CNRS Nantes University UFIP UFIP
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***  DOR Analysis   ***

elNémo ID: 20020923542496911

Job options:

ID        	=	 20020923542496911
JOBID     	=	 DOR Analysis 
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 DOR Analysis 

HEADER    MEMBRANE PROTEIN/AGONIST                14-JUL-19   6PT2              
TITLE     CRYSTAL STRUCTURE OF THE ACTIVE DELTA OPIOID RECEPTOR IN COMPLEX WITH 
TITLE    2 THE PEPTIDE AGONIST KGCHM07                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DELTA OPIOID RECEPTOR;                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: PEPTIDE AGONIST KGCHM07;                                   
COMPND   7 CHAIN: C, D;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  11 ORGANISM_TAXID: 32630                                                
KEYWDS    MEMBRANE PROTEIN, G PROTEIN-COUPLED RECEPTOR, GPCR, DOP, DOR, PEPTIDE 
KEYWDS   2 AGONIST, ACTIVE DOP-KGCHM07 STRUCTURE, LCP, MEMBRANE PROTEIN-AGONIST 
KEYWDS   3 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.CLAFF,J.YU,V.BLAIS,N.PATEL,C.MARTIN,L.WU,G.W.HAN,B.J.HOLLERAN,O.VAN 
AUTHOR   2 DER POORTEN,M.A.HANSON,P.SARRET,L.GENDRON,V.CHEREZOV,V.KATRITCH,     
AUTHOR   3 S.BALLET,Z.LIU,C.E.MULLER,R.C.STEVENS                                
REVDAT   2   18-DEC-19 6PT2    1       JRNL                                     
REVDAT   1   11-DEC-19 6PT2    0                                                
JRNL        AUTH   T.CLAFF,J.YU,V.BLAIS,N.PATEL,C.MARTIN,L.WU,G.W.HAN,          
JRNL        AUTH 2 B.J.HOLLERAN,O.VAN DER POORTEN,K.L.WHITE,M.A.HANSON,         
JRNL        AUTH 3 P.SARRET,L.GENDRON,V.CHEREZOV,V.KATRITCH,S.BALLET,Z.J.LIU,   
JRNL        AUTH 4 C.E.MULLER,R.C.STEVENS                                       
JRNL        TITL   ELUCIDATING THE ACTIVE DELTA-OPIOID RECEPTOR CRYSTAL         
JRNL        TITL 2 STRUCTURE WITH PEPTIDE AND SMALL-MOLECULE AGONISTS.          
JRNL        REF    SCI ADV                       V.   5 X9115 2019              
JRNL        REFN                   ESSN 2375-2548                               
JRNL        PMID   31807708                                                     
JRNL        DOI    10.1126/SCIADV.AAX9115                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.3                                        
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.51                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 26050                          
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)  : 0.247                          
REMARK   3   R VALUE            (WORKING SET)  : 0.246                          
REMARK   3   FREE R VALUE                      : 0.282                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.870                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1269                           
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               : 13                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.80                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.91                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 78.83                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2461                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2421                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2342                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2397                   
REMARK   3   BIN FREE R VALUE                        : 0.2913                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.84                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 119                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5833                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 136                                     
REMARK   3   SOLVENT ATOMS            : 3                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 115.4                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -19.36440                                            
REMARK   3    B22 (A**2) : 19.41710                                             
REMARK   3    B33 (A**2) : -0.05270                                             
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) : 0.470               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 1.117               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.378               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 1.166               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.385               
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      : 0.908                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.927                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6086   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 8290   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2014   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : 970    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6086   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 844    ; 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   : 7169   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.05                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.43                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.09                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|999 - A|1106 A|41 - A|329 }                        
REMARK   3    ORIGIN FOR THE GROUP (A):  -21.4415   36.1495  -30.5762           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0571 T22:   -0.2990                                    
REMARK   3     T33:   -0.3257 T12:    0.0253                                    
REMARK   3     T13:    0.0029 T23:   -0.0742                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8351 L22:    0.7218                                    
REMARK   3     L33:    2.6074 L12:    0.1331                                    
REMARK   3     L13:   -0.1896 L23:   -0.1726                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1301 S12:   -0.0003 S13:    0.0388                     
REMARK   3     S21:   -0.2132 S22:    0.0044 S23:   -0.0211                     
REMARK   3     S31:    0.0913 S32:    0.1446 S33:    0.1258                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|1002 - B|1104 B|1107 - B|1399 }                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -22.6141    6.4206  -40.0551           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1297 T22:   -0.3174                                    
REMARK   3     T33:   -0.3269 T12:    0.0277                                    
REMARK   3     T13:    0.0381 T23:   -0.0271                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.5187 L22:    1.6784                                    
REMARK   3     L33:    2.0434 L12:    0.0022                                    
REMARK   3     L13:    0.3393 L23:   -0.4139                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1879 S12:   -0.0552 S13:   -0.0197                     
REMARK   3     S21:   -0.0467 S22:    0.1469 S23:   -0.2479                     
REMARK   3     S31:   -0.2212 S32:   -0.0348 S33:    0.0410                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THERE ARE SOME UNKNOWN DENSITIES          
REMARK   3  LOCATED NEAR THE TWO FOLD OF THE MOLECULE CLOSE TO THE SIDE         
REMARK   3  CHAIN OF 152 HIS OF BOTH A AND B CHAINS. THEY HAVE NOT BEEN         
REMARK   3  MODELLED.                                                           
REMARK   4                                                                      
REMARK   4 6PT2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUL-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000243020.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26051                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.510                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.2                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.87                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.80400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4N6H                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 27-32% PEG400, 100-120 MM POTASSIUM      
REMARK 280  CITRATE TRIBASIC MONOHYDRATE AND 100 MM MES PH 6.0, LIPIDIC         
REMARK 280  CUBIC PHASE, TEMPERATURE 293K                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       24.48000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       79.32000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       70.44000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       79.32000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.48000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       70.44000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE AUTHOR STATES THAT THE BIOLOGICAL UNIT OF THIS PROTEIN   
REMARK 300 IS UNKNOWN.                                                          
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8960 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   951                                                      
REMARK 465     LYS A   952                                                      
REMARK 465     THR A   953                                                      
REMARK 465     ILE A   954                                                      
REMARK 465     ILE A   955                                                      
REMARK 465     ALA A   956                                                      
REMARK 465     LEU A   957                                                      
REMARK 465     SER A   958                                                      
REMARK 465     TYR A   959                                                      
REMARK 465     ILE A   960                                                      
REMARK 465     PHE A   961                                                      
REMARK 465     CYS A   962                                                      
REMARK 465     LEU A   963                                                      
REMARK 465     VAL A   964                                                      
REMARK 465     PHE A   965                                                      
REMARK 465     ALA A   966                                                      
REMARK 465     ASP A   967                                                      
REMARK 465     TYR A   968                                                      
REMARK 465     LYS A   969                                                      
REMARK 465     ASP A   970                                                      
REMARK 465     ASP A   971                                                      
REMARK 465     ASP A   972                                                      
REMARK 465     ASP A   973                                                      
REMARK 465     ALA A   974                                                      
REMARK 465     LYS A   975                                                      
REMARK 465     LEU A   976                                                      
REMARK 465     GLN A   977                                                      
REMARK 465     THR A   978                                                      
REMARK 465     MET A   979                                                      
REMARK 465     HIS A   980                                                      
REMARK 465     HIS A   981                                                      
REMARK 465     HIS A   982                                                      
REMARK 465     HIS A   983                                                      
REMARK 465     HIS A   984                                                      
REMARK 465     HIS A   985                                                      
REMARK 465     HIS A   986                                                      
REMARK 465     HIS A   987                                                      
REMARK 465     HIS A   988                                                      
REMARK 465     HIS A   989                                                      
REMARK 465     GLU A   990                                                      
REMARK 465     ASN A   991                                                      
REMARK 465     LEU A   992                                                      
REMARK 465     TYR A   993                                                      
REMARK 465     PHE A   994                                                      
REMARK 465     GLN A   995                                                      
REMARK 465     GLY A   996                                                      
REMARK 465     GLY A   997                                                      
REMARK 465     THR A   998                                                      
REMARK 465     ARG A   330                                                      
REMARK 465     GLN A   331                                                      
REMARK 465     LEU A   332                                                      
REMARK 465     CYS A   333                                                      
REMARK 465     ARG A   334                                                      
REMARK 465     LYS A   335                                                      
REMARK 465     PRO A   336                                                      
REMARK 465     CYS A   337                                                      
REMARK 465     GLY A   338                                                      
REMARK 465     MET B   951                                                      
REMARK 465     LYS B   952                                                      
REMARK 465     THR B   953                                                      
REMARK 465     ILE B   954                                                      
REMARK 465     ILE B   955                                                      
REMARK 465     ALA B   956                                                      
REMARK 465     LEU B   957                                                      
REMARK 465     SER B   958                                                      
REMARK 465     TYR B   959                                                      
REMARK 465     ILE B   960                                                      
REMARK 465     PHE B   961                                                      
REMARK 465     CYS B   962                                                      
REMARK 465     LEU B   963                                                      
REMARK 465     VAL B   964                                                      
REMARK 465     PHE B   965                                                      
REMARK 465     ALA B   966                                                      
REMARK 465     ASP B   967                                                      
REMARK 465     TYR B   968                                                      
REMARK 465     LYS B   969                                                      
REMARK 465     ASP B   970                                                      
REMARK 465     ASP B   971                                                      
REMARK 465     ASP B   972                                                      
REMARK 465     ASP B   973                                                      
REMARK 465     ALA B   974                                                      
REMARK 465     LYS B   975                                                      
REMARK 465     LEU B   976                                                      
REMARK 465     GLN B   977                                                      
REMARK 465     THR B   978                                                      
REMARK 465     MET B   979                                                      
REMARK 465     HIS B   980                                                      
REMARK 465     HIS B   981                                                      
REMARK 465     HIS B   982                                                      
REMARK 465     HIS B   983                                                      
REMARK 465     HIS B   984                                                      
REMARK 465     HIS B   985                                                      
REMARK 465     HIS B   986                                                      
REMARK 465     HIS B   987                                                      
REMARK 465     HIS B   988                                                      
REMARK 465     HIS B   989                                                      
REMARK 465     GLU B   990                                                      
REMARK 465     ASN B   991                                                      
REMARK 465     LEU B   992                                                      
REMARK 465     TYR B   993                                                      
REMARK 465     PHE B   994                                                      
REMARK 465     GLN B   995                                                      
REMARK 465     GLY B   996                                                      
REMARK 465     GLY B   997                                                      
REMARK 465     THR B   998                                                      
REMARK 465     THR B   999                                                      
REMARK 465     MET B  1000                                                      
REMARK 465     ALA B  1001                                                      
REMARK 465     LYS B  1019                                                      
REMARK 465     ALA B  1020                                                      
REMARK 465     ASP B  1021                                                      
REMARK 465     ASN B  1022                                                      
REMARK 465     ALA B  1043                                                      
REMARK 465     THR B  1044                                                      
REMARK 465     PRO B  1045                                                      
REMARK 465     PRO B  1046                                                      
REMARK 465     LYS B  1047                                                      
REMARK 465     LEU B  1048                                                      
REMARK 465     GLU B  1049                                                      
REMARK 465     ASP B  1050                                                      
REMARK 465     LYS B  1051                                                      
REMARK 465     SER B  1052                                                      
REMARK 465     PRO B  1053                                                      
REMARK 465     ASP B  1054                                                      
REMARK 465     SER B  1055                                                      
REMARK 465     PRO B  1056                                                      
REMARK 465     GLU B  1057                                                      
REMARK 465     ALA B  1079                                                      
REMARK 465     ASN B  1080                                                      
REMARK 465     GLU B  1081                                                      
REMARK 465     GLY B  1082                                                      
REMARK 465     LYS B  1083                                                      
REMARK 465     VAL B  1084                                                      
REMARK 465     LYS B  1085                                                      
REMARK 465     GLU B  1086                                                      
REMARK 465     ALA B  1087                                                      
REMARK 465     GLN B  1088                                                      
REMARK 465     ALA B  1089                                                      
REMARK 465     TYR B  1105                                                      
REMARK 465     LEU B  1106                                                      
REMARK 465     LEU B   245                                                      
REMARK 465     LEU B   246                                                      
REMARK 465     SER B   247                                                      
REMARK 465     GLY B   248                                                      
REMARK 465     SER B   249                                                      
REMARK 465     ARG B   334                                                      
REMARK 465     LYS B   335                                                      
REMARK 465     PRO B   336                                                      
REMARK 465     CYS B   337                                                      
REMARK 465     GLY B   338                                                      
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     GLU A1008    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1015    CG   CD   CE   NZ                                   
REMARK 470     GLU A1049    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1059    CG   CD   CE   NZ                                   
REMARK 470     LYS A1085    CG   CD   CE   NZ                                   
REMARK 470     LYS A  79    CG   CD   CE   NZ                                   
REMARK 470     LYS A  81    CG   CD   CE   NZ                                   
REMARK 470     GLU A 251    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 253    CG   OD1  OD2                                       
REMARK 470     ARG A 254    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 327    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B1002    CG   OD1  OD2                                       
REMARK 470     LEU B1003    CG   CD1  CD2                                       
REMARK 470     GLU B1004    CG   CD   OE1  OE2                                  
REMARK 470     GLU B1008    CG   CD   OE1  OE2                                  
REMARK 470     ASP B1012    CG   OD1  OD2                                       
REMARK 470     LYS B1015    CG   CD   CE   NZ                                   
REMARK 470     ILE B1017    CG1  CG2  CD1                                       
REMARK 470     GLU B1018    CG   CD   OE1  OE2                                  
REMARK 470     LYS B1027    CG   CD   CE   NZ                                   
REMARK 470     LYS B1032    CG   CD   CE   NZ                                   
REMARK 470     ARG B1034    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B1038    CG   CD1  CD2                                       
REMARK 470     MET B1058    CG   SD   CE                                        
REMARK 470     LYS B1059    CG   CD   CE   NZ                                   
REMARK 470     ARG B1062    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE B1065    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP B1066    CG   OD1  OD2                                       
REMARK 470     LEU B1068    CG   CD1  CD2                                       
REMARK 470     GLN B1071    CG   CD   OE1  NE2                                  
REMARK 470     LYS B1077    CG   CD   CE   NZ                                   
REMARK 470     LEU B1078    CG   CD1  CD2                                       
REMARK 470     GLU B1092    CG   CD   OE1  OE2                                  
REMARK 470     GLN B1093    CG   CD   OE1  NE2                                  
REMARK 470     LEU B1094    CG   CD1  CD2                                       
REMARK 470     LYS B1095    CG   CD   CE   NZ                                   
REMARK 470     ARG B1098    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B1099    CG   OD1  ND2                                       
REMARK 470     TYR B1101    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE B1102    CG1  CG2  CD1                                       
REMARK 470     GLN B1103    CG   CD   OE1  NE2                                  
REMARK 470     LYS B1104    CG   CD   CE   NZ                                   
REMARK 470     ARG B  41    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  79    CG   CD   CE   NZ                                   
REMARK 470     LYS B  81    CG   CD   CE   NZ                                   
REMARK 470     LYS B 155    CG   CD   CE   NZ                                   
REMARK 470     LYS B 250    CG   CD   CE   NZ                                   
REMARK 470     LYS B 252    CG   CD   CE   NZ                                   
REMARK 470     ARG B 257    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 261    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 291    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG B 292    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 295    CG   CD1  CD2                                       
REMARK 470     ARG B 330    CG   CD   NE   CZ   NH1  NH2                        
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 A1106       58.25   -116.52                                   
REMARK 500    TYR A  77      -64.98   -122.27                                   
REMARK 500    MET A  80       74.17    -67.35                                   
REMARK 500    ARG A 160       40.55    -73.24                                   
REMARK 500    PHE A 222      -60.19   -125.59                                   
REMARK 500    ASP A 290       87.84    -68.14                                   
REMARK 500    TYR B1101      -22.50   -141.53                                   
REMARK 500    SER B  42      -72.72    -56.28                                   
REMARK 500    TYR B  77      -61.02    -95.23                                   
REMARK 500    MET B  80       43.99     34.38                                   
REMARK 500    HIS B 152       75.97   -119.16                                   
REMARK 500    ARG B 160       42.31    -75.42                                   
REMARK 500    PHE B 222      -66.62   -131.04                                   
REMARK 500    ASP B 293      124.63    -37.58                                   
REMARK 500    LEU B 313       51.78   -114.65                                   
REMARK 500    DAR C   2      -22.64    154.84                                   
REMARK 500    DAR D   2      -16.54    141.28                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OLA B 1201                                                       
REMARK 610     OLA B 1202                                                       
REMARK 610     OLA B 1203                                                       
REMARK 610     OLA B 1204                                                       
REMARK 610     OLA B 1205                                                       
REMARK 610     OLC B 1206                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 1205                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC B 1206                
DBREF  6PT2 A  951   338  PDB    6PT2     6PT2           951    338             
DBREF  6PT2 B  951   338  PDB    6PT2     6PT2           951    338             
DBREF  6PT2 C    1     5  PDB    6PT2     6PT2             1      5             
DBREF  6PT2 D    1     5  PDB    6PT2     6PT2             1      5             
SEQRES   1 A  454  MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU          
SEQRES   2 A  454  VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP ALA LYS LEU          
SEQRES   3 A  454  GLN THR MET HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS          
SEQRES   4 A  454  GLU ASN LEU TYR PHE GLN GLY GLY THR THR MET ALA ASP          
SEQRES   5 A  454  LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS          
SEQRES   6 A  454  VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP          
SEQRES   7 A  454  ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN          
SEQRES   8 A  454  LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP          
SEQRES   9 A  454  SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE          
SEQRES  10 A  454  LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN          
SEQRES  11 A  454  GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN          
SEQRES  12 A  454  LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU          
SEQRES  13 A  454  ARG SER ALA SER SER LEU ALA LEU ALA ILE ALA ILE THR          
SEQRES  14 A  454  ALA LEU TYR SER ALA VAL CYS ALA VAL GLY LEU LEU GLY          
SEQRES  15 A  454  ASN VAL LEU VAL MET PHE VAL ILE VAL ARG TYR THR LYS          
SEQRES  16 A  454  MET LYS THR ALA THR ASN ILE TYR ILE PHE SER LEU ALA          
SEQRES  17 A  454  LEU ALA GLY ALA LEU ALA THR SER THR LEU PRO PHE GLN          
SEQRES  18 A  454  SER ALA ASP TYR LEU MET GLU THR TRP PRO PHE GLY GLU          
SEQRES  19 A  454  LEU LEU CYS LYS ALA VAL LEU SER ILE ASP TYR TYR SER          
SEQRES  20 A  454  MET PHE THR SER ILE PHE THR LEU THR MET MET CYS VAL          
SEQRES  21 A  454  ASP ARG TYR ILE ALA VAL CYS HIS PRO VAL LYS ALA LEU          
SEQRES  22 A  454  ASP PHE ARG THR PRO ALA LYS ALA LYS LEU ILE ASN ILE          
SEQRES  23 A  454  CYS ILE TRP VAL LEU ALA SER GLY VAL GLY VAL PRO ILE          
SEQRES  24 A  454  MET VAL MET ALA VAL THR ARG PRO ARG ASP GLY ALA VAL          
SEQRES  25 A  454  VAL CYS MET LEU GLN PHE PRO SER PRO SER TRP TYR TRP          
SEQRES  26 A  454  ASP THR VAL THR LYS ILE CYS VAL PHE LEU PHE ALA PHE          
SEQRES  27 A  454  VAL VAL PRO ILE LEU ILE ILE THR VAL CYS TYR GLY LEU          
SEQRES  28 A  454  MET LEU LEU ARG LEU ARG SER VAL ARG LEU LEU SER GLY          
SEQRES  29 A  454  SER LYS GLU LYS ASP ARG SER LEU ARG ARG ILE THR ARG          
SEQRES  30 A  454  MET VAL LEU VAL VAL VAL VAL ALA PHE VAL VAL CYS TRP          
SEQRES  31 A  454  ALA PRO ILE HIS ILE PHE VAL ILE VAL TRP THR LEU VAL          
SEQRES  32 A  454  ASP ILE ASP ARG ARG ASP PRO LEU VAL VAL ALA ALA LEU          
SEQRES  33 A  454  HIS LEU CYS ILE ALA LEU GLY TYR ILE ASN SER SER LEU          
SEQRES  34 A  454  ASN PRO VAL LEU TYR ALA PHE LEU ASP LYS ASN PHE LYS          
SEQRES  35 A  454  ARG CYS PHE ARG GLN LEU CYS ARG LYS PRO CYS GLY              
SEQRES   1 B  454  MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU          
SEQRES   2 B  454  VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP ALA LYS LEU          
SEQRES   3 B  454  GLN THR MET HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS          
SEQRES   4 B  454  GLU ASN LEU TYR PHE GLN GLY GLY THR THR MET ALA ASP          
SEQRES   5 B  454  LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS          
SEQRES   6 B  454  VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP          
SEQRES   7 B  454  ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN          
SEQRES   8 B  454  LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP          
SEQRES   9 B  454  SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE          
SEQRES  10 B  454  LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN          
SEQRES  11 B  454  GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN          
SEQRES  12 B  454  LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU          
SEQRES  13 B  454  ARG SER ALA SER SER LEU ALA LEU ALA ILE ALA ILE THR          
SEQRES  14 B  454  ALA LEU TYR SER ALA VAL CYS ALA VAL GLY LEU LEU GLY          
SEQRES  15 B  454  ASN VAL LEU VAL MET PHE VAL ILE VAL ARG TYR THR LYS          
SEQRES  16 B  454  MET LYS THR ALA THR ASN ILE TYR ILE PHE SER LEU ALA          
SEQRES  17 B  454  LEU ALA GLY ALA LEU ALA THR SER THR LEU PRO PHE GLN          
SEQRES  18 B  454  SER ALA ASP TYR LEU MET GLU THR TRP PRO PHE GLY GLU          
SEQRES  19 B  454  LEU LEU CYS LYS ALA VAL LEU SER ILE ASP TYR TYR SER          
SEQRES  20 B  454  MET PHE THR SER ILE PHE THR LEU THR MET MET CYS VAL          
SEQRES  21 B  454  ASP ARG TYR ILE ALA VAL CYS HIS PRO VAL LYS ALA LEU          
SEQRES  22 B  454  ASP PHE ARG THR PRO ALA LYS ALA LYS LEU ILE ASN ILE          
SEQRES  23 B  454  CYS ILE TRP VAL LEU ALA SER GLY VAL GLY VAL PRO ILE          
SEQRES  24 B  454  MET VAL MET ALA VAL THR ARG PRO ARG ASP GLY ALA VAL          
SEQRES  25 B  454  VAL CYS MET LEU GLN PHE PRO SER PRO SER TRP TYR TRP          
SEQRES  26 B  454  ASP THR VAL THR LYS ILE CYS VAL PHE LEU PHE ALA PHE          
SEQRES  27 B  454  VAL VAL PRO ILE LEU ILE ILE THR VAL CYS TYR GLY LEU          
SEQRES  28 B  454  MET LEU LEU ARG LEU ARG SER VAL ARG LEU LEU SER GLY          
SEQRES  29 B  454  SER LYS GLU LYS ASP ARG SER LEU ARG ARG ILE THR ARG          
SEQRES  30 B  454  MET VAL LEU VAL VAL VAL VAL ALA PHE VAL VAL CYS TRP          
SEQRES  31 B  454  ALA PRO ILE HIS ILE PHE VAL ILE VAL TRP THR LEU VAL          
SEQRES  32 B  454  ASP ILE ASP ARG ARG ASP PRO LEU VAL VAL ALA ALA LEU          
SEQRES  33 B  454  HIS LEU CYS ILE ALA LEU GLY TYR ILE ASN SER SER LEU          
SEQRES  34 B  454  ASN PRO VAL LEU TYR ALA PHE LEU ASP LYS ASN PHE LYS          
SEQRES  35 B  454  ARG CYS PHE ARG GLN LEU CYS ARG LYS PRO CYS GLY              
SEQRES   1 C    5  DI7 DAR PHE SAR OXJ                                          
SEQRES   1 D    5  DI7 DAR PHE SAR OXJ                                          
HET    DI7  C   1      14                                                       
HET    DAR  C   2      11                                                       
HET    SAR  C   4       5                                                       
HET    OXJ  C   5      17                                                       
HET    DI7  D   1      14                                                       
HET    DAR  D   2      11                                                       
HET    SAR  D   4       5                                                       
HET    OXJ  D   5      17                                                       
HET    CLR  A1201      28                                                       
HET    OLA  A1202      20                                                       
HET    OLA  A1203      20                                                       
HET    OLA  B1201      13                                                       
HET    OLA  B1202       9                                                       
HET    OLA  B1203       9                                                       
HET    OLA  B1204       9                                                       
HET    OLA  B1205       9                                                       
HET    OLC  B1206      19                                                       
HETNAM     DI7 2,6-DIMETHYL-L-TYROSINE                                          
HETNAM     DAR D-ARGININE                                                       
HETNAM     SAR SARCOSINE                                                        
HETNAM     OXJ 1-[3,5-BIS(TRIFLUOROMETHYL)PHENYL]-N-METHYLMETHANAMINE           
HETNAM     CLR CHOLESTEROL                                                      
HETNAM     OLA OLEIC ACID                                                       
HETNAM     OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETSYN     OLC 1-OLEOYL-R-GLYCEROL                                              
FORMUL   3  DI7    2(C11 H15 N O3)                                              
FORMUL   3  DAR    2(C6 H15 N4 O2 1+)                                           
FORMUL   3  SAR    2(C3 H7 N O2)                                                
FORMUL   3  OXJ    2(C10 H9 F6 N)                                               
FORMUL   5  CLR    C27 H46 O                                                    
FORMUL   6  OLA    7(C18 H34 O2)                                                
FORMUL  13  OLC    C21 H40 O4                                                   
FORMUL  14  HOH   *3(H2 O)                                                      
HELIX    1 AA1 THR A  999  LYS A 1019  1                                  21    
HELIX    2 AA2 ASN A 1022  GLN A 1041  1                                  20    
HELIX    3 AA3 SER A 1055  GLY A 1082  1                                  28    
HELIX    4 AA4 LYS A 1085  ALA A 1090  1                                   6    
HELIX    5 AA5 ALA A 1091  TYR A 1101  1                                  11    
HELIX    6 AA6 ILE A 1102  LEU A 1106  5                                   5    
HELIX    7 AA7 SER A   45  TYR A   77  1                                  33    
HELIX    8 AA8 THR A   82  SER A  100  1                                  19    
HELIX    9 AA9 THR A  101  GLU A  112  1                                  12    
HELIX   10 AB1 GLY A  117  HIS A  152  1                                  36    
HELIX   11 AB2 LYS A  155  ARG A  160  1                                   6    
HELIX   12 AB3 THR A  161  ALA A  176  1                                  16    
HELIX   13 AB4 ALA A  176  MET A  186  1                                  11    
HELIX   14 AB5 PRO A  205  PHE A  222  1                                  18    
HELIX   15 AB6 PHE A  222  SER A  247  1                                  26    
HELIX   16 AB7 ASP A  253  VAL A  287  1                                  35    
HELIX   17 AB8 ASP A  293  ASP A  322  1                                  30    
HELIX   18 AB9 ASP A  322  PHE A  329  1                                   8    
HELIX   19 AC1 LEU B 1003  GLU B 1018  1                                  16    
HELIX   20 AC2 ALA B 1024  LYS B 1042  1                                  19    
HELIX   21 AC3 LYS B 1059  LEU B 1078  1                                  20    
HELIX   22 AC4 GLU B 1092  ARG B 1098  1                                   7    
HELIX   23 AC5 ASN B 1099  TYR B 1101  5                                   3    
HELIX   24 AC6 SER B   42  TYR B   77  1                                  36    
HELIX   25 AC7 THR B   82  SER B  100  1                                  19    
HELIX   26 AC8 THR B  101  GLU B  112  1                                  12    
HELIX   27 AC9 PHE B  116  HIS B  152  1                                  37    
HELIX   28 AD1 HIS B  152  ARG B  160  1                                   9    
HELIX   29 AD2 THR B  161  ALA B  176  1                                  16    
HELIX   30 AD3 ALA B  176  MET B  186  1                                  11    
HELIX   31 AD4 PRO B  205  ALA B  221  1                                  17    
HELIX   32 AD5 PHE B  222  SER B  242  1                                  21    
HELIX   33 AD6 GLU B  251  VAL B  287  1                                  37    
HELIX   34 AD7 ASP B  293  LEU B  313  1                                  21    
HELIX   35 AD8 ASN B  314  PHE B  325  1                                  12    
HELIX   36 AD9 PHE B  325  PHE B  329  1                                   5    
SHEET    1 AA1 2 SER A  42  SER A  44  0                                        
SHEET    2 AA1 2 ARG B 330  LEU B 332 -1  O  GLN B 331   N  ALA A  43           
SHEET    1 AA2 2 ALA A 187  ARG A 192  0                                        
SHEET    2 AA2 2 ALA A 195  LEU A 200 -1  O  MET A 199   N  VAL A 188           
SHEET    1 AA3 2 ALA B 187  ARG B 192  0                                        
SHEET    2 AA3 2 ALA B 195  LEU B 200 -1  O  MET B 199   N  VAL B 188           
SSBOND   1 CYS A  121    CYS A  198                          1555   1555  2.05  
SSBOND   2 CYS B  121    CYS B  198                          1555   1555  2.04  
LINK         C   DI7 C   1                 N   DAR C   2     1555   1555  1.34  
LINK         C   DAR C   2                 N   PHE C   3     1555   1555  1.32  
LINK         C   PHE C   3                 N   SAR C   4     1555   1555  1.36  
LINK         C   SAR C   4                 NBO OXJ C   5     1555   1555  1.35  
LINK         C   DI7 D   1                 N   DAR D   2     1555   1555  1.33  
LINK         C   DAR D   2                 N   PHE D   3     1555   1555  1.33  
LINK         C   PHE D   3                 N   SAR D   4     1555   1555  1.36  
LINK         C   SAR D   4                 NBO OXJ D   5     1555   1555  1.34  
CISPEP   1 SER A  204    PRO A  205          0        -5.19                     
CISPEP   2 SER B  204    PRO B  205          0        -1.01                     
CISPEP   3 PHE C    3    SAR C    4          0        -4.90                     
CISPEP   4 PHE D    3    SAR D    4          0        -1.20                     
SITE     1 AC1  4 PRO A 276  ILE A 279  VAL A 283  ILE A 289                    
SITE     1 AC2  5 SER A 106  ALA A 107  LEU A 110  MET A 111                    
SITE     2 AC2  5 PHE B 325                                                     
SITE     1 AC3  1 TRP A 173                                                     
SITE     1 AC4  2 TYR B 318  ASP B 322                                          
SITE     1 AC5  1 TRP B 173                                                     
SITE     1 AC6  3 SER A 204  THR B 285  LEU B 286                               
SITE     1 AC7  3 LYS B 122  MET B 184  VAL B 185                               
SITE     1 AC8  2 ILE B 289  VAL B 296                                          
CRYST1   48.960  140.880  158.640  90.00  90.00  90.00 P 21 21 21    8          
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      0.020425  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007098  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006304        0.00000                         
ATOM      1  N   THR A 999     -32.045  38.405  -6.857  1.00140.84           N  
ANISOU    1  N   THR A 999    19387  17831  16294    647     36  -1292       N  
ATOM      2  CA  THR A 999     -31.996  37.755  -8.169  1.00140.11           C  
ANISOU    2  CA  THR A 999    19315  17670  16252    605     27  -1236       C  
ATOM      3  C   THR A 999     -31.839  36.225  -8.037  1.00144.03           C  
ANISOU    3  C   THR A 999    19823  18182  16718    537     72  -1156       C  
ATOM      4  O   THR A 999     -31.656  35.724  -6.924  1.00144.14           O  
ANISOU    4  O   THR A 999    19832  18259  16675    528    106  -1138       O  
ATOM      5  CB  THR A 999     -30.921  38.420  -9.075  1.00146.91           C  
ANISOU    5  CB  THR A 999    20237  18419  17162    612    -22  -1235       C  
ATOM      6  OG1 THR A 999     -30.951  37.828 -10.380  1.00146.87           O  
ANISOU    6  OG1 THR A 999    20254  18351  17198    576    -28  -1187       O  
ATOM      7  CG2 THR A 999     -29.507  38.352  -8.494  1.00143.25           C  
ANISOU    7  CG2 THR A 999    19808  17946  16672    596    -28  -1214       C  
ATOM      8  N   MET A1000     -31.941  35.488  -9.173  1.00140.01           N  
ANISOU    8  N   MET A1000    19342  17612  16241    490     74  -1110       N  
ATOM      9  CA  MET A1000     -31.772  34.025  -9.225  1.00139.41           C  
ANISOU    9  CA  MET A1000    19313  17518  16139    426    118  -1035       C  
ATOM     10  C   MET A1000     -30.304  33.630  -9.333  1.00139.38           C  
ANISOU   10  C   MET A1000    19379  17442  16136    444    117   -985       C  
ATOM     11  O   MET A1000     -29.951  32.485  -9.038  1.00139.02           O  
ANISOU   11  O   MET A1000    19384  17383  16054    422    159   -921       O  
ATOM     12  CB  MET A1000     -32.622  33.372 -10.333  1.00142.28           C  
ANISOU   12  CB  MET A1000    19685  17852  16521    359    125  -1016       C  
ATOM     13  CG  MET A1000     -34.127  33.465 -10.099  1.00147.47           C  
ANISOU   13  CG  MET A1000    20254  18618  17158    327    136  -1049       C  
ATOM     14  SD  MET A1000     -34.716  32.791  -8.515  1.00153.39           S  
ANISOU   14  SD  MET A1000    20965  19490  17827    289    200  -1035       S  
ATOM     15  CE  MET A1000     -34.853  34.334  -7.518  1.00150.23           C  
ANISOU   15  CE  MET A1000    20481  19177  17421    404    178  -1120       C  
ATOM     16  N   ALA A1001     -29.449  34.592  -9.744  1.00132.88           N  
ANISOU   16  N   ALA A1001    18559  16579  15349    485     72  -1011       N  
ATOM     17  CA  ALA A1001     -28.000  34.435  -9.834  1.00130.93           C  
ANISOU   17  CA  ALA A1001    18351  16298  15101    507     65   -969       C  
ATOM     18  C   ALA A1001     -27.513  34.285  -8.406  1.00130.20           C  
ANISOU   18  C   ALA A1001    18237  16287  14945    529     80   -957       C  
ATOM     19  O   ALA A1001     -26.778  33.344  -8.117  1.00129.31           O  
ANISOU   19  O   ALA A1001    18156  16177  14798    542    107   -888       O  
ATOM     20  CB  ALA A1001     -27.376  35.665 -10.478  1.00131.55           C  
ANISOU   20  CB  ALA A1001    18425  16337  15222    524     12  -1010       C  
ATOM     21  N   ASP A1002     -28.015  35.165  -7.498  1.00124.23           N  
ANISOU   21  N   ASP A1002    17435  15600  14168    540     65  -1022       N  
ATOM     22  CA  ASP A1002     -27.743  35.166  -6.057  1.00122.81           C  
ANISOU   22  CA  ASP A1002    17232  15513  13918    555     75  -1025       C  
ATOM     23  C   ASP A1002     -28.191  33.844  -5.443  1.00122.58           C  
ANISOU   23  C   ASP A1002    17218  15520  13837    537    132   -961       C  
ATOM     24  O   ASP A1002     -27.411  33.237  -4.710  1.00122.45           O  
ANISOU   24  O   ASP A1002    17220  15541  13766    554    146   -905       O  
ATOM     25  CB  ASP A1002     -28.448  36.345  -5.363  1.00125.17           C  
ANISOU   25  CB  ASP A1002    17492  15864  14203    571     58  -1118       C  
ATOM     26  CG  ASP A1002     -27.633  37.622  -5.287  1.00137.51           C  
ANISOU   26  CG  ASP A1002    19064  17411  15773    585      5  -1177       C  
ATOM     27  OD1 ASP A1002     -27.036  38.012  -6.319  1.00138.23           O  
ANISOU   27  OD1 ASP A1002    19179  17424  15917    576    -28  -1172       O  
ATOM     28  OD2 ASP A1002     -27.603  38.242  -4.198  1.00143.07           O  
ANISOU   28  OD2 ASP A1002    19757  18179  16424    595     -2  -1230       O  
ATOM     29  N   LEU A1003     -29.414  33.368  -5.795  1.00115.78           N  
ANISOU   29  N   LEU A1003    16355  14650  12987    497    164   -962       N  
ATOM     30  CA  LEU A1003     -29.956  32.096  -5.313  1.00114.34           C  
ANISOU   30  CA  LEU A1003    16202  14490  12754    452    223   -901       C  
ATOM     31  C   LEU A1003     -29.093  30.917  -5.757  1.00116.92           C  
ANISOU   31  C   LEU A1003    16618  14732  13073    453    246   -810       C  
ATOM     32  O   LEU A1003     -28.804  30.047  -4.933  1.00116.59           O  
ANISOU   32  O   LEU A1003    16619  14711  12968    458    282   -746       O  
ATOM     33  CB  LEU A1003     -31.435  31.905  -5.723  1.00114.01           C  
ANISOU   33  CB  LEU A1003    16127  14467  12723    389    246   -925       C  
ATOM     34  CG  LEU A1003     -32.123  30.551  -5.382  1.00118.28           C  
ANISOU   34  CG  LEU A1003    16709  15023  13209    306    310   -863       C  
ATOM     35  CD1 LEU A1003     -32.090  30.228  -3.883  1.00118.47           C  
ANISOU   35  CD1 LEU A1003    16728  15137  13148    311    347   -837       C  
ATOM     36  CD2 LEU A1003     -33.540  30.531  -5.875  1.00120.20           C  
ANISOU   36  CD2 LEU A1003    16897  15311  13463    232    322   -895       C  
ATOM     37  N   GLU A1004     -28.666  30.904  -7.042  1.00112.75           N  
ANISOU   37  N   GLU A1004    16125  14108  12605    458    227   -803       N  
ATOM     38  CA  GLU A1004     -27.833  29.844  -7.623  1.00112.27           C  
ANISOU   38  CA  GLU A1004    16159  13959  12542    476    254   -725       C  
ATOM     39  C   GLU A1004     -26.439  29.830  -6.986  1.00114.65           C  
ANISOU   39  C   GLU A1004    16457  14296  12808    558    243   -681       C  
ATOM     40  O   GLU A1004     -25.976  28.766  -6.574  1.00114.34           O  
ANISOU   40  O   GLU A1004    16485  14241  12718    590    283   -602       O  
ATOM     41  CB  GLU A1004     -27.744  29.985  -9.157  1.00113.17           C  
ANISOU   41  CB  GLU A1004    16300  13977  12721    464    235   -740       C  
ATOM     42  CG  GLU A1004     -27.522  28.672  -9.891  1.00124.15           C  
ANISOU   42  CG  GLU A1004    17809  15261  14101    451    282   -675       C  
ATOM     43  CD  GLU A1004     -27.300  28.799 -11.386  1.00146.83           C  
ANISOU   43  CD  GLU A1004    20715  18045  17027    444    267   -689       C  
ATOM     44  OE1 GLU A1004     -28.231  29.238 -12.100  1.00145.16           O  
ANISOU   44  OE1 GLU A1004    20477  17826  16850    381    243   -740       O  
ATOM     45  OE2 GLU A1004     -26.190  28.449 -11.846  1.00142.64           O1-
ANISOU   45  OE2 GLU A1004    20235  17464  16497    508    279   -648       O1-
ATOM     46  N   ASP A1005     -25.797  31.012  -6.875  1.00109.94           N  
ANISOU   46  N   ASP A1005    15787  13754  12232    589    190   -729       N  
ATOM     47  CA  ASP A1005     -24.471  31.173  -6.280  1.00109.84           C  
ANISOU   47  CA  ASP A1005    15746  13807  12181    650    168   -696       C  
ATOM     48  C   ASP A1005     -24.441  30.794  -4.805  1.00113.97           C  
ANISOU   48  C   ASP A1005    16258  14426  12619    669    184   -664       C  
ATOM     49  O   ASP A1005     -23.484  30.143  -4.381  1.00115.11           O  
ANISOU   49  O   ASP A1005    16420  14604  12714    730    193   -588       O  
ATOM     50  CB  ASP A1005     -23.930  32.591  -6.510  1.00111.54           C  
ANISOU   50  CB  ASP A1005    15893  14057  12430    644    106   -765       C  
ATOM     51  CG  ASP A1005     -23.606  32.891  -7.966  1.00123.15           C  
ANISOU   51  CG  ASP A1005    17380  15442  13971    636     91   -774       C  
ATOM     52  OD1 ASP A1005     -23.232  31.940  -8.704  1.00123.54           O  
ANISOU   52  OD1 ASP A1005    17482  15429  14027    664    125   -711       O  
ATOM     53  OD2 ASP A1005     -23.719  34.078  -8.368  1.00128.79           O  
ANISOU   53  OD2 ASP A1005    18064  16145  14726    606     47   -843       O  
ATOM     54  N   ASN A1006     -25.503  31.159  -4.036  1.00108.37           N  
ANISOU   54  N   ASN A1006    15522  13767  11888    624    190   -717       N  
ATOM     55  CA  ASN A1006     -25.645  30.800  -2.619  1.00107.54           C  
ANISOU   55  CA  ASN A1006    15410  13756  11694    630    211   -691       C  
ATOM     56  C   ASN A1006     -25.831  29.302  -2.467  1.00109.95           C  
ANISOU   56  C   ASN A1006    15805  14014  11956    633    272   -592       C  
ATOM     57  O   ASN A1006     -25.174  28.693  -1.627  1.00110.66           O  
ANISOU   57  O   ASN A1006    15920  14152  11972    682    284   -520       O  
ATOM     58  CB  ASN A1006     -26.790  31.561  -1.949  1.00106.43           C  
ANISOU   58  CB  ASN A1006    15219  13680  11539    585    212   -775       C  
ATOM     59  CG  ASN A1006     -26.453  32.994  -1.624  1.00116.22           C  
ANISOU   59  CG  ASN A1006    16396  14978  12784    596    156   -866       C  
ATOM     60  OD1 ASN A1006     -25.399  33.298  -1.046  1.00107.45           O  
ANISOU   60  OD1 ASN A1006    15266  13930  11630    622    122   -856       O  
ATOM     61  ND2 ASN A1006     -27.351  33.905  -1.976  1.00103.60           N  
ANISOU   61  ND2 ASN A1006    14769  13362  11231    576    145   -955       N  
ATOM     62  N   TRP A1007     -26.685  28.704  -3.312  1.00105.29           N  
ANISOU   62  N   TRP A1007    15273  13326  11406    578    309   -586       N  
ATOM     63  CA  TRP A1007     -26.926  27.264  -3.353  1.00105.46           C  
ANISOU   63  CA  TRP A1007    15411  13269  11390    560    371   -499       C  
ATOM     64  C   TRP A1007     -25.603  26.533  -3.667  1.00107.13           C  
ANISOU   64  C   TRP A1007    15696  13420  11589    658    378   -412       C  
ATOM     65  O   TRP A1007     -25.285  25.536  -3.008  1.00107.49           O  
ANISOU   65  O   TRP A1007    15823  13455  11565    699    416   -323       O  
ATOM     66  CB  TRP A1007     -28.029  26.946  -4.386  1.00104.37           C  
ANISOU   66  CB  TRP A1007    15313  13042  11302    465    397   -527       C  
ATOM     67  CG  TRP A1007     -28.504  25.522  -4.434  1.00106.51           C  
ANISOU   67  CG  TRP A1007    15717  13224  11528    407    463   -453       C  
ATOM     68  CD1 TRP A1007     -28.652  24.751  -5.550  1.00109.54           C  
ANISOU   68  CD1 TRP A1007    16207  13473  11939    366    490   -430       C  
ATOM     69  CD2 TRP A1007     -28.945  24.716  -3.327  1.00107.64           C  
ANISOU   69  CD2 TRP A1007    15916  13400  11584    367    514   -395       C  
ATOM     70  NE1 TRP A1007     -29.158  23.517  -5.212  1.00110.30           N  
ANISOU   70  NE1 TRP A1007    16431  13507  11972    297    554   -365       N  
ATOM     71  CE2 TRP A1007     -29.325  23.459  -3.851  1.00112.39           C  
ANISOU   71  CE2 TRP A1007    16667  13871  12166    297    570   -337       C  
ATOM     72  CE3 TRP A1007     -29.057  24.935  -1.940  1.00109.44           C  
ANISOU   72  CE3 TRP A1007    16089  13752  11740    376    518   -386       C  
ATOM     73  CZ2 TRP A1007     -29.802  22.422  -3.038  1.00112.87           C  
ANISOU   73  CZ2 TRP A1007    16830  13915  12140    233    631   -266       C  
ATOM     74  CZ3 TRP A1007     -29.519  23.905  -1.134  1.00112.10           C  
ANISOU   74  CZ3 TRP A1007    16518  14085  11992    321    578   -313       C  
ATOM     75  CH2 TRP A1007     -29.893  22.668  -1.682  1.00113.53           C  
ANISOU   75  CH2 TRP A1007    16851  14128  12156    247    634   -252       C  
ATOM     76  N   GLU A1008     -24.802  27.088  -4.608  1.00100.99           N  
ANISOU   76  N   GLU A1008    14883  12617  10873    704    341   -436       N  
ATOM     77  CA  GLU A1008     -23.494  26.566  -4.993  1.00100.57           C  
ANISOU   77  CA  GLU A1008    14869  12533  10810    810    345   -364       C  
ATOM     78  C   GLU A1008     -22.527  26.654  -3.819  1.00104.82           C  
ANISOU   78  C   GLU A1008    15351  13202  11275    893    321   -316       C  
ATOM     79  O   GLU A1008     -21.907  25.648  -3.497  1.00105.03           O  
ANISOU   79  O   GLU A1008    15449  13213  11244    981    354   -219       O  
ATOM     80  CB  GLU A1008     -22.941  27.299  -6.223  1.00101.24           C  
ANISOU   80  CB  GLU A1008    14907  12588  10972    822    310   -410       C  
ATOM     81  N   THR A1009     -22.450  27.828  -3.139  1.00101.88           N  
ANISOU   81  N   THR A1009    14861  12955  10895    865    266   -383       N  
ATOM     82  CA  THR A1009     -21.609  28.071  -1.952  1.00102.60           C  
ANISOU   82  CA  THR A1009    14884  13194  10906    919    232   -353       C  
ATOM     83  C   THR A1009     -21.904  27.048  -0.837  1.00109.69           C  
ANISOU   83  C   THR A1009    15852  14114  11711    945    275   -271       C  
ATOM     84  O   THR A1009     -20.968  26.507  -0.241  1.00110.33           O  
ANISOU   84  O   THR A1009    15939  14262  11721   1041    271   -184       O  
ATOM     85  CB  THR A1009     -21.763  29.519  -1.465  1.00108.63           C  
ANISOU   85  CB  THR A1009    15539  14058  11675    854    172   -459       C  
ATOM     86  OG1 THR A1009     -21.491  30.422  -2.534  1.00107.77           O  
ANISOU   86  OG1 THR A1009    15388  13911  11649    828    136   -524       O  
ATOM     87  CG2 THR A1009     -20.854  29.849  -0.297  1.00108.58           C  
ANISOU   87  CG2 THR A1009    15462  14213  11580    891    129   -439       C  
ATOM     88  N   LEU A1010     -23.200  26.772  -0.577  1.00107.69           N  
ANISOU   88  N   LEU A1010    15652  13812  11453    860    316   -295       N  
ATOM     89  CA  LEU A1010     -23.640  25.797   0.420  1.00109.27           C  
ANISOU   89  CA  LEU A1010    15933  14020  11564    858    365   -219       C  
ATOM     90  C   LEU A1010     -23.036  24.427   0.113  1.00115.13           C  
ANISOU   90  C   LEU A1010    16809  14658  12277    947    411    -97       C  
ATOM     91  O   LEU A1010     -22.368  23.863   0.977  1.00116.24           O  
ANISOU   91  O   LEU A1010    16978  14856  12330   1034    415     -6       O  
ATOM     92  CB  LEU A1010     -25.176  25.695   0.433  1.00109.57           C  
ANISOU   92  CB  LEU A1010    16002  14014  11615    734    408   -267       C  
ATOM     93  CG  LEU A1010     -25.938  26.804   1.130  1.00114.56           C  
ANISOU   93  CG  LEU A1010    16525  14764  12239    666    384   -368       C  
ATOM     94  CD1 LEU A1010     -27.285  27.009   0.490  1.00114.58           C  
ANISOU   94  CD1 LEU A1010    16518  14716  12300    564    409   -439       C  
ATOM     95  CD2 LEU A1010     -26.139  26.482   2.574  1.00118.50           C  
ANISOU   95  CD2 LEU A1010    17032  15367  12625    662    406   -327       C  
ATOM     96  N   ASN A1011     -23.235  23.927  -1.141  1.00111.53           N  
ANISOU   96  N   ASN A1011    16438  14048  11889    934    444    -95       N  
ATOM     97  CA  ASN A1011     -22.759  22.636  -1.654  1.00111.40           C  
ANISOU   97  CA  ASN A1011    16578  13896  11854   1017    498      5       C  
ATOM     98  C   ASN A1011     -21.237  22.529  -1.719  1.00115.00           C  
ANISOU   98  C   ASN A1011    17003  14404  12288   1185    475     72       C  
ATOM     99  O   ASN A1011     -20.696  21.522  -1.256  1.00115.84           O  
ANISOU   99  O   ASN A1011    17210  14484  12321   1296    509    183       O  
ATOM    100  CB  ASN A1011     -23.397  22.314  -3.003  1.00110.45           C  
ANISOU  100  CB  ASN A1011    16546  13612  11809    944    533    -33       C  
ATOM    101  CG  ASN A1011     -24.909  22.252  -2.977  1.00138.67           C  
ANISOU  101  CG  ASN A1011    20151  17147  15392    777    560    -85       C  
ATOM    102  OD1 ASN A1011     -25.545  22.089  -1.923  1.00132.90           O  
ANISOU  102  OD1 ASN A1011    19422  16476  14598    718    578    -69       O  
ATOM    103  ND2 ASN A1011     -25.521  22.380  -4.147  1.00131.73           N  
ANISOU  103  ND2 ASN A1011    19288  16178  14585    694    564   -147       N  
ATOM    104  N   ASP A1012     -20.550  23.563  -2.260  1.00110.19           N  
ANISOU  104  N   ASP A1012    16254  13878  11736   1206    417     10       N  
ATOM    105  CA  ASP A1012     -19.088  23.620  -2.352  1.00110.99           C  
ANISOU  105  CA  ASP A1012    16285  14069  11815   1349    389     64       C  
ATOM    106  C   ASP A1012     -18.427  23.530  -0.982  1.00118.04           C  
ANISOU  106  C   ASP A1012    17123  15124  12604   1430    360    136       C  
