOM    388  CB  LEU A 151     -28.076  41.517  -7.688  1.00119.65           C  
ANISOU  388  CB  LEU A 151    21701  10200  13560   1215   -343   2718       C  
ATOM    389  CG  LEU A 151     -26.688  41.116  -8.188  1.00120.90           C  
ANISOU  389  CG  LEU A 151    21801  10567  13571    674   -188   2827       C  
ATOM    390  CD1 LEU A 151     -25.754  42.310  -8.221  1.00121.70           C  
ANISOU  390  CD1 LEU A 151    22360  10214  13666    304   -136   3002       C  
ATOM    391  CD2 LEU A 151     -26.079  40.076  -7.293  1.00121.31           C  
ANISOU  391  CD2 LEU A 151    21428  10973  13693    457    -54   2554       C  
ATOM    392  N   LYS A 152     -30.855  40.860  -7.606  1.00116.58           N  
ANISOU  392  N   LYS A 152    20871  10099  13326   2240   -622   2582       N  
ATOM    393  CA  LYS A 152     -32.198  40.355  -7.266  1.00114.92           C  
ANISOU  393  CA  LYS A 152    20297  10123  13246   2701   -721   2451       C  
ATOM    394  C   LYS A 152     -32.972  39.750  -8.468  1.00112.50           C  
ANISOU  394  C   LYS A 152    19787  10125  12835   2912   -920   2620       C  
ATOM    395  O   LYS A 152     -34.153  39.406  -8.356  1.00112.50           O  
ANISOU  395  O   LYS A 152    19470  10326  12950   3284  -1039   2554       O  
ATOM    396  CB  LYS A 152     -33.023  41.405  -6.514  1.00116.68           C  
ANISOU  396  CB  LYS A 152    20734   9963  13637   3123   -758   2369       C  
ATOM    397  CG  LYS A 152     -32.686  41.469  -5.009  1.00119.97           C  
ANISOU  397  CG  LYS A 152    21103  10299  14183   3044   -574   2065       C  
ATOM    398  CD  LYS A 152     -31.215  41.789  -4.697  1.00123.36           C  
ANISOU  398  CD  LYS A 152    21742  10583  14546   2483   -432   2016       C  
ATOM    399  CE  LYS A 152     -31.023  42.699  -3.510  1.00126.49           C  
ANISOU  399  CE  LYS A 152    22519  10513  15028   2473   -372   1848       C  
ATOM    400  NZ  LYS A 152     -31.563  44.058  -3.768  1.00128.57           N  
ANISOU  400  NZ  LYS A 152    23346  10210  15296   2650   -497   2030       N  
ATOM    401  N   ASN A 153     -32.277  39.600  -9.603  1.00110.01           N  
ANISOU  401  N   ASN A 153    19634   9875  12289   2652   -950   2830       N  
ATOM    402  CA  ASN A 153     -32.708  38.825 -10.746  1.00107.84           C  
ANISOU  402  CA  ASN A 153    19174   9947  11854   2746  -1124   2948       C  
ATOM    403  C   ASN A 153     -32.078  37.397 -10.566  1.00105.30           C  
ANISOU  403  C   ASN A 153    18444  10076  11490   2438  -1006   2763       C  
ATOM    404  O   ASN A 153     -31.873  36.698 -11.559  1.00105.74           O  
ANISOU  404  O   ASN A 153    18429  10404  11345   2351  -1086   2841       O  
ATOM    405  CB  ASN A 153     -32.219  39.466 -12.035  1.00108.66           C  
ANISOU  405  CB  ASN A 153    19710   9889  11686   2637  -1193   3267       C  
ATOM    406  CG  ASN A 153     -33.066  40.634 -12.464  1.00112.38           C  
ANISOU  406  CG  ASN A 153    20546   9977  12174   3019  -1389   3481       C  
ATOM    407  OD1 ASN A 153     -32.562  41.705 -12.809  1.00113.62           O  
ANISOU  407  OD1 ASN A 153    21193   9729  12250   2906  -1353   3693       O  
ATOM    408  ND2 ASN A 153     -34.381  40.459 -12.457  1.00113.28           N  
ANISOU  408  ND2 ASN A 153    20426  10208  12406   3480  -1609   3446       N  
ATOM    409  N   VAL A 154     -31.773  36.984  -9.292  1.00102.30           N  
ANISOU  409  N   VAL A 154    17828   9756  11284   2293   -824   2515       N  
ATOM    410  CA  VAL A 154     -31.188  35.721  -8.880  1.00 99.87           C  
ANISOU  410  CA  VAL A 154    17160   9806  10978   2032   -706   2329       C  
ATOM    411  C   VAL A 154     -32.357  34.776  -8.673  1.00 96.98           C  
ANISOU  411  C   VAL A 154    16367   9740  10740   2291   -848   2210       C  
ATOM    412  O   VAL A 154     -32.876  34.655  -7.567  1.00 97.29           O  
ANISOU  412  O   VAL A 154    16180   9799  10986   2429   -794   2051       O  
ATOM    413  CB  VAL A 154     -30.354  35.902  -7.586  1.00100.43           C  
ANISOU  413  CB  VAL A 154    17221   9767  11173   1789   -482   2149       C  
ATOM    414  CG1 VAL A 154     -29.630  34.616  -7.216  1.00101.15           C  
ANISOU  414  CG1 VAL A 154    16971  10215  11247   1520   -370   1987       C  
ATOM    415  CG2 VAL A 154     -29.357  37.046  -7.729  1.00100.82           C  
ANISOU  415  CG2 VAL A 154    17705   9459  11142   1534   -380   2280       C  
ATOM    416  N   LYS A 155     -32.830  34.176  -9.764  1.00 94.13           N  
ANISOU  416  N   LYS A 155    15913   9605  10247   2364  -1041   2300       N  
ATOM    417  CA  LYS A 155     -33.973  33.278  -9.733  1.00 91.72           C  
ANISOU  417  CA  LYS A 155    15202   9582  10065   2569  -1222   2214       C  
ATOM    418  C   LYS A 155     -33.542  31.864 -10.051  1.00 87.94           C  
ANISOU  418  C   LYS A 155    14494   9426   9492   2325  -1233   2104       C  
ATOM    419  O   LYS A 155     -33.121  31.580 -11.171  1.00 88.08           O  
ANISOU  419  O   LYS A 155    14672   9531   9263   2223  -1314   2190       O  
ATOM    420  CB  LYS A 155     -35.063  33.740 -10.718  1.00 94.16           C  
ANISOU  420  CB  LYS A 155    15579   9870  10327   2910  -1517   2394       C  
ATOM    421  CG  LYS A 155     -36.050  34.740 -10.112  1.00 99.99           C  
ANISOU  421  CG  LYS A 155    16332  10386  11273   3289  -1553   2431       C  
ATOM    422  CD  LYS A 155     -37.157  35.196 -11.091  1.00105.77           C  
ANISOU  422  CD  LYS A 155    17109  11109  11969   3667  -1872   2625       C  
ATOM    423  CE  LYS A 155     -37.989  34.048 -11.636  1.00110.51           C  
ANISOU  423  CE  LYS A 155    17291  12107  12592   3727  -2133   2592       C  
ATOM    424  NZ  LYS A 155     -38.402  33.085 -10.568  1.00113.40           N  
ANISOU  424  NZ  LYS A 155    17147  12725  13215   3677  -2038   2383       N  
ATOM    425  N   HIS A 156     -33.666  30.975  -9.076  1.00 84.25           N  
ANISOU  425  N   HIS A 156    13673   9131   9207   2248  -1153   1917       N  
ATOM    426  CA  HIS A 156     -33.312  29.582  -9.263  1.00 81.52           C  
ANISOU  426  CA  HIS A 156    13112   9054   8808   2042  -1178   1797       C  
ATOM    427  C   HIS A 156     -34.277  28.705  -8.469  1.00 79.21           C  
ANISOU  427  C   HIS A 156    12384   8947   8766   2119  -1250   1677       C  
ATOM    428  O   HIS A 156     -34.686  29.093  -7.381  1.00 79.30           O  
ANISOU  428  O   HIS A 156    12262   8897   8972   2225  -1129   1634       O  
ATOM    429  CB  HIS A 156     -31.866  29.337  -8.794  1.00 81.36           C  
ANISOU  429  CB  HIS A 156    13180   9021   8712   1731   -916   1705       C  
ATOM    430  CG  HIS A 156     -31.280  28.066  -9.326  1.00 81.98           C  
ANISOU  430  CG  HIS A 156    13164   9329   8655   1550   -942   1615       C  
ATOM    431  ND1 HIS A 156     -31.499  26.852  -8.700  1.00 83.31           N  
ANISOU  431  ND1 HIS A 156    13017   9671   8967   1486   -967   1456       N  
ATOM    432  CD2 HIS A 156     -30.574  27.848 -10.458  1.00 82.41           C  
ANISOU  432  CD2 HIS A 156    13420   9456   8437   1455   -957   1667       C  
ATOM    433  CE1 HIS A 156     -30.895  25.947  -9.452  1.00 83.41           C  
ANISOU  433  CE1 HIS A 156    13068   9824   8802   1367  -1007   1399       C  
ATOM    434  NE2 HIS A 156     -30.311  26.503 -10.511  1.00 83.12           N  
ANISOU  434  NE2 HIS A 156    13330   9751   8502   1353   -988   1513       N  
ATOM    435  N   PRO A 157     -34.632  27.504  -8.966  1.00 76.99           N  
ANISOU  435  N   PRO A 157    11887   8891   8476   2054  -1437   1619       N  
ATOM    436  CA  PRO A 157     -35.550  26.637  -8.202  1.00 75.48           C  
ANISOU  436  CA  PRO A 157    11269   8872   8538   2073  -1503   1535       C  
ATOM    437  C   PRO A 157     -35.040  26.236  -6.818  1.00 74.03           C  
ANISOU  437  C   PRO A 157    10935   8699   8492   1917  -1235   1410       C  
ATOM    438  O   PRO A 157     -35.843  25.877  -5.944  1.00 74.87           O  
ANISOU  438  O   PRO A 157    10717   8912   8817   1971  -1211   1380       O  
ATOM    439  CB  PRO A 157     -35.668  25.385  -9.083  1.00 76.25           C  
ANISOU  439  CB  PRO A 157    11274   9146   8552   1944  -1747   1480       C  
ATOM    440  CG  PRO A 157     -35.286  25.819 -10.434  1.00 76.96           C  
ANISOU  440  CG  PRO A 157    11710   9182   8348   1990  -1877   1566       C  
ATOM    441  CD  PRO A 157     -34.295  26.919 -10.279  1.00 75.84           C  
ANISOU  441  CD  PRO A 157    11894   8842   8080   1968  -1613   1634       C  
ATOM    442  N   PHE A 158     -33.710  26.262  -6.613  1.00 71.35           N  
ANISOU  442  N   PHE A 158    10812   8279   8020   1717  -1037   1349       N  
ATOM    443  CA  PHE A 158     -33.143  25.834  -5.343  1.00 68.92           C  
ANISOU  443  CA  PHE A 158    10383   7994   7811   1562   -818   1233       C  
ATOM    444  C   PHE A 158     -32.533  26.966  -4.525  1.00 68.59           C  
ANISOU  444  C   PHE A 158    10535   7763   7762   1571   -588   1224       C  
ATOM    445  O   PHE A 158     -31.702  26.703  -3.672  1.00 69.01           O  
ANISOU  445  O   PHE A 158    10580   7822   7819   1401   -417   1130       O  
ATOM    446  CB  PHE A 158     -32.139  24.690  -5.552  1.00 67.32           C  
ANISOU  446  CB  PHE A 158    10190   7888   7500   1322   -798   1138       C  
ATOM    447  CG  PHE A 158     -32.658  23.586  -6.447  1.00 66.23           C  
ANISOU  447  CG  PHE A 158     9937   7886   7341   1306  -1051   1119       C  
ATOM    448  CD1 PHE A 158     -33.889  23.007  -6.216  1.00 66.05           C  
ANISOU  448  CD1 PHE A 158     9614   7965   7515   1367  -1218   1129       C  
ATOM    449  CD2 PHE A 158     -31.936  23.171  -7.553  1.00 66.21           C  
ANISOU  449  CD2 PHE A 158    10132   7911   7113   1233  -1128   1092       C  
ATOM    450  CE1 PHE A 158     -34.387  22.043  -7.073  1.00 66.19           C  
ANISOU  450  CE1 PHE A 158     9550   8080   7518   1326  -1492   1105       C  
ATOM    451  CE2 PHE A 158     -32.423  22.179  -8.383  1.00 66.25           C  
ANISOU  451  CE2 PHE A 158    10081   8015   7078   1227  -1385   1045       C  
ATOM    452  CZ  PHE A 158     -33.641  21.618  -8.135  1.00 65.81           C  
ANISOU  452  CZ  PHE A 158     9744   8028   7233   1259  -1584   1048       C  
ATOM    453  N   LEU A 159     -32.965  28.207  -4.739  1.00 68.14           N  
ANISOU  453  N   LEU A 159    10659   7528   7702   1773   -604   1317       N  
ATOM    454  CA  LEU A 159     -32.510  29.373  -3.965  1.00 68.52           C  
ANISOU  454  CA  LEU A 159    10937   7339   7756   1798   -420   1296       C  
ATOM    455  C   LEU A 159     -33.744  30.152  -3.484  1.00 70.03           C  
ANISOU  455  C   LEU A 159    11063   7449   8096   2138   -438   1321       C  
ATOM    456  O   LEU A 159     -34.759  30.131  -4.185  1.00 69.68           O  
ANISOU  456  O   LEU A 159    10890   7485   8102   2351   -624   1415       O  
ATOM    457  CB  LEU A 159     -31.669  30.323  -4.824  1.00 67.76           C  
ANISOU  457  CB  LEU A 159    11240   7022   7485   1712   -413   1403       C  
ATOM    458  CG  LEU A 159     -30.396  29.821  -5.453  1.00 67.63           C  
ANISOU  458  CG  LEU A 159    11322   7083   7291   1414   -362   1410       C  
ATOM    459  CD1 LEU A 159     -29.816  30.897  -6.388  1.00 68.06           C  
ANISOU  459  CD1 LEU A 159    11758   6929   7174   1363   -360   1575       C  
ATOM    460  CD2 LEU A 159     -29.392  29.458  -4.412  1.00 67.24           C  
ANISOU  460  CD2 LEU A 159    11206   7072   7272   1176   -176   1274       C  
ATOM    461  N   VAL A 160     -33.662  30.878  -2.329  1.00 71.58           N  
ANISOU  461  N   VAL A 160    11358   7490   8350   2212   -259   1231       N  
ATOM    462  CA  VAL A 160     -34.823  31.668  -1.877  1.00 73.77           C  
ANISOU  462  CA  VAL A 160    11592   7687   8751   2592   -253   1238       C  
ATOM    463  C   VAL A 160     -35.217  32.767  -2.858  1.00 76.43           C  
ANISOU  463  C   VAL A 160    12212   7779   9048   2828   -400   1384       C  
ATOM    464  O   VAL A 160     -34.365  33.428  -3.464  1.00 76.55           O  
ANISOU  464  O   VAL A 160    12606   7551   8928   2683   -414   1453       O  
ATOM    465  CB  VAL A 160     -34.780  32.258  -0.447  1.00 74.02           C  
ANISOU  465  CB  VAL A 160    11693   7603   8827   2689    -34   1087       C  
ATOM    466  CG1 VAL A 160     -35.457  31.346   0.552  1.00 74.46           C  
ANISOU  466  CG1 VAL A 160    11328   7972   8991   2734     73   1006       C  
ATOM    467  CG2 VAL A 160     -33.376  32.642  -0.017  1.00 74.49           C  
ANISOU  467  CG2 VAL A 160    12092   7446   8766   2394     83    996       C  
ATOM    468  N   GLY A 161     -36.521  32.959  -2.983  1.00 78.26           N  
ANISOU  468  N   GLY A 161    12244   8088   9403   3195   -508   1445       N  
ATOM    469  CA  GLY A 161     -37.057  33.996  -3.836  1.00 80.75           C  
ANISOU  469  CA  GLY A 161    12804   8180   9699   3492   -671   1595       C  
ATOM    470  C   GLY A 161     -37.459  35.237  -3.063  1.00 83.38           C  
ANISOU  470  C   GLY A 161    13337   8232  10110   3842   -559   1538       C  
ATOM    471  O   GLY A 161     -38.033  35.146  -1.977  1.00 83.27           O  
ANISOU  471  O   GLY A 161    13076   8347  10217   4024   -410   1410       O  
ATOM    472  N   LEU A 162     -37.163  36.409  -3.628  1.00 85.55           N  
ANISOU  472  N   LEU A 162    14086   8114  10305   3946   -628   1639       N  
ATOM    473  CA  LEU A 162     -37.550  37.671  -3.029  1.00 88.05           C  
ANISOU  473  CA  LEU A 162    14680   8088  10689   4314   -561   1588       C  
ATOM    474  C   LEU A 162     -38.821  38.124  -3.733  1.00 91.31           C  
ANISOU  474  C   LEU A 162    14987   8518  11190   4802   -770   1744       C  
ATOM    475  O   LEU A 162     -38.843  38.174  -4.951  1.00 91.35           O  
ANISOU  475  O   LEU A 162    15113   8487  11108   4784   -991   1944       O  
ATOM    476  CB  LEU A 162     -36.455  38.712  -3.244  1.00 87.86           C  
ANISOU  476  CB  LEU A 162    15271   7571  10541   4118   -539   1626       C  
ATOM    477  CG  LEU A 162     -36.770  40.051  -2.617  1.00 88.87           C  
ANISOU  477  CG  LEU A 162    15774   7262  10730   4481   -490   1551       C  
ATOM    478  CD1 LEU A 162     -36.591  39.983  -1.135  1.00 89.62           C  
ANISOU  478  CD1 LEU A 162    15813   7373  10864   4461   -256   1274       C  
ATOM    479  CD2 LEU A 162     -35.903  41.127  -3.186  1.00 89.15           C  
ANISOU  479  CD2 LEU A 162    16426   6784  10662   4308   -556   1676       C  
ATOM    480  N   HIS A 163     -39.880  38.424  -2.989  1.00 94.16           N  
ANISOU  480  N   HIS A 163    15101   8968  11708   5248   -704   1658       N  
ATOM    481  CA  HIS A 163     -41.142  38.874  -3.571  1.00 97.34           C  
ANISOU  481  CA  HIS A 163    15349   9415  12219   5765   -903   1801       C  
ATOM    482  C   HIS A 163     -41.041  40.367  -3.791  1.00 99.86           C  
ANISOU  482  C   HIS A 163    16266   9178  12496   6063   -955   1860       C  
ATOM    483  O   HIS A 163     -41.225  40.842  -4.910  1.00100.14           O  
ANISOU  483  O   HIS A 163    16526   9045  12476   6189  -1201   2080       O  
ATOM    484  CB  HIS A 163     -42.339  38.501  -2.665  1.00 99.20           C  
ANISOU  484  CB  HIS A 163    15021  10021  12650   6132   -781   1694       C  
ATOM    485  CG  HIS A 163     -42.581  37.020  -2.606  1.00103.17           C  
ANISOU  485  CG  HIS A 163    14927  11054  13217   5840   -783   1691       C  
ATOM    486  ND1 HIS A 163     -43.718  36.451  -3.156  1.00105.53           N  
ANISOU  486  ND1 HIS A 163    14724  11726  13648   6011  -1003   1830       N  
ATOM    487  CD2 HIS A 163     -41.788  36.031  -2.125  1.00104.37           C  
ANISOU  487  CD2 HIS A 163    14952  11386  13320   5376   -623   1577       C  
ATOM    488  CE1 HIS A 163     -43.584  35.144  -2.982  1.00106.02           C  
ANISOU  488  CE1 HIS A 163    14392  12151  13741   5627   -966   1791       C  
ATOM    489  NE2 HIS A 163     -42.444  34.845  -2.361  1.00105.60           N  
ANISOU  489  NE2 HIS A 163    14550  11992  13580   5258   -734   1644       N  
ATOM    490  N   PHE A 164     -40.667  41.095  -2.740  1.00101.57           N  
ANISOU  490  N   PHE A 164    16792   9082  12719   6139   -736   1666       N  
ATOM    491  CA  PHE A 164     -40.485  42.541  -2.780  1.00103.72           C  
ANISOU  491  CA  PHE A 164    17699   8750  12961   6388   -771   1683       C  
ATOM    492  C   PHE A 164     -39.632  43.000  -1.579  1.00106.01           C  
ANISOU  492  C   PHE A 164    18343   8732  13203   6205   -526   1421       C  
ATOM    493  O   PHE A 164     -39.326  42.200  -0.688  1.00105.87           O  
ANISOU  493  O   PHE A 164    18033   9015  13178   5972   -326   1233       O  
ATOM    494  CB  PHE A 164     -41.840  43.284  -2.858  1.00103.68           C  
ANISOU  494  CB  PHE A 164    17625   8676  13094   7119   -882   1741       C  
ATOM    495  CG  PHE A 164     -42.764  43.119  -1.675  1.00104.63           C  
ANISOU  495  CG  PHE A 164    17326   9076  13354   7545   -669   1525       C  
ATOM    496  CD1 PHE A 164     -43.574  42.005  -1.557  1.00105.58           C  
ANISOU  496  CD1 PHE A 164    16706   9821  13587   7613   -649   1544       C  
ATOM    497  CD2 PHE A 164     -42.853  44.099  -0.704  1.00105.56           C  
ANISOU  497  CD2 PHE A 164    17798   8829  13481   7885   -490   1308       C  
ATOM    498  CE1 PHE A 164     -44.428  41.859  -0.472  1.00106.27           C  
ANISOU  498  CE1 PHE A 164    16385  10200  13792   7993   -420   1374       C  
ATOM    499  CE2 PHE A 164     -43.715  43.954   0.373  1.00106.26           C  
ANISOU  499  CE2 PHE A 164    17501   9210  13662   8306   -262   1111       C  
ATOM    500  CZ  PHE A 164     -44.496  42.837   0.482  1.00106.06           C  
ANISOU  500  CZ  PHE A 164    16712   9840  13747   8354   -214   1159       C  
ATOM    501  N   SER A 165     -39.203  44.268  -1.584  1.00107.62           N  
ANISOU  501  N   SER A 165    19204   8322  13366   6282   -565   1419       N  
ATOM    502  CA  SER A 165     -38.388  44.814  -0.507  1.00109.74           C  
ANISOU  502  CA  SER A 165    19878   8233  13583   6106   -389   1165       C  
ATOM    503  C   SER A 165     -38.848  46.216  -0.181  1.00112.44           C  
ANISOU  503  C   SER A 165    20732   8013  13976   6635   -422   1084       C  
ATOM    504  O   SER A 165     -39.404  46.895  -1.035  1.00112.79           O  
ANISOU  504  O   SER A 165    20969   7818  14067   6986   -617   1294       O  
ATOM    505  CB  SER A 165     -36.913  44.824  -0.894  1.00110.67           C  
ANISOU  505  CB  SER A 165    20360   8112  13578   5427   -419   1242       C  
ATOM    506  OG  SER A 165     -36.670  45.677  -2.001  1.00112.56           O  
ANISOU  506  OG  SER A 165    21077   7909  13782   5410   -618   1506       O  
ATOM    507  N   PHE A 166     -38.628  46.652   1.054  1.00114.29           N  
ANISOU  507  N   PHE A 166    21213   8025  14188   6713   -247    776       N  
ATOM    508  CA  PHE A 166     -39.027  47.988   1.489  1.00116.69           C  
ANISOU  508  CA  PHE A 166    22062   7749  14526   7232   -267    641       C  
ATOM    509  C   PHE A 166     -38.147  48.486   2.654  1.00119.03           C  
ANISOU  509  C   PHE A 166    22832   7666  14727   6995   -135    316       C  
ATOM    510  O   PHE A 166     -37.284  47.746   3.136  1.00119.37           O  
ANISOU  510  O   PHE A 166    22703   7968  14685   6466    -21    204       O  
ATOM    511  CB  PHE A 166     -40.538  48.044   1.807  1.00116.94           C  
ANISOU  511  CB  PHE A 166    21713   8048  14669   8029   -199    575       C  
ATOM    512  CG  PHE A 166     -40.986  47.195   2.971  1.00118.22           C  
ANISOU  512  CG  PHE A 166    21326   8772  14821   8147     85    325       C  
ATOM    513  CD1 PHE A 166     -41.214  45.839   2.814  1.00119.30           C  
ANISOU  513  CD1 PHE A 166    20736   9604  14988   7911    145    432       C  
ATOM    514  CD2 PHE A 166     -41.223  47.761   4.211  1.00119.27           C  
ANISOU  514  CD2 PHE A 166    21688   8730  14901   8511    290    -10       C  
ATOM    515  CE1 PHE A 166     -41.635  45.059   3.887  1.00120.12           C  
ANISOU  515  CE1 PHE A 166    20349  10212  15079   7998    413    238       C  
ATOM    516  CE2 PHE A 166     -41.654  46.981   5.276  1.00120.06           C  
ANISOU  516  CE2 PHE A 166    21287   9371  14958   8623    572   -213       C  
ATOM    517  CZ  PHE A 166     -41.852  45.635   5.110  1.00119.90           C  
ANISOU  517  CZ  PHE A 166    20543  10034  14980   8354    636    -72       C  
ATOM    518  N   GLN A 167     -38.326  49.745   3.076  1.00120.59           N  
ANISOU  518  N   GLN A 167    23653   7230  14934   7374   -178    166       N  
ATOM    519  CA  GLN A 167     -37.520  50.315   4.145  1.00122.90           C  
ANISOU  519  CA  GLN A 167    24464   7102  15128   7160   -102   -159       C  
ATOM    520  C   GLN A 167     -38.285  51.361   4.989  1.00124.60           C  
ANISOU  520  C   GLN A 167    25094   6903  15347   7882    -41   -455       C  
ATOM    521  O   GLN A 167     -39.161  52.088   4.492  1.00124.67           O  
ANISOU  521  O   GLN A 167    25248   6663  15457   8497   -139   -348       O  
ATOM    522  CB  GLN A 167     -36.221  50.912   3.575  1.00125.51           C  
ANISOU  522  CB  GLN A 167    25379   6879  15431   6504   -290    -17       C  
ATOM    523  CG  GLN A 167     -36.404  52.290   2.932  1.00131.07           C  
ANISOU  523  CG  GLN A 167    26807   6790  16205   6787   -503    110       C  
ATOM    524  CD  GLN A 167     -35.202  52.710   2.149  1.00137.43           C  
ANISOU  524  CD  GLN A 167    28009   7205  17001   6114   -683    397       C  
ATOM    525  OE1 GLN A 167     -34.392  53.537   2.593  1.00139.19           O  
ANISOU  525  OE1 GLN A 167    28811   6878  17198   5714   -749    283       O  
ATOM    526  NE2 GLN A 167     -35.070  52.140   0.965  1.00138.69           N  
ANISOU  526  NE2 GLN A 167    27864   7657  17176   5972   -768    781       N  
ATOM    527  N   THR A 168     -37.907  51.458   6.262  1.00125.25           N  
ANISOU  527  N   THR A 168    25400   6888  15302   7812    106   -833       N  
ATOM    528  CA  THR A 168     -38.539  52.375   7.186  1.00126.06           C  
ANISOU  528  CA  THR A 168    25917   6624  15358   8476    195  -1176       C  
ATOM    529  C   THR A 168     -37.883  53.756   7.153  1.00127.59           C  
ANISOU  529  C   THR A 168    27075   5859  15545   8379    -21  -1281       C  
ATOM    530  O   THR A 168     -38.559  54.767   6.877  1.00128.59           O  
ANISOU  530  O   THR A 168    27636   5470  15754   8974   -126  -1274       O  
ATOM    531  CB  THR A 168     -38.591  51.749   8.603  1.00126.83           C  
ANISOU  531  CB  THR A 168    25719   7189  15283   8530    485  -1540       C  
ATOM    532  OG1 THR A 168     -37.341  51.133   8.911  1.00127.42           O  
ANISOU  532  OG1 THR A 168    25785   7381  15247   7718    470  -1587       O  
ATOM    533  CG2 THR A 168     -39.696  50.744   8.754  1.00127.35           C  
ANISOU  533  CG2 THR A 168    24924   8080  15385   8919    719  -1462       C  
ATOM    534  N   ALA A 169     -36.556  53.787   7.444  1.00127.49           N  
ANISOU  534  N   ALA A 169    27388   5608  15443   7617    -98  -1372       N  
ATOM    535  CA  ALA A 169     -35.594  54.915   7.629  1.00127.82           C  
ANISOU  535  CA  ALA A 169    28310   4797  15458   7249   -305  -1511       C  
ATOM    536  C   ALA A 169     -34.648  54.573   8.809  1.00127.64           C  
ANISOU  536  C   ALA A 169    28338   4899  15258   6728   -229  -1853       C  
ATOM    537  O   ALA A 169     -34.207  55.486   9.518  1.00128.13           O  
ANISOU  537  O   ALA A 169    29099   4337  15245   6657   -338  -2155       O  
ATOM    538  CB  ALA A 169     -36.300  56.266   7.912  1.00127.44           C  
ANISOU  538  CB  ALA A 169    28982   4006  15433   7973   -382  -1733       C  
ATOM    539  N   ASP A 170     -34.389  53.264   9.035  1.00126.66           N  
ANISOU  539  N   ASP A 170    27495   5566  15065   6400    -61  -1813       N  
ATOM    540  CA  ASP A 170     -33.565  52.708  10.100  1.00126.43           C  
ANISOU  540  CA  ASP A 170    27378   5800  14859   5937     18  -2088       C  
ATOM    541  C   ASP A 170     -33.482  51.185   9.979  1.00125.55           C  
ANISOU  541  C   ASP A 170    26402   6574  14728   5651    184  -1911       C  
ATOM    542  O   ASP A 170     -32.451  50.618  10.318  1.00125.93           O  
ANISOU  542  O   ASP A 170    26326   6832  14690   5038    167  -1962       O  
ATOM    543  CB  ASP A 170     -34.054  53.126  11.506  1.00128.80           C  
ANISOU  543  CB  ASP A 170    27999   5976  14964   6450    154  -2580       C  
ATOM    544  CG  ASP A 170     -35.557  53.081  11.727  1.00133.78           C  
ANISOU  544  CG  ASP A 170    28335   6913  15584   7369    396  -2661       C  
ATOM    545  OD1 ASP A 170     -36.133  51.973  11.646  1.00134.95           O  
ANISOU  545  OD1 ASP A 170    27711   7835  15727   7475    611  -2531       O  
ATOM    546  OD2 ASP A 170     -36.156  54.161  12.007  1.00134.82           O  
ANISOU  546  OD2 ASP A 170    29011   6502  15712   7988    370  -2863       O  
ATOM    547  N   LYS A 171     -34.550  50.520   9.497  1.00124.12           N  
ANISOU  547  N   LYS A 171    25629   6900  14632   6087    325  -1706       N  
ATOM    548  CA  LYS A 171     -34.569  49.061   9.308  1.00123.10           C  
ANISOU  548  CA  LYS A 171    24696   7571  14506   5837    462  -1522       C  
ATOM    549  C   LYS A 171     -34.802  48.728   7.810  1.00121.75           C  
ANISOU  549  C   LYS A 171    24200   7543  14515   5764    350  -1085       C  
ATOM    550  O   LYS A 171     -35.545  49.440   7.119  1.00122.09           O  
ANISOU  550  O   LYS A 171    24426   7292  14671   6219    262   -948       O  
ATOM    551  CB  LYS A 171     -35.634  48.388  10.206  1.00124.61           C  
ANISOU  551  CB  LYS A 171    24403   8335  14607   6374    748  -1700       C  
ATOM    552  CG  LYS A 171     -35.252  48.297  11.682  1.00127.81           C  
ANISOU  552  CG  LYS A 171    24978   8814  14772   6309    888  -2090       C  
ATOM    553  CD  LYS A 171     -36.454  48.031  12.599  1.00131.89           C  
ANISOU  553  CD  LYS A 171    25160   9776  15174   6967   1197  -2280       C  
ATOM    554  CE  LYS A 171     -37.363  49.239  12.736  1.00135.67           C  
ANISOU  554  CE  LYS A 171    26049   9830  15667   7745   1237  -2456       C  
ATOM    555  NZ  LYS A 171     -37.867  49.440  14.129  1.00137.35           N  
ANISOU  555  NZ  LYS A 171    26394  10164  15629   8221   1497  -2854       N  
ATOM    556  N   LEU A 172     -34.144  47.676   7.300  1.00119.75           N  
ANISOU  556  N   LEU A 172    23503   7723  14274   5207    337   -872       N  
ATOM    557  CA  LEU A 172     -34.270  47.308   5.891  1.00118.34           C  
ANISOU  557  CA  LEU A 172    23047   7698  14219   5093    224   -481       C  
ATOM    558  C   LEU A 172     -35.007  45.982   5.791  1.00116.26           C  
ANISOU  558  C   LEU A 172    22003   8188  13983   5229    363   -382       C  
ATOM    559  O   LEU A 172     -34.535  45.010   6.361  1.00116.29           O  
ANISOU  559  O   LEU A 172    21668   8608  13910   4898    478   -470       O  
ATOM    560  CB  LEU A 172     -32.868  47.166   5.301  1.00118.74           C  
ANISOU  560  CB  LEU A 172    23238   7626  14251   4328     95   -314       C  
ATOM    561  CG  LEU A 172     -32.678  47.703   3.901  1.00120.60           C  
ANISOU  561  CG  LEU A 172    23655   7597  14568   4194    -83     51       C  
ATOM    562  CD1 LEU A 172     -32.912  49.196   3.855  1.00121.15           C  
ANISOU  562  CD1 LEU A 172    24414   6927  14690   4522   -220     48       C  
ATOM    563  CD2 LEU A 172     -31.292  47.374   3.391  1.00121.50           C  
ANISOU  563  CD2 LEU A 172    23792   7729  14645   3429   -144    208       C  
ATOM    564  N   TYR A 173     -36.156  45.924   5.089  1.00114.26           N  
ANISOU  564  N   TYR A 173    21463   8108  13843   5702    336   -195       N  
ATOM    565  CA  TYR A 173     -36.931  44.676   5.020  1.00112.76           C  
ANISOU  565  CA  TYR A 173    20523   8621  13701   5821    448   -102       C  
ATOM    566  C   TYR A 173     -36.940  43.999   3.645  1.00109.45           C  
ANISOU  566  C   TYR A 173    19770   8458  13359   5593    288    241       C  
ATOM    567  O   TYR A 173     -37.216  44.650   2.638  1.00109.44           O  
ANISOU  567  O   TYR A 173    19996   8170  13417   5757    105    449       O  
ATOM    568  CB  TYR A 173     -38.382  44.882   5.490  1.00113.62           C  
ANISOU  568  CB  TYR A 173    20393   8902  13877   6566    575   -195       C  
ATOM    569  CG  TYR A 173     -38.562  45.613   6.803  1.00115.41           C  
ANISOU  569  CG  TYR A 173    20955   8896  14000   6919    753   -548       C  
ATOM    570  CD1 TYR A 173     -38.607  46.997   6.847  1.00117.06           C  
ANISOU  570  CD1 TYR A 173    21822   8448  14207   7263    666   -667       C  
ATOM    571  CD2 TYR A 173     -38.793  44.919   7.983  1.00116.64           C  
ANISOU  571  CD2 TYR A 173    20775   9494  14051   6965   1011   -758       C  
ATOM    572  CE1 TYR A 173     -38.826  47.676   8.038  1.00118.52           C  
ANISOU  572  CE1 TYR A 173    22343   8413  14278   7643    824  -1021       C  
ATOM    573  CE2 TYR A 173     -38.997  45.586   9.187  1.00117.96           C  
ANISOU  573  CE2 TYR A 173    21262   9477  14080   7332   1187  -1094       C  
ATOM    574  CZ  TYR A 173     -39.018  46.970   9.211  1.00119.49           C  
ANISOU  574  CZ  TYR A 173    22126   9009  14265   7683   1091  -1242       C  
ATOM    575  OH  TYR A 173     -39.248  47.669  10.380  1.00121.17           O  
ANISOU  575  OH  TYR A 173    22703   9013  14323   8091   1256  -1605       O  
ATOM    576  N   PHE A 174     -36.690  42.675   3.620  1.00106.48           N  
ANISOU  576  N   PHE A 174    18864   8624  12968   5253    352    294       N  
ATOM    577  CA  PHE A 174     -36.689  41.867   2.399  1.00103.98           C  
ANISOU  577  CA  PHE A 174    18205   8607  12697   5030    210    573       C  
ATOM    578  C   PHE A 174     -37.724  40.770   2.536  1.00101.30           C  
ANISOU  578  C   PHE A 174    17186   8862  12444   5245    286    600       C  
ATOM    579  O   PHE A 174     -37.508  39.832   3.284  1.00101.21           O  
ANISOU  579  O   PHE A 174    16859   9199  12398   5025    439    486       O  
ATOM    580  CB  PHE A 174     -35.303  41.249   2.153  1.00103.73           C  
ANISOU  580  CB  PHE A 174    18205   8637  12569   4352    193    615       C  
ATOM    581  CG  PHE A 174     -34.216  42.278   1.960  1.00104.37           C  
ANISOU  581  CG  PHE A 174    18905   8171  12581   4055    121    613       C  
ATOM    582  CD1 PHE A 174     -34.085  42.955   0.761  1.00105.19           C  
ANISOU  582  CD1 PHE A 174    19346   7931  12690   4043    -53    852       C  
ATOM    583  CD2 PHE A 174     -33.342  42.587   2.985  1.00105.14           C  
ANISOU  583  CD2 PHE A 174    19253   8092  12602   3777    216    384       C  
ATOM    584  CE1 PHE A 174     -33.108  43.930   0.596  1.00105.78           C  
ANISOU  584  CE1 PHE A 174    19991   7485  12716   3739   -114    876       C  
ATOM    585  CE2 PHE A 174     -32.363  43.559   2.813  1.00105.84           C  
ANISOU  585  CE2 PHE A 174    19898   7666  12651   3469    130    389       C  
ATOM    586  CZ  PHE A 174     -32.252  44.224   1.620  1.00105.50           C  
ANISOU  586  CZ  PHE A 174    20175   7278  12633   3438    -26    644       C  
ATOM    587  N   VAL A 175     -38.858  40.894   1.850  1.00 99.19           N  
ANISOU  587  N   VAL A 175    16689   8707  12292   5668    170    758       N  
ATOM    588  CA  VAL A 175     -39.925  39.895   1.928  1.00 97.74           C  
ANISOU  588  CA  VAL A 175    15825   9091  12220   5858    215    808       C  
ATOM    589  C   VAL A 175     -39.609  38.665   1.063  1.00 96.24           C  
ANISOU  589  C   VAL A 175    15293   9244  12031   5413     76    983       C  
ATOM    590  O   VAL A 175     -39.768  38.699  -0.156  1.00 96.57           O  
ANISOU  590  O   VAL A 175    15346   9257  12089   5422   -160   1190       O  
ATOM    591  CB  VAL A 175     -41.298  40.509   1.586  1.00 98.10           C  
ANISOU  591  CB  VAL A 175    15709   9158  12405   6511    135    896       C  
ATOM    592  CG1 VAL A 175     -42.409  39.486   1.769  1.00 98.56           C  
ANISOU  592  CG1 VAL A 175    15017   9833  12599   6671    198    945       C  
ATOM    593  CG2 VAL A 175     -41.563  41.751   2.429  1.00 98.32           C  
ANISOU  593  CG2 VAL A 175    16142   8799  12417   6986    274    699       C  
ATOM    594  N   LEU A 176     -39.170  37.581   1.704  1.00 94.37           N  
ANISOU  594  N   LEU A 176    14785   9316  11757   5040    213    893       N  
ATOM    595  CA  LEU A 176     -38.761  36.344   1.043  1.00 92.99           C  
ANISOU  595  CA  LEU A 176    14326   9438  11569   4607    105   1009       C  
ATOM    596  C   LEU A 176     -39.779  35.203   1.192  1.00 92.89           C  
ANISOU  596  C   LEU A 176    13663   9941  11690   4678    116   1060       C  
ATOM    597  O   LEU A 176     -40.722  35.308   1.965  1.00 92.92           O  
ANISOU  597  O   LEU A 176    13394  10124  11788   5022    262   1001       O  
ATOM    598  CB  LEU A 176     -37.398  35.915   1.610  1.00 91.96           C  
ANISOU  598  CB  LEU A 176    14379   9255  11307   4113    226    885       C  
ATOM    599  CG  LEU A 176     -36.314  36.952   1.495  1.00 91.89           C  
ANISOU  599  CG  LEU A 176    14965   8767  11183   3952    213    841       C  
ATOM    600  CD1 LEU A 176     -35.609  37.154   2.804  1.00 91.72           C  
ANISOU  600  CD1 LEU A 176    15128   8641  11080   3811    407    611       C  
ATOM    601  CD2 LEU A 176     -35.388  36.629   0.371  1.00 92.24           C  
ANISOU  601  CD2 LEU A 176    15139   8762  11144   3551     67    992       C  
ATOM    602  N   ASP A 177     -39.590  34.120   0.437  1.00 92.82           N  
ANISOU  602  N   ASP A 177    13411  10170  11688   4349    -35   1171       N  
ATOM    603  CA  ASP A 177     -40.440  32.938   0.515  1.00 93.36           C  
ANISOU  603  CA  ASP A 177    12889  10693  11892   4316    -60   1228       C  
ATOM    604  C   ASP A 177     -40.245  32.265   1.872  1.00 93.82           C  
ANISOU  604  C   ASP A 177    12753  10951  11945   4158    214   1092       C  
ATOM    605  O   ASP A 177     -39.096  32.117   2.300  1.00 93.93           O  
ANISOU  605  O   ASP A 177    13042  10825  11824   3851    314    986       O  
ATOM    606  CB  ASP A 177     -39.984  31.926  -0.540  1.00 94.63           C  
ANISOU  606  CB  ASP A 177    12966  10974  12015   3933   -285   1329       C  
ATOM    607  CG  ASP A 177     -40.596  32.116  -1.896  1.00 98.29           C  
ANISOU  607  CG  ASP A 177    13409  11434  12505   4092   -594   1497       C  
ATOM    608  OD1 ASP A 177     -41.786  32.493  -1.957  1.00 99.36           O  
ANISOU  608  OD1 ASP A 177    13301  11673  12777   4485   -668   1569       O  
ATOM    609  OD2 ASP A 177     -39.892  31.863  -2.904  1.00 99.55           O  
ANISOU  609  OD2 ASP A 177    13781  11511  12534   3835   -764   1558       O  
ATOM    610  N   TYR A 178     -41.335  31.824   2.534  1.00 93.78           N  
ANISOU  610  N   TYR A 178    12262  11292  12077   4349    331   1113       N  
ATOM    611  CA  TYR A 178     -41.178  31.091   3.793  1.00 94.22           C  
ANISOU  611  CA  TYR A 178    12127  11568  12104   4180    592   1021       C  
ATOM    612  C   TYR A 178     -41.072  29.619   3.438  1.00 93.98           C  
ANISOU  612  C   TYR A 178    11774  11797  12137   3763    471   1120       C  
ATOM    613  O   TYR A 178     -41.973  29.073   2.802  1.00 94.10           O  
ANISOU  613  O   TYR A 178    11394  12046  12313   3789    300   1260       O  
ATOM    614  CB  TYR A 178     -42.325  31.346   4.789  1.00 94.70           C  
ANISOU  614  CB  TYR A 178    11848  11884  12251   4578    834   1001       C  
ATOM    615  CG  TYR A 178     -42.281  30.400   5.967  1.00 96.04           C  
ANISOU  615  CG  TYR A 178    11753  12350  12386   4368   1085    969       C  
ATOM    616  CD1 TYR A 178     -41.168  30.339   6.795  1.00 97.31           C  
ANISOU  616  CD1 TYR A 178    12259  12364  12349   4137   1240    819       C  
ATOM    617  CD2 TYR A 178     -43.320  29.514   6.210  1.00 97.23           C  
ANISOU  617  CD2 TYR A 178    11307  12936  12703   4360   1143   1111       C  
ATOM    618  CE1 TYR A 178     -41.090  29.420   7.838  1.00 98.40           C  
ANISOU  618  CE1 TYR A 178    12184  12772  12433   3933   1446    815       C  
ATOM    619  CE2 TYR A 178     -43.259  28.598   7.258  1.00 98.36           C  
ANISOU  619  CE2 TYR A 178    11229  13341  12804   4132   1371   1120       C  
ATOM    620  CZ  TYR A 178     -42.140  28.550   8.068  1.00 99.32           C  
ANISOU  620  CZ  TYR A 178    11732  13301  12705   3931   1521    975       C  
ATOM    621  OH  TYR A 178     -42.075  27.647   9.105  1.00100.69           O  
ANISOU  621  OH  TYR A 178    11716  13727  12813   3719   1732   1004       O  
ATOM    622  N   ILE A 179     -39.962  28.985   3.820  1.00 93.47           N  
ANISOU  622  N   ILE A 179    11887  11678  11950   3385    535   1046       N  
ATOM    623  CA  ILE A 179     -39.755  27.579   3.510  1.00 93.42           C  
ANISOU  623  CA  ILE A 179    11641  11859  11993   3002    416   1121       C  
ATOM    624  C   ILE A 179     -40.201  26.709   4.708  1.00 93.28           C  
ANISOU  624  C   ILE A 179    11268  12143  12031   2913    633   1140       C  
ATOM    625  O   ILE A 179     -39.716  26.856   5.835  1.00 93.38           O  
ANISOU  625  O   ILE A 179    11431  12134  11914   2898    872   1036       O  
ATOM    626  CB  ILE A 179     -38.325  27.321   2.983  1.00 93.80           C  
ANISOU  626  CB  ILE A 179    12060  11688  11893   2665    309   1062       C  
ATOM    627  CG1 ILE A 179     -38.254  27.627   1.482  1.00 94.65           C  
ANISOU  627  CG1 ILE A 179    12321  11651  11990   2682     34   1137       C  
ATOM    628  CG2 ILE A 179     -37.898  25.892   3.200  1.00 94.33           C  
ANISOU  628  CG2 ILE A 179    11951  11917  11972   2303    288   1079       C  
ATOM    629  CD1 ILE A 179     -38.269  29.023   1.096  1.00 95.95           C  
ANISOU  629  CD1 ILE A 179    12804  11553  12100   2963     15   1132       C  
ATOM    630  N   ASN A 180     -41.179  25.828   4.423  1.00 92.68           N  
ANISOU  630  N   ASN A 180    10719  12352  12145   2853    531   1287       N  
ATOM    631  CA  ASN A 180     -41.911  24.952   5.330  1.00 92.32           C  
ANISOU  631  CA  ASN A 180    10234  12637  12206   2765    701   1380       C  
ATOM    632  C   ASN A 180     -41.195  23.706   5.927  1.00 91.45           C  
ANISOU  632  C   ASN A 180    10128  12576  12045   2350    752   1395       C  
ATOM    633  O   ASN A 180     -41.350  23.441   7.125  1.00 91.89           O  
ANISOU  633  O   ASN A 180    10046  12807  12060   2334   1017   1418       O  
ATOM    634  CB  ASN A 180     -43.158  24.467   4.603  1.00 93.84           C  
ANISOU  634  CB  ASN A 180     9926  13083  12646   2794    504   1551       C  
ATOM    635  CG  ASN A 180     -44.424  24.580   5.402  1.00 98.63           C  
ANISOU  635  CG  ASN A 180    10054  14034  13387   3048    735   1648       C  
ATOM    636  OD1 ASN A 180     -45.533  24.495   4.852  1.00100.17           O  
ANISOU  636  OD1 ASN A 180     9820  14448  13790   3175    593   1778       O  
ATOM    637  ND2 ASN A 180     -44.305  24.780   6.716  1.00 99.94           N  
ANISOU  637  ND2 ASN A 180    10265  14282  13425   3138   1098   1589       N  
ATOM    638  N   GLY A 181     -40.500  22.928   5.087  1.00 89.62           N  
ANISOU  638  N   GLY A 181    10035  12206  11809   2045    501   1394       N  
ATOM    639  CA  GLY A 181     -39.885  21.651   5.447  1.00 88.10           C  
ANISOU  639  CA  GLY A 181     9840  12034  11601   1673    487   1421       C  
ATOM    640  C   GLY A 181     -38.754  21.601   6.453  1.00 86.26           C  
ANISOU  640  C   GLY A 181     9902  11706  11167   1572    690   1320       C  
ATOM    641  O   GLY A 181     -38.285  20.509   6.797  1.00 86.33           O  
ANISOU  641  O   GLY A 181     9895  11740  11168   1294    677   1363       O  
ATOM    642  N   GLY A 182     -38.286  22.758   6.897  1.00 84.53           N  
ANISOU  642  N   GLY A 182     9975  11356  10785   1788    844   1186       N  
ATOM    643  CA  GLY A 182     -37.218  22.810   7.890  1.00 83.45           C  
ANISOU  643  CA  GLY A 182    10125  11138  10446   1696   1008   1075       C  
ATOM    644  C   GLY A 182     -35.824  22.518   7.377  1.00 81.61           C  
ANISOU  644  C   GLY A 182    10200  10695  10113   1460    851    992       C  
ATOM    645  O   GLY A 182     -35.639  22.234   6.192  1.00 81.83           O  
ANISOU  645  O   GLY A 182    10249  10632  10209   1364    626   1013       O  
ATOM    646  N   GLU A 183     -34.824  22.628   8.263  1.00 79.58           N  
ANISOU  646  N   GLU A 183    10185  10374   9676   1381    969    890       N  
ATOM    647  CA  GLU A 183     -33.441  22.397   7.874  1.00 78.67           C  
ANISOU  647  CA  GLU A 183    10323  10100   9468   1173    843    811       C  
ATOM    648  C   GLU A 183     -33.227  20.974   7.413  1.00 77.64           C  
ANISOU  648  C   GLU A 183    10049  10025   9426    937    687    902       C  
ATOM    649  O   GLU A 183     -33.905  20.062   7.869  1.00 78.02           O  
ANISOU  649  O   GLU A 183     9856  10226   9564    865    717   1019       O  
ATOM    650  CB  GLU A 183     -32.496  22.708   9.027  1.00 81.06           C  
ANISOU  650  CB  GLU A 183    10856  10367   9575   1128    977    696       C  
ATOM    651  CG  GLU A 183     -32.389  24.181   9.338  1.00 86.78           C  
ANISOU  651  CG  GLU A 183    11839  10943  10191   1320   1074    557       C  
ATOM    652  CD  GLU A 183     -32.647  24.527  10.789  1.00 96.43           C  
ANISOU  652  CD  GLU A 183    13110  12262  11268   1456   1295    488       C  
ATOM    653  OE1 GLU A 183     -32.209  25.622  11.218  1.00 98.36           O  
ANISOU  653  OE1 GLU A 183    13653  12344  11375   1553   1349    328       O  
ATOM    654  OE2 GLU A 183     -33.292  23.714  11.495  1.00 99.52           O  
ANISOU  654  OE2 GLU A 183    13258  12884  11672   1460   1413    593       O  
ATOM    655  N   LEU A 184     -32.326  20.787   6.471  1.00 76.42           N  
ANISOU  655  N   LEU A 184    10048   9742   9247    822    522    852       N  
ATOM    656  CA  LEU A 184     -32.021  19.469   5.930  1.00 75.56           C  
ANISOU  656  CA  LEU A 184     9864   9642   9203    635    357    900       C  
ATOM    657  C   LEU A 184     -31.347  18.612   7.029  1.00 75.22           C  
ANISOU  657  C   LEU A 184     9840   9650   9092    495    428    909       C  
ATOM    658  O   LEU A 184     -31.656  17.424   7.166  1.00 75.27           O  
ANISOU  658  O   LEU A 184     9704   9706   9190    374    362   1007       O  
ATOM    659  CB  LEU A 184     -31.051  19.652   4.736  1.00 74.73           C  
ANISOU  659  CB  LEU A 184     9959   9404   9033    595    213    820       C  
ATOM    660  CG  LEU A 184     -30.925  18.614   3.611  1.00 75.07           C  
ANISOU  660  CG  LEU A 184     9976   9420   9127    489      1    832       C  
ATOM    661  CD1 LEU A 184     -29.491  18.386   3.265  1.00 75.30           C  
ANISOU  661  CD1 LEU A 184    10186   9391   9032    403    -21    743       C  
ATOM    662  CD2 LEU A 184     -31.624  17.299   3.893  1.00 75.43           C  
ANISOU  662  CD2 LEU A 184     9807   9533   9321    384    -86    926       C  
ATOM    663  N   PHE A 185     -30.444  19.216   7.808  1.00 74.61           N  
ANISOU  663  N   PHE A 185     9947   9548   8854    506    541    815       N  
ATOM    664  CA  PHE A 185     -29.703  18.463   8.807  1.00 75.08           C  
ANISOU  664  CA  PHE A 185    10045   9659   8823    392    575    824       C  
ATOM    665  C   PHE A 185     -30.501  18.195  10.087  1.00 74.52           C  
ANISOU  665  C   PHE A 185     9854   9734   8725    417    741    924       C  
ATOM    666  O   PHE A 185     -30.040  17.444  10.934  1.00 74.48           O  
ANISOU  666  O   PHE A 185     9876   9783   8641    324    762    971       O  
ATOM    667  CB  PHE A 185     -28.336  19.070   9.062  1.00 76.04           C  
ANISOU  667  CB  PHE A 185    10386   9719   8785    358    580    691       C  
ATOM    668  CG  PHE A 185     -27.371  18.715   7.945  1.00 78.24           C  
ANISOU  668  CG  PHE A 185    10721   9921   9085    277    426    646       C  
ATOM    669  CD1 PHE A 185     -27.762  18.779   6.617  1.00 79.89           C  
ANISOU  669  CD1 PHE A 185    10904  10066   9385    309    329    657       C  
ATOM    670  CD2 PHE A 185     -26.060  18.380   8.217  1.00 79.62           C  
ANISOU  670  CD2 PHE A 185    10974  10110   9170    189    384    589       C  
ATOM    671  CE1 PHE A 185     -26.863  18.496   5.592  1.00 80.91           C  
ANISOU  671  CE1 PHE A 185    11102  10150   9490    259    221    609       C  
ATOM    672  CE2 PHE A 185     -25.163  18.119   7.185  1.00 80.64           C  
ANISOU  672  CE2 PHE A 185    11131  10204   9303    147    281    544       C  
ATOM    673  CZ  PHE A 185     -25.572  18.156   5.884  1.00 80.55           C  
ANISOU  673  CZ  PHE A 185    11111  10133   9359    184    214    553       C  
ATOM    674  N   TYR A 186     -31.742  18.679  10.170  1.00 73.94           N  
ANISOU  674  N   TYR A 186     9623   9745   8724    546    854    980       N  
ATOM    675  CA  TYR A 186     -32.676  18.269  11.189  1.00 73.71           C  
ANISOU  675  CA  TYR A 186     9407   9901   8699    563   1025   1116       C  
ATOM    676  C   TYR A 186     -33.086  16.811  10.822  1.00 73.09           C  
ANISOU  676  C   TYR A 186     9126   9846   8799    361    889   1291       C  
ATOM    677  O   TYR A 186     -33.188  15.961  11.701  1.00 73.06           O  
ANISOU  677  O   TYR A 186     9067   9927   8764    245    959   1423       O  
ATOM    678  CB  TYR A 186     -33.897  19.185  11.173  1.00 74.22           C  
ANISOU  678  CB  TYR A 186     9312  10064   8826    782   1167   1127       C  
ATOM    679  CG  TYR A 186     -35.092  18.610  11.901  1.00 75.96           C  
ANISOU  679  CG  TYR A 186     9219  10523   9121    779   1332   1316       C  
ATOM    680  CD1 TYR A 186     -35.062  18.403  13.271  1.00 77.03           C  
ANISOU  680  CD1 TYR A 186     9378  10811   9078    784   1554   1368       C  
ATOM    681  CD2 TYR A 186     -36.233  18.235  11.211  1.00 77.58           C  
ANISOU  681  CD2 TYR A 186     9094  10817   9565    752   1257   1455       C  
ATOM    682  CE1 TYR A 186     -36.147  17.854  13.938  1.00 78.56           C  
ANISOU  682  CE1 TYR A 186     9269  11252   9328    762   1737   1572       C  
ATOM    683  CE2 TYR A 186     -37.325  17.688  11.868  1.00 78.79           C  
ANISOU  683  CE2 TYR A 186     8913  11215   9807    711   1416   1655       C  
ATOM    684  CZ  TYR A 186     -37.281  17.503  13.233  1.00 80.01           C  
ANISOU  684  CZ  TYR A 186     9090  11530   9779    716   1675   1721       C  
ATOM    685  OH  TYR A 186     -38.374  16.971  13.876  1.00 82.48           O  
ANISOU  685  OH  TYR A 186     9056  12115  10169    665   1866   1946       O  
ATOM    686  N   HIS A 187     -33.310  16.537   9.526  1.00 72.76           N  
ANISOU  686  N   HIS A 187     9008   9709   8929    314    683   1292       N  
ATOM    687  CA  HIS A 187     -33.629  15.221   8.997  1.00 73.06           C  
ANISOU  687  CA  HIS A 187     8913   9706   9141    117    496   1411       C  
ATOM    688  C   HIS A 187     -32.422  14.270   9.082  1.00 72.23           C  
ANISOU  688  C   HIS A 187     9016   9463   8967    -17    374   1379       C  
ATOM    689  O   HIS A 187     -32.597  13.069   9.311  1.00 72.57           O  
ANISOU  689  O   HIS A 187     9001   9473   9099   -185    296   1510       O  
ATOM    690  CB  HIS A 187     -34.153  15.352   7.568  1.00 74.46           C  
ANISOU  690  CB  HIS A 187     9005   9818   9470    140    291   1377       C  
ATOM    691  CG  HIS A 187     -35.409  16.164   7.488  1.00 78.23           C  
ANISOU  691  CG  HIS A 187     9247  10440  10036    297    381   1427       C  
ATOM    692  ND1 HIS A 187     -35.420  17.429   6.919  1.00 80.60           N  
ANISOU  692  ND1 HIS A 187     9650  10699  10274    516    397   1310       N  
ATOM    693  CD2 HIS A 187     -36.650  15.884   7.949  1.00 79.78           C  
ANISOU  693  CD2 HIS A 187     9106  10826  10380    273    464   1593       C  
ATOM    694  CE1 HIS A 187     -36.673  17.855   7.005  1.00 81.14           C  
ANISOU  694  CE1 HIS A 187     9450  10923  10458    653    470   1394       C  
ATOM    695  NE2 HIS A 187     -37.453  16.956   7.608  1.00 81.18           N  
ANISOU  695  NE2 HIS A 187     9157  11093  10595    512    519   1564       N  
ATOM    696  N   LEU A 188     -31.205  14.807   8.948  1.00 71.04           N  
ANISOU  696  N   LEU A 188     9097   9233   8664     57    361   1218       N  
ATOM    697  CA  LEU A 188     -29.985  14.019   9.088  1.00 71.00           C  
ANISOU  697  CA  LEU A 188     9258   9136   8584    -20    263   1181       C  
ATOM    698  C   LEU A 188     -29.801  13.569  10.523  1.00 71.41           C  
ANISOU  698  C   LEU A 188     9333   9271   8531    -69    384   1286       C  
ATOM    699  O   LEU A 188     -29.369  12.457  10.740  1.00 71.15           O  
ANISOU  699  O   LEU A 188     9351   9166   8515   -165    282   1361       O  
ATOM    700  CB  LEU A 188     -28.732  14.781   8.601  1.00 70.96           C  
ANISOU  700  CB  LEU A 188     9439   9074   8450     59    235    999       C  
ATOM    701  CG  LEU A 188     -27.437  13.958   8.557  1.00 71.57           C  
ANISOU  701  CG  LEU A 188     9638   9087   8469     17    121    952       C  
ATOM    702  CD1 LEU A 188     -27.562  12.811   7.606  1.00 71.80           C  
ANISOU  702  CD1 LEU A 188     9657   8994   8630    -34    -71    972       C  
ATOM    703  CD2 LEU A 188     -26.273  14.799   8.158  1.00 71.99           C  
ANISOU  703  CD2 LEU A 188     9809   9140   8403     72    129    800       C  
ATOM    704  N   GLN A 189     -30.148  14.417  11.503  1.00 72.05           N  
ANISOU  704  N   GLN A 189     9397   9493   8485     14    597   1294       N  
ATOM    705  CA  GLN A 189     -30.062  14.077  12.914  1.00 72.97           C  
ANISOU  705  CA  GLN A 189     9553   9722   8449    -14    734   1397       C  
ATOM    706  C   GLN A 189     -30.979  12.896  13.224  1.00 73.37           C  
ANISOU  706  C   GLN A 189     9440   9809   8630   -162    741   1641       C  
ATOM    707  O   GLN A 189     -30.533  11.985  13.914  1.00 73.88           O  
ANISOU  707  O   GLN A 189     9592   9851   8626   -254    710   1756       O  
ATOM    708  CB  GLN A 189     -30.379  15.302  13.800  1.00 75.44           C  
ANISOU  708  CB  GLN A 189     9894  10181   8587    137    970   1329       C  
ATOM    709  CG  GLN A 189     -30.701  14.995  15.286  1.00 80.93           C  
ANISOU  709  CG  GLN A 189    10593  11053   9102    131   1165   1466       C  
ATOM    710  CD  GLN A 189     -32.192  15.034  15.682  1.00 86.67           C  
ANISOU  710  CD  GLN A 189    11071  11966   9892    170   1388   1626       C  
ATOM    711  OE1 GLN A 189     -32.604  14.448  16.711  1.00 88.11           O  
ANISOU  711  OE1 GLN A 189    11197  12304   9976    111   1543   1813       O  
ATOM    712  NE2 GLN A 189     -33.037  15.721  14.884  1.00 86.84           N  
ANISOU  712  NE2 GLN A 189    10924  11996  10073    276   1413   1573       N  
ATOM    713  N   ARG A 190     -32.217  12.866  12.685  1.00 73.33           N  
ANISOU  713  N   ARG A 190     9195   9847   8819   -200    757   1733       N  
ATOM    714  CA  ARG A 190     -33.131  11.755  12.970  1.00 74.29           C  
ANISOU  714  CA  ARG A 190     9129  10006   9092   -394    759   1985       C  
ATOM    715  C   ARG A 190     -32.608  10.410  12.466  1.00 73.62           C  
ANISOU  715  C   ARG A 190     9157   9687   9128   -572    496   2041       C  
ATOM    716  O   ARG A 190     -32.849   9.375  13.104  1.00 74.69           O  
ANISOU  716  O   ARG A 190     9288   9797   9294   -740    497   2253       O  
ATOM    717  CB  ARG A 190     -34.545  11.978  12.383  1.00 77.64           C  
ANISOU  717  CB  ARG A 190     9229  10536   9734   -417    784   2067       C  
ATOM    718  CG  ARG A 190     -35.109  13.388  12.508  1.00 84.64           C  
ANISOU  718  CG  ARG A 190    10005  11606  10550   -175    991   1968       C  
ATOM    719  CD  ARG A 190     -36.626  13.388  12.641  1.00 91.08           C  
ANISOU  719  CD  ARG A 190    10433  12650  11522   -197   1139   2155       C  
ATOM    720  NE  ARG A 190     -37.034  12.729  13.884  1.00 97.86           N  
ANISOU  720  NE  ARG A 190    11197  13680  12305   -323   1353   2388       N  
ATOM    721  CZ  ARG A 190     -38.181  12.959  14.523  1.00102.22           C  
ANISOU  721  CZ  ARG A 190    11436  14523  12880   -288   1617   2557       C  
ATOM    722  NH1 ARG A 190     -39.059  13.834  14.036  1.00102.79           N  
ANISOU  722  NH1 ARG A 190    11241  14744  13069   -106   1684   2509       N  
ATOM    723  NH2 ARG A 190     -38.456  12.320  15.657  1.00101.63           N  
ANISOU  723  NH2 ARG A 190    11308  14607  12701   -420   1825   2787       N  
ATOM    724  N   GLU A 191     -31.887  10.424  11.339  1.00 71.73           N  
ANISOU  724  N   GLU A 191     9040   9271   8945   -524    279   1855       N  
ATOM    725  CA  GLU A 191     -31.420   9.219  10.673  1.00 70.58           C  
ANISOU  725  CA  GLU A 191     9018   8884   8915   -638     18   1857       C  
ATOM    726  C   GLU A 191     -29.942   8.879  10.794  1.00 68.46           C  
ANISOU  726  C   GLU A 191     9011   8496   8505   -548    -72   1745       C  
ATOM    727  O   GLU A 191     -29.544   7.804  10.352  1.00 68.45           O  
ANISOU  727  O   GLU A 191     9132   8285   8590   -605   -277   1750       O  
ATOM    728  CB  GLU A 191     -31.787   9.333   9.202  1.00 73.74           C  
ANISOU  728  CB  GLU A 191     9362   9185   9470   -635   -173   1732       C  
ATOM    729  CG  GLU A 191     -33.288   9.284   9.049  1.00 80.94           C  
ANISOU  729  CG  GLU A 191     9982  10194  10576   -768   -162   1881       C  
ATOM    730  CD  GLU A 191     -33.792   9.731   7.703  1.00 90.77           C  
ANISOU  730  CD  GLU A 191    11135  11432  11920   -706   -305   1753       C  
ATOM    731  OE1 GLU A 191     -33.351   9.149   6.684  1.00 93.69           O  
ANISOU  731  OE1 GLU A 191    11661  11609  12328   -722   -552   1626       O  
ATOM    732  OE2 GLU A 191     -34.619  10.671   7.665  1.00 93.66           O  
ANISOU  732  OE2 GLU A 191    11289  11989  12309   -616   -172   1775       O  
ATOM    733  N   ALA A 192     -29.142   9.769  11.400  1.00 66.58           N  
ANISOU  733  N   ALA A 192     8855   8387   8057   -405     66   1644       N  
ATOM    734  CA  ALA A 192     -27.681   9.734  11.570  1.00 65.40           C  
ANISOU  734  CA  ALA A 192     8892   8199   7758   -301     -1   1523       C  
ATOM    735  C   ALA A 192     -26.941   9.968  10.223  1.00 64.71           C  
ANISOU  735  C   ALA A 192     8862   8015   7708   -207   -141   1310       C  
ATOM    736  O   ALA A 192     -26.058  10.828  10.151  1.00 65.89           O  
ANISOU  736  O   ALA A 192     9060   8245   7730   -107    -92   1163       O  
ATOM    737  CB  ALA A 192     -27.220   8.467  12.269  1.00 65.05           C  
ANISOU  737  CB  ALA A 192     8967   8049   7701   -357   -100   1670       C  
ATOM    738  N   CYS A 193     -27.343   9.264   9.153  1.00 62.20           N  
ANISOU  738  N   CYS A 193     8541   7539   7553   -253   -308   1295       N  
ATOM    739  CA  CYS A 193     -26.781   9.466   7.833  1.00 60.66           C  
ANISOU  739  CA  CYS A 193     8408   7278   7363   -157   -419   1105       C  
ATOM    740  C   CYS A 193     -27.784   9.074   6.715  1.00 59.30           C  
ANISOU  740  C   CYS A 193     8188   6989   7354   -231   -567   1100       C  
ATOM    741  O   CYS A 193     -28.778   8.376   6.977  1.00 59.21           O  
ANISOU  741  O   CYS A 193     8095   6914   7490   -383   -625   1251       O  
ATOM    742  CB  CYS A 193     -25.404   8.817   7.661  1.00 61.42           C  
ANISOU  742  CB  CYS A 193     8650   7298   7388    -45   -523   1006       C  
ATOM    743  SG  CYS A 193     -25.323   7.032   8.001  1.00 65.23           S  
ANISOU  743  SG  CYS A 193     9266   7544   7976    -86   -713   1125       S  
ATOM    744  N   PHE A 194     -27.581   9.620   5.494  1.00 57.59           N  
ANISOU  744  N   PHE A 194     8007   6772   7103   -139   -622    940       N  
ATOM    745  CA  PHE A 194     -28.450   9.353   4.353  1.00 56.70           C  
ANISOU  745  CA  PHE A 194     7874   6569   7102   -187   -792    908       C  
ATOM    746  C   PHE A 194     -27.816   8.300   3.435  1.00 56.44           C  
ANISOU  746  C   PHE A 194     8035   6346   7064   -136  -1002    778       C  
ATOM    747  O   PHE A 194     -26.597   8.167   3.399  1.00 56.35           O  
ANISOU  747  O   PHE A 194     8145   6332   6933     -1   -972    677       O  
ATOM    748  CB  PHE A 194     -28.688  10.624   3.504  1.00 56.33           C  
ANISOU  748  CB  PHE A 194     7783   6634   6984    -96   -736    821       C  
ATOM    749  CG  PHE A 194     -29.365  11.820   4.135  1.00 56.92           C  
ANISOU  749  CG  PHE A 194     7701   6867   7060    -87   -548    905       C  
ATOM    750  CD1 PHE A 194     -30.192  11.672   5.237  1.00 57.52           C  
ANISOU  750  CD1 PHE A 194     7616   7012   7229   -180   -450   1067       C  
ATOM    751  CD2 PHE A 194     -29.184  13.092   3.617  1.00 57.53           C  
ANISOU  751  CD2 PHE A 194     7807   7018   7036     28   -459    827       C  
ATOM    752  CE1 PHE A 194     -30.806  12.778   5.816  1.00 57.79           C  
ANISOU  752  CE1 PHE A 194     7517   7198   7244   -121   -260   1120       C  
ATOM    753  CE2 PHE A 194     -29.787  14.196   4.214  1.00 57.95           C  
ANISOU  753  CE2 PHE A 194     7753   7178   7086     75   -293    885       C  
ATOM    754  CZ  PHE A 194     -30.601  14.030   5.303  1.00 57.35           C  
ANISOU  754  CZ  PHE A 194     7514   7182   7095     19   -192   1018       C  
ATOM    755  N   LEU A 195     -28.641   7.588   2.647  1.00 55.93           N  
ANISOU  755  N   LEU A 195     7995   6133   7124   -232  -1223    768       N  
ATOM    756  CA  LEU A 195     -28.119   6.671   1.639  1.00 55.54           C  
ANISOU  756  CA  LEU A 195     8172   5888   7044   -156  -1437    603       C  
ATOM    757  C   LEU A 195     -27.620   7.479   0.431  1.00 55.40           C  
ANISOU  757  C   LEU A 195     8230   5975   6846     16  -1416    423       C  
ATOM    758  O   LEU A 195     -28.014   8.641   0.251  1.00 56.09           O  
ANISOU  758  O   LEU A 195     8194   6230   6888     24  -1304    453       O  
ATOM    759  CB  LEU A 195     -29.187   5.654   1.223  1.00 55.32           C  
ANISOU  759  CB  LEU A 195     8169   5646   7203   -348  -1711    642       C  
ATOM    760  CG  LEU A 195     -29.746   4.812   2.389  1.00 56.18           C  
ANISOU  760  CG  LEU A 195     8204   5642   7499   -563  -1726    863       C  
ATOM    761  CD1 LEU A 195     -30.842   3.850   1.920  1.00 55.74           C  
ANISOU  761  CD1 LEU A 195     8142   5379   7657   -814  -2010    920       C  
ATOM    762  CD2 LEU A 195     -28.631   4.083   3.162  1.00 56.44           C  
ANISOU  762  CD2 LEU A 195     8422   5544   7477   -463  -1691    870       C  
ATOM    763  N   GLU A 196     -26.751   6.885  -0.383  1.00 54.31           N  
ANISOU  763  N   GLU A 196     8306   5737   6594    170  -1513    245       N  
ATOM    764  CA  GLU A 196     -26.175   7.582  -1.520  1.00 54.09           C  
ANISOU  764  CA  GLU A 196     8365   5829   6360    337  -1464     91       C  
ATOM    765  C   GLU A 196     -27.218   8.145  -2.499  1.00 54.51           C  
ANISOU  765  C   GLU A 196     8398   5914   6401    277  -1586     82       C  
ATOM    766  O   GLU A 196     -27.050   9.294  -2.900  1.00 54.46           O  
ANISOU  766  O   GLU A 196     8348   6079   6264    345  -1444     85       O  
ATOM    767  CB  GLU A 196     -25.133   6.732  -2.205  1.00 55.72           C  
ANISOU  767  CB  GLU A 196     8797   5939   6436    535  -1534   -100       C  
ATOM    768  CG  GLU A 196     -24.061   6.333  -1.218  1.00 61.48           C  
ANISOU  768  CG  GLU A 196     9507   6677   7177    628  -1413    -73       C  
ATOM    769  CD  GLU A 196     -22.729   5.949  -1.822  1.00 69.41           C  
ANISOU  769  CD  GLU A 196    10640   7724   8007    898  -1361   -252       C  
ATOM    770  OE1 GLU A 196     -22.526   6.212  -3.032  1.00 71.40           O  
ANISOU  770  OE1 GLU A 196    10990   8055   8083   1019  -1352   -394       O  
ATOM    771  OE2 GLU A 196     -21.886   5.390  -1.080  1.00 70.66           O  
ANISOU  771  OE2 GLU A 196    10793   7859   8195   1004  -1324   -241       O  
ATOM    772  N   PRO A 197     -28.328   7.451  -2.846  1.00 54.75           N  
ANISOU  772  N   PRO A 197     8440   5790   6573    134  -1850     93       N  
ATOM    773  CA  PRO A 197     -29.312   8.069  -3.741  1.00 54.89           C  
ANISOU  773  CA  PRO A 197     8404   5878   6574     93  -1981     96       C  
ATOM    774  C   PRO A 197     -29.876   9.380  -3.201  1.00 56.25           C  
ANISOU  774  C   PRO A 197     8326   6253   6796     62  -1791    262       C  
ATOM    775  O   PRO A 197     -30.009  10.342  -3.954  1.00 56.49           O  
ANISOU  775  O   PRO A 197     8369   6398   6698    155  -1768    245       O  
ATOM    776  CB  PRO A 197     -30.377   6.982  -3.863  1.00 55.20           C  
ANISOU  776  CB  PRO A 197     8440   5719   6816   -108  -2301    112       C  
ATOM    777  CG  PRO A 197     -29.627   5.720  -3.661  1.00 55.47           C  
ANISOU  777  CG  PRO A 197     8695   5520   6862    -83  -2380     11       C  
ATOM    778  CD  PRO A 197     -28.701   6.051  -2.558  1.00 54.26           C  
ANISOU  778  CD  PRO A 197     8464   5468   6685      1  -2076     96       C  
ATOM    779  N   ARG A 198     -30.160   9.429  -1.881  1.00 57.49           N  
ANISOU  779  N   ARG A 198     8284   6445   7115    -46  -1645    421       N  
ATOM    780  CA  ARG A 198     -30.724  10.580  -1.152  1.00 58.26           C  
ANISOU  780  CA  ARG A 198     8152   6717   7268    -55  -1447    568       C  
ATOM    781  C   ARG A 198     -29.722  11.731  -1.104  1.00 58.76           C  
ANISOU  781  C   ARG A 198     8291   6896   7139    102  -1204    523       C  
ATOM    782  O   ARG A 198     -30.067  12.861  -1.443  1.00 59.13           O  
ANISOU  782  O   ARG A 198     8294   7037   7134    172  -1139    553       O  
ATOM    783  CB  ARG A 198     -31.135  10.152   0.263  1.00 59.87           C  
ANISOU  783  CB  ARG A 198     8173   6929   7646   -198  -1342    730       C  
ATOM    784  CG  ARG A 198     -31.781  11.256   1.081  1.00 65.01           C  
ANISOU  784  CG  ARG A 198     8593   7763   8346   -181  -1133    865       C  
ATOM    785  CD  ARG A 198     -33.150  10.843   1.589  1.00 70.19           C  
ANISOU  785  CD  ARG A 198     8978   8462   9229   -353  -1188   1039       C  
ATOM    786  NE  ARG A 198     -33.239  10.832   3.049  1.00 74.74           N  
ANISOU  786  NE  ARG A 198     9425   9129   9843   -405   -949   1182       N  
ATOM    787  CZ  ARG A 198     -33.793  11.800   3.774  1.00 78.46           C  
ANISOU  787  CZ  ARG A 198     9711   9787  10315   -328   -729   1270       C  
ATOM    788  NH1 ARG A 198     -34.296  12.878   3.182  1.00 79.23           N  
ANISOU  788  NH1 ARG A 198     9728   9977  10400   -185   -723   1236       N  
ATOM    789  NH2 ARG A 198     -33.826  11.711   5.094  1.00 78.21           N  
ANISOU  789  NH2 ARG A 198     9600   9843  10275   -367   -513   1387       N  
ATOM    790  N   ALA A 199     -28.472  11.433  -0.726  1.00 58.51           N  
ANISOU  790  N   ALA A 199     8375   6847   7008    153  -1090    455       N  
ATOM    791  CA  ALA A 199     -27.398  12.412  -0.682  1.00 58.60           C  
ANISOU  791  CA  ALA A 199     8445   6968   6852    256   -879    413       C  
ATOM    792  C   ALA A 199     -27.084  12.948  -2.091  1.00 59.03           C  
ANISOU  792  C   ALA A 199     8645   7056   6728    362   -916    321       C  
ATOM    793  O   ALA A 199     -26.771  14.124  -2.244  1.00 59.54           O  
ANISOU  793  O   ALA A 199     8725   7209   6690    403   -767    346       O  
ATOM    794  CB  ALA A 199     -26.158  11.780  -0.067  1.00 58.49           C  
ANISOU  794  CB  ALA A 199     8486   6947   6791    286   -802    362       C  
ATOM    795  N   ARG A 200     -27.177  12.097  -3.115  1.00 58.83           N  
ANISOU  795  N   ARG A 200     8751   6950   6652    400  -1117    217       N  
ATOM    796  CA  ARG A 200     -26.918  12.493  -4.502  1.00 59.21           C  
ANISOU  796  CA  ARG A 200     8966   7043   6486    511  -1161    130       C  
ATOM    797  C   ARG A 200     -27.916  13.537  -4.942  1.00 58.86           C  
ANISOU  797  C   ARG A 200     8872   7044   6446    502  -1206    228       C  
ATOM    798  O   ARG A 200     -27.529  14.485  -5.611  1.00 58.90           O  
ANISOU  798  O   ARG A 200     8977   7128   6276    579  -1108    240       O  
ATOM    799  CB  ARG A 200     -26.999  11.280  -5.440  1.00 60.79           C  
ANISOU  799  CB  ARG A 200     9341   7127   6628    557  -1407    -19       C  
ATOM    800  CG  ARG A 200     -26.865  11.599  -6.945  1.00 64.23           C  
ANISOU  800  CG  ARG A 200     9984   7624   6798    685  -1474   -117       C  
ATOM    801  CD  ARG A 200     -26.876  10.353  -7.812  1.00 67.50           C  
ANISOU  801  CD  ARG A 200    10615   7909   7124    753  -1719   -305       C  
ATOM    802  NE  ARG A 200     -25.976   9.336  -7.256  1.00 70.87           N  
ANISOU  802  NE  ARG A 200    11085   8245   7598    807  -1668   -401       N  
ATOM    803  CZ  ARG A 200     -26.372   8.140  -6.841  1.00 72.62           C  
ANISOU  803  CZ  ARG A 200    11339   8250   8002    729  -1874   -446       C  
ATOM    804  NH1 ARG A 200     -27.642   7.769  -6.978  1.00 73.04           N  
ANISOU  804  NH1 ARG A 200    11368   8174   8210    565  -2149   -413       N  
ATOM    805  NH2 ARG A 200     -25.500   7.298  -6.296  1.00 71.07           N  
ANISOU  805  NH2 ARG A 200    11197   7964   7844    809  -1819   -512       N  
ATOM    806  N   PHE A 201     -29.195  13.354  -4.578  1.00 58.36           N  
ANISOU  806  N   PHE A 201     8648   6939   6587    412  -1352    312       N  
ATOM    807  CA  PHE A 201     -30.267  14.276  -4.912  1.00 58.86           C  
ANISOU  807  CA  PHE A 201     8615   7055   6694    434  -1418    414       C  
ATOM    808  C   PHE A 201     -30.028  15.661  -4.299  1.00 57.93           C  
ANISOU  808  C   PHE A 201     8450   7007   6554    492  -1159    510       C  
ATOM    809  O   PHE A 201     -30.188  16.666  -4.979  1.00 57.31           O  
ANISOU  809  O   PHE A 201     8450   6955   6370    584  -1155    554       O  
ATOM    810  CB  PHE A 201     -31.584  13.708  -4.393  1.00 59.85           C  
ANISOU  810  CB  PHE A 201     8501   7159   7079    313  -1582    498       C  
ATOM    811  CG  PHE A 201     -32.791  14.572  -4.673  1.00 61.47           C  
ANISOU  811  CG  PHE A 201     8546   7447   7362    363  -1671    608       C  
ATOM    812  CD1 PHE A 201     -33.453  14.492  -5.887  1.00 62.14           C  
ANISOU  812  CD1 PHE A 201     8685   7534   7392    393  -1959    579       C  
ATOM    813  CD2 PHE A 201     -33.303  15.416  -3.698  1.00 62.64           C  
ANISOU  813  CD2 PHE A 201     8488   7676   7635    400  -1483    735       C  
ATOM    814  CE1 PHE A 201     -34.599  15.234  -6.117  1.00 63.05           C  
ANISOU  814  CE1 PHE A 201     8621   7739   7596    459  -2069    692       C  
ATOM    815  CE2 PHE A 201     -34.441  16.172  -3.940  1.00 63.36           C  
ANISOU  815  CE2 PHE A 201     8412   7849   7812    490  -1568    835       C  
ATOM    816  CZ  PHE A 201     -35.085  16.068  -5.144  1.00 63.04           C  
ANISOU  816  CZ  PHE A 201     8396   7819   7737    519  -1866    822       C  
ATOM    817  N   TYR A 202     -29.655  15.710  -3.013  1.00 57.46           N  
ANISOU  817  N   TYR A 202     8289   6959   6585    437   -963    543       N  
ATOM    818  CA  TYR A 202     -29.400  16.961  -2.317  1.00 57.37           C  
ANISOU  818  CA  TYR A 202     8265   6982   6552    477   -737    603       C  
ATOM    819  C   TYR A 202     -28.136  17.629  -2.833  1.00 57.31           C  
ANISOU  819  C   TYR A 202     8454   6983   6338    507   -606    555       C  
ATOM    820  O   TYR A 202     -28.157  18.830  -3.082  1.00 57.50           O  
ANISOU  820  O   TYR A 202     8559   6992   6295    558   -526    610       O  
ATOM    821  CB  TYR A 202     -29.331  16.734  -0.805  1.00 57.50           C  
ANISOU  821  CB  TYR A 202     8144   7018   6687    406   -590    635       C  
ATOM    822  CG  TYR A 202     -30.636  16.230  -0.221  1.00 58.60           C  
ANISOU  822  CG  TYR A 202     8057   7182   7027    360   -666    725       C  
ATOM    823  CD1 TYR A 202     -31.859  16.695  -0.690  1.00 59.40           C  
ANISOU  823  CD1 TYR A 202     8035   7318   7218    425   -771    796       C  
ATOM    824  CD2 TYR A 202     -30.646  15.307   0.816  1.00 59.53           C  
ANISOU  824  CD2 TYR A 202     8068   7304   7245    251   -630    759       C  
ATOM    825  CE1 TYR A 202     -33.058  16.237  -0.157  1.00 60.15           C  
ANISOU  825  CE1 TYR A 202     7865   7478   7510    368   -826    896       C  
ATOM    826  CE2 TYR A 202     -31.838  14.843   1.355  1.00 60.23           C  
ANISOU  826  CE2 TYR A 202     7929   7438   7518    178   -674    873       C  
ATOM    827  CZ  TYR A 202     -33.040  15.325   0.880  1.00 61.00           C  
ANISOU  827  CZ  TYR A 202     7864   7597   7715    231   -761    940       C  
ATOM    828  OH  TYR A 202     -34.207  14.853   1.416  1.00 62.45           O  
ANISOU  828  OH  TYR A 202     7769   7865   8094    142   -791   1068       O  
ATOM    829  N   ALA A 203     -27.042  16.862  -3.026  1.00 56.85           N  
ANISOU  829  N   ALA A 203     8470   6947   6183    481   -584    463       N  
ATOM    830  CA  ALA A 203     -25.818  17.447  -3.558  1.00 56.81           C  
ANISOU  830  CA  ALA A 203     8600   6998   5987    495   -443    434       C  
ATOM    831  C   ALA A 203     -26.039  17.878  -5.009  1.00 57.61           C  
ANISOU  831  C   ALA A 203     8863   7106   5918    572   -525    450       C  
ATOM    832  O   ALA A 203     -25.460  18.881  -5.412  1.00 58.55           O  
ANISOU  832  O   ALA A 203     9091   7252   5903    567   -393    505       O  
ATOM    833  CB  ALA A 203     -24.652  16.483  -3.442  1.00 56.51           C  
ANISOU  833  CB  ALA A 203     8560   7018   5892    490   -398    334       C  
ATOM    834  N   ALA A 204     -26.916  17.190  -5.777  1.00 56.95           N  
ANISOU  834  N   ALA A 204     8808   6993   5838    627   -757    417       N  
ATOM    835  CA  ALA A 204     -27.202  17.617  -7.146  1.00 57.22           C  
ANISOU  835  CA  ALA A 204     9016   7044   5680    713   -865    439       C  
ATOM    836  C   ALA A 204     -27.951  18.946  -7.145  1.00 57.32           C  
ANISOU  836  C   ALA A 204     9033   7018   5730    747   -852    585       C  
ATOM    837  O   ALA A 204     -27.560  19.853  -7.871  1.00 57.57           O  
ANISOU  837  O   ALA A 204     9238   7059   5578    785   -777    657       O  
ATOM    838  CB  ALA A 204     -27.979  16.556  -7.906  1.00 57.36           C  
ANISOU  838  CB  ALA A 204     9070   7034   5691    751  -1156    351       C  
ATOM    839  N   GLU A 205     -28.974  19.100  -6.285  1.00 57.23           N  
ANISOU  839  N   GLU A 205     8834   6961   5948    744   -903    642       N  
ATOM    840  CA  GLU A 205     -29.712  20.362  -6.202  1.00 57.44           C  
ANISOU  840  CA  GLU A 205     8859   6939   6026    829   -884    767       C  
ATOM    841  C   GLU A 205     -28.815  21.525  -5.692  1.00 58.27           C  
ANISOU  841  C   GLU A 205     9083   6985   6072    796   -627    815       C  
ATOM    842  O   GLU A 205     -28.903  22.645  -6.214  1.00 59.13           O  
ANISOU  842  O   GLU A 205     9358   7022   6086    863   -606    914       O  
ATOM    843  CB  GLU A 205     -31.011  20.210  -5.400  1.00 58.32           C  
ANISOU  843  CB  GLU A 205     8711   7056   6392    859   -970    809       C  
ATOM    844  CG  GLU A 205     -31.950  19.204  -6.039  1.00 62.50           C  
ANISOU  844  CG  GLU A 205     9125   7634   6990    849  -1259    783       C  