ATOM    107  O   ASP A1012     -17.430  22.820  -0.844  1.00119.13           O  
ANISOU  107  O   ASP A1012    17284  15294  12685   1584    372    239       O  
ATOM    108  CB  ASP A1012     -18.620  24.902  -3.055  1.00112.13           C  
ANISOU  108  CB  ASP A1012    16280  14291  12031   1310    328    -26       C  
ATOM    109  CG  ASP A1012     -18.898  24.948  -4.546  1.00126.79           C  
ANISOU  109  CG  ASP A1012    18185  16010  13982   1272    351    -75       C  
ATOM    110  OD1 ASP A1012     -18.782  23.886  -5.212  1.00128.21           O  
ANISOU  110  OD1 ASP A1012    18495  16059  14161   1343    411    -15       O  
ATOM    111  OD2 ASP A1012     -19.205  26.047  -5.056  1.00133.24           O1-
ANISOU  111  OD2 ASP A1012    18917  16843  14864   1177    310   -172       O1-
ATOM    112  N   ASN A1013     -18.992  24.226   0.036  1.00115.44           N  
ANISOU  112  N   ASN A1013    16722  14900  12241   1335    324     83       N  
ATOM    113  CA  ASN A1013     -18.448  24.227   1.395  1.00116.44           C  
ANISOU  113  CA  ASN A1013    16792  15193  12258   1392    291    140       C  
ATOM    114  C   ASN A1013     -18.732  22.942   2.173  1.00123.12           C  
ANISOU  114  C   ASN A1013    17785  15982  13014   1452    348    256       C  
ATOM    115  O   ASN A1013     -18.079  22.724   3.190  1.00123.68           O  
ANISOU  115  O   ASN A1013    17826  16184  12984   1537    324    334       O  
ATOM    116  CB  ASN A1013     -18.862  25.462   2.174  1.00114.27           C  
ANISOU  116  CB  ASN A1013    16398  15050  11970   1275    234     37       C  
ATOM    117  CG  ASN A1013     -18.040  26.669   1.796  1.00131.69           C  
ANISOU  117  CG  ASN A1013    18455  17366  14215   1257    162    -38       C  
ATOM    118  OD1 ASN A1013     -16.813  26.707   1.961  1.00125.19           O  
ANISOU  118  OD1 ASN A1013    17551  16672  13346   1346    122     16       O  
ATOM    119  ND2 ASN A1013     -18.696  27.685   1.270  1.00122.84           N  
ANISOU  119  ND2 ASN A1013    17296  16204  13175   1141    144   -160       N  
ATOM    120  N   LEU A1014     -19.662  22.078   1.691  1.00121.33           N  
ANISOU  120  N   LEU A1014    17721  15563  12815   1403    422    273       N  
ATOM    121  CA  LEU A1014     -19.943  20.765   2.295  1.00123.09           C  
ANISOU  121  CA  LEU A1014    18120  15695  12953   1448    486    390       C  
ATOM    122  C   LEU A1014     -18.771  19.835   1.984  1.00130.15           C  
ANISOU  122  C   LEU A1014    19095  16544  13811   1649    507    511       C  
ATOM    123  O   LEU A1014     -18.311  19.118   2.869  1.00131.27           O  
ANISOU  123  O   LEU A1014    19299  16729  13849   1762    517    627       O  
ATOM    124  CB  LEU A1014     -21.250  20.154   1.761  1.00122.81           C  
ANISOU  124  CB  LEU A1014    18238  15467  12957   1315    557    365       C  
ATOM    125  CG  LEU A1014     -22.510  20.378   2.589  1.00127.26           C  
ANISOU  125  CG  LEU A1014    18795  16072  13488   1153    572    319       C  
ATOM    126  CD1 LEU A1014     -23.738  20.372   1.708  1.00126.74           C  
ANISOU  126  CD1 LEU A1014    18776  15878  13500    995    610    239       C  
ATOM    127  CD2 LEU A1014     -22.653  19.333   3.675  1.00130.21           C  
ANISOU  127  CD2 LEU A1014    19305  16429  13740   1179    619    439       C  
ATOM    128  N   LYS A1015     -18.267  19.886   0.731  1.00128.00           N  
ANISOU  128  N   LYS A1015    18817  16200  13620   1704    513    486       N  
ATOM    129  CA  LYS A1015     -17.119  19.113   0.256  1.00129.73           C  
ANISOU  129  CA  LYS A1015    19093  16384  13814   1909    537    585       C  
ATOM    130  C   LYS A1015     -15.825  19.571   0.950  1.00136.63           C  
ANISOU  130  C   LYS A1015    19791  17500  14623   2047    469    637       C  
ATOM    131  O   LYS A1015     -14.928  18.751   1.156  1.00137.73           O  
ANISOU  131  O   LYS A1015    19981  17659  14690   2243    488    759       O  
ATOM    132  CB  LYS A1015     -16.984  19.221  -1.271  1.00131.35           C  
ANISOU  132  CB  LYS A1015    19312  16473  14121   1908    560    524       C  
ATOM    133  N   VAL A1016     -15.737  20.876   1.309  1.00134.06           N  
ANISOU  133  N   VAL A1016    19263  17359  14315   1944    389    545       N  
ATOM    134  CA  VAL A1016     -14.590  21.474   2.010  1.00135.60           C  
ANISOU  134  CA  VAL A1016    19271  17807  14442   2025    312    574       C  
ATOM    135  C   VAL A1016     -14.404  20.764   3.372  1.00144.20           C  
ANISOU  135  C   VAL A1016    20412  18983  15397   2119    309    693       C  
ATOM    136  O   VAL A1016     -13.290  20.330   3.681  1.00145.24           O  
ANISOU  136  O   VAL A1016    20499  19236  15451   2301    291    802       O  
ATOM    137  CB  VAL A1016     -14.705  23.029   2.127  1.00137.95           C  
ANISOU  137  CB  VAL A1016    19382  18249  14783   1859    233    436       C  
ATOM    138  CG1 VAL A1016     -13.633  23.621   3.045  1.00138.53           C  
ANISOU  138  CG1 VAL A1016    19278  18593  14764   1907    149    463       C  
ATOM    139  CG2 VAL A1016     -14.645  23.692   0.754  1.00136.30           C  
ANISOU  139  CG2 VAL A1016    19122  17973  14695   1799    230    344       C  
ATOM    140  N   ILE A1017     -15.513  20.594   4.136  1.00142.70           N  
ANISOU  140  N   ILE A1017    20318  18727  15175   2003    333    679       N  
ATOM    141  CA  ILE A1017     -15.555  19.900   5.435  1.00144.81           C  
ANISOU  141  CA  ILE A1017    20661  19050  15311   2063    340    789       C  
ATOM    142  C   ILE A1017     -15.251  18.408   5.225  1.00153.56           C  
ANISOU  142  C   ILE A1017    21973  19999  16373   2243    414    938       C  
ATOM    143  O   ILE A1017     -14.492  17.823   6.001  1.00154.88           O  
ANISOU  143  O   ILE A1017    22155  20265  16427   2407    401   1067       O  
ATOM    144  CB  ILE A1017     -16.909  20.138   6.177  1.00146.99           C  
ANISOU  144  CB  ILE A1017    20989  19290  15571   1873    359    724       C  
ATOM    145  CG1 ILE A1017     -17.129  21.637   6.460  1.00145.65           C  
ANISOU  145  CG1 ILE A1017    20628  19281  15433   1725    287    578       C  
ATOM    146  CG2 ILE A1017     -16.994  19.325   7.486  1.00149.48           C  
ANISOU  146  CG2 ILE A1017    21405  19647  15742   1930    377    848       C  
ATOM    147  CD1 ILE A1017     -18.567  22.084   6.487  1.00148.39           C  
ANISOU  147  CD1 ILE A1017    21007  19545  15829   1533    318    467       C  
ATOM    148  N   GLU A1018     -15.823  17.814   4.154  1.00152.18           N  
ANISOU  148  N   GLU A1018    21961  19580  16281   2216    490    919       N  
ATOM    149  CA  GLU A1018     -15.642  16.413   3.765  1.00154.53           C  
ANISOU  149  CA  GLU A1018    22490  19677  16547   2368    572   1039       C  
ATOM    150  C   GLU A1018     -14.148  16.068   3.637  1.00161.50           C  
ANISOU  150  C   GLU A1018    23314  20666  17381   2634    554   1144       C  
ATOM    151  O   GLU A1018     -13.705  15.050   4.178  1.00162.82           O  
ANISOU  151  O   GLU A1018    23615  20802  17448   2815    585   1289       O  
ATOM    152  CB  GLU A1018     -16.382  16.131   2.441  1.00155.18           C  
ANISOU  152  CB  GLU A1018    22709  19512  16739   2272    639    965       C  
ATOM    153  CG  GLU A1018     -16.844  14.695   2.261  1.00169.91           C  
ANISOU  153  CG  GLU A1018    24879  21114  18564   2313    737   1057       C  
ATOM    154  CD  GLU A1018     -18.120  14.339   3.001  1.00195.58           C  
ANISOU  154  CD  GLU A1018    28263  24276  21773   2128    774   1059       C  
ATOM    155  OE1 GLU A1018     -19.195  14.852   2.613  1.00190.62           O  
ANISOU  155  OE1 GLU A1018    27606  23601  21219   1908    778    942       O  
ATOM    156  OE2 GLU A1018     -18.046  13.541   3.965  1.00191.12           O1-
ANISOU  156  OE2 GLU A1018    27829  23695  21095   2204    799   1183       O1-
ATOM    157  N   LYS A1019     -13.376  16.957   2.973  1.00158.41           N  
ANISOU  157  N   LYS A1019    22715  20421  17054   2657    501   1075       N  
ATOM    158  CA  LYS A1019     -11.937  16.806   2.736  1.00159.75           C  
ANISOU  158  CA  LYS A1019    22777  20735  17185   2891    479   1157       C  
ATOM    159  C   LYS A1019     -11.058  17.679   3.670  1.00164.01           C  
ANISOU  159  C   LYS A1019    23055  21611  17651   2914    373   1168       C  
ATOM    160  O   LYS A1019      -9.869  17.881   3.393  1.00164.01           O  
ANISOU  160  O   LYS A1019    22896  21788  17632   3059    338   1205       O  
ATOM    161  CB  LYS A1019     -11.613  17.045   1.247  1.00161.77           C  
ANISOU  161  CB  LYS A1019    22999  20917  17551   2906    506   1085       C  
ATOM    162  CG  LYS A1019     -12.085  15.916   0.330  1.00179.90           C  
ANISOU  162  CG  LYS A1019    25568  22904  19883   2963    613   1112       C  
ATOM    163  CD  LYS A1019     -11.669  16.142  -1.116  1.00191.60           C  
ANISOU  163  CD  LYS A1019    27009  24332  21457   2994    639   1046       C  
ATOM    164  CE  LYS A1019     -12.002  14.959  -1.993  1.00204.11           C  
ANISOU  164  CE  LYS A1019    28877  25620  23058   3073    747   1078       C  
ATOM    165  NZ  LYS A1019     -11.548  15.167  -3.392  1.00212.50           N1+
ANISOU  165  NZ  LYS A1019    29901  26643  24198   3113    775   1016       N1+
ATOM    166  N   ALA A1020     -11.634  18.154   4.793  1.00160.59           N  
ANISOU  166  N   ALA A1020    22579  21272  17164   2773    326   1140       N  
ATOM    167  CA  ALA A1020     -10.913  18.960   5.782  1.00161.19           C  
ANISOU  167  CA  ALA A1020    22434  21658  17155   2769    225   1144       C  
ATOM    168  C   ALA A1020     -10.143  18.075   6.768  1.00167.57           C  
ANISOU  168  C   ALA A1020    23270  22587  17811   2991    213   1319       C  
ATOM    169  O   ALA A1020     -10.531  16.929   7.004  1.00168.13           O  
ANISOU  169  O   ALA A1020    23566  22479  17835   3089    284   1424       O  
ATOM    170  CB  ALA A1020     -11.874  19.866   6.533  1.00160.89           C  
ANISOU  170  CB  ALA A1020    22350  21663  17119   2529    184   1030       C  
ATOM    171  N   ASP A1021      -9.060  18.619   7.347  1.00165.20           N  
ANISOU  171  N   ASP A1021    22746  22596  17428   3061    122   1353       N  
ATOM    172  CA  ASP A1021      -8.196  17.925   8.306  1.00167.32           C  
ANISOU  172  CA  ASP A1021    22994  23040  17541   3279     91   1520       C  
ATOM    173  C   ASP A1021      -8.043  18.674   9.641  1.00170.79           C  
ANISOU  173  C   ASP A1021    23275  23753  17865   3178    -11   1507       C  
ATOM    174  O   ASP A1021      -7.706  18.049  10.650  1.00171.89           O  
ANISOU  174  O   ASP A1021    23448  24000  17863   3315    -31   1642       O  
ATOM    175  CB  ASP A1021      -6.822  17.618   7.676  1.00170.84           C  
ANISOU  175  CB  ASP A1021    23318  23626  17968   3525     83   1609       C  
ATOM    176  CG  ASP A1021      -6.220  18.760   6.872  1.00182.78           C  
ANISOU  176  CG  ASP A1021    24585  25302  19561   3423     29   1491       C  
ATOM    177  OD1 ASP A1021      -5.702  19.716   7.493  1.00184.34           O  
ANISOU  177  OD1 ASP A1021    24557  25782  19701   3324    -72   1449       O  
ATOM    178  OD2 ASP A1021      -6.262  18.694   5.622  1.00187.59           O1-
ANISOU  178  OD2 ASP A1021    25237  25755  20285   3435     90   1441       O1-
ATOM    179  N   ASN A1022      -8.294  20.004   9.640  1.00165.43           N  
ANISOU  179  N   ASN A1022    22437  23180  17238   2942    -73   1345       N  
ATOM    180  CA  ASN A1022      -8.195  20.887  10.809  1.00165.10           C  
ANISOU  180  CA  ASN A1022    22248  23388  17095   2809   -170   1298       C  
ATOM    181  C   ASN A1022      -9.507  21.616  11.113  1.00165.93           C  
ANISOU  181  C   ASN A1022    22421  23373  17252   2550   -158   1148       C  
ATOM    182  O   ASN A1022     -10.326  21.821  10.214  1.00164.07           O  
ANISOU  182  O   ASN A1022    22268  22917  17156   2439   -100   1046       O  
ATOM    183  CB  ASN A1022      -7.066  21.909  10.616  1.00166.77           C  
ANISOU  183  CB  ASN A1022    22186  23886  17294   2775   -267   1245       C  
ATOM    184  CG  ASN A1022      -5.691  21.365  10.913  1.00195.05           C  
ANISOU  184  CG  ASN A1022    25636  27721  20754   3014   -315   1403       C  
ATOM    185  OD1 ASN A1022      -5.316  21.140  12.072  1.00191.50           O  
ANISOU  185  OD1 ASN A1022    25143  27468  20150   3084   -372   1497       O  
ATOM    186  ND2 ASN A1022      -4.901  21.156   9.871  1.00187.12           N  
ANISOU  186  ND2 ASN A1022    24557  26732  19809   3150   -292   1438       N  
ATOM    187  N   ALA A1023      -9.679  22.037  12.383  1.00161.91           N  
ANISOU  187  N   ALA A1023    21866  23028  16624   2460   -216   1134       N  
ATOM    188  CA  ALA A1023     -10.843  22.775  12.889  1.00159.89           C  
ANISOU  188  CA  ALA A1023    21655  22710  16386   2233   -210    996       C  
ATOM    189  C   ALA A1023     -11.019  24.134  12.217  1.00160.34           C  
ANISOU  189  C   ALA A1023    21594  22771  16557   2041   -244    808       C  
ATOM    190  O   ALA A1023     -12.152  24.586  12.078  1.00158.72           O  
ANISOU  190  O   ALA A1023    21465  22413  16429   1886   -204    689       O  
ATOM    191  CB  ALA A1023     -10.739  22.951  14.398  1.00161.95           C  
ANISOU  191  CB  ALA A1023    21872  23187  16473   2203   -273   1028       C  
ATOM    192  N   ALA A1024      -9.903  24.776  11.799  1.00155.63           N  
ANISOU  192  N   ALA A1024    20813  22352  15966   2054   -317    787       N  
ATOM    193  CA  ALA A1024      -9.880  26.077  11.114  1.00153.35           C  
ANISOU  193  CA  ALA A1024    20413  22078  15776   1879   -355    623       C  
ATOM    194  C   ALA A1024     -10.572  26.001   9.749  1.00152.76           C  
ANISOU  194  C   ALA A1024    20437  21726  15877   1852   -274    561       C  
ATOM    195  O   ALA A1024     -11.207  26.972   9.321  1.00150.76           O  
ANISOU  195  O   ALA A1024    20180  21386  15715   1682   -276    412       O  
ATOM    196  CB  ALA A1024      -8.441  26.550  10.940  1.00155.12           C  
ANISOU  196  CB  ALA A1024    20427  22560  15953   1916   -441    647       C  
ATOM    197  N   GLN A1025     -10.441  24.834   9.080  1.00147.27           N  
ANISOU  197  N   GLN A1025    19841  20894  15221   2026   -204    678       N  
ATOM    198  CA  GLN A1025     -11.023  24.534   7.775  1.00144.55           C  
ANISOU  198  CA  GLN A1025    19607  20290  15026   2024   -124    642       C  
ATOM    199  C   GLN A1025     -12.522  24.275   7.901  1.00144.35           C  
ANISOU  199  C   GLN A1025    19760  20040  15047   1922    -54    592       C  
ATOM    200  O   GLN A1025     -13.303  24.806   7.104  1.00142.38           O  
ANISOU  200  O   GLN A1025    19543  19639  14918   1797    -25    476       O  
ATOM    201  CB  GLN A1025     -10.321  23.325   7.141  1.00146.70           C  
ANISOU  201  CB  GLN A1025    19939  20503  15298   2254    -72    787       C  
ATOM    202  CG  GLN A1025      -8.959  23.647   6.551  1.00157.31           C  
ANISOU  202  CG  GLN A1025    21098  22032  16640   2344   -120    813       C  
ATOM    203  CD  GLN A1025      -8.280  22.397   6.073  1.00176.44           C  
ANISOU  203  CD  GLN A1025    23588  24409  19043   2600    -63    963       C  
ATOM    204  OE1 GLN A1025      -8.594  21.855   5.005  1.00172.27           O  
ANISOU  204  OE1 GLN A1025    23186  23656  18611   2651     18    962       O  
ATOM    205  NE2 GLN A1025      -7.337  21.909   6.860  1.00169.18           N  
ANISOU  205  NE2 GLN A1025    22588  23701  17990   2773   -103   1095       N  
ATOM    206  N   VAL A1026     -12.917  23.470   8.908  1.00139.04           N  
ANISOU  206  N   VAL A1026    19197  19361  14272   1974    -27    683       N  
ATOM    207  CA  VAL A1026     -14.312  23.124   9.194  1.00137.23           C  
ANISOU  207  CA  VAL A1026    19129  18953  14060   1875     43    654       C  
ATOM    208  C   VAL A1026     -15.098  24.375   9.629  1.00139.00           C  
ANISOU  208  C   VAL A1026    19281  19232  14301   1672      9    493       C  
ATOM    209  O   VAL A1026     -16.216  24.572   9.159  1.00137.25           O  
ANISOU  209  O   VAL A1026    19131  18849  14170   1558     60    404       O  
ATOM    210  CB  VAL A1026     -14.426  21.964  10.226  1.00142.23           C  
ANISOU  210  CB  VAL A1026    19894  19585  14561   1979     77    803       C  
ATOM    211  CG1 VAL A1026     -15.877  21.550  10.446  1.00141.42           C  
ANISOU  211  CG1 VAL A1026    19958  19299  14474   1862    158    778       C  
ATOM    212  CG2 VAL A1026     -13.594  20.757   9.800  1.00143.16           C  
ANISOU  212  CG2 VAL A1026    20096  19642  14655   2205    111    964       C  
ATOM    213  N   LYS A1027     -14.489  25.231  10.487  1.00135.69           N  
ANISOU  213  N   LYS A1027    18721  19045  13792   1632    -77    454       N  
ATOM    214  CA  LYS A1027     -15.086  26.454  11.046  1.00134.39           C  
ANISOU  214  CA  LYS A1027    18494  18950  13617   1457   -114    303       C  
ATOM    215  C   LYS A1027     -15.506  27.487  10.004  1.00135.34           C  
ANISOU  215  C   LYS A1027    18576  18965  13882   1336   -115    151       C  
ATOM    216  O   LYS A1027     -16.662  27.908  10.025  1.00133.90           O  
ANISOU  216  O   LYS A1027    18448  18681  13746   1226    -78     50       O  
ATOM    217  CB  LYS A1027     -14.166  27.102  12.095  1.00137.76           C  
ANISOU  217  CB  LYS A1027    18786  19650  13907   1443   -211    298       C  
ATOM    218  CG  LYS A1027     -14.916  27.773  13.246  1.00147.62           C  
ANISOU  218  CG  LYS A1027    20046  20975  15070   1314   -224    204       C  
ATOM    219  CD  LYS A1027     -13.979  28.385  14.290  1.00157.19           C  
ANISOU  219  CD  LYS A1027    21134  22459  16132   1291   -324    198       C  
ATOM    220  CE  LYS A1027     -13.349  27.358  15.208  1.00169.86           C  
ANISOU  220  CE  LYS A1027    22747  24208  17585   1432   -342    371       C  
ATOM    221  NZ  LYS A1027     -12.511  27.991  16.261  1.00180.85           N  
ANISOU  221  NZ  LYS A1027    24013  25881  18820   1391   -445    357       N  
ATOM    222  N   ASP A1028     -14.585  27.893   9.105  1.00130.72           N  
ANISOU  222  N   ASP A1028    17897  18412  13361   1361   -155    138       N  
ATOM    223  CA  ASP A1028     -14.870  28.903   8.084  1.00128.87           C  
ANISOU  223  CA  ASP A1028    17628  18081  13255   1249   -162      3       C  
ATOM    224  C   ASP A1028     -15.817  28.413   6.987  1.00128.53           C  
ANISOU  224  C   ASP A1028    17701  17791  13343   1250    -80     -9       C  
ATOM    225  O   ASP A1028     -16.560  29.224   6.423  1.00126.41           O  
ANISOU  225  O   ASP A1028    17440  17422  13167   1141    -72   -130       O  
ATOM    226  CB  ASP A1028     -13.580  29.483   7.489  1.00131.64           C  
ANISOU  226  CB  ASP A1028    17841  18554  13620   1259   -229     -2       C  
ATOM    227  CG  ASP A1028     -13.756  30.879   6.910  1.00144.86           C  
ANISOU  227  CG  ASP A1028    19467  20196  15377   1104   -264   -157       C  
ATOM    228  OD1 ASP A1028     -14.079  31.813   7.687  1.00145.35           O  
ANISOU  228  OD1 ASP A1028    19513  20324  15389    986   -304   -260       O  
ATOM    229  OD2 ASP A1028     -13.555  31.043   5.685  1.00151.91           O1-
ANISOU  229  OD2 ASP A1028    20348  20993  16377   1104   -251   -175       O1-
ATOM    230  N   ALA A1029     -15.807  27.090   6.704  1.00123.26           N  
ANISOU  230  N   ALA A1029    17133  17025  12676   1374    -19    117       N  
ATOM    231  CA  ALA A1029     -16.697  26.464   5.720  1.00120.77           C  
ANISOU  231  CA  ALA A1029    16944  16477  12465   1369     61    117       C  
ATOM    232  C   ALA A1029     -18.144  26.540   6.214  1.00120.82           C  
ANISOU  232  C   ALA A1029    17029  16404  12474   1255    105     53       C  
ATOM    233  O   ALA A1029     -19.035  26.833   5.422  1.00119.14           O  
ANISOU  233  O   ALA A1029    16850  16056  12362   1172    137    -30       O  
ATOM    234  CB  ALA A1029     -16.292  25.021   5.485  1.00122.26           C  
ANISOU  234  CB  ALA A1029    17240  16586  12626   1525    115    268       C  
ATOM    235  N   LEU A1030     -18.361  26.325   7.530  1.00116.12           N  
ANISOU  235  N   LEU A1030    16450  15912  11759   1251    104     89       N  
ATOM    236  CA  LEU A1030     -19.667  26.426   8.182  1.00115.00           C  
ANISOU  236  CA  LEU A1030    16362  15738  11593   1146    146     32       C  
ATOM    237  C   LEU A1030     -20.083  27.897   8.317  1.00117.32           C  
ANISOU  237  C   LEU A1030    16560  16098  11919   1029    104   -130       C  
ATOM    238  O   LEU A1030     -21.273  28.187   8.236  1.00116.63           O  
ANISOU  238  O   LEU A1030    16503  15939  11874    943    145   -211       O  
ATOM    239  CB  LEU A1030     -19.668  25.735   9.556  1.00116.31           C  
ANISOU  239  CB  LEU A1030    16576  16005  11609   1184    159    129       C  
ATOM    240  CG  LEU A1030     -19.616  24.203   9.555  1.00121.53           C  
ANISOU  240  CG  LEU A1030    17383  16563  12230   1285    221    290       C  
ATOM    241  CD1 LEU A1030     -19.008  23.680  10.838  1.00123.34           C  
ANISOU  241  CD1 LEU A1030    17624  16940  12300   1370    198    406       C  
ATOM    242  CD2 LEU A1030     -20.992  23.597   9.348  1.00123.31           C  
ANISOU  242  CD2 LEU A1030    17738  16623  12490   1194    310    285       C  
ATOM    243  N   THR A1031     -19.108  28.820   8.501  1.00112.90           N  
ANISOU  243  N   THR A1031    15888  15675  11332   1027     22   -178       N  
ATOM    244  CA  THR A1031     -19.342  30.268   8.584  1.00111.77           C  
ANISOU  244  CA  THR A1031    15676  15580  11214    920    -22   -333       C  
ATOM    245  C   THR A1031     -19.898  30.763   7.233  1.00113.65           C  
ANISOU  245  C   THR A1031    15925  15654  11604    875     -2   -417       C  
ATOM    246  O   THR A1031     -20.872  31.523   7.220  1.00113.13           O  
ANISOU  246  O   THR A1031    15867  15540  11577    798     13   -530       O  
ATOM    247  CB  THR A1031     -18.041  31.027   8.979  1.00120.67           C  
ANISOU  247  CB  THR A1031    16694  16882  12273    915   -115   -351       C  
ATOM    248  OG1 THR A1031     -17.441  30.427  10.128  1.00121.62           O  
ANISOU  248  OG1 THR A1031    16799  17164  12248    975   -138   -252       O  
ATOM    249  CG2 THR A1031     -18.274  32.525   9.244  1.00116.98           C  
ANISOU  249  CG2 THR A1031    16185  16457  11805    795   -160   -513       C  
ATOM    250  N   LYS A1032     -19.273  30.330   6.106  1.00108.55           N  
ANISOU  250  N   LYS A1032    15280  14928  11037    932     -1   -358       N  
ATOM    251  CA  LYS A1032     -19.681  30.679   4.737  1.00106.32           C  
ANISOU  251  CA  LYS A1032    15013  14493  10891    898     16   -419       C  
ATOM    252  C   LYS A1032     -21.050  30.072   4.437  1.00108.62           C  
ANISOU  252  C   LYS A1032    15395  14643  11231    872     92   -422       C  
ATOM    253  O   LYS A1032     -21.950  30.787   4.000  1.00107.01           O  
ANISOU  253  O   LYS A1032    15190  14373  11097    802    100   -523       O  
ATOM    254  CB  LYS A1032     -18.643  30.195   3.710  1.00108.35           C  
ANISOU  254  CB  LYS A1032    15256  14715  11199    976      8   -342       C  
ATOM    255  CG  LYS A1032     -17.365  31.021   3.657  1.00117.89           C  
ANISOU  255  CG  LYS A1032    16351  16058  12386    970    -68   -362       C  
ATOM    256  CD  LYS A1032     -16.293  30.268   2.891  1.00127.45           C  
ANISOU  256  CD  LYS A1032    17539  17274  13612   1079    -63   -256       C  
ATOM    257  CE  LYS A1032     -15.027  31.063   2.730  1.00140.24           C  
ANISOU  257  CE  LYS A1032    19030  19043  15213   1061   -134   -272       C  
ATOM    258  NZ  LYS A1032     -13.894  30.197   2.312  1.00152.15           N  
ANISOU  258  NZ  LYS A1032    20496  20616  16699   1197   -127   -149       N  
ATOM    259  N   MET A1033     -21.209  28.766   4.732  1.00106.22           N  
ANISOU  259  N   MET A1033    15174  14304  10879    926    146   -308       N  
ATOM    260  CA  MET A1033     -22.437  27.984   4.576  1.00106.74           C  
ANISOU  260  CA  MET A1033    15337  14254  10967    887    222   -288       C  
ATOM    261  C   MET A1033     -23.618  28.589   5.365  1.00111.38           C  
ANISOU  261  C   MET A1033    15901  14895  11522    797    239   -378       C  
ATOM    262  O   MET A1033     -24.743  28.580   4.858  1.00111.22           O  
ANISOU  262  O   MET A1033    15906  14792  11562    732    282   -424       O  
ATOM    263  CB  MET A1033     -22.186  26.550   5.045  1.00110.53           C  
ANISOU  263  CB  MET A1033    15918  14710  11367    960    268   -142       C  
ATOM    264  CG  MET A1033     -23.183  25.565   4.517  1.00114.91           C  
ANISOU  264  CG  MET A1033    16597  15108  11957    917    346   -104       C  
ATOM    265  SD  MET A1033     -22.889  23.885   5.088  1.00121.29           S  
ANISOU  265  SD  MET A1033    17563  15860  12663    999    405     70       S  
ATOM    266  CE  MET A1033     -21.318  23.572   4.360  1.00118.15           C  
ANISOU  266  CE  MET A1033    17162  15443  12288   1162    371    147       C  
ATOM    267  N   ARG A1034     -23.360  29.102   6.600  1.00107.37           N  
ANISOU  267  N   ARG A1034    15343  14538  10913    794    207   -402       N  
ATOM    268  CA  ARG A1034     -24.365  29.754   7.441  1.00106.45           C  
ANISOU  268  CA  ARG A1034    15201  14493  10751    725    225   -493       C  
ATOM    269  C   ARG A1034     -24.822  31.059   6.787  1.00108.31           C  
ANISOU  269  C   ARG A1034    15381  14693  11079    678    199   -637       C  
ATOM    270  O   ARG A1034     -26.024  31.288   6.662  1.00108.51           O  
ANISOU  270  O   ARG A1034    15407  14686  11137    632    242   -701       O  
ATOM    271  CB  ARG A1034     -23.821  30.036   8.846  1.00106.83           C  
ANISOU  271  CB  ARG A1034    15217  14710  10663    738    190   -489       C  
ATOM    272  CG  ARG A1034     -24.907  30.044   9.906  1.00113.64           C  
ANISOU  272  CG  ARG A1034    16094  15644  11440    686    242   -523       C  
ATOM    273  CD  ARG A1034     -24.682  31.111  10.951  1.00118.46           C  
ANISOU  273  CD  ARG A1034    16649  16402  11959    666    197   -616       C  
ATOM    274  NE  ARG A1034     -25.951  31.494  11.563  1.00125.49           N  
ANISOU  274  NE  ARG A1034    17537  17332  12813    615    253   -701       N  
ATOM    275  CZ  ARG A1034     -26.120  31.766  12.851  1.00136.36           C  
ANISOU  275  CZ  ARG A1034    18907  18846  14058    598    260   -733       C  
ATOM    276  NH1 ARG A1034     -25.090  31.711  13.687  1.00132.10           N  
ANISOU  276  NH1 ARG A1034    18362  18421  13408    622    206   -686       N  
ATOM    277  NH2 ARG A1034     -27.317  32.096  13.314  1.00114.75           N1+
ANISOU  277  NH2 ARG A1034    16162  16146  11291    560    321   -811       N1+
ATOM    278  N   ALA A1035     -23.870  31.891   6.333  1.00102.67           N  
ANISOU  278  N   ALA A1035    14619  13987  10403    692    131   -682       N  
ATOM    279  CA  ALA A1035     -24.180  33.156   5.682  1.00101.15           C  
ANISOU  279  CA  ALA A1035    14395  13745  10294    653    102   -810       C  
ATOM    280  C   ALA A1035     -24.876  32.946   4.346  1.00103.85           C  
ANISOU  280  C   ALA A1035    14761  13940  10758    645    134   -814       C  
ATOM    281  O   ALA A1035     -25.753  33.735   4.005  1.00103.30           O  
ANISOU  281  O   ALA A1035    14677  13830  10741    616    141   -911       O  
ATOM    282  CB  ALA A1035     -22.923  33.985   5.510  1.00101.76           C  
ANISOU  282  CB  ALA A1035    14428  13864  10372    651     24   -840       C  
ATOM    283  N   ALA A1036     -24.524  31.872   3.611  1.00100.02           N  
ANISOU  283  N   ALA A1036    14316  13378  10310    676    155   -711       N  
ATOM    284  CA  ALA A1036     -25.148  31.568   2.315  1.00 99.43           C  
ANISOU  284  CA  ALA A1036    14273  13165  10340    659    184   -711       C  
ATOM    285  C   ALA A1036     -26.547  30.957   2.483  1.00103.28           C  
ANISOU  285  C   ALA A1036    14793  13630  10819    613    252   -707       C  
ATOM    286  O   ALA A1036     -27.386  31.139   1.596  1.00102.74           O  
ANISOU  286  O   ALA A1036    14721  13488  10828    577    266   -753       O  
ATOM    287  CB  ALA A1036     -24.256  30.658   1.475  1.00 99.85           C  
ANISOU  287  CB  ALA A1036    14371  13142  10427    709    188   -611       C  
ATOM    288  N   ALA A1037     -26.806  30.254   3.616  1.00 99.14           N  
ANISOU  288  N   ALA A1037    14294  13180  10195    607    291   -651       N  
ATOM    289  CA  ALA A1037     -28.117  29.663   3.905  1.00 98.82           C  
ANISOU  289  CA  ALA A1037    14276  13142  10128    544    360   -642       C  
ATOM    290  C   ALA A1037     -29.133  30.764   4.263  1.00102.42           C  
ANISOU  290  C   ALA A1037    14653  13676  10586    512    363   -764       C  
ATOM    291  O   ALA A1037     -30.278  30.716   3.800  1.00102.79           O  
ANISOU  291  O   ALA A1037    14681  13703  10672    464    399   -797       O  
ATOM    292  CB  ALA A1037     -28.008  28.657   5.036  1.00100.43           C  
ANISOU  292  CB  ALA A1037    14538  13407  10216    545    400   -544       C  
ATOM    293  N   LEU A1038     -28.696  31.770   5.058  1.00 97.25           N  
ANISOU  293  N   LEU A1038    13953  13113   9883    543    323   -834       N  
ATOM    294  CA  LEU A1038     -29.506  32.920   5.474  1.00 96.24           C  
ANISOU  294  CA  LEU A1038    13767  13053   9746    539    325   -958       C  
ATOM    295  C   LEU A1038     -29.790  33.854   4.302  1.00 97.11           C  
ANISOU  295  C   LEU A1038    13851  13074   9971    550    293  -1042       C  
ATOM    296  O   LEU A1038     -30.850  34.471   4.255  1.00 96.37           O  
ANISOU  296  O   LEU A1038    13716  13004   9895    551    316  -1122       O  
ATOM    297  CB  LEU A1038     -28.843  33.688   6.635  1.00 96.80           C  
ANISOU  297  CB  LEU A1038    13826  13230   9725    562    289  -1010       C  
ATOM    298  CG  LEU A1038     -28.680  32.931   7.953  1.00102.44           C  
ANISOU  298  CG  LEU A1038    14559  14057  10305    555    318   -938       C  
ATOM    299  CD1 LEU A1038     -27.648  33.595   8.836  1.00103.20           C  
ANISOU  299  CD1 LEU A1038    14649  14245  10318    575    259   -971       C  
ATOM    300  CD2 LEU A1038     -30.009  32.768   8.679  1.00105.70           C  
ANISOU  300  CD2 LEU A1038    14952  14553  10656    522    393   -966       C  
ATOM    301  N   ASP A1039     -28.848  33.939   3.357  1.00 93.04           N  
ANISOU  301  N   ASP A1039    13358  12465   9527    566    243  -1019       N  
ATOM    302  CA  ASP A1039     -28.957  34.734   2.127  1.00 92.40           C  
ANISOU  302  CA  ASP A1039    13267  12286   9554    575    209  -1080       C  
ATOM    303  C   ASP A1039     -29.940  34.073   1.139  1.00 92.80           C  
ANISOU  303  C   ASP A1039    13317  12270   9671    546    248  -1049       C  
ATOM    304  O   ASP A1039     -30.769  34.776   0.557  1.00 90.05           O  
ANISOU  304  O   ASP A1039    12936  11902   9377    552    244  -1120       O  
ATOM    305  CB  ASP A1039     -27.569  34.884   1.473  1.00 94.63           C  
ANISOU  305  CB  ASP A1039    13572  12506   9878    588    151  -1049       C  
ATOM    306  CG  ASP A1039     -27.254  36.275   0.965  1.00112.20           C  
ANISOU  306  CG  ASP A1039    15790  14687  12155    594     96  -1144       C  
ATOM    307  OD1 ASP A1039     -27.052  37.188   1.811  1.00115.56           O  
ANISOU  307  OD1 ASP A1039    16211  15173  12524    595     71  -1218       O  
ATOM    308  OD2 ASP A1039     -27.179  36.449  -0.274  1.00118.99           O1-
ANISOU  308  OD2 ASP A1039    16661  15447  13104    593     77  -1144       O1-
ATOM    309  N   ALA A1040     -29.836  32.725   0.960  1.00 89.78           N  
ANISOU  309  N   ALA A1040    12981  11856   9277    516    283   -944       N  
ATOM    310  CA  ALA A1040     -30.692  31.922   0.079  1.00 90.08           C  
ANISOU  310  CA  ALA A1040    13037  11831   9359    464    321   -907       C  
ATOM    311  C   ALA A1040     -32.150  31.833   0.560  1.00 96.50           C  
ANISOU  311  C   ALA A1040    13797  12734  10135    415    374   -938       C  
ATOM    312  O   ALA A1040     -33.041  31.777  -0.289  1.00 96.06           O  
ANISOU  312  O   ALA A1040    13715  12654  10130    376    384   -956       O  
ATOM    313  CB  ALA A1040     -30.118  30.528  -0.104  1.00 90.83           C  
ANISOU  313  CB  ALA A1040    13221  11857   9434    446    349   -791       C  
ATOM    314  N   GLN A1041     -32.407  31.837   1.899  1.00 94.57           N  
ANISOU  314  N   GLN A1041    13530  12607   9796    415    406   -946       N  
ATOM    315  CA  GLN A1041     -33.779  31.774   2.427  1.00 95.19           C  
ANISOU  315  CA  GLN A1041    13545  12797   9827    369    463   -975       C  
ATOM    316  C   GLN A1041     -34.575  33.057   2.155  1.00101.82           C  
ANISOU  316  C   GLN A1041    14293  13685  10709    418    446  -1091       C  
ATOM    317  O   GLN A1041     -35.807  33.032   2.204  1.00103.20           O  
ANISOU  317  O   GLN A1041    14395  13950  10868    388    489  -1116       O  
ATOM    318  CB  GLN A1041     -33.841  31.359   3.909  1.00 96.60           C  
ANISOU  318  CB  GLN A1041    13729  13090   9883    353    509   -944       C  
ATOM    319  CG  GLN A1041     -33.434  32.393   4.925  1.00101.75           C  
ANISOU  319  CG  GLN A1041    14353  13828  10481    423    486  -1020       C  
ATOM    320  CD  GLN A1041     -33.860  32.016   6.331  1.00110.91           C  
ANISOU  320  CD  GLN A1041    15503  15126  11513    395    544  -1001       C  
ATOM    321  OE1 GLN A1041     -34.700  31.133   6.549  1.00 98.28           O  
ANISOU  321  OE1 GLN A1041    13899  13575   9869    320    609   -945       O  
ATOM    322  NE2 GLN A1041     -33.293  32.696   7.326  1.00103.22           N  
ANISOU  322  NE2 GLN A1041    14529  14221  10467    446    522  -1048       N  
ATOM    323  N   LYS A1042     -33.871  34.155   1.840  1.00 98.58           N  
ANISOU  323  N   LYS A1042    13891  13217  10349    493    385  -1156       N  
ATOM    324  CA  LYS A1042     -34.455  35.446   1.477  1.00 99.02           C  
ANISOU  324  CA  LYS A1042    13893  13280  10449    559    361  -1262       C  
ATOM    325  C   LYS A1042     -34.984  35.416   0.009  1.00105.91           C  
ANISOU  325  C   LYS A1042    14745  14079  11419    546    342  -1256       C  
ATOM    326  O   LYS A1042     -35.955  36.113  -0.307  1.00106.71           O  
ANISOU  326  O   LYS A1042    14779  14224  11544    589    344  -1319       O  
ATOM    327  CB  LYS A1042     -33.407  36.560   1.635  1.00100.19           C  
ANISOU  327  CB  LYS A1042    14087  13372  10609    622    302  -1325       C  
ATOM    328  CG  LYS A1042     -32.989  36.841   3.072  1.00106.07           C  
ANISOU  328  CG  LYS A1042    14845  14205  11250    636    313  -1356       C  
ATOM    329  CD  LYS A1042     -32.015  38.000   3.139  1.00110.99           C  
ANISOU  329  CD  LYS A1042    15517  14771  11882    675    250  -1426       C  
ATOM    330  CE  LYS A1042     -31.664  38.383   4.548  1.00121.84           C  
ANISOU  330  CE  LYS A1042    16908  16241  13146    683    255  -1473       C  
ATOM    331  NZ  LYS A1042     -30.489  39.292   4.576  1.00132.78           N1+
ANISOU  331  NZ  LYS A1042    18350  17569  14530    683    187  -1522       N1+
ATOM    332  N   ALA A1043     -34.346  34.609  -0.874  1.00102.93           N  
ANISOU  332  N   ALA A1043    14426  13594  11089    496    323  -1179       N  
ATOM    333  CA  ALA A1043     -34.706  34.474  -2.295  1.00103.09           C  
ANISOU  333  CA  ALA A1043    14443  13536  11191    472    301  -1166       C  
ATOM    334  C   ALA A1043     -35.989  33.693  -2.497  1.00110.46           C  
ANISOU  334  C   ALA A1043    15319  14545  12104    393    349  -1139       C  
ATOM    335  O   ALA A1043     -36.409  32.967  -1.599  1.00111.16           O  
ANISOU  335  O   ALA A1043    15395  14721  12118    337    404  -1105       O  
ATOM    336  CB  ALA A1043     -33.569  33.814  -3.076  1.00102.77           C  
ANISOU  336  CB  ALA A1043    14492  13364  11191    446    276  -1096       C  
ATOM    337  N   THR A1044     -36.614  33.850  -3.676  1.00109.02           N  
ANISOU  337  N   THR A1044    15102  14337  11982    381    325  -1152       N  
ATOM    338  CA  THR A1044     -37.834  33.131  -4.059  1.00110.36           C  
ANISOU  338  CA  THR A1044    15209  14588  12135    287    358  -1128       C  
ATOM    339  C   THR A1044     -37.482  32.118  -5.169  1.00113.59           C  
ANISOU  339  C   THR A1044    15706  14875  12580    193    348  -1060       C  
ATOM    340  O   THR A1044     -36.977  32.543  -6.207  1.00112.23           O  
ANISOU  340  O   THR A1044    15568  14599  12477    232    297  -1071       O  
ATOM    341  CB  THR A1044     -39.024  34.083  -4.362  1.00122.89           C  
ANISOU  341  CB  THR A1044    16666  16289  13738    346    345  -1199       C  
ATOM    342  OG1 THR A1044     -40.096  33.323  -4.922  1.00125.43           O  
ANISOU  342  OG1 THR A1044    16921  16692  14044    237    366  -1167       O  
ATOM    343  CG2 THR A1044     -38.662  35.236  -5.300  1.00122.05           C  
ANISOU  343  CG2 THR A1044    16573  16088  13711    453    275  -1248       C  
ATOM    344  N   PRO A1045     -37.669  30.782  -4.951  1.00110.41           N  
ANISOU  344  N   PRO A1045    15356  14470  12125     71    400   -989       N  
ATOM    345  CA  PRO A1045     -37.282  29.801  -5.982  1.00110.10           C  
ANISOU  345  CA  PRO A1045    15427  14294  12111    -11    396   -930       C  
ATOM    346  C   PRO A1045     -37.989  29.992  -7.327  1.00116.09           C  
ANISOU  346  C   PRO A1045    16141  15050  12919    -53    359   -956       C  
ATOM    347  O   PRO A1045     -39.147  30.425  -7.321  1.00117.01           O  
ANISOU  347  O   PRO A1045    16129  15307  13022    -71    357   -995       O  
ATOM    348  CB  PRO A1045     -37.660  28.448  -5.361  1.00112.40           C  
ANISOU  348  CB  PRO A1045    15781  14605  12323   -142    465   -861       C  
ATOM    349  CG  PRO A1045     -37.810  28.691  -3.940  1.00117.37           C  
ANISOU  349  CG  PRO A1045    16355  15352  12888   -108    501   -869       C  
ATOM    350  CD  PRO A1045     -38.251  30.107  -3.776  1.00112.91           C  
ANISOU  350  CD  PRO A1045    15651  14899  12351     -1    467   -959       C  
ATOM    351  N   PRO A1046     -37.341  29.659  -8.482  1.00112.31           N  
ANISOU  351  N   PRO A1046    15760  14425  12487    -68    330   -932       N  
ATOM    352  CA  PRO A1046     -38.032  29.792  -9.782  1.00112.05           C  
ANISOU  352  CA  PRO A1046    15690  14396  12489   -118    292   -953       C  
ATOM    353  C   PRO A1046     -39.339  28.992  -9.817  1.00115.77           C  
ANISOU  353  C   PRO A1046    16109  14977  12901   -275    325   -939       C  
ATOM    354  O   PRO A1046     -40.351  29.502 -10.309  1.00116.04           O  
ANISOU  354  O   PRO A1046    16018  15131  12940   -291    295   -976       O  
ATOM    355  CB  PRO A1046     -37.001  29.270 -10.788  1.00113.21           C  
ANISOU  355  CB  PRO A1046    15981  14362  12671   -125    277   -918       C  
ATOM    356  CG  PRO A1046     -35.683  29.416 -10.087  1.00117.25           C  
ANISOU  356  CG  PRO A1046    16559  14798  13192    -21    285   -898       C  
ATOM    357  CD  PRO A1046     -35.982  29.109  -8.661  1.00113.28           C  
ANISOU  357  CD  PRO A1046    16028  14389  12625    -37    334   -882       C  
ATOM    358  N   LYS A1047     -39.326  27.777  -9.209  1.00111.24           N  
ANISOU  358  N   LYS A1047    15626  14377  12263   -389    388   -883       N  
ATOM    359  CA  LYS A1047     -40.469  26.872  -9.030  1.00111.80           C  
ANISOU  359  CA  LYS A1047    15669  14548  12261   -569    433   -859       C  
ATOM    360  C   LYS A1047     -41.671  27.621  -8.383  1.00114.91           C  
ANISOU  360  C   LYS A1047    15855  15179  12625   -557    437   -905       C  
ATOM    361  O   LYS A1047     -42.799  27.496  -8.871  1.00115.01           O  
ANISOU  361  O   LYS A1047    15766  15322  12613   -665    430   -918       O  
ATOM    362  CB  LYS A1047     -40.033  25.673  -8.151  1.00114.83           C  
ANISOU  362  CB  LYS A1047    16200  14852  12578   -648    505   -789       C  
ATOM    363  CG  LYS A1047     -41.035  24.520  -8.055  1.00130.01           C  
ANISOU  363  CG  LYS A1047    18152  16829  14418   -869    559   -751       C  
ATOM    364  CD  LYS A1047     -40.701  23.565  -6.901  1.00137.21           C  
ANISOU  364  CD  LYS A1047    19190  17689  15255   -920    633   -681       C  
ATOM    365  CE  LYS A1047     -41.790  22.540  -6.662  1.00140.73           C  
ANISOU  365  CE  LYS A1047    19653  18210  15608  -1153    691   -645       C  
ATOM    366  NZ  LYS A1047     -41.640  21.865  -5.344  1.00142.55           N1+
ANISOU  366  NZ  LYS A1047    19966  18440  15758  -1189    763   -581       N1+
ATOM    367  N   LEU A1048     -41.403  28.428  -7.318  1.00109.88           N  
ANISOU  367  N   LEU A1048    15155  14606  11989   -419    446   -933       N  
ATOM    368  CA  LEU A1048     -42.412  29.196  -6.580  1.00109.57           C  
ANISOU  368  CA  LEU A1048    14932  14782  11917   -373    460   -981       C  
ATOM    369  C   LEU A1048     -42.360  30.713  -6.854  1.00113.77           C  
ANISOU  369  C   LEU A1048    15369  15346  12514   -182    402  -1054       C  
ATOM    370  O   LEU A1048     -42.694  31.490  -5.957  1.00113.91           O  
ANISOU  370  O   LEU A1048    15288  15484  12508    -81    420  -1098       O  
ATOM    371  CB  LEU A1048     -42.328  28.945  -5.052  1.00109.53           C  
ANISOU  371  CB  LEU A1048    14932  14845  11840   -372    528   -962       C  
ATOM    372  CG  LEU A1048     -41.930  27.576  -4.493  1.00113.66           C  
ANISOU  372  CG  LEU A1048    15603  15283  12299   -506    588   -880       C  
ATOM    373  CD1 LEU A1048     -41.674  27.679  -3.015  1.00114.05           C  
ANISOU  373  CD1 LEU A1048    15649  15398  12287   -450    636   -872       C  
ATOM    374  CD2 LEU A1048     -43.003  26.542  -4.723  1.00116.29           C  
ANISOU  374  CD2 LEU A1048    15920  15699  12568   -722    630   -842       C  
ATOM    375  N   GLU A1049     -41.970  31.144  -8.077  1.00110.54           N  
ANISOU  375  N   GLU A1049    14997  14826  12178   -133    336  -1067       N  
ATOM    376  CA  GLU A1049     -41.906  32.579  -8.437  1.00110.42           C  
ANISOU  376  CA  GLU A1049    14918  14815  12222     42    278  -1129       C  
ATOM    377  C   GLU A1049     -43.308  33.211  -8.486  1.00116.31           C  
ANISOU  377  C   GLU A1049    15476  15772  12944     80    272  -1171       C  
ATOM    378  O   GLU A1049     -43.477  34.393  -8.176  1.00116.18           O  
ANISOU  378  O   GLU A1049    15390  15808  12944    243    256  -1227       O  
ATOM    379  CB  GLU A1049     -41.169  32.790  -9.771  1.00110.88           C  
ANISOU  379  CB  GLU A1049    15070  14707  12354     66    214  -1122       C  
ATOM    380  N   ASP A1050     -44.310  32.390  -8.842  1.00114.54           N  
ANISOU  380  N   ASP A1050    15173  15674  12674    -73    288  -1141       N  
ATOM    381  CA  ASP A1050     -45.737  32.720  -8.940  1.00115.71           C  
ANISOU  381  CA  ASP A1050    15120  16063  12782    -72    287  -1165       C  
ATOM    382  C   ASP A1050     -46.436  32.706  -7.564  1.00117.83           C  
ANISOU  382  C   ASP A1050    15272  16524  12974    -68    362  -1180       C  
ATOM    383  O   ASP A1050     -47.640  32.974  -7.487  1.00118.96           O  
ANISOU  383  O   ASP A1050    15229  16899  13073    -59    373  -1199       O  
ATOM    384  CB  ASP A1050     -46.422  31.690  -9.870  1.00118.88           C  
ANISOU  384  CB  ASP A1050    15497  16522  13151   -279    275  -1122       C  
ATOM    385  CG  ASP A1050     -46.342  30.252  -9.365  1.00135.46           C  
ANISOU  385  CG  ASP A1050    17690  18592  15188   -495    341  -1067       C  
ATOM    386  OD1 ASP A1050     -45.213  29.704  -9.296  1.00136.11           O1-
ANISOU  386  OD1 ASP A1050    17964  18459  15294   -518    354  -1037       O1-
ATOM    387  OD2 ASP A1050     -47.406  29.678  -9.035  1.00144.54           O  
ANISOU  387  OD2 ASP A1050    18723  19935  16260   -639    381  -1052       O  
ATOM    388  N   LYS A1051     -45.686  32.361  -6.495  1.00111.29           N  
ANISOU  388  N   LYS A1051    14548  15613  12122    -77    414  -1167       N  
ATOM    389  CA  LYS A1051     -46.202  32.209  -5.138  1.00110.88           C  
ANISOU  389  CA  LYS A1051    14417  15724  11988    -93    491  -1173       C  
ATOM    390  C   LYS A1051     -45.852  33.370  -4.202  1.00113.86           C  
ANISOU  390  C   LYS A1051    14781  16110  12370    113    502  -1238       C  
ATOM    391  O   LYS A1051     -44.770  33.966  -4.298  1.00111.51           O  
ANISOU  391  O   LYS A1051    14605  15631  12132    224    462  -1259       O  
ATOM    392  CB  LYS A1051     -45.766  30.862  -4.547  1.00112.43           C  
ANISOU  392  CB  LYS A1051    14740  15848  12131   -274    548  -1103       C  
ATOM    393  CG  LYS A1051     -46.055  29.672  -5.470  1.00119.02           C  
ANISOU  393  CG  LYS A1051    15627  16642  12953   -489    543  -1043       C  
ATOM    394  CD  LYS A1051     -47.026  28.647  -4.891  1.00130.17           C  
ANISOU  394  CD  LYS A1051    16974  18223  14261   -697    615  -1000       C  
ATOM    395  CE  LYS A1051     -48.480  29.051  -4.963  1.00144.17           C  
ANISOU  395  CE  LYS A1051    18502  20286  15988   -718    622  -1033       C  
ATOM    396  NZ  LYS A1051     -48.934  29.683  -3.695  1.00155.56           N1+
ANISOU  396  NZ  LYS A1051    19813  21915  17376   -606    680  -1069       N1+
ATOM    397  N   SER A1052     -46.811  33.684  -3.304  1.00111.88           N  
ANISOU  397  N   SER A1052    14378  16083  12047    156    559  -1271       N  
ATOM    398  CA  SER A1052     -46.772  34.747  -2.291  1.00111.53           C  
ANISOU  398  CA  SER A1052    14300  16096  11980    342    586  -1342       C  
ATOM    399  C   SER A1052     -45.649  34.533  -1.283  1.00113.17           C  
ANISOU  399  C   SER A1052    14661  16171  12166    337    613  -1334       C  
ATOM    400  O   SER A1052     -45.469  33.405  -0.822  1.00112.56           O  
ANISOU  400  O   SER A1052    14640  16088  12039    178    656  -1269       O  
ATOM    401  CB  SER A1052     -48.109  34.820  -1.553  1.00116.65           C  
ANISOU  401  CB  SER A1052    14749  17036  12538    349    657  -1365       C  
ATOM    402  OG  SER A1052     -48.168  35.903  -0.640  1.00125.74           O  
ANISOU  402  OG  SER A1052    15867  18246  13661    546    687  -1445       O  
ATOM    403  N   PRO A1053     -44.915  35.592  -0.870  1.00108.66           N  
ANISOU  403  N   PRO A1053    14161  15502  11621    505    590  -1398       N  
ATOM    404  CA  PRO A1053     -43.845  35.397   0.125  1.00107.92           C  
ANISOU  404  CA  PRO A1053    14200  15310  11496    494    610  -1390       C  
ATOM    405  C   PRO A1053     -44.302  34.724   1.421  1.00113.03           C  
ANISOU  405  C   PRO A1053    14800  16116  12028    413    697  -1367       C  
ATOM    406  O   PRO A1053     -43.474  34.164   2.127  1.00111.88           O  
ANISOU  406  O   PRO A1053    14766  15897  11847    354    714  -1326       O  
ATOM    407  CB  PRO A1053     -43.319  36.814   0.359  1.00109.37           C  
ANISOU  407  CB  PRO A1053    14430  15417  11709    685    575  -1481       C  
ATOM    408  CG  PRO A1053     -43.640  37.533  -0.898  1.00113.35           C  
ANISOU  408  CG  PRO A1053    14899  15873  12297    770    514  -1508       C  
ATOM    409  CD  PRO A1053     -44.979  37.001  -1.306  1.00109.95           C  
ANISOU  409  CD  PRO A1053    14305  15633  11840    703    543  -1478       C  
ATOM    410  N   ASP A1054     -45.620  34.725   1.695  1.00111.72           N  
ANISOU  410  N   ASP A1054    14466  16179  11802    403    754  -1384       N  
ATOM    411  CA  ASP A1054     -46.206  34.104   2.879  1.00113.09           C  
ANISOU  411  CA  ASP A1054    14577  16535  11859    315    845  -1361       C  
ATOM    412  C   ASP A1054     -47.030  32.834   2.567  1.00117.38           C  
ANISOU  412  C   ASP A1054    15048  17190  12359     97    884  -1277       C  
ATOM    413  O   ASP A1054     -47.709  32.318   3.460  1.00118.03           O  
ANISOU  413  O   ASP A1054    15056  17452  12339      7    965  -1254       O  
ATOM    414  CB  ASP A1054     -47.021  35.135   3.673  1.00116.84           C  
ANISOU  414  CB  ASP A1054    14917  17204  12272    474    895  -1453       C  
ATOM    415  CG  ASP A1054     -46.203  36.333   4.116  1.00130.92           C  
ANISOU  415  CG  ASP A1054    16800  18867  14077    664    865  -1540       C  
ATOM    416  OD1 ASP A1054     -45.445  36.203   5.107  1.00130.97           O  
ANISOU  416  OD1 ASP A1054    16910  18823  14028    649    886  -1540       O  
ATOM    417  OD2 ASP A1054     -46.317  37.402   3.468  1.00138.98           O1-
ANISOU  417  OD2 ASP A1054    17800  19842  15163    823    819  -1608       O1-
ATOM    418  N   SER A1055     -46.941  32.312   1.313  1.00113.30           N  
ANISOU  418  N   SER A1055    14569  16564  11915      1    829  -1231       N  
ATOM    419  CA  SER A1055     -47.632  31.091   0.871  1.00113.77           C  
ANISOU  419  CA  SER A1055    14594  16696  11939   -226    856  -1154       C  
ATOM    420  C   SER A1055     -47.067  29.863   1.595  1.00119.67           C  
ANISOU  420  C   SER A1055    15493  17356  12621   -390    906  -1069       C  
ATOM    421  O   SER A1055     -45.879  29.869   1.915  1.00119.19           O  
ANISOU  421  O   SER A1055    15592  17110  12585   -327    885  -1056       O  
ATOM    422  CB  SER A1055     -47.503  30.910  -0.638  1.00115.40           C  
ANISOU  422  CB  SER A1055    14837  16775  12235   -274    779  -1135       C  
ATOM    423  OG  SER A1055     -46.153  30.814  -1.053  1.00117.87           O  
ANISOU  423  OG  SER A1055    15347  16816  12621   -239    726  -1115       O  
ATOM    424  N   PRO A1056     -47.868  28.802   1.869  1.00117.98           N  
ANISOU  424  N   PRO A1056    15238  17270  12319   -602    972  -1007       N  
ATOM    425  CA  PRO A1056     -47.328  27.637   2.604  1.00117.91           C  
ANISOU  425  CA  PRO A1056    15397  17164  12241   -748   1023   -919       C  
ATOM    426  C   PRO A1056     -46.057  26.989   2.026  1.00119.75           C  
ANISOU  426  C   PRO A1056    15863  17099  12537   -770    975   -861       C  
ATOM    427  O   PRO A1056     -45.240  26.468   2.792  1.00119.72           O  
ANISOU  427  O   PRO A1056    16009  16987  12493   -775   1000   -807       O  
ATOM    428  CB  PRO A1056     -48.504  26.658   2.623  1.00121.40           C  
ANISOU  428  CB  PRO A1056    15756  17777  12592   -993   1088   -865       C  
ATOM    429  CG  PRO A1056     -49.704  27.520   2.510  1.00126.95           C  
ANISOU  429  CG  PRO A1056    16199  18754  13282   -928   1096   -937       C  
ATOM    430  CD  PRO A1056     -49.308  28.627   1.584  1.00121.15           C  
ANISOU  430  CD  PRO A1056    15439  17923  12669   -719   1004  -1010       C  
ATOM    431  N   GLU A1057     -45.883  27.033   0.694  1.00113.75           N  
ANISOU  431  N   GLU A1057    15131  16218  11870   -772    907   -870       N  
ATOM    432  CA  GLU A1057     -44.712  26.466   0.010  1.00111.75           C  
ANISOU  432  CA  GLU A1057    15087  15693  11680   -779    863   -822       C  
ATOM    433  C   GLU A1057     -43.461  27.305   0.310  1.00111.90           C  
ANISOU  433  C   GLU A1057    15175  15586  11758   -568    818   -855       C  
ATOM    434  O   GLU A1057     -42.388  26.757   0.571  1.00110.54           O  
ANISOU  434  O   GLU A1057    15169  15248  11582   -556    817   -799       O  
ATOM    435  CB  GLU A1057     -44.951  26.379  -1.513  1.00112.74           C  
ANISOU  435  CB  GLU A1057    15207  15749  11880   -836    805   -833       C  
ATOM    436  CG  GLU A1057     -46.236  25.670  -1.921  1.00125.90           C  
ANISOU  436  CG  GLU A1057    16784  17564  13488  -1055    836   -811       C  
ATOM    437  CD  GLU A1057     -47.480  26.526  -2.102  1.00149.73           C  
ANISOU  437  CD  GLU A1057    19544  20846  16499  -1021    825   -877       C  
ATOM    438  OE1 GLU A1057     -47.594  27.588  -1.446  1.00143.09           O  
ANISOU  438  OE1 GLU A1057    18581  20124  15662   -841    829   -937       O  
ATOM    439  OE2 GLU A1057     -48.350  26.123  -2.908  1.00146.16           O1-
ANISOU  439  OE2 GLU A1057    19015  20486  16032  -1174    813   -870       O1-
ATOM    440  N   MET A1058     -43.627  28.638   0.290  1.00106.31           N  
ANISOU  440  N   MET A1058    14336  14963  11093   -402    781   -946       N  
ATOM    441  CA  MET A1058     -42.600  29.643   0.545  1.00104.27           C  
ANISOU  441  CA  MET A1058    14121  14613  10886   -212    735   -996       C  
ATOM    442  C   MET A1058     -42.154  29.636   2.020  1.00105.26           C  
ANISOU  442  C   MET A1058    14285  14784  10927   -173    781   -987       C  
ATOM    443  O   MET A1058     -40.979  29.875   2.317  1.00103.64           O  
ANISOU  443  O   MET A1058    14183  14456  10739    -84    748   -983       O  
ATOM    444  CB  MET A1058     -43.138  31.013   0.129  1.00106.95           C  
ANISOU  444  CB  MET A1058    14318  15040  11278    -68    695  -1095       C  
ATOM    445  CG  MET A1058     -42.081  32.002  -0.228  1.00110.03           C  
ANISOU  445  CG  MET A1058    14778  15280  11749     90    625  -1143       C  
ATOM    446  SD  MET A1058     -41.025  31.526  -1.609  1.00113.50           S  
ANISOU  446  SD  MET A1058    15362  15477  12285     53    558  -1092       S  
ATOM    447  CE  MET A1058     -39.480  32.060  -0.938  1.00109.36           C  
ANISOU  447  CE  MET A1058    14953  14825  11773    173    528  -1104       C  
ATOM    448  N   LYS A1059     -43.093  29.336   2.934  1.00100.78           N  
ANISOU  448  N   LYS A1059    13629  14403  10258   -247    856   -979       N  
ATOM    449  CA  LYS A1059     -42.834  29.209   4.363  1.00 99.98           C  
ANISOU  449  CA  LYS A1059    13561  14370  10058   -234    909   -962       C  
ATOM    450  C   LYS A1059     -42.054  27.924   4.625  1.00102.06           C  
ANISOU  450  C   LYS A1059    14002  14495  10280   -342    927   -848       C  
ATOM    451  O   LYS A1059     -41.227  27.894   5.528  1.00100.55           O  
ANISOU  451  O   LYS A1059    13894  14270  10040   -284    931   -825       O  
ATOM    452  CB  LYS A1059     -44.155  29.201   5.145  1.00104.06           C  
ANISOU  452  CB  LYS A1059    13925  15140  10475   -295    990   -982       C  
ATOM    453  N   ASP A1060     -42.318  26.864   3.824  1.00 99.93           N  
ANISOU  453  N   ASP A1060    13798  14144  10024   -495    937   -778       N  
ATOM    454  CA  ASP A1060     -41.658  25.555   3.905  1.00100.11           C  
ANISOU  454  CA  ASP A1060    14015  14011  10012   -598    959   -665       C  
ATOM    455  C   ASP A1060     -40.210  25.623   3.400  1.00101.47           C  
ANISOU  455  C   ASP A1060    14324  13969  10262   -478    893   -646       C  
ATOM    456  O   ASP A1060     -39.330  24.978   3.969  1.00100.69           O  
ANISOU  456  O   ASP A1060    14365  13775  10118   -463    904   -569       O  
ATOM    457  CB  ASP A1060     -42.456  24.493   3.135  1.00103.30           C  
ANISOU  457  CB  ASP A1060    14454  14390  10403   -803    991   -611       C  
ATOM    458  CG  ASP A1060     -41.922  23.085   3.334  1.00122.85           C  
ANISOU  458  CG  ASP A1060    17151  16705  12823   -918   1031   -493       C  
ATOM    459  OD1 ASP A1060     -42.219  22.483   4.389  1.00126.83           O  
ANISOU  459  OD1 ASP A1060    17691  17284  13216  -1005   1100   -433       O  
ATOM    460  OD2 ASP A1060     -41.194  22.588   2.438  1.00129.69           O1-
ANISOU  460  OD2 ASP A1060    18161  17365  13750   -912    996   -458       O1-
ATOM    461  N   PHE A1061     -39.975  26.394   2.325  1.00 96.62           N  
ANISOU  461  N   PHE A1061    13664  13288   9757   -393    824   -711       N  
ATOM    462  CA  PHE A1061     -38.652  26.614   1.755  1.00 95.17           C  
ANISOU  462  CA  PHE A1061    13581  12930   9652   -278    760   -705       C  
ATOM    463  C   PHE A1061     -37.766  27.293   2.806  1.00 97.90           C  
ANISOU  463  C   PHE A1061    13926  13307   9965   -142    741   -725       C  
ATOM    464  O   PHE A1061     -36.645  26.844   3.030  1.00 98.37           O  
ANISOU  464  O   PHE A1061    14103  13261  10012    -97    727   -662       O  
ATOM    465  CB  PHE A1061     -38.769  27.460   0.474  1.00 96.34           C  
ANISOU  465  CB  PHE A1061    13656  13040   9911   -222    696   -780       C  
ATOM    466  CG  PHE A1061     -37.482  27.957  -0.144  1.00 96.99           C  
ANISOU  466  CG  PHE A1061    13806  12972  10075    -99    627   -791       C  
ATOM    467  CD1 PHE A1061     -36.613  27.080  -0.784  1.00 99.79           C  
ANISOU  467  CD1 PHE A1061    14306  13156  10455   -119    619   -719       C  
ATOM    468  CD2 PHE A1061     -37.171  29.313  -0.146  1.00 98.88           C  
ANISOU  468  CD2 PHE A1061    13966  13242  10363     32    575   -878       C  
ATOM    469  CE1 PHE A1061     -35.434  27.547  -1.383  1.00 99.76           C  
ANISOU  469  CE1 PHE A1061    14347  13037  10522     -9    560   -729       C  
ATOM    470  CE2 PHE A1061     -36.000  29.780  -0.762  1.00100.42           C  
ANISOU  470  CE2 PHE A1061    14218  13309  10629    123    514   -887       C  
ATOM    471  CZ  PHE A1061     -35.135  28.894  -1.369  1.00 97.62           C  
ANISOU  471  CZ  PHE A1061    13987  12809  10297    102    507   -811       C  
ATOM    472  N   ARG A1062     -38.302  28.316   3.499  1.00 92.72           N  
ANISOU  472  N   ARG A1062    13140  12807   9282    -81    746   -810       N  