ATOM    845  CD  GLU A 205     -33.403  19.185  -5.593  1.00 69.16           C  
ANISOU  845  CD  GLU A 205     9679   8527   8072    886  -1387    866       C  
ATOM    846  OE1 GLU A 205     -33.679  19.513  -4.419  1.00 69.96           O  
ANISOU  846  OE1 GLU A 205     9607   8646   8329    896  -1212    914       O  
ATOM    847  OE2 GLU A 205     -34.272  18.850  -6.430  1.00 71.91           O  
ANISOU  847  OE2 GLU A 205     9966   8915   8441    911  -1666    881       O  
ATOM    848  N   ILE A 206     -27.894  21.243  -4.759  1.00 57.77           N  
ANISOU  848  N   ILE A 206     8960   6943   6048    682   -458    749       N  
ATOM    849  CA  ILE A 206     -26.974  22.268  -4.279  1.00 57.99           C  
ANISOU  849  CA  ILE A 206     9092   6917   6023    605   -250    777       C  
ATOM    850  C   ILE A 206     -25.953  22.618  -5.378  1.00 58.98           C  
ANISOU  850  C   ILE A 206     9410   7078   5923    555   -185    812       C  
ATOM    851  O   ILE A 206     -25.680  23.790  -5.595  1.00 58.98           O  
ANISOU  851  O   ILE A 206     9570   6986   5854    525    -97    909       O  
ATOM    852  CB  ILE A 206     -26.295  21.824  -2.967  1.00 57.91           C  
ANISOU  852  CB  ILE A 206     8950   6948   6104    494   -124    696       C  
ATOM    853  CG1 ILE A 206     -27.315  21.652  -1.829  1.00 57.86           C  
ANISOU  853  CG1 ILE A 206     8779   6920   6286    542   -140    693       C  
ATOM    854  CG2 ILE A 206     -25.208  22.798  -2.577  1.00 58.52           C  
ANISOU  854  CG2 ILE A 206     9134   6988   6112    374     51    707       C  
ATOM    855  CD1 ILE A 206     -26.756  20.941  -0.618  1.00 58.22           C  
ANISOU  855  CD1 ILE A 206     8703   7027   6390    447    -58    625       C  
ATOM    856  N   ALA A 207     -25.429  21.612  -6.106  1.00 59.55           N  
ANISOU  856  N   ALA A 207     9480   7274   5871    556   -226    740       N  
ATOM    857  CA  ALA A 207     -24.436  21.858  -7.150  1.00 60.69           C  
ANISOU  857  CA  ALA A 207     9782   7505   5773    526   -126    774       C  
ATOM    858  C   ALA A 207     -24.983  22.726  -8.275  1.00 63.04           C  
ANISOU  858  C   ALA A 207    10296   7741   5917    603   -199    909       C  
ATOM    859  O   ALA A 207     -24.273  23.619  -8.747  1.00 64.05           O  
ANISOU  859  O   ALA A 207    10578   7862   5897    526    -54   1023       O  
ATOM    860  CB  ALA A 207     -23.909  20.548  -7.701  1.00 60.34           C  
ANISOU  860  CB  ALA A 207     9707   7604   5614    575   -164    644       C  
ATOM    861  N   SER A 208     -26.248  22.495  -8.699  1.00 63.30           N  
ANISOU  861  N   SER A 208    10337   7728   5987    742   -432    915       N  
ATOM    862  CA  SER A 208     -26.822  23.311  -9.750  1.00 63.87           C  
ANISOU  862  CA  SER A 208    10617   7745   5908    842   -536   1055       C  
ATOM    863  C   SER A 208     -27.078  24.736  -9.266  1.00 64.09           C  
ANISOU  863  C   SER A 208    10725   7591   6035    841   -458   1199       C  
ATOM    864  O   SER A 208     -26.840  25.671 -10.024  1.00 64.40           O  
ANISOU  864  O   SER A 208    11002   7561   5906    847   -420   1351       O  
ATOM    865  CB  SER A 208     -28.046  22.653 -10.381  1.00 66.00           C  
ANISOU  865  CB  SER A 208    10856   8040   6180    986   -840   1019       C  
ATOM    866  OG  SER A 208     -29.254  22.929  -9.701  1.00 69.92           O  
ANISOU  866  OG  SER A 208    11176   8456   6936   1058   -966   1047       O  
ATOM    867  N   ALA A 209     -27.485  24.922  -7.995  1.00 64.02           N  
ANISOU  867  N   ALA A 209    10552   7495   6279    834   -420   1156       N  
ATOM    868  CA  ALA A 209     -27.665  26.285  -7.462  1.00 64.39           C  
ANISOU  868  CA  ALA A 209    10714   7339   6412    854   -338   1256       C  
ATOM    869  C   ALA A 209     -26.321  26.999  -7.329  1.00 64.48           C  
ANISOU  869  C   ALA A 209    10882   7290   6328    646   -118   1303       C  
ATOM    870  O   ALA A 209     -26.245  28.193  -7.547  1.00 64.48           O  
ANISOU  870  O   ALA A 209    11111   7104   6286    631    -75   1436       O  
ATOM    871  CB  ALA A 209     -28.376  26.255  -6.122  1.00 64.69           C  
ANISOU  871  CB  ALA A 209    10548   7329   6702    914   -328   1175       C  
ATOM    872  N   LEU A 210     -25.259  26.266  -6.996  1.00 64.73           N  
ANISOU  872  N   LEU A 210    10786   7474   6333    482      8   1204       N  
ATOM    873  CA  LEU A 210     -23.927  26.831  -6.885  1.00 65.26           C  
ANISOU  873  CA  LEU A 210    10930   7542   6325    257    206   1249       C  
ATOM    874  C   LEU A 210     -23.447  27.218  -8.253  1.00 67.48           C  
ANISOU  874  C   LEU A 210    11414   7870   6356    217    254   1403       C  
ATOM    875  O   LEU A 210     -23.024  28.345  -8.428  1.00 68.67           O  
ANISOU  875  O   LEU A 210    11756   7878   6456     82    351   1550       O  
ATOM    876  CB  LEU A 210     -22.956  25.854  -6.219  1.00 64.29           C  
ANISOU  876  CB  LEU A 210    10574   7614   6240    134    304   1107       C  
ATOM    877  CG  LEU A 210     -23.162  25.658  -4.743  1.00 63.96           C  
ANISOU  877  CG  LEU A 210    10372   7523   6408    114    303    987       C  
ATOM    878  CD1 LEU A 210     -22.348  24.523  -4.255  1.00 64.02           C  
ANISOU  878  CD1 LEU A 210    10162   7731   6433     48    350    865       C  
ATOM    879  CD2 LEU A 210     -22.877  26.930  -3.976  1.00 64.16           C  
ANISOU  879  CD2 LEU A 210    10525   7351   6502    -21    387   1028       C  
ATOM    880  N   GLY A 211     -23.599  26.338  -9.241  1.00 68.18           N  
ANISOU  880  N   GLY A 211    11495   8136   6276    335    174   1377       N  
ATOM    881  CA  GLY A 211     -23.202  26.628 -10.612  1.00 69.22           C  
ANISOU  881  CA  GLY A 211    11839   8348   6114    330    223   1522       C  
ATOM    882  C   GLY A 211     -23.888  27.851 -11.181  1.00 70.65           C  
ANISOU  882  C   GLY A 211    12302   8307   6233    393    139   1730       C  
ATOM    883  O   GLY A 211     -23.266  28.625 -11.913  1.00 71.50           O  
ANISOU  883  O   GLY A 211    12625   8390   6152    276    265   1920       O  
ATOM    884  N   TYR A 212     -25.167  28.049 -10.827  1.00 71.30           N  
ANISOU  884  N   TYR A 212    12378   8230   6481    581    -66   1711       N  
ATOM    885  CA  TYR A 212     -25.957  29.199 -11.270  1.00 72.96           C  
ANISOU  885  CA  TYR A 212    12844   8208   6669    707   -179   1900       C  
ATOM    886  C   TYR A 212     -25.429  30.498 -10.646  1.00 74.31           C  
ANISOU  886  C   TYR A 212    13181   8113   6940    542    -25   2012       C  
ATOM    887  O   TYR A 212     -25.307  31.516 -11.350  1.00 74.88           O  
ANISOU  887  O   TYR A 212    13560   8016   6877    509     -7   2232       O  
ATOM    888  CB  TYR A 212     -27.435  29.004 -10.920  1.00 73.32           C  
ANISOU  888  CB  TYR A 212    12762   8192   6904    966   -422   1832       C  
ATOM    889  CG  TYR A 212     -28.294  30.229 -11.157  1.00 74.76           C  
ANISOU  889  CG  TYR A 212    13170   8118   7116   1147   -541   2010       C  
ATOM    890  CD1 TYR A 212     -28.552  30.684 -12.446  1.00 76.17           C  
ANISOU  890  CD1 TYR A 212    13621   8268   7050   1249   -662   2207       C  
ATOM    891  CD2 TYR A 212     -28.843  30.936 -10.094  1.00 75.75           C  
ANISOU  891  CD2 TYR A 212    13261   8026   7495   1239   -531   1981       C  
ATOM    892  CE1 TYR A 212     -29.339  31.810 -12.672  1.00 77.25           C  
ANISOU  892  CE1 TYR A 212    13983   8150   7217   1446   -790   2385       C  
ATOM    893  CE2 TYR A 212     -29.633  32.063 -10.307  1.00 76.90           C  
ANISOU  893  CE2 TYR A 212    13628   7917   7674   1454   -644   2134       C  
ATOM    894  CZ  TYR A 212     -29.876  32.498 -11.598  1.00 78.30           C  
ANISOU  894  CZ  TYR A 212    14070   8053   7628   1556   -780   2344       C  
ATOM    895  OH  TYR A 212     -30.663  33.601 -11.818  1.00 80.21           O  
ANISOU  895  OH  TYR A 212    14542   8028   7905   1799   -911   2509       O  
ATOM    896  N   LEU A 213     -25.109  30.451  -9.337  1.00 74.26           N  
ANISOU  896  N   LEU A 213    12999   8058   7157    431     70   1863       N  
ATOM    897  CA  LEU A 213     -24.546  31.566  -8.587  1.00 74.93           C  
ANISOU  897  CA  LEU A 213    13229   7890   7352    244    194   1911       C  
ATOM    898  C   LEU A 213     -23.196  31.935  -9.175  1.00 76.46           C  
ANISOU  898  C   LEU A 213    13544   8134   7373    -64    379   2057       C  
ATOM    899  O   LEU A 213     -22.935  33.114  -9.410  1.00 77.10           O  
ANISOU  899  O   LEU A 213    13911   7957   7427   -195    422   2239       O  
ATOM    900  CB  LEU A 213     -24.368  31.187  -7.105  1.00 74.61           C  
ANISOU  900  CB  LEU A 213    12947   7875   7528    174    250   1692       C  
ATOM    901  CG  LEU A 213     -25.608  31.183  -6.240  1.00 75.14           C  
ANISOU  901  CG  LEU A 213    12931   7827   7791    426    136   1575       C  
ATOM    902  CD1 LEU A 213     -25.242  30.883  -4.828  1.00 75.27           C  
ANISOU  902  CD1 LEU A 213    12765   7877   7956    317    224   1388       C  
ATOM    903  CD2 LEU A 213     -26.345  32.526  -6.309  1.00 75.66           C  
ANISOU  903  CD2 LEU A 213    13302   7542   7904    582     68   1694       C  
ATOM    904  N   HIS A 214     -22.358  30.934  -9.478  1.00 77.08           N  
ANISOU  904  N   HIS A 214    13410   8546   7334   -173    489   1992       N  
ATOM    905  CA  HIS A 214     -21.053  31.191 -10.073  1.00 78.26           C  
ANISOU  905  CA  HIS A 214    13599   8826   7312   -453    697   2135       C  
ATOM    906  C   HIS A 214     -21.148  31.799 -11.457  1.00 79.85           C  
ANISOU  906  C   HIS A 214    14106   8987   7246   -431    708   2399       C  
ATOM    907  O   HIS A 214     -20.258  32.557 -11.833  1.00 80.09           O  
ANISOU  907  O   HIS A 214    14270   8985   7174   -701    879   2600       O  
ATOM    908  CB  HIS A 214     -20.176  29.938 -10.063  1.00 78.34           C  
ANISOU  908  CB  HIS A 214    13288   9221   7257   -504    816   1986       C  
ATOM    909  CG  HIS A 214     -19.895  29.406  -8.697  1.00 79.37           C  
ANISOU  909  CG  HIS A 214    13138   9396   7624   -570    821   1771       C  
ATOM    910  ND1 HIS A 214     -19.455  28.115  -8.516  1.00 81.27           N  
ANISOU  910  ND1 HIS A 214    13092   9932   7856   -515    857   1601       N  
ATOM    911  CD2 HIS A 214     -20.012  29.998  -7.486  1.00 80.15           C  
ANISOU  911  CD2 HIS A 214    13237   9271   7947   -663    784   1702       C  
ATOM    912  CE1 HIS A 214     -19.332  27.955  -7.210  1.00 81.47           C  
ANISOU  912  CE1 HIS A 214    12944   9913   8097   -583    835   1457       C  
ATOM    913  NE2 HIS A 214     -19.664  29.060  -6.553  1.00 81.33           N  
ANISOU  913  NE2 HIS A 214    13090   9598   8212   -674    794   1504       N  
ATOM    914  N   SER A 215     -22.236  31.520 -12.200  1.00 80.84           N  
ANISOU  914  N   SER A 215    14348   9108   7258   -129    517   2418       N  
ATOM    915  CA  SER A 215     -22.430  32.152 -13.510  1.00 82.62           C  
ANISOU  915  CA  SER A 215    14908   9279   7205    -75    490   2684       C  
ATOM    916  C   SER A 215     -22.823  33.621 -13.355  1.00 83.23           C  
ANISOU  916  C   SER A 215    15314   8929   7381   -112    433   2893       C  
ATOM    917  O   SER A 215     -22.554  34.410 -14.246  1.00 83.52           O  
ANISOU  917  O   SER A 215    15656   8864   7212   -210    492   3172       O  
ATOM    918  CB  SER A 215     -23.451  31.400 -14.364  1.00 85.07           C  
ANISOU  918  CB  SER A 215    15242   9725   7355    256    262   2632       C  
ATOM    919  OG  SER A 215     -24.784  31.614 -13.930  1.00 88.50           O  
ANISOU  919  OG  SER A 215    15684   9944   7998    505      8   2576       O  
ATOM    920  N   LEU A 216     -23.459  33.988 -12.229  1.00 83.42           N  
ANISOU  920  N   LEU A 216    15298   8693   7705    -20    322   2762       N  
ATOM    921  CA  LEU A 216     -23.797  35.371 -11.886  1.00 83.71           C  
ANISOU  921  CA  LEU A 216    15654   8281   7872    -31    268   2904       C  
ATOM    922  C   LEU A 216     -22.600  36.078 -11.181  1.00 84.13           C  
ANISOU  922  C   LEU A 216    15756   8176   8031   -447    465   2937       C  
ATOM    923  O   LEU A 216     -22.763  37.192 -10.692  1.00 84.43           O  
ANISOU  923  O   LEU A 216    16063   7805   8212   -498    421   3002       O  
ATOM    924  CB  LEU A 216     -24.998  35.344 -10.927  1.00 83.67           C  
ANISOU  924  CB  LEU A 216    15545   8117   8130    277     89   2704       C  
ATOM    925  CG  LEU A 216     -26.407  35.715 -11.418  1.00 84.68           C  
ANISOU  925  CG  LEU A 216    15823   8092   8258    683   -157   2787       C  
ATOM    926  CD1 LEU A 216     -26.644  35.370 -12.858  1.00 85.08           C  
ANISOU  926  CD1 LEU A 216    15970   8340   8017    798   -259   2958       C  
ATOM    927  CD2 LEU A 216     -27.459  35.037 -10.559  1.00 85.38           C  
ANISOU  927  CD2 LEU A 216    15590   8282   8571    959   -281   2538       C  
ATOM    928  N   ASN A 217     -21.421  35.416 -11.118  1.00 83.91           N  
ANISOU  928  N   ASN A 217    15466   8473   7944   -730    662   2882       N  
ATOM    929  CA  ASN A 217     -20.181  35.855 -10.490  1.00 84.39           C  
ANISOU  929  CA  ASN A 217    15464   8497   8104  -1152    836   2896       C  
ATOM    930  C   ASN A 217     -20.293  36.014  -8.969  1.00 83.31           C  
ANISOU  930  C   ASN A 217    15226   8167   8262  -1181    767   2648       C  
ATOM    931  O   ASN A 217     -19.541  36.785  -8.366  1.00 83.61           O  
ANISOU  931  O   ASN A 217    15354   7998   8414  -1509    825   2675       O  
ATOM    932  CB  ASN A 217     -19.632  37.102 -11.146  1.00 86.98           C  
ANISOU  932  CB  ASN A 217    16156   8560   8333  -1442    922   3228       C  
ATOM    933  CG  ASN A 217     -18.159  36.984 -11.425  1.00 92.87           C  
ANISOU  933  CG  ASN A 217    16720   9578   8989  -1875   1175   3347       C  
ATOM    934  OD1 ASN A 217     -17.364  36.750 -10.502  1.00 94.53           O  
ANISOU  934  OD1 ASN A 217    16652   9894   9370  -2110   1244   3183       O  
ATOM    935  ND2 ASN A 217     -17.759  37.150 -12.707  1.00 94.56           N  
ANISOU  935  ND2 ASN A 217    17076   9930   8921  -1986   1319   3648       N  
ATOM    936  N   ILE A 218     -21.198  35.236  -8.353  1.00 81.64           N  
ANISOU  936  N   ILE A 218    14818   8044   8158   -857    644   2406       N  
ATOM    937  CA  ILE A 218     -21.470  35.241  -6.924  1.00 80.34           C  
ANISOU  937  CA  ILE A 218    14551   7748   8226   -811    583   2161       C  
ATOM    938  C   ILE A 218     -20.780  34.067  -6.233  1.00 79.25           C  
ANISOU  938  C   ILE A 218    14001   7976   8136   -916    662   1952       C  
ATOM    939  O   ILE A 218     -20.695  32.983  -6.809  1.00 79.51           O  
ANISOU  939  O   ILE A 218    13800   8350   8058   -822    692   1924       O  
ATOM    940  CB  ILE A 218     -23.003  35.175  -6.720  1.00 80.66           C  
ANISOU  940  CB  ILE A 218    14640   7657   8351   -372    411   2070       C  
ATOM    941  CG1 ILE A 218     -23.692  36.374  -7.399  1.00 81.75           C  
ANISOU  941  CG1 ILE A 218    15193   7426   8444   -219    311   2287       C  
ATOM    942  CG2 ILE A 218     -23.370  35.076  -5.241  1.00 81.12           C  
ANISOU  942  CG2 ILE A 218    14589   7620   8613   -288    380   1818       C  
ATOM    943  CD1 ILE A 218     -25.222  36.412  -7.299  1.00 83.11           C  
ANISOU  943  CD1 ILE A 218    15390   7484   8704    243    135   2227       C  
ATOM    944  N   VAL A 219     -20.269  34.282  -5.000  1.00 77.73           N  
ANISOU  944  N   VAL A 219    13742   7698   8095  -1103    677   1800       N  
ATOM    945  CA  VAL A 219     -19.658  33.214  -4.215  1.00 76.38           C  
ANISOU  945  CA  VAL A 219    13198   7846   7977  -1178    722   1606       C  
ATOM    946  C   VAL A 219     -20.450  33.102  -2.921  1.00 75.31           C  
ANISOU  946  C   VAL A 219    13031   7593   7990   -984    624   1383       C  
ATOM    947  O   VAL A 219     -20.663  34.100  -2.242  1.00 75.80           O  
ANISOU  947  O   VAL A 219    13333   7329   8137  -1025    578   1338       O  
ATOM    948  CB  VAL A 219     -18.130  33.372  -3.985  1.00 76.28           C  
ANISOU  948  CB  VAL A 219    13055   7961   7966  -1602    837   1641       C  
ATOM    949  CG1 VAL A 219     -17.609  32.289  -3.053  1.00 76.68           C  
ANISOU  949  CG1 VAL A 219    12735   8317   8084  -1621    843   1433       C  
ATOM    950  CG2 VAL A 219     -17.373  33.327  -5.301  1.00 76.32           C  
ANISOU  950  CG2 VAL A 219    13026   8172   7799  -1760    981   1869       C  
ATOM    951  N   TYR A 220     -20.970  31.915  -2.632  1.00 73.93           N  
ANISOU  951  N   TYR A 220    12593   7665   7834   -754    592   1252       N  
ATOM    952  CA  TYR A 220     -21.766  31.650  -1.440  1.00 73.42           C  
ANISOU  952  CA  TYR A 220    12452   7560   7884   -558    530   1065       C  
ATOM    953  C   TYR A 220     -20.860  31.834  -0.212  1.00 74.15           C  
ANISOU  953  C   TYR A 220    12497   7645   8032   -801    556    927       C  
ATOM    954  O   TYR A 220     -21.208  32.599   0.689  1.00 74.33           O  
ANISOU  954  O   TYR A 220    12708   7419   8115   -770    519    827       O  
ATOM    955  CB  TYR A 220     -22.298  30.211  -1.520  1.00 72.41           C  
ANISOU  955  CB  TYR A 220    12025   7731   7755   -352    500    996       C  
ATOM    956  CG  TYR A 220     -23.577  29.918  -0.771  1.00 71.75           C  
ANISOU  956  CG  TYR A 220    11875   7616   7773    -70    435    892       C  
ATOM    957  CD1 TYR A 220     -23.705  30.224   0.576  1.00 72.09           C  
ANISOU  957  CD1 TYR A 220    11942   7561   7890    -58    454    754       C  
ATOM    958  CD2 TYR A 220     -24.604  29.209  -1.373  1.00 72.19           C  
ANISOU  958  CD2 TYR A 220    11808   7784   7838    168    358    926       C  
ATOM    959  CE1 TYR A 220     -24.849  29.881   1.288  1.00 72.75           C  
ANISOU  959  CE1 TYR A 220    11923   7670   8047    199    435    673       C  
ATOM    960  CE2 TYR A 220     -25.757  28.881  -0.681  1.00 72.94           C  
ANISOU  960  CE2 TYR A 220    11779   7895   8039    396    314    853       C  
ATOM    961  CZ  TYR A 220     -25.869  29.200   0.654  1.00 73.63           C  
ANISOU  961  CZ  TYR A 220    11877   7906   8193    415    373    734       C  
ATOM    962  OH  TYR A 220     -27.015  28.850   1.316  1.00 74.86           O  
ANISOU  962  OH  TYR A 220    11883   8122   8437    643    366    682       O  
ATOM    963  N   ARG A 221     -19.671  31.180  -0.231  1.00 74.17           N  
ANISOU  963  N   ARG A 221    12259   7921   8000  -1033    612    921       N  
ATOM    964  CA  ARG A 221     -18.630  31.192   0.786  1.00 74.75           C  
ANISOU  964  CA  ARG A 221    12223   8067   8112  -1289    611    810       C  
ATOM    965  C   ARG A 221     -19.049  30.495   2.095  1.00 75.05           C  
ANISOU  965  C   ARG A 221    12127   8194   8195  -1128    556    615       C  
ATOM    966  O   ARG A 221     -18.299  29.663   2.608  1.00 75.82           O  
ANISOU  966  O   ARG A 221    11964   8556   8288  -1205    554    547       O  
ATOM    967  CB  ARG A 221     -18.110  32.617   1.035  1.00 76.35           C  
ANISOU  967  CB  ARG A 221    12715   7949   8346  -1570    588    841       C  
ATOM    968  CG  ARG A 221     -16.766  32.670   1.744  1.00 79.71           C  
ANISOU  968  CG  ARG A 221    12990   8500   8798  -1939    575    786       C  
ATOM    969  CD  ARG A 221     -16.887  33.232   3.132  1.00 84.21           C  
ANISOU  969  CD  ARG A 221    13728   8855   9413  -1996    464    592       C  
ATOM    970  NE  ARG A 221     -17.447  34.583   3.123  1.00 89.14           N  
ANISOU  970  NE  ARG A 221    14793   9014  10063  -1987    418    600       N  
ATOM    971  CZ  ARG A 221     -17.744  35.281   4.217  1.00 93.24           C  
ANISOU  971  CZ  ARG A 221    15571   9259  10599  -1962    324    415       C  
ATOM    972  NH1 ARG A 221     -17.532  34.762   5.425  1.00 93.09           N  
ANISOU  972  NH1 ARG A 221    15411   9406  10554  -1962    266    217       N  
ATOM    973  NH2 ARG A 221     -18.266  36.498   4.115  1.00 93.86           N  
ANISOU  973  NH2 ARG A 221    16074   8888  10701  -1911    283    423       N  
ATOM    974  N   ASP A 222     -20.248  30.811   2.606  1.00 73.84           N  
ANISOU  974  N   ASP A 222    12145   7837   8074   -887    521    540       N  
ATOM    975  CA  ASP A 222     -20.813  30.301   3.839  1.00 73.08           C  
ANISOU  975  CA  ASP A 222    11969   7803   7995   -717    499    382       C  
ATOM    976  C   ASP A 222     -21.913  29.230   3.655  1.00 71.54           C  
ANISOU  976  C   ASP A 222    11581   7777   7824   -417    508    400       C  
ATOM    977  O   ASP A 222     -22.919  29.266   4.359  1.00 71.82           O  
ANISOU  977  O   ASP A 222    11647   7755   7886   -198    515    332       O  
ATOM    978  CB  ASP A 222     -21.342  31.479   4.668  1.00 75.99           C  
ANISOU  978  CB  ASP A 222    12656   7847   8371   -646    478    276       C  
ATOM    979  CG  ASP A 222     -20.332  32.594   4.860  1.00 83.70           C  
ANISOU  979  CG  ASP A 222    13869   8594   9338   -971    433    249       C  
ATOM    980  OD1 ASP A 222     -19.289  32.349   5.514  1.00 85.48           O  
ANISOU  980  OD1 ASP A 222    13975   8962   9541  -1221    393    171       O  
ATOM    981  OD2 ASP A 222     -20.588  33.715   4.374  1.00 86.72           O  
ANISOU  981  OD2 ASP A 222    14562   8645   9742   -979    419    311       O  
ATOM    982  N   LEU A 223     -21.725  28.267   2.743  1.00 69.94           N  
ANISOU  982  N   LEU A 223    11177   7787   7611   -410    508    486       N  
ATOM    983  CA  LEU A 223     -22.692  27.174   2.564  1.00 68.73           C  
ANISOU  983  CA  LEU A 223    10842   7778   7493   -180    482    497       C  
ATOM    984  C   LEU A 223     -22.593  26.249   3.801  1.00 68.97           C  
ANISOU  984  C   LEU A 223    10690   7975   7541   -171    481    396       C  
ATOM    985  O   LEU A 223     -21.686  25.419   3.869  1.00 69.59           O  
ANISOU  985  O   LEU A 223    10610   8235   7596   -284    469    380       O  
ATOM    986  CB  LEU A 223     -22.333  26.362   1.305  1.00 67.61           C  
ANISOU  986  CB  LEU A 223    10584   7797   7309   -194    463    584       C  
ATOM    987  CG  LEU A 223     -23.393  25.557   0.496  1.00 67.48           C  
ANISOU  987  CG  LEU A 223    10469   7855   7315     15    390    627       C  
ATOM    988  CD1 LEU A 223     -22.849  24.232   0.050  1.00 67.48           C  
ANISOU  988  CD1 LEU A 223    10285   8071   7283     -8    364    603       C  
ATOM    989  CD2 LEU A 223     -24.706  25.380   1.190  1.00 67.39           C  
ANISOU  989  CD2 LEU A 223    10404   7798   7405    207    354    601       C  
ATOM    990  N   LYS A 224     -23.497  26.412   4.777  1.00 67.90           N  
ANISOU  990  N   LYS A 224    10581   7784   7434    -21    501    337       N  
ATOM    991  CA  LYS A 224     -23.549  25.586   5.992  1.00 67.16           C  
ANISOU  991  CA  LYS A 224    10351   7839   7329      3    514    268       C  
ATOM    992  C   LYS A 224     -24.860  24.767   5.963  1.00 67.39           C  
ANISOU  992  C   LYS A 224    10219   7953   7435    207    519    327       C  
ATOM    993  O   LYS A 224     -25.839  25.222   5.378  1.00 67.89           O  
ANISOU  993  O   LYS A 224    10314   7927   7554    359    519    378       O  
ATOM    994  CB  LYS A 224     -23.630  26.506   7.238  1.00 67.28           C  
ANISOU  994  CB  LYS A 224    10551   7732   7282     16    561    152       C  
ATOM    995  CG  LYS A 224     -22.419  27.340   7.526  1.00 69.31           C  
ANISOU  995  CG  LYS A 224    10967   7896   7470   -220    526     73       C  
ATOM    996  CD  LYS A 224     -22.776  28.498   8.409  1.00 73.88           C  
ANISOU  996  CD  LYS A 224    11822   8256   7991   -165    551    -50       C  
ATOM    997  CE  LYS A 224     -21.886  29.686   8.093  1.00 81.14           C  
ANISOU  997  CE  LYS A 224    12972   8957   8901   -406    492    -81       C  
ATOM    998  NZ  LYS A 224     -22.275  30.947   8.821  1.00 85.39           N  
ANISOU  998  NZ  LYS A 224    13862   9186   9397   -330    496   -208       N  
ATOM    999  N   PRO A 225     -24.967  23.644   6.695  1.00 67.00           N  
ANISOU  999  N   PRO A 225    10000   8065   7391    213    521    329       N  
ATOM   1000  CA  PRO A 225     -26.258  22.949   6.802  1.00 66.78           C  
ANISOU 1000  CA  PRO A 225     9810   8112   7450    361    534    401       C  
ATOM   1001  C   PRO A 225     -27.324  23.838   7.453  1.00 67.39           C  
ANISOU 1001  C   PRO A 225     9947   8129   7528    541    642    379       C  
ATOM   1002  O   PRO A 225     -28.506  23.669   7.176  1.00 67.34           O  
ANISOU 1002  O   PRO A 225     9805   8162   7620    688    653    454       O  
ATOM   1003  CB  PRO A 225     -25.925  21.772   7.716  1.00 67.02           C  
ANISOU 1003  CB  PRO A 225     9716   8293   7456    289    531    412       C  
ATOM   1004  CG  PRO A 225     -24.475  21.552   7.532  1.00 67.40           C  
ANISOU 1004  CG  PRO A 225     9803   8366   7440    134    466    363       C  
ATOM   1005  CD  PRO A 225     -23.945  22.949   7.490  1.00 66.36           C  
ANISOU 1005  CD  PRO A 225     9863   8107   7243     80    500    285       C  
ATOM   1006  N   GLU A 226     -26.915  24.787   8.317  1.00 67.60           N  
ANISOU 1006  N   GLU A 226    10174   8066   7446    538    713    268       N  
ATOM   1007  CA  GLU A 226     -27.796  25.763   8.965  1.00 67.89           C  
ANISOU 1007  CA  GLU A 226    10328   8017   7452    746    826    207       C  
ATOM   1008  C   GLU A 226     -28.615  26.554   7.901  1.00 67.09           C  
ANISOU 1008  C   GLU A 226    10269   7768   7454    919    801    261       C  
ATOM   1009  O   GLU A 226     -29.773  26.895   8.143  1.00 67.46           O  
ANISOU 1009  O   GLU A 226    10257   7829   7546   1164    882    275       O  
ATOM   1010  CB  GLU A 226     -26.915  26.706   9.816  1.00 71.42           C  
ANISOU 1010  CB  GLU A 226    11061   8325   7751    664    844     48       C  
ATOM   1011  CG  GLU A 226     -27.545  28.017  10.246  1.00 80.39           C  
ANISOU 1011  CG  GLU A 226    12432   9272   8839    881    932    -59       C  
ATOM   1012  CD  GLU A 226     -26.719  28.852  11.213  1.00 93.15           C  
ANISOU 1012  CD  GLU A 226    14359  10739  10294    789    926   -244       C  
ATOM   1013  OE1 GLU A 226     -25.547  29.160  10.889  1.00 95.62           O  
ANISOU 1013  OE1 GLU A 226    14792  10945  10594    526    808   -275       O  
ATOM   1014  OE2 GLU A 226     -27.249  29.210  12.293  1.00 97.17           O  
ANISOU 1014  OE2 GLU A 226    14989  11248  10684    978   1038   -361       O  
ATOM   1015  N   ASN A 227     -28.012  26.796   6.719  1.00 65.53           N  
ANISOU 1015  N   ASN A 227    10160   7454   7285    802    691    305       N  
ATOM   1016  CA  ASN A 227     -28.573  27.548   5.603  1.00 64.97           C  
ANISOU 1016  CA  ASN A 227    10180   7229   7279    933    633    377       C  
ATOM   1017  C   ASN A 227     -29.249  26.710   4.526  1.00 64.07           C  
ANISOU 1017  C   ASN A 227     9838   7244   7263    982    532    507       C  
ATOM   1018  O   ASN A 227     -29.764  27.277   3.573  1.00 64.17           O  
ANISOU 1018  O   ASN A 227     9920   7151   7311   1101    459    579       O  
ATOM   1019  CB  ASN A 227     -27.467  28.340   4.938  1.00 66.74           C  
ANISOU 1019  CB  ASN A 227    10661   7257   7441    748    580    371       C  
ATOM   1020  CG  ASN A 227     -26.742  29.281   5.868  1.00 72.79           C  
ANISOU 1020  CG  ASN A 227    11686   7848   8121    648    629    239       C  
ATOM   1021  OD1 ASN A 227     -27.336  29.997   6.723  1.00 74.01           O  
ANISOU 1021  OD1 ASN A 227    11979   7889   8252    829    699    139       O  
ATOM   1022  ND2 ASN A 227     -25.426  29.306   5.708  1.00 74.53           N  
ANISOU 1022  ND2 ASN A 227    11978   8052   8290    360    588    228       N  
ATOM   1023  N   ILE A 228     -29.200  25.383   4.619  1.00 62.90           N  
ANISOU 1023  N   ILE A 228     9453   7299   7148    881    501    537       N  
ATOM   1024  CA  ILE A 228     -29.786  24.502   3.618  1.00 61.84           C  
ANISOU 1024  CA  ILE A 228     9128   7266   7100    895    371    634       C  
ATOM   1025  C   ILE A 228     -31.136  24.030   4.112  1.00 62.94           C  
ANISOU 1025  C   ILE A 228     9005   7545   7363   1038    392    692       C  
ATOM   1026  O   ILE A 228     -31.181  23.229   5.043  1.00 63.53           O  
ANISOU 1026  O   ILE A 228     8934   7751   7452    968    463    690       O  
ATOM   1027  CB  ILE A 228     -28.852  23.310   3.378  1.00 60.40           C  
ANISOU 1027  CB  ILE A 228     8882   7182   6884    689    305    624       C  
ATOM   1028  CG1 ILE A 228     -27.486  23.787   2.914  1.00 60.06           C  
ANISOU 1028  CG1 ILE A 228     9042   7054   6723    548    312    581       C  
ATOM   1029  CG2 ILE A 228     -29.471  22.335   2.390  1.00 60.59           C  
ANISOU 1029  CG2 ILE A 228     8749   7285   6987    700    148    694       C  
ATOM   1030  CD1 ILE A 228     -26.449  22.731   2.922  1.00 60.85           C  
ANISOU 1030  CD1 ILE A 228     9073   7266   6780    390    284    550       C  
ATOM   1031  N   LEU A 229     -32.239  24.523   3.523  1.00 63.15           N  
ANISOU 1031  N   LEU A 229     8957   7558   7477   1238    336    760       N  
ATOM   1032  CA  LEU A 229     -33.576  24.124   3.988  1.00 63.86           C  
ANISOU 1032  CA  LEU A 229     8735   7823   7706   1374    368    832       C  
ATOM   1033  C   LEU A 229     -34.295  23.202   2.997  1.00 64.48           C  
ANISOU 1033  C   LEU A 229     8576   8010   7912   1330    160    935       C  
ATOM   1034  O   LEU A 229     -33.810  22.978   1.901  1.00 64.75           O  
ANISOU 1034  O   LEU A 229     8730   7970   7901   1246     -8    937       O  
ATOM   1035  CB  LEU A 229     -34.456  25.357   4.320  1.00 63.89           C  
ANISOU 1035  CB  LEU A 229     8758   7781   7736   1684    479    824       C  
ATOM   1036  CG  LEU A 229     -33.828  26.536   5.030  1.00 64.59           C  
ANISOU 1036  CG  LEU A 229     9179   7669   7691   1771    621    699       C  
ATOM   1037  CD1 LEU A 229     -34.752  27.695   5.010  1.00 64.92           C  
ANISOU 1037  CD1 LEU A 229     9277   7612   7778   2113    658    701       C  
ATOM   1038  CD2 LEU A 229     -33.496  26.196   6.432  1.00 64.98           C  
ANISOU 1038  CD2 LEU A 229     9220   7813   7656   1710    806    615       C  
ATOM   1039  N   LEU A 230     -35.454  22.674   3.379  1.00 64.90           N  
ANISOU 1039  N   LEU A 230     8294   8250   8117   1377    169   1022       N  
ATOM   1040  CA  LEU A 230     -36.236  21.797   2.524  1.00 65.91           C  
ANISOU 1040  CA  LEU A 230     8171   8482   8388   1307    -56   1117       C  
ATOM   1041  C   LEU A 230     -37.619  22.405   2.338  1.00 67.93           C  
ANISOU 1041  C   LEU A 230     8172   8855   8784   1558    -83   1207       C  
ATOM   1042  O   LEU A 230     -38.250  22.744   3.330  1.00 67.60           O  
ANISOU 1042  O   LEU A 230     7958   8935   8793   1705    124   1231       O  
ATOM   1043  CB  LEU A 230     -36.351  20.426   3.215  1.00 65.17           C  
ANISOU 1043  CB  LEU A 230     7855   8523   8384   1076    -38   1171       C  
ATOM   1044  CG  LEU A 230     -35.795  19.202   2.489  1.00 65.22           C  
ANISOU 1044  CG  LEU A 230     7919   8467   8393    827   -253   1155       C  
ATOM   1045  CD1 LEU A 230     -34.441  19.479   1.795  1.00 64.94           C  
ANISOU 1045  CD1 LEU A 230     8247   8257   8169    799   -297   1035       C  
ATOM   1046  CD2 LEU A 230     -35.693  18.043   3.436  1.00 65.39           C  
ANISOU 1046  CD2 LEU A 230     7818   8555   8472    622   -181   1206       C  
ATOM   1047  N   ASP A 231     -38.098  22.554   1.091  1.00 69.86           N  
ANISOU 1047  N   ASP A 231     8385   9081   9076   1633   -335   1255       N  
ATOM   1048  CA  ASP A 231     -39.431  23.119   0.880  1.00 72.29           C  
ANISOU 1048  CA  ASP A 231     8415   9523   9530   1897   -392   1350       C  
ATOM   1049  C   ASP A 231     -40.526  22.085   1.267  1.00 74.45           C  
ANISOU 1049  C   ASP A 231     8188  10073  10026   1778   -434   1466       C  
ATOM   1050  O   ASP A 231     -40.195  20.948   1.641  1.00 74.74           O  
ANISOU 1050  O   ASP A 231     8162  10146  10089   1481   -433   1473       O  
ATOM   1051  CB  ASP A 231     -39.594  23.735  -0.529  1.00 74.36           C  
ANISOU 1051  CB  ASP A 231     8830   9677   9748   2044   -657   1378       C  
ATOM   1052  CG  ASP A 231     -39.653  22.773  -1.693  1.00 80.12           C  
ANISOU 1052  CG  ASP A 231     9523  10436  10485   1838   -986   1402       C  
ATOM   1053  OD1 ASP A 231     -39.937  21.580  -1.463  1.00 80.97           O  
ANISOU 1053  OD1 ASP A 231     9385  10672  10710   1600  -1056   1421       O  
ATOM   1054  OD2 ASP A 231     -39.427  23.220  -2.852  1.00 82.96           O  
ANISOU 1054  OD2 ASP A 231    10125  10678  10718   1916  -1180   1404       O  
ATOM   1055  N   SER A 232     -41.819  22.477   1.227  1.00 75.49           N  
ANISOU 1055  N   SER A 232     7957  10400  10325   2007   -465   1570       N  
ATOM   1056  CA  SER A 232     -42.895  21.561   1.613  1.00 76.70           C  
ANISOU 1056  CA  SER A 232     7588  10846  10709   1871   -492   1707       C  
ATOM   1057  C   SER A 232     -42.917  20.278   0.777  1.00 77.41           C  
ANISOU 1057  C   SER A 232     7599  10929  10884   1511   -826   1741       C  
ATOM   1058  O   SER A 232     -43.391  19.247   1.258  1.00 78.17           O  
ANISOU 1058  O   SER A 232     7390  11175  11136   1249   -823   1835       O  
ATOM   1059  CB  SER A 232     -44.244  22.254   1.516  1.00 78.69           C  
ANISOU 1059  CB  SER A 232     7444  11324  11131   2197   -517   1814       C  
ATOM   1060  OG  SER A 232     -44.593  22.451   0.153  1.00 82.36           O  
ANISOU 1060  OG  SER A 232     7925  11741  11628   2272   -890   1838       O  
ATOM   1061  N   GLN A 233     -42.434  20.342  -0.480  1.00 77.01           N  
ANISOU 1061  N   GLN A 233     7841  10697  10721   1495  -1116   1669       N  
ATOM   1062  CA  GLN A 233     -42.432  19.172  -1.360  1.00 76.90           C  
ANISOU 1062  CA  GLN A 233     7820  10648  10750   1191  -1458   1661       C  
ATOM   1063  C   GLN A 233     -41.214  18.253  -1.151  1.00 76.16           C  
ANISOU 1063  C   GLN A 233     8041  10367  10528    910  -1406   1555       C  
ATOM   1064  O   GLN A 233     -41.294  17.067  -1.458  1.00 76.73           O  
ANISOU 1064  O   GLN A 233     8057  10416  10680    630  -1622   1555       O  
ATOM   1065  CB  GLN A 233     -42.589  19.583  -2.836  1.00 78.57           C  
ANISOU 1065  CB  GLN A 233     8192  10788  10871   1320  -1803   1633       C  
ATOM   1066  N   GLY A 234     -40.123  18.787  -0.608  1.00 74.63           N  
ANISOU 1066  N   GLY A 234     8167  10038  10151    988  -1137   1467       N  
ATOM   1067  CA  GLY A 234     -38.918  18.007  -0.353  1.00 73.64           C  
ANISOU 1067  CA  GLY A 234     8316   9760   9904    771  -1075   1372       C  
ATOM   1068  C   GLY A 234     -37.683  18.437  -1.127  1.00 72.28           C  
ANISOU 1068  C   GLY A 234     8583   9393   9488    824  -1108   1239       C  
ATOM   1069  O   GLY A 234     -36.648  17.770  -1.064  1.00 72.47           O  
ANISOU 1069  O   GLY A 234     8818   9308   9410    668  -1091   1153       O  
ATOM   1070  N   HIS A 235     -37.768  19.560  -1.851  1.00 70.72           N  
ANISOU 1070  N   HIS A 235     8521   9155   9193   1050  -1148   1236       N  
ATOM   1071  CA  HIS A 235     -36.646  20.094  -2.620  1.00 69.67           C  
ANISOU 1071  CA  HIS A 235     8792   8858   8821   1092  -1153   1148       C  
ATOM   1072  C   HIS A 235     -35.740  21.043  -1.798  1.00 68.39           C  
ANISOU 1072  C   HIS A 235     8840   8599   8548   1169   -846   1106       C  
ATOM   1073  O   HIS A 235     -36.208  21.722  -0.889  1.00 68.25           O  
ANISOU 1073  O   HIS A 235     8706   8619   8606   1307   -666   1141       O  
ATOM   1074  CB  HIS A 235     -37.149  20.800  -3.899  1.00 70.38           C  
ANISOU 1074  CB  HIS A 235     8971   8930   8838   1269  -1378   1193       C  
ATOM   1075  CG  HIS A 235     -37.618  19.861  -4.963  1.00 71.64           C  
ANISOU 1075  CG  HIS A 235     9070   9141   9009   1161  -1726   1184       C  
ATOM   1076  ND1 HIS A 235     -38.946  19.765  -5.298  1.00 73.04           N  
ANISOU 1076  ND1 HIS A 235     8928   9458   9364   1211  -1962   1273       N  
ATOM   1077  CD2 HIS A 235     -36.913  18.982  -5.714  1.00 72.74           C  
ANISOU 1077  CD2 HIS A 235     9427   9210   8999   1009  -1875   1081       C  
ATOM   1078  CE1 HIS A 235     -39.013  18.847  -6.253  1.00 73.62           C  
ANISOU 1078  CE1 HIS A 235     9061   9525   9388   1065  -2274   1217       C  
ATOM   1079  NE2 HIS A 235     -37.813  18.343  -6.531  1.00 73.62           N  
ANISOU 1079  NE2 HIS A 235     9398   9392   9183    956  -2225   1092       N  
ATOM   1080  N   ILE A 236     -34.440  21.080  -2.135  1.00 67.47           N  
ANISOU 1080  N   ILE A 236     9026   8364   8243   1080   -794   1023       N  
ATOM   1081  CA  ILE A 236     -33.417  21.931  -1.513  1.00 66.94           C  
ANISOU 1081  CA  ILE A 236     9183   8193   8059   1092   -554    974       C  
ATOM   1082  C   ILE A 236     -33.717  23.400  -1.840  1.00 67.55           C  
ANISOU 1082  C   ILE A 236     9415   8163   8090   1306   -525   1026       C  
ATOM   1083  O   ILE A 236     -34.025  23.720  -2.985  1.00 67.89           O  
ANISOU 1083  O   ILE A 236     9548   8175   8074   1395   -700   1083       O  
ATOM   1084  CB  ILE A 236     -32.003  21.533  -2.088  1.00 66.13           C  
ANISOU 1084  CB  ILE A 236     9319   8031   7776    937   -554    895       C  
ATOM   1085  CG1 ILE A 236     -31.497  20.206  -1.522  1.00 66.42           C  
ANISOU 1085  CG1 ILE A 236     9257   8130   7852    763   -542    830       C  
ATOM   1086  CG2 ILE A 236     -30.945  22.632  -1.951  1.00 65.93           C  
ANISOU 1086  CG2 ILE A 236     9552   7890   7608    934   -377    873       C  
ATOM   1087  CD1 ILE A 236     -31.231  20.229  -0.092  1.00 67.80           C  
ANISOU 1087  CD1 ILE A 236     9356   8326   8080    718   -343    816       C  
ATOM   1088  N   VAL A 237     -33.649  24.287  -0.846  1.00 67.48           N  
ANISOU 1088  N   VAL A 237     9463   8083   8095   1399   -321   1005       N  
ATOM   1089  CA  VAL A 237     -33.740  25.725  -1.091  1.00 67.75           C  
ANISOU 1089  CA  VAL A 237     9725   7942   8076   1593   -285   1039       C  
ATOM   1090  C   VAL A 237     -32.697  26.377  -0.169  1.00 67.73           C  
ANISOU 1090  C   VAL A 237     9947   7799   7987   1509    -70    948       C  
ATOM   1091  O   VAL A 237     -32.708  26.173   1.046  1.00 67.48           O  
ANISOU 1091  O   VAL A 237     9809   7832   8001   1489     78    879       O  
ATOM   1092  CB  VAL A 237     -35.147  26.407  -1.130  1.00 68.23           C  
ANISOU 1092  CB  VAL A 237     9637   8022   8264   1906   -346   1119       C  
ATOM   1093  CG1 VAL A 237     -36.245  25.520  -0.560  1.00 68.89           C  
ANISOU 1093  CG1 VAL A 237     9287   8354   8533   1938   -369   1148       C  
ATOM   1094  CG2 VAL A 237     -35.148  27.811  -0.513  1.00 68.31           C  
ANISOU 1094  CG2 VAL A 237     9865   7835   8256   2118   -184   1091       C  
ATOM   1095  N   LEU A 238     -31.702  27.020  -0.794  1.00 67.76           N  
ANISOU 1095  N   LEU A 238    10258   7635   7853   1414    -67    955       N  
ATOM   1096  CA  LEU A 238     -30.587  27.629  -0.092  1.00 68.28           C  
ANISOU 1096  CA  LEU A 238    10543   7562   7837   1271     89    876       C  
ATOM   1097  C   LEU A 238     -30.900  29.057   0.297  1.00 69.87           C  
ANISOU 1097  C   LEU A 238    10976   7523   8050   1452    156    869       C  
ATOM   1098  O   LEU A 238     -31.588  29.776  -0.430  1.00 70.41           O  
ANISOU 1098  O   LEU A 238    11142   7473   8138   1661     65    962       O  
ATOM   1099  CB  LEU A 238     -29.308  27.564  -0.941  1.00 67.68           C  
ANISOU 1099  CB  LEU A 238    10645   7453   7620   1038     73    900       C  
ATOM   1100  CG  LEU A 238     -28.943  26.171  -1.462  1.00 67.99           C  
ANISOU 1100  CG  LEU A 238    10504   7704   7625    905      1    888       C  
ATOM   1101  CD1 LEU A 238     -27.806  26.226  -2.444  1.00 67.91           C  
ANISOU 1101  CD1 LEU A 238    10663   7687   7453    744      7    924       C  
ATOM   1102  CD2 LEU A 238     -28.640  25.226  -0.336  1.00 68.23           C  
ANISOU 1102  CD2 LEU A 238    10338   7869   7716    800     76    788       C  
ATOM   1103  N   THR A 239     -30.437  29.444   1.481  1.00 70.37           N  
ANISOU 1103  N   THR A 239    11137   7507   8095   1392    298    750       N  
ATOM   1104  CA  THR A 239     -30.596  30.773   2.050  1.00 71.37           C  
ANISOU 1104  CA  THR A 239    11536   7367   8215   1546    371    690       C  
ATOM   1105  C   THR A 239     -29.217  31.305   2.495  1.00 73.47           C  
ANISOU 1105  C   THR A 239    12073   7461   8382   1263    431    604       C  
ATOM   1106  O   THR A 239     -28.270  30.540   2.660  1.00 73.16           O  
ANISOU 1106  O   THR A 239    11930   7573   8294    994    447    574       O  
ATOM   1107  CB  THR A 239     -31.575  30.722   3.238  1.00 71.37           C  
ANISOU 1107  CB  THR A 239    11367   7468   8283   1796    483    597       C  
ATOM   1108  OG1 THR A 239     -30.977  30.002   4.308  1.00 72.00           O  
ANISOU 1108  OG1 THR A 239    11336   7707   8315   1609    586    491       O  
ATOM   1109  CG2 THR A 239     -32.882  30.063   2.892  1.00 71.42           C  
ANISOU 1109  CG2 THR A 239    11022   7703   8413   2016    427    694       C  
ATOM   1110  N   ASP A 240     -29.110  32.605   2.680  1.00 75.58           N  
ANISOU 1110  N   ASP A 240    12684   7404   8628   1324    448    565       N  
ATOM   1111  CA  ASP A 240     -27.894  33.231   3.177  1.00 78.25           C  
ANISOU 1111  CA  ASP A 240    13291   7548   8893   1041    478    478       C  
ATOM   1112  C   ASP A 240     -26.702  33.137   2.227  1.00 80.05           C  
ANISOU 1112  C   ASP A 240    13573   7777   9065    694    431    596       C  
ATOM   1113  O   ASP A 240     -25.578  32.871   2.668  1.00 80.75           O  
ANISOU 1113  O   ASP A 240    13634   7938   9107    392    460    532       O  
ATOM   1114  CB  ASP A 240     -27.543  32.676   4.562  1.00 81.08           C  
ANISOU 1114  CB  ASP A 240    13524   8070   9212    951    563    301       C  
ATOM   1115  CG  ASP A 240     -27.737  33.668   5.679  1.00 88.37           C  
ANISOU 1115  CG  ASP A 240    14737   8743  10096   1075    615    126       C  
ATOM   1116  OD1 ASP A 240     -27.408  34.873   5.476  1.00 89.08           O  
ANISOU 1116  OD1 ASP A 240    15202   8467  10178   1031    565    117       O  
ATOM   1117  OD2 ASP A 240     -28.200  33.248   6.765  1.00 92.16           O  
ANISOU 1117  OD2 ASP A 240    15096   9382  10540   1212    705     -2       O  
ATOM   1118  N   PHE A 241     -26.929  33.393   0.936  1.00 80.52           N  
ANISOU 1118  N   PHE A 241    13709   7769   9115    746    362    774       N  
ATOM   1119  CA  PHE A 241     -25.841  33.368  -0.033  1.00 81.86           C  
ANISOU 1119  CA  PHE A 241    13938   7962   9201    441    352    908       C  
ATOM   1120  C   PHE A 241     -25.268  34.742  -0.305  1.00 84.63           C  
ANISOU 1120  C   PHE A 241    14694   7937   9525    281    343    993       C  
ATOM   1121  O   PHE A 241     -24.892  35.058  -1.428  1.00 84.23           O  
ANISOU 1121  O   PHE A 241    14767   7833   9402    153    326   1182       O  
ATOM   1122  CB  PHE A 241     -26.216  32.645  -1.319  1.00 81.26           C  
ANISOU 1122  CB  PHE A 241    13702   8095   9078    530    289   1055       C  
ATOM   1123  CG  PHE A 241     -27.617  32.868  -1.820  1.00 81.18           C  
ANISOU 1123  CG  PHE A 241    13708   8021   9115    895    187   1129       C  
ATOM   1124  CD1 PHE A 241     -27.910  33.935  -2.648  1.00 81.38           C  
ANISOU 1124  CD1 PHE A 241    14044   7772   9105   1004    118   1285       C  
ATOM   1125  CD2 PHE A 241     -28.633  31.984  -1.500  1.00 81.53           C  
ANISOU 1125  CD2 PHE A 241    13442   8291   9245   1120    150   1064       C  
ATOM   1126  CE1 PHE A 241     -29.189  34.117  -3.133  1.00 81.91           C  
ANISOU 1126  CE1 PHE A 241    14097   7808   9218   1362     -2   1362       C  
ATOM   1127  CE2 PHE A 241     -29.912  32.175  -1.982  1.00 81.94           C  
ANISOU 1127  CE2 PHE A 241    13454   8324   9357   1446     40   1142       C  
ATOM   1128  CZ  PHE A 241     -30.178  33.229  -2.809  1.00 81.75           C  
ANISOU 1128  CZ  PHE A 241    13724   8044   9292   1579    -43   1286       C  
ATOM   1129  N   GLY A 242     -25.184  35.531   0.758  1.00 87.54           N  
ANISOU 1129  N   GLY A 242    15280   8042   9937    274    355    851       N  
ATOM   1130  CA  GLY A 242     -24.564  36.842   0.795  1.00 90.47           C  
ANISOU 1130  CA  GLY A 242    16064   8004  10306     68    330    884       C  
ATOM   1131  C   GLY A 242     -25.104  37.925  -0.099  1.00 93.57           C  
ANISOU 1131  C   GLY A 242    16825   8024  10706    229    262   1059       C  
ATOM   1132  O   GLY A 242     -24.355  38.848  -0.440  1.00 93.88           O  
ANISOU 1132  O   GLY A 242    17188   7753  10730    -48    240   1165       O  
ATOM   1133  N   LEU A 243     -26.396  37.855  -0.470  1.00 95.80           N  
ANISOU 1133  N   LEU A 243    17065   8318  11017    664    215   1102       N  
ATOM   1134  CA  LEU A 243     -26.983  38.932  -1.287  1.00 98.33           C  
ANISOU 1134  CA  LEU A 243    17757   8260  11343    873    123   1275       C  
ATOM   1135  C   LEU A 243     -27.006  40.252  -0.462  1.00101.12           C  
ANISOU 1135  C   LEU A 243    18555   8108  11758    928    101   1148       C  
ATOM   1136  O   LEU A 243     -26.741  41.327  -0.999  1.00101.52           O  
ANISOU 1136  O   LEU A 243    19032   7738  11803    838     35   1296       O  
ATOM   1137  CB  LEU A 243     -28.385  38.560  -1.805  1.00 98.23           C  
ANISOU 1137  CB  LEU A 243    17567   8395  11361   1345     49   1344       C  
ATOM   1138  CG  LEU A 243     -28.549  38.488  -3.317  1.00 98.82           C  
ANISOU 1138  CG  LEU A 243    17657   8549  11342   1358    -43   1615       C  
ATOM   1139  CD1 LEU A 243     -28.241  39.820  -3.968  1.00 99.21           C  
ANISOU 1139  CD1 LEU A 243    18212   8144  11338   1258    -99   1824       C  
ATOM   1140  CD2 LEU A 243     -27.694  37.404  -3.898  1.00 99.13           C  
ANISOU 1140  CD2 LEU A 243    17400   8986  11278   1038     14   1656       C  
ATOM   1141  N   CYS A 244     -27.251  40.148   0.854  1.00102.81           N  
ANISOU 1141  N   CYS A 244    18696   8355  12012   1051    156    875       N  
ATOM   1142  CA  CYS A 244     -27.213  41.283   1.761  1.00104.94           C  
ANISOU 1142  CA  CYS A 244    19395   8169  12310   1097    134    696       C  
ATOM   1143  C   CYS A 244     -26.752  40.831   3.163  1.00106.31           C  
ANISOU 1143  C   CYS A 244    19425   8516  12453    961    207    408       C  
ATOM   1144  O   CYS A 244     -27.558  40.307   3.936  1.00106.54           O  
ANISOU 1144  O   CYS A 244    19227   8775  12480   1292    283    247       O  
ATOM   1145  CB  CYS A 244     -28.557  42.003   1.804  1.00106.53           C  
ANISOU 1145  CB  CYS A 244    19813   8094  12568   1666     95    668       C  
ATOM   1146  SG  CYS A 244     -28.465  43.764   1.372  1.00112.88           S  
ANISOU 1146  SG  CYS A 244    21351   8134  13405   1678    -38    771       S  
ATOM   1147  N   LYS A 245     -25.438  41.012   3.462  1.00106.78           N  
ANISOU 1147  N   LYS A 245    19599   8491  12481    459    181    365       N  
ATOM   1148  CA  LYS A 245     -24.777  40.658   4.726  1.00107.46           C  
ANISOU 1148  CA  LYS A 245    19593   8721  12517    250    204    114       C  
ATOM   1149  C   LYS A 245     -25.037  39.217   5.185  1.00107.90           C  
ANISOU 1149  C   LYS A 245    19122   9342  12535    363    305     46       C  
ATOM   1150  O   LYS A 245     -24.310  38.301   4.799  1.00108.04           O  
ANISOU 1150  O   LYS A 245    18805   9703  12542     87    324    154       O  
ATOM   1151  CB  LYS A 245     -25.125  41.657   5.837  1.00109.36           C  
ANISOU 1151  CB  LYS A 245    20265   8554  12734    450    167   -157       C  
ATOM   1152  N   THR A 254     -12.289  32.461  22.419  1.00 85.27           N  
ANISOU 1152  N   THR A 254    15025   9998   7375  -2594  -1846  -2247       N  
ATOM   1153  CA  THR A 254     -12.739  31.241  21.744  1.00 85.98           C  
ANISOU 1153  CA  THR A 254    14714  10347   7606  -2336  -1583  -1965       C  
ATOM   1154  C   THR A 254     -13.064  30.114  22.796  1.00 85.78           C  
ANISOU 1154  C   THR A 254    14628  10660   7305  -2037  -1554  -1926       C  
ATOM   1155  O   THR A 254     -13.123  30.391  23.999  1.00 85.76           O  
ANISOU 1155  O   THR A 254    14942  10666   6977  -1981  -1684  -2124       O  
ATOM   1156  CB  THR A 254     -11.735  30.829  20.598  1.00 87.76           C  
ANISOU 1156  CB  THR A 254    14447  10738   8161  -2613  -1632  -1739       C  
ATOM   1157  OG1 THR A 254     -12.420  30.032  19.616  1.00 88.22           O  
ANISOU 1157  OG1 THR A 254    14250  10880   8389  -2357  -1337  -1509       O  
ATOM   1158  CG2 THR A 254     -10.486  30.079  21.131  1.00 88.45           C  
ANISOU 1158  CG2 THR A 254    14187  11212   8208  -2801  -1914  -1696       C  
ATOM   1159  N   SER A 255     -13.350  28.879  22.311  1.00 85.15           N  
ANISOU 1159  N   SER A 255    14183  10824   7344  -1837  -1373  -1669       N  
ATOM   1160  CA  SER A 255     -13.693  27.686  23.073  1.00 84.71           C  
ANISOU 1160  CA  SER A 255    14033  11061   7092  -1573  -1316  -1557       C  
ATOM   1161  C   SER A 255     -12.597  26.634  22.905  1.00 83.60           C  
ANISOU 1161  C   SER A 255    13466  11241   7058  -1687  -1504  -1383       C  
ATOM   1162  O   SER A 255     -11.927  26.577  21.872  1.00 83.88           O  
ANISOU 1162  O   SER A 255    13187  11302   7382  -1862  -1532  -1278       O  
ATOM   1163  CB  SER A 255     -15.004  27.094  22.545  1.00 86.20           C  
ANISOU 1163  CB  SER A 255    14153  11226   7372  -1251   -959  -1388       C  
ATOM   1164  OG  SER A 255     -14.898  26.676  21.191  1.00 87.34           O  
ANISOU 1164  OG  SER A 255    13958  11370   7855  -1300   -866  -1198       O  
ATOM   1165  N   THR A 256     -12.451  25.772  23.901  1.00 82.19           N  
ANISOU 1165  N   THR A 256    13277  11315   6637  -1558  -1614  -1337       N  
ATOM   1166  CA  THR A 256     -11.481  24.683  23.854  1.00 81.32           C  
ANISOU 1166  CA  THR A 256    12781  11510   6606  -1588  -1796  -1163       C  
ATOM   1167  C   THR A 256     -12.171  23.457  23.227  1.00 80.03           C  
ANISOU 1167  C   THR A 256    12400  11419   6591  -1319  -1541   -907       C  
ATOM   1168  O   THR A 256     -11.646  22.844  22.298  1.00 80.27           O  
ANISOU 1168  O   THR A 256    12075  11539   6885  -1342  -1541   -761       O  
ATOM   1169  CB  THR A 256     -10.768  24.469  25.229  1.00 82.82           C  
ANISOU 1169  CB  THR A 256    13076  11924   6467  -1622  -2120  -1242       C  
ATOM   1170  OG1 THR A 256     -10.312  23.124  25.360  1.00 83.75           O  
ANISOU 1170  OG1 THR A 256    12891  12326   6602  -1482  -2210  -1019       O  
ATOM   1171  CG2 THR A 256     -11.616  24.849  26.440  1.00 83.69           C  
ANISOU 1171  CG2 THR A 256    13662  11967   6171  -1459  -2060  -1390       C  
ATOM   1172  N   PHE A 257     -13.390  23.159  23.680  1.00 78.60           N  
ANISOU 1172  N   PHE A 257    12438  11183   6244  -1071  -1312   -863       N  
ATOM   1173  CA  PHE A 257     -14.175  22.056  23.147  1.00 77.04           C  
ANISOU 1173  CA  PHE A 257    12077  11016   6179   -849  -1080   -630       C  
ATOM   1174  C   PHE A 257     -15.397  22.545  22.423  1.00 77.00           C  
ANISOU 1174  C   PHE A 257    12164  10786   6305   -754   -775   -640       C  
ATOM   1175  O   PHE A 257     -15.832  23.684  22.585  1.00 77.00           O  
ANISOU 1175  O   PHE A 257    12428  10609   6221   -781   -708   -824       O  
ATOM   1176  CB  PHE A 257     -14.585  21.063  24.237  1.00 75.79           C  
ANISOU 1176  CB  PHE A 257    12024  11025   5747   -651  -1063   -497       C  
ATOM   1177  CG  PHE A 257     -13.423  20.520  25.008  1.00 75.00           C  
ANISOU 1177  CG  PHE A 257    11848  11155   5495   -705  -1388   -466       C  
ATOM   1178  CD1 PHE A 257     -12.637  19.516  24.484  1.00 75.39           C  
ANISOU 1178  CD1 PHE A 257    11562  11333   5750   -688  -1520   -297       C  
ATOM   1179  CD2 PHE A 257     -13.109  21.020  26.252  1.00 75.24           C  
ANISOU 1179  CD2 PHE A 257    12147  11274   5169   -754  -1579   -620       C  
ATOM   1180  CE1 PHE A 257     -11.552  19.029  25.195  1.00 76.06           C  
ANISOU 1180  CE1 PHE A 257    11553  11642   5706   -708  -1839   -264       C  
ATOM   1181  CE2 PHE A 257     -12.032  20.523  26.962  1.00 75.87           C  
ANISOU 1181  CE2 PHE A 257    12143  11580   5102   -798  -1915   -585       C  
ATOM   1182  CZ  PHE A 257     -11.278  19.511  26.446  1.00 75.71           C  
ANISOU 1182  CZ  PHE A 257    11764  11698   5306   -765  -2042   -396       C  
ATOM   1183  N   CYS A 258     -15.943  21.640  21.621  1.00 77.00           N  
ANISOU 1183  N   CYS A 258    11952  10791   6513   -628   -612   -441       N  
ATOM   1184  CA  CYS A 258     -17.077  21.764  20.753  1.00 77.27           C  
ANISOU 1184  CA  CYS A 258    11970  10665   6726   -520   -351   -385       C  
ATOM   1185  C   CYS A 258     -16.814  22.816  19.698  1.00 78.01           C  
ANISOU 1185  C   CYS A 258    12047  10570   7022   -668   -348   -497       C  
ATOM   1186  O   CYS A 258     -16.107  22.489  18.723  1.00 79.53           O  
ANISOU 1186  O   CYS A 258    11992  10797   7431   -768   -418   -424       O  
ATOM   1187  CB  CYS A 258     -18.380  21.942  21.522  1.00 78.02           C  
ANISOU 1187  CB  CYS A 258    12290  10730   6624   -332   -130   -394       C  
ATOM   1188  SG  CYS A 258     -18.653  20.645  22.762  1.00 82.70           S  
ANISOU 1188  SG  CYS A 258    12904  11562   6956   -192   -114   -205       S  
ATOM   1189  N   GLY A 259     -17.306  24.038  19.848  1.00 76.94           N  
ANISOU 1189  N   GLY A 259    12174  10239   6819   -678   -273   -664       N  
ATOM   1190  CA  GLY A 259     -17.082  25.048  18.820  1.00 76.72           C  
ANISOU 1190  CA  GLY A 259    12164   9998   6988   -827   -273   -737       C  
ATOM   1191  C   GLY A 259     -17.909  24.696  17.605  1.00 76.31           C  
ANISOU 1191  C   GLY A 259    11959   9873   7164   -696    -78   -588       C  
ATOM   1192  O   GLY A 259     -17.963  23.531  17.206  1.00 76.24           O  
ANISOU 1192  O   GLY A 259    11708  10008   7251   -617    -48   -420       O  
ATOM   1193  N   THR A 260     -18.592  25.688  17.036  1.00 76.03           N  
ANISOU 1193  N   THR A 260    12084   9598   7204   -657     38   -652       N  
ATOM   1194  CA  THR A 260     -19.484  25.501  15.901  1.00 76.06           C  
ANISOU 1194  CA  THR A 260    11974   9524   7403   -518    202   -523       C  
ATOM   1195  C   THR A 260     -18.783  24.854  14.729  1.00 74.71           C  
ANISOU 1195  C   THR A 260    11528   9430   7428   -636    145   -390       C  
ATOM   1196  O   THR A 260     -17.674  25.257  14.374  1.00 75.04           O  
ANISOU 1196  O   THR A 260    11530   9466   7517   -860     25   -425       O  
ATOM   1197  CB  THR A 260     -20.142  26.824  15.558  1.00 78.67           C  
ANISOU 1197  CB  THR A 260    12562   9573   7758   -455    290   -628       C  
ATOM   1198  OG1 THR A 260     -19.109  27.710  15.140  1.00 80.70           O  
ANISOU 1198  OG1 THR A 260    12928   9673   8061   -720    149   -714       O  
ATOM   1199  CG2 THR A 260     -20.875  27.437  16.773  1.00 79.47           C  
ANISOU 1199  CG2 THR A 260    12942   9618   7635   -271    373   -782       C  
ATOM   1200  N   PRO A 261     -19.375  23.790  14.167  1.00 73.04           N  
ANISOU 1200  N   PRO A 261    11117   9315   7321   -495    224   -238       N  
ATOM   1201  CA  PRO A 261     -18.727  23.104  13.039  1.00 72.24           C  
ANISOU 1201  CA  PRO A 261    10780   9293   7375   -564    176   -134       C  
ATOM   1202  C   PRO A 261     -18.231  24.025  11.921  1.00 71.58           C  
ANISOU 1202  C   PRO A 261    10718   9083   7395   -712    175   -149       C  
ATOM   1203  O   PRO A 261     -18.841  25.067  11.616  1.00 71.49           O  
ANISOU 1203  O   PRO A 261    10897   8862   7403   -695    245   -188       O  
ATOM   1204  CB  PRO A 261     -19.789  22.114  12.562  1.00 72.77           C  
ANISOU 1204  CB  PRO A 261    10730   9384   7534   -374    269     -3       C  
ATOM   1205  CG  PRO A 261     -20.634  21.876  13.752  1.00 73.43           C  
ANISOU 1205  CG  PRO A 261    10897   9510   7492   -251    335      1       C  
ATOM   1206  CD  PRO A 261     -20.667  23.170  14.512  1.00 72.04           C  
ANISOU 1206  CD  PRO A 261    10970   9229   7174   -276    359   -156       C  
ATOM   1207  N   GLU A 262     -17.081  23.659  11.355  1.00 70.74           N  
ANISOU 1207  N   GLU A 262    10418   9113   7348   -851     99   -110       N  
ATOM   1208  CA  GLU A 262     -16.461  24.468  10.328  1.00 70.54           C  
ANISOU 1208  CA  GLU A 262    10387   9015   7401  -1029    113    -94       C  
ATOM   1209  C   GLU A 262     -16.570  23.862   8.942  1.00 69.77           C  
ANISOU 1209  C   GLU A 262    10136   8969   7403   -946    192     22       C  
ATOM   1210  O   GLU A 262     -16.126  22.735   8.734  1.00 70.26           O  
ANISOU 1210  O   GLU A 262     9981   9226   7488   -882    164     68       O  
ATOM   1211  CB  GLU A 262     -14.987  24.743  10.677  1.00 72.75           C  
ANISOU 1211  CB  GLU A 262    10548   9431   7661  -1290    -15   -139       C  
ATOM   1212  CG  GLU A 262     -14.365  25.817   9.808  1.00 76.74           C  
ANISOU 1212  CG  GLU A 262    11083   9838   8236  -1541      8   -112       C  
ATOM   1213  CD  GLU A 262     -14.991  27.183  10.007  1.00 82.34           C  
ANISOU 1213  CD  GLU A 262    12145  10215   8923  -1614     24   -185       C  
ATOM   1214  OE1 GLU A 262     -14.569  27.894  10.948  1.00 83.75           O  
ANISOU 1214  OE1 GLU A 262    12476  10308   9035  -1786    -95   -309       O  
ATOM   1215  OE2 GLU A 262     -15.913  27.538   9.237  1.00 83.55           O  
ANISOU 1215  OE2 GLU A 262    12440  10186   9120  -1485    138   -126       O  
ATOM   1216  N   TYR A 263     -17.154  24.608   7.986  1.00 68.32           N  
ANISOU 1216  N   TYR A 263    10089   8606   7265   -931    277     66       N  
ATOM   1217  CA  TYR A 263     -17.238  24.155   6.594  1.00 67.37           C  
ANISOU 1217  CA  TYR A 263     9865   8535   7199   -861    340    168       C  
ATOM   1218  C   TYR A 263     -16.433  25.033   5.645  1.00 68.39           C  
ANISOU 1218  C   TYR A 263    10011   8640   7336  -1069    385    225       C  
ATOM   1219  O   TYR A 263     -16.378  24.731   4.451  1.00 69.08           O  
ANISOU 1219  O   TYR A 263    10028   8793   7427  -1021    450    311       O  
ATOM   1220  CB  TYR A 263     -18.690  24.038   6.095  1.00 66.08           C  
ANISOU 1220  CB  TYR A 263     9806   8233   7068   -643    389    210       C  
ATOM   1221  CG  TYR A 263     -19.543  23.188   6.997  1.00 65.56           C  
ANISOU 1221  CG  TYR A 263     9700   8205   7007   -472    369    187       C  
ATOM   1222  CD1 TYR A 263     -20.002  23.678   8.214  1.00 65.67           C  
ANISOU 1222  CD1 TYR A 263     9838   8146   6967   -452    376    116       C  
ATOM   1223  CD2 TYR A 263     -19.831  21.866   6.676  1.00 65.67           C  
ANISOU 1223  CD2 TYR A 263     9562   8328   7063   -343    344    238       C  
ATOM   1224  CE1 TYR A 263     -20.695  22.872   9.103  1.00 65.73           C  
ANISOU 1224  CE1 TYR A 263     9793   8227   6954   -318    383    121       C  
ATOM   1225  CE2 TYR A 263     -20.543  21.053   7.552  1.00 66.18           C  
ANISOU 1225  CE2 TYR A 263     9583   8426   7135   -233    327    249       C  
ATOM   1226  CZ  TYR A 263     -20.963  21.561   8.774  1.00 66.47           C  
ANISOU 1226  CZ  TYR A 263     9720   8427   7109   -226    359    204       C  
ATOM   1227  OH  TYR A 263     -21.724  20.834   9.657  1.00 67.53           O  
ANISOU 1227  OH  TYR A 263     9816   8613   7229   -126    377    241       O  
ATOM   1228  N   LEU A 264     -15.841  26.129   6.139  1.00 68.53           N  
ANISOU 1228  N   LEU A 264    10143   8553   7344  -1309    350    185       N  
ATOM   1229  CA  LEU A 264     -15.053  27.046   5.329  1.00 69.45           C  
ANISOU 1229  CA  LEU A 264    10285   8626   7478  -1568    392    267       C  
ATOM   1230  C   LEU A 264     -13.806  26.332   4.794  1.00 70.17           C  
ANISOU 1230  C   LEU A 264    10040   9046   7574  -1670    424    330       C  
ATOM   1231  O   LEU A 264     -13.175  25.549   5.520  1.00 70.50           O  
ANISOU 1231  O   LEU A 264     9861   9308   7617  -1654    348    268       O  
ATOM   1232  CB  LEU A 264     -14.661  28.261   6.188  1.00 69.76           C  
ANISOU 1232  CB  LEU A 264    10521   8467   7518  -1830    305    186       C  
ATOM   1233  CG  LEU A 264     -15.396  29.615   6.030  1.00 70.83           C  
ANISOU 1233  CG  LEU A 264    11043   8208   7663  -1867    318    188       C  
ATOM   1234  CD1 LEU A 264     -16.828  29.481   5.566  1.00 71.21           C  
ANISOU 1234  CD1 LEU A 264    11235   8116   7707  -1531    389    219       C  
ATOM   1235  CD2 LEU A 264     -15.306  30.432   7.326  1.00 70.91           C  
ANISOU 1235  CD2 LEU A 264    11282   8017   7644  -1997    194     21       C  
ATOM   1236  N   ALA A 265     -13.488  26.565   3.510  1.00 70.07           N  
ANISOU 1236  N   ALA A 265     9991   9082   7550  -1739    544    460       N  
ATOM   1237  CA  ALA A 265     -12.334  25.952   2.858  1.00 70.47           C  
ANISOU 1237  CA  ALA A 265     9721   9468   7589  -1805    623    530       C  
ATOM   1238  C   ALA A 265     -11.032  26.361   3.559  1.00 70.99           C  
ANISOU 1238  C   ALA A 265     9580   9688   7705  -2122    555    515       C  
ATOM   1239  O   ALA A 265     -10.987  27.450   4.135  1.00 71.47           O  
ANISOU 1239  O   ALA A 265     9826   9532   7799  -2373    472    488       O  
ATOM   1240  CB  ALA A 265     -12.301  26.369   1.398  1.00 70.46           C  
ANISOU 1240  CB  ALA A 265     9784   9459   7529  -1854    782    685       C  
ATOM   1241  N   PRO A 266      -9.961  25.533   3.535  1.00 70.68           N  
ANISOU 1241  N   PRO A 266     9161  10017   7677  -2114    570    524       N  
ATOM   1242  CA  PRO A 266      -8.718  25.930   4.218  1.00 71.07           C  
ANISOU 1242  CA  PRO A 266     8967  10247   7789  -2427    475    516       C  
ATOM   1243  C   PRO A 266      -8.199  27.339   3.874  1.00 72.49           C  
ANISOU 1243  C   PRO A 266     9222  10308   8012  -2863    514    624       C  
ATOM   1244  O   PRO A 266      -7.775  28.056   4.780  1.00 72.59           O  
ANISOU 1244  O   PRO A 266     9267  10234   8080  -3155    353    565       O  
ATOM   1245  CB  PRO A 266      -7.718  24.823   3.842  1.00 71.07           C  
ANISOU 1245  CB  PRO A 266     8525  10685   7792  -2283    538    544       C  
ATOM   1246  CG  PRO A 266      -8.362  24.028   2.767  1.00 70.99           C  
ANISOU 1246  CG  PRO A 266     8575  10692   7704  -1951    700    579       C  
ATOM   1247  CD  PRO A 266      -9.832  24.200   2.922  1.00 69.64           C  
ANISOU 1247  CD  PRO A 266     8810  10147   7505  -1804    654    529       C  
ATOM   1248  N   GLU A 267      -8.304  27.776   2.606  1.00 73.58           N  
ANISOU 1248  N   GLU A 267     9440  10405   8113  -2917    707    783       N  
ATOM   1249  CA  GLU A 267      -7.830  29.109   2.225  1.00 75.20           C  
ANISOU 1249  CA  GLU A 267     9747  10467   8360  -3351    753    926       C  
ATOM   1250  C   GLU A 267      -8.615  30.229   2.896  1.00 77.50           C  
ANISOU 1250  C   GLU A 267    10498  10265   8683  -3494    607    855       C  
ATOM   1251  O   GLU A 267      -8.054  31.297   3.145  1.00 78.27           O  
ANISOU 1251  O   GLU A 267    10676  10209   8852  -3908    535    902       O  
ATOM   1252  CB  GLU A 267      -7.768  29.302   0.704  1.00 75.96           C  
ANISOU 1252  CB  GLU A 267     9848  10642   8373  -3360   1005   1138       C  
ATOM   1253  CG  GLU A 267      -9.088  29.113  -0.015  1.00 77.66           C  
ANISOU 1253  CG  GLU A 267    10412  10615   8482  -3018   1069   1145       C  
ATOM   1254  CD  GLU A 267      -9.334  27.721  -0.560  1.00 80.71           C  
ANISOU 1254  CD  GLU A 267    10635  11259   8772  -2591   1151   1089       C  
ATOM   1255  OE1 GLU A 267      -8.540  26.800  -0.256  1.00 80.05           O  
ANISOU 1255  OE1 GLU A 267    10186  11521   8709  -2497   1151   1020       O  
ATOM   1256  OE2 GLU A 267     -10.328  27.555  -1.301  1.00 82.78           O  
ANISOU 1256  OE2 GLU A 267    11146  11367   8940  -2344   1198   1113       O  
ATOM   1257  N   VAL A 268      -9.893  29.995   3.197  1.00 78.30           N  
ANISOU 1257  N   VAL A 268    10896  10117   8737  -3157    559    741       N  
ATOM   1258  CA  VAL A 268     -10.698  30.994   3.883  1.00 79.99           C  
ANISOU 1258  CA  VAL A 268    11543   9880   8967  -3209    436    648       C  
ATOM   1259  C   VAL A 268     -10.248  31.074   5.357  1.00 82.10           C  
ANISOU 1259  C   VAL A 268    11778  10151   9266  -3351    222    458       C  
ATOM   1260  O   VAL A 268     -10.097  32.175   5.904  1.00 82.71           O  
ANISOU 1260  O   VAL A 268    12105   9943   9380  -3642     97    403       O  
ATOM   1261  CB  VAL A 268     -12.202  30.693   3.729  1.00 80.58           C  
ANISOU 1261  CB  VAL A 268    11881   9751   8984  -2786    472    599       C  
ATOM   1262  CG1 VAL A 268     -13.044  31.781   4.377  1.00 81.16           C  
ANISOU 1262  CG1 VAL A 268    12391   9376   9069  -2781    369    495       C  
ATOM   1263  CG2 VAL A 268     -12.565  30.556   2.256  1.00 81.01           C  
ANISOU 1263  CG2 VAL A 268    11967   9827   8987  -2665    643    783       C  
ATOM   1264  N   LEU A 269      -9.963  29.906   5.969  1.00 82.69           N  
ANISOU 1264  N   LEU A 269    11556  10546   9315  -3158    165    363       N  
ATOM   1265  CA  LEU A 269      -9.507  29.801   7.339  1.00 83.50           C  
ANISOU 1265  CA  LEU A 269    11598  10720   9409  -3249    -47    197       C  
ATOM   1266  C   LEU A 269      -8.178  30.501   7.562  1.00 85.26           C  
ANISOU 1266  C   LEU A 269    11640  11045   9711  -3728   -169    225       C  
ATOM   1267  O   LEU A 269      -8.073  31.235   8.551  1.00 85.73           O  
ANISOU 1267  O   LEU A 269    11925  10885   9763  -3947   -365     89       O  
ATOM   1268  CB  LEU A 269      -9.493  28.345   7.797  1.00 83.38           C  
ANISOU 1268  CB  LEU A 269    11308  11026   9348  -2925    -72    140       C  
ATOM   1269  CG  LEU A 269     -10.896  27.724   7.846  1.00 84.38           C  
ANISOU 1269  CG  LEU A 269    11651  11004   9405  -2510     -6     89       C  
ATOM   1270  CD1 LEU A 269     -10.841  26.251   8.036  1.00 84.87           C  
ANISOU 1270  CD1 LEU A 269    11447  11357   9443  -2221     -7     85       C  
ATOM   1271  CD2 LEU A 269     -11.738  28.344   8.928  1.00 84.62           C  
ANISOU 1271  CD2 LEU A 269    12040  10745   9366  -2475   -115    -67       C  
ATOM   1272  N   HIS A 270      -7.193  30.371   6.639  1.00 86.38           N  
ANISOU 1272  N   HIS A 270    11396  11503   9924  -3911    -53    398       N  
ATOM   1273  CA  HIS A 270      -5.950  31.128   6.851  1.00 88.14           C  
ANISOU 1273  CA  HIS A 270    11415  11827  10246  -4422   -172    447       C  
ATOM   1274  C   HIS A 270      -5.908  32.393   6.013  1.00 88.94           C  
ANISOU 1274  C   HIS A 270    11741  11641  10409  -4785    -69    612       C  
ATOM   1275  O   HIS A 270      -4.852  32.782   5.529  1.00 88.91           O  
ANISOU 1275  O   HIS A 270    11443  11842  10496  -5165    -16    777       O  
ATOM   1276  CB  HIS A 270      -4.636  30.338   6.761  1.00 89.66           C  
ANISOU 1276  CB  HIS A 270    10994  12573  10499  -4497   -171    520       C  
ATOM   1277  CG  HIS A 270      -4.691  29.076   5.983  1.00 92.72           C  
ANISOU 1277  CG  HIS A 270    11099  13291  10842  -4091     48    602       C  
ATOM   1278  ND1 HIS A 270      -4.500  27.852   6.594  1.00 94.65           N  
ANISOU 1278  ND1 HIS A 270    11070  13838  11057  -3764    -31    509       N  
ATOM   1279  CD2 HIS A 270      -4.834  28.891   4.652  1.00 94.38           C  
ANISOU 1279  CD2 HIS A 270    11278  13562  11021  -3979    325    764       C  
ATOM   1280  CE1 HIS A 270      -4.574  26.956   5.626  1.00 95.65           C  
ANISOU 1280  CE1 HIS A 270    11030  14167  11147  -3453    195    597       C  
ATOM   1281  NE2 HIS A 270      -4.777  27.534   4.438  1.00 95.89           N  
ANISOU 1281  NE2 HIS A 270    11196  14077  11162  -3567    415    744       N  
ATOM   1282  N   LYS A 271      -7.058  33.082   5.924  1.00 89.47           N  
ANISOU 1282  N   LYS A 271    12339  11223  10432  -4676    -56    570       N  
ATOM   1283  CA  LYS A 271      -7.238  34.386   5.287  1.00 90.47           C  
ANISOU 1283  CA  LYS A 271    12830  10940  10604  -4966     -6    704       C  
ATOM   1284  C   LYS A 271      -6.385  34.591   4.029  1.00 92.14           C  
ANISOU 1284  C   LYS A 271    12769  11371  10870  -5268    198    999       C  
ATOM   1285  O   LYS A 271      -5.433  35.371   4.030  1.00 92.29           O  
ANISOU 1285  O   LYS A 271    12683  11387  10996  -5785    131   1100       O  
ATOM   1286  CB  LYS A 271      -6.992  35.488   6.326  1.00 91.34           C  
ANISOU 1286  CB  LYS A 271    13255  10678  10771  -5336   -276    552       C  
ATOM   1287  CG  LYS A 271      -7.831  35.300   7.592  1.00 94.47           C  
ANISOU 1287  CG  LYS A 271    13937  10888  11069  -5018   -452    255       C  
ATOM   1288  CD  LYS A 271      -7.471  36.291   8.690  1.00 98.25           C  
ANISOU 1288  CD  LYS A 271    14755  11010  11568  -5363   -735     66       C  
ATOM   1289  CE  LYS A 271      -8.502  36.349   9.800  1.00101.45           C  
ANISOU 1289  CE  LYS A 271    15530  11188  11830  -5003   -857   -222       C  
ATOM   1290  NZ  LYS A 271      -8.441  37.646  10.545  1.00103.15           N  
ANISOU 1290  NZ  LYS A 271    16240  10915  12038  -5283  -1096   -413       N  
ATOM   1291  N   GLN A 272      -6.695  33.811   2.990  1.00 93.08           N  
ANISOU 1291  N   GLN A 272    12750  11711  10904  -4948    445   1132       N  
ATOM   1292  CA  GLN A 272      -5.991  33.793   1.711  1.00 94.36           C  
ANISOU 1292  CA  GLN A 272    12648  12151  11054  -5123    696   1410       C  
ATOM   1293  C   GLN A 272      -6.963  34.087   0.562  1.00 95.21           C  
ANISOU 1293  C   GLN A 272    13128  11998  11049  -4910    877   1563       C  
ATOM   1294  O   GLN A 272      -8.181  33.955   0.733  1.00 95.31           O  
ANISOU 1294  O   GLN A 272    13474  11738  11002  -4530    820   1435       O  
ATOM   1295  CB  GLN A 272      -5.378  32.387   1.489  1.00 96.24           C  
ANISOU 1295  CB  GLN A 272    12330  12990  11247  -4859    825   1403       C  
ATOM   1296  CG  GLN A 272      -4.380  31.956   2.533  1.00100.04           C  
ANISOU 1296  CG  GLN A 272    12385  13798  11827  -4998    646   1274       C  
ATOM   1297  CD  GLN A 272      -3.105  32.754   2.504  1.00104.70           C  
ANISOU 1297  CD  GLN A 272    12695  14536  12550  -5593    616   1425       C  
ATOM   1298  OE1 GLN A 272      -2.746  33.401   1.507  1.00106.49           O  
ANISOU 1298  OE1 GLN A 272    12911  14763  12787  -5895    811   1677       O  
ATOM   1299  NE2 GLN A 272      -2.378  32.698   3.607  1.00105.21           N  
ANISOU 1299  NE2 GLN A 272    12511  14749  12715  -5786    363   1285       N  
ATOM   1300  N   PRO A 273      -6.453  34.436  -0.643  1.00 95.54           N  
ANISOU 1300  N   PRO A 273    13097  12158  11047  -5132   1101   1850       N  
ATOM   1301  CA  PRO A 273      -7.362  34.636  -1.781  1.00 95.55           C  
ANISOU 1301  CA  PRO A 273    13448  11953  10905  -4898   1258   2005       C  