ATOM    473  CA  ARG A1062     -37.614  29.057   4.555  1.00 91.39           C  
ANISOU  473  CA  ARG A1062    12965  12690   9069     31    731   -847       C  
ATOM    474  C   ARG A1062     -37.337  28.217   5.807  1.00 98.45           C  
ANISOU  474  C   ARG A1062    13935  13630   9843    -13    782   -764       C  
ATOM    475  O   ARG A1062     -36.259  28.351   6.389  1.00 98.33           O  
ANISOU  475  O   ARG A1062    13981  13581   9800     64    751   -745       O  
ATOM    476  CB  ARG A1062     -38.366  30.338   4.895  1.00 87.18           C  
ANISOU  476  CB  ARG A1062    12292  12300   8533    106    732   -965       C  
ATOM    477  CG  ARG A1062     -38.252  31.390   3.795  1.00 92.02           C  
ANISOU  477  CG  ARG A1062    12862  12840   9260    196    664  -1046       C  
ATOM    478  CD  ARG A1062     -38.647  32.778   4.252  1.00 92.48           C  
ANISOU  478  CD  ARG A1062    12828  12998   9310    312    657  -1164       C  
ATOM    479  NE  ARG A1062     -40.036  32.812   4.710  1.00 97.38           N  
ANISOU  479  NE  ARG A1062    13326  13804   9871    285    724  -1195       N  
ATOM    480  CZ  ARG A1062     -41.070  33.115   3.935  1.00107.89           C  
ANISOU  480  CZ  ARG A1062    14548  15199  11247    289    727  -1231       C  
ATOM    481  NH1 ARG A1062     -40.881  33.451   2.661  1.00 87.06           N1+
ANISOU  481  NH1 ARG A1062    11921  12444   8715    320    664  -1244       N1+
ATOM    482  NH2 ARG A1062     -42.302  33.098   4.428  1.00 92.14           N  
ANISOU  482  NH2 ARG A1062    12426  13399   9184    264    794  -1253       N  
ATOM    483  N   HIS A1063     -38.288  27.327   6.195  1.00 96.97           N  
ANISOU  483  N   HIS A1063    13744  13520   9579   -145    858   -709       N  
ATOM    484  CA  HIS A1063     -38.182  26.411   7.342  1.00 97.62           C  
ANISOU  484  CA  HIS A1063    13910  13644   9537   -209    916   -617       C  
ATOM    485  C   HIS A1063     -37.022  25.419   7.176  1.00100.62           C  
ANISOU  485  C   HIS A1063    14469  13846   9918   -200    897   -504       C  
ATOM    486  O   HIS A1063     -36.369  25.068   8.159  1.00100.54           O  
ANISOU  486  O   HIS A1063    14532  13849   9820   -165    906   -441       O  
ATOM    487  CB  HIS A1063     -39.512  25.670   7.586  1.00 99.85           C  
ANISOU  487  CB  HIS A1063    14153  14038   9746   -376   1002   -582       C  
ATOM    488  CG  HIS A1063     -39.481  24.722   8.753  1.00104.40           C  
ANISOU  488  CG  HIS A1063    14825  14655  10186   -455   1068   -481       C  
ATOM    489  ND1 HIS A1063     -39.201  25.160  10.039  1.00106.42           N  
ANISOU  489  ND1 HIS A1063    15058  15029  10348   -381   1081   -496       N  
ATOM    490  CD2 HIS A1063     -39.693  23.387   8.787  1.00106.80           C  
ANISOU  490  CD2 HIS A1063    15258  14888  10430   -602   1122   -366       C  
ATOM    491  CE1 HIS A1063     -39.238  24.080  10.800  1.00106.79           C  
ANISOU  491  CE1 HIS A1063    15214  15079  10282   -479   1141   -384       C  
ATOM    492  NE2 HIS A1063     -39.535  22.993  10.094  1.00107.47           N  
ANISOU  492  NE2 HIS A1063    15401  15048  10386   -614   1169   -302       N  
ATOM    493  N   GLY A1064     -36.773  25.002   5.937  1.00 96.90           N  
ANISOU  493  N   GLY A1064    14063  13216   9537   -221    869   -479       N  
ATOM    494  CA  GLY A1064     -35.666  24.123   5.581  1.00 96.83           C  
ANISOU  494  CA  GLY A1064    14222  13028   9542   -188    851   -382       C  
ATOM    495  C   GLY A1064     -34.336  24.749   5.950  1.00100.86           C  
ANISOU  495  C   GLY A1064    14735  13526  10062    -27    788   -391       C  
ATOM    496  O   GLY A1064     -33.488  24.087   6.561  1.00101.82           O  
ANISOU  496  O   GLY A1064    14964  13606  10118     18    792   -297       O  
ATOM    497  N   PHE A1065     -34.185  26.058   5.642  1.00 95.92           N  
ANISOU  497  N   PHE A1065    13989  12949   9507     55    730   -502       N  
ATOM    498  CA  PHE A1065     -32.998  26.839   5.988  1.00 95.06           C  
ANISOU  498  CA  PHE A1065    13863  12851   9404    184    665   -530       C  
ATOM    499  C   PHE A1065     -32.860  27.101   7.493  1.00 99.41           C  
ANISOU  499  C   PHE A1065    14389  13547   9835    212    677   -532       C  
ATOM    500  O   PHE A1065     -31.732  27.170   7.980  1.00 98.76           O  
ANISOU  500  O   PHE A1065    14340  13467   9716    293    635   -497       O  
ATOM    501  CB  PHE A1065     -32.924  28.132   5.182  1.00 95.49           C  
ANISOU  501  CB  PHE A1065    13822  12897   9564    244    603   -647       C  
ATOM    502  CG  PHE A1065     -32.575  27.851   3.746  1.00 96.03           C  
ANISOU  502  CG  PHE A1065    13937  12811   9739    245    575   -628       C  
ATOM    503  CD1 PHE A1065     -31.283  27.486   3.387  1.00 99.15           C  
ANISOU  503  CD1 PHE A1065    14412  13105  10157    313    539   -565       C  
ATOM    504  CD2 PHE A1065     -33.545  27.908   2.756  1.00 97.84           C  
ANISOU  504  CD2 PHE A1065    14127  13009  10037    179    586   -668       C  
ATOM    505  CE1 PHE A1065     -30.968  27.177   2.062  1.00 99.42           C  
ANISOU  505  CE1 PHE A1065    14495  12999  10280    316    521   -547       C  
ATOM    506  CE2 PHE A1065     -33.227  27.621   1.429  1.00100.22           C  
ANISOU  506  CE2 PHE A1065    14481  13171  10427    174    561   -651       C  
ATOM    507  CZ  PHE A1065     -31.940  27.262   1.091  1.00 98.30           C  
ANISOU  507  CZ  PHE A1065    14326  12820  10205    243    532   -593       C  
ATOM    508  N   ASP A1066     -33.996  27.200   8.231  1.00 96.98           N  
ANISOU  508  N   ASP A1066    14020  13372   9458    144    736   -566       N  
ATOM    509  CA  ASP A1066     -34.020  27.381   9.693  1.00 97.69           C  
ANISOU  509  CA  ASP A1066    14090  13609   9417    156    761   -568       C  
ATOM    510  C   ASP A1066     -33.404  26.174  10.359  1.00102.32           C  
ANISOU  510  C   ASP A1066    14806  14163   9909    141    784   -425       C  
ATOM    511  O   ASP A1066     -32.610  26.350  11.275  1.00102.11           O  
ANISOU  511  O   ASP A1066    14794  14201   9800    208    756   -405       O  
ATOM    512  CB  ASP A1066     -35.452  27.575  10.222  1.00100.33           C  
ANISOU  512  CB  ASP A1066    14334  14091   9694     77    834   -622       C  
ATOM    513  CG  ASP A1066     -35.990  28.987  10.136  1.00109.13           C  
ANISOU  513  CG  ASP A1066    15317  15296  10851    138    816   -772       C  
ATOM    514  OD1 ASP A1066     -35.169  29.932   9.997  1.00107.52           O  
ANISOU  514  OD1 ASP A1066    15104  15057  10693    237    746   -840       O  
ATOM    515  OD2 ASP A1066     -37.233  29.154  10.224  1.00117.32           O1-
ANISOU  515  OD2 ASP A1066    16262  16444  11870     87    874   -819       O1-
ATOM    516  N   ILE A1067     -33.753  24.948   9.874  1.00 99.94           N  
ANISOU  516  N   ILE A1067    14605  13755   9611     54    833   -325       N  
ATOM    517  CA  ILE A1067     -33.227  23.661  10.357  1.00101.03           C  
ANISOU  517  CA  ILE A1067    14901  13823   9663     42    863   -175       C  
ATOM    518  C   ILE A1067     -31.734  23.549  10.001  1.00104.65           C  
ANISOU  518  C   ILE A1067    15428  14175  10159    177    793   -121       C  
ATOM    519  O   ILE A1067     -30.932  23.146  10.849  1.00105.06           O  
ANISOU  519  O   ILE A1067    15546  14256  10118    244    783    -35       O  
ATOM    520  CB  ILE A1067     -34.061  22.441   9.859  1.00104.89           C  
ANISOU  520  CB  ILE A1067    15499  14208  10147   -101    937    -95       C  
ATOM    521  CG1 ILE A1067     -35.559  22.586  10.201  1.00106.16           C  
ANISOU  521  CG1 ILE A1067    15563  14509  10265   -245   1006   -148       C  
ATOM    522  CG2 ILE A1067     -33.520  21.121  10.423  1.00106.20           C  
ANISOU  522  CG2 ILE A1067    15855  14282  10213   -105    974     65       C  
ATOM    523  CD1 ILE A1067     -36.473  21.862   9.196  1.00114.87           C  
ANISOU  523  CD1 ILE A1067    16706  15523  11418   -396   1050   -130       C  
ATOM    524  N   LEU A1068     -31.363  23.948   8.773  1.00100.53           N  
ANISOU  524  N   LEU A1068    14879  13551   9768    220    745   -173       N  
ATOM    525  CA  LEU A1068     -29.980  23.950   8.305  1.00100.44           C  
ANISOU  525  CA  LEU A1068    14905  13457   9801    346    681   -135       C  
ATOM    526  C   LEU A1068     -29.090  24.859   9.159  1.00106.64           C  
ANISOU  526  C   LEU A1068    15604  14378  10535    442    616   -173       C  
ATOM    527  O   LEU A1068     -28.066  24.383   9.646  1.00108.24           O  
ANISOU  527  O   LEU A1068    15864  14589  10673    527    592    -80       O  
ATOM    528  CB  LEU A1068     -29.922  24.389   6.848  1.00 99.38           C  
ANISOU  528  CB  LEU A1068    14735  13214   9809    354    647   -203       C  
ATOM    529  CG  LEU A1068     -28.772  23.827   6.040  1.00104.35           C  
ANISOU  529  CG  LEU A1068    15453  13708  10488    448    619   -129       C  
ATOM    530  CD1 LEU A1068     -29.083  22.413   5.559  1.00105.62           C  
ANISOU  530  CD1 LEU A1068    15782  13711  10639    395    684    -27       C  
ATOM    531  CD2 LEU A1068     -28.487  24.702   4.847  1.00104.55           C  
ANISOU  531  CD2 LEU A1068    15400  13685  10640    477    565   -220       C  
ATOM    532  N   VAL A1069     -29.497  26.143   9.379  1.00102.16           N  
ANISOU  532  N   VAL A1069    14908  13921   9987    428    590   -308       N  
ATOM    533  CA  VAL A1069     -28.751  27.140  10.168  1.00101.83           C  
ANISOU  533  CA  VAL A1069    14791  14006   9894    493    527   -369       C  
ATOM    534  C   VAL A1069     -28.552  26.663  11.619  1.00109.09           C  
ANISOU  534  C   VAL A1069    15747  15047  10653    501    546   -293       C  
ATOM    535  O   VAL A1069     -27.461  26.830  12.176  1.00109.98           O  
ANISOU  535  O   VAL A1069    15852  15229  10704    575    489   -262       O  
ATOM    536  CB  VAL A1069     -29.379  28.562  10.060  1.00104.79           C  
ANISOU  536  CB  VAL A1069    15052  14443  10318    472    508   -533       C  
ATOM    537  CG1 VAL A1069     -28.823  29.526  11.109  1.00105.05           C  
ANISOU  537  CG1 VAL A1069    15033  14616  10266    509    461   -602       C  
ATOM    538  CG2 VAL A1069     -29.173  29.139   8.667  1.00103.28           C  
ANISOU  538  CG2 VAL A1069    14831  14136  10273    492    465   -594       C  
ATOM    539  N   GLY A1070     -29.597  26.055  12.191  1.00106.24           N  
ANISOU  539  N   GLY A1070    15424  14720  10222    419    626   -259       N  
ATOM    540  CA  GLY A1070     -29.582  25.494  13.534  1.00106.79           C  
ANISOU  540  CA  GLY A1070    15544  14898  10133    410    658   -177       C  
ATOM    541  C   GLY A1070     -28.535  24.409  13.638  1.00110.73           C  
ANISOU  541  C   GLY A1070    16160  15327  10583    485    641    -19       C  
ATOM    542  O   GLY A1070     -27.700  24.440  14.546  1.00110.78           O  
ANISOU  542  O   GLY A1070    16168  15437  10484    554    600     30       O  
ATOM    543  N   GLN A1071     -28.533  23.484  12.656  1.00107.07           N  
ANISOU  543  N   GLN A1071    15796  14690  10197    481    669     59       N  
ATOM    544  CA  GLN A1071     -27.568  22.390  12.575  1.00107.66           C  
ANISOU  544  CA  GLN A1071    16002  14667  10238    573    662    212       C  
ATOM    545  C   GLN A1071     -26.145  22.876  12.315  1.00111.86           C  
ANISOU  545  C   GLN A1071    16473  15227  10800    713    570    211       C  
ATOM    546  O   GLN A1071     -25.221  22.335  12.929  1.00113.83           O  
ANISOU  546  O   GLN A1071    16774  15518  10958    815    545    325       O  
ATOM    547  CB  GLN A1071     -27.994  21.350  11.555  1.00108.93           C  
ANISOU  547  CB  GLN A1071    16296  14624  10469    527    720    276       C  
ATOM    548  CG  GLN A1071     -28.988  20.346  12.120  1.00131.27           C  
ANISOU  548  CG  GLN A1071    19249  17421  13206    407    813    358       C  
ATOM    549  CD  GLN A1071     -29.479  19.400  11.055  1.00157.54           C  
ANISOU  549  CD  GLN A1071    22711  20544  16602    332    869    402       C  
ATOM    550  OE1 GLN A1071     -29.446  18.173  11.213  1.00157.18           O  
ANISOU  550  OE1 GLN A1071    22853  20379  16489    319    922    533       O  
ATOM    551  NE2 GLN A1071     -29.940  19.955   9.943  1.00146.80           N  
ANISOU  551  NE2 GLN A1071    21270  19135  15371    278    857    293       N  
ATOM    552  N   ILE A1072     -25.965  23.909  11.446  1.00105.36           N  
ANISOU  552  N   ILE A1072    15538  14396  10098    718    519     89       N  
ATOM    553  CA  ILE A1072     -24.667  24.548  11.176  1.00104.03           C  
ANISOU  553  CA  ILE A1072    15289  14278   9961    821    431     69       C  
ATOM    554  C   ILE A1072     -24.094  25.098  12.517  1.00111.67           C  
ANISOU  554  C   ILE A1072    16187  15448  10795    851    378     63       C  
ATOM    555  O   ILE A1072     -22.923  24.864  12.811  1.00113.36           O  
ANISOU  555  O   ILE A1072    16393  15728  10949    954    326    145       O  
ATOM    556  CB  ILE A1072     -24.790  25.647  10.080  1.00104.71           C  
ANISOU  556  CB  ILE A1072    15277  14319  10189    788    395    -71       C  
ATOM    557  CG1 ILE A1072     -24.965  25.016   8.678  1.00104.13           C  
ANISOU  557  CG1 ILE A1072    15275  14054  10235    788    428    -42       C  
ATOM    558  CG2 ILE A1072     -23.584  26.588  10.098  1.00104.19           C  
ANISOU  558  CG2 ILE A1072    15106  14355  10126    852    302   -117       C  
ATOM    559  CD1 ILE A1072     -25.607  25.934   7.581  1.00107.00           C  
ANISOU  559  CD1 ILE A1072    15567  14354  10734    721    418   -176       C  
ATOM    560  N   ASP A1073     -24.933  25.766  13.344  1.00108.61           N  
ANISOU  560  N   ASP A1073    15751  15166  10348    765    396    -29       N  
ATOM    561  CA  ASP A1073     -24.529  26.302  14.645  1.00110.28           C  
ANISOU  561  CA  ASP A1073    15910  15569  10422    774    354    -49       C  
ATOM    562  C   ASP A1073     -24.153  25.212  15.671  1.00116.08           C  
ANISOU  562  C   ASP A1073    16732  16367  11004    827    370    111       C  
ATOM    563  O   ASP A1073     -23.407  25.497  16.613  1.00116.10           O  
ANISOU  563  O   ASP A1073    16692  16530  10889    869    312    129       O  
ATOM    564  CB  ASP A1073     -25.614  27.232  15.217  1.00112.73           C  
ANISOU  564  CB  ASP A1073    16164  15961  10706    677    384   -190       C  
ATOM    565  CG  ASP A1073     -25.828  28.519  14.441  1.00123.37           C  
ANISOU  565  CG  ASP A1073    17424  17278  12174    647    352   -354       C  
ATOM    566  OD1 ASP A1073     -24.921  28.908  13.671  1.00123.09           O  
ANISOU  566  OD1 ASP A1073    17352  17199  12218    691    285   -370       O  
ATOM    567  OD2 ASP A1073     -26.897  29.145  14.617  1.00129.96           O1-
ANISOU  567  OD2 ASP A1073    18227  18136  13017    585    394   -463       O1-
ATOM    568  N   ASP A1074     -24.680  23.980  15.498  1.00113.49           N  
ANISOU  568  N   ASP A1074    16535  15915  10672    819    448    227       N  
ATOM    569  CA  ASP A1074     -24.356  22.843  16.363  1.00115.07           C  
ANISOU  569  CA  ASP A1074    16850  16139  10733    876    471    395       C  
ATOM    570  C   ASP A1074     -22.966  22.341  15.972  1.00119.78           C  
ANISOU  570  C   ASP A1074    17468  16707  11336   1033    412    507       C  
ATOM    571  O   ASP A1074     -22.167  21.990  16.840  1.00120.32           O  
ANISOU  571  O   ASP A1074    17551  16891  11276   1125    373    611       O  
ATOM    572  CB  ASP A1074     -25.391  21.710  16.213  1.00117.46           C  
ANISOU  572  CB  ASP A1074    17304  16293  11032    800    577    478       C  
ATOM    573  CG  ASP A1074     -26.777  21.986  16.769  1.00127.98           C  
ANISOU  573  CG  ASP A1074    18616  17686  12324    648    648    400       C  
ATOM    574  OD1 ASP A1074     -26.907  22.885  17.636  1.00128.65           O  
ANISOU  574  OD1 ASP A1074    18600  17947  12336    622    624    311       O  
ATOM    575  OD2 ASP A1074     -27.732  21.290  16.350  1.00133.26           O1-
ANISOU  575  OD2 ASP A1074    19372  18234  13026    552    730    429       O1-
ATOM    576  N   ALA A1075     -22.680  22.326  14.654  1.00115.57           N  
ANISOU  576  N   ALA A1075    16930  16032  10948   1069    404    485       N  
ATOM    577  CA  ALA A1075     -21.394  21.918  14.095  1.00115.30           C  
ANISOU  577  CA  ALA A1075    16900  15970  10939   1224    357    576       C  
ATOM    578  C   ALA A1075     -20.319  22.982  14.378  1.00118.59           C  
ANISOU  578  C   ALA A1075    17145  16583  11330   1272    250    514       C  
ATOM    579  O   ALA A1075     -19.153  22.634  14.539  1.00119.09           O  
ANISOU  579  O   ALA A1075    17186  16727  11335   1408    199    616       O  
ATOM    580  CB  ALA A1075     -21.529  21.670  12.600  1.00114.69           C  
ANISOU  580  CB  ALA A1075    16867  15691  11020   1227    388    553       C  
ATOM    581  N   LEU A1076     -20.718  24.266  14.464  1.00114.37           N  
ANISOU  581  N   LEU A1076    16494  16131  10831   1160    218    350       N  
ATOM    582  CA  LEU A1076     -19.817  25.382  14.761  1.00114.89           C  
ANISOU  582  CA  LEU A1076    16410  16376  10867   1164    119    270       C  
ATOM    583  C   LEU A1076     -19.263  25.290  16.194  1.00124.75           C  
ANISOU  583  C   LEU A1076    17636  17833  11929   1201     73    339       C  
ATOM    584  O   LEU A1076     -18.050  25.434  16.383  1.00125.05           O  
ANISOU  584  O   LEU A1076    17590  18012  11910   1282     -8    385       O  
ATOM    585  CB  LEU A1076     -20.523  26.732  14.543  1.00113.28           C  
ANISOU  585  CB  LEU A1076    16128  16177  10738   1032    110     76       C  
ATOM    586  CG  LEU A1076     -20.288  27.435  13.212  1.00115.64           C  
ANISOU  586  CG  LEU A1076    16365  16377  11195   1015     83    -15       C  
ATOM    587  CD1 LEU A1076     -21.312  28.519  12.999  1.00114.45           C  
ANISOU  587  CD1 LEU A1076    16186  16185  11115    898    101   -184       C  
ATOM    588  CD2 LEU A1076     -18.896  28.040  13.138  1.00117.80           C  
ANISOU  588  CD2 LEU A1076    16526  16783  11449   1060    -14    -21       C  
ATOM    589  N   LYS A1077     -20.149  25.020  17.193  1.00124.80           N  
ANISOU  589  N   LYS A1077    17713  17871  11833   1140    126    350       N  
ATOM    590  CA  LYS A1077     -19.764  24.859  18.598  1.00127.27           C  
ANISOU  590  CA  LYS A1077    18024  18377  11956   1167     92    420       C  
ATOM    591  C   LYS A1077     -18.800  23.670  18.786  1.00134.80           C  
ANISOU  591  C   LYS A1077    19039  19350  12828   1330     74    624       C  
ATOM    592  O   LYS A1077     -17.897  23.773  19.609  1.00135.73           O  
ANISOU  592  O   LYS A1077    19091  19666  12814   1393     -3    679       O  
ATOM    593  CB  LYS A1077     -20.981  24.810  19.555  1.00130.50           C  
ANISOU  593  CB  LYS A1077    18501  18811  12274   1062    164    389       C  
ATOM    594  CG  LYS A1077     -21.991  23.687  19.305  1.00146.41           C  
ANISOU  594  CG  LYS A1077    20664  20646  14318   1040    276    476       C  
ATOM    595  CD  LYS A1077     -23.172  23.679  20.291  1.00156.05           C  
ANISOU  595  CD  LYS A1077    21930  21925  15437    927    349    445       C  
ATOM    596  CE  LYS A1077     -24.392  24.413  19.776  1.00162.32           C  
ANISOU  596  CE  LYS A1077    22682  22652  16341    801    406    283       C  
ATOM    597  NZ  LYS A1077     -25.622  24.040  20.524  1.00169.01           N1+
ANISOU  597  NZ  LYS A1077    23592  23524  17102    701    503    292       N1+
ATOM    598  N   LEU A1078     -18.936  22.594  17.975  1.00132.89           N  
ANISOU  598  N   LEU A1078    18920  18908  12665   1405    139    731       N  
ATOM    599  CA  LEU A1078     -18.025  21.440  18.002  1.00135.10           C  
ANISOU  599  CA  LEU A1078    19278  19173  12883   1587    131    924       C  
ATOM    600  C   LEU A1078     -16.640  21.828  17.446  1.00141.58           C  
ANISOU  600  C   LEU A1078    19957  20100  13738   1705     39    931       C  
ATOM    601  O   LEU A1078     -15.631  21.393  17.993  1.00142.73           O  
ANISOU  601  O   LEU A1078    20074  20389  13767   1848    -15   1059       O  
ATOM    602  CB  LEU A1078     -18.584  20.239  17.213  1.00135.15           C  
ANISOU  602  CB  LEU A1078    19473  18911  12966   1624    232   1017       C  
ATOM    603  CG  LEU A1078     -19.880  19.592  17.709  1.00140.44           C  
ANISOU  603  CG  LEU A1078    20304  19467  13589   1512    331   1047       C  
ATOM    604  CD1 LEU A1078     -20.476  18.697  16.636  1.00140.35           C  
ANISOU  604  CD1 LEU A1078    20453  19181  13691   1499    421   1085       C  
ATOM    605  CD2 LEU A1078     -19.661  18.798  18.983  1.00144.62           C  
ANISOU  605  CD2 LEU A1078    20932  20089  13927   1583    335   1205       C  
ATOM    606  N   ALA A1079     -16.600  22.642  16.361  1.00138.43           N  
ANISOU  606  N   ALA A1079    19463  19641  13492   1646     23    800       N  
ATOM    607  CA  ALA A1079     -15.363  23.137  15.737  1.00138.60           C  
ANISOU  607  CA  ALA A1079    19337  19768  13558   1724    -58    787       C  
ATOM    608  C   ALA A1079     -14.660  24.140  16.672  1.00144.71           C  
ANISOU  608  C   ALA A1079    19945  20822  14214   1674   -165    728       C  
ATOM    609  O   ALA A1079     -13.425  24.158  16.736  1.00145.35           O  
ANISOU  609  O   ALA A1079    19913  21077  14238   1778   -242    795       O  
ATOM    610  CB  ALA A1079     -15.672  23.796  14.399  1.00137.39           C  
ANISOU  610  CB  ALA A1079    19145  19469  13590   1642    -41    654       C  
ATOM    611  N   ASN A1080     -15.458  24.958  17.403  1.00141.40           N  
ANISOU  611  N   ASN A1080    19515  20457  13754   1515   -167    601       N  
ATOM    612  CA  ASN A1080     -14.974  25.945  18.368  1.00142.14           C  
ANISOU  612  CA  ASN A1080    19485  20797  13724   1438   -259    524       C  
ATOM    613  C   ASN A1080     -14.457  25.262  19.643  1.00149.21           C  
ANISOU  613  C   ASN A1080    20394  21879  14418   1531   -295    670       C  
ATOM    614  O   ASN A1080     -13.485  25.738  20.231  1.00149.97           O  
ANISOU  614  O   ASN A1080    20363  22216  14403   1540   -395    675       O  
ATOM    615  CB  ASN A1080     -16.060  26.976  18.691  1.00140.75           C  
ANISOU  615  CB  ASN A1080    19320  20592  13568   1256   -234    341       C  
ATOM    616  CG  ASN A1080     -16.220  28.065  17.651  1.00155.66           C  
ANISOU  616  CG  ASN A1080    21144  22386  15614   1158   -245    176       C  
ATOM    617  OD1 ASN A1080     -15.339  28.908  17.445  1.00145.68           O  
ANISOU  617  OD1 ASN A1080    19761  21238  14352   1123   -329    112       O  
ATOM    618  ND2 ASN A1080     -17.363  28.092  16.988  1.00146.78           N  
ANISOU  618  ND2 ASN A1080    20098  21056  14615   1102   -162    105       N  
ATOM    619  N   GLU A1081     -15.094  24.138  20.052  1.00147.21           N  
ANISOU  619  N   GLU A1081    20298  21519  14114   1594   -215    794       N  
ATOM    620  CA  GLU A1081     -14.717  23.336  21.227  1.00149.57           C  
ANISOU  620  CA  GLU A1081    20646  21961  14221   1696   -234    955       C  
ATOM    621  C   GLU A1081     -13.376  22.599  21.027  1.00155.99           C  
ANISOU  621  C   GLU A1081    21413  22867  14990   1908   -291   1126       C  
ATOM    622  O   GLU A1081     -12.705  22.268  22.011  1.00157.91           O  
ANISOU  622  O   GLU A1081    21627  23313  15059   1999   -351   1242       O  
ATOM    623  CB  GLU A1081     -15.810  22.302  21.555  1.00151.21           C  
ANISOU  623  CB  GLU A1081    21057  21991  14403   1697   -122   1043       C  
ATOM    624  CG  GLU A1081     -16.905  22.783  22.494  1.00160.70           C  
ANISOU  624  CG  GLU A1081    22297  23235  15527   1532    -83    945       C  
ATOM    625  CD  GLU A1081     -18.140  21.901  22.565  1.00178.02           C  
ANISOU  625  CD  GLU A1081    24674  25234  17731   1487     42   1001       C  
ATOM    626  OE1 GLU A1081     -18.393  21.131  21.609  1.00165.19           O  
ANISOU  626  OE1 GLU A1081    23153  23387  16226   1534    108   1060       O  
ATOM    627  OE2 GLU A1081     -18.866  21.990  23.582  1.00173.27           O1-
ANISOU  627  OE2 GLU A1081    24115  24709  17011   1394     75    981       O1-
ATOM    628  N   GLY A1082     -13.035  22.313  19.769  1.00151.59           N  
ANISOU  628  N   GLY A1082    20853  22164  14581   1994   -267   1145       N  
ATOM    629  CA  GLY A1082     -11.815  21.608  19.394  1.00152.26           C  
ANISOU  629  CA  GLY A1082    20893  22316  14643   2213   -304   1298       C  
ATOM    630  C   GLY A1082     -12.047  20.237  18.792  1.00156.00           C  
ANISOU  630  C   GLY A1082    21562  22539  15170   2372   -206   1443       C  
ATOM    631  O   GLY A1082     -11.087  19.491  18.588  1.00157.07           O  
ANISOU  631  O   GLY A1082    21693  22718  15268   2588   -223   1592       O  
ATOM    632  N   LYS A1083     -13.319  19.893  18.498  1.00151.33           N  
ANISOU  632  N   LYS A1083    21147  21690  14661   2268   -101   1402       N  
ATOM    633  CA  LYS A1083     -13.707  18.614  17.894  1.00151.45           C  
ANISOU  633  CA  LYS A1083    21380  21434  14729   2376      1   1520       C  
ATOM    634  C   LYS A1083     -13.794  18.733  16.366  1.00154.57           C  
ANISOU  634  C   LYS A1083    21776  21635  15320   2365     43   1438       C  
ATOM    635  O   LYS A1083     -14.411  19.664  15.844  1.00152.54           O  
ANISOU  635  O   LYS A1083    21445  21335  15177   2189     46   1267       O  
ATOM    636  CB  LYS A1083     -15.025  18.089  18.485  1.00153.64           C  
ANISOU  636  CB  LYS A1083    21852  21559  14965   2254     92   1534       C  
ATOM    637  CG  LYS A1083     -14.922  17.678  19.947  1.00163.97           C  
ANISOU  637  CG  LYS A1083    23208  23024  16068   2297     68   1655       C  
ATOM    638  CD  LYS A1083     -15.652  18.647  20.859  1.00168.66           C  
ANISOU  638  CD  LYS A1083    23720  23765  16600   2090     47   1521       C  
ATOM    639  CE  LYS A1083     -15.112  18.623  22.266  1.00179.52           C  
ANISOU  639  CE  LYS A1083    25053  25394  17762   2144    -23   1613       C  
ATOM    640  NZ  LYS A1083     -13.786  19.296  22.367  1.00188.72           N1+
ANISOU  640  NZ  LYS A1083    26002  26821  18880   2233   -150   1603       N1+
ATOM    641  N   VAL A1084     -13.152  17.789  15.661  1.00152.27           N  
ANISOU  641  N   VAL A1084    21569  21230  15055   2565     75   1562       N  
ATOM    642  CA  VAL A1084     -13.077  17.734  14.199  1.00151.24           C  
ANISOU  642  CA  VAL A1084    21453  20920  15090   2592    117   1509       C  
ATOM    643  C   VAL A1084     -13.741  16.473  13.617  1.00156.03           C  
ANISOU  643  C   VAL A1084    22334  21207  15742   2644    234   1592       C  
ATOM    644  O   VAL A1084     -13.984  16.413  12.411  1.00154.07           O  
ANISOU  644  O   VAL A1084    22134  20774  15632   2619    283   1528       O  
ATOM    645  CB  VAL A1084     -11.621  17.914  13.680  1.00156.01           C  
ANISOU  645  CB  VAL A1084    21886  21691  15700   2774     49   1551       C  
ATOM    646  CG1 VAL A1084     -11.072  19.288  14.043  1.00155.33           C  
ANISOU  646  CG1 VAL A1084    21532  21892  15593   2664    -63   1436       C  
ATOM    647  CG2 VAL A1084     -10.689  16.805  14.183  1.00158.28           C  
ANISOU  647  CG2 VAL A1084    22240  22046  15852   3050     44   1763       C  
ATOM    648  N   LYS A1085     -13.990  15.459  14.466  1.00155.15           N  
ANISOU  648  N   LYS A1085    22410  21033  15505   2716    277   1738       N  
ATOM    649  CA  LYS A1085     -14.628  14.202  14.071  1.00155.88           C  
ANISOU  649  CA  LYS A1085    22794  20820  15613   2749    389   1829       C  
ATOM    650  C   LYS A1085     -16.139  14.370  14.135  1.00158.94           C  
ANISOU  650  C   LYS A1085    23275  21066  16049   2482    453   1724       C  
ATOM    651  O   LYS A1085     -16.835  13.994  13.191  1.00157.12           O  
ANISOU  651  O   LYS A1085    23180  20593  15925   2401    529   1680       O  
ATOM    652  CB  LYS A1085     -14.170  13.050  14.982  1.00161.13           C  
ANISOU  652  CB  LYS A1085    23628  21482  16111   2948    405   2042       C  
ATOM    653  N   GLU A1086     -16.634  14.961  15.247  1.00156.47           N  
ANISOU  653  N   GLU A1086    22880  20922  15650   2343    420   1681       N  
ATOM    654  CA  GLU A1086     -18.051  15.234  15.503  1.00155.77           C  
ANISOU  654  CA  GLU A1086    22839  20763  15582   2094    475   1582       C  
ATOM    655  C   GLU A1086     -18.582  16.338  14.592  1.00157.52           C  
ANISOU  655  C   GLU A1086    22910  20973  15966   1931    463   1380       C  
ATOM    656  O   GLU A1086     -19.708  16.223  14.106  1.00156.46           O  
ANISOU  656  O   GLU A1086    22865  20673  15909   1771    535   1312       O  
ATOM    657  CB  GLU A1086     -18.281  15.608  16.972  1.00158.07           C  
ANISOU  657  CB  GLU A1086    23068  21268  15723   2023    440   1593       C  
ATOM    658  CG  GLU A1086     -18.026  14.477  17.947  1.00171.86           C  
ANISOU  658  CG  GLU A1086    24995  23006  17299   2148    464   1795       C  
ATOM    659  CD  GLU A1086     -16.978  14.813  18.987  1.00195.41           C  
ANISOU  659  CD  GLU A1086    27837  26274  20135   2281    363   1864       C  
ATOM    660  OE1 GLU A1086     -15.777  14.590  18.713  1.00193.11           O1-
ANISOU  660  OE1 GLU A1086    27494  26048  19830   2497    309   1952       O1-
ATOM    661  OE2 GLU A1086     -17.357  15.309  20.072  1.00186.80           O  
ANISOU  661  OE2 GLU A1086    26681  25356  18939   2167    338   1828       O  
ATOM    662  N   ALA A1087     -17.775  17.408  14.372  1.00152.93           N  
ANISOU  662  N   ALA A1087    22104  20573  15430   1966    372   1289       N  
ATOM    663  CA  ALA A1087     -18.111  18.546  13.507  1.00150.47           C  
ANISOU  663  CA  ALA A1087    21645  20261  15266   1834    349   1105       C  
ATOM    664  C   ALA A1087     -18.221  18.111  12.037  1.00154.33           C  
ANISOU  664  C   ALA A1087    22222  20517  15899   1857    402   1089       C  
ATOM    665  O   ALA A1087     -19.049  18.653  11.306  1.00152.70           O  
ANISOU  665  O   ALA A1087    21991  20220  15810   1708    427    959       O  
ATOM    666  CB  ALA A1087     -17.074  19.645  13.658  1.00150.71           C  
ANISOU  666  CB  ALA A1087    21446  20531  15288   1877    240   1040       C  
ATOM    667  N   GLN A1088     -17.406  17.115  11.621  1.00152.49           N  
ANISOU  667  N   GLN A1088    22100  20190  15649   2051    423   1225       N  
ATOM    668  CA  GLN A1088     -17.396  16.516  10.277  1.00151.79           C  
ANISOU  668  CA  GLN A1088    22129  19872  15673   2103    481   1231       C  
ATOM    669  C   GLN A1088     -18.601  15.564  10.117  1.00156.02           C  
ANISOU  669  C   GLN A1088    22910  20155  16214   1989    586   1260       C  
ATOM    670  O   GLN A1088     -19.168  15.463   9.026  1.00154.57           O  
ANISOU  670  O   GLN A1088    22795  19792  16145   1904    633   1190       O  
ATOM    671  CB  GLN A1088     -16.083  15.746  10.056  1.00154.39           C  
ANISOU  671  CB  GLN A1088    22500  20204  15955   2371    473   1374       C  
ATOM    672  CG  GLN A1088     -15.400  16.043   8.729  1.00165.17           C  
ANISOU  672  CG  GLN A1088    23783  21533  17441   2450    462   1318       C  
ATOM    673  CD  GLN A1088     -13.914  15.777   8.771  1.00181.45           C  
ANISOU  673  CD  GLN A1088    25764  23739  19441   2709    418   1431       C  
ATOM    674  OE1 GLN A1088     -13.098  16.702   8.708  1.00174.78           O  
ANISOU  674  OE1 GLN A1088    24684  23116  18610   2731    337   1378       O  
ATOM    675  NE2 GLN A1088     -13.524  14.511   8.870  1.00175.10           N  
ANISOU  675  NE2 GLN A1088    25154  22816  18562   2911    473   1591       N  
ATOM    676  N   ALA A1089     -18.980  14.868  11.215  1.00153.78           N  
ANISOU  676  N   ALA A1089    22760  19869  15800   1978    619   1367       N  
ATOM    677  CA  ALA A1089     -20.119  13.949  11.279  1.00154.06           C  
ANISOU  677  CA  ALA A1089    23030  19694  15812   1848    717   1409       C  
ATOM    678  C   ALA A1089     -21.441  14.723  11.226  1.00155.83           C  
ANISOU  678  C   ALA A1089    23169  19940  16100   1584    734   1255       C  
ATOM    679  O   ALA A1089     -22.414  14.232  10.651  1.00155.23           O  
ANISOU  679  O   ALA A1089    23230  19678  16073   1443    808   1231       O  
ATOM    680  CB  ALA A1089     -20.049  13.124  12.553  1.00156.90           C  
ANISOU  680  CB  ALA A1089    23533  20081  16001   1912    739   1568       C  
ATOM    681  N   ALA A1090     -21.470  15.934  11.824  1.00151.02           N  
ANISOU  681  N   ALA A1090    22334  19563  15485   1521    665   1152       N  
ATOM    682  CA  ALA A1090     -22.631  16.826  11.824  1.00149.35           C  
ANISOU  682  CA  ALA A1090    22011  19404  15329   1306    674    999       C  
ATOM    683  C   ALA A1090     -22.859  17.434  10.420  1.00151.37           C  
ANISOU  683  C   ALA A1090    22189  19570  15755   1247    666    866       C  
ATOM    684  O   ALA A1090     -23.964  17.887  10.126  1.00149.87           O  
ANISOU  684  O   ALA A1090    21959  19359  15627   1075    693    757       O  
ATOM    685  CB  ALA A1090     -22.448  17.925  12.863  1.00149.80           C  
ANISOU  685  CB  ALA A1090    21873  19722  15321   1287    603    930       C  
ATOM    686  N   ALA A1091     -21.818  17.425   9.554  1.00147.58           N  
ANISOU  686  N   ALA A1091    21685  19046  15342   1395    630    882       N  
ATOM    687  CA  ALA A1091     -21.892  17.913   8.173  1.00145.91           C  
ANISOU  687  CA  ALA A1091    21416  18742  15280   1359    623    774       C  
ATOM    688  C   ALA A1091     -22.649  16.912   7.299  1.00150.22           C  
ANISOU  688  C   ALA A1091    22166  19037  15873   1287    710    800       C  
ATOM    689  O   ALA A1091     -23.225  17.303   6.285  1.00148.37           O  
ANISOU  689  O   ALA A1091    21899  18724  15751   1184    718    695       O  
ATOM    690  CB  ALA A1091     -20.499  18.143   7.617  1.00146.44           C  
ANISOU  690  CB  ALA A1091    21399  18859  15384   1540    566    795       C  
ATOM    691  N   GLU A1092     -22.647  15.620   7.699  1.00148.84           N  
ANISOU  691  N   GLU A1092    22213  18733  15605   1338    773    942       N  
ATOM    692  CA  GLU A1092     -23.356  14.541   7.007  1.00149.23           C  
ANISOU  692  CA  GLU A1092    22496  18531  15673   1256    861    979       C  
ATOM    693  C   GLU A1092     -24.868  14.712   7.206  1.00151.21           C  
ANISOU  693  C   GLU A1092    22744  18782  15928   1000    903    903       C  
ATOM    694  O   GLU A1092     -25.625  14.528   6.249  1.00150.02           O  
ANISOU  694  O   GLU A1092    22655  18493  15852    869    942    842       O  
ATOM    695  CB  GLU A1092     -22.880  13.158   7.500  1.00152.93           C  
ANISOU  695  CB  GLU A1092    23217  18865  16026   1388    915   1158       C  
ATOM    696  CG  GLU A1092     -23.164  12.008   6.539  1.00166.34           C  
ANISOU  696  CG  GLU A1092    25182  20271  17748   1368    998   1203       C  
ATOM    697  CD  GLU A1092     -24.573  11.438   6.555  1.00188.42           C  
ANISOU  697  CD  GLU A1092    28137  22932  20522   1116   1075   1190       C  
ATOM    698  OE1 GLU A1092     -25.038  11.017   7.640  1.00181.25           O  
ANISOU  698  OE1 GLU A1092    27310  22055  19502   1045   1107   1268       O  
ATOM    699  OE2 GLU A1092     -25.209  11.402   5.476  1.00180.79           O1-
ANISOU  699  OE2 GLU A1092    27211  21837  19644    983   1103   1104       O1-
ATOM    700  N   GLN A1093     -25.302  15.090   8.438  1.00147.05           N  
ANISOU  700  N   GLN A1093    22133  18425  15313    930    893    904       N  
ATOM    701  CA  GLN A1093     -26.718  15.321   8.745  1.00146.22           C  
ANISOU  701  CA  GLN A1093    21994  18365  15199    700    935    832       C  
ATOM    702  C   GLN A1093     -27.236  16.614   8.084  1.00146.31           C  
ANISOU  702  C   GLN A1093    21783  18476  15332    610    891    658       C  
ATOM    703  O   GLN A1093     -28.450  16.813   7.991  1.00145.29           O  
ANISOU  703  O   GLN A1093    21616  18366  15223    428    926    585       O  
ATOM    704  CB  GLN A1093     -27.012  15.255  10.258  1.00148.85           C  
ANISOU  704  CB  GLN A1093    22321  18846  15390    662    949    893       C  
ATOM    705  CG  GLN A1093     -26.499  16.432  11.073  1.00167.09           C  
ANISOU  705  CG  GLN A1093    24409  21403  17674    738    870    830       C  
ATOM    706  CD  GLN A1093     -26.643  16.197  12.551  1.00192.61           C  
ANISOU  706  CD  GLN A1093    27669  24766  20748    722    887    909       C  
ATOM    707  OE1 GLN A1093     -25.779  15.590  13.193  1.00188.70           O  
ANISOU  707  OE1 GLN A1093    27102  24385  20212    574    916    848       O  
ATOM    708  NE2 GLN A1093     -27.743  16.672  13.121  1.00187.75           N  
ANISOU  708  NE2 GLN A1093    27155  24148  20035    885    871   1051       N  
ATOM    709  N   LEU A1094     -26.302  17.469   7.606  1.00140.61           N  
ANISOU  709  N   LEU A1094    20918  17818  14687    741    814    597       N  
ATOM    710  CA  LEU A1094     -26.590  18.702   6.879  1.00138.19           C  
ANISOU  710  CA  LEU A1094    20425  17583  14499    687    766    443       C  
ATOM    711  C   LEU A1094     -26.945  18.375   5.433  1.00140.47           C  
ANISOU  711  C   LEU A1094    20787  17690  14894    630    793    407       C  
ATOM    712  O   LEU A1094     -27.675  19.143   4.805  1.00139.34           O  
ANISOU  712  O   LEU A1094    20532  17575  14837    527    778    288       O  
ATOM    713  CB  LEU A1094     -25.398  19.672   6.923  1.00137.44           C  
ANISOU  713  CB  LEU A1094    20174  17616  14433    833    678    404       C  
ATOM    714  CG  LEU A1094     -25.287  20.565   8.153  1.00142.23           C  
ANISOU  714  CG  LEU A1094    20636  18441  14964    837    631    364       C  
ATOM    715  CD1 LEU A1094     -23.922  21.204   8.228  1.00142.04           C  
ANISOU  715  CD1 LEU A1094    20502  18527  14941    982    547    363       C  
ATOM    716  CD2 LEU A1094     -26.354  21.645   8.146  1.00144.21           C  
ANISOU  716  CD2 LEU A1094    20752  18777  15264    700    626    216       C  
ATOM    717  N   LYS A1095     -26.421  17.240   4.904  1.00136.57           N  
ANISOU  717  N   LYS A1095    20488  17012  14390    706    831    508       N  
ATOM    718  CA  LYS A1095     -26.701  16.749   3.550  1.00135.22           C  
ANISOU  718  CA  LYS A1095    20428  16649  14301    654    864    484       C  
ATOM    719  C   LYS A1095     -28.114  16.174   3.486  1.00137.89           C  
ANISOU  719  C   LYS A1095    20866  16909  14616    434    932    473       C  
ATOM    720  O   LYS A1095     -28.792  16.368   2.481  1.00136.47           O  
ANISOU  720  O   LYS A1095    20665  16672  14517    319    936    390       O  
ATOM    721  CB  LYS A1095     -25.674  15.699   3.101  1.00138.49           C  
ANISOU  721  CB  LYS A1095    21034  16890  14694    817    891    596       C  
ATOM    722  CG  LYS A1095     -24.435  16.292   2.454  1.00149.72           C  
ANISOU  722  CG  LYS A1095    22345  18355  16185    998    831    572       C  
ATOM    723  CD  LYS A1095     -23.503  15.212   1.922  1.00160.05           C  
ANISOU  723  CD  LYS A1095    23847  19493  17473   1169    869    677       C  
ATOM    724  CE  LYS A1095     -22.240  15.802   1.341  1.00169.81           C  
ANISOU  724  CE  LYS A1095    24952  20804  18765   1350    814    660       C  
ATOM    725  NZ  LYS A1095     -21.340  14.756   0.789  1.00178.64           N1+
ANISOU  725  NZ  LYS A1095    26250  21765  19859   1536    859    759       N1+
ATOM    726  N   THR A1096     -28.567  15.497   4.562  1.00135.07           N  
ANISOU  726  N   THR A1096    20609  16567  14144    367    982    557       N  
ATOM    727  CA  THR A1096     -29.919  14.928   4.655  1.00135.76           C  
ANISOU  727  CA  THR A1096    20784  16609  14189    137   1050    556       C  
ATOM    728  C   THR A1096     -30.985  16.031   4.768  1.00137.85           C  
ANISOU  728  C   THR A1096    20816  17066  14495     -5   1028    428       C  
ATOM    729  O   THR A1096     -32.108  15.846   4.296  1.00137.68           O  
ANISOU  729  O   THR A1096    20802  17021  14488   -195   1066    383       O  
ATOM    730  CB  THR A1096     -30.036  13.918   5.820  1.00149.22           C  
ANISOU  730  CB  THR A1096    22664  18283  15750    108   1113    691       C  
ATOM    731  OG1 THR A1096     -29.601  14.524   7.036  1.00149.64           O  
ANISOU  731  OG1 THR A1096    22586  18532  15739    208   1075    710       O  
ATOM    732  CG2 THR A1096     -29.267  12.620   5.568  1.00150.56           C  
ANISOU  732  CG2 THR A1096    23118  18215  15873    218   1155    824       C  
ATOM    733  N   THR A1097     -30.623  17.179   5.384  1.00132.76           N  
ANISOU  733  N   THR A1097    19968  16614  13862     90    968    367       N  
ATOM    734  CA  THR A1097     -31.510  18.330   5.595  1.00131.34           C  
ANISOU  734  CA  THR A1097    19569  16621  13713      0    945    243       C  
ATOM    735  C   THR A1097     -31.793  19.083   4.291  1.00133.25           C  
ANISOU  735  C   THR A1097    19702  16839  14089    -25    905    126       C  
ATOM    736  O   THR A1097     -32.958  19.319   3.974  1.00132.63           O  
ANISOU  736  O   THR A1097    19549  16812  14034   -173    926     58       O  
ATOM    737  CB  THR A1097     -30.962  19.224   6.711  1.00137.61           C  
ANISOU  737  CB  THR A1097    20224  17601  14460    112    898    222       C  
ATOM    738  OG1 THR A1097     -30.680  18.398   7.839  1.00139.02           O  
ANISOU  738  OG1 THR A1097    20525  17788  14507    135    936    345       O  
ATOM    739  CG2 THR A1097     -31.932  20.326   7.117  1.00135.19           C  
ANISOU  739  CG2 THR A1097    19722  17483  14161     28    891    101       C  
ATOM    740  N   ARG A1098     -30.743  19.438   3.527  1.00128.63           N  
ANISOU  740  N   ARG A1098    19103  16187  13584    117    849    109       N  
ATOM    741  CA  ARG A1098     -30.912  20.146   2.259  1.00127.43           C  
ANISOU  741  CA  ARG A1098    18860  16003  13553    103    809      7       C  
ATOM    742  C   ARG A1098     -31.502  19.246   1.158  1.00132.16           C  
ANISOU  742  C   ARG A1098    19599  16435  14182    -17    853     22       C  
ATOM    743  O   ARG A1098     -31.886  19.755   0.101  1.00131.11           O  
ANISOU  743  O   ARG A1098    19393  16285  14136    -62    825    -62       O  
ATOM    744  CB  ARG A1098     -29.614  20.851   1.811  1.00127.19           C  
ANISOU  744  CB  ARG A1098    18767  15969  13590    276    739    -17       C  
ATOM    745  CG  ARG A1098     -28.447  19.934   1.465  1.00138.24           C  
ANISOU  745  CG  ARG A1098    20323  17223  14977    402    749     85       C  
ATOM    746  CD  ARG A1098     -27.608  20.535   0.351  1.00145.16           C  
ANISOU  746  CD  ARG A1098    21140  18060  15953    502    696     35       C  
ATOM    747  NE  ARG A1098     -26.606  19.593  -0.150  1.00151.21           N  
ANISOU  747  NE  ARG A1098    22060  18683  16711    622    718    126       N  
ATOM    748  CZ  ARG A1098     -26.818  18.713  -1.123  1.00164.46           C  
ANISOU  748  CZ  ARG A1098    23898  20179  18410    583    765    150       C  
ATOM    749  NH1 ARG A1098     -28.006  18.636  -1.710  1.00151.83           N1+
ANISOU  749  NH1 ARG A1098    22319  18529  16841    409    789     90       N1+
ATOM    750  NH2 ARG A1098     -25.848  17.901  -1.513  1.00153.41           N  
ANISOU  750  NH2 ARG A1098    22641  18655  16995    719    789    231       N  
ATOM    751  N   ASN A1099     -31.588  17.919   1.424  1.00130.01           N  
ANISOU  751  N   ASN A1099    19534  16036  13829    -74    920    128       N  
ATOM    752  CA  ASN A1099     -32.149  16.907   0.523  1.00130.45           C  
ANISOU  752  CA  ASN A1099    19763  15915  13886   -210    970    151       C  
ATOM    753  C   ASN A1099     -33.653  16.695   0.772  1.00135.13           C  
ANISOU  753  C   ASN A1099    20328  16585  14432   -446   1016    126       C  
ATOM    754  O   ASN A1099     -34.439  16.715  -0.182  1.00134.30           O  
ANISOU  754  O   ASN A1099    20201  16455  14373   -582   1016     64       O  
ATOM    755  CB  ASN A1099     -31.384  15.580   0.648  1.00130.98           C  
ANISOU  755  CB  ASN A1099    20097  15785  13884   -139   1022    279       C  
ATOM    756  CG  ASN A1099     -30.124  15.479  -0.188  1.00150.09           C  
ANISOU  756  CG  ASN A1099    22589  18077  16363     51    995    297       C  
ATOM    757  OD1 ASN A1099     -29.435  16.467  -0.478  1.00142.54           O  
ANISOU  757  OD1 ASN A1099    21469  17210  15481    180    930    239       O  
ATOM    758  ND2 ASN A1099     -29.780  14.263  -0.577  1.00143.08           N  
ANISOU  758  ND2 ASN A1099    21956  16973  15435     73   1050    380       N  
ATOM    759  N   ALA A1100     -34.045  16.509   2.051  1.00132.59           N  
ANISOU  759  N   ALA A1100    19996  16371  14012   -497   1054    175       N  
ATOM    760  CA  ALA A1100     -35.435  16.286   2.463  1.00133.66           C  
ANISOU  760  CA  ALA A1100    20092  16610  14083   -721   1106    164       C  
ATOM    761  C   ALA A1100     -36.313  17.558   2.554  1.00137.15           C  
ANISOU  761  C   ALA A1100    20254  17289  14568   -763   1071     44       C  
ATOM    762  O   ALA A1100     -37.544  17.436   2.560  1.00137.73           O  
ANISOU  762  O   ALA A1100    20266  17459  14608   -953   1109     18       O  
ATOM    763  CB  ALA A1100     -35.468  15.535   3.785  1.00135.98           C  
ANISOU  763  CB  ALA A1100    20501  16921  14244   -755   1167    273       C  
ATOM    764  N   TYR A1101     -35.696  18.767   2.627  1.00131.82           N  
ANISOU  764  N   TYR A1101    19414  16710  13960   -589   1003    -27       N  
ATOM    765  CA  TYR A1101     -36.440  20.024   2.776  1.00130.37           C  
ANISOU  765  CA  TYR A1101    18986  16735  13812   -594    973   -140       C  
ATOM    766  C   TYR A1101     -36.310  21.024   1.618  1.00131.30           C  
ANISOU  766  C   TYR A1101    18984  16847  14057   -520    901   -243       C  
ATOM    767  O   TYR A1101     -37.330  21.485   1.101  1.00130.70           O  
ANISOU  767  O   TYR A1101    18782  16864  14016   -611    896   -316       O  
ATOM    768  CB  TYR A1101     -36.065  20.725   4.096  1.00131.64           C  
ANISOU  768  CB  TYR A1101    19052  17047  13918   -480    963   -148       C  
ATOM    769  CG  TYR A1101     -36.355  19.936   5.356  1.00135.49           C  
ANISOU  769  CG  TYR A1101    19621  17589  14269   -558   1032    -58       C  
ATOM    770  CD1 TYR A1101     -37.640  19.881   5.887  1.00138.88           C  
ANISOU  770  CD1 TYR A1101    19967  18172  14630   -717   1091    -75       C  
ATOM    771  CD2 TYR A1101     -35.331  19.315   6.063  1.00136.84           C  
ANISOU  771  CD2 TYR A1101    19941  17680  14374   -461   1038     46       C  
ATOM    772  CE1 TYR A1101     -37.910  19.174   7.059  1.00141.71           C  
ANISOU  772  CE1 TYR A1101    20402  18586  14854   -797   1159     11       C  
ATOM    773  CE2 TYR A1101     -35.585  18.614   7.242  1.00139.43           C  
ANISOU  773  CE2 TYR A1101    20351  18057  14568   -528   1101    136       C  
ATOM    774  CZ  TYR A1101     -36.878  18.544   7.736  1.00148.76           C  
ANISOU  774  CZ  TYR A1101    21460  19380  15683   -703   1163    117       C  
ATOM    775  OH  TYR A1101     -37.141  17.853   8.896  1.00151.23           O  
ANISOU  775  OH  TYR A1101    21858  19746  15857   -779   1228    209       O  
ATOM    776  N   ILE A1102     -35.068  21.398   1.248  1.00125.93           N  
ANISOU  776  N   ILE A1102    18333  16076  13440   -353    846   -245       N  
ATOM    777  CA  ILE A1102     -34.790  22.441   0.249  1.00123.90           C  
ANISOU  777  CA  ILE A1102    17967  15814  13296   -268    777   -336       C  
ATOM    778  C   ILE A1102     -34.724  21.939  -1.200  1.00123.99           C  
ANISOU  778  C   ILE A1102    18073  15663  13374   -313    767   -333       C  
ATOM    779  O   ILE A1102     -35.275  22.610  -2.072  1.00121.79           O  
ANISOU  779  O   ILE A1102    17690  15419  13165   -344    732   -412       O  
ATOM    780  CB  ILE A1102     -33.503  23.247   0.626  1.00126.61           C  
ANISOU  780  CB  ILE A1102    18268  16172  13665    -82    720   -349       C  
ATOM    781  CG1 ILE A1102     -33.652  23.959   1.991  1.00127.15           C  
ANISOU  781  CG1 ILE A1102    18226  16417  13668    -44    720   -379       C  
ATOM    782  CG2 ILE A1102     -33.113  24.255  -0.471  1.00126.60           C  
ANISOU  782  CG2 ILE A1102    18184  16142  13777     -4    651   -432       C  
ATOM    783  CD1 ILE A1102     -32.428  23.847   2.884  1.00134.79           C  
ANISOU  783  CD1 ILE A1102    19248  17387  14580     77    704   -317       C  
ATOM    784  N   GLN A1103     -34.018  20.812  -1.454  1.00120.44           N  
ANISOU  784  N   GLN A1103    17823  15037  12899   -302    797   -245       N  
ATOM    785  CA  GLN A1103     -33.777  20.215  -2.780  1.00119.94           C  
ANISOU  785  CA  GLN A1103    17888  14798  12886   -327    797   -236       C  
ATOM    786  C   GLN A1103     -34.972  20.281  -3.753  1.00122.49           C  
ANISOU  786  C   GLN A1103    18158  15141  13242   -492    793   -301       C  
ATOM    787  O   GLN A1103     -34.786  20.702  -4.896  1.00120.62           O  
ANISOU  787  O   GLN A1103    17894  14853  13083   -462    749   -353       O  
ATOM    788  CB  GLN A1103     -33.255  18.772  -2.662  1.00122.57           C  
ANISOU  788  CB  GLN A1103    18471  14949  13151   -335    857   -125       C  
ATOM    789  CG  GLN A1103     -32.567  18.247  -3.930  1.00143.46           C  
ANISOU  789  CG  GLN A1103    21264  17399  15844   -286    855   -113       C  
ATOM    790  CD  GLN A1103     -31.459  19.147  -4.439  1.00162.88           C  
ANISOU  790  CD  GLN A1103    23629  19871  18387   -100    792   -151       C  
ATOM    791  OE1 GLN A1103     -31.623  19.879  -5.422  1.00155.75           O  
ANISOU  791  OE1 GLN A1103    22629  18985  17563   -110    747   -231       O  
ATOM    792  NE2 GLN A1103     -30.310  19.117  -3.779  1.00157.57           N  
ANISOU  792  NE2 GLN A1103    22980  19199  17692     68    786    -91       N  
ATOM    793  N   LYS A1104     -36.187  19.913  -3.284  1.00119.50           N  
ANISOU  793  N   LYS A1104    17752  14855  12798   -667    836   -298       N  
ATOM    794  CA  LYS A1104     -37.444  19.938  -4.048  1.00119.17           C  
ANISOU  794  CA  LYS A1104    17635  14878  12766   -844    834   -352       C  
ATOM    795  C   LYS A1104     -37.744  21.296  -4.715  1.00121.84           C  
ANISOU  795  C   LYS A1104    17762  15338  13194   -776    762   -455       C  
ATOM    796  O   LYS A1104     -38.344  21.315  -5.788  1.00121.90           O  
ANISOU  796  O   LYS A1104    17743  15340  13233   -868    739   -495       O  
ATOM    797  CB  LYS A1104     -38.640  19.465  -3.186  1.00122.54           C  
ANISOU  797  CB  LYS A1104    18025  15439  13096  -1028    893   -329       C  
ATOM    798  CG  LYS A1104     -38.984  20.360  -1.989  1.00130.69           C  
ANISOU  798  CG  LYS A1104    18866  16688  14102   -963    894   -359       C  
ATOM    799  CD  LYS A1104     -40.008  19.742  -1.054  1.00140.61           C  
ANISOU  799  CD  LYS A1104    20109  18068  15248  -1140    966   -319       C  
ATOM    800  CE  LYS A1104     -39.362  18.996   0.091  1.00155.10           C  
ANISOU  800  CE  LYS A1104    22099  19833  16997  -1110   1018   -222       C  
ATOM    801  NZ  LYS A1104     -40.321  18.752   1.202  1.00166.69           N1+
ANISOU  801  NZ  LYS A1104    23505  21471  18358  -1247   1083   -195       N1+
ATOM    802  N   TYR A1105     -37.316  22.415  -4.089  1.00117.16           N  
ANISOU  802  N   TYR A1105    17033  14849  12634   -616    725   -495       N  
ATOM    803  CA  TYR A1105     -37.526  23.783  -4.584  1.00115.64           C  
ANISOU  803  CA  TYR A1105    16660  14759  12520   -529    659   -588       C  
ATOM    804  C   TYR A1105     -36.381  24.281  -5.466  1.00117.13           C  
ANISOU  804  C   TYR A1105    16890  14820  12795   -391    603   -606       C  
ATOM    805  O   TYR A1105     -36.595  25.180  -6.286  1.00115.17           O  
ANISOU  805  O   TYR A1105    16541  14603  12614   -354    549   -673       O  
ATOM    806  CB  TYR A1105     -37.756  24.769  -3.413  1.00116.38           C  
ANISOU  806  CB  TYR A1105    16598  15030  12592   -445    656   -631       C  
ATOM    807  CG  TYR A1105     -38.899  24.396  -2.494  1.00118.61           C  
ANISOU  807  CG  TYR A1105    16814  15467  12784   -571    717   -618       C  
ATOM    808  CD1 TYR A1105     -40.218  24.461  -2.928  1.00121.33           C  
ANISOU  808  CD1 TYR A1105    17040  15941  13119   -696    724   -656       C  
ATOM    809  CD2 TYR A1105     -38.662  23.990  -1.184  1.00119.64           C  
ANISOU  809  CD2 TYR A1105    16991  15635  12831   -566    766   -565       C  
ATOM    810  CE1 TYR A1105     -41.275  24.126  -2.084  1.00123.52           C  
ANISOU  810  CE1 TYR A1105    17241  16384  13307   -819    785   -642       C  
ATOM    811  CE2 TYR A1105     -39.710  23.643  -0.332  1.00121.46           C  
ANISOU  811  CE2 TYR A1105    17161  16018  12971   -690    828   -550       C  
ATOM    812  CZ  TYR A1105     -41.016  23.719  -0.786  1.00128.33           C  
ANISOU  812  CZ  TYR A1105    17906  17020  13834   -818    839   -590       C  
ATOM    813  OH  TYR A1105     -42.059  23.382   0.035  1.00128.82           O  
ANISOU  813  OH  TYR A1105    17893  17252  13801   -949    904   -575       O  
ATOM    814  N   LEU A1106     -35.169  23.722  -5.281  1.00113.71           N  
ANISOU  814  N   LEU A1106    16598  14254  12352   -309    615   -543       N  
ATOM    815  CA  LEU A1106     -33.987  24.141  -6.032  1.00112.95           C  
ANISOU  815  CA  LEU A1106    16535  14055  12326   -176    570   -552       C  
ATOM    816  C   LEU A1106     -33.420  23.016  -6.921  1.00118.60           C  
ANISOU  816  C   LEU A1106    17441  14582  13041   -199    597   -494       C  
ATOM    817  O   LEU A1106     -32.244  22.637  -6.808  1.00118.31           O  
ANISOU  817  O   LEU A1106    17504  14451  12998    -88    606   -440       O  
ATOM    818  CB  LEU A1106     -32.911  24.760  -5.104  1.00112.43           C  
ANISOU  818  CB  LEU A1106    16429  14031  12256    -24    548   -543       C  
ATOM    819  CG  LEU A1106     -33.363  25.887  -4.156  1.00116.82           C  
ANISOU  819  CG  LEU A1106    16825  14759  12803     10    525   -606       C  
ATOM    820  CD1 LEU A1106     -32.204  26.410  -3.343  1.00116.50           C  
ANISOU  820  CD1 LEU A1106    16768  14746  12750    141    499   -597       C  
ATOM    821  CD2 LEU A1106     -34.009  27.033  -4.914  1.00118.95           C  
ANISOU  821  CD2 LEU A1106    16965  15087  13143     13    476   -700       C  
ATOM    822  N   ARG A  41     -34.274  22.509  -7.833  1.00116.16           N  
ANISOU  822  N   ARG A  41    17177  14226  12731   -341    608   -510       N  
ATOM    823  CA  ARG A  41     -33.907  21.457  -8.784  1.00116.86           C  
ANISOU  823  CA  ARG A  41    17459  14131  12813   -383    637   -472       C  
ATOM    824  C   ARG A  41     -33.014  22.075  -9.881  1.00120.06           C  
ANISOU  824  C   ARG A  41    17851  14468  13296   -263    588   -506       C  
ATOM    825  O   ARG A  41     -33.249  23.216 -10.305  1.00119.13           O  
ANISOU  825  O   ARG A  41    17582  14443  13239   -236    529   -573       O  
ATOM    826  CB  ARG A  41     -35.154  20.778  -9.408  1.00118.68           C  
ANISOU  826  CB  ARG A  41    17736  14350  13008   -596    659   -487       C  
ATOM    827  CG  ARG A  41     -36.322  20.488  -8.445  1.00128.41           C  
ANISOU  827  CG  ARG A  41    18909  15713  14169   -745    696   -476       C  
ATOM    828  CD  ARG A  41     -36.393  19.053  -7.946  1.00131.84           C  
ANISOU  828  CD  ARG A  41    19554  16029  14511   -859    774   -394       C  
ATOM    829  NE  ARG A  41     -37.741  18.719  -7.467  1.00139.46           N  
ANISOU  829  NE  ARG A  41    20463  17119  15408  -1066    806   -395       N  
ATOM    830  CZ  ARG A  41     -38.036  17.694  -6.667  1.00155.18           C  
ANISOU  830  CZ  ARG A  41    22587  19070  17305  -1185    876   -325       C  
ATOM    831  NH1 ARG A  41     -37.075  16.899  -6.207  1.00142.39           N  
ANISOU  831  NH1 ARG A  41    21170  17282  15648  -1099    920   -244       N  
ATOM    832  NH2 ARG A  41     -39.290  17.478  -6.289  1.00140.33           N  
ANISOU  832  NH2 ARG A  41    20630  17328  15360  -1386    904   -331       N  
ATOM    833  N   SER A  42     -31.977  21.332 -10.307  1.00115.77           N  
ANISOU  833  N   SER A  42    17472  13768  12747   -185    616   -455       N  
ATOM    834  CA  SER A  42     -31.030  21.787 -11.326  1.00114.00           C  
ANISOU  834  CA  SER A  42    17249  13480  12584    -72    583   -477       C  
ATOM    835  C   SER A  42     -30.986  20.872 -12.553  1.00116.81           C  
ANISOU  835  C   SER A  42    17782  13670  12929   -130    614   -470       C  
ATOM    836  O   SER A  42     -31.397  19.708 -12.477  1.00117.84           O  
ANISOU  836  O   SER A  42    18079  13700  12997   -232    671   -433       O  
ATOM    837  CB  SER A  42     -29.639  21.956 -10.724  1.00116.80           C  
ANISOU  837  CB  SER A  42    17603  13834  12943    112    583   -430       C  
ATOM    838  OG  SER A  42     -29.594  23.086  -9.869  1.00125.62           O  
ANISOU  838  OG  SER A  42    18541  15106  14081    165    537   -461       O  
ATOM    839  N   ALA A  43     -30.487  21.418 -13.684  1.00110.79           N  
ANISOU  839  N   ALA A  43    16995  12878  12223    -72    578   -509       N  
ATOM    840  CA  ALA A  43     -30.324  20.736 -14.971  1.00110.19           C  
ANISOU  840  CA  ALA A  43    17074  12654  12139   -107    602   -516       C  
ATOM    841  C   ALA A  43     -28.909  21.007 -15.515  1.00112.71           C  
ANISOU  841  C   ALA A  43    17409  12922  12493     71    600   -502       C  
ATOM    842  O   ALA A  43     -28.267  21.955 -15.063  1.00111.67           O  
ANISOU  842  O   ALA A  43    17133  12894  12403    183    561   -504       O  
ATOM    843  CB  ALA A  43     -31.369  21.244 -15.954  1.00110.50           C  
ANISOU  843  CB  ALA A  43    17038  12744  12204   -245    553   -588       C  
ATOM    844  N   SER A  44     -28.419  20.183 -16.476  1.00108.70           N  
ANISOU  844  N   SER A  44    17078  12262  11963     92    644   -490       N  
ATOM    845  CA  SER A  44     -27.089  20.360 -17.086  1.00107.27           C  
ANISOU  845  CA  SER A  44    16913  12042  11805    260    652   -475       C  
ATOM    846  C   SER A  44     -27.138  21.147 -18.395  1.00109.96           C  
ANISOU  846  C   SER A  44    17186  12401  12193    230    606   -539       C  
ATOM    847  O   SER A  44     -28.016  20.900 -19.228  1.00110.85           O  
ANISOU  847  O   SER A  44    17361  12465  12293     91    599   -582       O  
ATOM    848  CB  SER A  44     -26.419  19.015 -17.334  1.00110.66           C  
ANISOU  848  CB  SER A  44    17577  12294  12173    334    738   -421       C  
ATOM    849  OG  SER A  44     -25.100  19.192 -17.828  1.00116.67           O  
ANISOU  849  OG  SER A  44    18330  13049  12951    513    751   -402       O  
ATOM    850  N   SER A  45     -26.161  22.058 -18.593  1.00103.77           N  
ANISOU  850  N   SER A  45    16282  11689  11456    356    574   -542       N  
ATOM    851  CA  SER A  45     -26.038  22.883 -19.803  1.00102.03           C  
ANISOU  851  CA  SER A  45    15999  11489  11278    344    531   -592       C  
ATOM    852  C   SER A  45     -25.013  22.303 -20.794  1.00103.45           C  
ANISOU  852  C   SER A  45    16306  11567  11435    440    585   -574       C  
ATOM    853  O   SER A  45     -24.523  23.019 -21.679  1.00102.68           O  
ANISOU  853  O   SER A  45    16147  11500  11368    472    559   -599       O  
ATOM    854  CB  SER A  45     -25.710  24.332 -19.443  1.00105.01           C  
ANISOU  854  CB  SER A  45    16173  12011  11715    394    462   -611       C  
ATOM    855  OG  SER A  45     -24.411  24.502 -18.899  1.00113.54           O  
ANISOU  855  OG  SER A  45    17206  13137  12797    540    477   -566       O  
ATOM    856  N   LEU A  46     -24.733  20.985 -20.658  1.00 97.81           N  
ANISOU  856  N   LEU A  46    15779  10723  10660    484    664   -531       N  
ATOM    857  CA  LEU A  46     -23.780  20.251 -21.475  1.00 96.73           C  
ANISOU  857  CA  LEU A  46    15790  10476  10488    597    733   -511       C  
ATOM    858  C   LEU A  46     -24.217  20.094 -22.924  1.00101.08           C  
ANISOU  858  C   LEU A  46    16442  10940  11024    498    737   -569       C  
ATOM    859  O   LEU A  46     -23.384  20.236 -23.812  1.00100.80           O  
ANISOU  859  O   LEU A  46    16420  10892  10988    587    757   -575       O  
ATOM    860  CB  LEU A  46     -23.452  18.887 -20.837  1.00 97.23           C  
ANISOU  860  CB  LEU A  46    16046  10412  10484    678    818   -447       C  
ATOM    861  CG  LEU A  46     -22.467  17.972 -21.576  1.00101.53           C  
ANISOU  861  CG  LEU A  46    16773  10825  10978    825    905   -421       C  
ATOM    862  CD1 LEU A  46     -21.064  18.551 -21.600  1.00101.02           C  
ANISOU  862  CD1 LEU A  46    16570  10876  10936   1024    907   -386       C  
ATOM    863  CD2 LEU A  46     -22.451  16.602 -20.969  1.00104.56           C  
ANISOU  863  CD2 LEU A  46    17382  11055  11291    875    985   -364       C  
ATOM    864  N   ALA A  47     -25.500  19.782 -23.168  1.00 98.19           N  
ANISOU  864  N   ALA A  47    16145  10525  10637    312    718   -610       N  
ATOM    865  CA  ALA A  47     -26.013  19.571 -24.527  1.00 98.20           C  
ANISOU  865  CA  ALA A  47    16250  10450  10611    196    716   -667       C  
ATOM    866  C   ALA A  47     -26.034  20.866 -25.345  1.00100.11           C  
ANISOU  866  C   ALA A  47    16322  10810  10907    178    640   -709       C  
ATOM    867  O   ALA A  47     -25.909  20.812 -26.577  1.00 98.91           O  
ANISOU  867  O   ALA A  47    16244  10607  10732    158    647   -742       O  
ATOM    868  CB  ALA A  47     -27.394  18.943 -24.476  1.00 99.74           C  
ANISOU  868  CB  ALA A  47    16538  10594  10763    -13    708   -696       C  
ATOM    869  N   LEU A  48     -26.178  22.028 -24.652  1.00 95.04           N  
ANISOU  869  N   LEU A  48    15464  10317  10329    190    569   -706       N  
ATOM    870  CA  LEU A  48     -26.160  23.350 -25.276  1.00 93.70           C  
ANISOU  870  CA  LEU A  48    15137  10253  10212    186    496   -737       C  
ATOM    871  C   LEU A  48     -24.721  23.707 -25.679  1.00 96.61           C  
ANISOU  871  C   LEU A  48    15482  10633  10594    339    523   -713       C  
ATOM    872  O   LEU A  48     -24.505  24.143 -26.810  1.00 98.15           O  
ANISOU  872  O   LEU A  48    15678  10826  10788    330    509   -737       O  
ATOM    873  CB  LEU A  48     -26.737  24.416 -24.337  1.00 93.14           C  
ANISOU  873  CB  LEU A  48    14874  10318  10197    161    423   -744       C  
ATOM    874  CG  LEU A  48     -27.059  25.758 -24.987  1.00 97.53           C  
ANISOU  874  CG  LEU A  48    15294  10963  10799    130    341   -780       C  
ATOM    875  CD1 LEU A  48     -28.432  25.723 -25.621  1.00 98.58           C  
ANISOU  875  CD1 LEU A  48    15436  11106  10913    -20    296   -822       C  
ATOM    876  CD2 LEU A  48     -26.949  26.907 -23.978  1.00 98.33           C  
ANISOU  876  CD2 LEU A  48    15223  11181  10958    185    290   -776       C  
ATOM    877  N   ALA A  49     -23.746  23.491 -24.766  1.00 90.20           N  
ANISOU  877  N   ALA A  49    14646   9841   9784    476    564   -661       N  
ATOM    878  CA  ALA A  49     -22.318  23.729 -24.979  1.00 88.47           C  
ANISOU  878  CA  ALA A  49    14386   9661   9567    628    597   -628       C  
ATOM    879  C   ALA A  49     -21.786  22.911 -26.167  1.00 91.12           C  
ANISOU  879  C   ALA A  49    14885   9888   9849    676    670   -632       C  
ATOM    880  O   ALA A  49     -20.964  23.433 -26.925  1.00 89.99           O  
ANISOU  880  O   ALA A  49    14690   9793   9711    736    675   -633       O  
ATOM    881  CB  ALA A  49     -21.536  23.400 -23.715  1.00 89.19           C  
ANISOU  881  CB  ALA A  49    14440   9796   9652    757    629   -568       C  
ATOM    882  N   ILE A  50     -22.279  21.647 -26.342  1.00 88.01           N  
ANISOU  882  N   ILE A  50    14695   9348   9399    639    728   -639       N  
ATOM    883  CA  ILE A  50     -21.911  20.738 -27.447  1.00 88.68           C  
ANISOU  883  CA  ILE A  50    14976   9302   9419    675    805   -654       C  
ATOM    884  C   ILE A  50     -22.463  21.305 -28.762  1.00 93.79           C  
ANISOU  884  C   ILE A  50    15618   9954  10065    548    759   -715       C  
ATOM    885  O   ILE A  50     -21.720  21.415 -29.740  1.00 93.97           O  
ANISOU  885  O   ILE A  50    15666   9974  10065    614    792   -723       O  
ATOM    886  CB  ILE A  50     -22.344  19.256 -27.211  1.00 92.53           C  
ANISOU  886  CB  ILE A  50    15706   9613   9839    652    878   -648       C  
ATOM    887  CG1 ILE A  50     -21.614  18.630 -26.010  1.00 93.33           C  
ANISOU  887  CG1 ILE A  50    15834   9701   9928    813    933   -574       C  
ATOM    888  CG2 ILE A  50     -22.114  18.402 -28.464  1.00 93.66           C  
ANISOU  888  CG2 ILE A  50    16070   9609   9909    665    952   -681       C  
ATOM    889  CD1 ILE A  50     -22.249  17.330 -25.480  1.00100.41           C  
ANISOU  889  CD1 ILE A  50    16953  10432  10766    760    987   -558       C  
ATOM    890  N   ALA A  51     -23.758  21.692 -28.767  1.00 90.05           N  
ANISOU  890  N   ALA A  51    15101   9503   9610    373    683   -754       N  
ATOM    891  CA  ALA A  51     -24.427  22.283 -29.919  1.00 89.05           C  
ANISOU  891  CA  ALA A  51    14955   9401   9480    248    625   -805       C  
ATOM    892  C   ALA A  51     -23.694  23.557 -30.349  1.00 93.04           C  
ANISOU  892  C   ALA A  51    15298  10021  10032    317    584   -797       C  
ATOM    893  O   ALA A  51     -23.404  23.713 -31.542  1.00 92.63           O  
ANISOU  893  O   ALA A  51    15292   9954   9950    312    593   -817       O  
ATOM    894  CB  ALA A  51     -25.878  22.585 -29.580  1.00 89.20           C  
ANISOU  894  CB  ALA A  51    14905   9469   9517     80    544   -833       C  
ATOM    895  N   ILE A  52     -23.340  24.434 -29.374  1.00 89.58           N  
ANISOU  895  N   ILE A  52    14683   9694   9659    378    544   -765       N  
ATOM    896  CA  ILE A  52     -22.610  25.684 -29.647  1.00 89.28           C  
ANISOU  896  CA  ILE A  52    14497   9763   9664    429    505   -754       C  
ATOM    897  C   ILE A  52     -21.244  25.384 -30.300  1.00 92.84           C  
ANISOU  897  C   ILE A  52    14994  10203  10077    553    583   -730       C  
ATOM    898  O   ILE A  52     -20.965  25.928 -31.364  1.00 92.84           O  
ANISOU  898  O   ILE A  52    14984  10225  10066    534    573   -743       O  
ATOM    899  CB  ILE A  52     -22.530  26.604 -28.399  1.00 92.01           C  
ANISOU  899  CB  ILE A  52    14668  10218  10075    456    451   -732       C  
ATOM    900  CG1 ILE A  52     -23.916  27.248 -28.130  1.00 91.71           C  
ANISOU  900  CG1 ILE A  52    14561  10212  10070    334    364   -767       C  
ATOM    901  CG2 ILE A  52     -21.442  27.682 -28.569  1.00 92.88           C  
ANISOU  901  CG2 ILE A  52    14654  10424  10213    522    434   -711       C  
ATOM    902  CD1 ILE A  52     -24.176  27.753 -26.717  1.00 93.54           C  
ANISOU  902  CD1 ILE A  52    14673  10520  10348    347    326   -756       C  
ATOM    903  N   THR A  53     -20.452  24.460 -29.707  1.00 88.37           N  
ANISOU  903  N   THR A  53    14490   9604   9484    681    664   -692       N  
ATOM    904  CA  THR A  53     -19.161  23.984 -30.230  1.00 87.74           C  
ANISOU  904  CA  THR A  53    14458   9521   9358    827    753   -665       C  
ATOM    905  C   THR A  53     -19.340  23.451 -31.657  1.00 90.78           C  
ANISOU  905  C   THR A  53    15007   9805   9681    786    796   -707       C  
ATOM    906  O   THR A  53     -18.527  23.777 -32.526  1.00 90.10           O  
ANISOU  906  O   THR A  53    14898   9766   9572    839    827   -704       O  
ATOM    907  CB  THR A  53     -18.544  22.939 -29.265  1.00 88.54           C  
ANISOU  907  CB  THR A  53    14621   9587   9433    975    828   -616       C  
ATOM    908  OG1 THR A  53     -18.391  23.552 -27.980  1.00 91.63           O  
ANISOU  908  OG1 THR A  53    14847  10092   9877    998    777   -580       O  
ATOM    909  CG2 THR A  53     -17.202  22.377 -29.749  1.00 78.76           C  
ANISOU  909  CG2 THR A  53    13426   8357   8140   1156    926   -583       C  
ATOM    910  N   ALA A  54     -20.420  22.658 -31.892  1.00 87.02           N  
ANISOU  910  N   ALA A  54    14693   9200   9171    678    797   -747       N  
ATOM    911  CA  ALA A  54     -20.775  22.105 -33.202  1.00 86.88           C  
ANISOU  911  CA  ALA A  54    14848   9079   9083    608    828   -797       C  
ATOM    912  C   ALA A  54     -21.046  23.243 -34.216  1.00 90.02           C  
ANISOU  912  C   ALA A  54    15149   9559   9495    508    754   -825       C  
ATOM    913  O   ALA A  54     -20.467  23.237 -35.306  1.00 90.01           O  
ANISOU  913  O   ALA A  54    15202   9552   9444    542    797   -837       O  
ATOM    914  CB  ALA A  54     -21.974  21.174 -33.084  1.00 87.67           C  
ANISOU  914  CB  ALA A  54    15115   9049   9147    477    825   -834       C  
ATOM    915  N   LEU A  55     -21.842  24.256 -33.814  1.00 84.59           N  
ANISOU  915  N   LEU A  55    14314   8956   8871    406    649   -827       N  
ATOM    916  CA  LEU A  55     -22.148  25.411 -34.652  1.00 83.56           C  
ANISOU  916  CA  LEU A  55    14092   8901   8757    323    571   -843       C  
ATOM    917  C   LEU A  55     -20.899  26.180 -35.036  1.00 88.27           C  
ANISOU  917  C   LEU A  55    14594   9580   9363    419    595   -810       C  
ATOM    918  O   LEU A  55     -20.722  26.430 -36.222  1.00 89.64           O  
ANISOU  918  O   LEU A  55    14810   9756   9493    391    601   -825       O  
ATOM    919  CB  LEU A  55     -23.180  26.340 -33.983  1.00 82.62           C  
ANISOU  919  CB  LEU A  55    13833   8853   8705    230    462   -846       C  
ATOM    920  CG  LEU A  55     -23.743  27.513 -34.820  1.00 85.72           C  
ANISOU  920  CG  LEU A  55    14150   9309   9110    143    371   -859       C  
ATOM    921  CD1 LEU A  55     -24.549  27.022 -36.015  1.00 86.22           C  
ANISOU  921  CD1 LEU A  55    14341   9319   9101     31    357   -901       C  
ATOM    922  CD2 LEU A  55     -24.616  28.392 -33.972  1.00 85.64           C  
ANISOU  922  CD2 LEU A  55    14001   9370   9168     98    279   -857       C  
ATOM    923  N   TYR A  56     -20.021  26.532 -34.073  1.00 84.84           N  
ANISOU  923  N   TYR A  56    14036   9225   8975    523    609   -766       N  
ATOM    924  CA  TYR A  56     -18.790  27.281 -34.386  1.00 85.70           C  
ANISOU  924  CA  TYR A  56    14040   9435   9087    596    631   -732       C  
ATOM    925  C   TYR A  56     -17.798  26.493 -35.248  1.00 91.84           C  
ANISOU  925  C   TYR A  56    14917  10189   9788    698    741   -727       C  
ATOM    926  O   TYR A  56     -17.224  27.054 -36.174  1.00 91.32           O  
ANISOU  926  O   TYR A  56    14822  10180   9696    693    753   -722       O  
ATOM    927  CB  TYR A  56     -18.100  27.850 -33.131  1.00 86.92           C  
ANISOU  927  CB  TYR A  56    14031   9695   9298    666    615   -688       C  
ATOM    928  CG  TYR A  56     -18.785  29.074 -32.558  1.00 88.44           C  
ANISOU  928  CG  TYR A  56    14101   9940   9560    570    507   -695       C  
ATOM    929  CD1 TYR A  56     -18.999  30.209 -33.335  1.00 90.72           C  
ANISOU  929  CD1 TYR A  56    14348  10259   9862    483    445   -704       C  
ATOM    930  CD2 TYR A  56     -19.195  29.109 -31.231  1.00 88.69           C  
ANISOU  930  CD2 TYR A  56    14069   9989   9639    575    472   -690       C  
ATOM    931  CE1 TYR A  56     -19.641  31.332 -32.816  1.00 91.05           C  
ANISOU  931  CE1 TYR A  56    14298  10333   9963    413    350   -711       C  
ATOM    932  CE2 TYR A  56     -19.828  30.231 -30.699  1.00 88.81           C  
ANISOU  932  CE2 TYR A  56    13983  10048   9712    501    380   -701       C  
ATOM    933  CZ  TYR A  56     -20.060  31.337 -31.498  1.00 94.53           C  
ANISOU  933  CZ  TYR A  56    14678  10789  10450    425    320   -713       C  
ATOM    934  OH  TYR A  56     -20.664  32.451 -30.970  1.00 95.38           O  
ANISOU  934  OH  TYR A  56    14702  10928  10610    372    235   -724       O  
ATOM    935  N   SER A  57     -17.641  25.194 -34.978  1.00 90.83           N  
ANISOU  935  N   SER A  57    14921   9972   9619    790    823   -729       N  
ATOM    936  CA  SER A  57     -16.753  24.304 -35.726  1.00 92.09           C  
ANISOU  936  CA  SER A  57    15200  10092   9698    913    939   -728       C  
ATOM    937  C   SER A  57     -17.208  24.092 -37.175  1.00 95.05           C  
ANISOU  937  C   SER A  57    15724  10388  10005    825    953   -781       C  
ATOM    938  O   SER A  57     -16.363  24.063 -38.070  1.00 94.64           O  
ANISOU  938  O   SER A  57    15694  10369   9895    895   1022   -780       O  
ATOM    939  CB  SER A  57     -16.615  22.974 -35.005  1.00 97.26           C  
ANISOU  939  CB  SER A  57    15984  10644  10325   1032   1017   -717       C  
ATOM    940  OG  SER A  57     -17.891  22.400 -34.783  1.00107.66           O  
ANISOU  940  OG  SER A  57    17435  11829  11643    912    981   -755       O  
ATOM    941  N   ALA A  58     -18.535  23.976 -37.407  1.00 91.32           N  
ANISOU  941  N   ALA A  58    15341   9827   9531    670    887   -828       N  
ATOM    942  CA  ALA A  58     -19.103  23.811 -38.751  1.00 91.94           C  
ANISOU  942  CA  ALA A  58    15556   9841   9538    564    883   -881       C  
ATOM    943  C   ALA A  58     -18.985  25.111 -39.538  1.00 96.50           C  
ANISOU  943  C   ALA A  58    16008  10531  10127    498    820   -870       C  
ATOM    944  O   ALA A  58     -18.587  25.082 -40.711  1.00 98.08           O  
ANISOU  944  O   ALA A  58    16279  10731  10254    500    863   -886       O  
ATOM    945  CB  ALA A  58     -20.560  23.383 -38.675  1.00 92.49           C  
ANISOU  945  CB  ALA A  58    15727   9817   9600    406    820   -926       C  
ATOM    946  N   VAL A  59     -19.315  26.254 -38.897  1.00 90.40           N  
ANISOU  946  N   VAL A  59    15061   9848   9440    442    721   -842       N  
ATOM    947  CA  VAL A  59     -19.207  27.535 -39.576  1.00 89.39           C  
ANISOU  947  CA  VAL A  59    14831   9811   9324    381    659   -824       C  
ATOM    948  C   VAL A  59     -17.725  27.885 -39.790  1.00 92.40           C  
ANISOU  948  C   VAL A  59    15133  10286   9690    488    732   -783       C  
ATOM    949  O   VAL A  59     -17.412  28.535 -40.785  1.00 93.35           O  
ANISOU  949  O   VAL A  59    15241  10455   9773    448    728   -775       O  
ATOM    950  CB  VAL A  59     -20.043  28.686 -38.968  1.00 92.35           C  
ANISOU  950  CB  VAL A  59    15072  10236   9781    291    534   -812       C  
ATOM    951  CG1 VAL A  59     -21.482  28.252 -38.757  1.00 92.06           C  
ANISOU  951  CG1 VAL A  59    15097  10133   9748    192    472   -851       C  
ATOM    952  CG2 VAL A  59     -19.458  29.183 -37.668  1.00 92.00           C  
ANISOU  952  CG2 VAL A  59    14879  10262   9816    362    526   -773       C  
ATOM    953  N   CYS A  60     -16.813  27.392 -38.915  1.00 85.97           N  
ANISOU  953  N   CYS A  60    14269   9505   8892    624    803   -753       N  
ATOM    954  CA  CYS A  60     -15.389  27.646 -39.102  1.00 84.86           C  
ANISOU  954  CA  CYS A  60    14036   9480   8727    728    877   -711       C  
ATOM    955  C   CYS A  60     -14.805  26.798 -40.230  1.00 90.24           C  
ANISOU  955  C   CYS A  60    14853  10129   9306    804    989   -732       C  
ATOM    956  O   CYS A  60     -14.183  27.350 -41.128  1.00 89.89           O  
ANISOU  956  O   CYS A  60    14770  10165   9218    791   1015   -718       O  
ATOM    957  CB  CYS A  60     -14.597  27.494 -37.809  1.00 84.25           C  
ANISOU  957  CB  CYS A  60    13837   9480   8694    849    905   -667       C  
ATOM    958  SG  CYS A  60     -12.819  27.794 -37.998  1.00 88.81           S  
ANISOU  958  SG  CYS A  60    14270  10242   9232    974    994   -611       S  
ATOM    959  N   ALA A  61     -15.007  25.473 -40.188  1.00 88.53           N  
ANISOU  959  N   ALA A  61    14805   9789   9044    880   1060   -764       N  
ATOM    960  CA  ALA A  61     -14.478  24.551 -41.189  1.00 90.35           C  
ANISOU  960  CA  ALA A  61    15194   9966   9170    971   1178   -792       C  
ATOM    961  C   ALA A  61     -14.926  24.858 -42.618  1.00 94.53           C  
ANISOU  961  C   ALA A  61    15817  10470   9631    848   1160   -834       C  
ATOM    962  O   ALA A  61     -14.070  24.961 -43.491  1.00 95.15           O  
ANISOU  962  O   ALA A  61    15892  10618   9641    904   1234   -827       O  
ATOM    963  CB  ALA A  61     -14.809  23.127 -40.812  1.00 92.13           C  
ANISOU  963  CB  ALA A  61    15613  10031   9362   1050   1242   -824       C  
ATOM    964  N   VAL A  62     -16.238  25.074 -42.846  1.00 90.32           N  
ANISOU  964  N   VAL A  62    15348   9859   9112    679   1059   -872       N  
ATOM    965  CA  VAL A  62     -16.783  25.450 -44.160  1.00 90.06           C  
ANISOU  965  CA  VAL A  62    15393   9815   9013    549   1021   -905       C  
ATOM    966  C   VAL A  62     -16.186  26.810 -44.593  1.00 94.59           C  
ANISOU  966  C   VAL A  62    15800  10535   9603    517    985   -855       C  
ATOM    967  O   VAL A  62     -15.623  26.907 -45.683  1.00 95.54           O  
ANISOU  967  O   VAL A  62    15962  10697   9642    525   1042   -857       O  
ATOM    968  CB  VAL A  62     -18.342  25.462 -44.172  1.00 92.88           C  
ANISOU  968  CB  VAL A  62    15816  10089   9384    379    907   -946       C  
ATOM    969  CG1 VAL A  62     -18.891  26.077 -45.452  1.00 92.73           C  
ANISOU  969  CG1 VAL A  62    15836  10093   9303    247    846   -965       C  
ATOM    970  CG2 VAL A  62     -18.901  24.065 -43.987  1.00 93.48           C  
ANISOU  970  CG2 VAL A  62    16088  10014   9416    379    954  -1001       C  
ATOM    971  N   GLY A  63     -16.278  27.806 -43.705  1.00 89.90           N  
ANISOU  971  N   GLY A  63    15034  10014   9111    482    898   -810       N  
ATOM    972  CA  GLY A  63     -15.812  29.172 -43.914  1.00 88.90           C  
ANISOU  972  CA  GLY A  63    14759  10007   9012    431    851   -759       C  
ATOM    973  C   GLY A  63     -14.340  29.358 -44.218  1.00 92.90           C  
ANISOU  973  C   GLY A  63    15184  10636   9478    522    949   -719       C  
ATOM    974  O   GLY A  63     -14.002  29.967 -45.232  1.00 92.56           O  
ANISOU  974  O   GLY A  63    15140  10652   9378    467    959   -704       O  
ATOM    975  N   LEU A  64     -13.459  28.853 -43.342  1.00 89.92           N  
ANISOU  975  N   LEU A  64    14730  10313   9123    660   1022   -697       N  
ATOM    976  CA  LEU A  64     -12.007  28.975 -43.473  1.00 91.11           C  
ANISOU  976  CA  LEU A  64    14769  10613   9235    762   1118   -653       C  
ATOM    977  C   LEU A  64     -11.456  28.156 -44.630  1.00 98.16           C  
ANISOU  977  C   LEU A  64    15786  11499  10009    846   1242   -679       C  
ATOM    978  O   LEU A  64     -10.910  28.737 -45.568  1.00 99.85           O  
ANISOU  978  O   LEU A  64    15967  11806  10163    803   1271   -660       O  
ATOM    979  CB  LEU A  64     -11.312  28.619 -42.146  1.00 91.53           C  
ANISOU  979  CB  LEU A  64    14701  10734   9341    895   1150   -619       C  
ATOM    980  CG  LEU A  64      -9.792  28.734 -42.070  1.00 98.14           C  
ANISOU  980  CG  LEU A  64    15385  11762  10142   1009   1242   -566       C  
ATOM    981  CD1 LEU A  64      -9.344  30.187 -42.017  1.00 98.46           C  
ANISOU  981  CD1 LEU A  64    15246  11948  10215    881   1178   -518       C  
ATOM    982  CD2 LEU A  64      -9.273  28.026 -40.839  1.00101.85           C  
ANISOU  982  CD2 LEU A  64    15784  12271  10643   1171   1281   -541       C  
ATOM    983  N   LEU A  65     -11.626  26.820 -44.591  1.00 94.69           N  
ANISOU  983  N   LEU A  65    15505  10943   9529    960   1316   -723       N  
ATOM    984  CA  LEU A  65     -11.130  25.901 -45.624  1.00 94.82           C  
ANISOU  984  CA  LEU A  65    15672  10929   9426   1062   1445   -759       C  
ATOM    985  C   LEU A  65     -11.766  26.165 -46.983  1.00 99.58           C  
ANISOU  985  C   LEU A  65    16403  11478   9953    920   1419   -801       C  
ATOM    986  O   LEU A  65     -11.072  26.063 -47.999  1.00101.64           O  
ANISOU  986  O   LEU A  65    16701  11801  10114    964   1511   -807       O  
ATOM    987  CB  LEU A  65     -11.306  24.432 -45.201  1.00 95.17           C  
ANISOU  987  CB  LEU A  65    15891  10824   9447   1201   1519   -801       C  
ATOM    988  CG  LEU A  65     -10.431  23.886 -44.048  1.00 99.38           C  
ANISOU  988  CG  LEU A  65    16330  11414  10014   1402   1587   -755       C  
ATOM    989  CD1 LEU A  65     -10.896  24.399 -42.670  1.00 98.49           C  
ANISOU  989  CD1 LEU A  65    16080  11316  10024   1344   1474   -719       C  
ATOM    990  CD2 LEU A  65     -10.509  22.389 -44.000  1.00100.58           C  
ANISOU  990  CD2 LEU A  65    16708  11402  10107   1551   1686   -798       C  
ATOM    991  N   GLY A  66     -13.051  26.546 -46.993  1.00 94.20           N  
ANISOU  991  N   GLY A  66    15774  10702   9314    755   1293   -825       N  
ATOM    992  CA  GLY A  66     -13.780  26.898 -48.211  1.00 93.76           C  
ANISOU  992  CA  GLY A  66    15825  10608   9190    608   1242   -857       C  
ATOM    993  C   GLY A  66     -13.185  28.095 -48.931  1.00 97.76           C  
ANISOU  993  C   GLY A  66    16215  11258   9673    543   1229   -805       C  
ATOM    994  O   GLY A  66     -12.889  28.010 -50.125  1.00 97.80           O  
ANISOU  994  O   GLY A  66    16305  11287   9568    531   1291   -821       O  
ATOM    995  N   ASN A  67     -12.952  29.209 -48.190  1.00 94.05           N  
ANISOU  995  N   ASN A  67    15553  10883   9297    501   1157   -742       N  
ATOM    996  CA  ASN A  67     -12.361  30.447 -48.726  1.00 93.82           C  
ANISOU  996  CA  ASN A  67    15410  10985   9254    421   1139   -683       C  
ATOM    997  C   ASN A  67     -10.862  30.327 -49.023  1.00 99.45           C  
ANISOU  997  C   ASN A  67    16036  11848   9901    528   1276   -650       C  
ATOM    998  O   ASN A  67     -10.370  31.003 -49.934  1.00 98.92           O  
ANISOU  998  O   ASN A  67    15943  11874   9766    461   1299   -619       O  
ATOM    999  CB  ASN A  67     -12.669  31.641 -47.842  1.00 90.99           C  
ANISOU  999  CB  ASN A  67    14908  10655   9009    330   1018   -635       C  
ATOM   1000  CG  ASN A  67     -14.116  32.051 -47.946  1.00105.75           C  
ANISOU 1000  CG  ASN A  67    16854  12413  10913    207    883   -656       C  
ATOM   1001  OD1 ASN A  67     -14.637  32.322 -49.029  1.00 94.37           O  
ANISOU 1001  OD1 ASN A  67    15509  10945   9404    119    849   -663       O  
ATOM   1002  ND2 ASN A  67     -14.805  32.090 -46.826  1.00 98.29           N  
ANISOU 1002  ND2 ASN A  67    15864  11412  10069    205    805   -664       N  
ATOM   1003  N   VAL A  68     -10.149  29.434 -48.296  1.00 97.54           N  
ANISOU 1003  N   VAL A  68    15755  11637   9669    698   1369   -655       N  
ATOM   1004  CA  VAL A  68      -8.737  29.132 -48.562  1.00 98.80           C  
ANISOU 1004  CA  VAL A  68    15830  11953   9755    834   1511   -627       C  
ATOM   1005  C   VAL A  68      -8.683  28.394 -49.914  1.00104.94           C  
ANISOU 1005  C   VAL A  68    16789  12685  10397    875   1612   -679       C  
ATOM   1006  O   VAL A  68      -7.823  28.707 -50.747  1.00106.84           O  
ANISOU 1006  O   VAL A  68    16980  13064  10551    882   1693   -653       O  
ATOM   1007  CB  VAL A  68      -8.040  28.368 -47.401  1.00102.28           C  
ANISOU 1007  CB  VAL A  68    16182  12442  10239   1024   1576   -613       C  
ATOM   1008  CG1 VAL A  68      -6.712  27.751 -47.853  1.00103.71           C  
ANISOU 1008  CG1 VAL A  68    16318  12766  10319   1205   1740   -599       C  
ATOM   1009  CG2 VAL A  68      -7.818  29.293 -46.201  1.00100.76           C  
ANISOU 1009  CG2 VAL A  68    15777  12350  10156    968   1488   -554       C  
ATOM   1010  N   LEU A  69      -9.663  27.488 -50.162  1.00100.49           N  
ANISOU 1010  N   LEU A  69    16440  11932   9809    877   1599   -752       N  
ATOM   1011  CA  LEU A  69      -9.780  26.792 -51.442  1.00101.31           C  
ANISOU 1011  CA  LEU A  69    16746  11970   9778    890   1680   -813       C  
ATOM   1012  C   LEU A  69     -10.129  27.783 -52.543  1.00105.40           C  
ANISOU 1012  C   LEU A  69    17276  12529  10242    709   1616   -799       C  
ATOM   1013  O   LEU A  69      -9.448  27.768 -53.560  1.00107.62           O  
ANISOU 1013  O   LEU A  69    17586  12895  10408    734   1712   -800       O  
ATOM   1014  CB  LEU A  69     -10.791  25.633 -51.383  1.00101.35           C  
ANISOU 1014  CB  LEU A  69    16981  11759   9767    903   1670   -896       C  
ATOM   1015  CG  LEU A  69     -11.105  24.890 -52.693  1.00106.46           C  
ANISOU 1015  CG  LEU A  69    17871  12310  10269    885   1736   -975       C  
ATOM   1016  CD1 LEU A  69      -9.909  24.085 -53.192  1.00108.32           C  
ANISOU 1016  CD1 LEU A  69    18161  12602  10395   1088   1922   -993       C  
ATOM   1017  CD2 LEU A  69     -12.308  23.998 -52.522  1.00107.47           C  
ANISOU 1017  CD2 LEU A  69    18206  12229  10398    828   1685  -1050       C  
ATOM   1018  N   VAL A  70     -11.133  28.675 -52.331  1.00100.27           N  
ANISOU 1018  N   VAL A  70    16597  11831   9669    539   1459   -779       N  
ATOM   1019  CA  VAL A  70     -11.516  29.720 -53.303  1.00 99.69           C  
ANISOU 1019  CA  VAL A  70    16533  11793   9551    371   1382   -751       C  
ATOM   1020  C   VAL A  70     -10.272  30.520 -53.707  1.00104.73           C  
ANISOU 1020  C   VAL A  70    17029  12617  10146    373   1454   -682       C  
ATOM   1021  O   VAL A  70      -9.958  30.557 -54.895  1.00105.40           O  
ANISOU 1021  O   VAL A  70    17187  12753  10109    346   1518   -686       O  
ATOM   1022  CB  VAL A  70     -12.684  30.628 -52.814  1.00101.63           C  
ANISOU 1022  CB  VAL A  70    16742  11974   9899    225   1204   -728       C  
ATOM   1023  CG1 VAL A  70     -12.818  31.883 -53.664  1.00101.18           C  
ANISOU 1023  CG1 VAL A  70    16662  11977   9806     80   1133   -673       C  
ATOM   1024  CG2 VAL A  70     -13.999  29.867 -52.807  1.00101.25           C  
ANISOU 1024  CG2 VAL A  70    16852  11768   9852    185   1136   -799       C  
ATOM   1025  N   MET A  71      -9.529  31.083 -52.717  1.00101.40           N  
ANISOU 1025  N   MET A  71    16408  12306   9816    405   1452   -622       N  
ATOM   1026  CA  MET A  71      -8.295  31.854 -52.937  1.00102.04           C  
ANISOU 1026  CA  MET A  71    16326  12583   9861    391   1518   -551       C  
ATOM   1027  C   MET A  71      -7.247  31.080 -53.744  1.00108.73           C  
ANISOU 1027  C   MET A  71    17196  13540  10576    522   1692   -568       C  
ATOM   1028  O   MET A  71      -6.640  31.663 -54.641  1.00109.52           O  
ANISOU 1028  O   MET A  71    17261  13764  10585    455   1743   -531       O  
ATOM   1029  CB  MET A  71      -7.685  32.342 -51.614  1.00103.49           C  
ANISOU 1029  CB  MET A  71    16300  12866  10157    417   1493   -499       C  
ATOM   1030  CG  MET A  71      -8.357  33.564 -51.032  1.00105.05           C  
ANISOU 1030  CG  MET A  71    16438  13018  10459    256   1339   -459       C  
ATOM   1031  SD  MET A  71      -7.552  34.187 -49.523  1.00107.95           S  
ANISOU 1031  SD  MET A  71    16565  13514  10937    268   1314   -403       S  
ATOM   1032  CE  MET A  71      -7.879  32.876 -48.376  1.00103.96           C  
ANISOU 1032  CE  MET A  71    16081  12918  10504    451   1329   -457       C  
ATOM   1033  N   PHE A  72      -7.057  29.774 -53.447  1.00106.98           N  
ANISOU 1033  N   PHE A  72    17044  13268  10335    711   1788   -624       N  
ATOM   1034  CA  PHE A  72      -6.109  28.904 -54.159  1.00109.38           C  
ANISOU 1034  CA  PHE A  72    17389  13658  10510    875   1963   -650       C  
ATOM   1035  C   PHE A  72      -6.469  28.726 -55.640  1.00114.65           C  
ANISOU 1035  C   PHE A  72    18251  14272  11039    808   2001   -698       C  
ATOM   1036  O   PHE A  72      -5.582  28.833 -56.490  1.00116.64           O  
ANISOU 1036  O   PHE A  72    18468  14673  11177    838   2114   -679       O  
ATOM   1037  CB  PHE A  72      -5.935  27.540 -53.453  1.00111.80           C  
ANISOU 1037  CB  PHE A  72    17761  13887  10831   1101   2048   -699       C  
ATOM   1038  CG  PHE A  72      -5.253  26.473 -54.286  1.00115.87           C  
ANISOU 1038  CG  PHE A  72    18397  14424  11203   1284   2224   -749       C  
ATOM   1039  CD1 PHE A  72      -3.886  26.534 -54.545  1.00120.93           C  
ANISOU 1039  CD1 PHE A  72    18881  15296  11771   1409   2361   -704       C  
ATOM   1040  CD2 PHE A  72      -5.974  25.400 -54.802  1.00118.78           C  
ANISOU 1040  CD2 PHE A  72    19038  14587  11504   1331   2258   -842       C  
ATOM   1041  CE1 PHE A  72      -3.257  25.546 -55.314  1.00123.68           C  
ANISOU 1041  CE1 PHE A  72    19343  15668  11981   1599   2532   -753       C  
ATOM   1042  CE2 PHE A  72      -5.341  24.413 -55.569  1.00123.54           C  
ANISOU 1042  CE2 PHE A  72    19774  15196  11968   1509   2427   -895       C  
ATOM   1043  CZ  PHE A  72      -3.989  24.493 -55.818  1.00123.04           C  
ANISOU 1043  CZ  PHE A  72    19553  15362  11836   1653   2566   -850       C  
ATOM   1044  N   VAL A  73      -7.754  28.453 -55.946  1.00109.64           N  
ANISOU 1044  N   VAL A  73    17813  13440  10405    715   1908   -757       N  
ATOM   1045  CA  VAL A  73      -8.235  28.286 -57.323  1.00110.13           C  
ANISOU 1045  CA  VAL A  73    18071  13444  10331    633   1923   -807       C  
ATOM   1046  C   VAL A  73      -8.068  29.598 -58.136  1.00115.50           C  
ANISOU 1046  C   VAL A  73    18671  14249  10964    462   1876   -735       C  
ATOM   1047  O   VAL A  73      -7.738  29.529 -59.312  1.00116.83           O  
ANISOU 1047  O   VAL A  73    18923  14477  10991    448   1958   -748       O  
ATOM   1048  CB  VAL A  73      -9.674  27.703 -57.388  1.00112.55           C  
ANISOU 1048  CB  VAL A  73    18586  13530  10646    557   1822   -884       C  
ATOM   1049  CG1 VAL A  73     -10.144  27.514 -58.829  1.00113.23           C  
ANISOU 1049  CG1 VAL A  73    18872  13572  10578    466   1834   -937       C  
ATOM   1050  CG2 VAL A  73      -9.773  26.389 -56.621  1.00112.19           C  
ANISOU 1050  CG2 VAL A  73    18639  13355  10634    716   1881   -950       C  
ATOM   1051  N   ILE A  74      -8.236  30.775 -57.505  1.00111.85           N  
ANISOU 1051  N   ILE A  74    18056  13826  10614    340   1754   -659       N  
ATOM   1052  CA  ILE A  74      -8.077  32.066 -58.183  1.00112.52           C  
ANISOU 1052  CA  ILE A  74    18080  14010  10661    174   1706   -582       C  
ATOM   1053  C   ILE A  74      -6.589  32.364 -58.451  1.00119.75           C  
ANISOU 1053  C   ILE A  74    18842  15149  11509    219   1845   -526       C  
ATOM   1054  O   ILE A  74      -6.221  32.712 -59.577  1.00120.29           O  
ANISOU 1054  O   ILE A  74    18949  15306  11451    151   1901   -503       O  
ATOM   1055  CB  ILE A  74      -8.837  33.212 -57.442  1.00113.79           C  
ANISOU 1055  CB  ILE A  74    18164  14112  10958     31   1529   -526       C  
ATOM   1056  CG1 ILE A  74     -10.360  33.069 -57.698  1.00113.36           C  
ANISOU 1056  CG1 ILE A  74    18280  13878  10915    -47   1397   -573       C  
ATOM   1057  CG2 ILE A  74      -8.313  34.621 -57.839  1.00114.05           C  
ANISOU 1057  CG2 ILE A  74    18096  14268  10971   -117   1502   -428       C  
ATOM   1058  CD1 ILE A  74     -11.275  34.120 -57.121  1.00119.01           C  
ANISOU 1058  CD1 ILE A  74    18950  14523  11746   -167   1224   -527       C  
ATOM   1059  N   VAL A  75      -5.741  32.201 -57.428  1.00117.58           N  
ANISOU 1059  N   VAL A  75    18389  14977  11309    333   1900   -502       N  
ATOM   1060  CA  VAL A  75      -4.307  32.461 -57.533  1.00119.41           C  
ANISOU 1060  CA  VAL A  75    18438  15451  11483    379   2028   -445       C  
ATOM   1061  C   VAL A  75      -3.620  31.483 -58.526  1.00129.83           C  
ANISOU 1061  C   VAL A  75    19837  16850  12642    529   2208   -493       C  
ATOM   1062  O   VAL A  75      -2.938  31.942 -59.445  1.00131.40           O  
ANISOU 1062  O   VAL A  75    19996  17206  12726    468   2287   -454       O  
ATOM   1063  CB  VAL A  75      -3.653  32.486 -56.118  1.00121.74           C  
ANISOU 1063  CB  VAL A  75    18517  15843  11896    468   2028   -410       C  
ATOM   1064  CG1 VAL A  75      -2.129  32.422 -56.177  1.00122.96           C  
ANISOU 1064  CG1 VAL A  75    18474  16269  11975    564   2181   -364       C  
ATOM   1065  CG2 VAL A  75      -4.106  33.713 -55.333  1.00119.89           C  
ANISOU 1065  CG2 VAL A  75    18190  15574  11788    288   1868   -352       C  
ATOM   1066  N   ARG A  76      -3.857  30.162 -58.377  1.00128.88           N  
ANISOU 1066  N   ARG A  76    19850  16610  12507    715   2271   -579       N  
ATOM   1067  CA  ARG A  76      -3.212  29.118 -59.173  1.00131.53           C  
ANISOU 1067  CA  ARG A  76    20280  16999  12697    893   2450   -635       C  
ATOM   1068  C   ARG A  76      -3.872  28.742 -60.516  1.00138.28           C  
ANISOU 1068  C   ARG A  76    21393  17734  13413    835   2470   -706       C  
ATOM   1069  O   ARG A  76      -3.145  28.281 -61.399  1.00140.12           O  
ANISOU 1069  O   ARG A  76    21670  18071  13499    933   2623   -731       O  
ATOM   1070  CB  ARG A  76      -3.042  27.848 -58.320  1.00132.66           C  
ANISOU 1070  CB  ARG A  76    20455  17066  12883   1140   2522   -690       C  
ATOM   1071  CG  ARG A  76      -1.676  27.162 -58.461  1.00148.17           C  
ANISOU 1071  CG  ARG A  76    22323  19224  14750   1380   2722   -687       C  
ATOM   1072  CD  ARG A  76      -0.504  27.991 -57.935  1.00160.21           C  
ANISOU 1072  CD  ARG A  76    23526  21038  16307   1376   2752   -583       C  
ATOM   1073  NE  ARG A  76      -0.625  28.306 -56.509  1.00164.47           N  
ANISOU 1073  NE  ARG A  76    23912  21569  17011   1365   2641   -538       N  
ATOM   1074  CZ  ARG A  76       0.057  29.265 -55.888  1.00176.52           C  
ANISOU 1074  CZ  ARG A  76    25174  23298  18596   1276   2603   -450       C  
ATOM   1075  NH1 ARG A  76       0.910  30.027 -56.563  1.00164.83           N1+
ANISOU 1075  NH1 ARG A  76    23549  22050  17027   1179   2666   -390       N1+
ATOM   1076  NH2 ARG A  76      -0.119  29.479 -54.591  1.00160.90           N  
ANISOU 1076  NH2 ARG A  76    23082  21295  16759   1269   2501   -420       N  
ATOM   1077  N   TYR A  77      -5.208  28.893 -60.682  1.00134.88           N  
ANISOU 1077  N   TYR A  77    21127  17103  13017    686   2323   -741       N  
ATOM   1078  CA  TYR A  77      -5.878  28.459 -61.923  1.00136.01           C  
ANISOU 1078  CA  TYR A  77    21519  17138  13020    628   2334   -814       C  
ATOM   1079  C   TYR A  77      -6.642  29.570 -62.655  1.00140.32           C  
ANISOU 1079  C   TYR A  77    22103  17670  13541    386   2197   -768       C  
ATOM   1080  O   TYR A  77      -6.256  29.912 -63.778  1.00140.88           O  
ANISOU 1080  O   TYR A  77    22210  17847  13473    324   2260   -750       O  
ATOM   1081  CB  TYR A  77      -6.775  27.233 -61.667  1.00136.99           C  
ANISOU 1081  CB  TYR A  77    21862  17032  13155    708   2317   -921       C  
ATOM   1082  CG  TYR A  77      -6.002  26.070 -61.084  1.00140.15           C  
ANISOU 1082  CG  TYR A  77    22267  17429  13555    966   2467   -966       C  
ATOM   1083  CD1 TYR A  77      -5.284  25.204 -61.904  1.00144.36           C  
ANISOU 1083  CD1 TYR A  77    22918  18002  13930   1126   2648  -1025       C  
ATOM   1084  CD2 TYR A  77      -5.931  25.875 -59.708  1.00140.11           C  
ANISOU 1084  CD2 TYR A  77    22142  17392  13700   1062   2432   -942       C  
ATOM   1085  CE1 TYR A  77      -4.535  24.156 -61.369  1.00146.76           C  
ANISOU 1085  CE1 TYR A  77    23227  18305  14228   1388   2791  -1058       C  
ATOM   1086  CE2 TYR A  77      -5.189  24.829 -59.162  1.00142.29           C  
ANISOU 1086  CE2 TYR A  77    22421  17672  13971   1314   2568   -970       C  
ATOM   1087  CZ  TYR A  77      -4.496  23.968 -59.996  1.00153.10           C  
ANISOU 1087  CZ  TYR A  77    23913  19074  15184   1483   2748  -1026       C  
ATOM   1088  OH  TYR A  77      -3.769  22.933 -59.452  1.00156.05           O  
ANISOU 1088  OH  TYR A  77    24299  19446  15548   1755   2884  -1050       O  
ATOM   1089  N   THR A  78      -7.713  30.126 -62.045  1.00136.31           N  
ANISOU 1089  N   THR A  78    21593  17040  13160    258   2016   -748       N  
ATOM   1090  CA  THR A  78      -8.479  31.227 -62.647  1.00136.03           C  
ANISOU 1090  CA  THR A  78    21589  16987  13109     48   1875   -694       C  
ATOM   1091  C   THR A  78      -7.763  32.548 -62.294  1.00140.47           C  
ANISOU 1091  C   THR A  78    21939  17699  13736    -37   1849   -576       C  
ATOM   1092  O   THR A  78      -8.245  33.333 -61.467  1.00139.12           O  
ANISOU 1092  O   THR A  78    21679  17479  13701   -119   1715   -526       O  
ATOM   1093  CB  THR A  78     -10.009  31.153 -62.347  1.00140.76           C  
ANISOU 1093  CB  THR A  78    22304  17396  13782    -41   1702   -733       C  
ATOM   1094  OG1 THR A  78     -10.672  32.285 -62.905  1.00141.05           O  
ANISOU 1094  OG1 THR A  78    22354  17435  13803   -219   1568   -668       O  
ATOM   1095  CG2 THR A  78     -10.346  31.007 -60.878  1.00136.15           C  
ANISOU 1095  CG2 THR A  78    21622  16732  13378     16   1631   -736       C  
ATOM   1096  N   LYS A  79      -6.571  32.751 -62.917  1.00137.96           N  
ANISOU 1096  N   LYS A  79    21541  17567  13310    -17   1989   -536       N  
ATOM   1097  CA  LYS A  79      -5.684  33.903 -62.745  1.00137.50           C  
ANISOU 1097  CA  LYS A  79    21287  17680  13275   -108   2000   -428       C  
ATOM   1098  C   LYS A  79      -6.482  35.195 -62.814  1.00139.95           C  
ANISOU 1098  C   LYS A  79    21619  17919  13639   -314   1828   -354       C  
ATOM   1099  O   LYS A  79      -7.270  35.373 -63.750  1.00140.61           O  
ANISOU 1099  O   LYS A  79    21866  17922  13638   -407   1764   -361       O  
ATOM   1100  CB  LYS A  79      -4.570  33.882 -63.800  1.00141.76           C  
ANISOU 1100  CB  LYS A  79    21801  18418  13645    -93   2167   -406       C  
ATOM   1101  N   MET A  80      -6.329  36.056 -61.787  1.00133.92           N  
ANISOU 1101  N   MET A  80    20698  17173  13012   -374   1750   -288       N  
ATOM   1102  CA  MET A  80      -7.049  37.327 -61.632  1.00132.31           C  
ANISOU 1102  CA  MET A  80    20507  16885  12879   -546   1586   -216       C  
ATOM   1103  C   MET A  80      -6.660  38.379 -62.701  1.00135.56           C  
ANISOU 1103  C   MET A  80    20947  17387  13171   -711   1598   -126       C  
ATOM   1104  O   MET A  80      -5.964  39.361 -62.423  1.00135.41           O  
ANISOU 1104  O   MET A  80    20807  17464  13177   -817   1601    -41       O  
ATOM   1105  CB  MET A  80      -6.954  37.888 -60.184  1.00133.47           C  
ANISOU 1105  CB  MET A  80    20495  17019  13200   -556   1510   -181       C  
ATOM   1106  CG  MET A  80      -5.598  37.699 -59.501  1.00137.60           C  
ANISOU 1106  CG  MET A  80    20812  17725  13744   -480   1634   -164       C  
ATOM   1107  SD  MET A  80      -5.689  37.884 -57.702  1.00139.86           S  
ANISOU 1107  SD  MET A  80    20943  17967  14229   -440   1546   -163       S  
ATOM   1108  CE  MET A  80      -4.142  37.156 -57.235  1.00137.66           C  
ANISOU 1108  CE  MET A  80    20459  17924  13923   -291   1720   -166       C  
ATOM   1109  N   LYS A  81      -7.154  38.155 -63.929  1.00131.49           N  
ANISOU 1109  N   LYS A  81    20605  16836  12519   -743   1601   -146       N  
ATOM   1110  CA  LYS A  81      -6.951  39.010 -65.096  1.00131.89           C  
ANISOU 1110  CA  LYS A  81    20726  16954  12433   -891   1610    -66       C  
ATOM   1111  C   LYS A  81      -8.263  39.740 -65.429  1.00134.01           C  
ANISOU 1111  C   LYS A  81    21143  17060  12715  -1001   1429    -31       C  
ATOM   1112  O   LYS A  81      -8.324  40.487 -66.412  1.00135.74           O  
ANISOU 1112  O   LYS A  81    21453  17301  12821  -1124   1407     41       O  
ATOM   1113  CB  LYS A  81      -6.443  38.179 -66.289  1.00135.68           C  
ANISOU 1113  CB  LYS A  81    21289  17539  12725   -833   1762   -114       C  
ATOM   1114  N   THR A  82      -9.307  39.523 -64.594  1.00126.36           N  
ANISOU 1114  N   THR A  82    20193  15938  11880   -949   1301    -76       N  
ATOM   1115  CA  THR A  82     -10.629  40.147 -64.715  1.00124.42           C  
ANISOU 1115  CA  THR A  82    20060  15547  11668  -1020   1121    -48       C  
ATOM   1116  C   THR A  82     -10.951  40.888 -63.418  1.00125.11           C  
ANISOU 1116  C   THR A  82    20046  15551  11938  -1032   1010    -12       C  
ATOM   1117  O   THR A  82     -10.391  40.540 -62.374  1.00124.32           O  
ANISOU 1117  O   THR A  82    19810  15482  11944   -958   1063    -44       O  
ATOM   1118  CB  THR A  82     -11.733  39.104 -65.045  1.00130.55           C  
ANISOU 1118  CB  THR A  82    20965  16228  12408   -951   1069   -146       C  
ATOM   1119  OG1 THR A  82     -11.902  38.183 -63.966  1.00128.58           O  
ANISOU 1119  OG1 THR A  82    20650  15924  12281   -830   1080   -233       O  
ATOM   1120  CG2 THR A  82     -11.483  38.359 -66.340  1.00130.31           C  
ANISOU 1120  CG2 THR A  82    21059  16267  12187   -944   1175   -192       C  
ATOM   1121  N   ALA A  83     -11.874  41.885 -63.479  1.00119.33           N  
ANISOU 1121  N   ALA A  83    19389  14714  11239  -1112    856     52       N  
ATOM   1122  CA  ALA A  83     -12.335  42.682 -62.332  1.00116.78           C  
ANISOU 1122  CA  ALA A  83    19001  14293  11077  -1122    739     85       C  
ATOM   1123  C   ALA A  83     -13.034  41.823 -61.262  1.00118.42           C  
ANISOU 1123  C   ALA A  83    19152  14426  11415  -1001    693     -8       C  
ATOM   1124  O   ALA A  83     -12.752  41.999 -60.078  1.00117.75           O  
ANISOU 1124  O   ALA A  83    18948  14328  11462   -971    688    -13       O  
ATOM   1125  CB  ALA A  83     -13.254  43.804 -62.797  1.00117.54           C  
ANISOU 1125  CB  ALA A  83    19215  14290  11154  -1203    592    168       C  
ATOM   1126  N   THR A  84     -13.909  40.880 -61.678  1.00113.54           N  
ANISOU 1126  N   THR A  84    18623  13766  10752   -944    663    -83       N  
ATOM   1127  CA  THR A  84     -14.647  39.951 -60.805  1.00111.68           C  
ANISOU 1127  CA  THR A  84    18358  13459  10615   -846    624   -175       C  
ATOM   1128  C   THR A  84     -13.708  39.082 -59.939  1.00113.53           C  
ANISOU 1128  C   THR A  84    18478  13744  10915   -748    752   -234       C  
ATOM   1129  O   THR A  84     -13.930  38.975 -58.729  1.00111.38           O  
ANISOU 1129  O   THR A  84    18116  13423  10779   -693    712   -258       O  
ATOM   1130  CB  THR A  84     -15.635  39.126 -61.656  1.00118.40           C  
ANISOU 1130  CB  THR A  84    19345  14275  11366   -840    583   -239       C  
ATOM   1131  OG1 THR A  84     -16.656  40.010 -62.116  1.00122.69           O  
ANISOU 1131  OG1 THR A  84    19959  14772  11885   -910    434   -177       O  
ATOM   1132  CG2 THR A  84     -16.278  37.971 -60.897  1.00112.35           C  
ANISOU 1132  CG2 THR A  84    18569  13446  10674   -756    570   -341       C  
ATOM   1133  N   ASN A  85     -12.658  38.492 -60.557  1.00110.10           N  
ANISOU 1133  N   ASN A  85    18044  13415  10375   -719    905   -252       N  
ATOM   1134  CA  ASN A  85     -11.680  37.630 -59.879  1.00109.16           C  
ANISOU 1134  CA  ASN A  85    17820  13365  10292   -605   1039   -300       C  
ATOM   1135  C   ASN A  85     -10.931  38.336 -58.746  1.00110.73           C  
ANISOU 1135  C   ASN A  85    17842  13618  10611   -610   1043   -247       C  
ATOM   1136  O   ASN A  85     -10.585  37.698 -57.753  1.00109.68           O  
ANISOU 1136  O   ASN A  85    17611  13498  10563   -505   1089   -287       O  
ATOM   1137  CB  ASN A  85     -10.723  36.991 -60.882  1.00110.15           C  
ANISOU 1137  CB  ASN A  85    17982  13606  10264   -568   1202   -321       C  
ATOM   1138  CG  ASN A  85     -11.312  35.848 -61.696  1.00127.79           C  
ANISOU 1138  CG  ASN A  85    20384  15780  12389   -516   1233   -412       C  
ATOM   1139  OD1 ASN A  85     -12.452  35.431 -61.477  1.00123.04           O  
ANISOU 1139  OD1 ASN A  85    19843  15258  11650   -483   1361   -439       O  
ATOM   1140  ND2 ASN A  85     -10.569  35.304 -62.655  1.00117.02           N  
ANISOU 1140  ND2 ASN A  85    19104  14284  11076   -515   1121   -466       N  
ATOM   1141  N   ILE A  86     -10.742  39.653 -58.871  1.00106.74           N  
ANISOU 1141  N   ILE A  86    17311  13135  10112   -736    988   -155       N  
ATOM   1142  CA  ILE A  86     -10.120  40.494 -57.846  1.00106.04           C  
ANISOU 1142  CA  ILE A  86    17077  13085  10128   -778    973   -102       C  
ATOM   1143  C   ILE A  86     -11.111  40.690 -56.663  1.00109.21           C  
ANISOU 1143  C   ILE A  86    17460  13352  10684   -748    839   -125       C  
ATOM   1144  O   ILE A  86     -10.700  40.607 -55.499  1.00108.57           O  
ANISOU 1144  O   ILE A  86    17250  13295  10705   -700    852   -139       O  
ATOM   1145  CB  ILE A  86      -9.590  41.821 -58.465  1.00109.51           C  
ANISOU 1145  CB  ILE A  86    17527  13579  10503   -940    966      1       C  
ATOM   1146  CG1 ILE A  86      -8.377  41.538 -59.390  1.00110.85           C  
ANISOU 1146  CG1 ILE A  86    17663  13925  10529   -959   1126     21       C  
ATOM   1147  CG2 ILE A  86      -9.226  42.842 -57.385  1.00109.26           C  
ANISOU 1147  CG2 ILE A  86    17386  13544  10583  -1016    914     53       C  
ATOM   1148  CD1 ILE A  86      -8.233  42.433 -60.554  1.00114.56           C  
ANISOU 1148  CD1 ILE A  86    18229  14423  10877  -1105   1124    103       C  
ATOM   1149  N   TYR A  87     -12.414  40.891 -56.970  1.00104.54           N  
ANISOU 1149  N   TYR A  87    16989  12632  10100   -768    714   -132       N  
ATOM   1150  CA  TYR A  87     -13.454  41.045 -55.956  1.00102.47           C  
ANISOU 1150  CA  TYR A  87    16712  12253   9968   -733    590   -156       C  
ATOM   1151  C   TYR A  87     -13.718  39.735 -55.223  1.00105.28           C  
ANISOU 1151  C   TYR A  87    17029  12590  10382   -608    623   -248       C  
ATOM   1152  O   TYR A  87     -13.848  39.765 -54.003  1.00105.07           O  
ANISOU 1152  O   TYR A  87    16913  12531  10477   -566    586   -264       O  
ATOM   1153  CB  TYR A  87     -14.747  41.633 -56.535  1.00103.60           C  
ANISOU 1153  CB  TYR A  87    16979  12294  10090   -780    451   -130       C  
ATOM   1154  CG  TYR A  87     -14.742  43.137 -56.750  1.00105.74           C  
ANISOU 1154  CG  TYR A  87    17286  12530  10359   -883    378    -32       C  
ATOM   1155  CD1 TYR A  87     -14.936  44.014 -55.688  1.00106.82           C  
ANISOU 1155  CD1 TYR A  87    17371  12599  10617   -894    301     -5       C  
ATOM   1156  CD2 TYR A  87     -14.621  43.679 -58.028  1.00108.03           C  
ANISOU 1156  CD2 TYR A  87    17684  12841  10519   -969    381     33       C  
ATOM   1157  CE1 TYR A  87     -14.950  45.397 -55.885  1.00108.37           C  
ANISOU 1157  CE1 TYR A  87    17631  12739  10806   -986    235     83       C  
ATOM   1158  CE2 TYR A  87     -14.641  45.057 -58.238  1.00109.43           C  
ANISOU 1158  CE2 TYR A  87    17921  12968  10689  -1063    314    129       C  
ATOM   1159  CZ  TYR A  87     -14.805  45.913 -57.164  1.00116.13           C  
ANISOU 1159  CZ  TYR A  87    18727  13736  11660  -1071    242    153       C  
ATOM   1160  OH  TYR A  87     -14.829  47.272 -57.377  1.00118.34           O  
ANISOU 1160  OH  TYR A  87    19093  13944  11926  -1162    179    246       O  
ATOM   1161  N   ILE A  88     -13.750  38.581 -55.926  1.00101.80           N  
ANISOU 1161  N   ILE A  88    16664  12164   9851   -552    697   -309       N  
ATOM   1162  CA  ILE A  88     -13.946  37.287 -55.243  1.00100.56           C  
ANISOU 1162  CA  ILE A  88    16496  11973   9740   -436    739   -395       C  
ATOM   1163  C   ILE A  88     -12.761  37.013 -54.288  1.00102.94           C  
ANISOU 1163  C   ILE A  88    16652  12359  10102   -355    842   -393       C  
ATOM   1164  O   ILE A  88     -12.980  36.443 -53.220  1.00102.54           O  
ANISOU 1164  O   ILE A  88    16549  12267  10145   -274    832   -434       O  
ATOM   1165  CB  ILE A  88     -14.261  36.057 -56.163  1.00104.47           C  
ANISOU 1165  CB  ILE A  88    17131  12443  10119   -396    800   -469       C  
ATOM   1166  CG1 ILE A  88     -15.346  36.350 -57.222  1.00105.19           C  
ANISOU 1166  CG1 ILE A  88    17358  12483  10126   -490    699   -466       C  
ATOM   1167  CG2 ILE A  88     -14.627  34.803 -55.330  1.00104.35           C  
ANISOU 1167  CG2 ILE A  88    17127  12358  10163   -292    824   -553       C  
ATOM   1168  CD1 ILE A  88     -15.397  35.308 -58.413  1.00109.82           C  
ANISOU 1168  CD1 ILE A  88    18098  13073  10556   -482    777   -531       C  
ATOM   1169  N   PHE A  89     -11.525  37.444 -54.655  1.00 98.06           N  
ANISOU 1169  N   PHE A  89    15961  11871   9426   -380    936   -342       N  
ATOM   1170  CA  PHE A  89     -10.347  37.258 -53.800  1.00 96.66           C  
ANISOU 1170  CA  PHE A  89    15624  11810   9293   -309   1029   -331       C  
ATOM   1171  C   PHE A  89     -10.469  38.076 -52.515  1.00 98.32           C  
ANISOU 1171  C   PHE A  89    15720  11997   9639   -348    935   -300       C  
ATOM   1172  O   PHE A  89     -10.088  37.592 -51.454  1.00 97.70           O  
ANISOU 1172  O   PHE A  89    15535  11953   9633   -257    966   -321       O  
ATOM   1173  CB  PHE A  89      -9.036  37.590 -54.540  1.00 99.33           C  
ANISOU 1173  CB  PHE A  89    15897  12318   9527   -346   1146   -279       C  
ATOM   1174  CG  PHE A  89      -7.791  37.284 -53.734  1.00100.63           C  
ANISOU 1174  CG  PHE A  89    15880  12635   9718   -260   1249   -268       C  
ATOM   1175  CD1 PHE A  89      -7.212  36.018 -53.767  1.00104.06           C  
ANISOU 1175  CD1 PHE A  89    16301  13133  10106    -92   1378   -318       C  
ATOM   1176  CD2 PHE A  89      -7.209  38.254 -52.923  1.00101.84           C  
ANISOU 1176  CD2 PHE A  89    15884  12870   9940   -344   1215   -209       C  
ATOM   1177  CE1 PHE A  89      -6.082  35.724 -52.996  1.00104.89           C  
ANISOU 1177  CE1 PHE A  89    16228  13395  10232      6   1467   -301       C  
ATOM   1178  CE2 PHE A  89      -6.077  37.960 -52.157  1.00105.01           C  
ANISOU 1178  CE2 PHE A  89    16104  13435  10359   -267   1300   -197       C  
ATOM   1179  CZ  PHE A  89      -5.516  36.698 -52.207  1.00103.66           C  
ANISOU 1179  CZ  PHE A  89    15905  13341  10141    -86   1425   -239       C  
ATOM   1180  N   SER A  90     -11.009  39.299 -52.611  1.00 93.80           N  
ANISOU 1180  N   SER A  90    15180  11364   9095   -475    823   -250       N  
ATOM   1181  CA  SER A  90     -11.181  40.184 -51.465  1.00 92.65           C  
ANISOU 1181  CA  SER A  90    14954  11181   9069   -520    732   -224       C  
ATOM   1182  C   SER A  90     -12.219  39.646 -50.479  1.00 96.52           C  
ANISOU 1182  C   SER A  90    15450  11559   9664   -436    655   -283       C  
ATOM   1183  O   SER A  90     -11.967  39.629 -49.266  1.00 96.19           O  
ANISOU 1183  O   SER A  90    15299  11534   9713   -397    647   -292       O  
ATOM   1184  CB  SER A  90     -11.522  41.596 -51.919  1.00 95.70           C  
ANISOU 1184  CB  SER A  90    15408  11510   9444   -663    640   -157       C  
ATOM   1185  OG  SER A  90     -11.387  42.530 -50.858  1.00104.46           O  
ANISOU 1185  OG  SER A  90    16440  12600  10649   -718    578   -129       O  
ATOM   1186  N   LEU A  91     -13.367  39.178 -50.994  1.00 92.67           N  
ANISOU 1186  N   LEU A  91    15084  10969   9155   -415    599   -322       N  
ATOM   1187  CA  LEU A  91     -14.414  38.587 -50.172  1.00 91.50           C  
ANISOU 1187  CA  LEU A  91    14947  10727   9091   -348    532   -378       C  
ATOM   1188  C   LEU A  91     -13.859  37.314 -49.528  1.00 96.44           C  
ANISOU 1188  C   LEU A  91    15517  11391   9733   -228    632   -430       C  
ATOM   1189  O   LEU A  91     -14.092  37.091 -48.338  1.00 96.66           O  
ANISOU 1189  O   LEU A  91    15477  11392   9856   -175    603   -451       O  
ATOM   1190  CB  LEU A  91     -15.629  38.223 -51.033  1.00 91.68           C  
ANISOU 1190  CB  LEU A  91    15107  10667   9059   -365    469   -410       C  
ATOM   1191  CG  LEU A  91     -16.846  39.125 -51.024  1.00 95.96           C  
ANISOU 1191  CG  LEU A  91    15690  11129   9641   -423    323   -386       C  
ATOM   1192  CD1 LEU A  91     -17.952  38.499 -51.844  1.00 95.85           C  
ANISOU 1192  CD1 LEU A  91    15789  11070   9558   -431    274   -425       C  
ATOM   1193  CD2 LEU A  91     -17.359  39.367 -49.616  1.00 98.00           C  
ANISOU 1193  CD2 LEU A  91    15863  11342  10031   -385    253   -401       C  
ATOM   1194  N   ALA A  92     -13.109  36.491 -50.313  1.00 93.55           N  
ANISOU 1194  N   ALA A  92    15188  11090   9268   -176    754   -446       N  
ATOM   1195  CA  ALA A  92     -12.507  35.232 -49.856  1.00 93.26           C  
ANISOU 1195  CA  ALA A  92    15124  11086   9227    -39    864   -490       C  
ATOM   1196  C   ALA A  92     -11.457  35.450 -48.754  1.00 96.54           C  
ANISOU 1196  C   ALA A  92    15364  11609   9707     12    907   -456       C  
ATOM   1197  O   ALA A  92     -11.516  34.765 -47.729  1.00 95.75           O  
ANISOU 1197  O   ALA A  92    15221  11486   9673    109    915   -485       O  
ATOM   1198  CB  ALA A  92     -11.910  34.473 -51.020  1.00 95.01           C  
ANISOU 1198  CB  ALA A  92    15429  11354   9317      7    986   -510       C  
ATOM   1199  N   LEU A  93     -10.536  36.427 -48.942  1.00 92.14           N  
ANISOU 1199  N   LEU A  93    14708  11172   9129    -64    926   -394       N  
ATOM   1200  CA  LEU A  93      -9.505  36.760 -47.959  1.00 91.33           C  
ANISOU 1200  CA  LEU A  93    14429  11199   9075    -46    958   -357       C  
ATOM   1201  C   LEU A  93     -10.135  37.194 -46.634  1.00 93.09           C  
ANISOU 1201  C   LEU A  93    14599  11349   9422    -64    849   -364       C  
ATOM   1202  O   LEU A  93      -9.676  36.757 -45.575  1.00 92.15           O  
ANISOU 1202  O   LEU A  93    14373  11287   9353     23    875   -370       O  
ATOM   1203  CB  LEU A  93      -8.537  37.837 -48.511  1.00 92.10           C  
ANISOU 1203  CB  LEU A  93    14448  11431   9114   -169    987   -289       C  
ATOM   1204  CG  LEU A  93      -7.385  38.319 -47.603  1.00 96.11           C  
ANISOU 1204  CG  LEU A  93    14760  12104   9653   -190   1016   -245       C  