ATOM   1302  C   PRO A 273      -8.150  33.369  -2.091  1.00 95.17           C  
ANISOU 1302  C   PRO A 273    13312  12127  10721  -4318   1331   1885       C  
ATOM   1303  O   PRO A 273      -7.586  32.281  -2.288  1.00 95.52           O  
ANISOU 1303  O   PRO A 273    12931  12648  10714  -4164   1447   1860       O  
ATOM   1304  CB  PRO A 273      -6.432  34.997  -2.942  1.00 96.39           C  
ANISOU 1304  CB  PRO A 273    13375  12293  10956  -5246   1509   2338       C  
ATOM   1305  CG  PRO A 273      -5.082  34.544  -2.523  1.00 97.13           C  
ANISOU 1305  CG  PRO A 273    12879  12879  11147  -5506   1540   2328       C  
ATOM   1306  CD  PRO A 273      -5.045  34.643  -1.028  1.00 95.43           C  
ANISOU 1306  CD  PRO A 273    12664  12501  11096  -5595   1227   2059       C  
ATOM   1307  N   TYR A 274      -9.471  33.515  -2.039  1.00 93.88           N  
ANISOU 1307  N   TYR A 274    13551  11602  10518  -3993   1236   1790       N  
ATOM   1308  CA  TYR A 274     -10.401  32.447  -2.333  1.00 92.69           C  
ANISOU 1308  CA  TYR A 274    13384  11575  10257  -3478   1264   1682       C  
ATOM   1309  C   TYR A 274     -11.294  32.838  -3.516  1.00 91.62           C  
ANISOU 1309  C   TYR A 274    13604  11225   9984  -3305   1350   1852       C  
ATOM   1310  O   TYR A 274     -11.413  34.020  -3.853  1.00 91.74           O  
ANISOU 1310  O   TYR A 274    13950  10897  10009  -3533   1345   2019       O  
ATOM   1311  CB  TYR A 274     -11.206  32.080  -1.086  1.00 92.28           C  
ANISOU 1311  CB  TYR A 274    13413  11362  10286  -3220   1060   1410       C  
ATOM   1312  CG  TYR A 274     -12.241  33.093  -0.652  1.00 92.57           C  
ANISOU 1312  CG  TYR A 274    13920  10880  10372  -3188    922   1358       C  
ATOM   1313  CD1 TYR A 274     -13.519  33.086  -1.195  1.00 93.30           C  
ANISOU 1313  CD1 TYR A 274    14293  10760  10398  -2841    922   1377       C  
ATOM   1314  CD2 TYR A 274     -11.993  33.959   0.402  1.00 93.30           C  
ANISOU 1314  CD2 TYR A 274    14163  10709  10576  -3460    768   1255       C  
ATOM   1315  CE1 TYR A 274     -14.491  33.981  -0.767  1.00 94.23           C  
ANISOU 1315  CE1 TYR A 274    14814  10423  10567  -2753    804   1320       C  
ATOM   1316  CE2 TYR A 274     -12.967  34.837   0.863  1.00 94.15           C  
ANISOU 1316  CE2 TYR A 274    14717  10339  10718  -3368    648   1171       C  
ATOM   1317  CZ  TYR A 274     -14.216  34.851   0.272  1.00 95.16           C  
ANISOU 1317  CZ  TYR A 274    15099  10271  10785  -3000    678   1209       C  
ATOM   1318  OH  TYR A 274     -15.180  35.728   0.717  1.00 96.77           O  
ANISOU 1318  OH  TYR A 274    15723  10020  11027  -2864    570   1126       O  
ATOM   1319  N   ASP A 275     -11.916  31.851  -4.146  1.00 90.43           N  
ANISOU 1319  N   ASP A 275    13402  11255   9702  -2905   1404   1811       N  
ATOM   1320  CA  ASP A 275     -12.762  32.098  -5.310  1.00 89.47           C  
ANISOU 1320  CA  ASP A 275    13588  10983   9423  -2712   1456   1963       C  
ATOM   1321  C   ASP A 275     -14.028  31.197  -5.273  1.00 87.58           C  
ANISOU 1321  C   ASP A 275    13415  10712   9151  -2234   1337   1789       C  
ATOM   1322  O   ASP A 275     -14.496  30.870  -4.187  1.00 87.52           O  
ANISOU 1322  O   ASP A 275    13374  10603   9279  -2109   1192   1586       O  
ATOM   1323  CB  ASP A 275     -11.938  32.009  -6.625  1.00 91.61           C  
ANISOU 1323  CB  ASP A 275    13736  11574   9497  -2832   1701   2198       C  
ATOM   1324  CG  ASP A 275     -11.027  30.795  -6.795  1.00 97.87           C  
ANISOU 1324  CG  ASP A 275    14075  12893  10216  -2724   1843   2114       C  
ATOM   1325  OD1 ASP A 275     -10.695  30.144  -5.777  1.00 99.59           O  
ANISOU 1325  OD1 ASP A 275    14020  13244  10576  -2673   1751   1906       O  
ATOM   1326  OD2 ASP A 275     -10.621  30.511  -7.950  1.00 99.98           O  
ANISOU 1326  OD2 ASP A 275    14275  13443  10271  -2678   2050   2260       O  
ATOM   1327  N   ARG A 276     -14.620  30.864  -6.424  1.00 85.86           N  
ANISOU 1327  N   ARG A 276    13308  10564   8750  -1989   1386   1876       N  
ATOM   1328  CA  ARG A 276     -15.802  30.003  -6.476  1.00 84.46           C  
ANISOU 1328  CA  ARG A 276    13173  10368   8551  -1581   1254   1728       C  
ATOM   1329  C   ARG A 276     -15.504  28.584  -5.998  1.00 81.90           C  
ANISOU 1329  C   ARG A 276    12504  10355   8258  -1414   1244   1520       C  
ATOM   1330  O   ARG A 276     -16.425  27.868  -5.625  1.00 81.87           O  
ANISOU 1330  O   ARG A 276    12498  10299   8312  -1148   1105   1369       O  
ATOM   1331  CB  ARG A 276     -16.398  29.941  -7.892  1.00 86.57           C  
ANISOU 1331  CB  ARG A 276    13649  10650   8593  -1385   1277   1872       C  
ATOM   1332  CG  ARG A 276     -15.721  30.831  -8.923  1.00 91.18           C  
ANISOU 1332  CG  ARG A 276    14383  11261   9000  -1629   1453   2152       C  
ATOM   1333  CD  ARG A 276     -15.706  30.167 -10.277  1.00 95.54           C  
ANISOU 1333  CD  ARG A 276    14945  12096   9261  -1434   1552   2224       C  
ATOM   1334  NE  ARG A 276     -14.858  28.975 -10.275  1.00 98.71           N  
ANISOU 1334  NE  ARG A 276    14983  12911   9610  -1372   1675   2076       N  
ATOM   1335  CZ  ARG A 276     -14.132  28.572 -11.315  1.00101.10           C  
ANISOU 1335  CZ  ARG A 276    15200  13557   9658  -1355   1884   2164       C  
ATOM   1336  NH1 ARG A 276     -14.155  29.254 -12.457  1.00 99.57           N  
ANISOU 1336  NH1 ARG A 276    15261  13355   9217  -1420   1999   2417       N  
ATOM   1337  NH2 ARG A 276     -13.383  27.483 -11.223  1.00101.36           N  
ANISOU 1337  NH2 ARG A 276    14904  13944   9666  -1250   1985   2006       N  
ATOM   1338  N   THR A 277     -14.227  28.172  -6.034  1.00 79.78           N  
ANISOU 1338  N   THR A 277    11941  10413   7958  -1566   1390   1524       N  
ATOM   1339  CA  THR A 277     -13.766  26.861  -5.603  1.00 78.16           C  
ANISOU 1339  CA  THR A 277    11414  10501   7783  -1404   1385   1343       C  
ATOM   1340  C   THR A 277     -14.067  26.590  -4.110  1.00 75.38           C  
ANISOU 1340  C   THR A 277    10975  10028   7639  -1383   1216   1162       C  
ATOM   1341  O   THR A 277     -14.119  25.427  -3.714  1.00 75.38           O  
ANISOU 1341  O   THR A 277    10794  10178   7671  -1179   1158   1012       O  
ATOM   1342  CB  THR A 277     -12.283  26.687  -5.968  1.00 79.92           C  
ANISOU 1342  CB  THR A 277    11328  11105   7932  -1566   1590   1414       C  
ATOM   1343  OG1 THR A 277     -11.511  27.717  -5.341  1.00 81.81           O  
ANISOU 1343  OG1 THR A 277    11493  11297   8293  -1964   1625   1515       O  
ATOM   1344  CG2 THR A 277     -12.051  26.725  -7.449  1.00 79.78           C  
ANISOU 1344  CG2 THR A 277    11385  11268   7659  -1508   1780   1567       C  
ATOM   1345  N   VAL A 278     -14.294  27.639  -3.292  1.00 73.01           N  
ANISOU 1345  N   VAL A 278    10834   9445   7463  -1577   1135   1175       N  
ATOM   1346  CA  VAL A 278     -14.650  27.437  -1.880  1.00 71.28           C  
ANISOU 1346  CA  VAL A 278    10578   9113   7392  -1536    986   1003       C  
ATOM   1347  C   VAL A 278     -15.995  26.751  -1.740  1.00 68.74           C  
ANISOU 1347  C   VAL A 278    10353   8680   7085  -1201    877    903       C  
ATOM   1348  O   VAL A 278     -16.160  25.909  -0.861  1.00 68.50           O  
ANISOU 1348  O   VAL A 278    10181   8721   7124  -1080    798    767       O  
ATOM   1349  CB  VAL A 278     -14.580  28.721  -1.040  1.00 72.09           C  
ANISOU 1349  CB  VAL A 278    10865   8932   7594  -1801    922   1008       C  
ATOM   1350  CG1 VAL A 278     -13.240  29.399  -1.241  1.00 73.08           C  
ANISOU 1350  CG1 VAL A 278    10874   9168   7724  -2190   1013   1128       C  
ATOM   1351  CG2 VAL A 278     -15.726  29.669  -1.374  1.00 72.23           C  
ANISOU 1351  CG2 VAL A 278    11265   8574   7605  -1717    880   1077       C  
ATOM   1352  N   ASP A 279     -16.930  27.056  -2.655  1.00 66.52           N  
ANISOU 1352  N   ASP A 279    10295   8248   6734  -1057    869    989       N  
ATOM   1353  CA  ASP A 279     -18.249  26.454  -2.700  1.00 64.43           C  
ANISOU 1353  CA  ASP A 279    10093   7899   6488   -762    757    923       C  
ATOM   1354  C   ASP A 279     -18.201  24.983  -3.029  1.00 62.19           C  
ANISOU 1354  C   ASP A 279     9612   7857   6161   -580    737    838       C  
ATOM   1355  O   ASP A 279     -19.017  24.216  -2.507  1.00 62.38           O  
ANISOU 1355  O   ASP A 279     9583   7852   6266   -409    628    740       O  
ATOM   1356  CB  ASP A 279     -19.143  27.215  -3.674  1.00 65.06           C  
ANISOU 1356  CB  ASP A 279    10441   7783   6494   -668    731   1054       C  
ATOM   1357  CG  ASP A 279     -19.381  28.651  -3.260  1.00 68.13           C  
ANISOU 1357  CG  ASP A 279    11078   7857   6950   -788    718   1123       C  
ATOM   1358  OD1 ASP A 279     -19.200  28.964  -2.071  1.00 68.81           O  
ANISOU 1358  OD1 ASP A 279    11146   7847   7150   -885    696   1022       O  
ATOM   1359  OD2 ASP A 279     -19.749  29.458  -4.119  1.00 69.91           O  
ANISOU 1359  OD2 ASP A 279    11542   7920   7101   -774    719   1273       O  
ATOM   1360  N   TRP A 280     -17.238  24.578  -3.849  1.00 60.03           N  
ANISOU 1360  N   TRP A 280     9231   7816   5760   -616    847    875       N  
ATOM   1361  CA  TRP A 280     -17.088  23.181  -4.165  1.00 59.18           C  
ANISOU 1361  CA  TRP A 280     8969   7915   5601   -422    828    771       C  
ATOM   1362  C   TRP A 280     -16.511  22.437  -2.943  1.00 58.48           C  
ANISOU 1362  C   TRP A 280     8645   7933   5643   -436    793    650       C  
ATOM   1363  O   TRP A 280     -16.981  21.343  -2.643  1.00 58.39           O  
ANISOU 1363  O   TRP A 280     8576   7931   5679   -254    690    547       O  
ATOM   1364  CB  TRP A 280     -16.341  23.002  -5.493  1.00 59.01           C  
ANISOU 1364  CB  TRP A 280     8938   8115   5370   -397    972    837       C  
ATOM   1365  CG  TRP A 280     -17.018  23.721  -6.637  1.00 59.60           C  
ANISOU 1365  CG  TRP A 280     9282   8072   5291   -370    977    970       C  
ATOM   1366  CD1 TRP A 280     -16.479  24.700  -7.426  1.00 60.82           C  
ANISOU 1366  CD1 TRP A 280     9546   8260   5302   -536   1130   1151       C  
ATOM   1367  CD2 TRP A 280     -18.375  23.537  -7.099  1.00 59.47           C  
ANISOU 1367  CD2 TRP A 280     9458   7889   5250   -173    807    954       C  
ATOM   1368  NE1 TRP A 280     -17.401  25.113  -8.366  1.00 60.91           N  
ANISOU 1368  NE1 TRP A 280     9833   8130   5179   -428   1062   1250       N  
ATOM   1369  CE2 TRP A 280     -18.575  24.420  -8.177  1.00 60.41           C  
ANISOU 1369  CE2 TRP A 280     9809   7950   5192   -201    853   1123       C  
ATOM   1370  CE3 TRP A 280     -19.443  22.724  -6.690  1.00 59.62           C  
ANISOU 1370  CE3 TRP A 280     9461   7810   5384      8    613    830       C  
ATOM   1371  CZ2 TRP A 280     -19.793  24.502  -8.851  1.00 60.66           C  
ANISOU 1371  CZ2 TRP A 280    10050   7841   5158    -29    689   1157       C  
ATOM   1372  CZ3 TRP A 280     -20.638  22.797  -7.370  1.00 60.10           C  
ANISOU 1372  CZ3 TRP A 280     9695   7745   5397    150    461    863       C  
ATOM   1373  CH2 TRP A 280     -20.804  23.674  -8.436  1.00 60.38           C  
ANISOU 1373  CH2 TRP A 280     9953   7736   5252    144    489   1018       C  
ATOM   1374  N   TRP A 281     -15.634  23.094  -2.133  1.00 57.70           N  
ANISOU 1374  N   TRP A 281     8441   7871   5613   -667    844    671       N  
ATOM   1375  CA  TRP A 281     -15.152  22.526  -0.865  1.00 56.56           C  
ANISOU 1375  CA  TRP A 281     8103   7809   5578   -687    776    568       C  
ATOM   1376  C   TRP A 281     -16.370  22.349   0.073  1.00 56.52           C  
ANISOU 1376  C   TRP A 281     8214   7590   5671   -577    639    500       C  
ATOM   1377  O   TRP A 281     -16.598  21.248   0.576  1.00 56.58           O  
ANISOU 1377  O   TRP A 281     8126   7649   5722   -425    559    423       O  
ATOM   1378  CB  TRP A 281     -14.077  23.423  -0.194  1.00 55.65           C  
ANISOU 1378  CB  TRP A 281     7885   7751   5510   -987    817    603       C  
ATOM   1379  CG  TRP A 281     -13.783  23.032   1.232  1.00 55.35           C  
ANISOU 1379  CG  TRP A 281     7710   7755   5565  -1009    701    499       C  
ATOM   1380  CD1 TRP A 281     -14.555  23.293   2.327  1.00 55.75           C  
ANISOU 1380  CD1 TRP A 281     7900   7607   5675  -1002    592    433       C  
ATOM   1381  CD2 TRP A 281     -12.684  22.231   1.699  1.00 55.19           C  
ANISOU 1381  CD2 TRP A 281     7394   8011   5565   -994    681    452       C  
ATOM   1382  NE1 TRP A 281     -14.002  22.718   3.441  1.00 55.96           N  
ANISOU 1382  NE1 TRP A 281     7760   7764   5737  -1006    502    356       N  
ATOM   1383  CE2 TRP A 281     -12.860  22.049   3.084  1.00 55.88           C  
ANISOU 1383  CE2 TRP A 281     7479   8038   5715   -996    539    369       C  
ATOM   1384  CE3 TRP A 281     -11.570  21.648   1.079  1.00 55.66           C  
ANISOU 1384  CE3 TRP A 281     7185   8379   5585   -956    776    474       C  
ATOM   1385  CZ2 TRP A 281     -11.950  21.330   3.864  1.00 56.77           C  
ANISOU 1385  CZ2 TRP A 281     7343   8374   5855   -972    459    320       C  
ATOM   1386  CZ3 TRP A 281     -10.682  20.918   1.847  1.00 56.49           C  
ANISOU 1386  CZ3 TRP A 281     7017   8709   5739   -909    705    416       C  
ATOM   1387  CH2 TRP A 281     -10.863  20.782   3.224  1.00 56.88           C  
ANISOU 1387  CH2 TRP A 281     7081   8678   5854   -925    534    346       C  
ATOM   1388  N   CYS A 282     -17.171  23.421   0.276  1.00 56.17           N  
ANISOU 1388  N   CYS A 282     8378   7308   5657   -641    621    538       N  
ATOM   1389  CA  CYS A 282     -18.366  23.377   1.124  1.00 56.04           C  
ANISOU 1389  CA  CYS A 282     8451   7121   5720   -523    532    486       C  
ATOM   1390  C   CYS A 282     -19.326  22.266   0.687  1.00 55.69           C  
ANISOU 1390  C   CYS A 282     8379   7089   5692   -294    461    470       C  
ATOM   1391  O   CYS A 282     -19.847  21.589   1.552  1.00 56.04           O  
ANISOU 1391  O   CYS A 282     8364   7121   5809   -212    396    421       O  
ATOM   1392  CB  CYS A 282     -19.071  24.729   1.171  1.00 57.50           C  
ANISOU 1392  CB  CYS A 282     8872   7053   5922   -572    540    529       C  
ATOM   1393  SG  CYS A 282     -18.105  26.082   1.904  1.00 62.97           S  
ANISOU 1393  SG  CYS A 282     9664   7643   6620   -874    574    522       S  
ATOM   1394  N   LEU A 283     -19.520  22.037  -0.638  1.00 55.25           N  
ANISOU 1394  N   LEU A 283     8373   7062   5558   -207    465    515       N  
ATOM   1395  CA  LEU A 283     -20.376  20.963  -1.166  1.00 54.84           C  
ANISOU 1395  CA  LEU A 283     8311   7012   5514    -19    360    486       C  
ATOM   1396  C   LEU A 283     -19.820  19.616  -0.713  1.00 54.79           C  
ANISOU 1396  C   LEU A 283     8144   7135   5539     41    320    399       C  
ATOM   1397  O   LEU A 283     -20.578  18.761  -0.253  1.00 55.23           O  
ANISOU 1397  O   LEU A 283     8168   7134   5684    129    214    368       O  
ATOM   1398  CB  LEU A 283     -20.413  21.001  -2.698  1.00 54.83           C  
ANISOU 1398  CB  LEU A 283     8419   7045   5370     47    368    531       C  
ATOM   1399  CG  LEU A 283     -21.665  20.518  -3.491  1.00 56.00           C  
ANISOU 1399  CG  LEU A 283     8656   7116   5506    210    219    531       C  
ATOM   1400  CD1 LEU A 283     -21.251  19.786  -4.745  1.00 56.30           C  
ANISOU 1400  CD1 LEU A 283     8740   7277   5376    306    204    488       C  
ATOM   1401  CD2 LEU A 283     -22.637  19.660  -2.688  1.00 56.16           C  
ANISOU 1401  CD2 LEU A 283     8581   7066   5691    280     83    479       C  
ATOM   1402  N   GLY A 284     -18.503  19.443  -0.801  1.00 53.88           N  
ANISOU 1402  N   GLY A 284     7921   7191   5360     -8    403    376       N  
ATOM   1403  CA  GLY A 284     -17.856  18.224  -0.342  1.00 53.40           C  
ANISOU 1403  CA  GLY A 284     7712   7250   5330     81    361    299       C  
ATOM   1404  C   GLY A 284     -18.047  18.012   1.150  1.00 52.80           C  
ANISOU 1404  C   GLY A 284     7571   7123   5366     37    296    287       C  
ATOM   1405  O   GLY A 284     -18.267  16.884   1.589  1.00 52.94           O  
ANISOU 1405  O   GLY A 284     7549   7126   5442    145    202    253       O  
ATOM   1406  N   ALA A 285     -18.003  19.101   1.942  1.00 51.71           N  
ANISOU 1406  N   ALA A 285     7458   6943   5248   -120    339    316       N  
ATOM   1407  CA  ALA A 285     -18.170  19.013   3.390  1.00 51.18           C  
ANISOU 1407  CA  ALA A 285     7361   6847   5239   -157    288    298       C  
ATOM   1408  C   ALA A 285     -19.619  18.687   3.770  1.00 51.65           C  
ANISOU 1408  C   ALA A 285     7499   6760   5367    -65    234    320       C  
ATOM   1409  O   ALA A 285     -19.846  17.900   4.676  1.00 52.51           O  
ANISOU 1409  O   ALA A 285     7559   6877   5514    -22    177    322       O  
ATOM   1410  CB  ALA A 285     -17.695  20.296   4.065  1.00 50.52           C  
ANISOU 1410  CB  ALA A 285     7317   6746   5132   -347    336    293       C  
ATOM   1411  N   VAL A 286     -20.588  19.280   3.083  1.00 51.14           N  
ANISOU 1411  N   VAL A 286     7540   6576   5314    -35    249    355       N  
ATOM   1412  CA  VAL A 286     -22.010  19.032   3.297  1.00 51.19           C  
ANISOU 1412  CA  VAL A 286     7569   6481   5402     52    203    391       C  
ATOM   1413  C   VAL A 286     -22.300  17.577   2.887  1.00 51.98           C  
ANISOU 1413  C   VAL A 286     7601   6595   5552    139     93    391       C  
ATOM   1414  O   VAL A 286     -22.960  16.853   3.623  1.00 52.65           O  
ANISOU 1414  O   VAL A 286     7633   6654   5718    157     44    424       O  
ATOM   1415  CB  VAL A 286     -22.817  20.069   2.467  1.00 51.72           C  
ANISOU 1415  CB  VAL A 286     7749   6438   5465     84    224    432       C  
ATOM   1416  CG1 VAL A 286     -24.183  19.539   2.042  1.00 52.85           C  
ANISOU 1416  CG1 VAL A 286     7858   6529   5692    196    132    475       C  
ATOM   1417  CG2 VAL A 286     -22.949  21.396   3.208  1.00 51.45           C  
ANISOU 1417  CG2 VAL A 286     7816   6313   5421     35    307    429       C  
ATOM   1418  N   LEU A 287     -21.760  17.137   1.733  1.00 51.93           N  
ANISOU 1418  N   LEU A 287     7615   6628   5488    187     58    354       N  
ATOM   1419  CA  LEU A 287     -21.918  15.760   1.256  1.00 52.08           C  
ANISOU 1419  CA  LEU A 287     7625   6626   5538    281    -65    319       C  
ATOM   1420  C   LEU A 287     -21.261  14.752   2.207  1.00 52.55           C  
ANISOU 1420  C   LEU A 287     7610   6720   5635    299    -99    301       C  
ATOM   1421  O   LEU A 287     -21.901  13.781   2.586  1.00 52.65           O  
ANISOU 1421  O   LEU A 287     7623   6642   5740    323   -206    325       O  
ATOM   1422  CB  LEU A 287     -21.405  15.605  -0.188  1.00 51.58           C  
ANISOU 1422  CB  LEU A 287     7635   6609   5355    361    -73    259       C  
ATOM   1423  CG  LEU A 287     -21.449  14.197  -0.800  1.00 51.95           C  
ANISOU 1423  CG  LEU A 287     7727   6610   5402    484   -212    178       C  
ATOM   1424  CD1 LEU A 287     -22.846  13.596  -0.750  1.00 52.29           C  
ANISOU 1424  CD1 LEU A 287     7800   6495   5572    468   -381    208       C  
ATOM   1425  CD2 LEU A 287     -20.940  14.216  -2.217  1.00 51.61           C  
ANISOU 1425  CD2 LEU A 287     7780   6640   5188    584   -187    106       C  
ATOM   1426  N   TYR A 288     -20.035  15.030   2.686  1.00 52.74           N  
ANISOU 1426  N   TYR A 288     7566   6873   5600    270    -21    278       N  
ATOM   1427  CA  TYR A 288     -19.333  14.161   3.636  1.00 53.42           C  
ANISOU 1427  CA  TYR A 288     7578   7012   5708    308    -69    273       C  
ATOM   1428  C   TYR A 288     -20.178  13.936   4.879  1.00 53.46           C  
ANISOU 1428  C   TYR A 288     7593   6935   5784    254   -107    353       C  
ATOM   1429  O   TYR A 288     -20.299  12.802   5.324  1.00 54.18           O  
ANISOU 1429  O   TYR A 288     7691   6964   5930    308   -203    388       O  
ATOM   1430  CB  TYR A 288     -17.959  14.736   4.028  1.00 53.79           C  
ANISOU 1430  CB  TYR A 288     7515   7240   5684    256      6    247       C  
ATOM   1431  CG  TYR A 288     -17.192  13.901   5.040  1.00 55.14           C  
ANISOU 1431  CG  TYR A 288     7597   7487   5867    316    -71    251       C  
ATOM   1432  CD1 TYR A 288     -17.571  13.869   6.377  1.00 56.01           C  
ANISOU 1432  CD1 TYR A 288     7728   7561   5991    255   -113    312       C  
ATOM   1433  CD2 TYR A 288     -16.031  13.226   4.681  1.00 56.26           C  
ANISOU 1433  CD2 TYR A 288     7629   7761   5985    450    -93    200       C  
ATOM   1434  CE1 TYR A 288     -16.892  13.098   7.301  1.00 56.68           C  
ANISOU 1434  CE1 TYR A 288     7756   7712   6066    320   -204    337       C  
ATOM   1435  CE2 TYR A 288     -15.304  12.499   5.615  1.00 57.22           C  
ANISOU 1435  CE2 TYR A 288     7667   7956   6120    532   -185    215       C  
ATOM   1436  CZ  TYR A 288     -15.735  12.447   6.929  1.00 58.36           C  
ANISOU 1436  CZ  TYR A 288     7857   8042   6274    458   -252    290       C  
ATOM   1437  OH  TYR A 288     -15.034  11.728   7.874  1.00 61.09           O  
ANISOU 1437  OH  TYR A 288     8143   8457   6609    546   -363    326       O  
ATOM   1438  N   GLU A 289     -20.800  14.996   5.394  1.00 52.51           N  
ANISOU 1438  N   GLU A 289     7492   6804   5656    160    -25    389       N  
ATOM   1439  CA  GLU A 289     -21.648  14.885   6.557  1.00 52.44           C  
ANISOU 1439  CA  GLU A 289     7485   6757   5682    125    -16    467       C  
ATOM   1440  C   GLU A 289     -22.911  14.058   6.305  1.00 52.47           C  
ANISOU 1440  C   GLU A 289     7485   6649   5804    143    -84    544       C  
ATOM   1441  O   GLU A 289     -23.252  13.234   7.157  1.00 51.88           O  
ANISOU 1441  O   GLU A 289     7393   6549   5769    124   -120    631       O  
ATOM   1442  CB  GLU A 289     -22.005  16.246   7.088  1.00 54.66           C  
ANISOU 1442  CB  GLU A 289     7805   7052   5911     63     99    459       C  
ATOM   1443  CG  GLU A 289     -22.640  16.138   8.454  1.00 61.57           C  
ANISOU 1443  CG  GLU A 289     8683   7945   6766     50    142    525       C  
ATOM   1444  CD  GLU A 289     -22.556  17.401   9.278  1.00 72.76           C  
ANISOU 1444  CD  GLU A 289    10177   9389   8079     13    244    471       C  
ATOM   1445  OE1 GLU A 289     -22.184  18.457   8.713  1.00 72.85           O  
ANISOU 1445  OE1 GLU A 289    10248   9366   8065    -23    274    395       O  
ATOM   1446  OE2 GLU A 289     -22.870  17.337  10.490  1.00 78.36           O  
ANISOU 1446  OE2 GLU A 289    10910  10143   8719     19    295    508       O  
ATOM   1447  N   MET A 290     -23.590  14.228   5.124  1.00 52.36           N  
ANISOU 1447  N   MET A 290     7485   6568   5842    165   -121    525       N  
ATOM   1448  CA  MET A 290     -24.777  13.398   4.803  1.00 52.01           C  
ANISOU 1448  CA  MET A 290     7412   6423   5926    151   -229    593       C  
ATOM   1449  C   MET A 290     -24.419  11.915   4.781  1.00 51.53           C  
ANISOU 1449  C   MET A 290     7391   6273   5916    166   -370    596       C  
ATOM   1450  O   MET A 290     -25.185  11.093   5.267  1.00 51.50           O  
ANISOU 1450  O   MET A 290     7360   6188   6019     97   -437    699       O  
ATOM   1451  CB  MET A 290     -25.413  13.779   3.466  1.00 52.11           C  
ANISOU 1451  CB  MET A 290     7446   6392   5962    181   -292    557       C  
ATOM   1452  CG  MET A 290     -26.028  15.142   3.480  1.00 54.25           C  
ANISOU 1452  CG  MET A 290     7694   6705   6215    191   -182    582       C  
ATOM   1453  SD  MET A 290     -26.939  15.518   1.968  1.00 57.76           S  
ANISOU 1453  SD  MET A 290     8161   7101   6685    246   -296    576       S  
ATOM   1454  CE  MET A 290     -25.709  16.247   1.016  1.00 53.67           C  
ANISOU 1454  CE  MET A 290     7795   6607   5992    291   -250    483       C  
ATOM   1455  N   LEU A 291     -23.225  11.580   4.285  1.00 50.94           N  
ANISOU 1455  N   LEU A 291     7377   6215   5764    259   -403    492       N  
ATOM   1456  CA  LEU A 291     -22.786  10.191   4.217  1.00 50.69           C  
ANISOU 1456  CA  LEU A 291     7415   6074   5772    329   -542    471       C  
ATOM   1457  C   LEU A 291     -22.252   9.620   5.538  1.00 49.90           C  
ANISOU 1457  C   LEU A 291     7302   5987   5673    328   -540    557       C  
ATOM   1458  O   LEU A 291     -22.587   8.501   5.873  1.00 49.61           O  
ANISOU 1458  O   LEU A 291     7326   5798   5725    311   -657    634       O  
ATOM   1459  CB  LEU A 291     -21.747   9.998   3.084  1.00 50.68           C  
ANISOU 1459  CB  LEU A 291     7476   6105   5674    484   -566    317       C  
ATOM   1460  CG  LEU A 291     -22.221  10.370   1.688  1.00 51.73           C  
ANISOU 1460  CG  LEU A 291     7672   6220   5764    505   -592    236       C  
ATOM   1461  CD1 LEU A 291     -21.126  10.159   0.667  1.00 52.23           C  
ANISOU 1461  CD1 LEU A 291     7799   6353   5693    675   -576     94       C  
ATOM   1462  CD2 LEU A 291     -23.445   9.577   1.296  1.00 52.37           C  
ANISOU 1462  CD2 LEU A 291     7825   6110   5964    447   -775    257       C  
ATOM   1463  N   TYR A 292     -21.436  10.363   6.273  1.00 49.59           N  
ANISOU 1463  N   TYR A 292     7198   6112   5530    334   -430    551       N  
ATOM   1464  CA  TYR A 292     -20.809   9.850   7.482  1.00 49.85           C  
ANISOU 1464  CA  TYR A 292     7229   6183   5529    355   -457    625       C  
ATOM   1465  C   TYR A 292     -21.439  10.263   8.817  1.00 51.26           C  
ANISOU 1465  C   TYR A 292     7390   6415   5672    237   -373    756       C  
ATOM   1466  O   TYR A 292     -21.132   9.638   9.836  1.00 52.40           O  
ANISOU 1466  O   TYR A 292     7568   6562   5780    247   -419    853       O  
ATOM   1467  CB  TYR A 292     -19.340  10.205   7.484  1.00 49.42           C  
ANISOU 1467  CB  TYR A 292     7106   6298   5372    448   -434    531       C  
ATOM   1468  CG  TYR A 292     -18.559   9.491   6.408  1.00 50.18           C  
ANISOU 1468  CG  TYR A 292     7211   6373   5481    621   -504    420       C  
ATOM   1469  CD1 TYR A 292     -18.255   8.143   6.522  1.00 50.76           C  
ANISOU 1469  CD1 TYR A 292     7361   6320   5604    770   -646    434       C  
ATOM   1470  CD2 TYR A 292     -18.089  10.175   5.289  1.00 51.05           C  
ANISOU 1470  CD2 TYR A 292     7271   6591   5535    654   -419    305       C  
ATOM   1471  CE1 TYR A 292     -17.504   7.490   5.555  1.00 51.60           C  
ANISOU 1471  CE1 TYR A 292     7491   6410   5703    978   -698    307       C  
ATOM   1472  CE2 TYR A 292     -17.310   9.539   4.329  1.00 51.46           C  
ANISOU 1472  CE2 TYR A 292     7327   6666   5560    843   -449    195       C  
ATOM   1473  CZ  TYR A 292     -17.019   8.195   4.469  1.00 52.63           C  
ANISOU 1473  CZ  TYR A 292     7549   6692   5757   1021   -587    183       C  
ATOM   1474  OH  TYR A 292     -16.241   7.548   3.547  1.00 54.62           O  
ANISOU 1474  OH  TYR A 292     7819   6967   5969   1257   -607     53       O  
ATOM   1475  N   GLY A 293     -22.294  11.276   8.831  1.00 50.91           N  
ANISOU 1475  N   GLY A 293     7308   6415   5620    151   -251    761       N  
ATOM   1476  CA  GLY A 293     -22.949  11.696  10.062  1.00 51.13           C  
ANISOU 1476  CA  GLY A 293     7327   6512   5589     77   -142    864       C  
ATOM   1477  C   GLY A 293     -22.265  12.823  10.807  1.00 51.61           C  
ANISOU 1477  C   GLY A 293     7401   6720   5490     71    -49    789       C  
ATOM   1478  O   GLY A 293     -22.879  13.427  11.688  1.00 52.06           O  
ANISOU 1478  O   GLY A 293     7477   6836   5468     35     67    829       O  
ATOM   1479  N   LEU A 294     -21.001  13.131  10.473  1.00 51.20           N  
ANISOU 1479  N   LEU A 294     7337   6734   5383    103    -99    676       N  
ATOM   1480  CA  LEU A 294     -20.298  14.241  11.110  1.00 51.73           C  
ANISOU 1480  CA  LEU A 294     7417   6923   5316     53    -48    594       C  
ATOM   1481  C   LEU A 294     -19.593  15.117  10.066  1.00 52.76           C  
ANISOU 1481  C   LEU A 294     7508   7080   5460     24    -28    471       C  
ATOM   1482  O   LEU A 294     -19.289  14.646   8.965  1.00 52.96           O  
ANISOU 1482  O   LEU A 294     7482   7081   5558     81    -67    448       O  
ATOM   1483  CB  LEU A 294     -19.293  13.725  12.150  1.00 52.16           C  
ANISOU 1483  CB  LEU A 294     7470   7086   5263     72   -148    620       C  
ATOM   1484  CG  LEU A 294     -19.822  13.522  13.604  1.00 54.47           C  
ANISOU 1484  CG  LEU A 294     7854   7414   5430     55   -120    728       C  
ATOM   1485  CD1 LEU A 294     -18.748  12.905  14.493  1.00 55.16           C  
ANISOU 1485  CD1 LEU A 294     7949   7609   5399     94   -261    763       C  
ATOM   1486  CD2 LEU A 294     -20.317  14.838  14.225  0.50 54.65           C  
ANISOU 1486  CD2 LEU A 294     7956   7479   5330     -8     15    657       C  
ATOM   1487  N   PRO A 295     -19.328  16.406  10.367  1.00 53.03           N  
ANISOU 1487  N   PRO A 295     7586   7151   5413    -68     36    395       N  
ATOM   1488  CA  PRO A 295     -18.595  17.247   9.407  1.00 53.58           C  
ANISOU 1488  CA  PRO A 295     7624   7240   5496   -136     60    315       C  
ATOM   1489  C   PRO A 295     -17.187  16.705   9.195  1.00 55.29           C  
ANISOU 1489  C   PRO A 295     7696   7605   5706   -129    -24    290       C  
ATOM   1490  O   PRO A 295     -16.611  16.144  10.126  1.00 55.49           O  
ANISOU 1490  O   PRO A 295     7675   7726   5681   -106   -116    306       O  
ATOM   1491  CB  PRO A 295     -18.523  18.593  10.123  1.00 53.80           C  
ANISOU 1491  CB  PRO A 295     7757   7252   5432   -257    105    246       C  
ATOM   1492  CG  PRO A 295     -19.595  18.538  11.140  1.00 54.09           C  
ANISOU 1492  CG  PRO A 295     7895   7239   5416   -198    153    279       C  
ATOM   1493  CD  PRO A 295     -19.615  17.146  11.602  1.00 52.39           C  
ANISOU 1493  CD  PRO A 295     7609   7088   5210   -119     86    375       C  
ATOM   1494  N   PRO A 296     -16.583  16.863   8.001  1.00 56.51           N  
ANISOU 1494  N   PRO A 296     7768   7806   5897   -133      9    260       N  
ATOM   1495  CA  PRO A 296     -15.221  16.330   7.808  1.00 57.19           C  
ANISOU 1495  CA  PRO A 296     7671   8079   5978    -93    -46    239       C  
ATOM   1496  C   PRO A 296     -14.206  16.941   8.796  1.00 58.81           C  
ANISOU 1496  C   PRO A 296     7786   8438   6123   -239   -109    209       C  
ATOM   1497  O   PRO A 296     -14.414  18.056   9.310  1.00 59.48           O  
ANISOU 1497  O   PRO A 296     7976   8462   6161   -408    -88    178       O  
ATOM   1498  CB  PRO A 296     -14.914  16.634   6.343  1.00 57.21           C  
ANISOU 1498  CB  PRO A 296     7621   8118   5997    -88     52    219       C  
ATOM   1499  CG  PRO A 296     -15.835  17.737   5.978  1.00 57.72           C  
ANISOU 1499  CG  PRO A 296     7848   8024   6057   -198    137    230       C  
ATOM   1500  CD  PRO A 296     -17.081  17.548   6.789  1.00 56.28           C  
ANISOU 1500  CD  PRO A 296     7803   7686   5895   -157    104    255       C  
ATOM   1501  N   PHE A 297     -13.138  16.181   9.112  1.00 58.44           N  
ANISOU 1501  N   PHE A 297     7554   8575   6074   -157   -210    212       N  
ATOM   1502  CA  PHE A 297     -12.101  16.655  10.019  1.00 58.57           C  
ANISOU 1502  CA  PHE A 297     7444   8771   6038   -293   -314    186       C  
ATOM   1503  C   PHE A 297     -12.586  16.944  11.448  1.00 58.59           C  
ANISOU 1503  C   PHE A 297     7622   8704   5937   -365   -404    180       C  
ATOM   1504  O   PHE A 297     -11.821  17.447  12.257  1.00 58.89           O  
ANISOU 1504  O   PHE A 297     7602   8867   5905   -503   -517    138       O  
ATOM   1505  CB  PHE A 297     -11.412  17.891   9.424  1.00 58.60           C  
ANISOU 1505  CB  PHE A 297     7348   8858   6058   -531   -240    149       C  
ATOM   1506  CG  PHE A 297     -11.013  17.760   7.971  1.00 59.06           C  
ANISOU 1506  CG  PHE A 297     7265   9000   6176   -475   -104    169       C  
ATOM   1507  CD1 PHE A 297      -9.870  17.063   7.607  1.00 59.75           C  
ANISOU 1507  CD1 PHE A 297     7063   9347   6292   -355   -119    176       C  
ATOM   1508  CD2 PHE A 297     -11.778  18.340   6.970  1.00 59.79           C  
ANISOU 1508  CD2 PHE A 297     7515   8928   6275   -517     40    182       C  
ATOM   1509  CE1 PHE A 297      -9.516  16.923   6.269  1.00 60.24           C  
ANISOU 1509  CE1 PHE A 297     7009   9510   6370   -274     34    186       C  
ATOM   1510  CE2 PHE A 297     -11.432  18.187   5.631  1.00 60.44           C  
ANISOU 1510  CE2 PHE A 297     7498   9102   6365   -450    169    203       C  
ATOM   1511  CZ  PHE A 297     -10.297  17.490   5.291  1.00 60.12           C  
ANISOU 1511  CZ  PHE A 297     7182   9328   6334   -331    178    201       C  
ATOM   1512  N   TYR A 298     -13.829  16.606  11.767  1.00 58.44           N  
ANISOU 1512  N   TYR A 298     7802   8507   5896   -274   -359    222       N  
ATOM   1513  CA  TYR A 298     -14.419  16.899  13.057  1.00 59.18           C  
ANISOU 1513  CA  TYR A 298     8077   8547   5860   -317   -390    222       C  
ATOM   1514  C   TYR A 298     -13.732  16.311  14.271  1.00 61.00           C  
ANISOU 1514  C   TYR A 298     8277   8928   5973   -278   -564    250       C  
ATOM   1515  O   TYR A 298     -13.560  15.108  14.355  1.00 62.30           O  
ANISOU 1515  O   TYR A 298     8379   9129   6164   -112   -641    342       O  
ATOM   1516  CB  TYR A 298     -15.899  16.474  13.086  1.00 58.79           C  
ANISOU 1516  CB  TYR A 298     8186   8324   5828   -212   -282    296       C  
ATOM   1517  CG  TYR A 298     -16.591  16.940  14.340  1.00 59.52           C  
ANISOU 1517  CG  TYR A 298     8463   8386   5765   -244   -253    292       C  
ATOM   1518  CD1 TYR A 298     -16.918  18.274  14.515  1.00 60.47           C  
ANISOU 1518  CD1 TYR A 298     8720   8436   5819   -352   -175    186       C  
ATOM   1519  CD2 TYR A 298     -16.780  16.080  15.412  1.00 60.72           C  
ANISOU 1519  CD2 TYR A 298     8671   8590   5810   -161   -313    391       C  
ATOM   1520  CE1 TYR A 298     -17.441  18.737  15.716  1.00 61.70           C  
ANISOU 1520  CE1 TYR A 298     9062   8586   5795   -351   -146    150       C  
ATOM   1521  CE2 TYR A 298     -17.297  16.533  16.621  1.00 61.82           C  
ANISOU 1521  CE2 TYR A 298     8986   8748   5755   -180   -273    383       C  
ATOM   1522  CZ  TYR A 298     -17.645  17.860  16.763  1.00 62.63           C  
ANISOU 1522  CZ  TYR A 298     9220   8793   5783   -263   -183    249       C  
ATOM   1523  OH  TYR A 298     -18.169  18.315  17.947  1.00 63.97           O  
ANISOU 1523  OH  TYR A 298     9585   8985   5734   -244   -127    216       O  
ATOM   1524  N   SER A 299     -13.516  17.137  15.294  1.00 60.82           N  
ANISOU 1524  N   SER A 299     8356   8955   5800   -416   -635    176       N  
ATOM   1525  CA  SER A 299     -13.068  16.677  16.591  1.00 61.04           C  
ANISOU 1525  CA  SER A 299     8416   9116   5660   -380   -810    205       C  
ATOM   1526  C   SER A 299     -13.778  17.489  17.656  1.00 62.22           C  
ANISOU 1526  C   SER A 299     8838   9198   5605   -457   -774    138       C  
ATOM   1527  O   SER A 299     -14.098  18.660  17.429  1.00 63.10           O  
ANISOU 1527  O   SER A 299     9062   9199   5715   -588   -684     19       O  
ATOM   1528  CB  SER A 299     -11.564  16.853  16.759  1.00 61.61           C  
ANISOU 1528  CB  SER A 299     8268   9411   5730   -477  -1012    148       C  
ATOM   1529  OG  SER A 299     -11.156  16.394  18.042  1.00 62.35           O  
ANISOU 1529  OG  SER A 299     8409   9641   5640   -429  -1214    180       O  
ATOM   1530  N   ARG A 300     -13.977  16.904  18.841  1.00 62.13           N  