ATOM   1205  CD1 LEU A  93      -6.461  37.180 -47.198  1.00 96.04           C  
ANISOU 1205  CD1 LEU A  93    14641  12231   9619    -18   1135   -260       C  
ATOM   1206  CD2 LEU A  93      -6.595  39.426 -48.274  1.00 99.08           C  
ANISOU 1206  CD2 LEU A  93    15089  12595   9961   -349   1036   -179       C  
ATOM   1207  N   ALA A  94     -11.215  38.017 -46.710  1.00 88.67           N  
ANISOU 1207  N   ALA A  94    14119  10665   8905   -163    728   -362       N  
ATOM   1208  CA  ALA A  94     -11.966  38.549 -45.567  1.00 86.68           C  
ANISOU 1208  CA  ALA A  94    13837  10333   8763   -185    619   -371       C  
ATOM   1209  C   ALA A  94     -12.717  37.456 -44.817  1.00 90.54           C  
ANISOU 1209  C   ALA A  94    14349  10745   9306    -72    609   -430       C  
ATOM   1210  O   ALA A  94     -12.581  37.381 -43.595  1.00 89.24           O  
ANISOU 1210  O   ALA A  94    14091  10600   9214    -28    594   -437       O  
ATOM   1211  CB  ALA A  94     -12.921  39.626 -46.021  1.00 86.61           C  
ANISOU 1211  CB  ALA A  94    13922  10220   8768   -293    507   -352       C  
ATOM   1212  N   GLY A  95     -13.458  36.610 -45.560  1.00 87.60           N  
ANISOU 1212  N   GLY A  95    14102  10293   8888    -37    619   -471       N  
ATOM   1213  CA  GLY A  95     -14.243  35.479 -45.054  1.00 86.20           C  
ANISOU 1213  CA  GLY A  95    13979  10031   8740     47    616   -528       C  
ATOM   1214  C   GLY A  95     -13.428  34.490 -44.249  1.00 88.98           C  
ANISOU 1214  C   GLY A  95    14265  10440   9105    176    710   -540       C  
ATOM   1215  O   GLY A  95     -13.870  34.038 -43.189  1.00 87.92           O  
ANISOU 1215  O   GLY A  95    14109  10259   9038    228    684   -563       O  
ATOM   1216  N   ALA A  96     -12.208  34.184 -44.750  1.00 86.19           N  
ANISOU 1216  N   ALA A  96    13873  10195   8679    232    823   -518       N  
ATOM   1217  CA  ALA A  96     -11.205  33.308 -44.148  1.00 86.08           C  
ANISOU 1217  CA  ALA A  96    13783  10267   8656    376    928   -515       C  
ATOM   1218  C   ALA A  96     -10.640  33.960 -42.881  1.00 89.63           C  
ANISOU 1218  C   ALA A  96    14058  10815   9183    372    892   -477       C  
ATOM   1219  O   ALA A  96     -10.610  33.304 -41.842  1.00 89.15           O  
ANISOU 1219  O   ALA A  96    13957  10750   9167    472    903   -487       O  
ATOM   1220  CB  ALA A  96     -10.093  33.024 -45.147  1.00 88.12           C  
ANISOU 1220  CB  ALA A  96    14035  10640   8808    427   1051   -497       C  
ATOM   1221  N   LEU A  97     -10.255  35.257 -42.940  1.00 86.69           N  
ANISOU 1221  N   LEU A  97    13597  10520   8822    247    844   -433       N  
ATOM   1222  CA  LEU A  97      -9.765  35.989 -41.758  1.00 86.96           C  
ANISOU 1222  CA  LEU A  97    13478  10641   8920    212    800   -403       C  
ATOM   1223  C   LEU A  97     -10.802  36.047 -40.621  1.00 89.67           C  
ANISOU 1223  C   LEU A  97    13837  10871   9362    212    702   -434       C  
ATOM   1224  O   LEU A  97     -10.448  35.851 -39.460  1.00 88.91           O  
ANISOU 1224  O   LEU A  97    13639  10833   9308    271    702   -429       O  
ATOM   1225  CB  LEU A  97      -9.283  37.406 -42.116  1.00 87.50           C  
ANISOU 1225  CB  LEU A  97    13489  10782   8975     50    763   -357       C  
ATOM   1226  CG  LEU A  97      -7.860  37.517 -42.668  1.00 93.55           C  
ANISOU 1226  CG  LEU A  97    14147  11742   9657     40    863   -310       C  
ATOM   1227  CD1 LEU A  97      -7.557  38.945 -43.082  1.00 94.15           C  
ANISOU 1227  CD1 LEU A  97    14202  11858   9714   -150    819   -265       C  
ATOM   1228  CD2 LEU A  97      -6.816  37.031 -41.649  1.00 95.75           C  
ANISOU 1228  CD2 LEU A  97    14250  12188   9941    143    921   -293       C  
ATOM   1229  N   ALA A  98     -12.082  36.270 -40.979  1.00 85.27           N  
ANISOU 1229  N   ALA A  98    13403  10165   8830    154    623   -464       N  
ATOM   1230  CA  ALA A  98     -13.236  36.326 -40.087  1.00 83.52           C  
ANISOU 1230  CA  ALA A  98    13208   9835   8690    150    532   -496       C  
ATOM   1231  C   ALA A  98     -13.397  35.028 -39.280  1.00 87.45           C  
ANISOU 1231  C   ALA A  98    13710  10310   9208    277    574   -526       C  
ATOM   1232  O   ALA A  98     -13.388  35.062 -38.046  1.00 85.74           O  
ANISOU 1232  O   ALA A  98    13413  10114   9051    307    546   -526       O  
ATOM   1233  CB  ALA A  98     -14.499  36.589 -40.903  1.00 83.64           C  
ANISOU 1233  CB  ALA A  98    13353   9727   8700     83    460   -518       C  
ATOM   1234  N   THR A  99     -13.487  33.885 -39.991  1.00 84.67           N  
ANISOU 1234  N   THR A  99    13462   9912   8798    350    646   -550       N  
ATOM   1235  CA  THR A  99     -13.705  32.560 -39.412  1.00 83.77           C  
ANISOU 1235  CA  THR A  99    13398   9743   8686    466    695   -579       C  
ATOM   1236  C   THR A  99     -12.507  32.014 -38.659  1.00 87.50           C  
ANISOU 1236  C   THR A  99    13768  10326   9151    595    777   -548       C  
ATOM   1237  O   THR A  99     -12.684  31.076 -37.884  1.00 86.88           O  
ANISOU 1237  O   THR A  99    13718  10203   9089    692    802   -561       O  
ATOM   1238  CB  THR A  99     -14.194  31.584 -40.473  1.00 93.04           C  
ANISOU 1238  CB  THR A  99    14742  10819   9790    486    744   -618       C  
ATOM   1239  OG1 THR A  99     -13.233  31.541 -41.524  1.00 97.09           O  
ANISOU 1239  OG1 THR A  99    15264  11406  10221    513    831   -601       O  
ATOM   1240  CG2 THR A  99     -15.572  31.953 -41.023  1.00 90.13           C  
ANISOU 1240  CG2 THR A  99    14468  10347   9430    365    649   -650       C  
ATOM   1241  N   SER A 100     -11.298  32.601 -38.835  1.00 85.19           N  
ANISOU 1241  N   SER A 100    13352  10187   8829    596    818   -504       N  
ATOM   1242  CA  SER A 100     -10.102  32.131 -38.107  1.00 85.51           C  
ANISOU 1242  CA  SER A 100    13266  10369   8853    725    891   -468       C  
ATOM   1243  C   SER A 100     -10.161  32.457 -36.593  1.00 89.35           C  
ANISOU 1243  C   SER A 100    13640  10894   9416    724    824   -455       C  
ATOM   1244  O   SER A 100      -9.450  31.842 -35.808  1.00 89.09           O  
ANISOU 1244  O   SER A 100    13526  10950   9374    849    872   -429       O  
ATOM   1245  CB  SER A 100      -8.818  32.638 -38.760  1.00 88.34           C  
ANISOU 1245  CB  SER A 100    13511  10905   9148    714    955   -424       C  
ATOM   1246  OG  SER A 100      -8.672  34.043 -38.646  1.00 94.82           O  
ANISOU 1246  OG  SER A 100    14235  11794   9998    552    879   -400       O  
ATOM   1247  N   THR A 101     -11.053  33.390 -36.200  1.00 85.47           N  
ANISOU 1247  N   THR A 101    13153  10331   8990    593    714   -473       N  
ATOM   1248  CA  THR A 101     -11.312  33.827 -34.827  1.00 84.98           C  
ANISOU 1248  CA  THR A 101    13007  10283   8996    569    639   -473       C  
ATOM   1249  C   THR A 101     -12.083  32.754 -34.039  1.00 89.99           C  
ANISOU 1249  C   THR A 101    13715  10818   9661    664    641   -498       C  
ATOM   1250  O   THR A 101     -11.821  32.559 -32.845  1.00 90.76           O  
ANISOU 1250  O   THR A 101    13730  10971   9782    723    633   -483       O  
ATOM   1251  CB  THR A 101     -12.210  35.076 -34.859  1.00 92.64           C  
ANISOU 1251  CB  THR A 101    14002  11177  10018    416    531   -494       C  
ATOM   1252  OG1 THR A 101     -11.623  36.105 -35.646  1.00 97.79           O  
ANISOU 1252  OG1 THR A 101    14620  11894  10641    311    525   -469       O  
ATOM   1253  CG2 THR A 101     -12.526  35.597 -33.490  1.00 91.55           C  
ANISOU 1253  CG2 THR A 101    13793  11047   9945    389    456   -503       C  
ATOM   1254  N   LEU A 102     -13.073  32.108 -34.707  1.00 84.37           N  
ANISOU 1254  N   LEU A 102    13159   9958   8939    661    645   -536       N  
ATOM   1255  CA  LEU A 102     -14.033  31.155 -34.147  1.00 82.94           C  
ANISOU 1255  CA  LEU A 102    13076   9657   8779    705    640   -566       C  
ATOM   1256  C   LEU A 102     -13.427  30.079 -33.214  1.00 89.05           C  
ANISOU 1256  C   LEU A 102    13830  10464   9539    857    708   -541       C  
ATOM   1257  O   LEU A 102     -14.001  29.910 -32.133  1.00 88.32           O  
ANISOU 1257  O   LEU A 102    13729  10339   9491    861    666   -546       O  
ATOM   1258  CB  LEU A 102     -14.889  30.527 -35.251  1.00 82.36           C  
ANISOU 1258  CB  LEU A 102    13174   9451   8668    674    657   -606       C  
ATOM   1259  CG  LEU A 102     -15.689  31.524 -36.082  1.00 85.32           C  
ANISOU 1259  CG  LEU A 102    13576   9788   9055    533    576   -627       C  
ATOM   1260  CD1 LEU A 102     -16.364  30.852 -37.211  1.00 85.69           C  
ANISOU 1260  CD1 LEU A 102    13778   9733   9047    505    598   -663       C  
ATOM   1261  CD2 LEU A 102     -16.691  32.290 -35.245  1.00 86.16           C  
ANISOU 1261  CD2 LEU A 102    13634   9867   9235    454    470   -641       C  
ATOM   1262  N   PRO A 103     -12.278  29.400 -33.518  1.00 87.29           N  
ANISOU 1262  N   PRO A 103    13593  10318   9256    990    808   -509       N  
ATOM   1263  CA  PRO A 103     -11.720  28.439 -32.543  1.00 87.54           C  
ANISOU 1263  CA  PRO A 103    13603  10385   9274   1151    864   -475       C  
ATOM   1264  C   PRO A 103     -11.401  29.044 -31.163  1.00 91.25           C  
ANISOU 1264  C   PRO A 103    13908  10974   9789   1145    803   -443       C  
ATOM   1265  O   PRO A 103     -11.589  28.372 -30.155  1.00 90.52           O  
ANISOU 1265  O   PRO A 103    13833  10854   9708   1224    806   -430       O  
ATOM   1266  CB  PRO A 103     -10.454  27.931 -33.246  1.00 90.38           C  
ANISOU 1266  CB  PRO A 103    13940  10843   9557   1289    974   -442       C  
ATOM   1267  CG  PRO A 103     -10.715  28.129 -34.694  1.00 94.33           C  
ANISOU 1267  CG  PRO A 103    14539  11280  10022   1210    994   -478       C  
ATOM   1268  CD  PRO A 103     -11.447  29.431 -34.745  1.00 89.19           C  
ANISOU 1268  CD  PRO A 103    13838  10620   9431   1016    881   -498       C  
ATOM   1269  N   PHE A 104     -10.963  30.319 -31.118  1.00 87.97           N  
ANISOU 1269  N   PHE A 104    13347  10682   9395   1040    747   -433       N  
ATOM   1270  CA  PHE A 104     -10.616  31.045 -29.884  1.00 87.54           C  
ANISOU 1270  CA  PHE A 104    13138  10749   9374   1007    683   -411       C  
ATOM   1271  C   PHE A 104     -11.856  31.479 -29.128  1.00 91.13           C  
ANISOU 1271  C   PHE A 104    13633  11096   9894    908    592   -451       C  
ATOM   1272  O   PHE A 104     -11.893  31.379 -27.899  1.00 92.35           O  
ANISOU 1272  O   PHE A 104    13732  11290  10069    940    563   -440       O  
ATOM   1273  CB  PHE A 104      -9.734  32.267 -30.199  1.00 89.65           C  
ANISOU 1273  CB  PHE A 104    13261  11172   9629    906    659   -392       C  
ATOM   1274  CG  PHE A 104      -8.472  31.916 -30.958  1.00 92.40           C  
ANISOU 1274  CG  PHE A 104    13543  11660   9905    995    753   -350       C  
ATOM   1275  CD1 PHE A 104      -8.493  31.755 -32.341  1.00 93.90           C  
ANISOU 1275  CD1 PHE A 104    13826  11793  10058    987    808   -363       C  
ATOM   1276  CD2 PHE A 104      -7.266  31.728 -30.287  1.00 95.41           C  
ANISOU 1276  CD2 PHE A 104    13762  12244  10247   1094    788   -296       C  
ATOM   1277  CE1 PHE A 104      -7.340  31.402 -33.032  1.00 95.85           C  
ANISOU 1277  CE1 PHE A 104    14010  12178  10232   1080    904   -326       C  
ATOM   1278  CE2 PHE A 104      -6.110  31.383 -30.985  1.00 98.90           C  
ANISOU 1278  CE2 PHE A 104    14127  12835  10616   1191    880   -255       C  
ATOM   1279  CZ  PHE A 104      -6.156  31.218 -32.352  1.00 96.60           C  
ANISOU 1279  CZ  PHE A 104    13934  12479  10290   1186    941   -272       C  
ATOM   1280  N   GLN A 105     -12.867  31.968 -29.861  1.00 85.95           N  
ANISOU 1280  N   GLN A 105    13072  10319   9268    795    546   -495       N  
ATOM   1281  CA  GLN A 105     -14.154  32.421 -29.339  1.00 84.20           C  
ANISOU 1281  CA  GLN A 105    12890   9997   9103    705    463   -536       C  
ATOM   1282  C   GLN A 105     -14.922  31.304 -28.665  1.00 89.88           C  
ANISOU 1282  C   GLN A 105    13693  10627   9829    772    480   -547       C  
ATOM   1283  O   GLN A 105     -15.492  31.553 -27.602  1.00 89.72           O  
ANISOU 1283  O   GLN A 105    13637  10605   9847    746    427   -559       O  
ATOM   1284  CB  GLN A 105     -15.010  32.972 -30.464  1.00 84.39           C  
ANISOU 1284  CB  GLN A 105    13002   9922   9139    600    424   -571       C  
ATOM   1285  CG  GLN A 105     -14.828  34.434 -30.741  1.00 84.03           C  
ANISOU 1285  CG  GLN A 105    12894   9921   9112    488    362   -572       C  
ATOM   1286  CD  GLN A 105     -15.918  34.893 -31.670  1.00 90.62           C  
ANISOU 1286  CD  GLN A 105    13826  10644   9960    404    313   -603       C  
ATOM   1287  OE1 GLN A 105     -17.101  34.754 -31.372  1.00 76.02           O  
ANISOU 1287  OE1 GLN A 105    12003   8797   8084    350    316   -593       O  
ATOM   1288  NE2 GLN A 105     -15.541  35.473 -32.819  1.00 83.52           N  
ANISOU 1288  NE2 GLN A 105    12981   9658   9096    391    267   -637       N  
ATOM   1289  N   SER A 106     -14.961  30.088 -29.289  1.00 87.91           N  
ANISOU 1289  N   SER A 106    13567  10296   9537    851    556   -545       N  
ATOM   1290  CA  SER A 106     -15.663  28.913 -28.745  1.00 88.70           C  
ANISOU 1290  CA  SER A 106    13778  10292   9631    904    584   -551       C  
ATOM   1291  C   SER A 106     -14.908  28.233 -27.577  1.00 95.86           C  
ANISOU 1291  C   SER A 106    14634  11267  10521   1038    625   -502       C  
ATOM   1292  O   SER A 106     -15.559  27.660 -26.699  1.00 96.69           O  
ANISOU 1292  O   SER A 106    14789  11312  10636   1050    617   -502       O  
ATOM   1293  CB  SER A 106     -16.027  27.909 -29.834  1.00 90.77           C  
ANISOU 1293  CB  SER A 106    14216  10426   9848    921    647   -573       C  
ATOM   1294  OG  SER A 106     -14.885  27.202 -30.270  1.00 97.83           O  
ANISOU 1294  OG  SER A 106    15134  11353  10683   1057    743   -540       O  
ATOM   1295  N   ALA A 107     -13.550  28.318 -27.555  1.00 92.52           N  
ANISOU 1295  N   ALA A 107    14106  10983  10066   1135    667   -456       N  
ATOM   1296  CA  ALA A 107     -12.715  27.805 -26.465  1.00 92.19           C  
ANISOU 1296  CA  ALA A 107    13987  11042  10000   1271    697   -400       C  
ATOM   1297  C   ALA A 107     -12.952  28.682 -25.234  1.00 95.98           C  
ANISOU 1297  C   ALA A 107    14342  11604  10523   1193    608   -403       C  
ATOM   1298  O   ALA A 107     -13.012  28.165 -24.121  1.00 96.62           O  
ANISOU 1298  O   ALA A 107    14416  11698  10598   1259    607   -377       O  
ATOM   1299  CB  ALA A 107     -11.252  27.848 -26.855  1.00 93.66           C  
ANISOU 1299  CB  ALA A 107    14063  11387  10136   1376    753   -353       C  
ATOM   1300  N   ASP A 108     -13.131  30.002 -25.448  1.00 91.87           N  
ANISOU 1300  N   ASP A 108    13741  11125  10040   1052    536   -437       N  
ATOM   1301  CA  ASP A 108     -13.427  31.001 -24.416  1.00 91.26           C  
ANISOU 1301  CA  ASP A 108    13566  11108  10003    960    450   -455       C  
ATOM   1302  C   ASP A 108     -14.786  30.698 -23.754  1.00 92.93           C  
ANISOU 1302  C   ASP A 108    13864  11198  10248    924    416   -489       C  
ATOM   1303  O   ASP A 108     -14.876  30.717 -22.518  1.00 91.88           O  
ANISOU 1303  O   ASP A 108    13678  11114  10118    938    388   -480       O  
ATOM   1304  CB  ASP A 108     -13.407  32.419 -25.031  1.00 93.02           C  
ANISOU 1304  CB  ASP A 108    13733  11358  10252    819    391   -487       C  
ATOM   1305  CG  ASP A 108     -13.731  33.544 -24.060  1.00100.85           C  
ANISOU 1305  CG  ASP A 108    14650  12390  11280    720    305   -516       C  
ATOM   1306  OD1 ASP A 108     -14.929  33.730 -23.744  1.00 98.58           O1-
ANISOU 1306  OD1 ASP A 108    14424  12000  11032    670    261   -558       O1-
ATOM   1307  OD2 ASP A 108     -12.790  34.251 -23.637  1.00109.40           O1-
ANISOU 1307  OD2 ASP A 108    15612  13611  12344    688    283   -498       O1-
ATOM   1308  N   TYR A 109     -15.827  30.418 -24.586  1.00 88.39           N  
ANISOU 1308  N   TYR A 109    13416  10479   9689    872    420   -526       N  
ATOM   1309  CA  TYR A 109     -17.176  30.067 -24.142  1.00 88.12           C  
ANISOU 1309  CA  TYR A 109    13462  10340   9679    823    395   -559       C  
ATOM   1310  C   TYR A 109     -17.143  28.767 -23.304  1.00 93.34           C  
ANISOU 1310  C   TYR A 109    14185  10973  10307    924    449   -522       C  
ATOM   1311  O   TYR A 109     -17.741  28.713 -22.228  1.00 93.65           O  
ANISOU 1311  O   TYR A 109    14210  11016  10358    906    421   -526       O  
ATOM   1312  CB  TYR A 109     -18.151  29.935 -25.341  1.00 89.89           C  
ANISOU 1312  CB  TYR A 109    13802  10443   9911    746    392   -599       C  
ATOM   1313  CG  TYR A 109     -19.475  29.299 -24.967  1.00 93.44           C  
ANISOU 1313  CG  TYR A 109    14337  10799  10368    700    382   -625       C  
ATOM   1314  CD1 TYR A 109     -20.421  29.999 -24.222  1.00 95.16           C  
ANISOU 1314  CD1 TYR A 109    14496  11036  10625    626    313   -656       C  
ATOM   1315  CD2 TYR A 109     -19.752  27.969 -25.290  1.00 95.59           C  
ANISOU 1315  CD2 TYR A 109    14753  10968  10600    729    446   -618       C  
ATOM   1316  CE1 TYR A 109     -21.612  29.398 -23.810  1.00 97.07           C  
ANISOU 1316  CE1 TYR A 109    14798  11219  10866    579    309   -675       C  
ATOM   1317  CE2 TYR A 109     -20.936  27.352 -24.873  1.00 97.08           C  
ANISOU 1317  CE2 TYR A 109    15018  11083  10786    666    440   -637       C  
ATOM   1318  CZ  TYR A 109     -21.861  28.071 -24.126  1.00106.41           C  
ANISOU 1318  CZ  TYR A 109    16116  12308  12007    589    371   -664       C  
ATOM   1319  OH  TYR A 109     -23.039  27.491 -23.709  1.00108.65           O  
ANISOU 1319  OH  TYR A 109    16456  12543  12283    518    367   -681       O  
ATOM   1320  N   LEU A 110     -16.451  27.728 -23.792  1.00 89.78           N  
ANISOU 1320  N   LEU A 110    13812  10492   9808   1035    531   -485       N  
ATOM   1321  CA  LEU A 110     -16.375  26.475 -23.055  1.00 89.91           C  
ANISOU 1321  CA  LEU A 110    13913  10462   9786   1142    588   -442       C  
ATOM   1322  C   LEU A 110     -15.670  26.640 -21.695  1.00 96.28           C  
ANISOU 1322  C   LEU A 110    14593  11406  10582   1219    570   -394       C  
ATOM   1323  O   LEU A 110     -16.262  26.312 -20.660  1.00 96.86           O  
ANISOU 1323  O   LEU A 110    14689  11457  10655   1211    555   -386       O  
ATOM   1324  CB  LEU A 110     -15.741  25.359 -23.893  1.00 89.96           C  
ANISOU 1324  CB  LEU A 110    14046  10397   9738   1264    685   -414       C  
ATOM   1325  CG  LEU A 110     -16.526  24.913 -25.113  1.00 93.32           C  
ANISOU 1325  CG  LEU A 110    14635  10667  10155   1190    711   -462       C  
ATOM   1326  CD1 LEU A 110     -15.663  24.088 -26.032  1.00 94.26           C  
ANISOU 1326  CD1 LEU A 110    14853  10744  10215   1319    807   -441       C  
ATOM   1327  CD2 LEU A 110     -17.792  24.163 -24.729  1.00 93.76           C  
ANISOU 1327  CD2 LEU A 110    14832  10584  10209   1113    709   -484       C  
ATOM   1328  N   MET A 111     -14.459  27.227 -21.697  1.00 91.85           N  
ANISOU 1328  N   MET A 111    13891  10999  10009   1273    564   -365       N  
ATOM   1329  CA  MET A 111     -13.641  27.416 -20.502  1.00 91.25           C  
ANISOU 1329  CA  MET A 111    13680  11082   9909   1344    544   -317       C  
ATOM   1330  C   MET A 111     -14.132  28.468 -19.515  1.00 95.08           C  
ANISOU 1330  C   MET A 111    14064  11633  10429   1226    455   -352       C  
ATOM   1331  O   MET A 111     -13.690  28.453 -18.358  1.00 95.04           O  
ANISOU 1331  O   MET A 111    13976  11739  10396   1275    435   -316       O  
ATOM   1332  CB  MET A 111     -12.205  27.714 -20.892  1.00 93.89           C  
ANISOU 1332  CB  MET A 111    13885  11579  10209   1423    566   -276       C  
ATOM   1333  CG  MET A 111     -11.549  26.571 -21.551  1.00 98.22           C  
ANISOU 1333  CG  MET A 111    14518  12094  10707   1588    663   -230       C  
ATOM   1334  SD  MET A 111      -9.845  26.975 -21.852  1.00103.62           S  
ANISOU 1334  SD  MET A 111    15009  13019  11343   1681    688   -177       S  
ATOM   1335  CE  MET A 111      -9.770  26.612 -23.569  1.00100.52           C  
ANISOU 1335  CE  MET A 111    14732  12520  10939   1703    767   -202       C  
ATOM   1336  N   GLU A 112     -15.030  29.382 -19.958  1.00 90.95           N  
ANISOU 1336  N   GLU A 112    13551  11046   9959   1080    401   -420       N  
ATOM   1337  CA  GLU A 112     -15.568  30.500 -19.155  1.00 89.48           C  
ANISOU 1337  CA  GLU A 112    13287  10905   9807    970    320   -465       C  
ATOM   1338  C   GLU A 112     -14.408  31.423 -18.714  1.00 91.50           C  
ANISOU 1338  C   GLU A 112    13387  11335  10043    959    282   -451       C  
ATOM   1339  O   GLU A 112     -14.461  32.011 -17.631  1.00 90.39           O  
ANISOU 1339  O   GLU A 112    13175  11270   9900    917    230   -466       O  
ATOM   1340  CB  GLU A 112     -16.401  30.000 -17.944  1.00 90.94           C  
ANISOU 1340  CB  GLU A 112    13508  11060   9985    979    312   -465       C  
ATOM   1341  CG  GLU A 112     -17.697  29.280 -18.286  1.00104.90           C  
ANISOU 1341  CG  GLU A 112    15415  12672  11771    942    335   -489       C  
ATOM   1342  CD  GLU A 112     -17.958  28.003 -17.502  1.00135.58           C  
ANISOU 1342  CD  GLU A 112    19388  16511  15616   1015    384   -443       C  
ATOM   1343  OE1 GLU A 112     -18.173  28.091 -16.271  1.00131.28           O  
ANISOU 1343  OE1 GLU A 112    18797  16026  15057   1013    359   -435       O  
ATOM   1344  OE2 GLU A 112     -17.965  26.915 -18.125  1.00133.01           O  
ANISOU 1344  OE2 GLU A 112    19189  16082  15267   1070    449   -417       O  
ATOM   1345  N   THR A 113     -13.352  31.530 -19.577  1.00 88.25           N  
ANISOU 1345  N   THR A 113    12925  10994   9611    988    312   -423       N  
ATOM   1346  CA  THR A 113     -12.108  32.307 -19.383  1.00 88.21           C  
ANISOU 1346  CA  THR A 113    12767  11174   9577    966    287   -401       C  
ATOM   1347  C   THR A 113     -11.310  32.471 -20.704  1.00 88.78           C  
ANISOU 1347  C   THR A 113    12815  11281   9636    964    326   -385       C  
ATOM   1348  O   THR A 113     -11.451  31.641 -21.614  1.00 87.96           O  
ANISOU 1348  O   THR A 113    12809  11084   9529   1038    391   -373       O  
ATOM   1349  CB  THR A 113     -11.232  31.675 -18.241  1.00100.66           C  
ANISOU 1349  CB  THR A 113    14248  12906  11092   1085    299   -336       C  
ATOM   1350  OG1 THR A 113     -10.175  32.561 -17.864  1.00105.27           O  
ANISOU 1350  OG1 THR A 113    14669  13686  11642   1028    257   -324       O  
ATOM   1351  CG2 THR A 113     -10.657  30.300 -18.604  1.00 98.56           C  
ANISOU 1351  CG2 THR A 113    14025  12641  10783   1269    388   -266       C  
ATOM   1352  N   TRP A 114     -10.464  33.532 -20.789  1.00 82.74           N  
ANISOU 1352  N   TRP A 114    11926  10654   8856    872    291   -386       N  
ATOM   1353  CA  TRP A 114      -9.590  33.762 -21.941  1.00 81.94           C  
ANISOU 1353  CA  TRP A 114    11779  10622   8731    858    330   -364       C  
ATOM   1354  C   TRP A 114      -8.185  33.183 -21.632  1.00 89.70           C  
ANISOU 1354  C   TRP A 114    12620  11820   9643    982    376   -290       C  
ATOM   1355  O   TRP A 114      -7.410  33.790 -20.881  1.00 91.25           O  
ANISOU 1355  O   TRP A 114    12668  12197   9805    930    333   -274       O  
ATOM   1356  CB  TRP A 114      -9.543  35.239 -22.384  1.00 78.84           C  
ANISOU 1356  CB  TRP A 114    11356  10240   8360    670    271   -405       C  
ATOM   1357  CG  TRP A 114      -8.663  35.444 -23.581  1.00 79.40           C  
ANISOU 1357  CG  TRP A 114    11383  10386   8399    647    317   -378       C  
ATOM   1358  CD1 TRP A 114      -7.334  35.750 -23.570  1.00 83.25           C  
ANISOU 1358  CD1 TRP A 114    11714  11089   8829    628    331   -335       C  
ATOM   1359  CD2 TRP A 114      -9.014  35.225 -24.966  1.00 78.67           C  
ANISOU 1359  CD2 TRP A 114    11400  10173   8320    651    363   -387       C  
ATOM   1360  NE1 TRP A 114      -6.844  35.789 -24.859  1.00 83.21           N  
ANISOU 1360  NE1 TRP A 114    11710  11103   8801    616    386   -316       N  
ATOM   1361  CE2 TRP A 114      -7.847  35.446 -25.734  1.00 83.60           C  
ANISOU 1361  CE2 TRP A 114    11928  10944   8891    636    408   -348       C  
ATOM   1362  CE3 TRP A 114     -10.203  34.871 -25.634  1.00 78.25           C  
ANISOU 1362  CE3 TRP A 114    11510   9914   8308    659    370   -423       C  
ATOM   1363  CZ2 TRP A 114      -7.843  35.358 -27.140  1.00 82.23           C  
ANISOU 1363  CZ2 TRP A 114    11828  10709   8708    629    460   -347       C  
ATOM   1364  CZ3 TRP A 114     -10.188  34.766 -27.018  1.00 79.04           C  
ANISOU 1364  CZ3 TRP A 114    11681   9955   8395    651    415   -423       C  
ATOM   1365  CH2 TRP A 114      -9.022  35.014 -27.756  1.00 80.43           C  
ANISOU 1365  CH2 TRP A 114    11770  10271   8520    638    461   -386       C  
ATOM   1366  N   PRO A 115      -7.844  32.006 -22.203  1.00 86.40           N  
ANISOU 1366  N   PRO A 115    12246  11389   9195   1150    464   -246       N  
ATOM   1367  CA  PRO A 115      -6.559  31.375 -21.876  1.00 87.50           C  
ANISOU 1367  CA  PRO A 115    12250  11736   9261   1304    513   -169       C  
ATOM   1368  C   PRO A 115      -5.405  31.673 -22.825  1.00 93.05           C  
ANISOU 1368  C   PRO A 115    12834  12604   9918   1303    559   -139       C  
ATOM   1369  O   PRO A 115      -4.346  31.078 -22.671  1.00 94.31           O  
ANISOU 1369  O   PRO A 115    12876  12945  10011   1454    609    -72       O  
ATOM   1370  CB  PRO A 115      -6.911  29.894 -21.968  1.00 89.28           C  
ANISOU 1370  CB  PRO A 115    12619  11828   9475   1502    591   -140       C  
ATOM   1371  CG  PRO A 115      -7.862  29.839 -23.107  1.00 92.65           C  
ANISOU 1371  CG  PRO A 115    13220  12036   9948   1436    614   -196       C  
ATOM   1372  CD  PRO A 115      -8.653  31.123 -23.066  1.00 87.15           C  
ANISOU 1372  CD  PRO A 115    12524  11278   9312   1219    524   -263       C  
ATOM   1373  N   PHE A 116      -5.602  32.541 -23.819  1.00 89.92           N  
ANISOU 1373  N   PHE A 116    12467  12150   9548   1148    547   -181       N  
ATOM   1374  CA  PHE A 116      -4.607  32.769 -24.875  1.00 90.31           C  
ANISOU 1374  CA  PHE A 116    12427  12336   9550   1140    603   -153       C  
ATOM   1375  C   PHE A 116      -3.671  33.981 -24.676  1.00 95.47           C  
ANISOU 1375  C   PHE A 116    12890  13215  10170    974    553   -141       C  
ATOM   1376  O   PHE A 116      -2.690  34.117 -25.416  1.00 95.61           O  
ANISOU 1376  O   PHE A 116    12796  13397  10133    973    604   -106       O  
ATOM   1377  CB  PHE A 116      -5.318  32.848 -26.231  1.00 90.69           C  
ANISOU 1377  CB  PHE A 116    12636  12190   9630   1082    635   -197       C  
ATOM   1378  CG  PHE A 116      -6.286  31.717 -26.496  1.00 90.91           C  
ANISOU 1378  CG  PHE A 116    12862  11994   9684   1207    679   -217       C  
ATOM   1379  CD1 PHE A 116      -5.832  30.478 -26.935  1.00 94.34           C  
ANISOU 1379  CD1 PHE A 116    13342  12433  10069   1410    781   -180       C  
ATOM   1380  CD2 PHE A 116      -7.656  31.899 -26.334  1.00 91.11           C  
ANISOU 1380  CD2 PHE A 116    13032  11808   9776   1117    622   -274       C  
ATOM   1381  CE1 PHE A 116      -6.727  29.438 -27.189  1.00 94.50           C  
ANISOU 1381  CE1 PHE A 116    13566  12235  10105   1503    823   -203       C  
ATOM   1382  CE2 PHE A 116      -8.552  30.859 -26.594  1.00 93.26           C  
ANISOU 1382  CE2 PHE A 116    13484  11887  10064   1205    661   -294       C  
ATOM   1383  CZ  PHE A 116      -8.079  29.635 -27.010  1.00 92.50           C  
ANISOU 1383  CZ  PHE A 116    13446  11783   9916   1388    760   -260       C  
ATOM   1384  N   GLY A 117      -3.951  34.808 -23.669  1.00 92.57           N  
ANISOU 1384  N   GLY A 117    12486  12861   9826    836    458   -171       N  
ATOM   1385  CA  GLY A 117      -3.151  35.987 -23.361  1.00 93.37           C  
ANISOU 1385  CA  GLY A 117    12430  13155   9891    652    401   -169       C  
ATOM   1386  C   GLY A 117      -3.600  37.232 -24.094  1.00 97.31           C  
ANISOU 1386  C   GLY A 117    13014  13532  10427    427    360   -222       C  
ATOM   1387  O   GLY A 117      -4.431  37.147 -25.002  1.00 95.64           O  
ANISOU 1387  O   GLY A 117    12962  13112  10262    428    382   -252       O  
ATOM   1388  N   GLU A 118      -3.034  38.399 -23.707  1.00 95.76           N  
ANISOU 1388  N   GLU A 118    12716  13467  10201    228    298   -232       N  
ATOM   1389  CA  GLU A 118      -3.348  39.724 -24.258  1.00 95.62           C  
ANISOU 1389  CA  GLU A 118    12782  13342  10207     -3    251   -277       C  
ATOM   1390  C   GLU A 118      -2.994  39.894 -25.733  1.00100.94           C  
ANISOU 1390  C   GLU A 118    13478  14013  10862    -48    313   -254       C  
ATOM   1391  O   GLU A 118      -3.767  40.526 -26.450  1.00100.39           O  
ANISOU 1391  O   GLU A 118    13564  13742  10836   -146    294   -292       O  
ATOM   1392  CB  GLU A 118      -2.707  40.843 -23.424  1.00 97.94           C  
ANISOU 1392  CB  GLU A 118    12967  13788  10457   -207    176   -290       C  
ATOM   1393  CG  GLU A 118      -3.424  42.174 -23.569  1.00108.53           C  
ANISOU 1393  CG  GLU A 118    14462  14936  11840   -419    108   -356       C  
ATOM   1394  CD  GLU A 118      -2.788  43.333 -22.839  1.00134.70           C  
ANISOU 1394  CD  GLU A 118    17703  18374  15103   -646     38   -376       C  
ATOM   1395  OE1 GLU A 118      -1.663  43.730 -23.218  1.00134.26           O  
ANISOU 1395  OE1 GLU A 118    17515  18522  14975   -772     56   -336       O  
ATOM   1396  OE2 GLU A 118      -3.419  43.853 -21.892  1.00137.78           O1-
ANISOU 1396  OE2 GLU A 118    18172  18659  15518   -706    -32   -435       O1-
ATOM   1397  N   LEU A 119      -1.830  39.369 -26.178  1.00 98.88           N  
ANISOU 1397  N   LEU A 119    13058  13983  10529     25    388   -191       N  
ATOM   1398  CA  LEU A 119      -1.381  39.474 -27.569  1.00 99.26           C  
ANISOU 1398  CA  LEU A 119    13109  14062  10544    -11    459   -165       C  
ATOM   1399  C   LEU A 119      -2.350  38.762 -28.527  1.00100.92           C  
ANISOU 1399  C   LEU A 119    13511  14032  10803    118    509   -186       C  
ATOM   1400  O   LEU A 119      -2.716  39.339 -29.557  1.00100.31           O  
ANISOU 1400  O   LEU A 119    13545  13831  10737      8    513   -202       O  
ATOM   1401  CB  LEU A 119       0.068  38.975 -27.730  1.00101.43           C  
ANISOU 1401  CB  LEU A 119    13155  14659  10724     67    534    -93       C  
ATOM   1402  CG  LEU A 119       0.617  38.842 -29.164  1.00108.13           C  
ANISOU 1402  CG  LEU A 119    13990  15572  11525     77    630    -60       C  
ATOM   1403  CD1 LEU A 119       0.722  40.199 -29.878  1.00108.90           C  
ANISOU 1403  CD1 LEU A 119    14122  15648  11607   -204    599    -71       C  
ATOM   1404  CD2 LEU A 119       1.961  38.155 -29.161  1.00114.49           C  
ANISOU 1404  CD2 LEU A 119    14561  16703  12238    215    711     11       C  
ATOM   1405  N   LEU A 120      -2.795  37.535 -28.163  1.00 95.32           N  
ANISOU 1405  N   LEU A 120    12849  13251  10117    338    542   -185       N  
ATOM   1406  CA  LEU A 120      -3.764  36.777 -28.950  1.00 92.82           C  
ANISOU 1406  CA  LEU A 120    12721  12706   9841    451    584   -211       C  
ATOM   1407  C   LEU A 120      -5.154  37.381 -28.835  1.00 94.83           C  
ANISOU 1407  C   LEU A 120    13149  12707  10176    344    502   -274       C  
ATOM   1408  O   LEU A 120      -5.956  37.219 -29.747  1.00 94.05           O  
ANISOU 1408  O   LEU A 120    13202  12429  10103    351    518   -300       O  
ATOM   1409  CB  LEU A 120      -3.768  35.289 -28.609  1.00 92.45           C  
ANISOU 1409  CB  LEU A 120    12687  12656   9784    703    649   -189       C  
ATOM   1410  CG  LEU A 120      -3.081  34.395 -29.637  1.00 98.40           C  
ANISOU 1410  CG  LEU A 120    13428  13483  10475    859    767   -152       C  
ATOM   1411  CD1 LEU A 120      -2.892  32.989 -29.101  1.00 98.94           C  
ANISOU 1411  CD1 LEU A 120    13497  13574  10522   1115    830   -120       C  
ATOM   1412  CD2 LEU A 120      -3.851  34.354 -30.960  1.00100.57           C  
ANISOU 1412  CD2 LEU A 120    13890  13555  10768    823    799   -190       C  
ATOM   1413  N   CYS A 121      -5.418  38.129 -27.749  1.00 90.70           N  
ANISOU 1413  N   CYS A 121    12599  12180   9684    242    414   -300       N  
ATOM   1414  CA  CYS A 121      -6.679  38.848 -27.532  1.00 89.11           C  
ANISOU 1414  CA  CYS A 121    12544  11762   9552    143    334   -361       C  
ATOM   1415  C   CYS A 121      -6.756  40.051 -28.483  1.00 92.84           C  
ANISOU 1415  C   CYS A 121    13083  12167  10024    -40    308   -373       C  
ATOM   1416  O   CYS A 121      -7.829  40.353 -29.014  1.00 92.69           O  
ANISOU 1416  O   CYS A 121    13219  11948  10052    -70    278   -408       O  
ATOM   1417  CB  CYS A 121      -6.814  39.277 -26.075  1.00 88.88           C  
ANISOU 1417  CB  CYS A 121    12463  11765   9541     99    260   -385       C  
ATOM   1418  SG  CYS A 121      -8.221  40.368 -25.748  1.00 91.60           S  
ANISOU 1418  SG  CYS A 121    12969  11876   9958    -27    164   -461       S  
ATOM   1419  N   LYS A 122      -5.607  40.723 -28.692  1.00 88.57           N  
ANISOU 1419  N   LYS A 122    12425  11803   9424   -163    319   -339       N  
ATOM   1420  CA  LYS A 122      -5.460  41.869 -29.582  1.00 87.53           C  
ANISOU 1420  CA  LYS A 122    12349  11633   9275   -351    303   -337       C  
ATOM   1421  C   LYS A 122      -5.593  41.402 -31.016  1.00 90.84           C  
ANISOU 1421  C   LYS A 122    12846  11990   9678   -293    372   -316       C  
ATOM   1422  O   LYS A 122      -6.395  41.965 -31.756  1.00 90.71           O  
ANISOU 1422  O   LYS A 122    12981  11795   9688   -365    343   -336       O  
ATOM   1423  CB  LYS A 122      -4.122  42.573 -29.350  1.00 90.12           C  
ANISOU 1423  CB  LYS A 122    12515  12195   9532   -505    304   -301       C  
ATOM   1424  CG  LYS A 122      -4.127  43.403 -28.088  1.00 89.03           C  
ANISOU 1424  CG  LYS A 122    12348  12075   9403   -630    217   -335       C  
ATOM   1425  CD  LYS A 122      -2.830  44.132 -27.848  1.00 83.68           C  
ANISOU 1425  CD  LYS A 122    11514  11635   8646   -811    211   -305       C  
ATOM   1426  CE  LYS A 122      -2.911  44.939 -26.590  1.00 66.85           C  
ANISOU 1426  CE  LYS A 122     9381   9501   6518   -940    122   -349       C  
ATOM   1427  NZ  LYS A 122      -3.654  46.206 -26.813  1.00 76.03           N1+
ANISOU 1427  NZ  LYS A 122    10743  10430   7715  -1112     60   -397       N1+
ATOM   1428  N   ALA A 123      -4.859  40.335 -31.392  1.00 86.08           N  
ANISOU 1428  N   ALA A 123    12149  11529   9028   -149    464   -278       N  
ATOM   1429  CA  ALA A 123      -4.924  39.738 -32.726  1.00 84.53           C  
ANISOU 1429  CA  ALA A 123    12027  11286   8803    -73    542   -263       C  
ATOM   1430  C   ALA A 123      -6.370  39.322 -33.047  1.00 85.30           C  
ANISOU 1430  C   ALA A 123    12320  11128   8964     -2    517   -309       C  
ATOM   1431  O   ALA A 123      -6.850  39.674 -34.110  1.00 83.16           O  
ANISOU 1431  O   ALA A 123    12167  10742   8688    -65    516   -316       O  
ATOM   1432  CB  ALA A 123      -3.991  38.536 -32.812  1.00 85.66           C  
ANISOU 1432  CB  ALA A 123    12047  11611   8888    110    645   -223       C  
ATOM   1433  N   VAL A 124      -7.089  38.656 -32.090  1.00 81.35           N  
ANISOU 1433  N   VAL A 124    11848  10544   8515    111    488   -339       N  
ATOM   1434  CA  VAL A 124      -8.473  38.172 -32.265  1.00 78.92           C  
ANISOU 1434  CA  VAL A 124    11705  10019   8261    173    463   -382       C  
ATOM   1435  C   VAL A 124      -9.461  39.330 -32.452  1.00 82.02           C  
ANISOU 1435  C   VAL A 124    12208  10254   8701     31    372   -416       C  
ATOM   1436  O   VAL A 124     -10.087  39.408 -33.507  1.00 81.19           O  
ANISOU 1436  O   VAL A 124    12221  10033   8593      9    373   -424       O  
ATOM   1437  CB  VAL A 124      -8.907  37.166 -31.162  1.00 80.60           C  
ANISOU 1437  CB  VAL A 124    11912  10204   8507    316    462   -398       C  
ATOM   1438  CG1 VAL A 124     -10.422  37.095 -30.999  1.00 78.57           C  
ANISOU 1438  CG1 VAL A 124    11796   9742   8314    315    404   -448       C  
ATOM   1439  CG2 VAL A 124      -8.333  35.780 -31.435  1.00 80.81           C  
ANISOU 1439  CG2 VAL A 124    11921  10297   8487    495    564   -370       C  
ATOM   1440  N   LEU A 125      -9.567  40.231 -31.469  1.00 78.93           N  
ANISOU 1440  N   LEU A 125    11783   9863   8343    -59    298   -433       N  
ATOM   1441  CA  LEU A 125     -10.495  41.349 -31.535  1.00 78.96           C  
ANISOU 1441  CA  LEU A 125    11898   9713   8389   -170    214   -465       C  
ATOM   1442  C   LEU A 125     -10.281  42.252 -32.750  1.00 86.08           C  
ANISOU 1442  C   LEU A 125    12867  10582   9257   -296    213   -441       C  
ATOM   1443  O   LEU A 125     -11.266  42.597 -33.410  1.00 85.70           O  
ANISOU 1443  O   LEU A 125    12952  10379   9232   -312    175   -456       O  
ATOM   1444  CB  LEU A 125     -10.501  42.154 -30.231  1.00 78.97           C  
ANISOU 1444  CB  LEU A 125    11856   9730   8419   -241    145   -491       C  
ATOM   1445  CG  LEU A 125     -11.320  41.551 -29.082  1.00 83.46           C  
ANISOU 1445  CG  LEU A 125    12424  10249   9037   -135    117   -530       C  
ATOM   1446  CD1 LEU A 125     -11.233  42.410 -27.860  1.00 84.30           C  
ANISOU 1446  CD1 LEU A 125    12494  10381   9157   -214     54   -558       C  
ATOM   1447  CD2 LEU A 125     -12.787  41.428 -29.445  1.00 85.64           C  
ANISOU 1447  CD2 LEU A 125    12835  10343   9362    -88     84   -564       C  
ATOM   1448  N   SER A 126      -9.005  42.611 -33.066  1.00 84.20           N  
ANISOU 1448  N   SER A 126    12534  10501   8958   -386    255   -398       N  
ATOM   1449  CA  SER A 126      -8.671  43.460 -34.219  1.00 84.01           C  
ANISOU 1449  CA  SER A 126    12568  10463   8888   -521    264   -366       C  
ATOM   1450  C   SER A 126      -9.091  42.791 -35.514  1.00 87.91           C  
ANISOU 1450  C   SER A 126    13151  10890   9359   -444    313   -355       C  
ATOM   1451  O   SER A 126      -9.835  43.411 -36.263  1.00 88.01           O  
ANISOU 1451  O   SER A 126    13300  10761   9379   -502    272   -357       O  
ATOM   1452  CB  SER A 126      -7.197  43.852 -34.236  1.00 87.25           C  
ANISOU 1452  CB  SER A 126    12839  11084   9229   -633    308   -321       C  
ATOM   1453  OG  SER A 126      -6.347  42.728 -34.380  1.00 94.80           O  
ANISOU 1453  OG  SER A 126    13660  12218  10139   -512    400   -293       O  
ATOM   1454  N   ILE A 127      -8.715  41.503 -35.726  1.00 84.39           N  
ANISOU 1454  N   ILE A 127    12644  10534   8886   -302    396   -348       N  
ATOM   1455  CA  ILE A 127      -9.097  40.701 -36.905  1.00 84.19           C  
ANISOU 1455  CA  ILE A 127    12712  10447   8830   -219    451   -348       C  
ATOM   1456  C   ILE A 127     -10.625  40.600 -37.006  1.00 89.23           C  
ANISOU 1456  C   ILE A 127    13499  10883   9524   -184    384   -391       C  
ATOM   1457  O   ILE A 127     -11.162  40.670 -38.100  1.00 88.90           O  
ANISOU 1457  O   ILE A 127    13569  10753   9457   -205    381   -389       O  
ATOM   1458  CB  ILE A 127      -8.413  39.296 -36.925  1.00 87.09           C  
ANISOU 1458  CB  ILE A 127    13001  10934   9157    -55    555   -340       C  
ATOM   1459  CG1 ILE A 127      -6.872  39.340 -37.150  1.00 88.87           C  
ANISOU 1459  CG1 ILE A 127    13071  11390   9307    -75    637   -289       C  
ATOM   1460  CG2 ILE A 127      -9.058  38.359 -37.904  1.00 87.55           C  
ANISOU 1460  CG2 ILE A 127    13187  10886   9192     40    600   -360       C  
ATOM   1461  CD1 ILE A 127      -6.251  40.478 -38.021  1.00103.05           C  
ANISOU 1461  CD1 ILE A 127    14857  13252  11047   -256    640   -250       C  
ATOM   1462  N   ASP A 128     -11.315  40.474 -35.862  1.00 86.92           N  
ANISOU 1462  N   ASP A 128    13197  10530   9298   -138    328   -426       N  
ATOM   1463  CA  ASP A 128     -12.772  40.376 -35.795  1.00 86.13           C  
ANISOU 1463  CA  ASP A 128    13208  10267   9250   -104    263   -467       C  
ATOM   1464  C   ASP A 128     -13.464  41.632 -36.379  1.00 89.82           C  
ANISOU 1464  C   ASP A 128    13779  10622   9728   -213    185   -463       C  
ATOM   1465  O   ASP A 128     -14.251  41.493 -37.312  1.00 89.90           O  
ANISOU 1465  O   ASP A 128    13891  10543   9724   -203    170   -467       O  
ATOM   1466  CB  ASP A 128     -13.231  40.052 -34.354  1.00 87.31           C  
ANISOU 1466  CB  ASP A 128    13309  10404   9461    -39    228   -500       C  
ATOM   1467  CG  ASP A 128     -14.658  39.562 -34.222  1.00 97.68           C  
ANISOU 1467  CG  ASP A 128    14709  11589  10817     20    186   -541       C  
ATOM   1468  OD1 ASP A 128     -15.298  39.312 -35.264  1.00 98.32           O  
ANISOU 1468  OD1 ASP A 128    14885  11596  10877     21    186   -545       O  
ATOM   1469  OD2 ASP A 128     -15.139  39.437 -33.073  1.00105.34           O1-
ANISOU 1469  OD2 ASP A 128    15646  12544  11834     58    152   -568       O1-
ATOM   1470  N   TYR A 129     -13.131  42.840 -35.870  1.00 86.24           N  
ANISOU 1470  N   TYR A 129    13306  10173   9289   -318    138   -453       N  
ATOM   1471  CA  TYR A 129     -13.672  44.128 -36.341  1.00 85.80           C  
ANISOU 1471  CA  TYR A 129    13362   9999   9237   -416     67   -444       C  
ATOM   1472  C   TYR A 129     -13.204  44.473 -37.787  1.00 87.90           C  
ANISOU 1472  C   TYR A 129    13691  10275   9433   -495    100   -394       C  
ATOM   1473  O   TYR A 129     -14.013  44.905 -38.609  1.00 85.75           O  
ANISOU 1473  O   TYR A 129    13540   9891   9152   -509     57   -384       O  
ATOM   1474  CB  TYR A 129     -13.273  45.258 -35.379  1.00 87.20           C  
ANISOU 1474  CB  TYR A 129    13515  10178   9436   -514     21   -449       C  
ATOM   1475  CG  TYR A 129     -14.148  45.357 -34.152  1.00 89.28           C  
ANISOU 1475  CG  TYR A 129    13781  10373   9769   -453    -40   -501       C  
ATOM   1476  CD1 TYR A 129     -13.951  44.515 -33.063  1.00 90.47           C  
ANISOU 1476  CD1 TYR A 129    13820  10611   9944   -375    -17   -528       C  
ATOM   1477  CD2 TYR A 129     -15.135  46.336 -34.051  1.00 90.70           C  
ANISOU 1477  CD2 TYR A 129    14074  10406   9981   -469   -119   -520       C  
ATOM   1478  CE1 TYR A 129     -14.741  44.609 -31.922  1.00 89.66           C  
ANISOU 1478  CE1 TYR A 129    13717  10453   9895   -325    -68   -575       C  
ATOM   1479  CE2 TYR A 129     -15.934  46.442 -32.911  1.00 91.44           C  
ANISOU 1479  CE2 TYR A 129    14164  10448  10132   -406   -167   -570       C  
ATOM   1480  CZ  TYR A 129     -15.743  45.561 -31.854  1.00 98.92           C  
ANISOU 1480  CZ  TYR A 129    14996  11487  11100   -340   -140   -599       C  
ATOM   1481  OH  TYR A 129     -16.508  45.627 -30.710  1.00100.43           O  
ANISOU 1481  OH  TYR A 129    15180  11640  11340   -282   -182   -648       O  
ATOM   1482  N   TYR A 130     -11.904  44.258 -38.068  1.00 84.32           N  
ANISOU 1482  N   TYR A 130    13147   9968   8922   -540    179   -360       N  
ATOM   1483  CA  TYR A 130     -11.241  44.529 -39.330  1.00 84.81           C  
ANISOU 1483  CA  TYR A 130    13241  10079   8906   -622    229   -311       C  
ATOM   1484  C   TYR A 130     -11.857  43.790 -40.490  1.00 88.23           C  
ANISOU 1484  C   TYR A 130    13762  10459   9304   -548    254   -312       C  
ATOM   1485  O   TYR A 130     -12.337  44.430 -41.429  1.00 88.23           O  
ANISOU 1485  O   TYR A 130    13881  10369   9274   -609    218   -287       O  
ATOM   1486  CB  TYR A 130      -9.743  44.210 -39.234  1.00 86.74           C  
ANISOU 1486  CB  TYR A 130    13333  10528   9095   -653    319   -282       C  
ATOM   1487  CG  TYR A 130      -8.971  44.560 -40.488  1.00 88.98           C  
ANISOU 1487  CG  TYR A 130    13635  10885   9289   -753    378   -228       C  
ATOM   1488  CD1 TYR A 130      -8.780  45.885 -40.865  1.00 91.16           C  
ANISOU 1488  CD1 TYR A 130    13983  11117   9538   -928    339   -189       C  
ATOM   1489  CD2 TYR A 130      -8.411  43.570 -41.283  1.00 89.68           C  
ANISOU 1489  CD2 TYR A 130    13676  11085   9313   -673    478   -214       C  
ATOM   1490  CE1 TYR A 130      -8.039  46.213 -41.994  1.00 92.08           C  
ANISOU 1490  CE1 TYR A 130    14114  11310   9564  -1033    398   -134       C  
ATOM   1491  CE2 TYR A 130      -7.651  43.889 -42.400  1.00 91.30           C  
ANISOU 1491  CE2 TYR A 130    13885  11378   9427   -766    540   -165       C  
ATOM   1492  CZ  TYR A 130      -7.487  45.211 -42.765  1.00 99.45           C  
ANISOU 1492  CZ  TYR A 130    14981  12371  10432   -951    499   -123       C  
ATOM   1493  OH  TYR A 130      -6.769  45.531 -43.886  1.00105.60           O  
ANISOU 1493  OH  TYR A 130    15771  13236  11115  -1053    562    -69       O  
ATOM   1494  N   SER A 131     -11.825  42.446 -40.431  1.00 84.17           N  
ANISOU 1494  N   SER A 131    13198   9998   8784   -419    316   -338       N  
ATOM   1495  CA  SER A 131     -12.367  41.543 -41.445  1.00 83.39           C  
ANISOU 1495  CA  SER A 131    13185   9855   8645   -345    350   -352       C  
ATOM   1496  C   SER A 131     -13.854  41.782 -41.639  1.00 86.43           C  
ANISOU 1496  C   SER A 131    13689  10082   9066   -337    256   -376       C  
ATOM   1497  O   SER A 131     -14.357  41.510 -42.724  1.00 87.31           O  
ANISOU 1497  O   SER A 131    13896  10148   9127   -334    257   -374       O  
ATOM   1498  CB  SER A 131     -12.102  40.080 -41.086  1.00 86.60           C  
ANISOU 1498  CB  SER A 131    13533  10323   9048   -205    429   -383       C  
ATOM   1499  OG  SER A 131     -12.864  39.640 -39.970  1.00 93.17           O  
ANISOU 1499  OG  SER A 131    14350  11094   9956   -131    383   -424       O  
ATOM   1500  N   MET A 132     -14.557  42.303 -40.606  1.00 81.29           N  
ANISOU 1500  N   MET A 132    13030   9361   8495   -334    174   -399       N  
ATOM   1501  CA  MET A 132     -15.982  42.604 -40.733  1.00 80.00           C  
ANISOU 1501  CA  MET A 132    12961   9071   8364   -316     82   -418       C  
ATOM   1502  C   MET A 132     -16.179  43.726 -41.757  1.00 86.16           C  
ANISOU 1502  C   MET A 132    13847   9788   9101   -405     35   -372       C  
ATOM   1503  O   MET A 132     -16.979  43.582 -42.686  1.00 86.60           O  
ANISOU 1503  O   MET A 132    13991   9793   9122   -390      5   -367       O  
ATOM   1504  CB  MET A 132     -16.638  42.957 -39.385  1.00 80.63           C  
ANISOU 1504  CB  MET A 132    13003   9101   8530   -284     14   -452       C  
ATOM   1505  CG  MET A 132     -18.131  43.144 -39.532  1.00 83.23           C  
ANISOU 1505  CG  MET A 132    13408   9328   8886   -246    -72   -472       C  
ATOM   1506  SD  MET A 132     -19.089  43.633 -38.096  1.00 86.90           S  
ANISOU 1506  SD  MET A 132    13841   9735   9441   -196   -151   -513       S  
ATOM   1507  CE  MET A 132     -18.172  45.022 -37.563  1.00 84.22           C  
ANISOU 1507  CE  MET A 132    13503   9384   9114   -286   -165   -488       C  
ATOM   1508  N   PHE A 133     -15.398  44.804 -41.612  1.00 83.58           N  
ANISOU 1508  N   PHE A 133    13515   9473   8768   -503     32   -334       N  
ATOM   1509  CA  PHE A 133     -15.459  45.965 -42.479  1.00 84.68           C  
ANISOU 1509  CA  PHE A 133    13767   9543   8865   -598     -9   -282       C  
ATOM   1510  C   PHE A 133     -14.938  45.668 -43.886  1.00 91.19           C  
ANISOU 1510  C   PHE A 133    14633  10423   9591   -641     54   -240       C  
ATOM   1511  O   PHE A 133     -15.652  45.996 -44.839  1.00 91.91           O  
ANISOU 1511  O   PHE A 133    14839  10440   9643   -649      8   -214       O  
ATOM   1512  CB  PHE A 133     -14.780  47.166 -41.826  1.00 86.88           C  
ANISOU 1512  CB  PHE A 133    14043   9807   9161   -707    -28   -259       C  
ATOM   1513  CG  PHE A 133     -15.669  47.867 -40.822  1.00 87.96           C  
ANISOU 1513  CG  PHE A 133    14219   9827   9374   -671   -117   -291       C  
ATOM   1514  CD1 PHE A 133     -16.548  48.870 -41.224  1.00 91.79           C  
ANISOU 1514  CD1 PHE A 133    14846  10170   9860   -675   -198   -266       C  
ATOM   1515  CD2 PHE A 133     -15.634  47.522 -39.475  1.00 89.08           C  
ANISOU 1515  CD2 PHE A 133    14260  10006   9582   -622   -118   -343       C  
ATOM   1516  CE1 PHE A 133     -17.357  49.535 -40.295  1.00 92.43           C  
ANISOU 1516  CE1 PHE A 133    14967  10146  10006   -625   -272   -298       C  
ATOM   1517  CE2 PHE A 133     -16.454  48.174 -38.548  1.00 91.95           C  
ANISOU 1517  CE2 PHE A 133    14661  10266  10008   -584   -193   -376       C  
ATOM   1518  CZ  PHE A 133     -17.308  49.179 -38.963  1.00 90.78           C  
ANISOU 1518  CZ  PHE A 133    14654   9977   9860   -582   -267   -356       C  
ATOM   1519  N   THR A 134     -13.768  44.975 -44.027  1.00 87.77           N  
ANISOU 1519  N   THR A 134    14105  10128   9114   -652    158   -236       N  
ATOM   1520  CA  THR A 134     -13.228  44.601 -45.347  1.00 87.84           C  
ANISOU 1520  CA  THR A 134    14148  10204   9022   -680    232   -204       C  
ATOM   1521  C   THR A 134     -14.222  43.739 -46.112  1.00 92.57           C  
ANISOU 1521  C   THR A 134    14828  10750   9593   -594    219   -234       C  
ATOM   1522  O   THR A 134     -14.468  44.022 -47.277  1.00 94.23           O  
ANISOU 1522  O   THR A 134    15140  10932   9730   -638    209   -200       O  
ATOM   1523  CB  THR A 134     -11.827  43.969 -45.296  1.00 89.58           C  
ANISOU 1523  CB  THR A 134    14241  10598   9199   -681    352   -198       C  
ATOM   1524  OG1 THR A 134     -11.879  42.752 -44.567  1.00 91.03           O  
ANISOU 1524  OG1 THR A 134    14343  10821   9424   -547    390   -252       O  
ATOM   1525  CG2 THR A 134     -10.790  44.878 -44.698  1.00 86.84           C  
ANISOU 1525  CG2 THR A 134    13809  10330   8856   -798    363   -162       C  
ATOM   1526  N   SER A 135     -14.846  42.754 -45.441  1.00 88.07           N  
ANISOU 1526  N   SER A 135    14222  10162   9078   -485    212   -294       N  
ATOM   1527  CA  SER A 135     -15.852  41.844 -46.015  1.00 87.71           C  
ANISOU 1527  CA  SER A 135    14250  10068   9008   -418    196   -332       C  
ATOM   1528  C   SER A 135     -17.079  42.584 -46.530  1.00 91.97           C  
ANISOU 1528  C   SER A 135    14893  10506   9545   -445     83   -315       C  
ATOM   1529  O   SER A 135     -17.498  42.355 -47.660  1.00 90.92           O  
ANISOU 1529  O   SER A 135    14848  10363   9335   -458     76   -306       O  
ATOM   1530  CB  SER A 135     -16.297  40.812 -44.971  1.00 90.21           C  
ANISOU 1530  CB  SER A 135    14507  10376   9393   -318    201   -395       C  
ATOM   1531  OG  SER A 135     -17.251  39.880 -45.460  1.00100.50           O  
ANISOU 1531  OG  SER A 135    15882  11634  10669   -273    187   -436       O  
ATOM   1532  N   ILE A 136     -17.675  43.441 -45.673  1.00 89.19           N  
ANISOU 1532  N   ILE A 136    14529  10085   9273   -442     -4   -312       N  
ATOM   1533  CA  ILE A 136     -18.910  44.160 -45.963  1.00 88.82           C  
ANISOU 1533  CA  ILE A 136    14565   9948   9234   -435   -116   -295       C  
ATOM   1534  C   ILE A 136     -18.689  45.251 -47.030  1.00 93.75           C  
ANISOU 1534  C   ILE A 136    15295  10537   9787   -517   -141   -221       C  
ATOM   1535  O   ILE A 136     -19.515  45.379 -47.937  1.00 92.82           O  
ANISOU 1535  O   ILE A 136    15265  10388   9617   -510   -200   -198       O  
ATOM   1536  CB  ILE A 136     -19.563  44.660 -44.640  1.00 90.56           C  
ANISOU 1536  CB  ILE A 136    14739  10112   9558   -386   -187   -321       C  
ATOM   1537  CG1 ILE A 136     -20.116  43.465 -43.845  1.00 89.23           C  
ANISOU 1537  CG1 ILE A 136    14492   9973   9439   -305   -175   -389       C  
ATOM   1538  CG2 ILE A 136     -20.672  45.657 -44.905  1.00 91.48           C  
ANISOU 1538  CG2 ILE A 136    14939  10139   9679   -368   -297   -291       C  
ATOM   1539  CD1 ILE A 136     -20.339  43.702 -42.384  1.00 98.24           C  
ANISOU 1539  CD1 ILE A 136    15558  11095  10675   -262   -203   -421       C  
ATOM   1540  N   PHE A 137     -17.561  45.978 -46.965  1.00 91.67           N  
ANISOU 1540  N   PHE A 137    15025  10293   9512   -603    -95   -179       N  
ATOM   1541  CA  PHE A 137     -17.289  47.013 -47.954  1.00 93.03           C  
ANISOU 1541  CA  PHE A 137    15310  10428   9611   -696   -111   -103       C  
ATOM   1542  C   PHE A 137     -16.836  46.445 -49.302  1.00 96.34           C  
ANISOU 1542  C   PHE A 137    15767  10922   9914   -735    -43    -79       C  
ATOM   1543  O   PHE A 137     -17.144  47.063 -50.317  1.00 96.45           O  
ANISOU 1543  O   PHE A 137    15897  10893   9856   -779    -82    -21       O  
ATOM   1544  CB  PHE A 137     -16.349  48.097 -47.420  1.00 95.98           C  
ANISOU 1544  CB  PHE A 137    15680  10785  10003   -799    -96    -65       C  
ATOM   1545  CG  PHE A 137     -17.141  49.092 -46.602  1.00 98.30           C  
ANISOU 1545  CG  PHE A 137    16030  10948  10373   -771   -195    -66       C  
ATOM   1546  CD1 PHE A 137     -17.942  50.051 -47.225  1.00103.35           C  
ANISOU 1546  CD1 PHE A 137    16816  11468  10984   -768   -280    -12       C  
ATOM   1547  CD2 PHE A 137     -17.175  49.005 -45.214  1.00 99.47           C  
ANISOU 1547  CD2 PHE A 137    16087  11093  10615   -728   -205   -122       C  
ATOM   1548  CE1 PHE A 137     -18.737  50.920 -46.470  1.00104.25           C  
ANISOU 1548  CE1 PHE A 137    16987  11459  11165   -712   -367    -17       C  
ATOM   1549  CE2 PHE A 137     -17.960  49.880 -44.460  1.00102.23           C  
ANISOU 1549  CE2 PHE A 137    16493  11322  11028   -686   -291   -131       C  
ATOM   1550  CZ  PHE A 137     -18.736  50.827 -45.091  1.00101.80           C  
ANISOU 1550  CZ  PHE A 137    16586  11148  10947   -673   -369    -80       C  
ATOM   1551  N   THR A 138     -16.184  45.256 -49.335  1.00 91.85           N  
ANISOU 1551  N   THR A 138    15115  10460   9323   -705     57   -123       N  
ATOM   1552  CA  THR A 138     -15.832  44.645 -50.616  1.00 91.88           C  
ANISOU 1552  CA  THR A 138    15167  10531   9211   -726    127   -111       C  
ATOM   1553  C   THR A 138     -17.090  44.055 -51.272  1.00 94.09           C  
ANISOU 1553  C   THR A 138    15528  10765   9456   -668     63   -140       C  
ATOM   1554  O   THR A 138     -17.197  44.092 -52.497  1.00 95.76           O  
ANISOU 1554  O   THR A 138    15834  10989   9563   -708     65   -109       O  
ATOM   1555  CB  THR A 138     -14.638  43.680 -50.553  1.00105.75           C  
ANISOU 1555  CB  THR A 138    16827  12416  10938   -708    263   -140       C  
ATOM   1556  OG1 THR A 138     -14.353  43.277 -51.889  1.00114.04           O  
ANISOU 1556  OG1 THR A 138    17946  13519  11863   -733    326   -125       O  
ATOM   1557  CG2 THR A 138     -14.922  42.426 -49.780  1.00108.37           C  
ANISOU 1557  CG2 THR A 138    17089  12759  11327   -591    289   -220       C  
ATOM   1558  N   LEU A 139     -18.044  43.534 -50.463  1.00 87.40           N  
ANISOU 1558  N   LEU A 139    14643   9877   8690   -585      6   -198       N  
ATOM   1559  CA  LEU A 139     -19.319  42.992 -50.939  1.00 85.45           C  
ANISOU 1559  CA  LEU A 139    14452   9602   8414   -544    -65   -228       C  
ATOM   1560  C   LEU A 139     -20.148  44.142 -51.541  1.00 90.92           C  
ANISOU 1560  C   LEU A 139    15234  10233   9078   -570   -180   -163       C  
ATOM   1561  O   LEU A 139     -20.635  44.011 -52.666  1.00 90.57           O  
ANISOU 1561  O   LEU A 139    15274  10203   8937   -590   -210   -144       O  
ATOM   1562  CB  LEU A 139     -20.079  42.296 -49.796  1.00 83.21           C  
ANISOU 1562  CB  LEU A 139    14091   9297   8226   -466    -98   -297       C  
ATOM   1563  CG  LEU A 139     -21.544  41.902 -50.063  1.00 85.67           C  
ANISOU 1563  CG  LEU A 139    14438   9590   8523   -437   -191   -326       C  
ATOM   1564  CD1 LEU A 139     -21.641  40.574 -50.822  1.00 84.94           C  
ANISOU 1564  CD1 LEU A 139    14392   9538   8344   -447   -136   -379       C  
ATOM   1565  CD2 LEU A 139     -22.377  41.896 -48.765  1.00 83.60           C  
ANISOU 1565  CD2 LEU A 139    14092   9299   8373   -374   -253   -363       C  
ATOM   1566  N   THR A 140     -20.252  45.280 -50.814  1.00 88.45           N  
ANISOU 1566  N   THR A 140    14914   9852   8841   -567   -240   -125       N  
ATOM   1567  CA  THR A 140     -20.997  46.473 -51.245  1.00 89.62           C  
ANISOU 1567  CA  THR A 140    15158   9924   8969   -567   -347    -56       C  
ATOM   1568  C   THR A 140     -20.534  46.948 -52.631  1.00 96.00           C  
ANISOU 1568  C   THR A 140    16081  10741   9653   -650   -329     19       C  
ATOM   1569  O   THR A 140     -21.363  47.168 -53.523  1.00 95.44           O  
ANISOU 1569  O   THR A 140    16093  10658   9510   -636   -405     57       O  
ATOM   1570  CB  THR A 140     -20.943  47.568 -50.162  1.00 95.47           C  
ANISOU 1570  CB  THR A 140    15889  10579   9808   -553   -388    -37       C  
ATOM   1571  OG1 THR A 140     -21.390  47.014 -48.925  1.00 96.43           O  
ANISOU 1571  OG1 THR A 140    15901  10708  10032   -476   -398   -110       O  
ATOM   1572  CG2 THR A 140     -21.796  48.784 -50.504  1.00 92.88           C  
ANISOU 1572  CG2 THR A 140    15672  10153   9465   -523   -499     31       C  
ATOM   1573  N   MET A 141     -19.206  47.040 -52.812  1.00 94.96           N  
ANISOU 1573  N   MET A 141    15942  10649   9489   -736   -226     40       N  
ATOM   1574  CA  MET A 141     -18.581  47.446 -54.062  1.00 97.11           C  
ANISOU 1574  CA  MET A 141    16311  10947   9638   -829   -186    110       C  
ATOM   1575  C   MET A 141     -18.840  46.451 -55.183  1.00102.79           C  
ANISOU 1575  C   MET A 141    17065  11742  10248   -821   -159     86       C  
ATOM   1576  O   MET A 141     -18.996  46.886 -56.322  1.00104.36           O  
ANISOU 1576  O   MET A 141    17375  11939  10338   -868   -186    149       O  
ATOM   1577  CB  MET A 141     -17.085  47.754 -53.883  1.00100.26           C  
ANISOU 1577  CB  MET A 141    16669  11396  10029   -930    -77    135       C  
ATOM   1578  CG  MET A 141     -16.823  49.010 -53.068  1.00104.85           C  
ANISOU 1578  CG  MET A 141    17269  11889  10682   -981   -116    178       C  
ATOM   1579  SD  MET A 141     -17.746  50.468 -53.656  1.00111.46           S  
ANISOU 1579  SD  MET A 141    18296  12570  11485   -992   -244    275       S  
ATOM   1580  CE  MET A 141     -18.494  51.001 -52.091  1.00106.96           C  
ANISOU 1580  CE  MET A 141    17688  11885  11066   -898   -331    232       C  
ATOM   1581  N   MET A 142     -18.955  45.137 -54.865  1.00 98.96           N  
ANISOU 1581  N   MET A 142    16502  11314   9784   -763   -111     -4       N  
ATOM   1582  CA  MET A 142     -19.276  44.119 -55.867  1.00 99.52           C  
ANISOU 1582  CA  MET A 142    16623  11442   9748   -759    -87    -42       C  
ATOM   1583  C   MET A 142     -20.615  44.437 -56.516  1.00104.11           C  
ANISOU 1583  C   MET A 142    17286  11990  10280   -744   -219    -14       C  
ATOM   1584  O   MET A 142     -20.699  44.418 -57.739  1.00105.87           O  
ANISOU 1584  O   MET A 142    17603  12247  10374   -790   -223     18       O  
ATOM   1585  CB  MET A 142     -19.285  42.707 -55.277  1.00101.10           C  
ANISOU 1585  CB  MET A 142    16747  11677   9989   -696    -24   -144       C  
ATOM   1586  CG  MET A 142     -17.924  42.085 -55.239  1.00104.95           C  
ANISOU 1586  CG  MET A 142    17186  12235  10453   -702    126   -169       C  
ATOM   1587  SD  MET A 142     -17.929  40.278 -55.095  1.00108.59           S  
ANISOU 1587  SD  MET A 142    17632  12728  10900   -626    215   -281       S  
ATOM   1588  CE  MET A 142     -18.011  39.792 -56.817  1.00106.31           C  
ANISOU 1588  CE  MET A 142    17486  12481  10427   -676    251   -286       C  
ATOM   1589  N   CYS A 143     -21.632  44.809 -55.699  1.00 98.55           N  
ANISOU 1589  N   CYS A 143    16542  11232   9672   -678   -327    -20       N  
ATOM   1590  CA  CYS A 143     -22.978  45.200 -56.133  1.00 97.52           C  
ANISOU 1590  CA  CYS A 143    16459  11086   9508   -642   -464     12       C  
ATOM   1591  C   CYS A 143     -22.950  46.477 -56.955  1.00 99.43           C  
ANISOU 1591  C   CYS A 143    16816  11285   9679   -674   -519    124       C  
ATOM   1592  O   CYS A 143     -23.702  46.577 -57.925  1.00100.11           O  
ANISOU 1592  O   CYS A 143    16974  11400   9664   -673   -596    162       O  
ATOM   1593  CB  CYS A 143     -23.923  45.312 -54.942  1.00 97.10           C  
ANISOU 1593  CB  CYS A 143    16317  10998   9580   -553   -546    -21       C  
ATOM   1594  SG  CYS A 143     -24.078  43.780 -53.984  1.00 99.81           S  
ANISOU 1594  SG  CYS A 143    16540  11385   9998   -523   -486   -144       S  
ATOM   1595  N   VAL A 144     -22.047  47.431 -56.608  1.00 93.54           N  
ANISOU 1595  N   VAL A 144    16094  10474   8972   -712   -478    179       N  
ATOM   1596  CA  VAL A 144     -21.861  48.674 -57.369  1.00 93.21           C  
ANISOU 1596  CA  VAL A 144    16185  10373   8859   -760   -515    292       C  
ATOM   1597  C   VAL A 144     -21.257  48.302 -58.740  1.00 98.16           C  
ANISOU 1597  C   VAL A 144    16887  11077   9331   -851   -447    320       C  
ATOM   1598  O   VAL A 144     -21.716  48.808 -59.764  1.00 99.64           O  
ANISOU 1598  O   VAL A 144    17188  11259   9411   -865   -513    395       O  
ATOM   1599  CB  VAL A 144     -21.012  49.739 -56.619  1.00 95.80           C  
ANISOU 1599  CB  VAL A 144    16529  10609   9261   -806   -482    336       C  
ATOM   1600  CG1 VAL A 144     -20.824  51.002 -57.463  1.00 96.51           C  
ANISOU 1600  CG1 VAL A 144    16784  10623   9264   -870   -516    457       C  
ATOM   1601  CG2 VAL A 144     -21.631  50.091 -55.272  1.00 94.34           C  
ANISOU 1601  CG2 VAL A 144    16280  10347   9219   -712   -546    300       C  
ATOM   1602  N   ASP A 145     -20.272  47.378 -58.751  1.00 93.47           N  
ANISOU 1602  N   ASP A 145    16230  10563   8721   -899   -315    258       N  
ATOM   1603  CA  ASP A 145     -19.584  46.884 -59.947  1.00 93.53           C  
ANISOU 1603  CA  ASP A 145    16294  10659   8585   -975   -225    266       C  
ATOM   1604  C   ASP A 145     -20.530  46.147 -60.896  1.00 98.84           C  
ANISOU 1604  C   ASP A 145    17022  11383   9150   -952   -281    237       C  
ATOM   1605  O   ASP A 145     -20.423  46.315 -62.111  1.00 99.89           O  
ANISOU 1605  O   ASP A 145    17259  11554   9139  -1011   -276    289       O  
ATOM   1606  CB  ASP A 145     -18.408  45.994 -59.546  1.00 94.25           C  
ANISOU 1606  CB  ASP A 145    16287  10825   8699   -994    -73    196       C  
ATOM   1607  CG  ASP A 145     -17.548  45.573 -60.705  1.00105.96           C  
ANISOU 1607  CG  ASP A 145    17822  12403  10033  -1064     38    206       C  
ATOM   1608  OD1 ASP A 145     -16.946  46.462 -61.349  1.00107.56           O  
ANISOU 1608  OD1 ASP A 145    18097  12612  10160  -1154     60    297       O  
ATOM   1609  OD2 ASP A 145     -17.469  44.354 -60.968  1.00113.51           O1-
ANISOU 1609  OD2 ASP A 145    18758  13425  10944  -1030    108    123       O1-
ATOM   1610  N   ARG A 146     -21.470  45.356 -60.337  1.00 95.45           N  
ANISOU 1610  N   ARG A 146    16525  10959   8782   -878   -338    156       N  
ATOM   1611  CA  ARG A 146     -22.500  44.616 -61.083  1.00 96.08           C  
ANISOU 1611  CA  ARG A 146    16644  11094   8769   -868   -406    118       C  
ATOM   1612  C   ARG A 146     -23.473  45.617 -61.693  1.00100.34           C  
ANISOU 1612  C   ARG A 146    17259  11616   9251   -852   -552    214       C  
ATOM   1613  O   ARG A 146     -23.895  45.441 -62.834  1.00100.34           O  
ANISOU 1613  O   ARG A 146    17340  11675   9108   -887   -593    235       O  
ATOM   1614  CB  ARG A 146     -23.273  43.646 -60.163  1.00 96.86           C  
ANISOU 1614  CB  ARG A 146    16641  11199   8961   -806   -435     16       C  
ATOM   1615  CG  ARG A 146     -22.445  42.511 -59.551  1.00108.71           C  
ANISOU 1615  CG  ARG A 146    18078  12713  10512   -802   -298    -82       C  
ATOM   1616  CD  ARG A 146     -22.456  41.244 -60.386  1.00120.68           C  
ANISOU 1616  CD  ARG A 146    19658  14289  11906   -839   -237   -159       C  
ATOM   1617  NE  ARG A 146     -21.366  41.224 -61.363  1.00123.59           N  
ANISOU 1617  NE  ARG A 146    20104  14697  12156   -893   -125   -135       N  
ATOM   1618  CZ  ARG A 146     -21.524  41.410 -62.668  1.00126.86           C  
ANISOU 1618  CZ  ARG A 146    20629  15156  12415   -953   -149    -95       C  
ATOM   1619  NH1 ARG A 146     -22.733  41.627 -63.172  1.00115.53           N  
ANISOU 1619  NH1 ARG A 146    19238  13735  10922   -965   -288    -72       N  
ATOM   1620  NH2 ARG A 146     -20.477  41.370 -63.480  1.00104.28           N1+
ANISOU 1620  NH2 ARG A 146    17831  12341   9449   -999    -34    -77       N1+
ATOM   1621  N   TYR A 147     -23.813  46.675 -60.924  1.00 97.19           N  
ANISOU 1621  N   TYR A 147    16839  11133   8957   -792   -628    272       N  
ATOM   1622  CA  TYR A 147     -24.695  47.764 -61.350  1.00 97.87           C  
ANISOU 1622  CA  TYR A 147    17000  11182   9003   -745   -765    374       C  
ATOM   1623  C   TYR A 147     -24.144  48.475 -62.603  1.00100.89           C  
ANISOU 1623  C   TYR A 147    17531  11559   9242   -822   -749    480       C  
ATOM   1624  O   TYR A 147     -24.901  48.771 -63.529  1.00101.12           O  
ANISOU 1624  O   TYR A 147    17640  11623   9158   -807   -846    543       O  
ATOM   1625  CB  TYR A 147     -24.952  48.764 -60.188  1.00 98.75           C  
ANISOU 1625  CB  TYR A 147    17078  11183   9261   -659   -821    408       C  
ATOM   1626  CG  TYR A 147     -25.433  50.112 -60.670  1.00102.92           C  
ANISOU 1626  CG  TYR A 147    17727  11637   9741   -615   -925    535       C  
ATOM   1627  CD1 TYR A 147     -26.753  50.300 -61.068  1.00106.03           C  
ANISOU 1627  CD1 TYR A 147    18129  12073  10086   -521  -1064    573       C  
ATOM   1628  CD2 TYR A 147     -24.544  51.173 -60.832  1.00104.84           C  
ANISOU 1628  CD2 TYR A 147    18086  11778   9970   -674   -882    623       C  
ATOM   1629  CE1 TYR A 147     -27.183  51.515 -61.598  1.00108.68           C  
ANISOU 1629  CE1 TYR A 147    18590  12341  10362   -463  -1159    699       C  
ATOM   1630  CE2 TYR A 147     -24.962  52.392 -61.367  1.00107.47           C  
ANISOU 1630  CE2 TYR A 147    18563  12028  10244   -635   -972    747       C  
ATOM   1631  CZ  TYR A 147     -26.283  52.556 -61.752  1.00116.15           C  
ANISOU 1631  CZ  TYR A 147    19673  13162  11297   -518  -1111    786       C  
ATOM   1632  OH  TYR A 147     -26.706  53.749 -62.276  1.00119.79           O  
ANISOU 1632  OH  TYR A 147    20282  13538  11695   -457  -1201    915       O  
ATOM   1633  N   ILE A 148     -22.834  48.765 -62.607  1.00 96.40           N  
ANISOU 1633  N   ILE A 148    16995  10959   8673   -906   -629    502       N  
ATOM   1634  CA  ILE A 148     -22.164  49.462 -63.706  1.00 97.13           C  
ANISOU 1634  CA  ILE A 148    17225  11049   8633   -999   -595    604       C  
ATOM   1635  C   ILE A 148     -22.154  48.580 -64.961  1.00102.52           C  
ANISOU 1635  C   ILE A 148    17953  11851   9148  -1054   -559    578       C  
ATOM   1636  O   ILE A 148     -22.485  49.059 -66.038  1.00103.00           O  
ANISOU 1636  O   ILE A 148    18132  11929   9072  -1080   -619    664       O  
ATOM   1637  CB  ILE A 148     -20.771  49.983 -63.249  1.00 99.04           C  
ANISOU 1637  CB  ILE A 148    17463  11243   8925  -1086   -473    628       C  
ATOM   1638  CG1 ILE A 148     -20.961  51.104 -62.196  1.00 97.61           C  
ANISOU 1638  CG1 ILE A 148    17290  10923   8876  -1041   -538    675       C  
ATOM   1639  CG2 ILE A 148     -19.914  50.458 -64.443  1.00101.30           C  
ANISOU 1639  CG2 ILE A 148    17873  11560   9056  -1210   -404    719       C  
ATOM   1640  CD1 ILE A 148     -19.870  51.291 -61.229  1.00 95.74           C  
ANISOU 1640  CD1 ILE A 148    16982  10654   8743  -1100   -438    647       C  
ATOM   1641  N   ALA A 149     -21.864  47.279 -64.785  1.00 99.39           N  
ANISOU 1641  N   ALA A 149    17470  11531   8760  -1063   -470    458       N  
ATOM   1642  CA  ALA A 149     -21.851  46.256 -65.833  1.00 99.44           C  
ANISOU 1642  CA  ALA A 149    17521  11643   8617  -1109   -423    403       C  
ATOM   1643  C   ALA A 149     -23.214  46.128 -66.510  1.00104.74           C  
ANISOU 1643  C   ALA A 149    18240  12359   9198  -1080   -569    413       C  
ATOM   1644  O   ALA A 149     -23.278  46.119 -67.731  1.00106.29           O  
ANISOU 1644  O   ALA A 149    18542  12618   9226  -1136   -581    452       O  
ATOM   1645  CB  ALA A 149     -21.455  44.914 -65.229  1.00 98.68           C  
ANISOU 1645  CB  ALA A 149    17327  11585   8581  -1093   -315    265       C  
ATOM   1646  N   VAL A 150     -24.295  46.028 -65.714  1.00101.23           N  
ANISOU 1646  N   VAL A 150    17710  11897   8858   -996   -679    379       N  
ATOM   1647  CA  VAL A 150     -25.674  45.838 -66.168  1.00102.07           C  
ANISOU 1647  CA  VAL A 150    17819  12070   8894   -962   -825    380       C  
ATOM   1648  C   VAL A 150     -26.310  47.114 -66.778  1.00109.92           C  
ANISOU 1648  C   VAL A 150    18898  13048   9818   -922   -959    524       C  
ATOM   1649  O   VAL A 150     -26.894  47.021 -67.871  1.00111.38           O  
ANISOU 1649  O   VAL A 150    19154  13322   9846   -950  -1034    558       O  
ATOM   1650  CB  VAL A 150     -26.529  45.220 -65.020  1.00104.14           C  
ANISOU 1650  CB  VAL A 150    17940  12336   9293   -892   -879    289       C  
ATOM   1651  CG1 VAL A 150     -27.986  45.689 -65.021  1.00104.38           C  
ANISOU 1651  CG1 VAL A 150    17933  12411   9315   -815  -1057    338       C  
ATOM   1652  CG2 VAL A 150     -26.454  43.701 -65.060  1.00103.34           C  
ANISOU 1652  CG2 VAL A 150    17810  12296   9159   -949   -800    153       C  
ATOM   1653  N   CYS A 151     -26.196  48.283 -66.085  1.00106.20           N  
ANISOU 1653  N   CYS A 151    18431  12464   9458   -856   -990    607       N  
ATOM   1654  CA  CYS A 151     -26.852  49.538 -66.462  1.00106.62           C  
ANISOU 1654  CA  CYS A 151    18571  12472   9468   -785  -1118    744       C  
ATOM   1655  C   CYS A 151     -26.048  50.424 -67.409  1.00111.05           C  
ANISOU 1655  C   CYS A 151    19300  12983   9913   -859  -1078    865       C  
ATOM   1656  O   CYS A 151     -26.655  51.241 -68.112  1.00112.78           O  
ANISOU 1656  O   CYS A 151    19621  13194  10035   -815  -1187    981       O  
ATOM   1657  CB  CYS A 151     -27.286  50.301 -65.219  1.00106.65           C  
ANISOU 1657  CB  CYS A 151    18511  12369   9641   -664  -1178    763       C  
ATOM   1658  SG  CYS A 151     -28.312  49.331 -64.079  1.00109.42           S  
ANISOU 1658  SG  CYS A 151    18662  12790  10122   -578  -1229    632       S  
ATOM   1659  N   HIS A 152     -24.709  50.283 -67.445  1.00106.30           N  
ANISOU 1659  N   HIS A 152    18724  12355   9310   -968   -924    844       N  
ATOM   1660  CA  HIS A 152     -23.853  51.047 -68.372  1.00107.01           C  
ANISOU 1660  CA  HIS A 152    18967  12415   9278  -1065   -869    955       C  
ATOM   1661  C   HIS A 152     -22.852  50.070 -69.040  1.00109.54           C  
ANISOU 1661  C   HIS A 152    19283  12841   9498  -1187   -718    884       C  
ATOM   1662  O   HIS A 152     -21.657  50.153 -68.746  1.00108.28           O  
ANISOU 1662  O   HIS A 152    19109  12656   9377  -1262   -584    876       O  
ATOM   1663  CB  HIS A 152     -23.104  52.195 -67.654  1.00107.93           C  
ANISOU 1663  CB  HIS A 152    19130  12381   9498  -1083   -827   1028       C  
ATOM   1664  CG  HIS A 152     -23.945  53.052 -66.754  1.00111.54           C  
ANISOU 1664  CG  HIS A 152    19582  12717  10080   -952   -946   1069       C  
ATOM   1665  ND1 HIS A 152     -24.935  53.874 -67.255  1.00114.86           N  
ANISOU 1665  ND1 HIS A 152    20109  13100  10435   -857  -1089   1180       N  
ATOM   1666  CD2 HIS A 152     -23.870  53.228 -65.413  1.00112.28           C  
ANISOU 1666  CD2 HIS A 152    19586  12723  10351   -898   -933   1017       C  
ATOM   1667  CE1 HIS A 152     -25.449  54.499 -66.205  1.00113.74           C  
ANISOU 1667  CE1 HIS A 152    19937  12847  10433   -739  -1155   1186       C  
ATOM   1668  NE2 HIS A 152     -24.836  54.148 -65.078  1.00112.54           N  
ANISOU 1668  NE2 HIS A 152    19672  12660  10429   -766  -1065   1088       N  
ATOM   1669  N   PRO A 153     -23.310  49.125 -69.915  1.00106.03           N  
ANISOU 1669  N   PRO A 153    18848  12520   8919  -1207   -734    828       N  
ATOM   1670  CA  PRO A 153     -22.377  48.136 -70.491  1.00105.34           C  
ANISOU 1670  CA  PRO A 153    18763  12524   8737  -1302   -581    747       C  
ATOM   1671  C   PRO A 153     -21.294  48.681 -71.420  1.00110.34           C  
ANISOU 1671  C   PRO A 153    19513  13175   9236  -1412   -479    835       C  
ATOM   1672  O   PRO A 153     -20.246  48.048 -71.574  1.00109.63           O  
ANISOU 1672  O   PRO A 153    19398  13144   9113  -1478   -322    774       O  
ATOM   1673  CB  PRO A 153     -23.307  47.167 -71.224  1.00107.41           C  
ANISOU 1673  CB  PRO A 153    19037  12895   8877  -1297   -650    676       C  
ATOM   1674  CG  PRO A 153     -24.672  47.411 -70.652  1.00111.46           C  
ANISOU 1674  CG  PRO A 153    19487  13389   9474  -1193   -822    687       C  
ATOM   1675  CD  PRO A 153     -24.688  48.864 -70.383  1.00107.84           C  
ANISOU 1675  CD  PRO A 153    19081  12822   9073  -1145   -887    828       C  
ATOM   1676  N   VAL A 154     -21.535  49.843 -72.035  1.00108.00           N  
ANISOU 1676  N   VAL A 154    19346  12832   8859  -1428   -563    982       N  
ATOM   1677  CA  VAL A 154     -20.562  50.441 -72.940  1.00108.99           C  
ANISOU 1677  CA  VAL A 154    19594  12971   8846  -1546   -473   1081       C  
ATOM   1678  C   VAL A 154     -19.499  51.221 -72.157  1.00115.79           C  
ANISOU 1678  C   VAL A 154    20433  13739   9824  -1602   -379   1126       C  
ATOM   1679  O   VAL A 154     -18.303  51.085 -72.442  1.00115.79           O  
ANISOU 1679  O   VAL A 154    20428  13799   9769  -1709   -227   1122       O  
ATOM   1680  CB  VAL A 154     -21.221  51.276 -74.053  1.00112.94           C  
ANISOU 1680  CB  VAL A 154    20261  13468   9183  -1554   -594   1224       C  
ATOM   1681  CG1 VAL A 154     -20.222  51.551 -75.157  1.00114.02           C  
ANISOU 1681  CG1 VAL A 154    20520  13660   9141  -1693   -481   1300       C  
ATOM   1682  CG2 VAL A 154     -22.462  50.580 -74.610  1.00112.45           C  
ANISOU 1682  CG2 VAL A 154    20194  13502   9030  -1487   -719   1178       C  
ATOM   1683  N   LYS A 155     -19.941  52.021 -71.156  1.00113.37           N  
ANISOU 1683  N   LYS A 155    20108  13296   9672  -1529   -469   1165       N  
ATOM   1684  CA  LYS A 155     -19.053  52.807 -70.287  1.00113.16           C  
ANISOU 1684  CA  LYS A 155    20064  13166   9764  -1585   -401   1201       C  
ATOM   1685  C   LYS A 155     -18.253  51.894 -69.357  1.00115.25           C  
ANISOU 1685  C   LYS A 155    20149  13490  10151  -1594   -272   1067       C  
ATOM   1686  O   LYS A 155     -17.117  52.223 -69.019  1.00114.42           O  
ANISOU 1686  O   LYS A 155    20015  13382  10077  -1692   -160   1083       O  
ATOM   1687  CB  LYS A 155     -19.832  53.862 -69.479  1.00116.06           C  
ANISOU 1687  CB  LYS A 155    20477  13366  10256  -1490   -535   1266       C  
ATOM   1688  CG  LYS A 155     -20.597  54.867 -70.338  1.00131.91           C  
ANISOU 1688  CG  LYS A 155    22674  15301  12147  -1458   -664   1415       C  
ATOM   1689  CD  LYS A 155     -20.409  56.303 -69.874  1.00138.21           C  
ANISOU 1689  CD  LYS A 155    23604  15909  13003  -1475   -695   1532       C  
ATOM   1690  CE  LYS A 155     -20.967  57.279 -70.883  1.00146.34           C  
ANISOU 1690  CE  LYS A 155    24847  16868  13887  -1457   -798   1693       C  
ATOM   1691  NZ  LYS A 155     -20.139  57.359 -72.119  1.00153.42           N1+
ANISOU 1691  NZ  LYS A 155    25857  17843  14594  -1619   -709   1770       N1+
ATOM   1692  N   ALA A 156     -18.833  50.732 -68.980  1.00111.61           N  
ANISOU 1692  N   ALA A 156    19571  13091   9746  -1499   -288    938       N  
ATOM   1693  CA  ALA A 156     -18.201  49.717 -68.130  1.00110.91           C  
ANISOU 1693  CA  ALA A 156    19319  13058   9763  -1482   -174    807       C  
ATOM   1694  C   ALA A 156     -16.920  49.127 -68.741  1.00117.26           C  
ANISOU 1694  C   ALA A 156    20103  13987  10462  -1578      3    778       C  
ATOM   1695  O   ALA A 156     -16.079  48.621 -68.004  1.00116.51           O  
ANISOU 1695  O   ALA A 156    19882  13933  10453  -1579    115    707       O  
ATOM   1696  CB  ALA A 156     -19.184  48.600 -67.822  1.00110.60           C  
ANISOU 1696  CB  ALA A 156    19201  13052   9771  -1373   -235    690       C  
ATOM   1697  N   LEU A 157     -16.756  49.199 -70.073  1.00116.85           N  
ANISOU 1697  N   LEU A 157    20171  14006  10220  -1652     30    837       N  
ATOM   1698  CA  LEU A 157     -15.560  48.673 -70.739  1.00118.05           C  
ANISOU 1698  CA  LEU A 157    20308  14290  10253  -1737    203    814       C  
ATOM   1699  C   LEU A 157     -14.307  49.482 -70.388  1.00125.36           C  
ANISOU 1699  C   LEU A 157    21198  15223  11211  -1847    307    885       C  
ATOM   1700  O   LEU A 157     -13.187  48.985 -70.528  1.00125.09           O  
ANISOU 1700  O   LEU A 157    21086  15313  11129  -1897    466    849       O  
ATOM   1701  CB  LEU A 157     -15.770  48.529 -72.257  1.00119.36           C  
ANISOU 1701  CB  LEU A 157    20616  14536  10199  -1787    202    853       C  
ATOM   1702  CG  LEU A 157     -16.771  47.433 -72.702  1.00123.14           C  
ANISOU 1702  CG  LEU A 157    21116  15057  10615  -1706    139    752       C  
ATOM   1703  CD1 LEU A 157     -17.130  47.585 -74.172  1.00125.27           C  
ANISOU 1703  CD1 LEU A 157    21545  15388  10664  -1765     99    817       C  
ATOM   1704  CD2 LEU A 157     -16.234  46.017 -72.439  1.00122.86           C  
ANISOU 1704  CD2 LEU A 157    20980  15105  10595  -1662    278    599       C  
ATOM   1705  N   ASP A 158     -14.519  50.700 -69.854  1.00124.38           N  
ANISOU 1705  N   ASP A 158    21123  14965  11172  -1879    217    981       N  
ATOM   1706  CA  ASP A 158     -13.487  51.611 -69.382  1.00125.67           C  
ANISOU 1706  CA  ASP A 158    21266  15104  11378  -2000    286   1052       C  
ATOM   1707  C   ASP A 158     -13.334  51.459 -67.868  1.00127.94           C  
ANISOU 1707  C   ASP A 158    21398  15345  11870  -1941    288    975       C  
ATOM   1708  O   ASP A 158     -12.209  51.259 -67.411  1.00128.63           O  
ANISOU 1708  O   ASP A 158    21361  15526  11989  -2004    414    945       O  
ATOM   1709  CB  ASP A 158     -13.832  53.065 -69.761  1.00129.89           C  
ANISOU 1709  CB  ASP A 158    21988  15498  11865  -2078    185   1205       C  
ATOM   1710  CG  ASP A 158     -12.853  54.115 -69.254  1.00147.61           C  
ANISOU 1710  CG  ASP A 158    24244  17692  14151  -2228    243   1284       C  
ATOM   1711  OD1 ASP A 158     -11.847  54.379 -69.957  1.00150.93           O  
ANISOU 1711  OD1 ASP A 158    24693  18208  14443  -2383    357   1347       O  
ATOM   1712  OD2 ASP A 158     -13.102  54.687 -68.162  1.00153.18           O1-
ANISOU 1712  OD2 ASP A 158    24932  18263  15008  -2198    174   1281       O1-
ATOM   1713  N   PHE A 159     -14.450  51.546 -67.090  1.00121.81           N  
ANISOU 1713  N   PHE A 159    20618  14440  11223  -1818    150    943       N  
ATOM   1714  CA  PHE A 159     -14.398  51.450 -65.627  1.00119.19           C  
ANISOU 1714  CA  PHE A 159    20150  14057  11080  -1759    141    872       C  
ATOM   1715  C   PHE A 159     -14.038  50.060 -65.109  1.00119.40           C  
ANISOU 1715  C   PHE A 159    20001  14203  11164  -1681    236    736       C  
ATOM   1716  O   PHE A 159     -13.180  49.961 -64.232  1.00119.22           O  
ANISOU 1716  O   PHE A 159    19848  14221  11229  -1705    317    700       O  
ATOM   1717  CB  PHE A 159     -15.691  51.964 -64.932  1.00120.49           C  
ANISOU 1717  CB  PHE A 159    20360  14060  11360  -1644    -26    878       C  
ATOM   1718  CG  PHE A 159     -15.753  51.637 -63.441  1.00121.01           C  
ANISOU 1718  CG  PHE A 159    20277  14091  11612  -1564    -33    785       C  
ATOM   1719  CD1 PHE A 159     -15.039  52.390 -62.512  1.00124.15           C  
ANISOU 1719  CD1 PHE A 159    20639  14429  12102  -1637     -4    807       C  
ATOM   1720  CD2 PHE A 159     -16.465  50.528 -62.979  1.00121.88           C  
ANISOU 1720  CD2 PHE A 159    20282  14236  11793  -1431    -61    674       C  
ATOM   1721  CE1 PHE A 159     -15.049  52.047 -61.149  1.00123.57           C  
ANISOU 1721  CE1 PHE A 159    20425  14338  12189  -1566     -7    720       C  
ATOM   1722  CE2 PHE A 159     -16.462  50.182 -61.618  1.00122.83           C  
ANISOU 1722  CE2 PHE A 159    20264  14332  12073  -1363    -58    591       C  
ATOM   1723  CZ  PHE A 159     -15.772  50.955 -60.712  1.00120.80           C  
ANISOU 1723  CZ  PHE A 159    19972  14021  11906  -1425    -34    616       C  
ATOM   1724  N   ARG A 160     -14.726  49.003 -65.576  1.00112.81           N  
ANISOU 1724  N   ARG A 160    19166  13415  10283  -1585    218    660       N  
ATOM   1725  CA  ARG A 160     -14.545  47.645 -65.051  1.00110.44           C  
ANISOU 1725  CA  ARG A 160    18730  13194  10039  -1494    296    528       C  
ATOM   1726  C   ARG A 160     -13.218  46.966 -65.477  1.00115.23           C  
ANISOU 1726  C   ARG A 160    19268  13958  10556  -1540    479    497       C  
ATOM   1727  O   ARG A 160     -13.169  45.751 -65.707  1.00114.32           O  
ANISOU 1727  O   ARG A 160    19119  13918  10399  -1467    551    402       O  
ATOM   1728  CB  ARG A 160     -15.766  46.772 -65.360  1.00107.26           C  
ANISOU 1728  CB  ARG A 160    18366  12774   9614  -1394    211    456       C  
ATOM   1729  CG  ARG A 160     -17.043  47.300 -64.719  1.00107.09           C  
ANISOU 1729  CG  ARG A 160    18362  12629   9700  -1323     42    471       C  
ATOM   1730  CD  ARG A 160     -18.222  46.383 -64.923  1.00107.44           C  
ANISOU 1730  CD  ARG A 160    18416  12682   9726  -1239    -38    394       C  
ATOM   1731  NE  ARG A 160     -18.128  45.167 -64.119  1.00113.89           N  
ANISOU 1731  NE  ARG A 160    19116  13529  10630  -1170     26    268       N  
ATOM   1732  CZ  ARG A 160     -17.839  43.965 -64.606  1.00133.38           C  
ANISOU 1732  CZ  ARG A 160    21586  16075  13016  -1161    122    182       C  
ATOM   1733  NH1 ARG A 160     -17.628  43.801 -65.906  1.00122.78           N1+
ANISOU 1733  NH1 ARG A 160    20350  14801  11500  -1220    164    202       N1+
ATOM   1734  NH2 ARG A 160     -17.764  42.914 -63.798  1.00123.46           N  
ANISOU 1734  NH2 ARG A 160    20240  14824  11845  -1090    177     76       N  
ATOM   1735  N   THR A 161     -12.129  47.756 -65.476  1.00113.19           N  
ANISOU 1735  N   THR A 161    18982  13749  10275  -1659    557    573       N  
ATOM   1736  CA  THR A 161     -10.762  47.352 -65.780  1.00113.97           C  
ANISOU 1736  CA  THR A 161    18991  14019  10295  -1713    732    564       C  
ATOM   1737  C   THR A 161     -10.145  46.635 -64.536  1.00117.34           C  
ANISOU 1737  C   THR A 161    19224  14505  10856  -1631    807    476       C  
ATOM   1738  O   THR A 161     -10.469  47.021 -63.405  1.00116.86           O  
ANISOU 1738  O   THR A 161    19108  14349  10946  -1607    726    469       O  
ATOM   1739  CB  THR A 161      -9.997  48.577 -66.347  1.00120.27           C  
ANISOU 1739  CB  THR A 161    19851  14847  11000  -1895    767    694       C  
ATOM   1740  OG1 THR A 161      -9.548  48.271 -67.669  1.00124.07           O  
ANISOU 1740  OG1 THR A 161    20395  15454  11293  -1945    866    716       O  
ATOM   1741  CG2 THR A 161      -8.841  49.060 -65.471  1.00114.81           C  
ANISOU 1741  CG2 THR A 161    19017  14222  10383  -1986    843    718       C  
ATOM   1742  N   PRO A 162      -9.302  45.578 -64.707  1.00113.39           N  
ANISOU 1742  N   PRO A 162    18624  14158  10300  -1571    957    408       N  
ATOM   1743  CA  PRO A 162      -8.735  44.895 -63.524  1.00112.20           C  
ANISOU 1743  CA  PRO A 162    18293  14065  10271  -1476   1022    335       C  
ATOM   1744  C   PRO A 162      -7.867  45.787 -62.637  1.00116.22           C  
ANISOU 1744  C   PRO A 162    18677  14620  10862  -1576   1038    394       C  
ATOM   1745  O   PRO A 162      -7.958  45.663 -61.423  1.00115.60           O  
ANISOU 1745  O   PRO A 162    18496  14500  10926  -1514    999    352       O  
ATOM   1746  CB  PRO A 162      -7.970  43.705 -64.114  1.00114.79           C  
ANISOU 1746  CB  PRO A 162    18571  14552  10490  -1392   1187    269       C  
ATOM   1747  CG  PRO A 162      -7.719  44.063 -65.515  1.00120.81           C  
ANISOU 1747  CG  PRO A 162    19448  15383  11073  -1495   1236    331       C  
ATOM   1748  CD  PRO A 162      -8.839  44.951 -65.959  1.00116.16           C  
ANISOU 1748  CD  PRO A 162    19027  14635  10472  -1573   1076    395       C  
ATOM   1749  N   ALA A 163      -7.091  46.726 -63.225  1.00113.84           N  
ANISOU 1749  N   ALA A 163    18393  14396  10465  -1744   1085    492       N  
ATOM   1750  CA  ALA A 163      -6.259  47.687 -62.483  1.00113.64           C  
ANISOU 1750  CA  ALA A 163    18268  14414  10495  -1882   1096    556       C  
ATOM   1751  C   ALA A 163      -7.113  48.659 -61.646  1.00116.76           C  
ANISOU 1751  C   ALA A 163    18741  14601  11021  -1920    935    584       C  
ATOM   1752  O   ALA A 163      -6.652  49.110 -60.593  1.00116.83           O  
ANISOU 1752  O   ALA A 163    18647  14617  11127  -1973    925    588       O  
ATOM   1753  CB  ALA A 163      -5.353  48.459 -63.428  1.00116.21           C  
ANISOU 1753  CB  ALA A 163    18625  14858  10671  -2072   1180    657       C  
ATOM   1754  N   LYS A 164      -8.353  48.966 -62.100  1.00111.88           N  
ANISOU 1754  N   LYS A 164    18302  13807  10399  -1887    810    602       N  
ATOM   1755  CA  LYS A 164      -9.290  49.822 -61.363  1.00110.36           C  
ANISOU 1755  CA  LYS A 164    18195  13413  10324  -1885    656    624       C  
ATOM   1756  C   LYS A 164      -9.925  49.032 -60.210  1.00110.96           C  
ANISOU 1756  C   LYS A 164    18171  13438  10552  -1719    605    519       C  
ATOM   1757  O   LYS A 164     -10.092  49.593 -59.122  1.00109.90           O  
ANISOU 1757  O   LYS A 164    18003  13215  10539  -1726    537    516       O  
ATOM   1758  CB  LYS A 164     -10.361  50.429 -62.282  1.00113.47           C  
ANISOU 1758  CB  LYS A 164    18801  13664  10649  -1893    544    689       C  
ATOM   1759  CG  LYS A 164      -9.911  51.710 -62.978  1.00133.14           C  
ANISOU 1759  CG  LYS A 164    21426  16121  13039  -2080    545    818       C  
ATOM   1760  CD  LYS A 164     -10.978  52.256 -63.928  1.00146.04           C  
ANISOU 1760  CD  LYS A 164    23273  17622  14593  -2066    432    890       C  
ATOM   1761  CE  LYS A 164     -10.607  53.573 -64.565  1.00160.58           C  
ANISOU 1761  CE  LYS A 164    25276  19402  16337  -2245    425   1027       C  
ATOM   1762  NZ  LYS A 164     -11.799  54.278 -65.113  1.00169.35           N1+
ANISOU 1762  NZ  LYS A 164    26594  20338  17412  -2198    283   1101       N1+
ATOM   1763  N   ALA A 165     -10.247  47.727 -60.436  1.00105.54           N  
ANISOU 1763  N   ALA A 165    17444  12806   9850  -1577    643    432       N  
ATOM   1764  CA  ALA A 165     -10.813  46.844 -59.405  1.00103.44           C  
ANISOU 1764  CA  ALA A 165    17088  12502   9713  -1425    608    332       C  
ATOM   1765  C   ALA A 165      -9.778  46.571 -58.320  1.00107.47           C  
ANISOU 1765  C   ALA A 165    17412  13118  10303  -1417    693    299       C  
ATOM   1766  O   ALA A 165     -10.115  46.628 -57.133  1.00105.65           O  
ANISOU 1766  O   ALA A 165    17118  12818  10206  -1364    630    262       O  
ATOM   1767  CB  ALA A 165     -11.294  45.539 -60.012  1.00103.70           C  
ANISOU 1767  CB  ALA A 165    17148  12566   9688  -1305    641    253       C  
ATOM   1768  N   LYS A 166      -8.506  46.336 -58.733  1.00105.95           N  
ANISOU 1768  N   LYS A 166    17129  13105  10021  -1471    834    317       N  
ATOM   1769  CA  LYS A 166      -7.348  46.118 -57.854  1.00106.22           C  
ANISOU 1769  CA  LYS A 166    16968  13289  10101  -1473    927    300       C  
ATOM   1770  C   LYS A 166      -7.237  47.280 -56.835  1.00109.93           C  
ANISOU 1770  C   LYS A 166    17407  13692  10671  -1589    847    344       C  
ATOM   1771  O   LYS A 166      -7.226  47.030 -55.630  1.00108.42           O  
ANISOU 1771  O   LYS A 166    17104  13496  10595  -1522    824    295       O  
ATOM   1772  CB  LYS A 166      -6.059  45.979 -58.697  1.00110.40           C  
ANISOU 1772  CB  LYS A 166    17424  14032  10490  -1545   1081    339       C  
ATOM   1773  CG  LYS A 166      -4.810  45.607 -57.902  1.00127.14           C  
ANISOU 1773  CG  LYS A 166    19319  16353  12636  -1527   1189    323       C  
ATOM   1774  CD  LYS A 166      -3.540  45.747 -58.736  1.00140.03           C  
ANISOU 1774  CD  LYS A 166    20872  18210  14124  -1630   1332    380       C  
ATOM   1775  CE  LYS A 166      -2.289  45.484 -57.930  1.00149.45           C  
ANISOU 1775  CE  LYS A 166    21821  19628  15335  -1621   1430    376       C  
ATOM   1776  NZ  LYS A 166      -1.057  45.797 -58.704  1.00158.32           N1+
ANISOU 1776  NZ  LYS A 166    22853  20988  16315  -1751   1562    443       N1+
ATOM   1777  N   LEU A 167      -7.247  48.539 -57.338  1.00107.45           N  
ANISOU 1777  N   LEU A 167    17214  13307  10306  -1758    799    433       N  
ATOM   1778  CA  LEU A 167      -7.169  49.794 -56.583  1.00107.10           C  
ANISOU 1778  CA  LEU A 167    17196  13169  10328  -1895    724    483       C  
ATOM   1779  C   LEU A 167      -8.297  49.952 -55.552  1.00109.18           C  
ANISOU 1779  C   LEU A 167    17505  13243  10736  -1794    590    435       C  
ATOM   1780  O   LEU A 167      -8.010  50.280 -54.397  1.00107.98           O  
ANISOU 1780  O   LEU A 167    17266  13085  10676  -1824    568    415       O  
ATOM   1781  CB  LEU A 167      -7.135  50.986 -57.556  1.00108.54           C  
ANISOU 1781  CB  LEU A 167    17553  13280  10406  -2074    700    590       C  
ATOM   1782  CG  LEU A 167      -7.235  52.383 -56.958  1.00113.85           C  
ANISOU 1782  CG  LEU A 167    18327  13801  11131  -2219    611    647       C  
ATOM   1783  CD1 LEU A 167      -5.998  52.731 -56.130  1.00115.01           C  
ANISOU 1783  CD1 LEU A 167    18317  14084  11296  -2366    677    653       C  
ATOM   1784  CD2 LEU A 167      -7.465  53.408 -58.036  1.00117.60           C  
ANISOU 1784  CD2 LEU A 167    19018  14166  11499  -2350    576    753       C  
ATOM   1785  N   ILE A 168      -9.569  49.724 -55.969  1.00104.67           N  
ANISOU 1785  N   ILE A 168    17062  12533  10176  -1680    503    417       N  
ATOM   1786  CA  ILE A 168     -10.749  49.809 -55.086  1.00102.05           C  
ANISOU 1786  CA  ILE A 168    16768  12038   9970  -1569    379    371       C  
ATOM   1787  C   ILE A 168     -10.572  48.911 -53.871  1.00101.50           C  
ANISOU 1787  C   ILE A 168    16524  12034  10008  -1460    407    281       C  
ATOM   1788  O   ILE A 168     -10.700  49.406 -52.753  1.00100.85           O  
ANISOU 1788  O   ILE A 168    16408  11883  10027  -1467    350    265       O  
ATOM   1789  CB  ILE A 168     -12.103  49.560 -55.826  1.00104.28           C  
ANISOU 1789  CB  ILE A 168    17185  12208  10228  -1463    290    366       C  
ATOM   1790  CG1 ILE A 168     -12.380  50.679 -56.858  1.00105.11           C  
ANISOU 1790  CG1 ILE A 168    17480  12220  10238  -1566    236    469       C  
ATOM   1791  CG2 ILE A 168     -13.281  49.393 -54.820  1.00102.56           C  
ANISOU 1791  CG2 ILE A 168    16957  11870  10142  -1327    180    304       C  
ATOM   1792  CD1 ILE A 168     -13.370  50.350 -57.900  1.00108.79           C  
ANISOU 1792  CD1 ILE A 168    18059  12648  10628  -1491    180    479       C  
ATOM   1793  N   ASN A 169     -10.212  47.627 -54.089  1.00 96.09           N  
ANISOU 1793  N   ASN A 169    15738  11482   9292  -1363    500    226       N  
ATOM   1794  CA  ASN A 169     -10.006  46.642 -53.014  1.00 94.84           C  
ANISOU 1794  CA  ASN A 169    15424  11391   9222  -1243    538    146       C  
ATOM   1795  C   ASN A 169      -8.871  47.022 -52.066  1.00 99.81           C  
ANISOU 1795  C   ASN A 169    15903  12131   9889  -1322    586    159       C  
ATOM   1796  O   ASN A 169      -9.069  46.911 -50.861  1.00 97.52           O  
ANISOU 1796  O   ASN A 169    15536  11810   9706  -1264    544    114       O  
ATOM   1797  CB  ASN A 169      -9.844  45.224 -53.558  1.00 92.71           C  
ANISOU 1797  CB  ASN A 169    15112  11219   8893  -1120    633     92       C  
ATOM   1798  CG  ASN A 169     -11.096  44.740 -54.252  1.00104.26           C  
ANISOU 1798  CG  ASN A 169    16712  12569  10333  -1042    569     61       C  
ATOM   1799  OD1 ASN A 169     -11.167  44.649 -55.485  1.00 94.24           O  
ANISOU 1799  OD1 ASN A 169    15540  11317   8949  -1071    596     84       O  
ATOM   1800  ND2 ASN A 169     -12.134  44.466 -53.479  1.00 88.66           N  
ANISOU 1800  ND2 ASN A 169    14745  10484   8459   -952    478     10       N  
ATOM   1801  N   ILE A 170      -7.725  47.543 -52.596  1.00 99.00           N  
ANISOU 1801  N   ILE A 170    15762  12159   9695  -1468    667    222       N  
ATOM   1802  CA  ILE A 170      -6.588  48.013 -51.784  1.00 99.53           C  
ANISOU 1802  CA  ILE A 170    15681  12357   9779  -1579    709    243       C  
ATOM   1803  C   ILE A 170      -7.082  49.144 -50.900  1.00104.89           C  
ANISOU 1803  C   ILE A 170    16432  12875  10546  -1667    592    254       C  
ATOM   1804  O   ILE A 170      -6.839  49.098 -49.698  1.00105.53           O  
ANISOU 1804  O   ILE A 170    16399  12989  10710  -1650    576    216       O  
ATOM   1805  CB  ILE A 170      -5.323  48.409 -52.615  1.00104.24           C  
ANISOU 1805  CB  ILE A 170    16225  13135  10246  -1741    817    314       C  
ATOM   1806  CG1 ILE A 170      -4.763  47.194 -53.388  1.00105.44           C  
ANISOU 1806  CG1 ILE A 170    16288  13466  10310  -1624    948    292       C  
ATOM   1807  CG2 ILE A 170      -4.221  49.039 -51.730  1.00104.35           C  
ANISOU 1807  CG2 ILE A 170    16088  13284  10274  -1890    841    339       C  
ATOM   1808  CD1 ILE A 170      -3.977  47.534 -54.671  1.00115.00           C  
ANISOU 1808  CD1 ILE A 170    17522  14805  11367  -1756   1044    364       C  
ATOM   1809  N   CYS A 171      -7.842  50.109 -51.471  1.00101.84           N  
ANISOU 1809  N   CYS A 171    16244  12307  10142  -1741    508    302       N  
ATOM   1810  CA  CYS A 171      -8.405  51.238 -50.716  1.00101.39           C  
ANISOU 1810  CA  CYS A 171    16295  12069  10161  -1807    396    313       C  
ATOM   1811  C   CYS A 171      -9.280  50.785 -49.564  1.00101.89           C  
ANISOU 1811  C   CYS A 171    16317  12043  10353  -1647    323    232       C  
ATOM   1812  O   CYS A 171      -9.171  51.359 -48.489  1.00100.93           O  
ANISOU 1812  O   CYS A 171    16170  11878  10300  -1696    280    214       O  
ATOM   1813  CB  CYS A 171      -9.127  52.229 -51.621  1.00102.57           C  
ANISOU 1813  CB  CYS A 171    16675  12037  10258  -1871    324    382       C  
ATOM   1814  SG  CYS A 171      -8.032  53.109 -52.759  1.00108.81           S  
ANISOU 1814  SG  CYS A 171    17540  12903  10899  -2116    399    492       S  
ATOM   1815  N   ILE A 172     -10.100  49.730 -49.772  1.00 96.14           N  
ANISOU 1815  N   ILE A 172    15581  11300   9649  -1468    313    182       N  
ATOM   1816  CA  ILE A 172     -10.957  49.149 -48.729  1.00 94.17           C  
ANISOU 1816  CA  ILE A 172    15282  10985   9513  -1314    254    105       C  
ATOM   1817  C   ILE A 172     -10.081  48.614 -47.580  1.00 99.23           C  
ANISOU 1817  C   ILE A 172    15732  11766  10205  -1298    312     60       C  
ATOM   1818  O   ILE A 172     -10.282  49.018 -46.436  1.00 99.25           O  
ANISOU 1818  O   ILE A 172    15709  11712  10292  -1297    255     31       O  
ATOM   1819  CB  ILE A 172     -11.925  48.041 -49.272  1.00 95.09           C  
ANISOU 1819  CB  ILE A 172    15427  11076   9625  -1154    244     62       C  
ATOM   1820  CG1 ILE A 172     -12.862  48.588 -50.368  1.00 94.10           C  
ANISOU 1820  CG1 ILE A 172    15481  10827   9445  -1164    172    108       C  
ATOM   1821  CG2 ILE A 172     -12.715  47.368 -48.104  1.00 93.18           C  
ANISOU 1821  CG2 ILE A 172    15118  10791   9498  -1011    196    -17       C  
ATOM   1822  CD1 ILE A 172     -13.446  47.586 -51.196  1.00 91.75           C  
ANISOU 1822  CD1 ILE A 172    15210  10554   9097  -1069    187     81       C  
ATOM   1823  N   TRP A 173      -9.109  47.729 -47.902  1.00 96.00           N  
ANISOU 1823  N   TRP A 173    15194  11544   9738  -1277    425     57       N  
ATOM   1824  CA  TRP A 173      -8.192  47.098 -46.957  1.00 95.59           C  
ANISOU 1824  CA  TRP A 173    14948  11657   9715  -1240    491     26       C  
ATOM   1825  C   TRP A 173      -7.273  48.084 -46.240  1.00 99.87           C  
ANISOU 1825  C   TRP A 173    15416  12271  10260  -1408    486     57       C  
ATOM   1826  O   TRP A 173      -6.927  47.845 -45.086  1.00 98.30           O  
ANISOU 1826  O   TRP A 173    15086  12144  10118  -1376    484     22       O  
ATOM   1827  CB  TRP A 173      -7.403  45.980 -47.633  1.00 94.90           C  
ANISOU 1827  CB  TRP A 173    14760  11748   9548  -1163    617     24       C  
ATOM   1828  CG  TRP A 173      -8.232  44.755 -47.867  1.00 95.07           C  
ANISOU 1828  CG  TRP A 173    14825  11709   9588   -978    625    -33       C  
ATOM   1829  CD1 TRP A 173      -9.079  44.527 -48.911  1.00 98.06           C  
ANISOU 1829  CD1 TRP A 173    15349  11985   9923   -943    605    -36       C  
ATOM   1830  CD2 TRP A 173      -8.312  43.595 -47.024  1.00 94.10           C  
ANISOU 1830  CD2 TRP A 173    14608  11623   9524   -814    652    -94       C  
ATOM   1831  NE1 TRP A 173      -9.655  43.284 -48.794  1.00 96.97           N  
ANISOU 1831  NE1 TRP A 173    15215  11821   9810   -782    621   -101       N  
ATOM   1832  CE2 TRP A 173      -9.225  42.701 -47.627  1.00 97.90           C  
ANISOU 1832  CE2 TRP A 173    15194  12010   9993   -698    650   -136       C  
ATOM   1833  CE3 TRP A 173      -7.700  43.220 -45.815  1.00 94.85           C  
ANISOU 1833  CE3 TRP A 173    14544  11820   9673   -758    675   -115       C  
ATOM   1834  CZ2 TRP A 173      -9.534  41.452 -47.065  1.00 96.21           C  
ANISOU 1834  CZ2 TRP A 173    14945  11788   9820   -536    676   -197       C  
ATOM   1835  CZ3 TRP A 173      -8.016  41.992 -45.255  1.00 95.29           C  
ANISOU 1835  CZ3 TRP A 173    14565  11870   9772   -583    698   -170       C  
ATOM   1836  CH2 TRP A 173      -8.924  41.125 -45.875  1.00 95.46           C  
ANISOU 1836  CH2 TRP A 173    14706  11783   9783   -477    701   -211       C  
ATOM   1837  N   VAL A 174      -6.918  49.206 -46.888  1.00 98.28           N  
ANISOU 1837  N   VAL A 174    15307  12043   9993  -1594    480    123       N  
ATOM   1838  CA  VAL A 174      -6.086  50.232 -46.251  1.00 99.18           C  
ANISOU 1838  CA  VAL A 174    15377  12208  10098  -1789    470    152       C  
ATOM   1839  C   VAL A 174      -6.979  51.161 -45.388  1.00102.54           C  
ANISOU 1839  C   VAL A 174    15936  12412  10611  -1816    348    128       C  
ATOM   1840  O   VAL A 174      -6.590  51.490 -44.273  1.00101.73           O  
ANISOU 1840  O   VAL A 174    15756  12346  10552  -1877    325    102       O  
ATOM   1841  CB  VAL A 174      -5.124  50.970 -47.232  1.00104.55           C  
ANISOU 1841  CB  VAL A 174    16080  12986  10658  -2000    533    234       C  
ATOM   1842  CG1 VAL A 174      -5.870  51.846 -48.221  1.00104.91           C  
ANISOU 1842  CG1 VAL A 174    16368  12829  10665  -2072    478    286       C  
ATOM   1843  CG2 VAL A 174      -4.066  51.778 -46.488  1.00105.59           C  
ANISOU 1843  CG2 VAL A 174    16117  13231  10771  -2209    541    256       C  
ATOM   1844  N   LEU A 175      -8.198  51.503 -45.877  1.00 99.08           N  
ANISOU 1844  N   LEU A 175    15689  11760  10196  -1750    272    132       N  
ATOM   1845  CA  LEU A 175      -9.205  52.328 -45.198  1.00 98.86           C  
ANISOU 1845  CA  LEU A 175    15805  11513  10246  -1732    160    110       C  
ATOM   1846  C   LEU A 175      -9.663  51.681 -43.901  1.00100.39           C  
ANISOU 1846  C   LEU A 175    15891  11709  10543  -1587    127     28       C  
ATOM   1847  O   LEU A 175      -9.753  52.362 -42.884  1.00100.38           O  
ANISOU 1847  O   LEU A 175    15912  11633  10594  -1635     73      0       O  
ATOM   1848  CB  LEU A 175     -10.420  52.495 -46.120  1.00 99.60           C  
ANISOU 1848  CB  LEU A 175    16081  11433  10332  -1642     99    133       C  
ATOM   1849  CG  LEU A 175     -11.494  53.502 -45.723  1.00106.38           C  
ANISOU 1849  CG  LEU A 175    17117  12057  11245  -1615    -13    131       C  
ATOM   1850  CD1 LEU A 175     -11.232  54.870 -46.380  1.00108.88           C  
ANISOU 1850  CD1 LEU A 175    17626  12252  11490  -1791    -33    212       C  
ATOM   1851  CD2 LEU A 175     -12.870  52.997 -46.144  1.00109.39           C  
ANISOU 1851  CD2 LEU A 175    17562  12343  11656  -1425    -72    113       C  
ATOM   1852  N   ALA A 176      -9.942  50.364 -43.939  1.00 95.14           N  
ANISOU 1852  N   ALA A 176    15120  11126   9901  -1417    163    -12       N  
ATOM   1853  CA  ALA A 176     -10.430  49.574 -42.811  1.00 93.15           C  
ANISOU 1853  CA  ALA A 176    14770  10882   9739  -1267    140    -85       C  
ATOM   1854  C   ALA A 176      -9.470  49.492 -41.589  1.00 97.23           C  
ANISOU 1854  C   ALA A 176    15122  11539  10280  -1316    168   -111       C  
ATOM   1855  O   ALA A 176      -9.900  49.035 -40.523  1.00 95.70           O  
ANISOU 1855  O   ALA A 176    14866  11335  10161  -1209    138   -167       O  
ATOM   1856  CB  ALA A 176     -10.822  48.192 -43.282  1.00 92.78           C  
ANISOU 1856  CB  ALA A 176    14673  10889   9691  -1102    184   -111       C  
ATOM   1857  N   SER A 177      -8.210  49.990 -41.724  1.00 94.78           N  
ANISOU 1857  N   SER A 177    14744  11365   9903  -1486    220    -67       N  
ATOM   1858  CA  SER A 177      -7.203  50.023 -40.649  1.00 94.89           C  
ANISOU 1858  CA  SER A 177    14594  11541   9921  -1561    242    -83       C  
ATOM   1859  C   SER A 177      -7.515  51.103 -39.568  1.00 99.33           C  
ANISOU 1859  C   SER A 177    15235  11973  10533  -1656    153   -114       C  
ATOM   1860  O   SER A 177      -6.914  51.101 -38.486  1.00 97.85           O  
ANISOU 1860  O   SER A 177    14923  11897  10360  -1699    151   -141       O  
ATOM   1861  CB  SER A 177      -5.811  50.228 -41.232  1.00 99.39           C  
ANISOU 1861  CB  SER A 177    15061  12314  10390  -1723    325    -24       C  
ATOM   1862  OG  SER A 177      -5.723  51.518 -41.809  1.00108.73           O  
ANISOU 1862  OG  SER A 177    16398  13391  11524  -1926    296     25       O  
ATOM   1863  N   GLY A 178      -8.460  51.999 -39.876  1.00 96.44           N  
ANISOU 1863  N   GLY A 178    15081  11376  10188  -1679     81   -109       N  
ATOM   1864  CA  GLY A 178      -8.951  53.001 -38.941  1.00 96.32           C  
ANISOU 1864  CA  GLY A 178    15178  11198  10219  -1734     -2   -145       C  
ATOM   1865  C   GLY A 178      -9.867  52.358 -37.909  1.00 99.18           C  
ANISOU 1865  C   GLY A 178    15496  11513  10674  -1542    -46   -218       C  
ATOM   1866  O   GLY A 178     -10.294  53.009 -36.955  1.00 98.39           O  
ANISOU 1866  O   GLY A 178    15465  11301  10618  -1554   -108   -262       O  
ATOM   1867  N   VAL A 179     -10.204  51.069 -38.120  1.00 95.13           N  
ANISOU 1867  N   VAL A 179    14882  11077  10185  -1367    -10   -232       N  
ATOM   1868  CA  VAL A 179     -11.039  50.246 -37.240  1.00 93.26           C  
ANISOU 1868  CA  VAL A 179    14587  10819  10027  -1186    -37   -294       C  
ATOM   1869  C   VAL A 179     -10.155  49.154 -36.588  1.00 97.34           C  
ANISOU 1869  C   VAL A 179    14892  11552  10540  -1137     28   -309       C  
ATOM   1870  O   VAL A 179     -10.146  49.036 -35.366  1.00 97.43           O  
ANISOU 1870  O   VAL A 179    14829  11597  10592  -1106      5   -352       O  
ATOM   1871  CB  VAL A 179     -12.274  49.666 -37.977  1.00 95.17           C  
ANISOU 1871  CB  VAL A 179    14911  10953  10295  -1029    -58   -299       C  
ATOM   1872  CG1 VAL A 179     -13.192  48.923 -37.011  1.00 93.03           C  
ANISOU 1872  CG1 VAL A 179    14590  10657  10102   -868    -89   -362       C  
ATOM   1873  CG2 VAL A 179     -13.042  50.773 -38.701  1.00 95.53           C  
ANISOU 1873  CG2 VAL A 179    15157  10810  10330  -1071   -121   -269       C  
ATOM   1874  N   GLY A 180      -9.388  48.431 -37.407  1.00 93.14           N  
ANISOU 1874  N   GLY A 180    14271  11166   9951  -1129    110   -270       N  
ATOM   1875  CA  GLY A 180      -8.477  47.372 -36.981  1.00 92.55           C  
ANISOU 1875  CA  GLY A 180    14003  11304   9859  -1062    183   -271       C  
ATOM   1876  C   GLY A 180      -7.424  47.791 -35.975  1.00 96.22           C  
ANISOU 1876  C   GLY A 180    14333  11921  10305  -1176    184   -270       C  
ATOM   1877  O   GLY A 180      -7.269  47.129 -34.950  1.00 95.65           O  
ANISOU 1877  O   GLY A 180    14139  11941  10261  -1084    187   -300       O  
ATOM   1878  N   VAL A 181      -6.695  48.884 -36.256  1.00 93.70           N  
ANISOU 1878  N   VAL A 181    14038  11633   9929  -1386    179   -236       N  
ATOM   1879  CA  VAL A 181      -5.646  49.439 -35.381  1.00 94.53           C  
ANISOU 1879  CA  VAL A 181    14025  11893  10000  -1543    173   -234       C  
ATOM   1880  C   VAL A 181      -6.240  49.964 -34.034  1.00 98.32           C  
ANISOU 1880  C   VAL A 181    14556  12259  10541  -1552     86   -296       C  
ATOM   1881  O   VAL A 181      -5.796  49.473 -32.992  1.00 98.62           O  
ANISOU 1881  O   VAL A 181    14442  12443  10586  -1510     88   -320       O  
ATOM   1882  CB  VAL A 181      -4.739  50.484 -36.093  1.00 99.62           C  
ANISOU 1882  CB  VAL A 181    14697  12596  10558  -1792    194   -179       C  
ATOM   1883  CG1 VAL A 181      -3.783  51.160 -35.110  1.00100.54           C  
ANISOU 1883  CG1 VAL A 181    14708  12855  10636  -1983    171   -186       C  
ATOM   1884  CG2 VAL A 181      -3.973  49.855 -37.259  1.00 99.75           C  
ANISOU 1884  CG2 VAL A 181    14615  12784  10502  -1777    294   -119       C  
ATOM   1885  N   PRO A 182      -7.235  50.899 -33.989  1.00 93.24           N  
ANISOU 1885  N   PRO A 182    14120  11368   9938  -1587     13   -325       N  
ATOM   1886  CA  PRO A 182      -7.784  51.316 -32.678  1.00 92.24           C  
ANISOU 1886  CA  PRO A 182    14035  11147   9863  -1575    -58   -391       C  
ATOM   1887  C   PRO A 182      -8.296  50.156 -31.812  1.00 95.36           C  
ANISOU 1887  C   PRO A 182    14321  11593  10319  -1365    -58   -434       C  
ATOM   1888  O   PRO A 182      -8.099  50.193 -30.596  1.00 95.62           O  
ANISOU 1888  O   PRO A 182    14280  11689  10361  -1378    -86   -473       O  
ATOM   1889  CB  PRO A 182      -8.910  52.280 -33.055  1.00 93.64           C  
ANISOU 1889  CB  PRO A 182    14458  11048  10074  -1582   -120   -405       C  
ATOM   1890  CG  PRO A 182      -8.531  52.782 -34.388  1.00 98.98           C  
ANISOU 1890  CG  PRO A 182    15220  11698  10691  -1701    -90   -338       C  
ATOM   1891  CD  PRO A 182      -7.897  51.628 -35.089  1.00 94.45           C  
ANISOU 1891  CD  PRO A 182    14479  11323  10086  -1629     -8   -297       C  
ATOM   1892  N   ILE A 183      -8.915  49.108 -32.437  1.00 89.81           N  
ANISOU 1892  N   ILE A 183    13609  10867   9647  -1183    -24   -424       N  
ATOM   1893  CA  ILE A 183      -9.397  47.909 -31.734  1.00 87.53           C  
ANISOU 1893  CA  ILE A 183    13231  10619   9408   -990    -14   -456       C  
ATOM   1894  C   ILE A 183      -8.207  47.126 -31.162  1.00 93.82           C  
ANISOU 1894  C   ILE A 183    13818  11665  10165   -973     41   -436       C  
ATOM   1895  O   ILE A 183      -8.278  46.663 -30.023  1.00 93.10           O  
ANISOU 1895  O   ILE A 183    13646  11628  10099   -895     25   -468       O  
ATOM   1896  CB  ILE A 183     -10.366  47.045 -32.591  1.00 88.29           C  
ANISOU 1896  CB  ILE A 183    13393  10618   9536   -829      7   -452       C  
ATOM   1897  CG1 ILE A 183     -11.682  47.805 -32.943  1.00 87.68           C  
ANISOU 1897  CG1 ILE A 183    13504  10312   9501   -819    -62   -474       C  
ATOM   1898  CG2 ILE A 183     -10.660  45.668 -31.954  1.00 86.53           C  
ANISOU 1898  CG2 ILE A 183    13073  10458   9346   -649     36   -475       C  
ATOM   1899  CD1 ILE A 183     -12.614  48.353 -31.744  1.00 93.91           C  
ANISOU 1899  CD1 ILE A 183    14354  10979  10349   -784   -137   -537       C  
ATOM   1900  N   MET A 184      -7.099  47.045 -31.926  1.00 92.36           N  
ANISOU 1900  N   MET A 184    13544  11639   9911  -1049    104   -382       N  
ATOM   1901  CA  MET A 184      -5.842  46.420 -31.508  1.00 93.38           C  
ANISOU 1901  CA  MET A 184    13459  12033   9987  -1040    159   -351       C  
ATOM   1902  C   MET A 184      -5.227  47.183 -30.311  1.00 98.66           C  
ANISOU 1902  C   MET A 184    14049  12803  10634  -1186    107   -371       C  
ATOM   1903  O   MET A 184      -4.660  46.545 -29.420  1.00100.20           O  
ANISOU 1903  O   MET A 184    14081  13176  10814  -1119    118   -370       O  
ATOM   1904  CB  MET A 184      -4.855  46.418 -32.672  1.00 97.03           C  
ANISOU 1904  CB  MET A 184    13857  12637  10371  -1115    234   -289       C  
ATOM   1905  CG  MET A 184      -3.750  45.413 -32.533  1.00101.72           C  
ANISOU 1905  CG  MET A 184    14233  13501  10913  -1021    313   -252       C  
ATOM   1906  SD  MET A 184      -2.594  45.526 -33.918  1.00107.68           S  
ANISOU 1906  SD  MET A 184    14910  14437  11568  -1120    407   -181       S  
ATOM   1907  CE  MET A 184      -3.550  44.744 -35.236  1.00102.93           C  
ANISOU 1907  CE  MET A 184    14469  13648  10991   -952    457   -184       C  
ATOM   1908  N   VAL A 185      -5.342  48.528 -30.282  1.00 93.59           N  
ANISOU 1908  N   VAL A 185    13532  12045   9983  -1383     49   -389       N  
ATOM   1909  CA  VAL A 185      -4.807  49.337 -29.178  1.00 93.92           C  
ANISOU 1909  CA  VAL A 185    13531  12160   9996  -1548     -5   -418       C  
ATOM   1910  C   VAL A 185      -5.631  49.127 -27.871  1.00 95.41           C  
ANISOU 1910  C   VAL A 185    13745  12261  10245  -1435    -63   -485       C  
ATOM   1911  O   VAL A 185      -5.049  48.879 -26.811  1.00 94.36           O  
ANISOU 1911  O   VAL A 185    13470  12297  10086  -1441    -76   -496       O  
ATOM   1912  CB  VAL A 185      -4.671  50.831 -29.572  1.00 99.15           C  
ANISOU 1912  CB  VAL A 185    14349  12702  10622  -1800    -43   -419       C  
ATOM   1913  CG1 VAL A 185      -3.994  51.641 -28.472  1.00100.18           C  
ANISOU 1913  CG1 VAL A 185    14434  12926  10705  -1997    -93   -451       C  
ATOM   1914  CG2 VAL A 185      -3.903  50.987 -30.879  1.00100.06           C  
ANISOU 1914  CG2 VAL A 185    14440  12905  10672  -1910     20   -348       C  
ATOM   1915  N   MET A 186      -6.982  49.192 -27.977  1.00 90.62           N  
ANISOU 1915  N   MET A 186    13311  11409   9712  -1325    -95   -523       N  
ATOM   1916  CA  MET A 186      -7.956  49.031 -26.887  1.00 88.57           C  
ANISOU 1916  CA  MET A 186    13098  11042   9511  -1210   -144   -587       C  
ATOM   1917  C   MET A 186      -8.174  47.596 -26.399  1.00 91.42           C  
ANISOU 1917  C   MET A 186    13335  11498   9903   -997   -111   -584       C  
ATOM   1918  O   MET A 186      -8.565  47.423 -25.247  1.00 91.27           O  
ANISOU 1918  O   MET A 186    13297  11476   9906   -937   -145   -627       O  
ATOM   1919  CB  MET A 186      -9.300  49.652 -27.265  1.00 90.14           C  
ANISOU 1919  CB  MET A 186    13513  10969   9769  -1171   -186   -622       C  
ATOM   1920  CG  MET A 186      -9.221  51.152 -27.515  1.00 95.09           C  
ANISOU 1920  CG  MET A 186    14302  11461  10368  -1365   -228   -633       C  
ATOM   1921  SD  MET A 186     -10.855  51.866 -27.811  1.00 98.97           S  
ANISOU 1921  SD  MET A 186    15040  11640  10924  -1274   -281   -672       S  
ATOM   1922  CE  MET A 186     -11.111  51.440 -29.538  1.00 94.91           C  
ANISOU 1922  CE  MET A 186    14568  11081  10412  -1214   -238   -601       C  
ATOM   1923  N   ALA A 187      -7.928  46.568 -27.250  1.00 86.88           N  
ANISOU 1923  N   ALA A 187    12689  10999   9322   -883    -42   -534       N  
ATOM   1924  CA  ALA A 187      -8.096  45.161 -26.876  1.00 84.62           C  
ANISOU 1924  CA  ALA A 187    12312  10784   9057   -681     -2   -525       C  
ATOM   1925  C   ALA A 187      -7.138  44.766 -25.737  1.00 88.24           C  
ANISOU 1925  C   ALA A 187    12590  11466   9472   -672      1   -514       C  
ATOM   1926  O   ALA A 187      -5.927  44.870 -25.896  1.00 88.45           O  
ANISOU 1926  O   ALA A 187    12486  11690   9433   -757     29   -471       O  
ATOM   1927  CB  ALA A 187      -7.891  44.271 -28.085  1.00 84.98           C  
ANISOU 1927  CB  ALA A 187    12338  10863   9088   -583     75   -476       C  
ATOM   1928  N   VAL A 188      -7.684  44.381 -24.568  1.00 84.46           N  
ANISOU 1928  N   VAL A 188    12101  10967   9022   -581    -31   -549       N  
ATOM   1929  CA  VAL A 188      -6.898  43.998 -23.376  1.00 84.78           C  
ANISOU 1929  CA  VAL A 188    11982  11212   9019   -560    -39   -539       C  
ATOM   1930  C   VAL A 188      -7.507  42.815 -22.637  1.00 89.27           C  
ANISOU 1930  C   VAL A 188    12535  11764   9620   -359    -25   -542       C  
ATOM   1931  O   VAL A 188      -8.722  42.631 -22.679  1.00 87.77           O  
ANISOU 1931  O   VAL A 188    12474  11384   9492   -286    -36   -578       O  
ATOM   1932  CB  VAL A 188      -6.683  45.175 -22.354  1.00 88.40           C  
ANISOU 1932  CB  VAL A 188    12442  11696   9449   -739   -115   -587       C  
ATOM   1933  CG1 VAL A 188      -5.767  46.269 -22.901  1.00 89.20           C  
ANISOU 1933  CG1 VAL A 188    12529  11868   9494   -965   -126   -573       C  
ATOM   1934  CG2 VAL A 188      -8.003  45.737 -21.810  1.00 86.61           C  
ANISOU 1934  CG2 VAL A 188    12385  11241   9283   -734   -171   -662       C  
ATOM   1935  N   THR A 189      -6.676  42.078 -21.871  1.00 88.31           N  
ANISOU 1935  N   THR A 189    12255  11849   9450   -281     -6   -503       N  
ATOM   1936  CA  THR A 189      -7.158  41.011 -20.979  1.00 87.95           C  
ANISOU 1936  CA  THR A 189    12197  11798   9421   -105      2   -500       C  