ANISOU 1530  N   ARG A 300     8954   9254   5400   -365   -849    211       N  
ATOM   1531  CA  ARG A 300     -14.544  17.652  19.957  1.00 63.00           C  
ANISOU 1531  CA  ARG A 300     9336   9343   5257   -410   -816    131       C  
ATOM   1532  C   ARG A 300     -13.533  18.759  20.394  1.00 64.64           C  
ANISOU 1532  C   ARG A 300     9571   9629   5358   -610  -1002    -60       C  
ATOM   1533  O   ARG A 300     -13.942  19.781  20.914  1.00 65.65           O  
ANISOU 1533  O   ARG A 300     9936   9667   5342   -693   -956   -205       O  
ATOM   1534  CB  ARG A 300     -14.908  16.704  21.113  1.00 63.39           C  
ANISOU 1534  CB  ARG A 300     9516   9478   5091   -271   -851    279       C  
ATOM   1535  CG  ARG A 300     -15.164  17.410  22.409  1.00 66.19           C  
ANISOU 1535  CG  ARG A 300    10148   9882   5118   -302   -856    181       C  
ATOM   1536  CD  ARG A 300     -15.526  16.481  23.532  1.00 69.26           C  
ANISOU 1536  CD  ARG A 300    10677  10378   5260   -171   -873    355       C  
ATOM   1537  NE  ARG A 300     -16.806  16.896  24.082  1.00 71.02           N  
ANISOU 1537  NE  ARG A 300    11127  10552   5304   -113   -616    356       N  
ATOM   1538  CZ  ARG A 300     -16.958  17.608  25.179  1.00 74.81           C  
ANISOU 1538  CZ  ARG A 300    11871  11107   5445   -110   -608    235       C  
ATOM   1539  NH1 ARG A 300     -15.911  17.933  25.916  1.00 76.10           N  
ANISOU 1539  NH1 ARG A 300    12124  11390   5401   -186   -882    108       N  
ATOM   1540  NH2 ARG A 300     -18.166  17.953  25.585  1.00 76.84           N  
ANISOU 1540  NH2 ARG A 300    12301  11340   5555    -18   -333    240       N  
ATOM   1541  N   ASN A 301     -12.218  18.557  20.178  1.00 64.47           N  
ANISOU 1541  N   ASN A 301     9304   9773   5417   -687  -1219    -63       N  
ATOM   1542  CA  ASN A 301     -11.161  19.526  20.482  1.00 64.31           C  
ANISOU 1542  CA  ASN A 301     9239   9848   5349   -924  -1427   -221       C  
ATOM   1543  C   ASN A 301     -11.066  20.513  19.280  1.00 64.35           C  
ANISOU 1543  C   ASN A 301     9162   9711   5576  -1110  -1300   -304       C  
ATOM   1544  O   ASN A 301     -10.721  20.094  18.168  1.00 64.15           O  
ANISOU 1544  O   ASN A 301     8878   9721   5775  -1079  -1222   -218       O  
ATOM   1545  CB  ASN A 301      -9.881  18.734  20.653  1.00 65.22           C  
ANISOU 1545  CB  ASN A 301     9046  10227   5505   -895  -1677   -143       C  
ATOM   1546  CG  ASN A 301      -8.607  19.479  20.881  1.00 69.47           C  
ANISOU 1546  CG  ASN A 301     9422  10936   6037  -1146  -1938   -264       C  
ATOM   1547  OD1 ASN A 301      -7.607  18.896  21.309  1.00 70.94           O  
ANISOU 1547  OD1 ASN A 301     9396  11370   6188  -1108  -2188   -214       O  
ATOM   1548  ND2 ASN A 301      -8.580  20.757  20.570  1.00 70.87           N  
ANISOU 1548  ND2 ASN A 301     9675  10985   6267  -1413  -1902   -412       N  
ATOM   1549  N   THR A 302     -11.396  21.811  19.488  1.00 64.09           N  
ANISOU 1549  N   THR A 302     9382   9502   5466  -1287  -1274   -468       N  
ATOM   1550  CA  THR A 302     -11.398  22.768  18.364  1.00 63.90           C  
ANISOU 1550  CA  THR A 302     9335   9303   5641  -1461  -1152   -517       C  
ATOM   1551  C   THR A 302     -10.038  22.884  17.702  1.00 63.78           C  
ANISOU 1551  C   THR A 302     8972   9460   5801  -1682  -1286   -493       C  
ATOM   1552  O   THR A 302      -9.946  22.796  16.485  1.00 63.42           O  
ANISOU 1552  O   THR A 302     8738   9401   5955  -1690  -1139   -407       O  
ATOM   1553  CB  THR A 302     -11.950  24.157  18.727  1.00 64.88           C  
ANISOU 1553  CB  THR A 302     9830   9165   5658  -1596  -1122   -698       C  
ATOM   1554  OG1 THR A 302     -12.754  24.138  19.907  1.00 65.78           O  
ANISOU 1554  OG1 THR A 302    10251   9229   5512  -1421  -1090   -768       O  
ATOM   1555  CG2 THR A 302     -12.723  24.768  17.598  1.00 65.38           C  
ANISOU 1555  CG2 THR A 302     9968   8978   5896  -1604   -898   -681       C  
ATOM   1556  N   ALA A 303      -8.963  23.016  18.515  1.00 64.01           N  
ANISOU 1556  N   ALA A 303     8894   9684   5744  -1852  -1567   -559       N  
ATOM   1557  CA  ALA A 303      -7.586  23.114  18.039  1.00 64.23           C  
ANISOU 1557  CA  ALA A 303     8531   9940   5935  -2077  -1715   -528       C  
ATOM   1558  C   ALA A 303      -7.239  21.917  17.167  1.00 65.55           C  
ANISOU 1558  C   ALA A 303     8324  10315   6266  -1852  -1612   -357       C  
ATOM   1559  O   ALA A 303      -6.592  22.082  16.139  1.00 66.30           O  
ANISOU 1559  O   ALA A 303     8132  10508   6551  -1969  -1532   -300       O  
ATOM   1560  CB  ALA A 303      -6.643  23.179  19.215  1.00 63.86           C  
ANISOU 1560  CB  ALA A 303     8419  10104   5742  -2221  -2064   -611       C  
ATOM   1561  N   GLU A 304      -7.729  20.723  17.539  1.00 65.18           N  
ANISOU 1561  N   GLU A 304     8312  10315   6140  -1520  -1594   -271       N  
ATOM   1562  CA  GLU A 304      -7.504  19.505  16.789  1.00 64.77           C  
ANISOU 1562  CA  GLU A 304     7985  10399   6224  -1260  -1511   -131       C  
ATOM   1563  C   GLU A 304      -8.262  19.539  15.480  1.00 63.95           C  
ANISOU 1563  C   GLU A 304     7919  10111   6268  -1198  -1219    -88       C  
ATOM   1564  O   GLU A 304      -7.684  19.226  14.454  1.00 64.02           O  
ANISOU 1564  O   GLU A 304     7646  10248   6430  -1166  -1138    -32       O  
ATOM   1565  CB  GLU A 304      -7.910  18.303  17.627  1.00 67.07           C  
ANISOU 1565  CB  GLU A 304     8390  10711   6383   -960  -1585    -47       C  
ATOM   1566  CG  GLU A 304      -7.363  16.973  17.168  1.00 72.37           C  
ANISOU 1566  CG  GLU A 304     8777  11553   7165   -686  -1623     79       C  
ATOM   1567  CD  GLU A 304      -7.736  15.891  18.156  1.00 81.34           C  
ANISOU 1567  CD  GLU A 304    10082  12675   8148   -440  -1740    178       C  
ATOM   1568  OE1 GLU A 304      -8.817  15.284  17.987  1.00 82.54           O  
ANISOU 1568  OE1 GLU A 304    10443  12618   8299   -279  -1577    255       O  
ATOM   1569  OE2 GLU A 304      -6.984  15.694  19.139  1.00 85.30           O  
ANISOU 1569  OE2 GLU A 304    10521  13371   8520   -431  -2003    187       O  
ATOM   1570  N   MET A 305      -9.526  19.958  15.498  1.00 63.35           N  
ANISOU 1570  N   MET A 305     8180   9757   6135  -1172  -1064   -118       N  
ATOM   1571  CA  MET A 305     -10.355  20.062  14.299  1.00 63.02           C  
ANISOU 1571  CA  MET A 305     8202   9530   6213  -1112   -818    -79       C  
ATOM   1572  C   MET A 305      -9.758  21.012  13.252  1.00 63.52           C  
ANISOU 1572  C   MET A 305     8136   9597   6403  -1351   -738    -96       C  
ATOM   1573  O   MET A 305      -9.689  20.649  12.089  1.00 63.72           O  
ANISOU 1573  O   MET A 305     8011   9658   6541  -1268   -596    -25       O  
ATOM   1574  CB  MET A 305     -11.774  20.499  14.667  1.00 63.14           C  
ANISOU 1574  CB  MET A 305     8576   9278   6137  -1058   -699   -114       C  
ATOM   1575  CG  MET A 305     -12.680  20.618  13.472  1.00 65.66           C  
ANISOU 1575  CG  MET A 305     8956   9416   6576   -987   -482    -70       C  
ATOM   1576  SD  MET A 305     -14.392  20.967  13.893  1.00 70.32           S  
ANISOU 1576  SD  MET A 305     9884   9749   7086   -867   -340    -89       S  
ATOM   1577  CE  MET A 305     -14.197  22.446  14.943  1.00 65.21           C  
ANISOU 1577  CE  MET A 305     9494   9003   6282  -1080   -428   -259       C  
ATOM   1578  N   TYR A 306      -9.320  22.208  13.652  1.00 63.75           N  
ANISOU 1578  N   TYR A 306     8242   9581   6401  -1655   -831   -185       N  
ATOM   1579  CA  TYR A 306      -8.694  23.147  12.730  1.00 64.25           C  
ANISOU 1579  CA  TYR A 306     8190   9638   6585  -1934   -765   -170       C  
ATOM   1580  C   TYR A 306      -7.381  22.604  12.210  1.00 64.89           C  
ANISOU 1580  C   TYR A 306     7812  10070   6772  -1973   -802    -89       C  
ATOM   1581  O   TYR A 306      -7.053  22.809  11.037  1.00 65.58           O  
ANISOU 1581  O   TYR A 306     7735  10215   6966  -2041   -638     -9       O  
ATOM   1582  CB  TYR A 306      -8.527  24.520  13.368  1.00 64.79           C  
ANISOU 1582  CB  TYR A 306     8478   9538   6602  -2270   -891   -287       C  
ATOM   1583  CG  TYR A 306      -9.840  25.261  13.394  1.00 66.62           C  
ANISOU 1583  CG  TYR A 306     9146   9396   6772  -2214   -769   -352       C  
ATOM   1584  CD1 TYR A 306     -10.251  26.018  12.311  1.00 68.17           C  
ANISOU 1584  CD1 TYR A 306     9459   9377   7065  -2299   -596   -301       C  
ATOM   1585  CD2 TYR A 306     -10.727  25.108  14.450  1.00 67.71           C  
ANISOU 1585  CD2 TYR A 306     9564   9417   6746  -2029   -805   -444       C  
ATOM   1586  CE1 TYR A 306     -11.492  26.643  12.295  1.00 69.42           C  
ANISOU 1586  CE1 TYR A 306     9993   9204   7179  -2192   -489   -351       C  
ATOM   1587  CE2 TYR A 306     -11.963  25.743  14.453  1.00 68.87           C  
ANISOU 1587  CE2 TYR A 306    10067   9257   6842  -1929   -671   -502       C  
ATOM   1588  CZ  TYR A 306     -12.343  26.512  13.372  1.00 70.11           C  
ANISOU 1588  CZ  TYR A 306    10323   9195   7119  -2000   -523   -459       C  
ATOM   1589  OH  TYR A 306     -13.563  27.143  13.355  1.00 71.73           O  
ANISOU 1589  OH  TYR A 306    10862   9107   7287  -1862   -402   -510       O  
ATOM   1590  N   ASP A 307      -6.648  21.859  13.044  1.00 64.68           N  
ANISOU 1590  N   ASP A 307     7572  10297   6704  -1895  -1006    -99       N  
ATOM   1591  CA  ASP A 307      -5.417  21.228  12.605  1.00 64.81           C  
ANISOU 1591  CA  ASP A 307     7117  10681   6826  -1857  -1043    -23       C  
ATOM   1592  C   ASP A 307      -5.718  20.142  11.555  1.00 64.92           C  
ANISOU 1592  C   ASP A 307     7025  10740   6900  -1503   -836     62       C  
ATOM   1593  O   ASP A 307      -4.930  19.964  10.634  1.00 65.65           O  
ANISOU 1593  O   ASP A 307     6784  11071   7090  -1489   -732    124       O  
ATOM   1594  CB  ASP A 307      -4.666  20.632  13.772  1.00 65.65           C  
ANISOU 1594  CB  ASP A 307     7047  11031   6867  -1796  -1332    -47       C  
ATOM   1595  CG  ASP A 307      -3.387  20.004  13.324  1.00 70.11           C  
ANISOU 1595  CG  ASP A 307     7095  11994   7551  -1705  -1368     32       C  
ATOM   1596  OD1 ASP A 307      -2.403  20.749  13.119  1.00 71.03           O  
ANISOU 1596  OD1 ASP A 307     6902  12326   7761  -2016  -1421     44       O  
ATOM   1597  OD2 ASP A 307      -3.372  18.772  13.144  1.00 72.61           O  
ANISOU 1597  OD2 ASP A 307     7310  12402   7875  -1322  -1336     87       O  
ATOM   1598  N   ASN A 308      -6.839  19.424  11.684  1.00 63.83           N  
ANISOU 1598  N   ASN A 308     7164  10387   6699  -1225   -779     62       N  
ATOM   1599  CA  ASN A 308      -7.202  18.407  10.713  1.00 63.69           C  
ANISOU 1599  CA  ASN A 308     7104  10361   6734   -913   -621    118       C  
ATOM   1600  C   ASN A 308      -7.507  19.110   9.391  1.00 64.09           C  
ANISOU 1600  C   ASN A 308     7204  10310   6836  -1026   -385    140       C  
ATOM   1601  O   ASN A 308      -6.775  18.886   8.445  1.00 64.57           O  
ANISOU 1601  O   ASN A 308     7007  10572   6953   -967   -268    183       O  
ATOM   1602  CB  ASN A 308      -8.412  17.585  11.186  1.00 64.33           C  
ANISOU 1602  CB  ASN A 308     7485  10206   6750   -663   -633    125       C  
ATOM   1603  CG  ASN A 308      -8.220  16.775  12.433  1.00 66.94           C  
ANISOU 1603  CG  ASN A 308     7819  10612   7004   -517   -844    142       C  
ATOM   1604  OD1 ASN A 308      -9.171  16.547  13.178  1.00 68.35           O  
ANISOU 1604  OD1 ASN A 308     8272  10604   7093   -447   -870    154       O  
ATOM   1605  ND2 ASN A 308      -6.997  16.335  12.710  1.00 67.41           N  
ANISOU 1605  ND2 ASN A 308     7566  10959   7086   -464   -998    157       N  
ATOM   1606  N   ILE A 309      -8.477  20.064   9.376  1.00 63.74           N  
ANISOU 1606  N   ILE A 309     7483   9977   6759  -1193   -320    115       N  
ATOM   1607  CA  ILE A 309      -8.897  20.834   8.213  1.00 63.95           C  
ANISOU 1607  CA  ILE A 309     7627   9857   6815  -1301   -125    151       C  
ATOM   1608  C   ILE A 309      -7.728  21.408   7.446  1.00 66.04           C  
ANISOU 1608  C   ILE A 309     7606  10348   7136  -1524    -41    212       C  
ATOM   1609  O   ILE A 309      -7.718  21.348   6.220  1.00 66.64           O  
ANISOU 1609  O   ILE A 309     7631  10469   7222  -1462    146    277       O  
ATOM   1610  CB  ILE A 309      -9.876  21.976   8.589  1.00 63.20           C  
ANISOU 1610  CB  ILE A 309     7900   9432   6680  -1470   -122    107       C  
ATOM   1611  CG1 ILE A 309     -11.130  21.442   9.273  1.00 63.59           C  
ANISOU 1611  CG1 ILE A 309     8203   9288   6671  -1235   -148     70       C  
ATOM   1612  CG2 ILE A 309     -10.255  22.786   7.347  1.00 63.39           C  
ANISOU 1612  CG2 ILE A 309     8048   9304   6733  -1579     57    169       C  
ATOM   1613  CD1 ILE A 309     -12.113  22.498   9.766  1.00 64.41           C  
ANISOU 1613  CD1 ILE A 309     8648   9101   6723  -1327   -136     11       C  
ATOM   1614  N   LEU A 310      -6.748  21.966   8.154  1.00 66.85           N  
ANISOU 1614  N   LEU A 310     7520  10612   7268  -1793   -182    197       N  
ATOM   1615  CA  LEU A 310      -5.637  22.640   7.498  1.00 68.10           C  
ANISOU 1615  CA  LEU A 310     7381  10994   7498  -2082   -103    278       C  
ATOM   1616  C   LEU A 310      -4.398  21.780   7.211  1.00 69.67           C  
ANISOU 1616  C   LEU A 310     7079  11642   7750  -1954    -91    326       C  
ATOM   1617  O   LEU A 310      -3.705  22.062   6.231  1.00 70.59           O  
ANISOU 1617  O   LEU A 310     6939  11972   7908  -2072     88    424       O  
ATOM   1618  CB  LEU A 310      -5.232  23.897   8.310  1.00 68.02           C  
ANISOU 1618  CB  LEU A 310     7441  10889   7514  -2524   -270    241       C  
ATOM   1619  CG  LEU A 310      -6.386  24.873   8.638  1.00 69.07           C  
ANISOU 1619  CG  LEU A 310     8085  10566   7591  -2634   -288    171       C  
ATOM   1620  CD1 LEU A 310      -6.025  25.805   9.753  1.00 69.48           C  
ANISOU 1620  CD1 LEU A 310     8249  10519   7632  -2959   -525     71       C  
ATOM   1621  CD2 LEU A 310      -6.820  25.663   7.433  1.00 69.34           C  
ANISOU 1621  CD2 LEU A 310     8298  10398   7651  -2757    -74    270       C  
ATOM   1622  N   ASN A 311      -4.069  20.794   8.059  1.00 70.02           N  
ANISOU 1622  N   ASN A 311     6972  11846   7789  -1719   -274    273       N  
ATOM   1623  CA  ASN A 311      -2.811  20.061   7.905  1.00 71.23           C  
ANISOU 1623  CA  ASN A 311     6622  12438   8004  -1585   -296    314       C  
ATOM   1624  C   ASN A 311      -2.878  18.565   7.894  1.00 72.19           C  
ANISOU 1624  C   ASN A 311     6676  12648   8103  -1087   -310    290       C  
ATOM   1625  O   ASN A 311      -1.827  17.946   7.804  1.00 72.46           O  
ANISOU 1625  O   ASN A 311     6295  13043   8191   -926   -339    315       O  
ATOM   1626  CB  ASN A 311      -1.814  20.455   8.993  1.00 73.49           C  
ANISOU 1626  CB  ASN A 311     6646  12941   8337  -1843   -571    295       C  
ATOM   1627  CG  ASN A 311      -1.920  21.873   9.497  1.00 79.02           C  
ANISOU 1627  CG  ASN A 311     7543  13442   9040  -2337   -677    267       C  
ATOM   1628  OD1 ASN A 311      -2.149  22.107  10.686  1.00 80.75           O  
ANISOU 1628  OD1 ASN A 311     7955  13531   9197  -2436   -932    174       O  
ATOM   1629  ND2 ASN A 311      -1.768  22.850   8.599  1.00 80.46           N  
ANISOU 1629  ND2 ASN A 311     7711  13580   9278  -2651   -488    347       N  
ATOM   1630  N   LYS A 312      -4.049  17.968   8.050  1.00 73.08           N  
ANISOU 1630  N   LYS A 312     7175  12443   8151   -844   -312    246       N  
ATOM   1631  CA  LYS A 312      -4.145  16.508   8.084  1.00 74.44           C  
ANISOU 1631  CA  LYS A 312     7333  12638   8312   -392   -355    229       C  
ATOM   1632  C   LYS A 312      -4.864  15.947   6.859  1.00 75.74           C  
ANISOU 1632  C   LYS A 312     7670  12655   8454   -140   -137    219       C  
ATOM   1633  O   LYS A 312      -5.900  16.463   6.431  1.00 75.55           O  
ANISOU 1633  O   LYS A 312     7961  12353   8392   -250    -30    215       O  
ATOM   1634  CB  LYS A 312      -4.799  16.018   9.387  1.00 75.96           C  
ANISOU 1634  CB  LYS A 312     7795  12618   8449   -294   -584    203       C  
ATOM   1635  CG  LYS A 312      -4.063  16.458  10.633  1.00 79.86           C  
ANISOU 1635  CG  LYS A 312     8135  13282   8925   -487   -838    198       C  
ATOM   1636  CD  LYS A 312      -2.852  15.620  10.899  1.00 84.62           C  
ANISOU 1636  CD  LYS A 312     8302  14262   9586   -283   -963    228       C  
ATOM   1637  CE  LYS A 312      -1.662  16.466  11.284  1.00 89.24           C  
ANISOU 1637  CE  LYS A 312     8537  15155  10214   -621  -1108    234       C  
ATOM   1638  NZ  LYS A 312      -1.613  16.736  12.743  1.00 91.67           N  
ANISOU 1638  NZ  LYS A 312     8976  15424  10428   -742  -1423    202       N  
ATOM   1639  N   PRO A 313      -4.326  14.853   6.288  1.00 76.57           N  
ANISOU 1639  N   PRO A 313     7580  12939   8573    228    -90    204       N  
ATOM   1640  CA  PRO A 313      -4.992  14.238   5.137  1.00 76.80           C  
ANISOU 1640  CA  PRO A 313     7810  12814   8556    490     81    165       C  
ATOM   1641  C   PRO A 313      -6.404  13.772   5.484  1.00 77.08           C  
ANISOU 1641  C   PRO A 313     8288  12429   8569    572    -15    138       C  
ATOM   1642  O   PRO A 313      -6.686  13.405   6.630  1.00 76.97           O  
ANISOU 1642  O   PRO A 313     8377  12297   8571    594   -213    151       O  
ATOM   1643  CB  PRO A 313      -4.060  13.081   4.758  1.00 77.36           C  
ANISOU 1643  CB  PRO A 313     7603  13145   8645    902     91    129       C  
ATOM   1644  CG  PRO A 313      -3.264  12.804   5.973  1.00 77.74           C  
ANISOU 1644  CG  PRO A 313     7413  13367   8758    928   -146    158       C  
ATOM   1645  CD  PRO A 313      -3.099  14.120   6.665  1.00 76.24           C  
ANISOU 1645  CD  PRO A 313     7145  13239   8583    451   -207    209       C  
ATOM   1646  N   LEU A 314      -7.303  13.867   4.497  1.00 77.34           N  
ANISOU 1646  N   LEU A 314     8572  12257   8557    588    126    117       N  
ATOM   1647  CA  LEU A 314      -8.704  13.511   4.646  1.00 77.76           C  
ANISOU 1647  CA  LEU A 314     9003  11937   8604    632     59    103       C  
ATOM   1648  C   LEU A 314      -8.859  12.026   4.916  1.00 78.22           C  
ANISOU 1648  C   LEU A 314     9151  11876   8693    971    -82     71       C  
ATOM   1649  O   LEU A 314      -8.253  11.197   4.231  1.00 78.35           O  
ANISOU 1649  O   LEU A 314     9060  12006   8703   1264    -47     14       O  
ATOM   1650  CB  LEU A 314      -9.479  13.931   3.392  1.00 77.80           C  
ANISOU 1650  CB  LEU A 314     9198  11811   8551    595    225     88       C  
ATOM   1651  CG  LEU A 314     -10.961  13.545   3.333  1.00 79.09           C  
ANISOU 1651  CG  LEU A 314     9706  11624   8722    647    159     74       C  
ATOM   1652  CD1 LEU A 314     -11.767  14.201   4.458  1.00 79.14           C  
ANISOU 1652  CD1 LEU A 314     9852  11452   8765    420     74    129       C  
ATOM   1653  CD2 LEU A 314     -11.547  13.855   1.951  1.00 79.71           C  
ANISOU 1653  CD2 LEU A 314     9932  11632   8723    659    295     52       C  
ATOM   1654  N   GLN A 315      -9.651  11.700   5.949  1.00 78.19           N  
ANISOU 1654  N   GLN A 315     9350  11641   8717    935   -236    114       N  
ATOM   1655  CA  GLN A 315      -9.916  10.329   6.374  1.00 78.30           C  
ANISOU 1655  CA  GLN A 315     9496  11484   8769   1200   -391    123       C  
ATOM   1656  C   GLN A 315     -11.273   9.834   5.864  1.00 76.93           C  
ANISOU 1656  C   GLN A 315     9639  10974   8616   1233   -391    113       C  
ATOM   1657  O   GLN A 315     -12.279  10.012   6.557  1.00 77.19           O  
ANISOU 1657  O   GLN A 315     9846  10816   8665   1076   -444    183       O  
ATOM   1658  CB  GLN A 315      -9.901  10.260   7.913  1.00 81.14           C  
ANISOU 1658  CB  GLN A 315     9870  11833   9128   1123   -564    212       C  
ATOM   1659  CG  GLN A 315      -9.104   9.081   8.479  1.00 86.84           C  
ANISOU 1659  CG  GLN A 315    10506  12615   9875   1421   -736    240       C  
ATOM   1660  CD  GLN A 315      -7.605   9.289   8.376  1.00 92.64           C  
ANISOU 1660  CD  GLN A 315    10856  13732  10611   1505   -741    209       C  
ATOM   1661  OE1 GLN A 315      -7.010   9.245   7.282  1.00 94.69           O  
ANISOU 1661  OE1 GLN A 315    10928  14165  10884   1629   -600    133       O  
ATOM   1662  NE2 GLN A 315      -6.962   9.508   9.523  1.00 92.78           N  
ANISOU 1662  NE2 GLN A 315    10736  13912  10605   1440   -905    272       N  
ATOM   1663  N   LEU A 316     -11.311   9.205   4.677  1.00 75.13           N  
ANISOU 1663  N   LEU A 316     9479  10687   8381   1438   -339     22       N  
ATOM   1664  CA  LEU A 316     -12.570   8.669   4.168  1.00 74.07           C  
ANISOU 1664  CA  LEU A 316     9637  10233   8275   1458   -387      2       C  
ATOM   1665  C   LEU A 316     -12.730   7.254   4.688  1.00 73.19           C  
ANISOU 1665  C   LEU A 316     9676   9897   8237   1667   -576     21       C  
ATOM   1666  O   LEU A 316     -11.887   6.404   4.414  1.00 73.23           O  
ANISOU 1666  O   LEU A 316     9638   9947   8241   1965   -621    -51       O  
ATOM   1667  CB  LEU A 316     -12.648   8.721   2.636  1.00 73.91           C  
ANISOU 1667  CB  LEU A 316     9677  10224   8180   1555   -270   -114       C  
ATOM   1668  CG  LEU A 316     -12.622  10.114   2.014  1.00 74.53           C  
ANISOU 1668  CG  LEU A 316     9663  10477   8178   1335    -85   -101       C  
ATOM   1669  CD1 LEU A 316     -12.718  10.026   0.514  1.00 74.89           C  
ANISOU 1669  CD1 LEU A 316     9814  10527   8115   1459     12   -201       C  
ATOM   1670  CD2 LEU A 316     -13.727  10.993   2.560  1.00 74.72           C  
ANISOU 1670  CD2 LEU A 316     9793  10356   8242   1044    -97     -9       C  
ATOM   1671  N   LYS A 317     -13.777   7.011   5.487  1.00 72.22           N  
ANISOU 1671  N   LYS A 317     9724   9539   8176   1518   -679    133       N  
ATOM   1672  CA  LYS A 317     -14.024   5.712   6.099  1.00 71.77           C  
ANISOU 1672  CA  LYS A 317     9841   9231   8196   1651   -864    202       C  
ATOM   1673  C   LYS A 317     -14.589   4.697   5.082  1.00 70.84           C  
ANISOU 1673  C   LYS A 317     9963   8819   8134   1797   -951    107       C  
ATOM   1674  O   LYS A 317     -15.044   5.067   4.002  1.00 70.68           O  
ANISOU 1674  O   LYS A 317     9992   8781   8082   1750   -875      4       O  
ATOM   1675  CB  LYS A 317     -14.856   5.856   7.382  1.00 74.15           C  
ANISOU 1675  CB  LYS A 317    10217   9435   8522   1419   -914    381       C  
ATOM   1676  CG  LYS A 317     -13.948   5.985   8.610  1.00 79.43           C  
ANISOU 1676  CG  LYS A 317    10730  10325   9123   1427   -947    461       C  
ATOM   1677  CD  LYS A 317     -14.615   6.636   9.823  1.00 84.87           C  
ANISOU 1677  CD  LYS A 317    11466  11016   9764   1175   -929    604       C  
ATOM   1678  CE  LYS A 317     -14.069   8.019  10.119  1.00 89.71           C  
ANISOU 1678  CE  LYS A 317    11893  11918  10275   1028   -837    566       C  
ATOM   1679  NZ  LYS A 317     -15.010   9.102   9.696  1.00 92.38           N  
ANISOU 1679  NZ  LYS A 317    12228  12264  10608    824   -672    504       N  
ATOM   1680  N   PRO A 318     -14.459   3.396   5.378  1.00 70.22           N  
ANISOU 1680  N   PRO A 318    10052   8503   8124   1998  -1127    129       N  
ATOM   1681  CA  PRO A 318     -14.756   2.376   4.369  1.00 70.01           C  
ANISOU 1681  CA  PRO A 318    10275   8186   8138   2182  -1235     -6       C  
ATOM   1682  C   PRO A 318     -16.164   2.131   3.852  1.00 70.19           C  
ANISOU 1682  C   PRO A 318    10531   7905   8235   1973  -1319     -7       C  
ATOM   1683  O   PRO A 318     -16.243   1.276   2.926  1.00 71.63           O  
ANISOU 1683  O   PRO A 318    10932   7857   8426   2155  -1431   -162       O  
ATOM   1684  CB  PRO A 318     -14.313   1.073   5.041  1.00 70.18           C  
ANISOU 1684  CB  PRO A 318    10450   7981   8236   2421  -1431     55       C  
ATOM   1685  CG  PRO A 318     -13.392   1.464   6.091  1.00 70.60           C  
ANISOU 1685  CG  PRO A 318    10259   8321   8246   2468  -1395    165       C  
ATOM   1686  CD  PRO A 318     -13.838   2.792   6.573  1.00 69.37           C  
ANISOU 1686  CD  PRO A 318     9924   8394   8041   2117  -1248    258       C  
ATOM   1687  N   ASN A 319     -17.240   2.764   4.387  1.00 68.47           N  
ANISOU 1687  N   ASN A 319    10277   7671   8066   1632  -1285    143       N  
ATOM   1688  CA  ASN A 319     -18.550   2.286   3.936  1.00 68.29           C  
ANISOU 1688  CA  ASN A 319    10455   7344   8148   1457  -1412    155       C  
ATOM   1689  C   ASN A 319     -19.285   3.147   2.929  1.00 67.03           C  
ANISOU 1689  C   ASN A 319    10251   7272   7944   1312  -1333     66       C  
ATOM   1690  O   ASN A 319     -20.508   3.216   2.960  1.00 67.37           O  
ANISOU 1690  O   ASN A 319    10329   7186   8082   1068  -1393    154       O  
ATOM   1691  CB  ASN A 319     -19.418   1.948   5.109  1.00 70.77           C  
ANISOU 1691  CB  ASN A 319    10812   7494   8584   1215  -1486    396       C  
ATOM   1692  CG  ASN A 319     -18.960   0.635   5.666  1.00 75.82           C  
ANISOU 1692  CG  ASN A 319    11641   7880   9287   1386  -1659    461       C  
ATOM   1693  OD1 ASN A 319     -18.950  -0.408   4.966  1.00 76.88           O  
ANISOU 1693  OD1 ASN A 319    12018   7713   9481   1543  -1835    343       O  
ATOM   1694  ND2 ASN A 319     -18.496   0.681   6.906  1.00 77.00           N  
ANISOU 1694  ND2 ASN A 319    11705   8147   9405   1390  -1625    632       N  
ATOM   1695  N   ILE A 320     -18.557   3.715   1.963  1.00 65.26           N  
ANISOU 1695  N   ILE A 320     9960   7260   7577   1476  -1213   -103       N  
ATOM   1696  CA  ILE A 320     -19.177   4.469   0.882  1.00 63.95           C  
ANISOU 1696  CA  ILE A 320     9797   7164   7337   1379  -1157   -187       C  
ATOM   1697  C   ILE A 320     -18.630   3.948  -0.440  1.00 64.40           C  
ANISOU 1697  C   ILE A 320    10016   7187   7266   1646  -1195   -417       C  
ATOM   1698  O   ILE A 320     -17.521   3.406  -0.469  1.00 65.17           O  
ANISOU 1698  O   ILE A 320    10116   7342   7303   1925  -1165   -511       O  
ATOM   1699  CB  ILE A 320     -19.071   6.003   1.002  1.00 62.80           C  
ANISOU 1699  CB  ILE A 320     9423   7332   7108   1242   -934   -124       C  
ATOM   1700  CG1 ILE A 320     -17.614   6.462   0.959  1.00 62.99           C  
ANISOU 1700  CG1 ILE A 320     9286   7642   7006   1416   -767   -185       C  
ATOM   1701  CG2 ILE A 320     -19.830   6.541   2.210  1.00 62.49           C  
ANISOU 1701  CG2 ILE A 320     9272   7300   7171    991   -901     71       C  
ATOM   1702  CD1 ILE A 320     -17.428   7.851   0.488  1.00 63.59           C  
ANISOU 1702  CD1 ILE A 320     9217   7971   6972   1305   -573   -177       C  
ATOM   1703  N   THR A 321     -19.399   4.101  -1.532  1.00 63.53           N  
ANISOU 1703  N   THR A 321    10040   6999   7099   1585  -1265   -513       N  
ATOM   1704  CA  THR A 321     -18.978   3.624  -2.848  1.00 63.23           C  
ANISOU 1704  CA  THR A 321    10201   6932   6892   1844  -1304   -749       C  
ATOM   1705  C   THR A 321     -17.687   4.276  -3.319  1.00 63.74           C  
ANISOU 1705  C   THR A 321    10110   7356   6754   2065  -1044   -826       C  
ATOM   1706  O   THR A 321     -17.352   5.376  -2.874  1.00 64.04           O  
ANISOU 1706  O   THR A 321     9893   7663   6775   1935   -847   -697       O  
ATOM   1707  CB  THR A 321     -20.075   3.856  -3.895  1.00 62.57           C  
ANISOU 1707  CB  THR A 321    10269   6757   6747   1712  -1427   -818       C  
ATOM   1708  OG1 THR A 321     -20.329   5.248  -3.955  1.00 62.65           O  
ANISOU 1708  OG1 THR A 321    10078   7029   6698   1542  -1250   -702       O  
ATOM   1709  CG2 THR A 321     -21.337   3.082  -3.605  1.00 62.44           C  
ANISOU 1709  CG2 THR A 321    10397   6389   6936   1494  -1713   -764       C  
ATOM   1710  N   ASN A 322     -16.978   3.609  -4.245  1.00 63.64           N  
ANISOU 1710  N   ASN A 322    10253   7346   6580   2392  -1039  -1040       N  
ATOM   1711  CA  ASN A 322     -15.781   4.171  -4.840  1.00 64.23           C  
ANISOU 1711  CA  ASN A 322    10164   7794   6445   2606   -770  -1111       C  
ATOM   1712  C   ASN A 322     -16.108   5.508  -5.588  1.00 63.19           C  
ANISOU 1712  C   ASN A 322     9954   7900   6157   2410   -605  -1050       C  
ATOM   1713  O   ASN A 322     -15.309   6.443  -5.559  1.00 63.27           O  
ANISOU 1713  O   ASN A 322     9715   8242   6084   2382   -355   -967       O  
ATOM   1714  CB  ASN A 322     -15.082   3.127  -5.714  1.00 67.44           C  
ANISOU 1714  CB  ASN A 322    10779   8153   6693   3027   -791  -1364       C  
ATOM   1715  CG  ASN A 322     -15.984   2.359  -6.689  1.00 75.16           C  
ANISOU 1715  CG  ASN A 322    12167   8804   7589   3081  -1031  -1558       C  
ATOM   1716  OD1 ASN A 322     -17.195   2.632  -6.841  1.00 77.71           O  
ANISOU 1716  OD1 ASN A 322    12597   8960   7971   2787  -1192  -1498       O  
ATOM   1717  ND2 ASN A 322     -15.398   1.391  -7.428  1.00 76.29           N  
ANISOU 1717  ND2 ASN A 322    12548   8861   7577   3477  -1067  -1812       N  
ATOM   1718  N   SER A 323     -17.329   5.634  -6.133  1.00 62.11           N  
ANISOU 1718  N   SER A 323    10011   7577   6012   2238   -766  -1057       N  
ATOM   1719  CA  SER A 323     -17.780   6.850  -6.814  1.00 61.89           C  
ANISOU 1719  CA  SER A 323     9949   7719   5849   2063   -659   -979       C  
ATOM   1720  C   SER A 323     -17.842   8.045  -5.851  1.00 62.25           C  
ANISOU 1720  C   SER A 323     9718   7910   6026   1791   -514   -749       C  
ATOM   1721  O   SER A 323     -17.316   9.112  -6.162  1.00 62.70           O  
ANISOU 1721  O   SER A 323     9644   8227   5953   1742   -292   -676       O  
ATOM   1722  CB  SER A 323     -19.149   6.628  -7.452  1.00 62.14           C  
ANISOU 1722  CB  SER A 323    10222   7504   5884   1944   -920  -1025       C  
ATOM   1723  OG  SER A 323     -19.173   5.392  -8.140  1.00 64.46           O  
ANISOU 1723  OG  SER A 323    10810   7589   6092   2164  -1113  -1254       O  
ATOM   1724  N   ALA A 324     -18.492   7.864  -4.687  1.00 61.58           N  
ANISOU 1724  N   ALA A 324     9564   7648   6184   1611   -640   -632       N  
ATOM   1725  CA  ALA A 324     -18.629   8.904  -3.674  1.00 61.20           C  
ANISOU 1725  CA  ALA A 324     9299   7702   6251   1377   -526   -443       C  
ATOM   1726  C   ALA A 324     -17.270   9.267  -3.112  1.00 61.48           C  
ANISOU 1726  C   ALA A 324     9115   7988   6256   1432   -325   -410       C  
ATOM   1727  O   ALA A 324     -17.003  10.434  -2.852  1.00 61.38           O  
ANISOU 1727  O   ALA A 324     8952   8146   6224   1273   -169   -303       O  
ATOM   1728  CB  ALA A 324     -19.546   8.423  -2.557  1.00 61.07           C  
ANISOU 1728  CB  ALA A 324     9274   7463   6466   1221   -690   -342       C  
ATOM   1729  N   ARG A 325     -16.412   8.266  -2.924  1.00 61.84           N  
ANISOU 1729  N   ARG A 325     9145   8045   6307   1658   -348   -500       N  
ATOM   1730  CA  ARG A 325     -15.062   8.412  -2.425  1.00 62.81           C  
ANISOU 1730  CA  ARG A 325     9027   8425   6413   1755   -196   -482       C  
ATOM   1731  C   ARG A 325     -14.230   9.293  -3.384  1.00 63.30           C  
ANISOU 1731  C   ARG A 325     8966   8807   6278   1787     50   -502       C  
ATOM   1732  O   ARG A 325     -13.619  10.259  -2.945  1.00 63.11           O  
ANISOU 1732  O   ARG A 325     8713   9003   6261   1626    200   -393       O  
ATOM   1733  CB  ARG A 325     -14.465   7.013  -2.271  1.00 64.63           C  
ANISOU 1733  CB  ARG A 325     9318   8559   6682   2059   -308   -596       C  
ATOM   1734  CG  ARG A 325     -13.177   6.967  -1.533  1.00 68.79           C  
ANISOU 1734  CG  ARG A 325     9575   9325   7237   2183   -217   -563       C  
ATOM   1735  CD  ARG A 325     -12.842   5.546  -1.170  1.00 73.88           C  
ANISOU 1735  CD  ARG A 325    10325   9791   7955   2483   -382   -645       C  
ATOM   1736  NE  ARG A 325     -11.854   5.526  -0.095  1.00 79.42           N  
ANISOU 1736  NE  ARG A 325    10763  10679   8734   2547   -368   -558       N  
ATOM   1737  CZ  ARG A 325     -12.138   5.294   1.183  1.00 83.29           C  
ANISOU 1737  CZ  ARG A 325    11252  11030   9365   2429   -516   -426       C  
ATOM   1738  NH1 ARG A 325     -13.386   5.018   1.555  1.00 82.24           N  
ANISOU 1738  NH1 ARG A 325    11351  10573   9325   2240   -665   -355       N  
ATOM   1739  NH2 ARG A 325     -11.174   5.315   2.096  1.00 84.91           N  
ANISOU 1739  NH2 ARG A 325    11215  11438   9607   2502   -520   -354       N  
ATOM   1740  N   HIS A 326     -14.273   9.016  -4.700  1.00 63.72           N  
ANISOU 1740  N   HIS A 326     9191   8879   6142   1965     86   -630       N  
ATOM   1741  CA  HIS A 326     -13.546   9.827  -5.676  1.00 64.18           C  
ANISOU 1741  CA  HIS A 326     9154   9250   5980   1989    341   -622       C  
ATOM   1742  C   HIS A 326     -14.052  11.273  -5.654  1.00 62.72           C  
ANISOU 1742  C   HIS A 326     8934   9102   5794   1653    424   -450       C  
ATOM   1743  O   HIS A 326     -13.241  12.188  -5.607  1.00 63.15           O  
ANISOU 1743  O   HIS A 326     8778   9411   5806   1526    629   -345       O  
ATOM   1744  CB  HIS A 326     -13.661   9.209  -7.060  1.00 66.90           C  
ANISOU 1744  CB  HIS A 326     9753   9579   6089   2249    340   -797       C  
ATOM   1745  CG  HIS A 326     -12.862   9.891  -8.127  1.00 73.14           C  
ANISOU 1745  CG  HIS A 326    10469  10713   6608   2309    625   -784       C  
ATOM   1746  ND1 HIS A 326     -13.328  11.036  -8.766  1.00 76.25           N  
ANISOU 1746  ND1 HIS A 326    10930  11163   6877   2079    716   -653       N  
ATOM   1747  CD2 HIS A 326     -11.704   9.510  -8.715  1.00 75.29           C  
ANISOU 1747  CD2 HIS A 326    10631  11277   6699   2595    835   -882       C  
ATOM   1748  CE1 HIS A 326     -12.425  11.331  -9.691  1.00 77.09           C  
ANISOU 1748  CE1 HIS A 326    10970  11595   6727   2197    984   -654       C  
ATOM   1749  NE2 HIS A 326     -11.428  10.444  -9.701  1.00 76.99           N  
ANISOU 1749  NE2 HIS A 326    10830  11754   6668   2509   1078   -793       N  
ATOM   1750  N   LEU A 327     -15.375  11.478  -5.606  1.00 60.79           N  
ANISOU 1750  N   LEU A 327     8880   8596   5622   1503    253   -411       N  
ATOM   1751  CA  LEU A 327     -15.952  12.815  -5.548  1.00 59.41           C  
ANISOU 1751  CA  LEU A 327     8702   8408   5461   1233    304   -256       C  
ATOM   1752  C   LEU A 327     -15.501  13.572  -4.277  1.00 59.11           C  
ANISOU 1752  C   LEU A 327     8436   8440   5585   1023    378   -132       C  
ATOM   1753  O   LEU A 327     -15.013  14.688  -4.401  1.00 59.51           O  
ANISOU 1753  O   LEU A 327     8394   8638   5579    859    542    -29       O  
ATOM   1754  CB  LEU A 327     -17.479  12.738  -5.624  1.00 58.92           C  
ANISOU 1754  CB  LEU A 327     8840   8066   5480   1160     84   -248       C  
ATOM   1755  CG  LEU A 327     -18.229  14.062  -5.530  1.00 59.59           C  
ANISOU 1755  CG  LEU A 327     8941   8104   5595    938    111    -96       C  
ATOM   1756  CD1 LEU A 327     -17.918  14.956  -6.725  1.00 60.31           C  
ANISOU 1756  CD1 LEU A 327     9116   8346   5452    928    266    -41       C  
ATOM   1757  CD2 LEU A 327     -19.704  13.842  -5.428  1.00 59.24           C  
ANISOU 1757  CD2 LEU A 327     9021   7826   5662    898   -111    -88       C  
ATOM   1758  N   LEU A 328     -15.615  12.971  -3.076  1.00 58.19           N  
ANISOU 1758  N   LEU A 328     8246   8214   5649   1020    252   -140       N  
ATOM   1759  CA  LEU A 328     -15.192  13.637  -1.848  1.00 58.02           C  