ATOM   1937  C   THR A 189      -7.171  41.556 -19.554  1.00 91.86           C  
ANISOU 1937  C   THR A 189    12655  12354   9895   -176    -68   -539       C  
ATOM   1938  O   THR A 189      -6.167  42.119 -19.098  1.00 92.69           O  
ANISOU 1938  O   THR A 189    12640  12643   9935   -293    -96   -529       O  
ATOM   1939  CB  THR A 189      -6.385  39.693 -21.100  1.00 94.74           C  
ANISOU 1939  CB  THR A 189    12939  12817  10241     71     75   -426       C  
ATOM   1940  OG1 THR A 189      -4.994  39.921 -20.856  1.00 99.27           O  
ANISOU 1940  OG1 THR A 189    13328  13654  10736     10     75   -382       O  
ATOM   1941  CG2 THR A 189      -6.609  39.012 -22.422  1.00 89.89           C  
ANISOU 1941  CG2 THR A 189    12398  12105   9650    167    149   -402       C  
ATOM   1942  N   ARG A 190      -8.324  41.442 -18.880  1.00 87.21           N  
ANISOU 1942  N   ARG A 190    12169  11614   9353   -120    -95   -588       N  
ATOM   1943  CA  ARG A 190      -8.515  41.936 -17.516  1.00 87.44           C  
ANISOU 1943  CA  ARG A 190    12187  11673   9361   -176   -157   -635       C  
ATOM   1944  C   ARG A 190      -9.031  40.816 -16.591  1.00 91.98           C  
ANISOU 1944  C   ARG A 190    12750  12256   9941     -7   -142   -622       C  
ATOM   1945  O   ARG A 190      -9.819  39.984 -17.042  1.00 89.97           O  
ANISOU 1945  O   ARG A 190    12573  11876   9736    118   -100   -610       O  
ATOM   1946  CB  ARG A 190      -9.473  43.148 -17.504  1.00 86.08           C  
ANISOU 1946  CB  ARG A 190    12170  11304   9231   -296   -209   -719       C  
ATOM   1947  CG  ARG A 190      -8.938  44.374 -18.225  1.00 92.45           C  
ANISOU 1947  CG  ARG A 190    13012  12094  10021   -484   -232   -734       C  
ATOM   1948  CD  ARG A 190      -8.581  45.485 -17.273  1.00102.86           C  
ANISOU 1948  CD  ARG A 190    14333  13459  11289   -653   -297   -789       C  
ATOM   1949  NE  ARG A 190      -7.529  46.343 -17.820  1.00113.74           N  
ANISOU 1949  NE  ARG A 190    15674  14927  12615   -844   -308   -773       N  
ATOM   1950  CZ  ARG A 190      -6.226  46.142 -17.638  1.00129.99           C  
ANISOU 1950  CZ  ARG A 190    17555  17239  14598   -907   -302   -723       C  
ATOM   1951  NH1 ARG A 190      -5.798  45.108 -16.920  1.00109.09           N1+
ANISOU 1951  NH1 ARG A 190    14755  14776  11918   -775   -287   -680       N1+
ATOM   1952  NH2 ARG A 190      -5.340  46.972 -18.172  1.00123.95           N  
ANISOU 1952  NH2 ARG A 190    16760  16553  13782  -1102   -310   -710       N  
ATOM   1953  N   PRO A 191      -8.617  40.770 -15.302  1.00 91.64           N  
ANISOU 1953  N   PRO A 191    12617  12359   9841    -10   -178   -621       N  
ATOM   1954  CA  PRO A 191      -9.134  39.716 -14.416  1.00 91.68           C  
ANISOU 1954  CA  PRO A 191    12624  12364   9845    146   -162   -602       C  
ATOM   1955  C   PRO A 191     -10.501  40.073 -13.853  1.00 97.30           C  
ANISOU 1955  C   PRO A 191    13467  12898  10603    133   -190   -678       C  
ATOM   1956  O   PRO A 191     -10.729  41.223 -13.477  1.00 96.73           O  
ANISOU 1956  O   PRO A 191    13439  12784  10528      1   -243   -748       O  
ATOM   1957  CB  PRO A 191      -8.067  39.611 -13.329  1.00 94.48           C  
ANISOU 1957  CB  PRO A 191    12823  12965  10108    140   -192   -566       C  
ATOM   1958  CG  PRO A 191      -7.396  40.959 -13.305  1.00 99.62           C  
ANISOU 1958  CG  PRO A 191    13432  13699  10721    -72   -249   -609       C  
ATOM   1959  CD  PRO A 191      -7.703  41.686 -14.578  1.00 94.74           C  
ANISOU 1959  CD  PRO A 191    12915  12921  10161   -167   -236   -640       C  
ATOM   1960  N   ARG A 192     -11.427  39.105 -13.847  1.00 95.88           N  
ANISOU 1960  N   ARG A 192    13357  12609  10464    266   -151   -665       N  
ATOM   1961  CA  ARG A 192     -12.791  39.274 -13.342  1.00 96.51           C  
ANISOU 1961  CA  ARG A 192    13545  12541  10585    272   -167   -728       C  
ATOM   1962  C   ARG A 192     -13.239  37.949 -12.726  1.00104.79           C  
ANISOU 1962  C   ARG A 192    14598  13594  11624    415   -127   -684       C  
ATOM   1963  O   ARG A 192     -13.280  36.936 -13.444  1.00105.22           O  
ANISOU 1963  O   ARG A 192    14677  13605  11698    514    -71   -631       O  
ATOM   1964  CB  ARG A 192     -13.775  39.686 -14.472  1.00 95.77           C  
ANISOU 1964  CB  ARG A 192    13571  12251  10568    245   -159   -768       C  
ATOM   1965  CG  ARG A 192     -13.511  41.029 -15.167  1.00108.07           C  
ANISOU 1965  CG  ARG A 192    15162  13761  12138    107   -196   -809       C  
ATOM   1966  CD  ARG A 192     -13.988  42.232 -14.368  1.00120.54           C  
ANISOU 1966  CD  ARG A 192    16799  15291  13712     12   -253   -892       C  
ATOM   1967  NE  ARG A 192     -13.585  43.504 -14.980  1.00129.93           N  
ANISOU 1967  NE  ARG A 192    18035  16433  14900   -129   -287   -924       N  
ATOM   1968  CZ  ARG A 192     -12.534  44.227 -14.598  1.00146.55           C  
ANISOU 1968  CZ  ARG A 192    20086  18651  16946   -258   -320   -932       C  
ATOM   1969  NH1 ARG A 192     -11.758  43.814 -13.604  1.00135.33           N1+
ANISOU 1969  NH1 ARG A 192    18546  17414  15458   -256   -329   -909       N1+
ATOM   1970  NH2 ARG A 192     -12.254  45.372 -15.206  1.00135.02           N  
ANISOU 1970  NH2 ARG A 192    18693  17125  15483   -397   -346   -960       N  
ATOM   1971  N   ASP A 193     -13.570  37.953 -11.405  1.00103.33           N  
ANISOU 1971  N   ASP A 193    14401  13456  11402    422   -153   -707       N  
ATOM   1972  CA  ASP A 193     -14.060  36.790 -10.634  1.00103.90           C  
ANISOU 1972  CA  ASP A 193    14491  13533  11456    539   -119   -667       C  
ATOM   1973  C   ASP A 193     -13.157  35.542 -10.762  1.00107.73           C  
ANISOU 1973  C   ASP A 193    14919  14113  11901    667    -72   -564       C  
ATOM   1974  O   ASP A 193     -13.669  34.440 -10.994  1.00107.88           O  
ANISOU 1974  O   ASP A 193    15008  14044  11937    769    -17   -523       O  
ATOM   1975  CB  ASP A 193     -15.522  36.426 -11.034  1.00105.59           C  
ANISOU 1975  CB  ASP A 193    14822  13564  11735    567    -88   -698       C  
ATOM   1976  CG  ASP A 193     -16.619  37.286 -10.434  1.00122.74           C  
ANISOU 1976  CG  ASP A 193    17044  15668  13925    502   -123   -785       C  
ATOM   1977  OD1 ASP A 193     -16.918  37.114  -9.218  1.00126.23           O1-
ANISOU 1977  OD1 ASP A 193    17472  16168  14322    520   -131   -795       O1-
ATOM   1978  OD2 ASP A 193     -17.207  38.107 -11.182  1.00126.48           O  
ANISOU 1978  OD2 ASP A 193    17573  16032  14453    443   -140   -842       O  
ATOM   1979  N   GLY A 194     -11.836  35.723 -10.663  1.00102.93           N  
ANISOU 1979  N   GLY A 194    14189  13682  11236    660    -90   -523       N  
ATOM   1980  CA  GLY A 194     -10.890  34.611 -10.793  1.00101.97           C  
ANISOU 1980  CA  GLY A 194    14002  13673  11071    802    -44   -422       C  
ATOM   1981  C   GLY A 194     -10.658  34.106 -12.210  1.00101.66           C  
ANISOU 1981  C   GLY A 194    13997  13558  11070    863     17   -388       C  
ATOM   1982  O   GLY A 194      -9.726  33.338 -12.447  1.00101.85           O  
ANISOU 1982  O   GLY A 194    13958  13687  11053    983     58   -309       O  
ATOM   1983  N   ALA A 195     -11.496  34.540 -13.161  1.00 95.10           N  
ANISOU 1983  N   ALA A 195    13266  12553  10313    790     24   -446       N  
ATOM   1984  CA  ALA A 195     -11.413  34.226 -14.585  1.00 93.86           C  
ANISOU 1984  CA  ALA A 195    13159  12310  10194    819     76   -430       C  
ATOM   1985  C   ALA A 195     -10.721  35.384 -15.339  1.00 95.02           C  
ANISOU 1985  C   ALA A 195    13239  12520  10346    692     46   -457       C  
ATOM   1986  O   ALA A 195     -10.543  36.463 -14.771  1.00 94.25           O  
ANISOU 1986  O   ALA A 195    13089  12489  10234    567    -17   -500       O  
ATOM   1987  CB  ALA A 195     -12.814  33.993 -15.148  1.00 93.56           C  
ANISOU 1987  CB  ALA A 195    13272  12054  10223    807     95   -475       C  
ATOM   1988  N   VAL A 196     -10.326  35.156 -16.610  1.00 89.36           N  
ANISOU 1988  N   VAL A 196    12534  11778   9642    718     95   -431       N  
ATOM   1989  CA  VAL A 196      -9.693  36.186 -17.443  1.00 88.12           C  
ANISOU 1989  CA  VAL A 196    12325  11671   9486    593     77   -448       C  
ATOM   1990  C   VAL A 196     -10.657  36.573 -18.570  1.00 89.44           C  
ANISOU 1990  C   VAL A 196    12628  11637   9721    530     82   -496       C  
ATOM   1991  O   VAL A 196     -11.253  35.686 -19.185  1.00 88.55           O  
ANISOU 1991  O   VAL A 196    12609  11404   9633    621    132   -485       O  
ATOM   1992  CB  VAL A 196      -8.279  35.781 -17.948  1.00 91.96           C  
ANISOU 1992  CB  VAL A 196    12684  12343   9913    658    124   -375       C  
ATOM   1993  CG1 VAL A 196      -7.678  36.852 -18.861  1.00 91.63           C  
ANISOU 1993  CG1 VAL A 196    12595  12351   9868    508    110   -391       C  
ATOM   1994  CG2 VAL A 196      -7.345  35.489 -16.778  1.00 92.43           C  
ANISOU 1994  CG2 VAL A 196    12594  12626   9899    719    106   -324       C  
ATOM   1995  N   VAL A 197     -10.817  37.901 -18.811  1.00 84.86           N  
ANISOU 1995  N   VAL A 197    12066  11017   9161    372     28   -549       N  
ATOM   1996  CA  VAL A 197     -11.710  38.500 -19.816  1.00 83.15           C  
ANISOU 1996  CA  VAL A 197    11971  10622   9000    303     18   -593       C  
ATOM   1997  C   VAL A 197     -10.915  39.227 -20.898  1.00 87.31           C  
ANISOU 1997  C   VAL A 197    12473  11188   9512    204     24   -579       C  
ATOM   1998  O   VAL A 197     -10.074  40.047 -20.559  1.00 88.32           O  
ANISOU 1998  O   VAL A 197    12519  11435   9602     95     -8   -579       O  
ATOM   1999  CB  VAL A 197     -12.761  39.451 -19.152  1.00 86.01           C  
ANISOU 1999  CB  VAL A 197    12406  10873   9399    222    -49   -668       C  
ATOM   2000  CG1 VAL A 197     -13.671  40.099 -20.184  1.00 84.78           C  
ANISOU 2000  CG1 VAL A 197    12371  10546   9295    167    -65   -705       C  
ATOM   2001  CG2 VAL A 197     -13.600  38.714 -18.119  1.00 85.54           C  
ANISOU 2001  CG2 VAL A 197    12369  10783   9350    313    -48   -680       C  
ATOM   2002  N   CYS A 198     -11.192  38.921 -22.188  1.00 83.53           N  
ANISOU 2002  N   CYS A 198    12070  10613   9054    230     65   -567       N  
ATOM   2003  CA  CYS A 198     -10.666  39.578 -23.396  1.00 83.68           C  
ANISOU 2003  CA  CYS A 198    12097  10636   9061    137     77   -553       C  
ATOM   2004  C   CYS A 198     -11.763  40.605 -23.726  1.00 86.61           C  
ANISOU 2004  C   CYS A 198    12599  10827   9482     41     20   -609       C  
ATOM   2005  O   CYS A 198     -12.936  40.249 -23.890  1.00 86.04           O  
ANISOU 2005  O   CYS A 198    12623  10616   9454    101     15   -636       O  
ATOM   2006  CB  CYS A 198     -10.462  38.569 -24.527  1.00 84.40           C  
ANISOU 2006  CB  CYS A 198    12211  10717   9140    239    156   -512       C  
ATOM   2007  SG  CYS A 198      -9.919  39.283 -26.102  1.00 89.58           S  
ANISOU 2007  SG  CYS A 198    12890  11372   9773    132    180   -494       S  
ATOM   2008  N   MET A 199     -11.403  41.885 -23.698  1.00 82.78           N  
ANISOU 2008  N   MET A 199    12116  10352   8986   -106    -26   -628       N  
ATOM   2009  CA  MET A 199     -12.341  42.992 -23.830  1.00 82.05           C  
ANISOU 2009  CA  MET A 199    12149  10094   8931   -189    -85   -680       C  
ATOM   2010  C   MET A 199     -11.688  44.228 -24.448  1.00 86.73           C  
ANISOU 2010  C   MET A 199    12771  10685   9496   -353   -107   -674       C  
ATOM   2011  O   MET A 199     -10.475  44.242 -24.639  1.00 87.05           O  
ANISOU 2011  O   MET A 199    12712  10878   9484   -418    -79   -634       O  
ATOM   2012  CB  MET A 199     -12.844  43.347 -22.414  1.00 84.55           C  
ANISOU 2012  CB  MET A 199    12468  10397   9261   -189   -136   -733       C  
ATOM   2013  CG  MET A 199     -11.711  43.586 -21.410  1.00 89.96           C  
ANISOU 2013  CG  MET A 199    13032  11256   9890   -258   -149   -727       C  
ATOM   2014  SD  MET A 199     -12.197  44.402 -19.871  1.00 95.84           S  
ANISOU 2014  SD  MET A 199    13808  11975  10633   -311   -217   -802       S  
ATOM   2015  CE  MET A 199     -12.365  46.089 -20.438  1.00 93.04           C  
ANISOU 2015  CE  MET A 199    13596  11473  10283   -479   -266   -846       C  
ATOM   2016  N   LEU A 200     -12.483  45.289 -24.700  1.00 84.20           N  
ANISOU 2016  N   LEU A 200    12587  10200   9204   -420   -156   -712       N  
ATOM   2017  CA  LEU A 200     -11.980  46.570 -25.203  1.00 85.30           C  
ANISOU 2017  CA  LEU A 200    12792  10301   9315   -587   -182   -710       C  
ATOM   2018  C   LEU A 200     -11.988  47.597 -24.076  1.00 91.28           C  
ANISOU 2018  C   LEU A 200    13588  11031  10063   -685   -241   -766       C  
ATOM   2019  O   LEU A 200     -13.015  47.782 -23.418  1.00 91.89           O  
ANISOU 2019  O   LEU A 200    13740  10995  10179   -618   -276   -819       O  
ATOM   2020  CB  LEU A 200     -12.790  47.106 -26.400  1.00 85.01           C  
ANISOU 2020  CB  LEU A 200    12908  10087   9306   -592   -195   -704       C  
ATOM   2021  CG  LEU A 200     -12.797  46.295 -27.706  1.00 88.78           C  
ANISOU 2021  CG  LEU A 200    13381  10572   9780   -527   -142   -654       C  
ATOM   2022  CD1 LEU A 200     -13.915  46.769 -28.627  1.00 87.75           C  
ANISOU 2022  CD1 LEU A 200    13403  10258   9679   -504   -173   -659       C  
ATOM   2023  CD2 LEU A 200     -11.451  46.356 -28.410  1.00 91.60           C  
ANISOU 2023  CD2 LEU A 200    13664  11063  10075   -631    -95   -599       C  
ATOM   2024  N   GLN A 201     -10.825  48.230 -23.838  1.00 87.74           N  
ANISOU 2024  N   GLN A 201    13084  10697   9555   -846   -248   -756       N  
ATOM   2025  CA  GLN A 201     -10.608  49.262 -22.847  1.00 87.46           C  
ANISOU 2025  CA  GLN A 201    13092  10650   9490   -979   -301   -809       C  
ATOM   2026  C   GLN A 201     -10.784  50.614 -23.540  1.00 93.68           C  
ANISOU 2026  C   GLN A 201    14061  11261  10271  -1119   -330   -822       C  
ATOM   2027  O   GLN A 201      -9.854  51.121 -24.180  1.00 93.64           O  
ANISOU 2027  O   GLN A 201    14050  11312  10216  -1278   -318   -783       O  
ATOM   2028  CB  GLN A 201      -9.203  49.112 -22.237  1.00 89.47           C  
ANISOU 2028  CB  GLN A 201    13174  11149   9671  -1088   -292   -786       C  
ATOM   2029  CG  GLN A 201      -8.882  50.041 -21.049  1.00102.08           C  
ANISOU 2029  CG  GLN A 201    14794  12771  11222  -1236   -349   -847       C  
ATOM   2030  CD  GLN A 201      -9.697  49.727 -19.818  1.00117.44           C  
ANISOU 2030  CD  GLN A 201    16749  14679  13194  -1115   -376   -906       C  
ATOM   2031  OE1 GLN A 201      -9.291  48.921 -18.968  1.00107.21           O  
ANISOU 2031  OE1 GLN A 201    15610  13184  11941  -1070   -404   -964       O  
ATOM   2032  NE2 GLN A 201     -10.862  50.364 -19.693  1.00111.58           N  
ANISOU 2032  NE2 GLN A 201    15836  14137  12422  -1051   -367   -889       N  
ATOM   2033  N   PHE A 202     -12.001  51.176 -23.442  1.00 91.82           N  
ANISOU 2033  N   PHE A 202    13990  10814  10082  -1053   -366   -871       N  
ATOM   2034  CA  PHE A 202     -12.349  52.476 -24.026  1.00 92.87           C  
ANISOU 2034  CA  PHE A 202    14329  10746  10212  -1149   -398   -884       C  
ATOM   2035  C   PHE A 202     -11.892  53.654 -23.154  1.00 99.73           C  
ANISOU 2035  C   PHE A 202    15288  11575  11030  -1325   -439   -941       C  
ATOM   2036  O   PHE A 202     -11.904  53.537 -21.917  1.00 99.67           O  
ANISOU 2036  O   PHE A 202    15226  11631  11012  -1309   -458   -997       O  
ATOM   2037  CB  PHE A 202     -13.859  52.561 -24.290  1.00 93.77           C  
ANISOU 2037  CB  PHE A 202    14573  10665  10390   -981   -418   -909       C  
ATOM   2038  CG  PHE A 202     -14.297  51.673 -25.426  1.00 94.41           C  
ANISOU 2038  CG  PHE A 202    14614  10751  10505   -861   -385   -852       C  
ATOM   2039  CD1 PHE A 202     -14.107  52.064 -26.752  1.00 96.89           C  
ANISOU 2039  CD1 PHE A 202    15010  11001  10803   -925   -375   -796       C  
ATOM   2040  CD2 PHE A 202     -14.887  50.436 -25.176  1.00 94.30           C  
ANISOU 2040  CD2 PHE A 202    14491  10808  10532   -695   -363   -854       C  
ATOM   2041  CE1 PHE A 202     -14.479  51.226 -27.803  1.00 95.77           C  
ANISOU 2041  CE1 PHE A 202    14836  10873  10682   -823   -345   -748       C  
ATOM   2042  CE2 PHE A 202     -15.291  49.614 -26.231  1.00 95.44           C  
ANISOU 2042  CE2 PHE A 202    14614  10952  10699   -600   -334   -807       C  
ATOM   2043  CZ  PHE A 202     -15.081  50.016 -27.536  1.00 93.61           C  
ANISOU 2043  CZ  PHE A 202    14459  10661  10447   -663   -326   -757       C  
ATOM   2044  N   PRO A 203     -11.535  54.818 -23.770  1.00 98.07           N  
ANISOU 2044  N   PRO A 203    15234  11247  10782  -1497   -454   -930       N  
ATOM   2045  CA  PRO A 203     -11.109  55.984 -22.965  1.00 99.24           C  
ANISOU 2045  CA  PRO A 203    15499  11336  10873  -1684   -493   -990       C  
ATOM   2046  C   PRO A 203     -12.217  56.521 -22.064  1.00103.43           C  
ANISOU 2046  C   PRO A 203    16181  11684  11432  -1578   -531  -1078       C  
ATOM   2047  O   PRO A 203     -13.370  56.156 -22.269  1.00102.06           O  
ANISOU 2047  O   PRO A 203    16042  11412  11325  -1371   -529  -1083       O  
ATOM   2048  CB  PRO A 203     -10.708  57.015 -24.028  1.00101.97           C  
ANISOU 2048  CB  PRO A 203    16012  11554  11180  -1861   -493   -948       C  
ATOM   2049  CG  PRO A 203     -10.500  56.239 -25.274  1.00105.54           C  
ANISOU 2049  CG  PRO A 203    16357  12094  11648  -1804   -448   -858       C  
ATOM   2050  CD  PRO A 203     -11.486  55.132 -25.213  1.00 99.62           C  
ANISOU 2050  CD  PRO A 203    15520  11355  10975  -1541   -436   -863       C  
ATOM   2051  N   SER A 204     -11.884  57.393 -21.091  1.00101.93           N  
ANISOU 2051  N   SER A 204    16085  11457  11188  -1722   -563  -1150       N  
ATOM   2052  CA  SER A 204     -12.871  57.979 -20.163  1.00102.11           C  
ANISOU 2052  CA  SER A 204    16265  11308  11225  -1626   -593  -1243       C  
ATOM   2053  C   SER A 204     -13.897  58.898 -20.878  1.00105.31           C  
ANISOU 2053  C   SER A 204    16928  11422  11662  -1541   -605  -1249       C  
ATOM   2054  O   SER A 204     -13.462  59.813 -21.595  1.00106.03           O  
ANISOU 2054  O   SER A 204    17180  11390  11715  -1700   -612  -1222       O  
ATOM   2055  CB  SER A 204     -12.171  58.757 -19.051  1.00107.73           C  
ANISOU 2055  CB  SER A 204    17037  12041  11853  -1826   -623  -1320       C  
ATOM   2056  OG  SER A 204     -11.193  57.971 -18.392  1.00119.61           O  
ANISOU 2056  OG  SER A 204    18300  13828  13317  -1904   -619  -1308       O  
ATOM   2057  N   PRO A 205     -15.245  58.701 -20.711  1.00 99.39           N  
ANISOU 2057  N   PRO A 205    16223  10565  10975  -1296   -608  -1280       N  
ATOM   2058  CA  PRO A 205     -15.951  57.624 -19.988  1.00 96.67           C  
ANISOU 2058  CA  PRO A 205    15710  10343  10680  -1097   -596  -1305       C  
ATOM   2059  C   PRO A 205     -16.094  56.392 -20.892  1.00 98.37           C  
ANISOU 2059  C   PRO A 205    15747  10681  10948   -983   -567  -1220       C  
ATOM   2060  O   PRO A 205     -16.576  56.488 -22.031  1.00 97.44           O  
ANISOU 2060  O   PRO A 205    15700  10462  10862   -919   -564  -1167       O  
ATOM   2061  CB  PRO A 205     -17.295  58.271 -19.625  1.00 98.30           C  
ANISOU 2061  CB  PRO A 205    16089  10347  10913   -924   -613  -1371       C  
ATOM   2062  CG  PRO A 205     -17.464  59.458 -20.557  1.00104.81           C  
ANISOU 2062  CG  PRO A 205    17162  10936  11725   -971   -629  -1350       C  
ATOM   2063  CD  PRO A 205     -16.215  59.570 -21.402  1.00101.41           C  
ANISOU 2063  CD  PRO A 205    16711  10563  11256  -1195   -623  -1278       C  
ATOM   2064  N   SER A 206     -15.599  55.246 -20.413  1.00 93.34           N  
ANISOU 2064  N   SER A 206    14889  10264  10311   -969   -544  -1204       N  
ATOM   2065  CA  SER A 206     -15.561  54.027 -21.204  1.00 91.64           C  
ANISOU 2065  CA  SER A 206    14514  10172  10134   -881   -509  -1128       C  
ATOM   2066  C   SER A 206     -16.936  53.571 -21.699  1.00 95.51           C  
ANISOU 2066  C   SER A 206    15027  10573  10690   -672   -506  -1119       C  
ATOM   2067  O   SER A 206     -17.045  53.142 -22.850  1.00 94.47           O  
ANISOU 2067  O   SER A 206    14875  10438  10580   -635   -489  -1055       O  
ATOM   2068  CB  SER A 206     -14.827  52.923 -20.460  1.00 93.79           C  
ANISOU 2068  CB  SER A 206    14570  10679  10388   -883   -486  -1116       C  
ATOM   2069  OG  SER A 206     -15.536  52.558 -19.290  1.00106.92           O  
ANISOU 2069  OG  SER A 206    16196  12362  12066   -765   -493  -1176       O  
ATOM   2070  N   TRP A 207     -17.984  53.722 -20.861  1.00 92.49           N  
ANISOU 2070  N   TRP A 207    14691  10122  10331   -545   -522  -1185       N  
ATOM   2071  CA  TRP A 207     -19.367  53.349 -21.188  1.00 91.30           C  
ANISOU 2071  CA  TRP A 207    14549   9908  10235   -351   -522  -1183       C  
ATOM   2072  C   TRP A 207     -19.889  54.139 -22.388  1.00 96.26           C  
ANISOU 2072  C   TRP A 207    15335  10366  10876   -325   -543  -1150       C  
ATOM   2073  O   TRP A 207     -20.655  53.578 -23.186  1.00 96.57           O  
ANISOU 2073  O   TRP A 207    15338  10404  10950   -209   -540  -1109       O  
ATOM   2074  CB  TRP A 207     -20.297  53.557 -19.979  1.00 89.79           C  
ANISOU 2074  CB  TRP A 207    14380   9685  10050   -236   -532  -1265       C  
ATOM   2075  CG  TRP A 207     -20.294  54.961 -19.448  1.00 91.99           C  
ANISOU 2075  CG  TRP A 207    14847   9812  10293   -291   -560  -1333       C  
ATOM   2076  CD1 TRP A 207     -19.473  55.472 -18.489  1.00 95.78           C  
ANISOU 2076  CD1 TRP A 207    15360  10314  10718   -428   -568  -1387       C  
ATOM   2077  CD2 TRP A 207     -21.135  56.047 -19.877  1.00 92.52           C  
ANISOU 2077  CD2 TRP A 207    15111   9675  10368   -212   -583  -1352       C  
ATOM   2078  NE1 TRP A 207     -19.758  56.807 -18.281  1.00 96.41           N  
ANISOU 2078  NE1 TRP A 207    15658  10201  10771   -447   -591  -1447       N  
ATOM   2079  CE2 TRP A 207     -20.751  57.191 -19.143  1.00 97.41           C  
ANISOU 2079  CE2 TRP A 207    15894  10181  10936   -309   -599  -1422       C  
ATOM   2080  CE3 TRP A 207     -22.171  56.166 -20.820  1.00 93.41           C  
ANISOU 2080  CE3 TRP A 207    15281   9692  10519    -66   -594  -1315       C  
ATOM   2081  CZ2 TRP A 207     -21.369  58.429 -19.315  1.00 97.68           C  
ANISOU 2081  CZ2 TRP A 207    16161   9994  10961   -252   -619  -1456       C  
ATOM   2082  CZ3 TRP A 207     -22.760  57.406 -21.011  1.00 96.01           C  
ANISOU 2082  CZ3 TRP A 207    15825   9819  10837     -5   -619  -1340       C  
ATOM   2083  CH2 TRP A 207     -22.371  58.514 -20.253  1.00 97.86           C  
ANISOU 2083  CH2 TRP A 207    16233   9926  11024    -90   -628  -1411       C  
ATOM   2084  N   TYR A 208     -19.473  55.443 -22.506  1.00 91.72           N  
ANISOU 2084  N   TYR A 208    14940   9646  10263   -440   -566  -1165       N  
ATOM   2085  CA  TYR A 208     -19.878  56.348 -23.584  1.00 91.86           C  
ANISOU 2085  CA  TYR A 208    15139   9482  10280   -426   -589  -1129       C  
ATOM   2086  C   TYR A 208     -19.307  55.892 -24.928  1.00 96.70           C  
ANISOU 2086  C   TYR A 208    15702  10149  10891   -497   -573  -1037       C  
ATOM   2087  O   TYR A 208     -20.068  55.546 -25.836  1.00 96.08           O  
ANISOU 2087  O   TYR A 208    15619  10046  10840   -381   -578   -991       O  
ATOM   2088  CB  TYR A 208     -19.526  57.825 -23.278  1.00 93.86           C  
ANISOU 2088  CB  TYR A 208    15619   9556  10487   -542   -612  -1170       C  
ATOM   2089  CG  TYR A 208     -19.908  58.751 -24.415  1.00 95.76           C  
ANISOU 2089  CG  TYR A 208    16063   9600  10721   -524   -634  -1121       C  
ATOM   2090  CD1 TYR A 208     -21.244  59.032 -24.693  1.00 97.37           C  
ANISOU 2090  CD1 TYR A 208    16354   9686  10957   -311   -656  -1123       C  
ATOM   2091  CD2 TYR A 208     -18.940  59.274 -25.270  1.00 96.79           C  
ANISOU 2091  CD2 TYR A 208    16285   9681  10808   -715   -632  -1062       C  
ATOM   2092  CE1 TYR A 208     -21.603  59.844 -25.765  1.00 97.69           C  
ANISOU 2092  CE1 TYR A 208    16579   9553  10985   -279   -679  -1067       C  
ATOM   2093  CE2 TYR A 208     -19.289  60.076 -26.354  1.00 97.71           C  
ANISOU 2093  CE2 TYR A 208    16593   9617  10913   -697   -651  -1006       C  
ATOM   2094  CZ  TYR A 208     -20.621  60.360 -26.594  1.00102.32           C  
ANISOU 2094  CZ  TYR A 208    17271  10077  11528   -473   -677  -1007       C  
ATOM   2095  OH  TYR A 208     -20.975  61.124 -27.669  1.00103.26           O  
ANISOU 2095  OH  TYR A 208    17577  10027  11630   -440   -700   -944       O  
ATOM   2096  N   TRP A 209     -17.966  55.840 -25.018  1.00 93.58           N  
ANISOU 2096  N   TRP A 209    15255   9846  10455   -688   -552  -1011       N  
ATOM   2097  CA  TRP A 209     -17.207  55.420 -26.186  1.00 93.00           C  
ANISOU 2097  CA  TRP A 209    15123   9849  10364   -778   -526   -928       C  
ATOM   2098  C   TRP A 209     -17.515  54.014 -26.647  1.00 96.96           C  
ANISOU 2098  C   TRP A 209    15452  10488  10902   -655   -496   -891       C  
ATOM   2099  O   TRP A 209     -17.390  53.729 -27.839  1.00 97.25           O  
ANISOU 2099  O   TRP A 209    15486  10532  10931   -664   -480   -826       O  
ATOM   2100  CB  TRP A 209     -15.714  55.607 -25.941  1.00 91.97           C  
ANISOU 2100  CB  TRP A 209    14940   9829  10177   -998   -506   -918       C  
ATOM   2101  CG  TRP A 209     -15.344  57.050 -25.974  1.00 94.10           C  
ANISOU 2101  CG  TRP A 209    15418   9937  10397  -1161   -532   -932       C  
ATOM   2102  CD1 TRP A 209     -14.903  57.801 -24.932  1.00 98.07           C  
ANISOU 2102  CD1 TRP A 209    15989  10410  10861  -1285   -551   -998       C  
ATOM   2103  CD2 TRP A 209     -15.507  57.951 -27.081  1.00 94.90           C  
ANISOU 2103  CD2 TRP A 209    15716   9862  10480  -1208   -545   -882       C  
ATOM   2104  NE1 TRP A 209     -14.727  59.104 -25.333  1.00 99.23           N  
ANISOU 2104  NE1 TRP A 209    16370  10367  10965  -1421   -571   -993       N  
ATOM   2105  CE2 TRP A 209     -15.093  59.223 -26.648  1.00100.13           C  
ANISOU 2105  CE2 TRP A 209    16568  10385  11092  -1372   -568   -919       C  
ATOM   2106  CE3 TRP A 209     -15.917  57.792 -28.422  1.00 95.84           C  
ANISOU 2106  CE3 TRP A 209    15875   9929  10611  -1139   -540   -807       C  
ATOM   2107  CZ2 TRP A 209     -15.081  60.331 -27.495  1.00100.62           C  
ANISOU 2107  CZ2 TRP A 209    16865  10249  11118  -1463   -582   -878       C  
ATOM   2108  CZ3 TRP A 209     -15.921  58.898 -29.256  1.00 98.20           C  
ANISOU 2108  CZ3 TRP A 209    16394  10043  10872  -1222   -558   -765       C  
ATOM   2109  CH2 TRP A 209     -15.510  60.149 -28.789  1.00100.37           C  
ANISOU 2109  CH2 TRP A 209    16864  10173  11101  -1380   -577   -798       C  
ATOM   2110  N   ASP A 210     -17.949  53.152 -25.716  1.00 92.27           N  
ANISOU 2110  N   ASP A 210    14729   9991  10339   -545   -487   -933       N  
ATOM   2111  CA  ASP A 210     -18.353  51.787 -26.003  1.00 91.07           C  
ANISOU 2111  CA  ASP A 210    14433   9950  10218   -426   -458   -907       C  
ATOM   2112  C   ASP A 210     -19.681  51.840 -26.759  1.00 93.99           C  
ANISOU 2112  C   ASP A 210    14881  10212  10621   -289   -483   -895       C  
ATOM   2113  O   ASP A 210     -19.813  51.210 -27.809  1.00 92.48           O  
ANISOU 2113  O   ASP A 210    14659  10049  10432   -261   -468   -844       O  
ATOM   2114  CB  ASP A 210     -18.480  50.999 -24.687  1.00 92.93           C  
ANISOU 2114  CB  ASP A 210    14540  10299  10470   -359   -445   -956       C  
ATOM   2115  CG  ASP A 210     -19.057  49.610 -24.818  1.00109.31           C  
ANISOU 2115  CG  ASP A 210    16493  12463  12576   -234   -416   -938       C  
ATOM   2116  OD1 ASP A 210     -18.401  48.748 -25.449  1.00110.71           O  
ANISOU 2116  OD1 ASP A 210    16588  12736  12742   -257   -376   -888       O  
ATOM   2117  OD2 ASP A 210     -20.160  49.380 -24.285  1.00119.13           O1-
ANISOU 2117  OD2 ASP A 210    17730  13684  13851   -116   -429   -975       O1-
ATOM   2118  N   THR A 211     -20.633  52.652 -26.258  1.00 91.61           N  
ANISOU 2118  N   THR A 211    14683   9788  10335   -206   -523   -942       N  
ATOM   2119  CA  THR A 211     -21.948  52.845 -26.874  1.00 91.80           C  
ANISOU 2119  CA  THR A 211    14775   9722  10384    -63   -555   -931       C  
ATOM   2120  C   THR A 211     -21.823  53.505 -28.271  1.00 97.39           C  
ANISOU 2120  C   THR A 211    15613  10325  11066   -110   -573   -864       C  
ATOM   2121  O   THR A 211     -22.500  53.055 -29.197  1.00 97.67           O  
ANISOU 2121  O   THR A 211    15630  10371  11109    -31   -583   -823       O  
ATOM   2122  CB  THR A 211     -22.876  53.581 -25.909  1.00 97.28           C  
ANISOU 2122  CB  THR A 211    15542  10328  11091     46   -584   -999       C  
ATOM   2123  OG1 THR A 211     -22.859  52.902 -24.654  1.00 97.35           O  
ANISOU 2123  OG1 THR A 211    15425  10452  11114     68   -561  -1054       O  
ATOM   2124  CG2 THR A 211     -24.291  53.672 -26.419  1.00 91.30           C  
ANISOU 2124  CG2 THR A 211    14815   9519  10356    217   -616   -988       C  
ATOM   2125  N   VAL A 212     -20.922  54.524 -28.419  1.00 93.35           N  
ANISOU 2125  N   VAL A 212    15230   9723  10517   -254   -577   -852       N  
ATOM   2126  CA  VAL A 212     -20.610  55.241 -29.669  1.00 93.38           C  
ANISOU 2126  CA  VAL A 212    15373   9623  10485   -332   -589   -784       C  
ATOM   2127  C   VAL A 212     -20.078  54.277 -30.750  1.00 94.45           C  
ANISOU 2127  C   VAL A 212    15401   9880  10605   -382   -554   -718       C  
ATOM   2128  O   VAL A 212     -20.479  54.383 -31.909  1.00 93.33           O  
ANISOU 2128  O   VAL A 212    15328   9687  10448   -349   -569   -661       O  
ATOM   2129  CB  VAL A 212     -19.641  56.435 -29.412  1.00 99.01           C  
ANISOU 2129  CB  VAL A 212    16234  10231  11153   -509   -591   -791       C  
ATOM   2130  CG1 VAL A 212     -19.196  57.102 -30.714  1.00 99.58           C  
ANISOU 2130  CG1 VAL A 212    16446  10211  11180   -615   -595   -712       C  
ATOM   2131  CG2 VAL A 212     -20.291  57.469 -28.507  1.00100.00           C  
ANISOU 2131  CG2 VAL A 212    16511  10200  11286   -442   -626   -857       C  
ATOM   2132  N   THR A 213     -19.184  53.337 -30.354  1.00 89.42           N  
ANISOU 2132  N   THR A 213    14601   9409   9966   -450   -505   -725       N  
ATOM   2133  CA  THR A 213     -18.589  52.303 -31.215  1.00 87.25           C  
ANISOU 2133  CA  THR A 213    14213   9264   9673   -483   -458   -674       C  
ATOM   2134  C   THR A 213     -19.673  51.373 -31.742  1.00 88.37           C  
ANISOU 2134  C   THR A 213    14303   9431   9842   -334   -464   -667       C  
ATOM   2135  O   THR A 213     -19.690  51.094 -32.936  1.00 88.08           O  
ANISOU 2135  O   THR A 213    14287   9400   9779   -339   -455   -615       O  
ATOM   2136  CB  THR A 213     -17.462  51.560 -30.477  1.00 85.90           C  
ANISOU 2136  CB  THR A 213    13883   9261   9493   -558   -407   -690       C  
ATOM   2137  OG1 THR A 213     -16.487  52.519 -30.072  1.00 82.84           O  
ANISOU 2137  OG1 THR A 213    13548   8858   9069   -719   -410   -695       O  
ATOM   2138  CG2 THR A 213     -16.788  50.502 -31.342  1.00 80.23           C  
ANISOU 2138  CG2 THR A 213    13058   8677   8750   -576   -349   -639       C  
ATOM   2139  N   LYS A 214     -20.595  50.938 -30.866  1.00 83.60           N  
ANISOU 2139  N   LYS A 214    13639   8843   9281   -211   -481   -718       N  
ATOM   2140  CA  LYS A 214     -21.721  50.069 -31.229  1.00 82.68           C  
ANISOU 2140  CA  LYS A 214    13468   8760   9186    -83   -491   -718       C  
ATOM   2141  C   LYS A 214     -22.654  50.782 -32.223  1.00 86.67           C  
ANISOU 2141  C   LYS A 214    14095   9156   9680    -23   -545   -684       C  
ATOM   2142  O   LYS A 214     -23.155  50.119 -33.143  1.00 88.02           O  
ANISOU 2142  O   LYS A 214    14241   9366   9838     17   -548   -652       O  
ATOM   2143  CB  LYS A 214     -22.500  49.586 -29.983  1.00 84.33           C  
ANISOU 2143  CB  LYS A 214    13591   9014   9438     19   -497   -780       C  
ATOM   2144  CG  LYS A 214     -21.750  48.573 -29.131  1.00 87.17           C  
ANISOU 2144  CG  LYS A 214    13817   9500   9803    -13   -443   -802       C  
ATOM   2145  CD  LYS A 214     -22.304  48.528 -27.722  1.00 92.23           C  
ANISOU 2145  CD  LYS A 214    14406  10162  10474     56   -452   -864       C  
ATOM   2146  CE  LYS A 214     -21.435  47.705 -26.802  1.00100.12           C  
ANISOU 2146  CE  LYS A 214    15291  11280  11470     18   -406   -879       C  
ATOM   2147  NZ  LYS A 214     -22.007  47.540 -25.434  1.00 88.39           N1+
ANISOU 2147  NZ  LYS A 214    13753   9826  10005     85   -412   -936       N1+
ATOM   2148  N   ILE A 215     -22.853  52.128 -32.065  1.00 80.55           N  
ANISOU 2148  N   ILE A 215    13460   8243   8900    -17   -587   -687       N  
ATOM   2149  CA  ILE A 215     -23.679  52.947 -32.964  1.00 80.45           C  
ANISOU 2149  CA  ILE A 215    13582   8116   8871     54   -641   -645       C  
ATOM   2150  C   ILE A 215     -22.999  53.071 -34.339  1.00 85.70           C  
ANISOU 2150  C   ILE A 215    14318   8762   9484    -50   -630   -569       C  
ATOM   2151  O   ILE A 215     -23.652  52.802 -35.347  1.00 86.70           O  
ANISOU 2151  O   ILE A 215    14454   8899   9589     10   -656   -527       O  
ATOM   2152  CB  ILE A 215     -24.033  54.338 -32.377  1.00 84.32           C  
ANISOU 2152  CB  ILE A 215    14226   8448   9365     99   -681   -669       C  
ATOM   2153  CG1 ILE A 215     -24.905  54.230 -31.107  1.00 83.66           C  
ANISOU 2153  CG1 ILE A 215    14075   8388   9324    230   -692   -744       C  
ATOM   2154  CG2 ILE A 215     -24.687  55.262 -33.446  1.00 85.01           C  
ANISOU 2154  CG2 ILE A 215    14477   8403   9420    167   -734   -607       C  
ATOM   2155  CD1 ILE A 215     -24.696  55.411 -30.115  1.00 80.73           C  
ANISOU 2155  CD1 ILE A 215    13834   7886   8952    219   -700   -795       C  
ATOM   2156  N   CYS A 216     -21.706  53.468 -34.381  1.00 82.13           N  
ANISOU 2156  N   CYS A 216    13907   8296   9002   -209   -594   -552       N  
ATOM   2157  CA  CYS A 216     -20.935  53.601 -35.625  1.00 83.04           C  
ANISOU 2157  CA  CYS A 216    14082   8409   9060   -326   -572   -480       C  
ATOM   2158  C   CYS A 216     -20.771  52.285 -36.389  1.00 86.34           C  
ANISOU 2158  C   CYS A 216    14374   8969   9461   -322   -531   -458       C  
ATOM   2159  O   CYS A 216     -20.792  52.278 -37.627  1.00 85.44           O  
ANISOU 2159  O   CYS A 216    14318   8846   9300   -344   -533   -400       O  
ATOM   2160  CB  CYS A 216     -19.593  54.262 -35.362  1.00 84.42           C  
ANISOU 2160  CB  CYS A 216    14301   8570   9205   -507   -537   -472       C  
ATOM   2161  SG  CYS A 216     -19.734  55.970 -34.809  1.00 90.25           S  
ANISOU 2161  SG  CYS A 216    15257   9097   9938   -545   -585   -486       S  
ATOM   2162  N   VAL A 217     -20.638  51.164 -35.658  1.00 81.76           N  
ANISOU 2162  N   VAL A 217    13635   8514   8914   -292   -491   -505       N  
ATOM   2163  CA  VAL A 217     -20.545  49.863 -36.318  1.00 80.10           C  
ANISOU 2163  CA  VAL A 217    13327   8421   8687   -277   -448   -493       C  
ATOM   2164  C   VAL A 217     -21.901  49.525 -36.976  1.00 82.92           C  
ANISOU 2164  C   VAL A 217    13705   8758   9043   -162   -497   -486       C  
ATOM   2165  O   VAL A 217     -21.916  49.104 -38.128  1.00 82.42           O  
ANISOU 2165  O   VAL A 217    13661   8722   8932   -179   -487   -447       O  
ATOM   2166  CB  VAL A 217     -19.986  48.750 -35.401  1.00 82.15           C  
ANISOU 2166  CB  VAL A 217    13434   8807   8974   -271   -389   -537       C  
ATOM   2167  CG1 VAL A 217     -20.140  47.389 -36.054  1.00 81.60           C  
ANISOU 2167  CG1 VAL A 217    13293   8825   8886   -227   -349   -532       C  
ATOM   2168  CG2 VAL A 217     -18.516  49.002 -35.077  1.00 81.93           C  
ANISOU 2168  CG2 VAL A 217    13369   8838   8923   -397   -339   -525       C  
ATOM   2169  N   PHE A 218     -23.031  49.761 -36.262  1.00 78.55           N  
ANISOU 2169  N   PHE A 218    13146   8165   8533    -51   -550   -523       N  
ATOM   2170  CA  PHE A 218     -24.375  49.506 -36.792  1.00 77.31           C  
ANISOU 2170  CA  PHE A 218    12988   8015   8371     57   -604   -516       C  
ATOM   2171  C   PHE A 218     -24.690  50.366 -38.040  1.00 83.80           C  
ANISOU 2171  C   PHE A 218    13945   8754   9140     60   -655   -449       C  
ATOM   2172  O   PHE A 218     -25.340  49.894 -38.972  1.00 82.64           O  
ANISOU 2172  O   PHE A 218    13791   8651   8957     94   -681   -423       O  
ATOM   2173  CB  PHE A 218     -25.451  49.679 -35.696  1.00 77.77           C  
ANISOU 2173  CB  PHE A 218    13000   8067   8482    177   -645   -568       C  
ATOM   2174  CG  PHE A 218     -26.869  49.463 -36.180  1.00 79.22           C  
ANISOU 2174  CG  PHE A 218    13161   8284   8655    287   -704   -560       C  
ATOM   2175  CD1 PHE A 218     -27.306  48.205 -36.565  1.00 82.66           C  
ANISOU 2175  CD1 PHE A 218    13501   8830   9076    285   -691   -569       C  
ATOM   2176  CD2 PHE A 218     -27.743  50.527 -36.318  1.00 82.55           C  
ANISOU 2176  CD2 PHE A 218    13664   8628   9072    389   -773   -539       C  
ATOM   2177  CE1 PHE A 218     -28.600  48.012 -37.052  1.00 84.13           C  
ANISOU 2177  CE1 PHE A 218    13656   9068   9241    365   -751   -560       C  
ATOM   2178  CE2 PHE A 218     -29.037  50.335 -36.805  1.00 85.76           C  
ANISOU 2178  CE2 PHE A 218    14030   9094   9460    494   -832   -524       C  
ATOM   2179  CZ  PHE A 218     -29.456  49.082 -37.167  1.00 83.90           C  
ANISOU 2179  CZ  PHE A 218    13683   8986   9208    471   -823   -536       C  
ATOM   2180  N   LEU A 219     -24.222  51.621 -38.049  1.00 83.25           N  
ANISOU 2180  N   LEU A 219    14006   8566   9061     18   -670   -419       N  
ATOM   2181  CA  LEU A 219     -24.482  52.555 -39.141  1.00 84.38           C  
ANISOU 2181  CA  LEU A 219    14301   8609   9150     23   -718   -347       C  
ATOM   2182  C   LEU A 219     -23.613  52.343 -40.379  1.00 89.54           C  
ANISOU 2182  C   LEU A 219    14996   9290   9735   -100   -680   -287       C  
ATOM   2183  O   LEU A 219     -24.150  52.339 -41.478  1.00 90.13           O  
ANISOU 2183  O   LEU A 219    15123   9366   9758    -68   -717   -236       O  
ATOM   2184  CB  LEU A 219     -24.384  53.994 -38.649  1.00 85.10           C  
ANISOU 2184  CB  LEU A 219    14542   8540   9251     28   -747   -339       C  
ATOM   2185  CG  LEU A 219     -25.367  54.397 -37.554  1.00 89.89           C  
ANISOU 2185  CG  LEU A 219    15140   9102   9912    174   -789   -394       C  
ATOM   2186  CD1 LEU A 219     -25.013  55.743 -37.018  1.00 91.59           C  
ANISOU 2186  CD1 LEU A 219    15521   9149  10129    149   -798   -397       C  
ATOM   2187  CD2 LEU A 219     -26.811  54.424 -38.052  1.00 92.20           C  
ANISOU 2187  CD2 LEU A 219    15430   9408  10195    345   -859   -370       C  
ATOM   2188  N   PHE A 220     -22.294  52.151 -40.208  1.00 86.25           N  
ANISOU 2188  N   PHE A 220    14548   8911   9310   -235   -608   -291       N  
ATOM   2189  CA  PHE A 220     -21.364  51.967 -41.315  1.00 86.65           C  
ANISOU 2189  CA  PHE A 220    14628   9004   9291   -355   -559   -237       C  
ATOM   2190  C   PHE A 220     -21.358  50.575 -41.901  1.00 90.05           C  
ANISOU 2190  C   PHE A 220    14948   9570   9697   -343   -515   -249       C  
ATOM   2191  O   PHE A 220     -21.288  50.453 -43.127  1.00 91.55           O  
ANISOU 2191  O   PHE A 220    15192   9776   9816   -377   -509   -200       O  
ATOM   2192  CB  PHE A 220     -19.937  52.393 -40.936  1.00 89.06           C  
ANISOU 2192  CB  PHE A 220    14937   9314   9587   -508   -497   -232       C  
ATOM   2193  CG  PHE A 220     -19.756  53.891 -40.852  1.00 92.28           C  
ANISOU 2193  CG  PHE A 220    15514   9567   9980   -575   -533   -196       C  
ATOM   2194  CD1 PHE A 220     -19.428  54.632 -41.981  1.00 97.54           C  
ANISOU 2194  CD1 PHE A 220    16327  10162  10572   -662   -538   -115       C  
ATOM   2195  CD2 PHE A 220     -19.919  54.560 -39.647  1.00 94.51           C  
ANISOU 2195  CD2 PHE A 220    15827   9766  10317   -553   -560   -245       C  
ATOM   2196  CE1 PHE A 220     -19.270  56.017 -41.903  1.00100.16           C  
ANISOU 2196  CE1 PHE A 220    16841  10330  10884   -730   -569    -80       C  
ATOM   2197  CE2 PHE A 220     -19.766  55.943 -39.569  1.00 98.94           C  
ANISOU 2197  CE2 PHE A 220    16573  10163  10858   -616   -590   -217       C  
ATOM   2198  CZ  PHE A 220     -19.442  56.664 -40.697  1.00 99.03           C  
ANISOU 2198  CZ  PHE A 220    16738  10094  10797   -706   -595   -133       C  
ATOM   2199  N   ALA A 221     -21.373  49.531 -41.050  1.00 84.09           N  
ANISOU 2199  N   ALA A 221    14053   8904   8992   -300   -480   -314       N  
ATOM   2200  CA  ALA A 221     -21.308  48.124 -41.468  1.00 82.41           C  
ANISOU 2200  CA  ALA A 221    13751   8805   8758   -287   -429   -336       C  
ATOM   2201  C   ALA A 221     -22.681  47.449 -41.722  1.00 88.65           C  
ANISOU 2201  C   ALA A 221    14519   9614   9549   -187   -481   -358       C  
ATOM   2202  O   ALA A 221     -22.707  46.348 -42.274  1.00 89.25           O  
ANISOU 2202  O   ALA A 221    14558   9763   9590   -191   -445   -372       O  
ATOM   2203  CB  ALA A 221     -20.487  47.316 -40.480  1.00 81.67           C  
ANISOU 2203  CB  ALA A 221    13533   8794   8702   -302   -356   -383       C  
ATOM   2204  N   PHE A 222     -23.812  48.107 -41.378  1.00 85.80           N  
ANISOU 2204  N   PHE A 222    14185   9195   9220   -101   -565   -361       N  
ATOM   2205  CA  PHE A 222     -25.138  47.530 -41.617  1.00 85.14           C  
ANISOU 2205  CA  PHE A 222    14063   9156   9131    -16   -620   -378       C  
ATOM   2206  C   PHE A 222     -26.071  48.448 -42.425  1.00 89.79           C  
ANISOU 2206  C   PHE A 222    14744   9692   9679     41   -712   -323       C  
ATOM   2207  O   PHE A 222     -26.507  48.057 -43.505  1.00 90.29           O  
ANISOU 2207  O   PHE A 222    14830   9801   9676     34   -737   -295       O  
ATOM   2208  CB  PHE A 222     -25.790  47.074 -40.301  1.00 86.15           C  
ANISOU 2208  CB  PHE A 222    14081   9319   9332     58   -628   -444       C  
ATOM   2209  CG  PHE A 222     -27.120  46.375 -40.456  1.00 87.62           C  
ANISOU 2209  CG  PHE A 222    14206   9577   9509    123   -677   -465       C  
ATOM   2210  CD1 PHE A 222     -27.182  45.022 -40.755  1.00 89.28           C  
ANISOU 2210  CD1 PHE A 222    14362   9870   9692     83   -637   -495       C  
ATOM   2211  CD2 PHE A 222     -28.312  47.070 -40.299  1.00 90.31           C  
ANISOU 2211  CD2 PHE A 222    14544   9908   9861    224   -761   -457       C  
ATOM   2212  CE1 PHE A 222     -28.410  44.375 -40.884  1.00 89.83           C  
ANISOU 2212  CE1 PHE A 222    14375  10013   9745    116   -683   -516       C  
ATOM   2213  CE2 PHE A 222     -29.538  46.417 -40.423  1.00 92.62           C  
ANISOU 2213  CE2 PHE A 222    14758  10297  10138    272   -807   -475       C  
ATOM   2214  CZ  PHE A 222     -29.578  45.075 -40.717  1.00 89.49           C  
ANISOU 2214  CZ  PHE A 222    14307   9982   9712    204   -769   -505       C  
ATOM   2215  N   VAL A 223     -26.368  49.652 -41.912  1.00 85.98           N  
ANISOU 2215  N   VAL A 223    14324   9114   9230    103   -761   -307       N  
ATOM   2216  CA  VAL A 223     -27.275  50.618 -42.543  1.00 86.21           C  
ANISOU 2216  CA  VAL A 223    14449   9082   9223    189   -849   -250       C  
ATOM   2217  C   VAL A 223     -26.720  51.101 -43.878  1.00 92.05           C  
ANISOU 2217  C   VAL A 223    15321   9775   9880    112   -851   -170       C  
ATOM   2218  O   VAL A 223     -27.426  51.014 -44.893  1.00 92.21           O  
ANISOU 2218  O   VAL A 223    15368   9832   9835    148   -906   -126       O  
ATOM   2219  CB  VAL A 223     -27.630  51.813 -41.599  1.00 89.85           C  
ANISOU 2219  CB  VAL A 223    14970   9431   9738    284   -888   -256       C  
ATOM   2220  CG1 VAL A 223     -28.700  52.717 -42.209  1.00 90.36           C  
ANISOU 2220  CG1 VAL A 223    15126   9442   9765    412   -980   -195       C  
ATOM   2221  CG2 VAL A 223     -28.061  51.325 -40.218  1.00 88.97           C  
ANISOU 2221  CG2 VAL A 223    14727   9374   9704    349   -874   -338       C  
ATOM   2222  N   VAL A 224     -25.472  51.641 -43.875  1.00 89.65           N  
ANISOU 2222  N   VAL A 224    15097   9397   9570      0   -794   -147       N  
ATOM   2223  CA  VAL A 224     -24.856  52.213 -45.080  1.00 90.50           C  
ANISOU 2223  CA  VAL A 224    15338   9454   9594    -89   -788    -66       C  
ATOM   2224  C   VAL A 224     -24.780  51.131 -46.172  1.00 92.83           C  
ANISOU 2224  C   VAL A 224    15587   9868   9817   -138   -760    -57       C  
ATOM   2225  O   VAL A 224     -25.326  51.401 -47.244  1.00 93.77           O  
ANISOU 2225  O   VAL A 224    15785   9982   9861   -115   -815      3       O  
ATOM   2226  CB  VAL A 224     -23.521  53.004 -44.852  1.00 94.49           C  
ANISOU 2226  CB  VAL A 224    15930   9873  10098   -222   -729    -43       C  
ATOM   2227  CG1 VAL A 224     -22.822  53.325 -46.172  1.00 95.16           C  
ANISOU 2227  CG1 VAL A 224    16128   9944  10086   -336   -705     39       C  
ATOM   2228  CG2 VAL A 224     -23.779  54.295 -44.081  1.00 94.65           C  
ANISOU 2228  CG2 VAL A 224    16062   9740  10160   -172   -775    -38       C  
ATOM   2229  N   PRO A 225     -24.273  49.891 -45.894  1.00 86.66           N  
ANISOU 2229  N   PRO A 225    14683   9191   9052   -186   -685   -119       N  
ATOM   2230  CA  PRO A 225     -24.237  48.852 -46.935  1.00 85.68           C  
ANISOU 2230  CA  PRO A 225    14538   9165   8852   -227   -655   -119       C  
ATOM   2231  C   PRO A 225     -25.599  48.460 -47.482  1.00 90.38           C  
ANISOU 2231  C   PRO A 225    15118   9812   9411   -147   -738   -119       C  
ATOM   2232  O   PRO A 225     -25.692  48.288 -48.700  1.00 92.66           O  
ANISOU 2232  O   PRO A 225    15468  10135   9604   -184   -751    -80       O  
ATOM   2233  CB  PRO A 225     -23.544  47.685 -46.241  1.00 86.24           C  
ANISOU 2233  CB  PRO A 225    14490   9314   8965   -260   -563   -191       C  
ATOM   2234  CG  PRO A 225     -22.733  48.325 -45.196  1.00 90.80           C  
ANISOU 2234  CG  PRO A 225    15050   9841   9609   -287   -529   -200       C  
ATOM   2235  CD  PRO A 225     -23.604  49.403 -44.675  1.00 87.04           C  
ANISOU 2235  CD  PRO A 225    14626   9269   9178   -208   -618   -186       C  
ATOM   2236  N   ILE A 226     -26.655  48.371 -46.630  1.00 85.11           N  
ANISOU 2236  N   ILE A 226    14370   9160   8807    -45   -795   -160       N  
ATOM   2237  CA  ILE A 226     -28.023  48.056 -47.087  1.00 85.83           C  
ANISOU 2237  CA  ILE A 226    14425   9325   8861     28   -882   -158       C  
ATOM   2238  C   ILE A 226     -28.536  49.106 -48.063  1.00 91.12           C  
ANISOU 2238  C   ILE A 226    15209   9953   9459     74   -969    -68       C  
ATOM   2239  O   ILE A 226     -29.011  48.744 -49.133  1.00 90.96           O  
ANISOU 2239  O   ILE A 226    15207  10004   9348     57  -1009    -41       O  
ATOM   2240  CB  ILE A 226     -29.015  47.792 -45.926  1.00 88.97           C  
ANISOU 2240  CB  ILE A 226    14701   9767   9338    125   -920   -216       C  
ATOM   2241  CG1 ILE A 226     -28.828  46.379 -45.394  1.00 88.35           C  
ANISOU 2241  CG1 ILE A 226    14516   9768   9287     71   -851   -296       C  
ATOM   2242  CG2 ILE A 226     -30.490  48.023 -46.346  1.00 91.23           C  
ANISOU 2242  CG2 ILE A 226    14959  10121   9584    225  -1032   -188       C  
ATOM   2243  CD1 ILE A 226     -29.217  46.252 -43.981  1.00 98.81           C  
ANISOU 2243  CD1 ILE A 226    15738  11101  10705    134   -846   -352       C  
ATOM   2244  N   LEU A 227     -28.402  50.397 -47.709  1.00 89.71           N  
ANISOU 2244  N   LEU A 227    15119   9652   9313    127   -995    -22       N  
ATOM   2245  CA  LEU A 227     -28.811  51.527 -48.543  1.00 91.62           C  
ANISOU 2245  CA  LEU A 227    15497   9823   9491    185  -1073     73       C  
ATOM   2246  C   LEU A 227     -28.158  51.451 -49.917  1.00 96.50           C  
ANISOU 2246  C   LEU A 227    16216  10451  10001     73  -1049    135       C  
ATOM   2247  O   LEU A 227     -28.879  51.340 -50.905  1.00 98.51           O  
ANISOU 2247  O   LEU A 227    16490  10771  10167    102  -1116    179       O  
ATOM   2248  CB  LEU A 227     -28.450  52.858 -47.860  1.00 92.62           C  
ANISOU 2248  CB  LEU A 227    15736   9785   9671    226  -1075    103       C  
ATOM   2249  CG  LEU A 227     -29.553  53.656 -47.136  1.00 98.72           C  
ANISOU 2249  CG  LEU A 227    16511  10506  10491    407  -1155    106       C  
ATOM   2250  CD1 LEU A 227     -30.288  52.813 -46.070  1.00 98.35           C  
ANISOU 2250  CD1 LEU A 227    16276  10571  10521    478  -1155     14       C  
ATOM   2251  CD2 LEU A 227     -28.945  54.844 -46.431  1.00101.94           C  
ANISOU 2251  CD2 LEU A 227    17053  10733  10946    411  -1134    119       C  
ATOM   2252  N   ILE A 228     -26.811  51.442 -49.983  1.00 91.34           N  
ANISOU 2252  N   ILE A 228    15609   9752   9343    -58   -953    135       N  
ATOM   2253  CA  ILE A 228     -26.075  51.402 -51.249  1.00 91.58           C  
ANISOU 2253  CA  ILE A 228    15734   9797   9266   -171   -916    192       C  
ATOM   2254  C   ILE A 228     -26.537  50.235 -52.146  1.00 96.96           C  
ANISOU 2254  C   ILE A 228    16357  10617   9866   -191   -923    168       C  
ATOM   2255  O   ILE A 228     -26.858  50.473 -53.314  1.00 97.47           O  
ANISOU 2255  O   ILE A 228    16509  10703   9824   -198   -973    235       O  
ATOM   2256  CB  ILE A 228     -24.537  51.435 -51.029  1.00 93.59           C  
ANISOU 2256  CB  ILE A 228    16007  10019   9534   -309   -800    184       C  
ATOM   2257  CG1 ILE A 228     -24.109  52.795 -50.433  1.00 93.21           C  
ANISOU 2257  CG1 ILE A 228    16065   9819   9530   -320   -808    227       C  
ATOM   2258  CG2 ILE A 228     -23.785  51.158 -52.349  1.00 95.10           C  
ANISOU 2258  CG2 ILE A 228    16266  10262   9606   -425   -745    231       C  
ATOM   2259  CD1 ILE A 228     -22.725  52.854 -49.842  1.00 92.70           C  
ANISOU 2259  CD1 ILE A 228    15980   9740   9501   -449   -707    203       C  
ATOM   2260  N   ILE A 229     -26.625  49.005 -51.582  1.00 93.17           N  
ANISOU 2260  N   ILE A 229    15743  10227   9431   -198   -879     74       N  
ATOM   2261  CA  ILE A 229     -27.042  47.795 -52.306  1.00 93.07           C  
ANISOU 2261  CA  ILE A 229    15685  10334   9344   -232   -877     34       C  
ATOM   2262  C   ILE A 229     -28.526  47.885 -52.762  1.00 98.30           C  
ANISOU 2262  C   ILE A 229    16331  11062   9957   -149  -1005     59       C  
ATOM   2263  O   ILE A 229     -28.820  47.512 -53.907  1.00 98.65           O  
ANISOU 2263  O   ILE A 229    16419  11179   9886   -191  -1035     81       O  
ATOM   2264  CB  ILE A 229     -26.712  46.484 -51.516  1.00 94.69           C  
ANISOU 2264  CB  ILE A 229    15775  10594   9609   -262   -792    -71       C  
ATOM   2265  CG1 ILE A 229     -25.174  46.316 -51.340  1.00 94.05           C  
ANISOU 2265  CG1 ILE A 229    15707  10484   9544   -343   -664    -83       C  
ATOM   2266  CG2 ILE A 229     -27.321  45.238 -52.209  1.00 95.41           C  
ANISOU 2266  CG2 ILE A 229    15839  10792   9621   -296   -800   -119       C  
ATOM   2267  CD1 ILE A 229     -24.684  45.243 -50.303  1.00 91.53           C  
ANISOU 2267  CD1 ILE A 229    15278  10195   9302   -345   -576   -172       C  
ATOM   2268  N   THR A 230     -29.447  48.382 -51.884  1.00 94.38           N  
ANISOU 2268  N   THR A 230    15769  10553   9538    -29  -1080     55       N  
ATOM   2269  CA  THR A 230     -30.875  48.523 -52.226  1.00 94.93           C  
ANISOU 2269  CA  THR A 230    15796  10710   9563     66  -1203     83       C  
ATOM   2270  C   THR A 230     -31.041  49.528 -53.364  1.00100.49           C  
ANISOU 2270  C   THR A 230    16635  11380  10166     98  -1276    195       C  
ATOM   2271  O   THR A 230     -31.800  49.274 -54.306  1.00101.19           O  
ANISOU 2271  O   THR A 230    16721  11577  10150    101  -1351    225       O  
ATOM   2272  CB  THR A 230     -31.736  48.809 -50.990  1.00100.26           C  
ANISOU 2272  CB  THR A 230    16362  11390  10341    195  -1250     52       C  
ATOM   2273  OG1 THR A 230     -31.425  47.829 -50.007  1.00100.82           O  
ANISOU 2273  OG1 THR A 230    16327  11487  10495    146  -1171    -46       O  
ATOM   2274  CG2 THR A 230     -33.234  48.742 -51.279  1.00 98.11           C  
ANISOU 2274  CG2 THR A 230    16003  11254  10020    289  -1369     69       C  
ATOM   2275  N   VAL A 231     -30.274  50.627 -53.308  1.00 97.08           N  
ANISOU 2275  N   VAL A 231    16331  10802   9755    103  -1249    258       N  
ATOM   2276  CA  VAL A 231     -30.257  51.651 -54.351  1.00 98.20           C  
ANISOU 2276  CA  VAL A 231    16631  10880   9800    121  -1303    374       C  
ATOM   2277  C   VAL A 231     -29.717  51.041 -55.664  1.00102.02           C  
ANISOU 2277  C   VAL A 231    17175  11433  10156    -14  -1267    394       C  
ATOM   2278  O   VAL A 231     -30.309  51.293 -56.708  1.00102.37           O  
ANISOU 2278  O   VAL A 231    17279  11529  10086     12  -1348    465       O  
ATOM   2279  CB  VAL A 231     -29.540  52.952 -53.896  1.00101.83           C  
ANISOU 2279  CB  VAL A 231    17227  11151  10313    139  -1276    430       C  
ATOM   2280  CG1 VAL A 231     -29.442  53.973 -55.035  1.00102.89           C  
ANISOU 2280  CG1 VAL A 231    17551  11206  10336    140  -1323    558       C  
ATOM   2281  CG2 VAL A 231     -30.256  53.562 -52.686  1.00101.28           C  
ANISOU 2281  CG2 VAL A 231    17112  11020  10351    294  -1324    408       C  
ATOM   2282  N   CYS A 232     -28.669  50.177 -55.594  1.00 98.28           N  
ANISOU 2282  N   CYS A 232    16673  10975   9693   -144  -1147    326       N  
ATOM   2283  CA  CYS A 232     -28.127  49.454 -56.757  1.00 99.40           C  
ANISOU 2283  CA  CYS A 232    16863  11190   9714   -266  -1095    325       C  
ATOM   2284  C   CYS A 232     -29.212  48.555 -57.374  1.00106.39           C  
ANISOU 2284  C   CYS A 232    17683  12223  10516   -256  -1169    292       C  
ATOM   2285  O   CYS A 232     -29.349  48.536 -58.592  1.00106.98           O  
ANISOU 2285  O   CYS A 232    17838  12354  10455   -300  -1203    342       O  
ATOM   2286  CB  CYS A 232     -26.876  48.650 -56.401  1.00 98.24           C  
ANISOU 2286  CB  CYS A 232    16680  11042   9605   -373   -950    251       C  
ATOM   2287  SG  CYS A 232     -25.374  49.650 -56.215  1.00102.01           S  
ANISOU 2287  SG  CYS A 232    17254  11394  10111   -450   -856    309       S  
ATOM   2288  N   TYR A 233     -30.021  47.877 -56.529  1.00104.61           N  
ANISOU 2288  N   TYR A 233    17318  12065  10366   -204  -1199    213       N  
ATOM   2289  CA  TYR A 233     -31.132  47.019 -56.957  1.00105.96           C  
ANISOU 2289  CA  TYR A 233    17410  12384  10465   -210  -1275    174       C  
ATOM   2290  C   TYR A 233     -32.250  47.819 -57.639  1.00111.95           C  
ANISOU 2290  C   TYR A 233    18188  13205  11141   -115  -1421    268       C  
ATOM   2291  O   TYR A 233     -32.610  47.516 -58.779  1.00112.65           O  
ANISOU 2291  O   TYR A 233    18318  13391  11091   -168  -1471    295       O  
ATOM   2292  CB  TYR A 233     -31.687  46.219 -55.767  1.00106.91           C  
ANISOU 2292  CB  TYR A 233    17375  12552  10692   -183  -1267     76       C  
ATOM   2293  CG  TYR A 233     -32.868  45.330 -56.105  1.00110.38           C  
ANISOU 2293  CG  TYR A 233    17725  13153  11060   -209  -1345     32       C  
ATOM   2294  CD1 TYR A 233     -32.696  44.150 -56.826  1.00112.45           C  
ANISOU 2294  CD1 TYR A 233    18016  13483  11226   -342  -1301    -30       C  
ATOM   2295  CD2 TYR A 233     -34.150  45.639 -55.656  1.00111.92           C  
ANISOU 2295  CD2 TYR A 233    17805  13438  11282   -105  -1457     47       C  
ATOM   2296  CE1 TYR A 233     -33.774  43.314 -57.116  1.00113.33           C  
ANISOU 2296  CE1 TYR A 233    18054  13742  11265   -393  -1373    -76       C  
ATOM   2297  CE2 TYR A 233     -35.235  44.806 -55.936  1.00113.42           C  
ANISOU 2297  CE2 TYR A 233    17896  13797  11400   -150  -1530      6       C  
ATOM   2298  CZ  TYR A 233     -35.040  43.641 -56.662  1.00119.63           C  
ANISOU 2298  CZ  TYR A 233    18723  14643  12089   -305  -1489    -57       C  
ATOM   2299  OH  TYR A 233     -36.101  42.813 -56.936  1.00120.07           O  
ANISOU 2299  OH  TYR A 233    18693  14864  12066   -375  -1561   -101       O  
ATOM   2300  N   GLY A 234     -32.778  48.824 -56.931  1.00108.90           N  
ANISOU 2300  N   GLY A 234    17778  12764  10836     29  -1486    317       N  
ATOM   2301  CA  GLY A 234     -33.841  49.704 -57.408  1.00109.97           C  
ANISOU 2301  CA  GLY A 234    17927  12948  10907    161  -1623    414       C  
ATOM   2302  C   GLY A 234     -33.549  50.355 -58.745  1.00114.17           C  
ANISOU 2302  C   GLY A 234    18624  13454  11302    136  -1657    524       C  