ANISOU 1759  CA  LEU A 328     8039   8260   5745    837    294    -46       C  
ATOM   1760  C   LEU A 328     -13.695  13.921  -1.881  1.00 59.38           C  
ANISOU 1760  C   LEU A 328     7968   8741   5855    842    462    -37       C  
ATOM   1761  O   LEU A 328     -13.284  15.021  -1.562  1.00 59.53           O  
ANISOU 1761  O   LEU A 328     7869   8863   5886    617    559     56       O  
ATOM   1762  CB  LEU A 328     -15.557  12.833  -0.593  1.00 57.07           C  
ANISOU 1762  CB  LEU A 328     7911   7988   5787    860    127    -47       C  
ATOM   1763  CG  LEU A 328     -17.037  12.686  -0.274  1.00 56.69           C  
ANISOU 1763  CG  LEU A 328     8024   7676   5838    781    -14     -8       C  
ATOM   1764  CD1 LEU A 328     -17.241  11.804   0.934  1.00 56.10           C  
ANISOU 1764  CD1 LEU A 328     7933   7485   5897    801   -146     18       C  
ATOM   1765  CD2 LEU A 328     -17.687  14.027  -0.050  1.00 56.80           C  
ANISOU 1765  CD2 LEU A 328     8051   7664   5866    568     53     86       C  
ATOM   1766  N   GLU A 329     -12.887  12.976  -2.347  1.00 60.57           N  
ANISOU 1766  N   GLU A 329     8039   9037   5936   1098    498   -134       N  
ATOM   1767  CA  GLU A 329     -11.438  13.165  -2.473  1.00 62.72           C  
ANISOU 1767  CA  GLU A 329     8022   9657   6154   1136    672   -122       C  
ATOM   1768  C   GLU A 329     -11.090  14.429  -3.293  1.00 63.91           C  
ANISOU 1768  C   GLU A 329     8117   9991   6175    931    890    -20       C  
ATOM   1769  O   GLU A 329     -10.198  15.186  -2.917  1.00 64.48           O  
ANISOU 1769  O   GLU A 329     7938  10281   6281    739   1001     71       O  
ATOM   1770  CB  GLU A 329     -10.779  11.916  -3.127  1.00 66.66           C  
ANISOU 1770  CB  GLU A 329     8487  10274   6565   1522    697   -264       C  
ATOM   1771  CG  GLU A 329     -10.107  10.949  -2.151  1.00 75.07           C  
ANISOU 1771  CG  GLU A 329     9416  11341   7767   1715    559   -313       C  
ATOM   1772  CD  GLU A 329     -10.103   9.475  -2.537  1.00 85.06           C  
ANISOU 1772  CD  GLU A 329    10820  12504   8993   2122    474   -476       C  
ATOM   1773  OE1 GLU A 329     -10.377   9.167  -3.723  1.00 87.27           O  
ANISOU 1773  OE1 GLU A 329    11286  12765   9109   2286    544   -584       O  
ATOM   1774  OE2 GLU A 329      -9.827   8.629  -1.651  1.00 87.74           O  
ANISOU 1774  OE2 GLU A 329    11113  12767   9455   2286    323   -498       O  
ATOM   1775  N   GLY A 330     -11.830  14.643  -4.384  1.00 63.88           N  
ANISOU 1775  N   GLY A 330     8360   9886   6026    956    929    -25       N  
ATOM   1776  CA  GLY A 330     -11.631  15.756  -5.297  1.00 63.69           C  
ANISOU 1776  CA  GLY A 330     8355   9997   5849    784   1127     92       C  
ATOM   1777  C   GLY A 330     -12.224  17.067  -4.845  1.00 63.40           C  
ANISOU 1777  C   GLY A 330     8405   9788   5897    451   1099    235       C  
ATOM   1778  O   GLY A 330     -11.604  18.111  -5.021  1.00 64.27           O  
ANISOU 1778  O   GLY A 330     8423  10033   5965    221   1259    368       O  
ATOM   1779  N   LEU A 331     -13.426  17.036  -4.297  1.00 62.33           N  
ANISOU 1779  N   LEU A 331     8453   9351   5878    425    905    215       N  
ATOM   1780  CA  LEU A 331     -14.131  18.220  -3.792  1.00 61.94           C  
ANISOU 1780  CA  LEU A 331     8514   9107   5915    171    865    324       C  
ATOM   1781  C   LEU A 331     -13.453  18.773  -2.524  1.00 62.00           C  
ANISOU 1781  C   LEU A 331     8327   9162   6066    -43    866    361       C  
ATOM   1782  O   LEU A 331     -13.440  19.975  -2.296  1.00 62.31           O  
ANISOU 1782  O   LEU A 331     8407   9137   6132   -292    912    458       O  
ATOM   1783  CB  LEU A 331     -15.577  17.796  -3.431  1.00 61.47           C  
ANISOU 1783  CB  LEU A 331     8646   8761   5950    257    662    275       C  
ATOM   1784  CG  LEU A 331     -16.775  18.440  -4.138  1.00 61.48           C  
ANISOU 1784  CG  LEU A 331     8890   8574   5896    238    611    337       C  
ATOM   1785  CD1 LEU A 331     -16.492  18.810  -5.563  1.00 60.84           C  
ANISOU 1785  CD1 LEU A 331     8916   8608   5594    267    735    393       C  
ATOM   1786  CD2 LEU A 331     -18.005  17.559  -4.022  1.00 61.74           C  
ANISOU 1786  CD2 LEU A 331     9028   8423   6007    384    408    261       C  
ATOM   1787  N   LEU A 332     -12.935  17.887  -1.682  1.00 61.64           N  
ANISOU 1787  N   LEU A 332     8106   9206   6110     60    789    280       N  
ATOM   1788  CA  LEU A 332     -12.308  18.251  -0.420  1.00 61.75           C  
ANISOU 1788  CA  LEU A 332     7942   9280   6238   -113    742    296       C  
ATOM   1789  C   LEU A 332     -10.798  18.353  -0.583  1.00 63.12           C  
ANISOU 1789  C   LEU A 332     7804   9794   6386   -177    868    325       C  
ATOM   1790  O   LEU A 332     -10.051  17.903   0.279  1.00 63.03           O  
ANISOU 1790  O   LEU A 332     7567   9933   6449   -144    797    288       O  
ATOM   1791  CB  LEU A 332     -12.678  17.198   0.654  1.00 60.76           C  
ANISOU 1791  CB  LEU A 332     7812   9060   6214     42    563    217       C  
ATOM   1792  CG  LEU A 332     -13.667  17.544   1.786  1.00 61.27           C  
ANISOU 1792  CG  LEU A 332     8031   8885   6366    -61    439    228       C  
ATOM   1793  CD1 LEU A 332     -14.488  18.800   1.542  1.00 60.97           C  
ANISOU 1793  CD1 LEU A 332     8184   8668   6314   -239    488    286       C  
ATOM   1794  CD2 LEU A 332     -14.570  16.393   2.069  1.00 62.11           C  
ANISOU 1794  CD2 LEU A 332     8246   8833   6519    138    313    186       C  
ATOM   1795  N   GLN A 333     -10.347  18.937  -1.687  1.00 64.33           N  
ANISOU 1795  N   GLN A 333     7931  10085   6427   -269   1057    407       N  
ATOM   1796  CA  GLN A 333      -8.921  19.098  -1.953  1.00 66.50           C  
ANISOU 1796  CA  GLN A 333     7870  10725   6672   -355   1218    465       C  
ATOM   1797  C   GLN A 333      -8.424  20.381  -1.265  1.00 67.95           C  
ANISOU 1797  C   GLN A 333     7953  10914   6952   -770   1213    571       C  
ATOM   1798  O   GLN A 333      -8.983  21.449  -1.501  1.00 68.23           O  
ANISOU 1798  O   GLN A 333     8219  10738   6970   -997   1242    660       O  
ATOM   1799  CB  GLN A 333      -8.671  19.161  -3.466  1.00 69.20           C  
ANISOU 1799  CB  GLN A 333     8246  11226   6819   -276   1448    526       C  
ATOM   1800  CG  GLN A 333      -7.200  19.047  -3.834  1.00 75.60           C  
ANISOU 1800  CG  GLN A 333     8666  12474   7583   -314   1659    591       C  
ATOM   1801  CD  GLN A 333      -6.685  17.622  -3.811  1.00 81.40           C  
ANISOU 1801  CD  GLN A 333     9166  13446   8314     68   1653    452       C  
ATOM   1802  OE1 GLN A 333      -7.452  16.648  -3.880  1.00 83.66           O  
ANISOU 1802  OE1 GLN A 333     9654  13566   8567    398   1541    309       O  
ATOM   1803  NE2 GLN A 333      -5.364  17.476  -3.720  1.00 81.48           N  
ANISOU 1803  NE2 GLN A 333     8741  13847   8370     29   1765    496       N  
ATOM   1804  N   LYS A 334      -7.407  20.279  -0.391  1.00 68.43           N  
ANISOU 1804  N   LYS A 334     7690  11193   7118   -866   1148    556       N  
ATOM   1805  CA  LYS A 334      -6.896  21.448   0.323  1.00 69.17           C  
ANISOU 1805  CA  LYS A 334     7693  11283   7307  -1283   1097    633       C  
ATOM   1806  C   LYS A 334      -6.414  22.556  -0.623  1.00 71.25           C  
ANISOU 1806  C   LYS A 334     7920  11635   7516  -1593   1307    803       C  
ATOM   1807  O   LYS A 334      -6.775  23.725  -0.462  1.00 71.49           O  
ANISOU 1807  O   LYS A 334     8179  11407   7578  -1904   1275    876       O  
ATOM   1808  CB  LYS A 334      -5.814  21.035   1.325  1.00 69.19           C  
ANISOU 1808  CB  LYS A 334     7316  11558   7415  -1311    969    587       C  
ATOM   1809  CG  LYS A 334      -6.380  20.630   2.698  1.00 69.76           C  
ANISOU 1809  CG  LYS A 334     7528  11425   7550  -1214    706    469       C  
ATOM   1810  CD  LYS A 334      -5.380  19.796   3.464  1.00 69.50           C  
ANISOU 1810  CD  LYS A 334     7128  11697   7583  -1102    575    425       C  
ATOM   1811  CE  LYS A 334      -5.849  19.411   4.823  1.00 69.56           C  
ANISOU 1811  CE  LYS A 334     7278  11533   7618  -1020    324    337       C  
ATOM   1812  NZ  LYS A 334      -7.084  18.633   4.745  1.00 70.09           N  
ANISOU 1812  NZ  LYS A 334     7644  11347   7641   -701    311    282       N  
ATOM   1813  N   ASP A 335      -5.652  22.179  -1.643  1.00 72.66           N  
ANISOU 1813  N   ASP A 335     7851  12157   7598  -1486   1530    870       N  
ATOM   1814  CA  ASP A 335      -5.146  23.112  -2.642  1.00 74.46           C  
ANISOU 1814  CA  ASP A 335     8031  12518   7743  -1763   1770   1065       C  
ATOM   1815  C   ASP A 335      -6.259  23.479  -3.624  1.00 76.19           C  
ANISOU 1815  C   ASP A 335     8697  12447   7805  -1684   1852   1120       C  
ATOM   1816  O   ASP A 335      -6.589  22.657  -4.478  1.00 76.33           O  
ANISOU 1816  O   ASP A 335     8795  12541   7667  -1332   1943   1062       O  
ATOM   1817  CB  ASP A 335      -4.039  22.406  -3.404  1.00 76.43           C  
ANISOU 1817  CB  ASP A 335     7862  13273   7905  -1588   2006   1102       C  
ATOM   1818  CG  ASP A 335      -3.236  23.312  -4.288  1.00 81.93           C  
ANISOU 1818  CG  ASP A 335     8386  14218   8526  -1914   2283   1334       C  
ATOM   1819  OD1 ASP A 335      -3.826  24.275  -4.849  1.00 82.57           O  
ANISOU 1819  OD1 ASP A 335     8810  14030   8532  -2147   2344   1472       O  
ATOM   1820  OD2 ASP A 335      -2.015  23.056  -4.439  1.00 84.51           O  
ANISOU 1820  OD2 ASP A 335     8227  15018   8866  -1929   2447   1394       O  
ATOM   1821  N   ARG A 336      -6.796  24.713  -3.554  1.00 77.29           N  
ANISOU 1821  N   ARG A 336     9131  12261   7975  -2001   1810   1232       N  
ATOM   1822  CA  ARG A 336      -7.876  25.150  -4.445  1.00 79.00           C  
ANISOU 1822  CA  ARG A 336     9773  12193   8050  -1923   1855   1303       C  
ATOM   1823  C   ARG A 336      -7.554  24.987  -5.947  1.00 81.06           C  
ANISOU 1823  C   ARG A 336    10009  12717   8071  -1817   2130   1435       C  
ATOM   1824  O   ARG A 336      -8.490  24.805  -6.736  1.00 82.05           O  
ANISOU 1824  O   ARG A 336    10450  12688   8037  -1588   2134   1427       O  
ATOM   1825  CB  ARG A 336      -8.344  26.586  -4.133  1.00 80.60           C  
ANISOU 1825  CB  ARG A 336    10288  12002   8333  -2273   1769   1416       C  
ATOM   1826  CG  ARG A 336      -7.262  27.638  -4.312  1.00 85.14           C  
ANISOU 1826  CG  ARG A 336    10717  12685   8949  -2747   1899   1626       C  
ATOM   1827  CD  ARG A 336      -7.728  29.053  -4.014  1.00 90.04           C  
ANISOU 1827  CD  ARG A 336    11703  12850   9661  -3078   1781   1715       C  
ATOM   1828  NE  ARG A 336      -6.685  30.020  -4.360  1.00 95.20           N  
ANISOU 1828  NE  ARG A 336    12238  13585  10348  -3565   1911   1946       N  
ATOM   1829  CZ  ARG A 336      -6.547  30.574  -5.568  1.00 99.40           C  
ANISOU 1829  CZ  ARG A 336    12910  14123  10736  -3713   2122   2202       C  
ATOM   1830  NH1 ARG A 336      -7.406  30.285  -6.543  1.00 99.49           N  
ANISOU 1830  NH1 ARG A 336    13201  14057  10544  -3391   2203   2242       N  
ATOM   1831  NH2 ARG A 336      -5.555  31.429  -5.807  1.00 99.19           N  
ANISOU 1831  NH2 ARG A 336    12746  14180  10760  -4200   2241   2432       N  
ATOM   1832  N   THR A 337      -6.252  25.014  -6.353  1.00 81.06           N  
ANISOU 1832  N   THR A 337     9628  13139   8031  -1966   2358   1553       N  
ATOM   1833  CA  THR A 337      -5.921  24.819  -7.766  1.00 81.67           C  
ANISOU 1833  CA  THR A 337     9679  13512   7841  -1835   2654   1673       C  
ATOM   1834  C   THR A 337      -6.112  23.368  -8.233  1.00 81.16           C  
ANISOU 1834  C   THR A 337     9587  13626   7626  -1301   2676   1465       C  
ATOM   1835  O   THR A 337      -6.286  23.120  -9.428  1.00 81.86           O  
ANISOU 1835  O   THR A 337     9837  13823   7443  -1094   2845   1499       O  
ATOM   1836  CB  THR A 337      -4.524  25.341  -8.106  1.00 84.31           C  
ANISOU 1836  CB  THR A 337     9595  14271   8168  -2156   2926   1883       C  
ATOM   1837  OG1 THR A 337      -3.539  24.433  -7.605  1.00 86.18           O  
ANISOU 1837  OG1 THR A 337     9337  14914   8495  -1984   2956   1754       O  
ATOM   1838  CG2 THR A 337      -4.283  26.745  -7.580  1.00 84.97           C  
ANISOU 1838  CG2 THR A 337     9697  14151   8437  -2725   2861   2072       C  
ATOM   1839  N   LYS A 338      -6.058  22.412  -7.310  1.00 79.80           N  
ANISOU 1839  N   LYS A 338     9231  13479   7611  -1080   2499   1252       N  
ATOM   1840  CA  LYS A 338      -6.235  20.999  -7.644  1.00 78.73           C  
ANISOU 1840  CA  LYS A 338     9101  13450   7364   -581   2483   1042       C  
ATOM   1841  C   LYS A 338      -7.662  20.476  -7.378  1.00 76.97           C  
ANISOU 1841  C   LYS A 338     9278  12799   7167   -360   2210    880       C  
ATOM   1842  O   LYS A 338      -7.971  19.347  -7.749  1.00 77.41           O  
ANISOU 1842  O   LYS A 338     9422  12866   7123     23   2166    711       O  
ATOM   1843  CB  LYS A 338      -5.208  20.149  -6.874  1.00 80.59           C  
ANISOU 1843  CB  LYS A 338     8887  13989   7745   -430   2460    926       C  
ATOM   1844  CG  LYS A 338      -3.762  20.628  -7.042  1.00 84.33           C  
ANISOU 1844  CG  LYS A 338     8877  14934   8229   -656   2715   1089       C  
ATOM   1845  CD  LYS A 338      -2.781  19.740  -6.278  1.00 88.16           C  
ANISOU 1845  CD  LYS A 338     8899  15732   8865   -459   2660    971       C  
ATOM   1846  CE  LYS A 338      -1.377  20.279  -6.348  1.00 92.20           C  
ANISOU 1846  CE  LYS A 338     8873  16728   9432   -730   2881   1147       C  
ATOM   1847  NZ  LYS A 338      -0.955  20.537  -7.757  1.00 94.96           N  
ANISOU 1847  NZ  LYS A 338     9151  17410   9517   -694   3273   1290       N  
ATOM   1848  N   ARG A 339      -8.521  21.285  -6.752  1.00 74.84           N  
ANISOU 1848  N   ARG A 339     9245  12158   7033   -597   2030    931       N  
ATOM   1849  CA  ARG A 339      -9.872  20.907  -6.357  1.00 73.34           C  
ANISOU 1849  CA  ARG A 339     9367  11591   6906   -437   1778    806       C  
ATOM   1850  C   ARG A 339     -10.833  20.766  -7.525  1.00 72.50           C  
ANISOU 1850  C   ARG A 339     9604  11355   6589   -243   1781    802       C  
ATOM   1851  O   ARG A 339     -10.736  21.531  -8.470  1.00 72.74           O  
ANISOU 1851  O   ARG A 339     9753  11442   6442   -360   1941    961       O  
ATOM   1852  CB  ARG A 339     -10.403  21.973  -5.391  1.00 72.96           C  
ANISOU 1852  CB  ARG A 339     9447  11231   7041   -743   1632    875       C  
ATOM   1853  CG  ARG A 339     -11.667  21.611  -4.618  1.00 72.24           C  
ANISOU 1853  CG  ARG A 339     9571  10807   7071   -606   1383    750       C  
ATOM   1854  CD  ARG A 339     -12.048  22.737  -3.674  1.00 72.40           C  
ANISOU 1854  CD  ARG A 339     9705  10562   7241   -883   1282    807       C  
ATOM   1855  NE  ARG A 339     -10.969  23.002  -2.723  1.00 72.51           N  
ANISOU 1855  NE  ARG A 339     9448  10724   7379  -1108   1281    806       N  
ATOM   1856  CZ  ARG A 339     -10.767  24.158  -2.108  1.00 72.87           C  
ANISOU 1856  CZ  ARG A 339     9538  10631   7518  -1435   1247    875       C  
ATOM   1857  NH1 ARG A 339     -11.571  25.184  -2.331  1.00 72.32           N  
ANISOU 1857  NH1 ARG A 339     9790  10250   7438  -1552   1228    956       N  
ATOM   1858  NH2 ARG A 339      -9.757  24.297  -1.266  1.00 72.58           N  
ANISOU 1858  NH2 ARG A 339     9238  10755   7585  -1639   1213    858       N  
ATOM   1859  N   LEU A 340     -11.816  19.850  -7.424  1.00 71.54           N  
ANISOU 1859  N   LEU A 340     9655  11036   6489     23   1578    637       N  
ATOM   1860  CA  LEU A 340     -12.855  19.664  -8.430  1.00 71.59           C  
ANISOU 1860  CA  LEU A 340     9989  10892   6321    200   1503    610       C  
ATOM   1861  C   LEU A 340     -13.662  20.935  -8.537  1.00 72.50           C  
ANISOU 1861  C   LEU A 340    10338  10757   6450    -22   1455    775       C  
ATOM   1862  O   LEU A 340     -14.156  21.424  -7.531  1.00 72.27           O  
ANISOU 1862  O   LEU A 340    10321  10502   6634   -167   1324    789       O  
ATOM   1863  CB  LEU A 340     -13.793  18.521  -8.028  1.00 71.47           C  
ANISOU 1863  CB  LEU A 340    10074  10672   6410    439   1249    417       C  
ATOM   1864  CG  LEU A 340     -13.941  17.314  -8.966  1.00 72.44           C  
ANISOU 1864  CG  LEU A 340    10336  10846   6343    769   1203    253       C  
ATOM   1865  CD1 LEU A 340     -15.119  16.456  -8.550  1.00 73.00           C  
ANISOU 1865  CD1 LEU A 340    10558  10625   6555    889    909    120       C  
ATOM   1866  CD2 LEU A 340     -14.167  17.733 -10.384  1.00 72.66           C  
ANISOU 1866  CD2 LEU A 340    10600  10935   6072    811   1293    324       C  
ATOM   1867  N   GLY A 341     -13.740  21.481  -9.743  1.00 73.69           N  
ANISOU 1867  N   GLY A 341    10679  10961   6358    -34   1573    906       N  
ATOM   1868  CA  GLY A 341     -14.420  22.739 -10.030  1.00 75.03           C  
ANISOU 1868  CA  GLY A 341    11102  10900   6506   -217   1541   1094       C  
ATOM   1869  C   GLY A 341     -13.477  23.876 -10.395  1.00 76.41           C  
ANISOU 1869  C   GLY A 341    11238  11201   6593   -513   1786   1332       C  
ATOM   1870  O   GLY A 341     -13.928  24.943 -10.822  1.00 76.20           O  
ANISOU 1870  O   GLY A 341    11463  10983   6505   -657   1783   1519       O  
ATOM   1871  N   ALA A 342     -12.155  23.671 -10.233  1.00 77.52           N  
ANISOU 1871  N   ALA A 342    11055  11663   6734   -612   1993   1342       N  
ATOM   1872  CA  ALA A 342     -11.170  24.695 -10.561  1.00 78.98           C  
ANISOU 1872  CA  ALA A 342    11145  12006   6858   -942   2237   1586       C  
ATOM   1873  C   ALA A 342     -11.097  24.978 -12.051  1.00 80.69           C  
ANISOU 1873  C   ALA A 342    11560  12374   6724   -901   2437   1763       C  
ATOM   1874  O   ALA A 342     -11.071  26.146 -12.430  1.00 81.39           O  
ANISOU 1874  O   ALA A 342    11819  12345   6759  -1176   2521   2017       O  
ATOM   1875  CB  ALA A 342      -9.800  24.304 -10.036  1.00 79.10           C  
ANISOU 1875  CB  ALA A 342    10705  12375   6972  -1041   2395   1550       C  
ATOM   1876  N   LYS A 343     -11.097  23.941 -12.901  1.00 81.42           N  
ANISOU 1876  N   LYS A 343    11674  12700   6563   -557   2504   1635       N  
ATOM   1877  CA  LYS A 343     -10.997  24.162 -14.337  1.00 82.87           C  
ANISOU 1877  CA  LYS A 343    12066  13065   6356   -492   2705   1793       C  
ATOM   1878  C   LYS A 343     -12.299  24.717 -14.967  1.00 84.13           C  
ANISOU 1878  C   LYS A 343    12696  12891   6380   -436   2507   1884       C  
ATOM   1879  O   LYS A 343     -12.250  25.824 -15.520  1.00 85.17           O  
ANISOU 1879  O   LYS A 343    13017  12956   6390   -667   2616   2170       O  
ATOM   1880  CB  LYS A 343     -10.482  22.914 -15.072  1.00 84.80           C  
ANISOU 1880  CB  LYS A 343    12200  13688   6333   -129   2859   1611       C  
ATOM   1881  N   ASP A 344     -13.437  23.967 -14.946  1.00 83.65           N  
ANISOU 1881  N   ASP A 344    12821  12631   6331   -140   2215   1667       N  
ATOM   1882  CA  ASP A 344     -14.661  24.472 -15.596  1.00 83.62           C  
ANISOU 1882  CA  ASP A 344    13221  12359   6194    -67   2010   1761       C  
ATOM   1883  C   ASP A 344     -15.894  24.464 -14.686  1.00 81.51           C  
ANISOU 1883  C   ASP A 344    13022  11708   6238    -20   1663   1642       C  
ATOM   1884  O   ASP A 344     -17.000  24.182 -15.156  1.00 81.95           O  
ANISOU 1884  O   ASP A 344    13309  11622   6207    187   1424   1576       O  
ATOM   1885  CB  ASP A 344     -14.967  23.768 -16.941  1.00 87.04           C  
ANISOU 1885  CB  ASP A 344    13893  12968   6210    242   2002   1684       C  
ATOM   1886  CG  ASP A 344     -13.754  23.516 -17.818  1.00 96.52           C  
ANISOU 1886  CG  ASP A 344    15000  14605   7070    278   2371   1747       C  
ATOM   1887  OD1 ASP A 344     -12.930  22.643 -17.454  1.00 98.21           O  
ANISOU 1887  OD1 ASP A 344    14907  15066   7342    384   2506   1564       O  
ATOM   1888  OD2 ASP A 344     -13.637  24.175 -18.890  1.00101.20           O  
ANISOU 1888  OD2 ASP A 344    15827  15306   7320    222   2531   1987       O  
ATOM   1889  N   ASP A 345     -15.704  24.833 -13.405  1.00 78.71           N  
ANISOU 1889  N   ASP A 345    12467  11205   6233   -222   1638   1630       N  
ATOM   1890  CA  ASP A 345     -16.746  24.986 -12.394  1.00 76.55           C  
ANISOU 1890  CA  ASP A 345    12224  10598   6264   -213   1374   1546       C  
ATOM   1891  C   ASP A 345     -17.768  23.808 -12.374  1.00 74.32           C  
ANISOU 1891  C   ASP A 345    11967  10258   6014     88   1114   1313       C  
ATOM   1892  O   ASP A 345     -17.338  22.656 -12.358  1.00 73.71           O  
ANISOU 1892  O   ASP A 345    11734  10368   5905    232   1134   1126       O  
ATOM   1893  CB  ASP A 345     -17.407  26.376 -12.532  1.00 77.94           C  
ANISOU 1893  CB  ASP A 345    12677  10472   6466   -353   1310   1774       C  
ATOM   1894  CG  ASP A 345     -18.020  26.876 -11.236  1.00 83.02           C  
ANISOU 1894  CG  ASP A 345    13288  10809   7448   -430   1153   1720       C  
ATOM   1895  OD1 ASP A 345     -17.255  27.165 -10.289  1.00 84.39           O  
ANISOU 1895  OD1 ASP A 345    13276  10982   7805   -648   1248   1701       O  
ATOM   1896  OD2 ASP A 345     -19.265  26.969 -11.164  1.00 84.64           O  
ANISOU 1896  OD2 ASP A 345    13643  10791   7725   -262    933   1693       O  
ATOM   1897  N   PHE A 346     -19.090  24.092 -12.352  1.00 73.33           N  
ANISOU 1897  N   PHE A 346    12022   9872   5967    179    868   1328       N  
ATOM   1898  CA  PHE A 346     -20.202  23.142 -12.319  1.00 73.43           C  
ANISOU 1898  CA  PHE A 346    12048   9805   6048    403    594   1149       C  
ATOM   1899  C   PHE A 346     -20.081  21.972 -13.307  1.00 75.96           C  
ANISOU 1899  C   PHE A 346    12428  10324   6109    612    552    997       C  
ATOM   1900  O   PHE A 346     -20.466  20.860 -12.966  1.00 76.61           O  
ANISOU 1900  O   PHE A 346    12419  10388   6302    738    390    793       O  
ATOM   1901  CB  PHE A 346     -21.531  23.887 -12.523  1.00 71.55           C  
ANISOU 1901  CB  PHE A 346    12007   9324   5854    464    374   1260       C  
ATOM   1902  CG  PHE A 346     -22.759  23.011 -12.537  1.00 70.60           C  
ANISOU 1902  CG  PHE A 346    11869   9136   5818    656     74   1110       C  
ATOM   1903  CD1 PHE A 346     -23.088  22.232 -11.441  1.00 70.67           C  
ANISOU 1903  CD1 PHE A 346    11650   9095   6106    663    -17    947       C  
ATOM   1904  CD2 PHE A 346     -23.603  22.991 -13.634  1.00 70.61           C  
ANISOU 1904  CD2 PHE A 346    12081   9128   5619    810   -129   1148       C  
ATOM   1905  CE1 PHE A 346     -24.221  21.428 -11.456  1.00 70.97           C  
ANISOU 1905  CE1 PHE A 346    11652   9072   6239    792   -291    835       C  
ATOM   1906  CE2 PHE A 346     -24.742  22.193 -13.643  1.00 70.92           C  
ANISOU 1906  CE2 PHE A 346    12075   9112   5759    946   -431   1015       C  
ATOM   1907  CZ  PHE A 346     -25.042  21.413 -12.557  1.00 70.68           C  
ANISOU 1907  CZ  PHE A 346    11799   9031   6026    922   -503    864       C  
ATOM   1908  N   MET A 347     -19.512  22.209 -14.496  1.00 76.93           N  
ANISOU 1908  N   MET A 347    12720  10630   5880    643    707   1096       N  
ATOM   1909  CA  MET A 347     -19.336  21.210 -15.546  1.00 78.80           C  
ANISOU 1909  CA  MET A 347    13072  11065   5803    864    693    947       C  
ATOM   1910  C   MET A 347     -18.580  19.963 -15.145  1.00 78.89           C  
ANISOU 1910  C   MET A 347    12873  11230   5871    973    769    707       C  
ATOM   1911  O   MET A 347     -18.824  18.900 -15.711  1.00 79.66           O  
ANISOU 1911  O   MET A 347    13079  11366   5821   1193    630    501       O  
ATOM   1912  CB  MET A 347     -18.639  21.840 -16.738  1.00 81.33           C  
ANISOU 1912  CB  MET A 347    13579  11599   5723    848    935   1132       C  
ATOM   1913  CG  MET A 347     -19.352  23.055 -17.222  1.00 86.39           C  
ANISOU 1913  CG  MET A 347    14476  12071   6278    765    849   1391       C  
ATOM   1914  SD  MET A 347     -20.762  22.539 -18.184  1.00 96.45           S  
ANISOU 1914  SD  MET A 347    16045  13248   7353   1029    449   1287       S  
ATOM   1915  CE  MET A 347     -20.013  22.527 -19.811  1.00 95.10           C  
ANISOU 1915  CE  MET A 347    16158  13403   6574   1156    660   1354       C  
ATOM   1916  N   GLU A 348     -17.635  20.089 -14.219  1.00 77.91           N  
ANISOU 1916  N   GLU A 348    12468  11189   5946    829    973    728       N  
ATOM   1917  CA  GLU A 348     -16.856  18.948 -13.755  1.00 77.21           C  
ANISOU 1917  CA  GLU A 348    12159  11246   5933    951   1041    521       C  
ATOM   1918  C   GLU A 348     -17.680  18.106 -12.775  1.00 76.52           C  
ANISOU 1918  C   GLU A 348    12004  10919   6153   1008    756    348       C  
ATOM   1919  O   GLU A 348     -17.599  16.877 -12.803  1.00 77.27           O  
ANISOU 1919  O   GLU A 348    12088  11032   6238   1205    668    135       O  
ATOM   1920  CB  GLU A 348     -15.592  19.429 -13.054  1.00 78.62           C  
ANISOU 1920  CB  GLU A 348    12034  11604   6233    762   1320    625       C  
ATOM   1921  CG  GLU A 348     -14.774  20.429 -13.831  1.00 81.35           C  
ANISOU 1921  CG  GLU A 348    12395  12177   6337    614   1621    852       C  
ATOM   1922  CD  GLU A 348     -13.412  20.631 -13.210  1.00 85.31           C  
ANISOU 1922  CD  GLU A 348    12537  12920   6958    447   1881    913       C  
ATOM   1923  OE1 GLU A 348     -12.852  19.664 -12.647  1.00 84.84           O  
ANISOU 1923  OE1 GLU A 348    12240  12983   7012    591   1886    731       O  
ATOM   1924  OE2 GLU A 348     -12.907  21.770 -13.271  1.00 87.89           O  
ANISOU 1924  OE2 GLU A 348    12818  13302   7275    161   2062   1152       O  
ATOM   1925  N   ILE A 349     -18.448  18.777 -11.898  1.00 74.75           N  
ANISOU 1925  N   ILE A 349    11741  10467   6195    840    626    446       N  
ATOM   1926  CA  ILE A 349     -19.322  18.147 -10.917  1.00 73.76           C  
ANISOU 1926  CA  ILE A 349    11537  10128   6359    856    384    336       C  
ATOM   1927  C   ILE A 349     -20.424  17.390 -11.711  1.00 73.51           C  
ANISOU 1927  C   ILE A 349    11716   9987   6228   1023    105    219       C  
ATOM   1928  O   ILE A 349     -20.544  16.170 -11.616  1.00 73.43           O  
ANISOU 1928  O   ILE A 349    11703   9933   6265   1148    -36     32       O  
ATOM   1929  CB  ILE A 349     -19.926  19.238  -9.965  1.00 73.74           C  
ANISOU 1929  CB  ILE A 349    11474   9943   6599    660    352    487       C  
ATOM   1930  CG1 ILE A 349     -18.879  20.286  -9.471  1.00 74.29           C  
ANISOU 1930  CG1 ILE A 349    11418  10098   6709    452    603    624       C  
ATOM   1931  CG2 ILE A 349     -20.671  18.617  -8.820  1.00 74.06           C  
ANISOU 1931  CG2 ILE A 349    11394   9819   6927    663    165    397       C  
ATOM   1932  CD1 ILE A 349     -17.589  19.766  -8.943  1.00 75.01           C  
ANISOU 1932  CD1 ILE A 349    11273  10389   6837    428    766    548       C  
ATOM   1933  N   LYS A 350     -21.148  18.124 -12.578  1.00 73.14           N  
ANISOU 1933  N   LYS A 350    11874   9899   6018   1026     20    334       N  
ATOM   1934  CA  LYS A 350     -22.217  17.693 -13.466  1.00 73.04           C  
ANISOU 1934  CA  LYS A 350    12072   9806   5872   1155   -265    263       C  
ATOM   1935  C   LYS A 350     -21.887  16.351 -14.146  1.00 72.93           C  
ANISOU 1935  C   LYS A 350    12175   9870   5666   1347   -341     20       C  
ATOM   1936  O   LYS A 350     -22.758  15.482 -14.249  1.00 73.27           O  
ANISOU 1936  O   LYS A 350    12293   9772   5776   1412   -642   -126       O  
ATOM   1937  CB  LYS A 350     -22.394  18.784 -14.548  1.00 74.74           C  
ANISOU 1937  CB  LYS A 350    12516  10080   5803   1159   -225    448       C  
ATOM   1938  CG  LYS A 350     -23.813  18.985 -15.030  1.00 78.89           C  
ANISOU 1938  CG  LYS A 350    13185  10463   6328   1211   -553    493       C  
ATOM   1939  CD  LYS A 350     -23.873  19.214 -16.531  1.00 83.08           C  
ANISOU 1939  CD  LYS A 350    14030  11107   6429   1340   -613    530       C  
ATOM   1940  CE  LYS A 350     -25.297  19.322 -17.025  1.00 87.47           C  
ANISOU 1940  CE  LYS A 350    14706  11539   6990   1404   -988    568       C  
ATOM   1941  NZ  LYS A 350     -25.440  18.927 -18.467  1.00 90.59           N  
ANISOU 1941  NZ  LYS A 350    15412  12042   6964   1567  -1166    482       N  
ATOM   1942  N   SER A 351     -20.627  16.179 -14.611  1.00 72.04           N  
ANISOU 1942  N   SER A 351    12075   9980   5319   1439    -69    -26       N  
ATOM   1943  CA  SER A 351     -20.221  14.983 -15.349  1.00 71.69           C  
ANISOU 1943  CA  SER A 351    12180  10020   5042   1676   -106   -270       C  
ATOM   1944  C   SER A 351     -19.578  13.870 -14.524  1.00 69.74           C  
ANISOU 1944  C   SER A 351    11762   9745   4992   1761    -77   -453       C  
ATOM   1945  O   SER A 351     -19.363  12.791 -15.065  1.00 69.82           O  
ANISOU 1945  O   SER A 351    11928   9755   4844   1983   -155   -683       O  
ATOM   1946  CB  SER A 351     -19.293  15.364 -16.498  1.00 74.77           C  
ANISOU 1946  CB  SER A 351    12708  10701   5001   1793    177   -227       C  
ATOM   1947  OG  SER A 351     -18.143  16.009 -15.979  1.00 79.31           O  
ANISOU 1947  OG  SER A 351    13025  11465   5643   1672    534    -74       O  
ATOM   1948  N   HIS A 352     -19.292  14.110 -13.235  1.00 67.83           N  
ANISOU 1948  N   HIS A 352    11234   9464   5076   1605     17   -360       N  
ATOM   1949  CA  HIS A 352     -18.659  13.139 -12.355  1.00 66.24           C  
ANISOU 1949  CA  HIS A 352    10863   9239   5067   1684     40   -494       C  
ATOM   1950  C   HIS A 352     -19.417  11.808 -12.263  1.00 66.02           C  
ANISOU 1950  C   HIS A 352    10978   8953   5152   1794   -286   -700       C  
ATOM   1951  O   HIS A 352     -20.648  11.820 -12.248  1.00 66.30           O  
ANISOU 1951  O   HIS A 352    11101   8786   5303   1681   -553   -675       O  
ATOM   1952  CB  HIS A 352     -18.500  13.743 -10.954  1.00 65.50           C  
ANISOU 1952  CB  HIS A 352    10480   9113   5295   1464    125   -339       C  
ATOM   1953  CG  HIS A 352     -17.617  12.933 -10.066  1.00 65.76           C  
ANISOU 1953  CG  HIS A 352    10318   9185   5483   1546    190   -432       C  
ATOM   1954  ND1 HIS A 352     -18.120  11.879  -9.311  1.00 67.12           N  
ANISOU 1954  ND1 HIS A 352    10494   9127   5882   1581    -38   -535       N  
ATOM   1955  CD2 HIS A 352     -16.278  12.992  -9.896  1.00 66.22           C  
ANISOU 1955  CD2 HIS A 352    10178   9496   5488   1612    444   -427       C  
ATOM   1956  CE1 HIS A 352     -17.078  11.335  -8.711  1.00 67.31           C  
ANISOU 1956  CE1 HIS A 352    10353   9251   5972   1691     73   -591       C  
ATOM   1957  NE2 HIS A 352     -15.949  11.977  -9.021  1.00 67.43           N  
ANISOU 1957  NE2 HIS A 352    10219   9569   5831   1718    358   -535       N  
ATOM   1958  N   VAL A 353     -18.684  10.656 -12.155  1.00 65.25           N  
ANISOU 1958  N   VAL A 353    10895   8854   5044   2009   -273   -895       N  
ATOM   1959  CA  VAL A 353     -19.269   9.308 -11.977  1.00 65.44           C  
ANISOU 1959  CA  VAL A 353    11077   8586   5201   2103   -581  -1090       C  
ATOM   1960  C   VAL A 353     -20.470   9.291 -11.001  1.00 65.26           C  
ANISOU 1960  C   VAL A 353    10966   8299   5531   1844   -831   -979       C  
ATOM   1961  O   VAL A 353     -21.470   8.648 -11.295  1.00 66.07           O  
ANISOU 1961  O   VAL A 353    11247   8171   5684   1813  -1141  -1072       O  
ATOM   1962  CB  VAL A 353     -18.231   8.232 -11.521  1.00 66.76           C  
ANISOU 1962  CB  VAL A 353    11189   8755   5423   2336   -502  -1243       C  
ATOM   1963  CG1 VAL A 353     -17.248   7.891 -12.619  1.00 68.21           C  
ANISOU 1963  CG1 VAL A 353    11520   9152   5246   2668   -325  -1426       C  
ATOM   1964  CG2 VAL A 353     -17.475   8.662 -10.266  1.00 67.51           C  
ANISOU 1964  CG2 VAL A 353    10927   8986   5738   2229   -291  -1077       C  
ATOM   1965  N   PHE A 354     -20.350   9.977  -9.843  1.00 63.81           N  
ANISOU 1965  N   PHE A 354    10504   8161   5580   1659   -696   -787       N  
ATOM   1966  CA  PHE A 354     -21.345  10.014  -8.788  1.00 63.51           C  
ANISOU 1966  CA  PHE A 354    10340   7932   5857   1437   -855   -666       C  
ATOM   1967  C   PHE A 354     -22.666  10.590  -9.242  1.00 65.27           C  
ANISOU 1967  C   PHE A 354    10628   8077   6095   1297  -1037   -585       C  
ATOM   1968  O   PHE A 354     -23.699  10.188  -8.719  1.00 65.89           O  
ANISOU 1968  O   PHE A 354    10659   7972   6404   1162  -1250   -547       O  
ATOM   1969  CB  PHE A 354     -20.813  10.784  -7.551  1.00 61.95           C  
ANISOU 1969  CB  PHE A 354     9865   7847   5826   1301   -636   -495       C  
ATOM   1970  CG  PHE A 354     -21.709  10.747  -6.339  1.00 60.74           C  
ANISOU 1970  CG  PHE A 354     9581   7529   5968   1113   -754   -381       C  
ATOM   1971  CD1 PHE A 354     -21.785   9.614  -5.547  1.00 60.80           C  
ANISOU 1971  CD1 PHE A 354     9579   7370   6154   1125   -882   -425       C  
ATOM   1972  CD2 PHE A 354     -22.476  11.844  -5.991  1.00 60.90           C  
ANISOU 1972  CD2 PHE A 354     9501   7561   6078    942   -725   -223       C  
ATOM   1973  CE1 PHE A 354     -22.615   9.576  -4.433  1.00 61.05           C  
ANISOU 1973  CE1 PHE A 354     9487   7279   6429    944   -960   -296       C  
ATOM   1974  CE2 PHE A 354     -23.308  11.804  -4.879  1.00 61.25           C  
ANISOU 1974  CE2 PHE A 354     9414   7491   6368    795   -799   -120       C  
ATOM   1975  CZ  PHE A 354     -23.371  10.670  -4.105  1.00 60.82           C  
ANISOU 1975  CZ  PHE A 354     9337   7303   6470    786   -906   -150       C  
ATOM   1976  N   PHE A 355     -22.654  11.550 -10.179  1.00 65.82           N  
ANISOU 1976  N   PHE A 355    10786   8296   5926   1323   -952   -534       N  
ATOM   1977  CA  PHE A 355     -23.902  12.160 -10.646  1.00 66.24           C  
ANISOU 1977  CA  PHE A 355    10895   8289   5985   1225  -1143   -443       C  
ATOM   1978  C   PHE A 355     -24.414  11.537 -11.925  1.00 69.50           C  
ANISOU 1978  C   PHE A 355    11583   8646   6176   1339  -1402   -601       C  
ATOM   1979  O   PHE A 355     -25.157  12.187 -12.659  1.00 70.23           O  
ANISOU 1979  O   PHE A 355    11759   8763   6161   1313  -1531   -529       O  
ATOM   1980  CB  PHE A 355     -23.757  13.680 -10.767  1.00 64.31           C  
ANISOU 1980  CB  PHE A 355    10591   8191   5652   1160   -934   -247       C  
ATOM   1981  CG  PHE A 355     -23.566  14.333  -9.411  1.00 63.37           C  
ANISOU 1981  CG  PHE A 355    10223   8072   5782   1015   -756   -104       C  
ATOM   1982  CD1 PHE A 355     -24.620  14.440  -8.519  1.00 63.33           C  
ANISOU 1982  CD1 PHE A 355    10074   7938   6050    892   -880    -17       C  
ATOM   1983  CD2 PHE A 355     -22.334  14.826  -9.027  1.00 63.11           C  
ANISOU 1983  CD2 PHE A 355    10095   8184   5698   1002   -470    -64       C  
ATOM   1984  CE1 PHE A 355     -24.443  15.029  -7.273  1.00 63.26           C  
ANISOU 1984  CE1 PHE A 355     9876   7932   6227    782   -716     90       C  
ATOM   1985  CE2 PHE A 355     -22.166  15.421  -7.786  1.00 63.36           C  
ANISOU 1985  CE2 PHE A 355     9932   8206   5936    863   -343     44       C  
ATOM   1986  CZ  PHE A 355     -23.221  15.511  -6.917  1.00 62.89           C  
ANISOU 1986  CZ  PHE A 355     9777   8004   6114    766   -466    110       C  
ATOM   1987  N   SER A 356     -24.022  10.275 -12.210  1.00 71.32           N  
ANISOU 1987  N   SER A 356    11980   8791   6329   1481  -1500   -826       N  
ATOM   1988  CA  SER A 356     -24.414   9.543 -13.422  1.00 73.01           C  
ANISOU 1988  CA  SER A 356    12512   8925   6304   1607  -1769  -1032       C  
ATOM   1989  C   SER A 356     -25.904   9.429 -13.541  1.00 74.24           C  
ANISOU 1989  C   SER A 356    12677   8915   6616   1437  -2148  -1000       C  
ATOM   1990  O   SER A 356     -26.443   9.539 -14.633  1.00 75.36           O  
ANISOU 1990  O   SER A 356    13030   9078   6525   1488  -2356  -1067       O  
ATOM   1991  CB  SER A 356     -23.867   8.122 -13.386  1.00 75.12           C  
ANISOU 1991  CB  SER A 356    12937   9029   6575   1759  -1859  -1280       C  
ATOM   1992  OG  SER A 356     -22.478   8.108 -13.642  1.00 79.15           O  
ANISOU 1992  OG  SER A 356    13457   9727   6891   1984  -1534  -1352       O  
ATOM   1993  N   LEU A 357     -26.569   9.146 -12.425  1.00 74.05           N  
ANISOU 1993  N   LEU A 357    12420   8737   6977   1238  -2250   -901       N  
ATOM   1994  CA  LEU A 357     -28.001   8.941 -12.410  1.00 73.69           C  
ANISOU 1994  CA  LEU A 357    12303   8554   7144   1048  -2601   -852       C  
ATOM   1995  C   LEU A 357     -28.800  10.229 -12.492  1.00 74.03           C  
ANISOU 1995  C   LEU A 357    12168   8740   7221    969  -2589   -634       C  
ATOM   1996  O   LEU A 357     -30.024  10.159 -12.602  1.00 75.35           O  
ANISOU 1996  O   LEU A 357    12227   8842   7559    831  -2878   -577       O  
ATOM   1997  CB  LEU A 357     -28.382   8.096 -11.179  1.00 73.31           C  
ANISOU 1997  CB  LEU A 357    12071   8303   7481    866  -2683   -812       C  
ATOM   1998  CG  LEU A 357     -27.605   6.767 -11.035  1.00 73.67           C  
ANISOU 1998  CG  LEU A 357    12316   8153   7521    963  -2718  -1014       C  
ATOM   1999  CD1 LEU A 357     -28.104   5.961  -9.880  1.00 73.86           C  
ANISOU 1999  CD1 LEU A 357    12187   7960   7915    757  -2825   -933       C  
ATOM   2000  CD2 LEU A 357     -27.730   5.928 -12.278  1.00 73.85           C  
ANISOU 2000  CD2 LEU A 357    12705   8038   7317   1071  -3023  -1277       C  
ATOM   2001  N   ILE A 358     -28.137  11.397 -12.519  1.00 72.86           N  
ANISOU 2001  N   ILE A 358    11995   8779   6907   1059  -2278   -511       N  
ATOM   2002  CA  ILE A 358     -28.850  12.657 -12.611  1.00 72.35           C  
ANISOU 2002  CA  ILE A 358    11810   8811   6868   1019  -2269   -305       C  
ATOM   2003  C   ILE A 358     -29.055  13.135 -14.048  1.00 72.57           C  
ANISOU 2003  C   ILE A 358    12091   8933   6550   1142  -2411   -319       C  
ATOM   2004  O   ILE A 358     -28.085  13.322 -14.788  1.00 72.60           O  
ANISOU 2004  O   ILE A 358    12318   9050   6218   1281  -2229   -373       O  
ATOM   2005  CB  ILE A 358     -28.195  13.760 -11.743  1.00 71.70           C  
ANISOU 2005  CB  ILE A 358    11561   8825   6857   1000  -1890   -129       C  
ATOM   2006  CG1 ILE A 358     -28.039  13.330 -10.271  1.00 72.43           C  
ANISOU 2006  CG1 ILE A 358    11418   8843   7261    886  -1762   -108       C  
ATOM   2007  CG2 ILE A 358     -28.947  15.064 -11.874  1.00 71.52           C  
ANISOU 2007  CG2 ILE A 358    11459   8849   6865    991  -1904     71       C  
ATOM   2008  CD1 ILE A 358     -29.327  12.995  -9.546  1.00 73.46           C  
ANISOU 2008  CD1 ILE A 358    11332   8867   7715    741  -1974    -46       C  
ATOM   2009  N   ASN A 359     -30.329  13.348 -14.436  1.00 72.39           N  
ANISOU 2009  N   ASN A 359    12017   8887   6601   1093  -2734   -254       N  
ATOM   2010  CA  ASN A 359     -30.667  14.026 -15.680  1.00 72.62           C  
ANISOU 2010  CA  ASN A 359    12257   9017   6317   1211  -2883   -207       C  
ATOM   2011  C   ASN A 359     -30.761  15.450 -15.169  1.00 72.30           C  
ANISOU 2011  C   ASN A 359    12048   9043   6379   1214  -2650     54       C  
ATOM   2012  O   ASN A 359     -31.680  15.766 -14.402  1.00 72.30           O  
ANISOU 2012  O   ASN A 359    11766   9003   6703   1133  -2727    177       O  
ATOM   2013  CB  ASN A 359     -32.018  13.609 -16.223  1.00 74.38           C  
ANISOU 2013  CB  ASN A 359    12460   9192   6608   1157  -3365   -247       C  
ATOM   2014  CG  ASN A 359     -32.325  14.257 -17.548  1.00 78.88           C  
ANISOU 2014  CG  ASN A 359    13283   9876   6811   1301  -3547   -202       C  
ATOM   2015  OD1 ASN A 359     -32.454  13.582 -18.570  1.00 81.81           O  
ANISOU 2015  OD1 ASN A 359    13927  10243   6913   1356  -3835   -383       O  
ATOM   2016  ND2 ASN A 359     -32.447  15.576 -17.580  1.00 78.91           N  
ANISOU 2016  ND2 ASN A 359    13239   9970   6775   1375  -3398     36       N  
ATOM   2017  N   TRP A 360     -29.784  16.285 -15.520  1.00 71.79           N  
ANISOU 2017  N   TRP A 360    12147   9073   6055   1300  -2343    138       N  
ATOM   2018  CA  TRP A 360     -29.718  17.619 -14.966  1.00 72.02           C  
ANISOU 2018  CA  TRP A 360    12067   9113   6186   1284  -2103    369       C  
ATOM   2019  C   TRP A 360     -30.896  18.486 -15.370  1.00 74.58           C  
ANISOU 2019  C   TRP A 360    12376   9426   6536   1350  -2330    540       C  
ATOM   2020  O   TRP A 360     -31.336  19.297 -14.562  1.00 74.85           O  
ANISOU 2020  O   TRP A 360    12217   9406   6817   1332  -2241    692       O  
ATOM   2021  CB  TRP A 360     -28.369  18.256 -15.260  1.00 70.59           C  
ANISOU 2021  CB  TRP A 360    12063   9024   5734   1315  -1740    428       C  
ATOM   2022  CG  TRP A 360     -27.265  17.623 -14.457  1.00 69.46           C  
ANISOU 2022  CG  TRP A 360    11804   8899   5688   1247  -1476    310       C  
ATOM   2023  CD1 TRP A 360     -26.433  16.619 -14.855  1.00 69.77           C  
ANISOU 2023  CD1 TRP A 360    11955   9008   5545   1310  -1421    116       C  
ATOM   2024  CD2 TRP A 360     -26.954  17.876 -13.077  1.00 68.62           C  
ANISOU 2024  CD2 TRP A 360    11444   8736   5891   1128  -1269    365       C  
ATOM   2025  NE1 TRP A 360     -25.576  16.280 -13.831  1.00 69.54           N  
ANISOU 2025  NE1 TRP A 360    11742   8980   5701   1244  -1189     69       N  
ATOM   2026  CE2 TRP A 360     -25.873  17.041 -12.731  1.00 69.13           C  
ANISOU 2026  CE2 TRP A 360    11470   8855   5940   1118  -1100    221       C  
ATOM   2027  CE3 TRP A 360     -27.471  18.739 -12.108  1.00 68.46           C  
ANISOU 2027  CE3 TRP A 360    11242   8631   6138   1052  -1213    513       C  
ATOM   2028  CZ2 TRP A 360     -25.291  17.066 -11.467  1.00 69.36           C  
ANISOU 2028  CZ2 TRP A 360    11285   8866   6205   1017   -896    237       C  
ATOM   2029  CZ3 TRP A 360     -26.901  18.751 -10.856  1.00 68.88           C  
ANISOU 2029  CZ3 TRP A 360    11106   8659   6407    949  -1001    509       C  
ATOM   2030  CH2 TRP A 360     -25.818  17.932 -10.547  1.00 69.07           C  
ANISOU 2030  CH2 TRP A 360    11095   8748   6402    922   -854    380       C  
ATOM   2031  N   ASP A 361     -31.478  18.254 -16.554  1.00 76.53           N  
ANISOU 2031  N   ASP A 361    12815   9720   6542   1441  -2650    502       N  
ATOM   2032  CA  ASP A 361     -32.646  19.013 -16.987  1.00 78.44           C  
ANISOU 2032  CA  ASP A 361    13028   9969   6807   1531  -2920    666       C  
ATOM   2033  C   ASP A 361     -33.870  18.712 -16.123  1.00 79.61           C  
ANISOU 2033  C   ASP A 361    12786  10072   7389   1458  -3142    675       C  
ATOM   2034  O   ASP A 361     -34.476  19.648 -15.593  1.00 80.12           O  
ANISOU 2034  O   ASP A 361    12666  10119   7659   1517  -3105    854       O  
ATOM   2035  CB  ASP A 361     -32.928  18.795 -18.468  1.00 80.80           C  
ANISOU 2035  CB  ASP A 361    13638  10351   6711   1644  -3232    616       C  
ATOM   2036  CG  ASP A 361     -32.225  19.820 -19.322  1.00 88.65           C  
ANISOU 2036  CG  ASP A 361    14962  11408   7314   1763  -3032    786       C  
ATOM   2037  OD1 ASP A 361     -32.120  20.986 -18.883  1.00 90.42           O  
ANISOU 2037  OD1 ASP A 361    15137  11575   7645   1787  -2843   1013       O  
ATOM   2038  OD2 ASP A 361     -31.796  19.467 -20.440  1.00 92.40           O  
ANISOU 2038  OD2 ASP A 361    15763  11981   7365   1834  -3061    696       O  
ATOM   2039  N   ASP A 362     -34.193  17.420 -15.911  1.00 79.51           N  
ANISOU 2039  N   ASP A 362    12647  10034   7528   1330  -3345    489       N  
ATOM   2040  CA  ASP A 362     -35.324  17.056 -15.056  1.00 79.79           C  
ANISOU 2040  CA  ASP A 362    12281  10051   7985   1217  -3527    518       C  
ATOM   2041  C   ASP A 362     -35.131  17.556 -13.623  1.00 79.34           C  
ANISOU 2041  C   ASP A 362    11954   9958   8232   1171  -3170    627       C  
ATOM   2042  O   ASP A 362     -36.099  17.949 -12.975  1.00 79.28           O  
ANISOU 2042  O   ASP A 362    11626   9983   8513   1176  -3222    750       O  
ATOM   2043  CB  ASP A 362     -35.541  15.544 -15.053  1.00 82.16           C  
ANISOU 2043  CB  ASP A 362    12542  10288   8387   1043  -3778    311       C  
ATOM   2044  CG  ASP A 362     -35.800  14.936 -16.411  1.00 88.79           C  
ANISOU 2044  CG  ASP A 362    13652  11143   8943   1072  -4188    163       C  
ATOM   2045  OD1 ASP A 362     -36.102  15.692 -17.356  1.00 91.02           O  
ANISOU 2045  OD1 ASP A 362    14077  11518   8988   1224  -4347    255       O  
ATOM   2046  OD2 ASP A 362     -35.709  13.704 -16.530  1.00 91.55           O  
ANISOU 2046  OD2 ASP A 362    14094  11394   9296    951  -4366    -46       O  
ATOM   2047  N   LEU A 363     -33.878  17.568 -13.140  1.00 78.81           N  
ANISOU 2047  N   LEU A 363    12012   9847   8085   1140  -2810    580       N  
ATOM   2048  CA  LEU A 363     -33.533  18.038 -11.804  1.00 78.54           C  
ANISOU 2048  CA  LEU A 363    11786   9778   8279   1094  -2473    658       C  
ATOM   2049  C   LEU A 363     -33.990  19.506 -11.619  1.00 79.29           C  
ANISOU 2049  C   LEU A 363    11831   9875   8421   1234  -2376    855       C  
ATOM   2050  O   LEU A 363     -34.787  19.766 -10.723  1.00 79.69           O  
ANISOU 2050  O   LEU A 363    11590   9931   8757   1241  -2356    933       O  
ATOM   2051  CB  LEU A 363     -32.010  17.864 -11.589  1.00 77.91           C  
ANISOU 2051  CB  LEU A 363    11889   9675   8038   1052  -2156    569       C  
ATOM   2052  CG  LEU A 363     -31.400  17.755 -10.171  1.00 78.15           C  
ANISOU 2052  CG  LEU A 363    11744   9668   8283    947  -1866    559       C  
ATOM   2053  CD1 LEU A 363     -30.973  19.074  -9.651  1.00 78.44           C  
ANISOU 2053  CD1 LEU A 363    11799   9692   8314    985  -1581    688       C  
ATOM   2054  CD2 LEU A 363     -32.267  16.990  -9.206  1.00 78.38           C  
ANISOU 2054  CD2 LEU A 363    11469   9672   8640    838  -1977    554       C  
ATOM   2055  N   ILE A 364     -33.573  20.432 -12.502  1.00 79.27           N  
ANISOU 2055  N   ILE A 364    12116   9865   8138   1357  -2334    943       N  
ATOM   2056  CA  ILE A 364     -33.933  21.848 -12.380  1.00 80.16           C  
ANISOU 2056  CA  ILE A 364    12248   9923   8286   1504  -2254   1134       C  
ATOM   2057  C   ILE A 364     -35.430  22.087 -12.626  1.00 80.41           C  
ANISOU 2057  C   ILE A 364    12073  10005   8473   1646  -2576   1226       C  
ATOM   2058  O   ILE A 364     -36.045  22.919 -11.960  1.00 80.63           O  
ANISOU 2058  O   ILE A 364    11929   9999   8709   1765  -2509   1340       O  
ATOM   2059  CB  ILE A 364     -33.006  22.726 -13.265  1.00 81.41           C  
ANISOU 2059  CB  ILE A 364    12796  10038   8097   1565  -2116   1233       C  
ATOM   2060  CG1 ILE A 364     -31.631  22.887 -12.582  1.00 83.56           C  
ANISOU 2060  CG1 ILE A 364    13147  10259   8344   1429  -1726   1205       C  
ATOM   2061  CG2 ILE A 364     -33.589  24.102 -13.545  1.00 81.55           C  
ANISOU 2061  CG2 ILE A 364    12917   9971   8096   1753  -2177   1444       C  
ATOM   2062  CD1 ILE A 364     -30.492  21.857 -12.999  1.00 85.12           C  
ANISOU 2062  CD1 ILE A 364    13410  10550   8380   1299  -1624   1030       C  
ATOM   2063  N   ASN A 365     -36.030  21.305 -13.512  1.00 80.25           N  
ANISOU 2063  N   ASN A 365    12048  10074   8369   1636  -2933   1162       N  
ATOM   2064  CA  ASN A 365     -37.460  21.407 -13.775  1.00 80.46           C  
ANISOU 2064  CA  ASN A 365    11828  10188   8556   1745  -3283   1244       C  
ATOM   2065  C   ASN A 365     -38.335  20.670 -12.767  1.00 80.46           C  
ANISOU 2065  C   ASN A 365    11362  10259   8950   1624  -3350   1206       C  
ATOM   2066  O   ASN A 365     -39.493  20.415 -13.052  1.00 80.29           O  
ANISOU 2066  O   ASN A 365    11085  10350   9073   1648  -3684   1244       O  
ATOM   2067  CB  ASN A 365     -37.756  20.952 -15.179  1.00 81.79           C  
ANISOU 2067  CB  ASN A 365    12199  10428   8451   1774  -3673   1198       C  
ATOM   2068  CG  ASN A 365     -37.151  21.894 -16.169  1.00 85.61           C  
ANISOU 2068  CG  ASN A 365    13102  10872   8555   1939  -3619   1313       C  
ATOM   2069  OD1 ASN A 365     -36.244  21.534 -16.921  1.00 87.72           O  
ANISOU 2069  OD1 ASN A 365    13710  11139   8480   1891  -3559   1228       O  
ATOM   2070  ND2 ASN A 365     -37.612  23.140 -16.160  1.00 85.74           N  
ANISOU 2070  ND2 ASN A 365    13109  10849   8621   2147  -3613   1519       N  
ATOM   2071  N   LYS A 366     -37.778  20.310 -11.605  1.00 80.90           N  
ANISOU 2071  N   LYS A 366    11299  10267   9173   1483  -3042   1144       N  
ATOM   2072  CA  LYS A 366     -38.434  19.599 -10.507  1.00 81.52           C  
ANISOU 2072  CA  LYS A 366    10965  10408   9601   1341  -3021   1131       C  
ATOM   2073  C   LYS A 366     -39.270  18.396 -10.994  1.00 82.91           C  
ANISOU 2073  C   LYS A 366    10952  10664   9887   1172  -3422   1065       C  
ATOM   2074  O   LYS A 366     -40.325  18.090 -10.448  1.00 83.32           O  
ANISOU 2074  O   LYS A 366    10590  10826  10241   1102  -3535   1134       O  
ATOM   2075  CB  LYS A 366     -39.233  20.568  -9.620  1.00 81.60           C  
ANISOU 2075  CB  LYS A 366    10675  10480   9850   1514  -2870   1282       C  
ATOM   2076  CG  LYS A 366     -38.342  21.622  -8.947  1.00 82.73           C  
ANISOU 2076  CG  LYS A 366    11024  10497   9914   1622  -2472   1308       C  
ATOM   2077  CD  LYS A 366     -39.116  22.524  -7.989  1.00 84.85           C  
ANISOU 2077  CD  LYS A 366    11028  10805  10408   1817  -2307   1417       C  
ATOM   2078  CE  LYS A 366     -38.269  23.629  -7.411  1.00 87.95           C  
ANISOU 2078  CE  LYS A 366    11687  11029  10700   1927  -1972   1427       C  
ATOM   2079  NZ  LYS A 366     -38.371  23.705  -5.926  1.00 91.03           N  
ANISOU 2079  NZ  LYS A 366    11856  11444  11288   1935  -1683   1409       N  
ATOM   2080  N   LYS A 367     -38.785  17.717 -12.028  1.00 83.46           N  
ANISOU 2080  N   LYS A 367    11330  10680   9702   1102  -3636    928       N  
ATOM   2081  CA  LYS A 367     -39.445  16.526 -12.564  1.00 84.42           C  
ANISOU 2081  CA  LYS A 367    11362  10823   9891    917  -4047    824       C  
ATOM   2082  C   LYS A 367     -38.976  15.234 -11.880  1.00 85.19           C  
ANISOU 2082  C   LYS A 367    11440  10808  10123    657  -3967    688       C  
ATOM   2083  O   LYS A 367     -39.488  14.166 -12.194  1.00 85.36           O  
ANISOU 2083  O   LYS A 367    11399  10796  10239    462  -4298    597       O  
ATOM   2084  CB  LYS A 367     -39.253  16.432 -14.086  1.00 86.37           C  
ANISOU 2084  CB  LYS A 367    11992  11060   9764    999  -4360    723       C  
ATOM   2085  CG  LYS A 367     -40.169  17.348 -14.890  1.00 90.73           C  
ANISOU 2085  CG  LYS A 367    12490  11740  10242   1206  -4630    869       C  
ATOM   2086  CD  LYS A 367     -39.726  17.395 -16.353  1.00 96.61           C  
ANISOU 2086  CD  LYS A 367    13699  12476  10533   1310  -4866    780       C  
ATOM   2087  CE  LYS A 367     -40.883  17.469 -17.322  1.00101.68           C  
ANISOU 2087  CE  LYS A 367    14250  13246  11139   1375  -5391    827       C  
ATOM   2088  NZ  LYS A 367     -41.687  16.208 -17.338  1.00104.88           N  
ANISOU 2088  NZ  LYS A 367    14411  13669  11772   1107  -5785    694       N  
ATOM   2089  N   ILE A 368     -37.996  15.327 -10.968  1.00 85.67           N  
ANISOU 2089  N   ILE A 368    11571  10795  10187    651  -3555    677       N  
ATOM   2090  CA  ILE A 368     -37.478  14.212 -10.201  1.00 86.83           C  
ANISOU 2090  CA  ILE A 368    11706  10828  10457    447  -3443    580       C  
ATOM   2091  C   ILE A 368     -38.141  14.288  -8.824  1.00 87.43           C  
ANISOU 2091  C   ILE A 368    11356  10975  10887    349  -3267    735       C  
ATOM   2092  O   ILE A 368     -38.123  15.337  -8.177  1.00 87.55           O  
ANISOU 2092  O   ILE A 368    11256  11068  10940    496  -2986    853       O  
ATOM   2093  CB  ILE A 368     -35.931  14.314 -10.101  1.00 87.79           C  
ANISOU 2093  CB  ILE A 368    12155  10862  10338    527  -3109    483       C  
ATOM   2094  CG1 ILE A 368     -35.280  14.201 -11.498  1.00 89.08           C  
ANISOU 2094  CG1 ILE A 368    12729  10999  10118    644  -3240    341       C  
ATOM   2095  CG2 ILE A 368     -35.364  13.279  -9.123  1.00 88.10           C  
ANISOU 2095  CG2 ILE A 368    12160  10789  10524    357  -2974    412       C  
ATOM   2096  CD1 ILE A 368     -33.751  14.316 -11.507  1.00 90.55           C  
ANISOU 2096  CD1 ILE A 368    13194  11147  10063    723  -2911    252       C  
ATOM   2097  N   THR A 369     -38.777  13.200  -8.408  1.00 87.54           N  
ANISOU 2097  N   THR A 369    11150  10961  11151    100  -3439    740       N  
ATOM   2098  CA  THR A 369     -39.458  13.142  -7.123  1.00 88.01           C  
ANISOU 2098  CA  THR A 369    10794  11116  11531    -19  -3268    904       C  
ATOM   2099  C   THR A 369     -38.443  13.151  -6.004  1.00 87.67           C  
ANISOU 2099  C   THR A 369    10844  11004  11462    -13  -2859    903       C  
ATOM   2100  O   THR A 369     -37.489  12.375  -6.030  1.00 87.53           O  
ANISOU 2100  O   THR A 369    11101  10822  11332    -88  -2831    775       O  
ATOM   2101  CB  THR A 369     -40.287  11.855  -7.052  1.00 90.10           C  
ANISOU 2101  CB  THR A 369    10843  11340  12049   -340  -3577    920       C  
ATOM   2102  OG1 THR A 369     -41.176  11.803  -8.184  1.00 91.74           O  
ANISOU 2102  OG1 THR A 369    10981  11614  12260   -359  -4011    898       O  
ATOM   2103  CG2 THR A 369     -41.048  11.711  -5.724  1.00 90.22           C  
ANISOU 2103  CG2 THR A 369    10403  11484  12391   -499  -3387   1122       C  
ATOM   2104  N   PRO A 370     -38.624  14.027  -5.010  1.00 87.40           N  
ANISOU 2104  N   PRO A 370    10592  11096  11519     97  -2548   1036       N  
ATOM   2105  CA  PRO A 370     -37.690  14.052  -3.880  1.00 87.56           C  
ANISOU 2105  CA  PRO A 370    10698  11066  11505     93  -2184   1033       C  
ATOM   2106  C   PRO A 370     -37.713  12.740  -3.106  1.00 88.32           C  
ANISOU 2106  C   PRO A 370    10700  11089  11770   -175  -2197   1061       C  
ATOM   2107  O   PRO A 370     -38.765  12.124  -2.979  1.00 88.23           O  
ANISOU 2107  O   PRO A 370    10397  11135  11990   -361  -2370   1165       O  
ATOM   2108  CB  PRO A 370     -38.199  15.219  -3.028  1.00 87.98           C  
ANISOU 2108  CB  PRO A 370    10509  11282  11639    264  -1915   1166       C  
ATOM   2109  CG  PRO A 370     -39.061  16.015  -3.931  1.00 88.36           C  
ANISOU 2109  CG  PRO A 370    10450  11429  11695    435  -2113   1212       C  
ATOM   2110  CD  PRO A 370     -39.695  15.019  -4.842  1.00 86.72           C  
ANISOU 2110  CD  PRO A 370    10177  11208  11567    250  -2522   1184       C  
ATOM   2111  N   PRO A 371     -36.556  12.281  -2.602  1.00 89.21           N  
ANISOU 2111  N   PRO A 371    11049  11071  11776   -207  -2030    984       N  
ATOM   2112  CA  PRO A 371     -36.513  11.001  -1.875  1.00 90.43           C  
ANISOU 2112  CA  PRO A 371    11165  11116  12078   -448  -2056   1026       C  
ATOM   2113  C   PRO A 371     -37.216  10.986  -0.520  1.00 92.09           C  
ANISOU 2113  C   PRO A 371    11038  11466  12488   -559  -1842   1232       C  
ATOM   2114  O   PRO A 371     -37.319   9.926   0.094  1.00 92.05           O  
ANISOU 2114  O   PRO A 371    10987  11373  12615   -783  -1869   1312       O  
ATOM   2115  CB  PRO A 371     -35.016  10.760  -1.698  1.00 90.75           C  
ANISOU 2115  CB  PRO A 371    11544  11018  11921   -370  -1910    895       C  
ATOM   2116  CG  PRO A 371     -34.441  12.125  -1.661  1.00 90.79           C  
ANISOU 2116  CG  PRO A 371    11619  11134  11745   -139  -1664    866       C  
ATOM   2117  CD  PRO A 371     -35.220  12.887  -2.678  1.00 88.83           C  
ANISOU 2117  CD  PRO A 371    11305  10970  11476    -33  -1823    870       C  
ATOM   2118  N   PHE A 372     -37.706  12.146  -0.064  1.00 93.32           N  
ANISOU 2118  N   PHE A 372    10978  11828  12654   -393  -1630   1321       N  
ATOM   2119  CA  PHE A 372     -38.391  12.271   1.202  1.00 95.15           C  
ANISOU 2119  CA  PHE A 372    10890  12235  13028   -443  -1385   1504       C  
ATOM   2120  C   PHE A 372     -39.330  13.482   1.163  1.00 96.95           C  
ANISOU 2120  C   PHE A 372    10841  12689  13306   -229  -1292   1575       C  
ATOM   2121  O   PHE A 372     -38.926  14.545   0.694  1.00 96.73           O  
ANISOU 2121  O   PHE A 372    10988  12648  13119     22  -1240   1476       O  
ATOM   2122  CB  PHE A 372     -37.337  12.417   2.323  1.00 95.30           C  
ANISOU 2122  CB  PHE A 372    11099  12218  12891   -383  -1068   1485       C  
ATOM   2123  CG  PHE A 372     -37.843  12.932   3.648  1.00 96.36           C  
ANISOU 2123  CG  PHE A 372    10992  12558  13061   -331   -743   1632       C  
ATOM   2124  CD1 PHE A 372     -38.429  12.076   4.564  1.00 97.37           C  
ANISOU 2124  CD1 PHE A 372    10901  12763  13334   -552   -666   1817       C  
ATOM   2125  CD2 PHE A 372     -37.742  14.273   3.973  1.00 97.40           C  
ANISOU 2125  CD2 PHE A 372    11139  12798  13068    -59   -511   1586       C  
ATOM   2126  CE1 PHE A 372     -38.921  12.556   5.772  1.00 98.26           C  
ANISOU 2126  CE1 PHE A 372    10794  13100  13441   -483   -341   1954       C  
ATOM   2127  CE2 PHE A 372     -38.246  14.751   5.174  1.00 98.26           C  
ANISOU 2127  CE2 PHE A 372    11050  13103  13184     24   -209   1694       C  
ATOM   2128  CZ  PHE A 372     -38.824  13.890   6.071  1.00 98.11           C  
ANISOU 2128  CZ  PHE A 372    10800  13198  13281   -179   -113   1876       C  
ATOM   2129  N   ASN A 373     -40.571  13.333   1.668  1.00 98.55           N  
ANISOU 2129  N   ASN A 373    10609  13102  13733   -320  -1261   1758       N  
ATOM   2130  CA  ASN A 373     -41.479  14.471   1.775  1.00100.71           C  
ANISOU 2130  CA  ASN A 373    10585  13617  14065    -67  -1136   1832       C  
ATOM   2131  C   ASN A 373     -41.615  14.817   3.254  1.00103.19           C  
ANISOU 2131  C   ASN A 373    10732  14104  14372      6   -725   1941       C  
ATOM   2132  O   ASN A 373     -42.061  13.980   4.050  1.00103.21           O  
ANISOU 2132  O   ASN A 373    10495  14211  14510   -229   -638   2102       O  
ATOM   2133  CB  ASN A 373     -42.865  14.204   1.172  1.00101.69           C  
ANISOU 2133  CB  ASN A 373    10277  13918  14443   -163  -1406   1956       C  
ATOM   2134  CG  ASN A 373     -43.889  15.277   1.533  1.00104.88           C  
ANISOU 2134  CG  ASN A 373    10281  14623  14945    112  -1220   2071       C  
ATOM   2135  OD1 ASN A 373     -43.836  16.416   1.054  1.00106.04           O  
ANISOU 2135  OD1 ASN A 373    10544  14772  14975    456  -1178   1991       O  
ATOM   2136  ND2 ASN A 373     -44.809  14.954   2.435  1.00105.52           N  
ANISOU 2136  ND2 ASN A 373     9897  14960  15236    -21  -1078   2269       N  
ATOM   2137  N   PRO A 374     -41.292  16.069   3.622  1.00104.85           N  
ANISOU 2137  N   PRO A 374    11072  14346  14419    331   -475   1863       N  
ATOM   2138  CA  PRO A 374     -41.466  16.479   5.022  1.00106.37           C  
ANISOU 2138  CA  PRO A 374    11137  14714  14566    442    -84   1938       C  
ATOM   2139  C   PRO A 374     -42.954  16.675   5.383  1.00108.61           C  
ANISOU 2139  C   PRO A 374    10879  15331  15057    522     21   2120       C  
ATOM   2140  O   PRO A 374     -43.682  17.405   4.699  1.00108.72           O  
ANISOU 2140  O   PRO A 374    10697  15442  15168    732   -103   2122       O  
ATOM   2141  CB  PRO A 374     -40.634  17.773   5.128  1.00106.54           C  
ANISOU 2141  CB  PRO A 374    11514  14614  14351    758     83   1764       C  
ATOM   2142  CG  PRO A 374     -40.006  17.987   3.761  1.00106.40           C  
ANISOU 2142  CG  PRO A 374    11801  14363  14262    772   -206   1629       C  
ATOM   2143  CD  PRO A 374     -40.785  17.174   2.790  1.00104.46           C  
ANISOU 2143  CD  PRO A 374    11317  14163  14211    603   -539   1709       C  
ATOM   2144  N   ASN A 375     -43.416  15.980   6.440  1.00110.05           N  
ANISOU 2144  N   ASN A 375    10802  15705  15307    351    246   2291       N  
ATOM   2145  CA  ASN A 375     -44.812  16.046   6.896  1.00111.88           C  
ANISOU 2145  CA  ASN A 375    10465  16307  15736    394    398   2494       C  
ATOM   2146  C   ASN A 375     -45.184  17.445   7.408  1.00113.15           C  
ANISOU 2146  C   ASN A 375    10559  16646  15785    870    708   2431       C  
ATOM   2147  O   ASN A 375     -44.833  17.805   8.537  1.00113.49           O  
ANISOU 2147  O   ASN A 375    10737  16748  15634   1000   1062   2405       O  
ATOM   2148  CB  ASN A 375     -45.088  14.984   7.978  1.00113.16           C  
ANISOU 2148  CB  ASN A 375    10415  16622  15960     71    597   2714       C  
ATOM   2149  N   VAL A 376     -45.874  18.240   6.563  1.00113.51           N  
ANISOU 2149  N   VAL A 376    10434  16758  15938   1148    555   2396       N  
ATOM   2150  CA  VAL A 376     -46.285  19.606   6.910  1.00114.09           C  
ANISOU 2150  CA  VAL A 376    10466  16954  15928   1648    801   2323       C  
ATOM   2151  C   VAL A 376     -47.805  19.833   6.696  1.00114.55           C  
ANISOU 2151  C   VAL A 376     9890  17387  16248   1836    786   2487       C  
ATOM   2152  O   VAL A 376     -48.625  19.603   7.597  1.00114.55           O  
ANISOU 2152  O   VAL A 376     9434  17746  16345   1831   1064   2657       O  
ATOM   2153  CB  VAL A 376     -45.432  20.662   6.154  1.00114.57           C  
ANISOU 2153  CB  VAL A 376    11049  16672  15810   1909    660   2096       C  
ATOM   2154  CG1 VAL A 376     -44.018  20.749   6.726  1.00114.73           C  
ANISOU 2154  CG1 VAL A 376    11620  16419  15555   1833    807   1935       C  
ATOM   2155  CG2 VAL A 376     -45.398  20.370   4.658  1.00115.09           C  
ANISOU 2155  CG2 VAL A 376    11173  16575  15980   1767    202   2083       C  
TER    2156      VAL A 376                                                      
HETATM 2157  C1  GOL A 501     -37.743  28.629  -3.359  1.00 99.21           C  
HETATM 2158  O1  GOL A 501     -38.355  29.739  -2.746  1.00 98.88           O  
HETATM 2159  C2  GOL A 501     -38.443  28.343  -4.682  1.00 99.67           C  
HETATM 2160  O2  GOL A 501     -38.733  26.965  -4.760  1.00 99.60           O  
HETATM 2161  C3  GOL A 501     -37.554  28.719  -5.867  1.00100.16           C  
HETATM 2162  O3  GOL A 501     -36.859  29.935  -5.656  1.00100.41           O  
HETATM 2163  C1  GOL A 502      -9.107  20.839 -11.196  1.00 97.19           C  
HETATM 2164  O1  GOL A 502     -10.364  20.882 -11.829  1.00 97.03           O  
HETATM 2165  C2  GOL A 502      -8.324  19.627 -11.687  1.00 97.44           C  
HETATM 2166  O2  GOL A 502      -8.864  18.449 -11.123  1.00 97.21           O  
HETATM 2167  C3  GOL A 502      -6.847  19.774 -11.305  1.00 97.80           C  
HETATM 2168  O3  GOL A 502      -6.293  20.982 -11.800  1.00 97.91           O  
HETATM 2169  C4  86H A 503     -34.946  31.237   6.603  1.00 75.15           C  
HETATM 2170  C5  86H A 503     -36.126  31.109   5.887  1.00 74.87           C  
HETATM 2171  C6  86H A 503     -36.291  31.821   4.721  1.00 75.03           C  
HETATM 2172  C1  86H A 503     -34.027  32.206   6.185  1.00 75.37           C  
HETATM 2173  C2  86H A 503     -34.279  32.995   5.052  1.00 75.61           C  
HETATM 2174  C35 86H A 503     -31.943  30.579  10.385  1.00 75.99           C  
HETATM 2175  C34 86H A 503     -30.808  29.583  10.192  1.00 76.02           C  
HETATM 2176  N33 86H A 503     -31.489  28.275  10.221  1.00 76.17           N  
HETATM 2177  C32 86H A 503     -32.690  28.466   9.396  1.00 76.03           C  
HETATM 2178  C31 86H A 503     -33.161  29.891   9.732  1.00 76.04           C  
HETATM 2179  N30 86H A 503     -33.545  30.598   8.487  1.00 75.81           N  
HETATM 2180  C10 86H A 503     -34.740  30.441   7.912  1.00 75.16           C  
HETATM 2181  O11 86H A 503     -35.646  29.766   8.404  1.00 74.57           O  
HETATM 2182  C9  86H A 503     -37.184  30.317   5.977  1.00 74.76           C  
HETATM 2183  N8  86H A 503     -37.983  30.591   4.950  1.00 74.88           N  
HETATM 2184  N7  86H A 503     -37.457  31.430   4.212  1.00 75.05           N  
HETATM 2185  N3  86H A 503     -35.365  32.706   4.312  1.00 75.24           N  
HETATM 2186  C12 86H A 503     -33.283  33.823   4.516  1.00 76.41           C  
HETATM 2187  C17 86H A 503     -33.423  34.412   3.253  1.00 77.27           C  
HETATM 2188  C16 86H A 503     -32.421  35.207   2.688  1.00 77.94           C  
HETATM 2189  C13 86H A 503     -32.041  33.875   5.118  1.00 76.68           C  
HETATM 2190  C14 86H A 503     -31.019  34.589   4.531  1.00 77.41           C  
HETATM 2191  C15 86H A 503     -31.181  35.214   3.303  1.00 78.59           C  
HETATM 2192  N18 86H A 503     -30.074  35.703   2.773  1.00 80.42           N  
HETATM 2193  S19 86H A 503     -29.695  36.432   1.354  1.00 82.20           S  
HETATM 2194  O20 86H A 503     -28.593  37.449   1.484  1.00 82.44           O  
HETATM 2195  O21 86H A 503     -29.004  35.321   0.661  1.00 82.30           O  
HETATM 2196  C22 86H A 503     -30.895  36.806   0.139  1.00 83.90           C  
HETATM 2197  C27 86H A 503     -31.333  35.870  -0.786  1.00 84.02           C  
HETATM 2198  C26 86H A 503     -32.266  36.235  -1.756  1.00 84.23           C  
HETATM 2199  C25 86H A 503     -32.754  37.540  -1.809  1.00 84.81           C  
HETATM 2200  C24 86H A 503     -32.319  38.486  -0.877  1.00 85.58           C  
HETATM 2201 CL1  86H A 503     -32.867  40.143  -0.837  1.00 86.24          CL  
HETATM 2202  C23 86H A 503     -31.422  38.115   0.109  1.00 85.45           C  
HETATM 2203 CL2  86H A 503     -30.942  39.410   1.183  1.00 86.45          CL  
HETATM 2204  O   HOH A 601     -29.694  21.834   6.869  1.00 84.05           O  
HETATM 2205  O   HOH A 602     -22.751  12.953 -14.291  1.00 47.07           O  
HETATM 2206  O   HOH A 603     -25.579  13.130 -15.150  1.00 69.58           O  
HETATM 2207  O   HOH A 604     -14.669   9.221   6.912  1.00 76.53           O  
HETATM 2208  O   HOH A 605     -36.343  14.944  -0.069  1.00 63.42           O  
HETATM 2209  O   HOH A 606     -15.394  26.269  15.195  1.00 63.27           O  
HETATM 2210  O   HOH A 607     -41.375  51.345   0.906  1.00 78.14           O  
HETATM 2211  O   HOH A 608     -26.886  36.683   3.535  1.00 79.14           O  
HETATM 2212  O   HOH A 609      -8.924   9.358   0.812  1.00 80.94           O  
HETATM 2213  O   HOH A 610      -8.390  17.644   2.566  1.00 58.27           O  
HETATM 2214  O   HOH A 611      -8.770  23.120  21.959  1.00 59.16           O  
HETATM 2215  O   HOH A 612     -35.731  17.788  -8.961  1.00 64.73           O  
HETATM 2216  O   HOH A 613     -31.612   7.018   5.870  1.00 49.79           O  
HETATM 2217  O   HOH A 614     -35.026  31.968  -6.545  1.00 72.72           O  
HETATM 2218  O   HOH A 615     -14.293  14.028  18.870  1.00 49.40           O  
HETATM 2219  O   HOH A 616     -28.146  15.464 -17.775  1.00 73.50           O  
HETATM 2220  O   HOH A 617      -4.686  18.612  -1.122  1.00 98.76           O  
HETATM 2221  O   HOH A 618      -1.562  35.162  -0.582  1.00 90.48           O  
HETATM 2222  O   HOH A 619      -8.896   7.722   3.641  1.00 95.30           O  
HETATM 2223  O   HOH A 620     -26.082   3.931   0.511  1.00 65.85           O  
HETATM 2224  O   HOH A 621     -15.588  10.595 -12.865  1.00 61.07           O  
HETATM 2225  O   HOH A 622     -30.595   9.651  -7.155  1.00 65.27           O  
HETATM 2226  O   HOH A 623     -44.528  31.895   0.138  1.00 69.84           O  
HETATM 2227  O   HOH A 624     -11.326   6.389  -5.667  1.00 61.17           O  
CONECT 2157 2158 2159                                                           
CONECT 2158 2157                                                                
CONECT 2159 2157 2160 2161                                                      
CONECT 2160 2159                                                                
CONECT 2161 2159 2162                                                           
CONECT 2162 2161                                                                
CONECT 2163 2164 2165                                                           
CONECT 2164 2163                                                                
CONECT 2165 2163 2166 2167                                                      
CONECT 2166 2165                                                                
CONECT 2167 2165 2168                                                           
CONECT 2168 2167                                                                
CONECT 2169 2170 2172 2180                                                      
CONECT 2170 2169 2171 2182                                                      
CONECT 2171 2170 2184 2185                                                      
CONECT 2172 2169 2173                                                           
CONECT 2173 2172 2185 2186                                                      
CONECT 2174 2175 2178                                                           
CONECT 2175 2174 2176                                                           
CONECT 2176 2175 2177                                                           
CONECT 2177 2176 2178                                                           
CONECT 2178 2174 2177 2179                                                      
CONECT 2179 2178 2180                                                           
CONECT 2180 2169 2179 2181                                                      
CONECT 2181 2180                                                                
CONECT 2182 2170 2183                                                           
CONECT 2183 2182 2184                                                           
CONECT 2184 2171 2183                                                           
CONECT 2185 2171 2173                                                           
CONECT 2186 2173 2187 2189                                                      
CONECT 2187 2186 2188                                                           
CONECT 2188 2187 2191                                                           
CONECT 2189 2186 2190                                                           
CONECT 2190 2189 2191                                                           
CONECT 2191 2188 2190 2192                                                      
CONECT 2192 2191 2193                                                           
CONECT 2193 2192 2194 2195 2196                                                 
CONECT 2194 2193                                                                
CONECT 2195 2193                                                                
CONECT 2196 2193 2197 2202                                                      
CONECT 2197 2196 2198                                                           
CONECT 2198 2197 2199                                                           
CONECT 2199 2198 2200                                                           
CONECT 2200 2199 2201 2202                                                      
CONECT 2201 2200                                                                
CONECT 2202 2196 2200 2203                                                      
CONECT 2203 2202                                                                
MASTER      436    0    3   11    7    0    0    6 2226    1   47   29          
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.