ATOM   2303  O   GLY A 234     -34.454  50.501 -59.572  1.00114.96           O  
ANISOU 2303  O   GLY A 234    18721  13671  11289    186  -1770    586       O  
ATOM   2304  N   LEU A 235     -32.276  50.754 -58.962  1.00110.04           N  
ANISOU 2304  N   LEU A 235    18241  12789  10782     53  -1560    552       N  
ATOM   2305  CA  LEU A 235     -31.815  51.364 -60.209  1.00111.01           C  
ANISOU 2305  CA  LEU A 235    18534  12874  10773      4  -1569    657       C  
ATOM   2306  C   LEU A 235     -31.785  50.298 -61.309  1.00118.01           C  
ANISOU 2306  C   LEU A 235    19416  13903  11520   -127  -1557    622       C  
ATOM   2307  O   LEU A 235     -32.257  50.560 -62.418  1.00119.29           O  
ANISOU 2307  O   LEU A 235    19647  14138  11541   -119  -1642    702       O  
ATOM   2308  CB  LEU A 235     -30.434  52.022 -60.043  1.00109.94           C  
ANISOU 2308  CB  LEU A 235    18530  12563  10679    -70  -1458    688       C  
ATOM   2309  CG  LEU A 235     -30.401  53.350 -59.302  1.00114.42           C  
ANISOU 2309  CG  LEU A 235    19178  12960  11335     41  -1481    755       C  
ATOM   2310  CD1 LEU A 235     -28.998  53.696 -58.887  1.00113.93           C  
ANISOU 2310  CD1 LEU A 235    19197  12756  11333    -72  -1356    746       C  
ATOM   2311  CD2 LEU A 235     -30.982  54.473 -60.131  1.00118.72           C  
ANISOU 2311  CD2 LEU A 235    19870  13459  11779    143  -1589    896       C  
ATOM   2312  N   MET A 236     -31.276  49.088 -60.978  1.00114.13           N  
ANISOU 2312  N   MET A 236    18848  13453  11065   -238  -1456    501       N  
ATOM   2313  CA  MET A 236     -31.202  47.942 -61.882  1.00114.71           C  
ANISOU 2313  CA  MET A 236    18924  13645  11015   -366  -1426    442       C  
ATOM   2314  C   MET A 236     -32.591  47.500 -62.356  1.00122.65           C  
ANISOU 2314  C   MET A 236    19851  14820  11929   -340  -1560    436       C  
ATOM   2315  O   MET A 236     -32.745  47.216 -63.544  1.00123.31           O  
ANISOU 2315  O   MET A 236    20003  14997  11854   -413  -1595    460       O  
ATOM   2316  CB  MET A 236     -30.457  46.769 -61.229  1.00115.12           C  
ANISOU 2316  CB  MET A 236    18912  13685  11142   -456  -1292    312       C  
ATOM   2317  CG  MET A 236     -28.956  46.933 -61.214  1.00117.66           C  
ANISOU 2317  CG  MET A 236    19318  13900  11487   -526  -1150    316       C  
ATOM   2318  SD  MET A 236     -28.158  45.437 -60.599  1.00119.71           S  
ANISOU 2318  SD  MET A 236    19504  14172  11807   -609   -998    169       S  
ATOM   2319  CE  MET A 236     -27.280  46.072 -59.245  1.00115.41           C  
ANISOU 2319  CE  MET A 236    18911  13500  11439   -560   -922    171       C  
ATOM   2320  N   LEU A 237     -33.603  47.461 -61.447  1.00121.40           N  
ANISOU 2320  N   LEU A 237    19547  14719  11862   -241  -1636    407       N  
ATOM   2321  CA  LEU A 237     -34.970  47.078 -61.827  1.00123.45           C  
ANISOU 2321  CA  LEU A 237    19703  15167  12034   -219  -1769    404       C  
ATOM   2322  C   LEU A 237     -35.602  48.120 -62.740  1.00132.45           C  
ANISOU 2322  C   LEU A 237    20908  16358  13059   -121  -1900    543       C  
ATOM   2323  O   LEU A 237     -36.343  47.757 -63.646  1.00134.02           O  
ANISOU 2323  O   LEU A 237    21087  16722  13114   -161  -1992    558       O  
ATOM   2324  CB  LEU A 237     -35.892  46.709 -60.633  1.00122.84           C  
ANISOU 2324  CB  LEU A 237    19437  15162  12072   -149  -1808    336       C  
ATOM   2325  CG  LEU A 237     -36.247  47.771 -59.575  1.00127.63           C  
ANISOU 2325  CG  LEU A 237    19986  15694  12814     37  -1846    386       C  
ATOM   2326  CD1 LEU A 237     -37.474  48.587 -59.968  1.00129.76           C  
ANISOU 2326  CD1 LEU A 237    20208  16082  13014    190  -2005    488       C  
ATOM   2327  CD2 LEU A 237     -36.561  47.123 -58.261  1.00128.76           C  
ANISOU 2327  CD2 LEU A 237    19973  15860  13091     47  -1808    283       C  
ATOM   2328  N   LEU A 238     -35.272  49.401 -62.524  1.00131.81           N  
ANISOU 2328  N   LEU A 238    20918  16131  13032      2  -1905    643       N  
ATOM   2329  CA  LEU A 238     -35.757  50.530 -63.317  1.00135.03           C  
ANISOU 2329  CA  LEU A 238    21420  16546  13340    119  -2019    790       C  
ATOM   2330  C   LEU A 238     -35.158  50.512 -64.739  1.00143.18           C  
ANISOU 2330  C   LEU A 238    22613  17588  14202     -2  -2004    849       C  
ATOM   2331  O   LEU A 238     -35.892  50.693 -65.715  1.00144.11           O  
ANISOU 2331  O   LEU A 238    22750  17834  14170     27  -2120    926       O  
ATOM   2332  CB  LEU A 238     -35.392  51.841 -62.606  1.00135.11           C  
ANISOU 2332  CB  LEU A 238    21518  16355  13464    261  -2003    867       C  
ATOM   2333  CG  LEU A 238     -36.525  52.825 -62.379  1.00141.33           C  
ANISOU 2333  CG  LEU A 238    22272  17170  14258    487  -2138    962       C  
ATOM   2334  CD1 LEU A 238     -37.203  52.578 -61.040  1.00140.79           C  
ANISOU 2334  CD1 LEU A 238    22014  17147  14331    589  -2149    878       C  
ATOM   2335  CD2 LEU A 238     -36.008  54.239 -62.414  1.00144.62           C  
ANISOU 2335  CD2 LEU A 238    22886  17369  14693    588  -2129   1081       C  
ATOM   2336  N   ARG A 239     -33.830  50.269 -64.841  1.00141.49           N  
ANISOU 2336  N   ARG A 239    22503  17254  14004   -136  -1859    811       N  
ATOM   2337  CA  ARG A 239     -33.072  50.214 -66.096  1.00143.36           C  
ANISOU 2337  CA  ARG A 239    22894  17488  14088   -262  -1812    855       C  
ATOM   2338  C   ARG A 239     -33.469  49.016 -66.953  1.00150.26           C  
ANISOU 2338  C   ARG A 239    23726  18546  14818   -384  -1834    782       C  
ATOM   2339  O   ARG A 239     -33.303  49.056 -68.175  1.00150.93           O  
ANISOU 2339  O   ARG A 239    23927  18685  14735   -456  -1852    838       O  
ATOM   2340  CB  ARG A 239     -31.552  50.245 -65.837  1.00143.83           C  
ANISOU 2340  CB  ARG A 239    23044  17392  14213   -364  -1643    827       C  
ATOM   2341  CG  ARG A 239     -31.074  51.504 -65.088  1.00160.14           C  
ANISOU 2341  CG  ARG A 239    25181  19266  16398   -276  -1620    904       C  
ATOM   2342  CD  ARG A 239     -30.604  52.634 -65.989  1.00175.69           C  
ANISOU 2342  CD  ARG A 239    27350  21142  18262   -283  -1631   1051       C  
ATOM   2343  NE  ARG A 239     -30.503  53.906 -65.266  1.00184.17           N  
ANISOU 2343  NE  ARG A 239    28500  22036  19438   -174  -1648   1131       N  
ATOM   2344  CZ  ARG A 239     -29.433  54.308 -64.583  1.00194.21           C  
ANISOU 2344  CZ  ARG A 239    29824  23154  20813   -233  -1536   1117       C  
ATOM   2345  NH1 ARG A 239     -28.356  53.535 -64.507  1.00174.61           N1+
ANISOU 2345  NH1 ARG A 239    27306  20688  18350   -387  -1397   1031       N1+
ATOM   2346  NH2 ARG A 239     -29.434  55.485 -63.971  1.00182.70           N  
ANISOU 2346  NH2 ARG A 239    28455  21528  19434   -138  -1561   1188       N  
ATOM   2347  N   LEU A 240     -34.017  47.962 -66.316  1.00148.21           N  
ANISOU 2347  N   LEU A 240    23313  18382  14618   -415  -1836    658       N  
ATOM   2348  CA  LEU A 240     -34.503  46.777 -67.022  1.00149.44           C  
ANISOU 2348  CA  LEU A 240    23432  18707  14641   -542  -1863    576       C  
ATOM   2349  C   LEU A 240     -36.013  46.857 -67.292  1.00157.66           C  
ANISOU 2349  C   LEU A 240    24361  19941  15602   -473  -2044    616       C  
ATOM   2350  O   LEU A 240     -36.487  46.216 -68.234  1.00158.66           O  
ANISOU 2350  O   LEU A 240    24496  20225  15565   -576  -2103    594       O  
ATOM   2351  CB  LEU A 240     -34.090  45.463 -66.335  1.00147.57           C  
ANISOU 2351  CB  LEU A 240    23128  18456  14485   -651  -1744    415       C  
ATOM   2352  CG  LEU A 240     -32.609  45.065 -66.484  1.00150.71           C  
ANISOU 2352  CG  LEU A 240    23643  18729  14891   -751  -1566    364       C  
ATOM   2353  CD1 LEU A 240     -32.341  43.763 -65.815  1.00149.29           C  
ANISOU 2353  CD1 LEU A 240    23400  18543  14781   -832  -1464    214       C  
ATOM   2354  CD2 LEU A 240     -32.193  44.941 -67.945  1.00154.06           C  
ANISOU 2354  CD2 LEU A 240    24217  19203  15116   -854  -1548    397       C  
ATOM   2355  N   ARG A 241     -36.747  47.698 -66.518  1.00156.07           N  
ANISOU 2355  N   ARG A 241    24062  19735  15503   -295  -2132    681       N  
ATOM   2356  CA  ARG A 241     -38.177  47.961 -66.720  1.00158.43           C  
ANISOU 2356  CA  ARG A 241    24237  20228  15730   -192  -2306    740       C  
ATOM   2357  C   ARG A 241     -38.352  48.796 -68.005  1.00166.99           C  
ANISOU 2357  C   ARG A 241    25449  21360  16640   -143  -2406    887       C  
ATOM   2358  O   ARG A 241     -39.370  48.661 -68.684  1.00168.27           O  
ANISOU 2358  O   ARG A 241    25540  21733  16662   -134  -2544    924       O  
ATOM   2359  CB  ARG A 241     -38.782  48.698 -65.511  1.00158.40           C  
ANISOU 2359  CB  ARG A 241    24110  20188  15888      8  -2352    771       C  
ATOM   2360  CG  ARG A 241     -40.309  48.645 -65.449  1.00171.17           C  
ANISOU 2360  CG  ARG A 241    25536  22045  17455    103  -2512    792       C  
ATOM   2361  CD  ARG A 241     -40.864  49.149 -64.127  1.00180.74           C  
ANISOU 2361  CD  ARG A 241    26607  23231  18833    286  -2530    791       C  
ATOM   2362  NE  ARG A 241     -40.822  48.123 -63.082  1.00186.85           N  
ANISOU 2362  NE  ARG A 241    27250  24015  19729    187  -2446    644       N  
ATOM   2363  CZ  ARG A 241     -41.232  48.303 -61.829  1.00199.33           C  
ANISOU 2363  CZ  ARG A 241    28696  25583  21457    306  -2438    612       C  
ATOM   2364  NH1 ARG A 241     -41.722  49.477 -61.445  1.00187.14           N1+
ANISOU 2364  NH1 ARG A 241    27131  24010  19962    538  -2506    710       N1+
ATOM   2365  NH2 ARG A 241     -41.156  47.313 -60.951  1.00183.61           N  
ANISOU 2365  NH2 ARG A 241    26601  23601  19562    199  -2358    482       N  
ATOM   2366  N   SER A 242     -37.344  49.637 -68.335  1.00165.35           N  
ANISOU 2366  N   SER A 242    25428  20964  16433   -123  -2335    972       N  
ATOM   2367  CA  SER A 242     -37.304  50.488 -69.529  1.00167.91           C  
ANISOU 2367  CA  SER A 242    25910  21292  16596    -87  -2405   1120       C  
ATOM   2368  C   SER A 242     -37.075  49.668 -70.807  1.00174.77           C  
ANISOU 2368  C   SER A 242    26855  22284  17266   -276  -2395   1087       C  
ATOM   2369  O   SER A 242     -37.700  49.954 -71.826  1.00175.88           O  
ANISOU 2369  O   SER A 242    27032  22563  17233   -253  -2518   1181       O  
ATOM   2370  CB  SER A 242     -36.224  51.555 -69.385  1.00171.15           C  
ANISOU 2370  CB  SER A 242    26500  21453  17075    -40  -2313   1207       C  
ATOM   2371  OG  SER A 242     -34.945  50.965 -69.219  1.00178.49           O  
ANISOU 2371  OG  SER A 242    27493  22266  18059   -203  -2140   1113       O  
ATOM   2372  N   VAL A 243     -36.175  48.658 -70.748  1.00172.28           N  
ANISOU 2372  N   VAL A 243    26569  21919  16972   -452  -2248    956       N  
ATOM   2373  CA  VAL A 243     -35.853  47.728 -71.845  1.00173.67           C  
ANISOU 2373  CA  VAL A 243    26825  22191  16971   -639  -2209    894       C  
ATOM   2374  C   VAL A 243     -37.101  46.850 -72.113  1.00181.70           C  
ANISOU 2374  C   VAL A 243    27704  23450  17885   -695  -2335    827       C  
ATOM   2375  O   VAL A 243     -37.404  46.536 -73.270  1.00182.65           O  
ANISOU 2375  O   VAL A 243    27883  23714  17801   -790  -2401    843       O  
ATOM   2376  CB  VAL A 243     -34.576  46.895 -71.521  1.00175.54           C  
ANISOU 2376  CB  VAL A 243    27118  22299  17279   -776  -2009    766       C  
ATOM   2377  CG1 VAL A 243     -34.302  45.833 -72.584  1.00176.07           C  
ANISOU 2377  CG1 VAL A 243    27269  22466  17164   -958  -1960    682       C  
ATOM   2378  CG2 VAL A 243     -33.356  47.797 -71.351  1.00174.62           C  
ANISOU 2378  CG2 VAL A 243    27127  21981  17241   -741  -1894    841       C  
ATOM   2379  N   ARG A 244     -37.831  46.494 -71.028  1.00180.04           N  
ANISOU 2379  N   ARG A 244    27309  23289  17811   -642  -2371    757       N  
ATOM   2380  CA  ARG A 244     -39.091  45.742 -71.038  1.00181.85           C  
ANISOU 2380  CA  ARG A 244    27372  23751  17970   -690  -2493    696       C  
ATOM   2381  C   ARG A 244     -40.172  46.629 -71.688  1.00190.71           C  
ANISOU 2381  C   ARG A 244    28445  25048  18968   -557  -2686    846       C  
ATOM   2382  O   ARG A 244     -40.950  46.143 -72.513  1.00192.24           O  
ANISOU 2382  O   ARG A 244    28594  25463  18983   -646  -2798    839       O  
ATOM   2383  CB  ARG A 244     -39.486  45.360 -69.592  1.00180.49           C  
ANISOU 2383  CB  ARG A 244    27020  23562  17995   -643  -2468    607       C  
ATOM   2384  CG  ARG A 244     -40.831  44.639 -69.435  1.00190.75           C  
ANISOU 2384  CG  ARG A 244    28124  25110  19242   -693  -2591    547       C  
ATOM   2385  CD  ARG A 244     -41.192  44.405 -67.974  1.00197.66           C  
ANISOU 2385  CD  ARG A 244    28826  25961  20314   -630  -2561    477       C  
ATOM   2386  NE  ARG A 244     -41.636  45.628 -67.298  1.00203.61           N  
ANISOU 2386  NE  ARG A 244    29492  26690  21180   -385  -2630    589       N  
ATOM   2387  CZ  ARG A 244     -42.904  45.923 -67.026  1.00216.22           C  
ANISOU 2387  CZ  ARG A 244    30901  28488  22765   -269  -2771    637       C  
ATOM   2388  NH1 ARG A 244     -43.876  45.085 -67.364  1.00205.26           N1+
ANISOU 2388  NH1 ARG A 244    29377  27355  21257   -394  -2866    583       N1+
ATOM   2389  NH2 ARG A 244     -43.210  47.056 -66.409  1.00200.48           N  
ANISOU 2389  NH2 ARG A 244    28855  26445  20873    -30  -2816    736       N  
ATOM   2390  N   LEU A 245     -40.186  47.935 -71.330  1.00189.04           N  
ANISOU 2390  N   LEU A 245    28253  24731  18842   -343  -2723    980       N  
ATOM   2391  CA  LEU A 245     -41.107  48.951 -71.849  1.00191.75           C  
ANISOU 2391  CA  LEU A 245    28572  25200  19087   -165  -2894   1142       C  
ATOM   2392  C   LEU A 245     -40.810  49.270 -73.323  1.00198.97           C  
ANISOU 2392  C   LEU A 245    29668  26150  19783   -224  -2935   1243       C  
ATOM   2393  O   LEU A 245     -41.719  49.674 -74.050  1.00200.80           O  
ANISOU 2393  O   LEU A 245    29862  26570  19863   -145  -3096   1349       O  
ATOM   2394  CB  LEU A 245     -41.013  50.228 -70.989  1.00191.47           C  
ANISOU 2394  CB  LEU A 245    28553  24983  19213     76  -2890   1245       C  
ATOM   2395  CG  LEU A 245     -42.202  51.193 -71.012  1.00198.17           C  
ANISOU 2395  CG  LEU A 245    29310  25963  20024    321  -3064   1386       C  
ATOM   2396  CD1 LEU A 245     -43.362  50.670 -70.169  1.00198.23           C  
ANISOU 2396  CD1 LEU A 245    29044  26176  20099    376  -3142   1312       C  
ATOM   2397  CD2 LEU A 245     -41.788  52.555 -70.497  1.00200.67           C  
ANISOU 2397  CD2 LEU A 245    29752  26036  20458    534  -3034   1502       C  
ATOM   2398  N   LEU A 246     -39.542  49.088 -73.755  1.00195.80           N  
ANISOU 2398  N   LEU A 246    29455  25580  19361   -360  -2789   1212       N  
ATOM   2399  CA  LEU A 246     -39.075  49.322 -75.125  1.00197.53           C  
ANISOU 2399  CA  LEU A 246    29863  25812  19376   -440  -2794   1294       C  
ATOM   2400  C   LEU A 246     -39.649  48.276 -76.083  1.00204.19           C  
ANISOU 2400  C   LEU A 246    30671  26902  20012   -615  -2867   1221       C  
ATOM   2401  O   LEU A 246     -39.947  48.606 -77.234  1.00205.77           O  
ANISOU 2401  O   LEU A 246    30953  27224  20007   -622  -2967   1323       O  
ATOM   2402  CB  LEU A 246     -37.541  49.286 -75.167  1.00196.08           C  
ANISOU 2402  CB  LEU A 246    29859  25399  19243   -547  -2598   1258       C  
ATOM   2403  CG  LEU A 246     -36.879  50.042 -76.304  1.00201.91           C  
ANISOU 2403  CG  LEU A 246    30816  26074  19827   -566  -2583   1391       C  
ATOM   2404  CD1 LEU A 246     -36.372  51.396 -75.832  1.00201.82           C  
ANISOU 2404  CD1 LEU A 246    30907  25841  19933   -411  -2552   1525       C  
ATOM   2405  CD2 LEU A 246     -35.745  49.232 -76.894  1.00203.57           C  
ANISOU 2405  CD2 LEU A 246    31150  26239  19960   -774  -2422   1294       C  
ATOM   2406  N   SER A 247     -39.804  47.019 -75.594  1.00200.80           N  
ANISOU 2406  N   SER A 247    30128  26539  19630   -759  -2817   1046       N  
ATOM   2407  CA  SER A 247     -40.336  45.853 -76.312  1.00202.18           C  
ANISOU 2407  CA  SER A 247    30267  26925  19627   -957  -2868    940       C  
ATOM   2408  C   SER A 247     -39.642  45.618 -77.668  1.00208.18           C  
ANISOU 2408  C   SER A 247    31235  27689  20174  -1105  -2820    946       C  
ATOM   2409  O   SER A 247     -40.275  45.666 -78.730  1.00209.90           O  
ANISOU 2409  O   SER A 247    31475  28103  20175  -1146  -2952   1008       O  
ATOM   2410  CB  SER A 247     -41.857  45.929 -76.445  1.00207.70           C  
ANISOU 2410  CB  SER A 247    30776  27906  20233   -896  -3079    991       C  
ATOM   2411  OG  SER A 247     -42.486  45.887 -75.175  1.00215.22           O  
ANISOU 2411  OG  SER A 247    31524  28876  21373   -796  -3102    951       O  
ATOM   2412  N   GLY A 248     -38.332  45.394 -77.596  1.00203.86           N  
ANISOU 2412  N   GLY A 248    30835  26934  19690  -1175  -2630    886       N  
ATOM   2413  CA  GLY A 248     -37.482  45.133 -78.752  1.00204.57           C  
ANISOU 2413  CA  GLY A 248    31126  27000  19600  -1313  -2543    877       C  
ATOM   2414  C   GLY A 248     -37.094  43.672 -78.825  1.00207.57           C  
ANISOU 2414  C   GLY A 248    31541  27386  19939  -1514  -2425    679       C  
ATOM   2415  O   GLY A 248     -37.491  42.966 -79.758  1.00208.67           O  
ANISOU 2415  O   GLY A 248    31729  27685  19871  -1662  -2479    622       O  
ATOM   2416  N   SER A 249     -36.322  43.211 -77.820  1.00201.61           N  
ANISOU 2416  N   SER A 249    30769  26455  19381  -1518  -2263    573       N  
ATOM   2417  CA  SER A 249     -35.863  41.828 -77.687  1.00200.31           C  
ANISOU 2417  CA  SER A 249    30645  26252  19212  -1678  -2128    384       C  
ATOM   2418  C   SER A 249     -35.536  41.488 -76.227  1.00200.69           C  
ANISOU 2418  C   SER A 249    30587  26151  19516  -1623  -2023    297       C  
ATOM   2419  O   SER A 249     -34.536  41.963 -75.679  1.00198.71           O  
ANISOU 2419  O   SER A 249    30370  25723  19409  -1541  -1896    326       O  
ATOM   2420  CB  SER A 249     -34.666  41.552 -78.598  1.00204.32           C  
ANISOU 2420  CB  SER A 249    31360  26683  19591  -1773  -1975    354       C  
ATOM   2421  OG  SER A 249     -34.288  40.185 -78.573  1.00212.57           O  
ANISOU 2421  OG  SER A 249    32463  27697  20606  -1915  -1851    170       O  
ATOM   2422  N   LYS A 250     -36.400  40.670 -75.602  1.00196.12           N  
ANISOU 2422  N   LYS A 250    29877  25654  18985  -1678  -2080    194       N  
ATOM   2423  CA  LYS A 250     -36.225  40.182 -74.233  1.00193.45           C  
ANISOU 2423  CA  LYS A 250    29436  25198  18868  -1646  -1990     99       C  
ATOM   2424  C   LYS A 250     -35.499  38.810 -74.288  1.00196.48           C  
ANISOU 2424  C   LYS A 250    29937  25498  19220  -1798  -1827    -73       C  
ATOM   2425  O   LYS A 250     -35.345  38.138 -73.264  1.00194.70           O  
ANISOU 2425  O   LYS A 250    29653  25179  19144  -1803  -1742   -173       O  
ATOM   2426  CB  LYS A 250     -37.591  40.114 -73.505  1.00195.56           C  
ANISOU 2426  CB  LYS A 250    29496  25608  19200  -1617  -2141     95       C  
ATOM   2427  CG  LYS A 250     -37.526  40.022 -71.972  1.00200.84           C  
ANISOU 2427  CG  LYS A 250    30032  26161  20118  -1530  -2078     47       C  
ATOM   2428  CD  LYS A 250     -37.168  41.336 -71.274  1.00204.56           C  
ANISOU 2428  CD  LYS A 250    30453  26512  20759  -1322  -2072    174       C  
ATOM   2429  CE  LYS A 250     -36.939  41.124 -69.796  1.00205.85           C  
ANISOU 2429  CE  LYS A 250    30510  26551  21154  -1258  -1986    109       C  
ATOM   2430  NZ  LYS A 250     -36.565  42.384 -69.105  1.00209.01           N  
ANISOU 2430  NZ  LYS A 250    30878  26826  21712  -1070  -1977    220       N  
ATOM   2431  N   GLU A 251     -35.013  38.433 -75.499  1.00193.90           N  
ANISOU 2431  N   GLU A 251    29787  25196  18691  -1909  -1776   -103       N  
ATOM   2432  CA  GLU A 251     -34.281  37.196 -75.798  1.00193.32           C  
ANISOU 2432  CA  GLU A 251    29864  25046  18544  -2041  -1618   -258       C  
ATOM   2433  C   GLU A 251     -32.927  37.114 -75.076  1.00194.36           C  
ANISOU 2433  C   GLU A 251    30036  24970  18840  -1958  -1413   -292       C  
ATOM   2434  O   GLU A 251     -32.472  36.010 -74.763  1.00193.39           O  
ANISOU 2434  O   GLU A 251    29978  24761  18741  -2021  -1284   -432       O  
ATOM   2435  CB  GLU A 251     -34.092  37.032 -77.315  1.00196.60           C  
ANISOU 2435  CB  GLU A 251    30456  25548  18694  -2153  -1621   -259       C  
ATOM   2436  N   LYS A 252     -32.291  38.275 -74.816  1.00189.05           N  
ANISOU 2436  N   LYS A 252    29333  24223  18276  -1821  -1386   -164       N  
ATOM   2437  CA  LYS A 252     -31.007  38.370 -74.115  1.00186.70           C  
ANISOU 2437  CA  LYS A 252    29048  23754  18134  -1741  -1207   -175       C  
ATOM   2438  C   LYS A 252     -31.043  39.414 -72.968  1.00187.08           C  
ANISOU 2438  C   LYS A 252    28947  23729  18405  -1592  -1246    -75       C  
ATOM   2439  O   LYS A 252     -30.089  39.516 -72.189  1.00184.81           O  
ANISOU 2439  O   LYS A 252    28639  23312  18269  -1526  -1116    -86       O  
ATOM   2440  CB  LYS A 252     -29.856  38.623 -75.117  1.00190.18           C  
ANISOU 2440  CB  LYS A 252    29647  24168  18446  -1762  -1085   -138       C  
ATOM   2441  CG  LYS A 252     -28.459  38.198 -74.636  1.00202.97           C  
ANISOU 2441  CG  LYS A 252    31307  25652  20162  -1729   -868   -203       C  
ATOM   2442  CD  LYS A 252     -28.269  36.676 -74.532  1.00210.93           C  
ANISOU 2442  CD  LYS A 252    32384  26624  21135  -1801   -754   -382       C  
ATOM   2443  CE  LYS A 252     -26.881  36.287 -74.074  1.00217.11           C  
ANISOU 2443  CE  LYS A 252    33197  27290  22007  -1741   -541   -435       C  
ATOM   2444  NZ  LYS A 252     -26.629  36.645 -72.653  1.00220.46           N  
ANISOU 2444  NZ  LYS A 252    33467  27620  22678  -1630   -518   -409       N  
ATOM   2445  N   ASP A 253     -32.167  40.155 -72.850  1.00182.82           N  
ANISOU 2445  N   ASP A 253    28303  23282  17880  -1536  -1427     16       N  
ATOM   2446  CA  ASP A 253     -32.390  41.151 -71.798  1.00180.79           C  
ANISOU 2446  CA  ASP A 253    27914  22964  17816  -1388  -1482    107       C  
ATOM   2447  C   ASP A 253     -32.683  40.461 -70.464  1.00180.97           C  
ANISOU 2447  C   ASP A 253    27803  22942  18017  -1368  -1454      3       C  
ATOM   2448  O   ASP A 253     -32.422  41.035 -69.407  1.00179.07           O  
ANISOU 2448  O   ASP A 253    27477  22602  17962  -1257  -1426     37       O  
ATOM   2449  CB  ASP A 253     -33.542  42.092 -72.174  1.00184.00           C  
ANISOU 2449  CB  ASP A 253    28258  23495  18157  -1319  -1682    234       C  
ATOM   2450  N   ARG A 254     -33.220  39.224 -70.521  1.00176.29           N  
ANISOU 2450  N   ARG A 254    27205  22420  17359  -1486  -1459   -124       N  
ATOM   2451  CA  ARG A 254     -33.535  38.401 -69.354  1.00174.13           C  
ANISOU 2451  CA  ARG A 254    26826  22109  17226  -1496  -1428   -231       C  
ATOM   2452  C   ARG A 254     -32.262  37.880 -68.665  1.00174.98           C  
ANISOU 2452  C   ARG A 254    26985  22045  17455  -1475  -1232   -306       C  
ATOM   2453  O   ARG A 254     -32.311  37.542 -67.478  1.00173.58           O  
ANISOU 2453  O   ARG A 254    26710  21804  17439  -1435  -1195   -358       O  
ATOM   2454  CB  ARG A 254     -34.463  37.243 -69.745  1.00175.25           C  
ANISOU 2454  CB  ARG A 254    26976  22374  17236  -1654  -1491   -339       C  
ATOM   2455  N   SER A 255     -31.120  37.844 -69.400  1.00170.19           N  
ANISOU 2455  N   SER A 255    26522  21377  16767  -1496  -1107   -305       N  
ATOM   2456  CA  SER A 255     -29.808  37.407 -68.900  1.00168.20           C  
ANISOU 2456  CA  SER A 255    26316  20988  16605  -1464   -916   -364       C  
ATOM   2457  C   SER A 255     -29.218  38.390 -67.873  1.00169.14           C  
ANISOU 2457  C   SER A 255    26332  21013  16920  -1333   -883   -282       C  
ATOM   2458  O   SER A 255     -28.291  38.030 -67.142  1.00168.17           O  
ANISOU 2458  O   SER A 255    26197  20792  16908  -1294   -745   -331       O  
ATOM   2459  CB  SER A 255     -28.833  37.193 -70.053  1.00172.89           C  
ANISOU 2459  CB  SER A 255    27076  21576  17039  -1518   -801   -375       C  
ATOM   2460  OG  SER A 255     -27.571  36.740 -69.589  1.00180.77           O  
ANISOU 2460  OG  SER A 255    28104  22465  18114  -1476   -615   -430       O  
ATOM   2461  N   LEU A 256     -29.749  39.628 -67.831  1.00163.55           N  
ANISOU 2461  N   LEU A 256    25558  20336  16247  -1263  -1010   -157       N  
ATOM   2462  CA  LEU A 256     -29.342  40.659 -66.881  1.00160.84           C  
ANISOU 2462  CA  LEU A 256    25132  19902  16077  -1147   -999    -77       C  
ATOM   2463  C   LEU A 256     -30.342  40.711 -65.727  1.00162.11           C  
ANISOU 2463  C   LEU A 256    25139  20073  16381  -1080  -1096    -93       C  
ATOM   2464  O   LEU A 256     -29.964  41.105 -64.624  1.00160.90           O  
ANISOU 2464  O   LEU A 256    24908  19831  16396   -997  -1054    -83       O  
ATOM   2465  CB  LEU A 256     -29.199  42.030 -67.558  1.00161.60           C  
ANISOU 2465  CB  LEU A 256    25284  19998  16117  -1105  -1062     72       C  
ATOM   2466  CG  LEU A 256     -28.227  42.115 -68.746  1.00167.12           C  
ANISOU 2466  CG  LEU A 256    26135  20701  16663  -1176   -970    105       C  
ATOM   2467  CD1 LEU A 256     -28.370  43.439 -69.477  1.00168.45           C  
ANISOU 2467  CD1 LEU A 256    26368  20881  16753  -1145  -1062    260       C  
ATOM   2468  CD2 LEU A 256     -26.780  41.881 -68.317  1.00168.31           C  
ANISOU 2468  CD2 LEU A 256    26302  20757  16890  -1178   -783     66       C  
ATOM   2469  N   ARG A 257     -31.603  40.267 -65.969  1.00157.45           N  
ANISOU 2469  N   ARG A 257    24500  19605  15717  -1124  -1221   -123       N  
ATOM   2470  CA  ARG A 257     -32.681  40.183 -64.970  1.00155.66           C  
ANISOU 2470  CA  ARG A 257    24116  19427  15600  -1078  -1315   -145       C  
ATOM   2471  C   ARG A 257     -32.337  39.145 -63.889  1.00153.78           C  
ANISOU 2471  C   ARG A 257    23833  19113  15485  -1102  -1203   -265       C  
ATOM   2472  O   ARG A 257     -32.770  39.284 -62.742  1.00151.47           O  
ANISOU 2472  O   ARG A 257    23410  18804  15336  -1032  -1231   -272       O  
ATOM   2473  CB  ARG A 257     -34.041  39.883 -65.646  1.00159.23           C  
ANISOU 2473  CB  ARG A 257    24529  20059  15912  -1147  -1469   -149       C  
ATOM   2474  CG  ARG A 257     -35.260  39.805 -64.702  1.00174.85           C  
ANISOU 2474  CG  ARG A 257    26327  22129  17981  -1108  -1576   -166       C  
ATOM   2475  CD  ARG A 257     -35.668  41.145 -64.101  1.00189.08           C  
ANISOU 2475  CD  ARG A 257    28023  23928  19893   -932  -1665    -50       C  
ATOM   2476  NE  ARG A 257     -36.361  40.987 -62.818  1.00200.25           N  
ANISOU 2476  NE  ARG A 257    29270  25366  21450   -875  -1693    -90       N  
ATOM   2477  CZ  ARG A 257     -37.683  41.010 -62.661  1.00217.35           C  
ANISOU 2477  CZ  ARG A 257    31291  27701  23591   -856  -1828    -77       C  
ATOM   2478  NH1 ARG A 257     -38.482  41.184 -63.707  1.00208.14           N  
ANISOU 2478  NH1 ARG A 257    30121  26701  22263   -887  -1957    -23       N  
ATOM   2479  NH2 ARG A 257     -38.216  40.859 -61.456  1.00202.64           N1+
ANISOU 2479  NH2 ARG A 257    29278  25856  21860   -806  -1835   -115       N1+
ATOM   2480  N   ARG A 258     -31.532  38.126 -64.254  1.00147.81           N  
ANISOU 2480  N   ARG A 258    23191  18304  14666  -1190  -1072   -356       N  
ATOM   2481  CA  ARG A 258     -31.067  37.102 -63.321  1.00145.03           C  
ANISOU 2481  CA  ARG A 258    22826  17864  14414  -1203   -951   -463       C  
ATOM   2482  C   ARG A 258     -30.020  37.683 -62.351  1.00142.74           C  
ANISOU 2482  C   ARG A 258    22488  17455  14292  -1088   -852   -428       C  
ATOM   2483  O   ARG A 258     -29.950  37.243 -61.198  1.00141.03           O  
ANISOU 2483  O   ARG A 258    22196  17182  14208  -1053   -804   -480       O  
ATOM   2484  CB  ARG A 258     -30.572  35.832 -64.056  1.00146.69           C  
ANISOU 2484  CB  ARG A 258    23190  18053  14493  -1315   -842   -570       C  
ATOM   2485  CG  ARG A 258     -29.281  35.982 -64.870  1.00158.54           C  
ANISOU 2485  CG  ARG A 258    24820  19500  15917  -1304   -718   -550       C  
ATOM   2486  CD  ARG A 258     -28.582  34.651 -65.121  1.00170.31           C  
ANISOU 2486  CD  ARG A 258    26444  20929  17338  -1362   -568   -670       C  
ATOM   2487  NE  ARG A 258     -28.123  34.011 -63.881  1.00177.28           N  
ANISOU 2487  NE  ARG A 258    27277  21711  18372  -1303   -466   -734       N  
ATOM   2488  CZ  ARG A 258     -26.933  34.211 -63.321  1.00189.64           C  
ANISOU 2488  CZ  ARG A 258    28819  23198  20038  -1205   -340   -716       C  
ATOM   2489  NH1 ARG A 258     -26.055  35.034 -63.884  1.00176.91           N1+
ANISOU 2489  NH1 ARG A 258    27228  21596  18394  -1167   -294   -639       N1+
ATOM   2490  NH2 ARG A 258     -26.610  33.589 -62.195  1.00174.63           N  
ANISOU 2490  NH2 ARG A 258    26871  21218  18263  -1150   -261   -771       N  
ATOM   2491  N   ILE A 259     -29.241  38.696 -62.818  1.00136.06           N  
ANISOU 2491  N   ILE A 259    21687  16577  13432  -1041   -828   -334       N  
ATOM   2492  CA  ILE A 259     -28.207  39.399 -62.043  1.00133.28           C  
ANISOU 2492  CA  ILE A 259    21297  16127  13215   -955   -744   -289       C  
ATOM   2493  C   ILE A 259     -28.843  40.319 -60.978  1.00132.39           C  
ANISOU 2493  C   ILE A 259    21055  15996  13251   -859   -840   -233       C  
ATOM   2494  O   ILE A 259     -28.324  40.389 -59.865  1.00130.37           O  
ANISOU 2494  O   ILE A 259    20730  15666  13138   -802   -776   -250       O  
ATOM   2495  CB  ILE A 259     -27.166  40.128 -62.960  1.00136.95           C  
ANISOU 2495  CB  ILE A 259    21864  16573  13598   -966   -682   -210       C  
ATOM   2496  CG1 ILE A 259     -26.259  39.120 -63.726  1.00137.99           C  
ANISOU 2496  CG1 ILE A 259    22108  16708  13612  -1036   -540   -283       C  
ATOM   2497  CG2 ILE A 259     -26.321  41.177 -62.206  1.00136.94           C  
ANISOU 2497  CG2 ILE A 259    21815  16489  13727   -894   -637   -137       C  
ATOM   2498  CD1 ILE A 259     -25.193  38.240 -62.858  1.00144.75           C  
ANISOU 2498  CD1 ILE A 259    22938  17495  14564  -1003   -372   -370       C  
ATOM   2499  N   THR A 260     -29.960  40.996 -61.310  1.00127.14           N  
ANISOU 2499  N   THR A 260    20358  15404  12544   -833   -992   -167       N  
ATOM   2500  CA  THR A 260     -30.661  41.884 -60.377  1.00125.25           C  
ANISOU 2500  CA  THR A 260    20004  15156  12429   -724  -1087   -114       C  
ATOM   2501  C   THR A 260     -31.425  41.065 -59.327  1.00127.76           C  
ANISOU 2501  C   THR A 260    20196  15509  12836   -720  -1104   -202       C  
ATOM   2502  O   THR A 260     -31.490  41.495 -58.174  1.00126.47           O  
ANISOU 2502  O   THR A 260    19940  15297  12817   -633  -1106   -196       O  
ATOM   2503  CB  THR A 260     -31.518  42.962 -61.086  1.00128.68           C  
ANISOU 2503  CB  THR A 260    20450  15656  12785   -670  -1235     -3       C  
ATOM   2504  OG1 THR A 260     -32.889  42.576 -61.161  1.00128.01           O  
ANISOU 2504  OG1 THR A 260    20277  15709  12653   -676  -1358    -25       O  
ATOM   2505  CG2 THR A 260     -30.989  43.346 -62.452  1.00125.49           C  
ANISOU 2505  CG2 THR A 260    20193  15258  12231   -723  -1226     66       C  
ATOM   2506  N   ARG A 261     -31.959  39.871 -59.708  1.00124.18           N  
ANISOU 2506  N   ARG A 261    19752  15137  12294   -824  -1111   -287       N  
ATOM   2507  CA  ARG A 261     -32.664  38.960 -58.787  1.00123.05           C  
ANISOU 2507  CA  ARG A 261    19508  15028  12217   -852  -1118   -374       C  
ATOM   2508  C   ARG A 261     -31.677  38.440 -57.747  1.00124.21           C  
ANISOU 2508  C   ARG A 261    19651  15053  12492   -829   -976   -435       C  
ATOM   2509  O   ARG A 261     -32.049  38.248 -56.593  1.00123.14           O  
ANISOU 2509  O   ARG A 261    19408  14908  12471   -790   -979   -467       O  
ATOM   2510  CB  ARG A 261     -33.321  37.789 -59.532  1.00125.54           C  
ANISOU 2510  CB  ARG A 261    19870  15439  12391   -996  -1143   -452       C  
ATOM   2511  CG  ARG A 261     -34.648  38.133 -60.198  1.00141.93           C  
ANISOU 2511  CG  ARG A 261    21886  17683  14360  -1022  -1310   -406       C  
ATOM   2512  CD  ARG A 261     -35.295  36.900 -60.808  1.00159.58           C  
ANISOU 2512  CD  ARG A 261    24162  20014  16456  -1191  -1333   -496       C  
ATOM   2513  NE  ARG A 261     -36.128  37.216 -61.974  1.00175.29           N  
ANISOU 2513  NE  ARG A 261    26159  22162  18282  -1243  -1468   -446       N  
ATOM   2514  CZ  ARG A 261     -37.436  37.462 -61.929  1.00191.70           C  
ANISOU 2514  CZ  ARG A 261    28096  24412  20328  -1243  -1616   -414       C  
ATOM   2515  NH1 ARG A 261     -38.083  37.448 -60.769  1.00179.91           N  
ANISOU 2515  NH1 ARG A 261    26443  22955  18958  -1193  -1645   -429       N  
ATOM   2516  NH2 ARG A 261     -38.106  37.729 -63.043  1.00178.56           N1+
ANISOU 2516  NH2 ARG A 261    26443  22900  18502  -1287  -1737   -364       N1+
ATOM   2517  N   MET A 262     -30.407  38.264 -58.160  1.00120.02           N  
ANISOU 2517  N   MET A 262    19229  14439  11934   -845   -852   -443       N  
ATOM   2518  CA  MET A 262     -29.281  37.849 -57.329  1.00118.71           C  
ANISOU 2518  CA  MET A 262    19066  14171  11869   -811   -711   -486       C  
ATOM   2519  C   MET A 262     -28.898  38.989 -56.352  1.00118.31           C  
ANISOU 2519  C   MET A 262    18926  14063  11964   -703   -717   -420       C  
ATOM   2520  O   MET A 262     -28.428  38.699 -55.251  1.00116.82           O  
ANISOU 2520  O   MET A 262    18678  13818  11891   -662   -646   -457       O  
ATOM   2521  CB  MET A 262     -28.101  37.450 -58.235  1.00122.43           C  
ANISOU 2521  CB  MET A 262    19669  14605  12243   -852   -589   -500       C  
ATOM   2522  CG  MET A 262     -26.988  36.657 -57.542  1.00126.61           C  
ANISOU 2522  CG  MET A 262    20210  15055  12840   -824   -434   -563       C  
ATOM   2523  SD  MET A 262     -25.656  37.646 -56.769  1.00131.20           S  
ANISOU 2523  SD  MET A 262    20726  15576  13549   -730   -352   -496       S  
ATOM   2524  CE  MET A 262     -25.181  38.801 -58.177  1.00129.10           C  
ANISOU 2524  CE  MET A 262    20548  15340  13163   -763   -374   -393       C  
ATOM   2525  N   VAL A 263     -29.109  40.274 -56.745  1.00113.03           N  
ANISOU 2525  N   VAL A 263    18258  13404  11283   -657   -803   -322       N  
ATOM   2526  CA  VAL A 263     -28.843  41.448 -55.891  1.00111.24           C  
ANISOU 2526  CA  VAL A 263    17975  13113  11180   -563   -820   -259       C  
ATOM   2527  C   VAL A 263     -29.883  41.469 -54.760  1.00113.45           C  
ANISOU 2527  C   VAL A 263    18124  13418  11564   -497   -895   -284       C  
ATOM   2528  O   VAL A 263     -29.534  41.759 -53.619  1.00111.92           O  
ANISOU 2528  O   VAL A 263    17866  13163  11497   -437   -859   -292       O  
ATOM   2529  CB  VAL A 263     -28.747  42.788 -56.680  1.00115.40           C  
ANISOU 2529  CB  VAL A 263    18574  13622  11652   -535   -882   -146       C  
ATOM   2530  CG1 VAL A 263     -28.539  43.988 -55.754  1.00114.29           C  
ANISOU 2530  CG1 VAL A 263    18396  13395  11634   -444   -902    -89       C  
ATOM   2531  CG2 VAL A 263     -27.624  42.722 -57.702  1.00115.74           C  
ANISOU 2531  CG2 VAL A 263    18735  13645  11594   -609   -790   -124       C  
ATOM   2532  N   LEU A 264     -31.138  41.080 -55.065  1.00109.92           N  
ANISOU 2532  N   LEU A 264    17633  13076  11055   -520   -994   -301       N  
ATOM   2533  CA  LEU A 264     -32.196  40.961 -54.063  1.00108.65           C  
ANISOU 2533  CA  LEU A 264    17336  12971  10975   -472  -1060   -330       C  
ATOM   2534  C   LEU A 264     -31.841  39.819 -53.111  1.00108.19           C  
ANISOU 2534  C   LEU A 264    17240  12876  10990   -513   -960   -425       C  
ATOM   2535  O   LEU A 264     -32.050  39.954 -51.906  1.00107.86           O  
ANISOU 2535  O   LEU A 264    17100  12817  11065   -449   -958   -442       O  
ATOM   2536  CB  LEU A 264     -33.568  40.715 -54.717  1.00110.25           C  
ANISOU 2536  CB  LEU A 264    17493  13324  11075   -510  -1184   -327       C  
ATOM   2537  CG  LEU A 264     -34.808  40.862 -53.811  1.00115.42           C  
ANISOU 2537  CG  LEU A 264    17986  14072  11795   -444  -1275   -333       C  
ATOM   2538  CD1 LEU A 264     -34.944  42.278 -53.248  1.00115.44           C  
ANISOU 2538  CD1 LEU A 264    17943  14032  11886   -282  -1327   -254       C  
ATOM   2539  CD2 LEU A 264     -36.068  40.485 -54.555  1.00119.89           C  
ANISOU 2539  CD2 LEU A 264    18500  14814  12240   -506  -1390   -334       C  
ATOM   2540  N   VAL A 265     -31.254  38.725 -53.644  1.00101.09           N  
ANISOU 2540  N   VAL A 265    16432  11958  10020   -610   -871   -485       N  
ATOM   2541  CA  VAL A 265     -30.809  37.568 -52.851  1.00 98.89           C  
ANISOU 2541  CA  VAL A 265    16151  11628   9794   -642   -764   -571       C  
ATOM   2542  C   VAL A 265     -29.732  37.998 -51.830  1.00 98.49           C  
ANISOU 2542  C   VAL A 265    16067  11482   9872   -556   -677   -557       C  
ATOM   2543  O   VAL A 265     -29.917  37.769 -50.633  1.00 95.84           O  
ANISOU 2543  O   VAL A 265    15644  11131   9638   -519   -663   -588       O  
ATOM   2544  CB  VAL A 265     -30.389  36.368 -53.751  1.00103.18           C  
ANISOU 2544  CB  VAL A 265    16827  12159  10219   -748   -685   -634       C  
ATOM   2545  CG1 VAL A 265     -29.547  35.347 -52.992  1.00102.37           C  
ANISOU 2545  CG1 VAL A 265    16754  11970  10174   -744   -550   -703       C  
ATOM   2546  CG2 VAL A 265     -31.609  35.698 -54.371  1.00103.86           C  
ANISOU 2546  CG2 VAL A 265    16923  12345  10195   -855   -772   -673       C  
ATOM   2547  N   VAL A 266     -28.661  38.686 -52.310  1.00 94.38           N  
ANISOU 2547  N   VAL A 266    15611  10911   9340   -533   -627   -506       N  
ATOM   2548  CA  VAL A 266     -27.548  39.234 -51.513  1.00 92.97           C  
ANISOU 2548  CA  VAL A 266    15403  10660   9262   -472   -551   -483       C  
ATOM   2549  C   VAL A 266     -28.056  40.188 -50.396  1.00 96.55           C  
ANISOU 2549  C   VAL A 266    15753  11099   9834   -389   -622   -453       C  
ATOM   2550  O   VAL A 266     -27.594  40.079 -49.256  1.00 94.17           O  
ANISOU 2550  O   VAL A 266    15388  10758   9632   -350   -568   -478       O  
ATOM   2551  CB  VAL A 266     -26.463  39.913 -52.410  1.00 96.38           C  
ANISOU 2551  CB  VAL A 266    15920  11064   9634   -488   -501   -423       C  
ATOM   2552  CG1 VAL A 266     -25.418  40.666 -51.585  1.00 95.13           C  
ANISOU 2552  CG1 VAL A 266    15720  10849   9574   -443   -444   -390       C  
ATOM   2553  CG2 VAL A 266     -25.782  38.905 -53.318  1.00 96.58           C  
ANISOU 2553  CG2 VAL A 266    16041  11101   9552   -550   -403   -464       C  
ATOM   2554  N   VAL A 267     -29.011  41.089 -50.715  1.00 95.34           N  
ANISOU 2554  N   VAL A 267    15584  10979   9662   -355   -741   -399       N  
ATOM   2555  CA  VAL A 267     -29.510  42.052 -49.731  1.00 96.44           C  
ANISOU 2555  CA  VAL A 267    15643  11099   9903   -261   -805   -371       C  
ATOM   2556  C   VAL A 267     -30.365  41.363 -48.621  1.00100.39           C  
ANISOU 2556  C   VAL A 267    16024  11647  10472   -237   -822   -435       C  
ATOM   2557  O   VAL A 267     -30.155  41.677 -47.448  1.00 99.41           O  
ANISOU 2557  O   VAL A 267    15837  11481  10452   -178   -798   -448       O  
ATOM   2558  CB  VAL A 267     -30.190  43.313 -50.353  1.00102.29           C  
ANISOU 2558  CB  VAL A 267    16413  11848  10604   -201   -919   -287       C  
ATOM   2559  CG1 VAL A 267     -31.634  43.060 -50.790  1.00102.98           C  
ANISOU 2559  CG1 VAL A 267    16445  12055  10628   -192  -1030   -287       C  
ATOM   2560  CG2 VAL A 267     -30.101  44.509 -49.401  1.00102.15           C  
ANISOU 2560  CG2 VAL A 267    16371  11753  10690   -102   -941   -251       C  
ATOM   2561  N   VAL A 268     -31.255  40.405 -48.976  1.00 97.14           N  
ANISOU 2561  N   VAL A 268    15588  11325   9996   -298   -855   -478       N  
ATOM   2562  CA  VAL A 268     -32.101  39.661 -48.024  1.00 96.08           C  
ANISOU 2562  CA  VAL A 268    15347  11249   9909   -304   -868   -537       C  
ATOM   2563  C   VAL A 268     -31.221  38.794 -47.108  1.00 96.05           C  
ANISOU 2563  C   VAL A 268    15347  11175   9974   -323   -748   -595       C  
ATOM   2564  O   VAL A 268     -31.410  38.816 -45.892  1.00 94.37           O  
ANISOU 2564  O   VAL A 268    15046  10958   9853   -274   -739   -616       O  
ATOM   2565  CB  VAL A 268     -33.209  38.844 -48.748  1.00101.82           C  
ANISOU 2565  CB  VAL A 268    16062  12094  10533   -395   -932   -566       C  
ATOM   2566  CG1 VAL A 268     -33.999  37.977 -47.770  1.00101.53           C  
ANISOU 2566  CG1 VAL A 268    15924  12117  10537   -430   -930   -628       C  
ATOM   2567  CG2 VAL A 268     -34.156  39.766 -49.516  1.00102.97           C  
ANISOU 2567  CG2 VAL A 268    16177  12333  10615   -353  -1062   -500       C  
ATOM   2568  N   ALA A 269     -30.239  38.071 -47.689  1.00 91.29           N  
ANISOU 2568  N   ALA A 269    14846  10521   9320   -382   -655   -617       N  
ATOM   2569  CA  ALA A 269     -29.292  37.245 -46.937  1.00 89.76           C  
ANISOU 2569  CA  ALA A 269    14665  10262   9177   -381   -536   -662       C  
ATOM   2570  C   ALA A 269     -28.508  38.089 -45.920  1.00 92.81           C  
ANISOU 2570  C   ALA A 269    14993  10598   9673   -295   -505   -633       C  
ATOM   2571  O   ALA A 269     -28.418  37.696 -44.762  1.00 92.21           O  
ANISOU 2571  O   ALA A 269    14855  10508   9673   -265   -467   -665       O  
ATOM   2572  CB  ALA A 269     -28.346  36.518 -47.878  1.00 90.61           C  
ANISOU 2572  CB  ALA A 269    14895  10333   9199   -433   -445   -679       C  
ATOM   2573  N   PHE A 270     -28.009  39.275 -46.338  1.00 89.17           N  
ANISOU 2573  N   PHE A 270    14557  10111   9213   -264   -528   -572       N  
ATOM   2574  CA  PHE A 270     -27.261  40.223 -45.500  1.00 87.66           C  
ANISOU 2574  CA  PHE A 270    14328   9869   9109   -205   -508   -543       C  
ATOM   2575  C   PHE A 270     -28.135  40.706 -44.338  1.00 91.22           C  
ANISOU 2575  C   PHE A 270    14682  10331   9647   -139   -573   -552       C  
ATOM   2576  O   PHE A 270     -27.657  40.764 -43.198  1.00 89.93           O  
ANISOU 2576  O   PHE A 270    14465  10140   9564   -103   -531   -571       O  
ATOM   2577  CB  PHE A 270     -26.752  41.411 -46.341  1.00 89.78           C  
ANISOU 2577  CB  PHE A 270    14667  10104   9341   -209   -532   -472       C  
ATOM   2578  CG  PHE A 270     -25.843  42.385 -45.619  1.00 91.37           C  
ANISOU 2578  CG  PHE A 270    14855  10248   9615   -182   -504   -442       C  
ATOM   2579  CD1 PHE A 270     -24.467  42.183 -45.581  1.00 94.43           C  
ANISOU 2579  CD1 PHE A 270    15255  10624  10000   -218   -404   -440       C  
ATOM   2580  CD2 PHE A 270     -26.360  43.527 -45.005  1.00 93.02           C  
ANISOU 2580  CD2 PHE A 270    15042  10420   9883   -122   -579   -416       C  
ATOM   2581  CE1 PHE A 270     -23.628  43.093 -44.921  1.00 94.61           C  
ANISOU 2581  CE1 PHE A 270    15261  10609  10079   -216   -383   -414       C  
ATOM   2582  CE2 PHE A 270     -25.521  44.430 -44.350  1.00 95.11           C  
ANISOU 2582  CE2 PHE A 270    15312  10622  10202   -116   -554   -395       C  
ATOM   2583  CZ  PHE A 270     -24.162  44.205 -44.312  1.00 92.99           C  
ANISOU 2583  CZ  PHE A 270    15049  10352   9929   -174   -459   -394       C  
ATOM   2584  N   VAL A 271     -29.419  41.027 -44.623  1.00 87.94           N  
ANISOU 2584  N   VAL A 271    14238   9968   9208   -117   -674   -540       N  
ATOM   2585  CA  VAL A 271     -30.354  41.469 -43.591  1.00 87.26           C  
ANISOU 2585  CA  VAL A 271    14053   9912   9192    -42   -734   -550       C  
ATOM   2586  C   VAL A 271     -30.634  40.336 -42.600  1.00 91.60           C  
ANISOU 2586  C   VAL A 271    14524  10498   9780    -64   -689   -616       C  
ATOM   2587  O   VAL A 271     -30.363  40.522 -41.425  1.00 90.67           O  
ANISOU 2587  O   VAL A 271    14352  10355   9743    -16   -659   -633       O  
ATOM   2588  CB  VAL A 271     -31.655  42.097 -44.138  1.00 91.44           C  
ANISOU 2588  CB  VAL A 271    14554  10512   9679      4   -852   -515       C  
ATOM   2589  CG1 VAL A 271     -32.629  42.422 -43.000  1.00 91.25           C  
ANISOU 2589  CG1 VAL A 271    14412  10537   9723     92   -899   -534       C  
ATOM   2590  CG2 VAL A 271     -31.361  43.344 -44.963  1.00 91.53           C  
ANISOU 2590  CG2 VAL A 271    14654  10465   9657     43   -897   -441       C  
ATOM   2591  N   VAL A 272     -31.107  39.158 -43.078  1.00 89.04           N  
ANISOU 2591  N   VAL A 272    14211  10229   9393   -145   -679   -651       N  
ATOM   2592  CA  VAL A 272     -31.462  37.996 -42.240  1.00 88.17           C  
ANISOU 2592  CA  VAL A 272    14049  10147   9304   -184   -637   -709       C  
ATOM   2593  C   VAL A 272     -30.292  37.515 -41.352  1.00 91.07           C  
ANISOU 2593  C   VAL A 272    14433  10439   9731   -168   -530   -732       C  
ATOM   2594  O   VAL A 272     -30.543  37.142 -40.205  1.00 91.54           O  
ANISOU 2594  O   VAL A 272    14424  10510   9847   -149   -510   -761       O  
ATOM   2595  CB  VAL A 272     -32.122  36.809 -43.010  1.00 92.35           C  
ANISOU 2595  CB  VAL A 272    14618  10731   9739   -297   -644   -745       C  
ATOM   2596  CG1 VAL A 272     -33.419  37.227 -43.705  1.00 92.80           C  
ANISOU 2596  CG1 VAL A 272    14624  10901   9736   -315   -761   -724       C  
ATOM   2597  CG2 VAL A 272     -31.167  36.155 -43.995  1.00 92.49           C  
ANISOU 2597  CG2 VAL A 272    14771  10684   9686   -358   -571   -754       C  
ATOM   2598  N   CYS A 273     -29.037  37.564 -41.858  1.00 85.75           N  
ANISOU 2598  N   CYS A 273    13839   9701   9040   -171   -464   -714       N  
ATOM   2599  CA  CYS A 273     -27.833  37.137 -41.130  1.00 84.70           C  
ANISOU 2599  CA  CYS A 273    13712   9518   8952   -146   -363   -727       C  
ATOM   2600  C   CYS A 273     -27.336  38.139 -40.068  1.00 87.49           C  
ANISOU 2600  C   CYS A 273    13996   9853   9394    -76   -367   -707       C  
ATOM   2601  O   CYS A 273     -26.944  37.734 -38.967  1.00 87.29           O  
ANISOU 2601  O   CYS A 273    13923   9822   9420    -48   -317   -728       O  
ATOM   2602  CB  CYS A 273     -26.716  36.788 -42.110  1.00 85.47           C  
ANISOU 2602  CB  CYS A 273    13907   9582   8987   -173   -288   -716       C  
ATOM   2603  SG  CYS A 273     -27.032  35.317 -43.118  1.00 90.10           S  
ANISOU 2603  SG  CYS A 273    14602  10165   9466   -253   -247   -760       S  
ATOM   2604  N   TRP A 274     -27.316  39.434 -40.425  1.00 82.97           N  
ANISOU 2604  N   TRP A 274    13430   9266   8828    -53   -424   -664       N  
ATOM   2605  CA  TRP A 274     -26.792  40.522 -39.611  1.00 81.71           C  
ANISOU 2605  CA  TRP A 274    13237   9073   8735     -5   -431   -645       C  
ATOM   2606  C   TRP A 274     -27.793  41.216 -38.699  1.00 85.63           C  
ANISOU 2606  C   TRP A 274    13665   9581   9289     59   -502   -656       C  
ATOM   2607  O   TRP A 274     -27.381  41.693 -37.637  1.00 84.78           O  
ANISOU 2607  O   TRP A 274    13519   9452   9242     94   -487   -666       O  
ATOM   2608  CB  TRP A 274     -26.115  41.545 -40.522  1.00 80.48           C  
ANISOU 2608  CB  TRP A 274    13155   8875   8547    -24   -443   -592       C  
ATOM   2609  CG  TRP A 274     -24.796  41.067 -41.042  1.00 80.78           C  
ANISOU 2609  CG  TRP A 274    13234   8911   8547    -72   -353   -581       C  
ATOM   2610  CD1 TRP A 274     -24.503  40.674 -42.314  1.00 83.80           C  
ANISOU 2610  CD1 TRP A 274    13692   9303   8847   -120   -326   -565       C  
ATOM   2611  CD2 TRP A 274     -23.608  40.846 -40.267  1.00 80.08           C  
ANISOU 2611  CD2 TRP A 274    13105   8829   8493    -70   -273   -589       C  
ATOM   2612  NE1 TRP A 274     -23.184  40.285 -42.398  1.00 82.98           N  
ANISOU 2612  NE1 TRP A 274    13595   9209   8726   -139   -229   -560       N  
ATOM   2613  CE2 TRP A 274     -22.615  40.365 -41.152  1.00 84.32           C  
ANISOU 2613  CE2 TRP A 274    13688   9384   8967   -107   -197   -573       C  
ATOM   2614  CE3 TRP A 274     -23.286  41.014 -38.905  1.00 80.09           C  
ANISOU 2614  CE3 TRP A 274    13031   8834   8566    -36   -258   -608       C  
ATOM   2615  CZ2 TRP A 274     -21.319  40.050 -40.720  1.00 83.61           C  
ANISOU 2615  CZ2 TRP A 274    13557   9325   8884   -104   -108   -571       C  
ATOM   2616  CZ3 TRP A 274     -21.994  40.741 -38.486  1.00 81.43           C  
ANISOU 2616  CZ3 TRP A 274    13165   9033   8742    -44   -179   -604       C  
ATOM   2617  CH2 TRP A 274     -21.033  40.244 -39.379  1.00 82.71           C  
ANISOU 2617  CH2 TRP A 274    13360   9223   8841    -73   -104   -584       C  
ATOM   2618  N   ALA A 275     -29.080  41.320 -39.112  1.00 82.33           N  
ANISOU 2618  N   ALA A 275    13228   9209   8845     76   -580   -654       N  
ATOM   2619  CA  ALA A 275     -30.134  41.963 -38.312  1.00 81.80           C  
ANISOU 2619  CA  ALA A 275    13086   9172   8822    154   -646   -663       C  
ATOM   2620  C   ALA A 275     -30.303  41.364 -36.909  1.00 84.94           C  
ANISOU 2620  C   ALA A 275    13395   9602   9276    172   -607   -712       C  
ATOM   2621  O   ALA A 275     -30.291  42.163 -35.978  1.00 83.64           O  
ANISOU 2621  O   ALA A 275    13199   9415   9166    238   -619   -719       O  
ATOM   2622  CB  ALA A 275     -31.466  41.993 -39.052  1.00 82.97           C  
ANISOU 2622  CB  ALA A 275    13208   9398   8919    167   -730   -650       C  
ATOM   2623  N   PRO A 276     -30.391  40.009 -36.699  1.00 82.40           N  
ANISOU 2623  N   PRO A 276    13048   9320   8939    113   -557   -746       N  
ATOM   2624  CA  PRO A 276     -30.558  39.481 -35.323  1.00 81.90           C  
ANISOU 2624  CA  PRO A 276    12908   9286   8925    131   -521   -784       C  
ATOM   2625  C   PRO A 276     -29.488  39.894 -34.298  1.00 86.24           C  
ANISOU 2625  C   PRO A 276    13451   9783   9532    169   -472   -788       C  
ATOM   2626  O   PRO A 276     -29.861  40.262 -33.177  1.00 87.08           O  
ANISOU 2626  O   PRO A 276    13492   9911   9683    221   -483   -809       O  
ATOM   2627  CB  PRO A 276     -30.600  37.961 -35.525  1.00 83.52           C  
ANISOU 2627  CB  PRO A 276    13134   9510   9088     49   -467   -807       C  
ATOM   2628  CG  PRO A 276     -31.051  37.775 -36.944  1.00 88.48           C  
ANISOU 2628  CG  PRO A 276    13819  10158   9643     -9   -506   -794       C  
ATOM   2629  CD  PRO A 276     -30.418  38.903 -37.688  1.00 84.27           C  
ANISOU 2629  CD  PRO A 276    13339   9574   9106     27   -532   -751       C  
ATOM   2630  N   ILE A 277     -28.182  39.858 -34.670  1.00 81.52           N  
ANISOU 2630  N   ILE A 277    12915   9133   8926    142   -418   -769       N  
ATOM   2631  CA  ILE A 277     -27.090  40.245 -33.762  1.00 80.38           C  
ANISOU 2631  CA  ILE A 277    12755   8961   8824    162   -376   -769       C  
ATOM   2632  C   ILE A 277     -27.060  41.759 -33.574  1.00 86.72           C  
ANISOU 2632  C   ILE A 277    13570   9723   9655    199   -429   -756       C  
ATOM   2633  O   ILE A 277     -26.850  42.229 -32.446  1.00 88.18           O  
ANISOU 2633  O   ILE A 277    13719   9904   9883    231   -425   -777       O  
ATOM   2634  CB  ILE A 277     -25.685  39.640 -34.114  1.00 82.55           C  
ANISOU 2634  CB  ILE A 277    13068   9221   9074    126   -295   -752       C  
ATOM   2635  CG1 ILE A 277     -24.602  39.956 -33.034  1.00 81.51           C  
ANISOU 2635  CG1 ILE A 277    12893   9096   8981    143   -256   -753       C  
ATOM   2636  CG2 ILE A 277     -25.197  40.010 -35.511  1.00 83.61           C  
ANISOU 2636  CG2 ILE A 277    13279   9328   9160     86   -297   -716       C  
ATOM   2637  CD1 ILE A 277     -24.820  39.311 -31.658  1.00 82.60           C  
ANISOU 2637  CD1 ILE A 277    12963   9270   9152    178   -232   -783       C  
ATOM   2638  N   HIS A 278     -27.303  42.529 -34.648  1.00 82.69           N  
ANISOU 2638  N   HIS A 278    13124   9178   9116    196   -479   -723       N  
ATOM   2639  CA  HIS A 278     -27.303  43.982 -34.511  1.00 81.80           C  
ANISOU 2639  CA  HIS A 278    13053   9003   9024    234   -528   -707       C  
ATOM   2640  C   HIS A 278     -28.429  44.428 -33.577  1.00 85.53           C  
ANISOU 2640  C   HIS A 278    13471   9494   9534    321   -576   -739       C  
ATOM   2641  O   HIS A 278     -28.146  45.254 -32.728  1.00 85.83           O  
ANISOU 2641  O   HIS A 278    13519   9488   9606    353   -579   -755       O  
ATOM   2642  CB  HIS A 278     -27.266  44.711 -35.865  1.00 82.25           C  
ANISOU 2642  CB  HIS A 278    13206   9010   9035    215   -568   -655       C  
ATOM   2643  CG  HIS A 278     -25.869  44.817 -36.428  1.00 84.91           C  
ANISOU 2643  CG  HIS A 278    13603   9313   9347    133   -516   -624       C  
ATOM   2644  ND1 HIS A 278     -24.882  45.556 -35.790  1.00 86.36           N  
ANISOU 2644  ND1 HIS A 278    13804   9453   9555    104   -492   -623       N  
ATOM   2645  CD2 HIS A 278     -25.335  44.266 -37.542  1.00 85.97           C  
ANISOU 2645  CD2 HIS A 278    13776   9463   9425     72   -481   -597       C  
ATOM   2646  CE1 HIS A 278     -23.791  45.426 -36.531  1.00 85.12           C  
ANISOU 2646  CE1 HIS A 278    13682   9300   9359     25   -443   -590       C  
ATOM   2647  NE2 HIS A 278     -24.011  44.664 -37.593  1.00 85.38           N  
ANISOU 2647  NE2 HIS A 278    13731   9366   9344     11   -432   -574       N  
ATOM   2648  N   ILE A 279     -29.614  43.764 -33.602  1.00 82.74           N  
ANISOU 2648  N   ILE A 279    13050   9220   9170    350   -602   -755       N  
ATOM   2649  CA  ILE A 279     -30.735  44.047 -32.684  1.00 83.90           C  
ANISOU 2649  CA  ILE A 279    13118   9416   9344    436   -637   -787       C  
ATOM   2650  C   ILE A 279     -30.360  43.555 -31.268  1.00 91.34           C  
ANISOU 2650  C   ILE A 279    13998  10381  10325    432   -580   -831       C  
ATOM   2651  O   ILE A 279     -30.732  44.187 -30.277  1.00 91.23           O  
ANISOU 2651  O   ILE A 279    13953  10368  10342    502   -593   -860       O  
ATOM   2652  CB  ILE A 279     -32.117  43.471 -33.148  1.00 86.92           C  
ANISOU 2652  CB  ILE A 279    13429   9905   9693    452   -682   -787       C  
ATOM   2653  CG1 ILE A 279     -32.521  43.971 -34.548  1.00 87.23           C  
ANISOU 2653  CG1 ILE A 279    13526   9936   9682    463   -747   -738       C  
ATOM   2654  CG2 ILE A 279     -33.235  43.816 -32.141  1.00 87.91           C  
ANISOU 2654  CG2 ILE A 279    13457  10102   9842    549   -711   -818       C  
ATOM   2655  CD1 ILE A 279     -33.473  43.029 -35.303  1.00 86.91           C  
ANISOU 2655  CD1 ILE A 279    13429  10009   9586    414   -776   -735       C  
ATOM   2656  N   PHE A 280     -29.619  42.432 -31.182  1.00 89.62           N  
ANISOU 2656  N   PHE A 280    13771  10180  10101    357   -516   -835       N  
ATOM   2657  CA  PHE A 280     -29.166  41.870 -29.906  1.00 88.81           C  
ANISOU 2657  CA  PHE A 280    13617  10103  10026    352   -462   -865       C  
ATOM   2658  C   PHE A 280     -28.240  42.863 -29.184  1.00 91.85           C  
ANISOU 2658  C   PHE A 280    14028  10431  10439    369   -454   -872       C  
ATOM   2659  O   PHE A 280     -28.456  43.124 -28.010  1.00 90.99           O  
ANISOU 2659  O   PHE A 280    13875  10341  10354    410   -452   -907       O  
ATOM   2660  CB  PHE A 280     -28.510  40.478 -30.094  1.00 90.07           C  
ANISOU 2660  CB  PHE A 280    13781  10279  10163    286   -394   -858       C  
ATOM   2661  CG  PHE A 280     -28.774  39.447 -29.007  1.00 91.14           C  
ANISOU 2661  CG  PHE A 280    13855  10468  10307    284   -351   -883       C  
ATOM   2662  CD1 PHE A 280     -28.451  39.709 -27.679  1.00 93.84           C  
ANISOU 2662  CD1 PHE A 280    14152  10825  10679    319   -332   -904       C  
ATOM   2663  CD2 PHE A 280     -29.279  38.193 -29.324  1.00 92.73           C  
ANISOU 2663  CD2 PHE A 280    14058  10701  10476    236   -325   -885       C  
ATOM   2664  CE1 PHE A 280     -28.691  38.760 -26.685  1.00 94.44           C  
ANISOU 2664  CE1 PHE A 280    14179  10950  10755    316   -292   -920       C  
ATOM   2665  CE2 PHE A 280     -29.502  37.240 -28.331  1.00 95.03           C  
ANISOU 2665  CE2 PHE A 280    14309  11029  10768    226   -282   -902       C  
ATOM   2666  CZ  PHE A 280     -29.203  37.527 -27.021  1.00 93.02           C  
ANISOU 2666  CZ  PHE A 280    14007  10793  10545    269   -265   -916       C  
ATOM   2667  N   VAL A 281     -27.273  43.469 -29.903  1.00 89.08           N  
ANISOU 2667  N   VAL A 281    13752  10015  10077    329   -454   -842       N  
ATOM   2668  CA  VAL A 281     -26.323  44.465 -29.357  1.00 89.14           C  
ANISOU 2668  CA  VAL A 281    13799   9971  10101    313   -450   -846       C  
ATOM   2669  C   VAL A 281     -27.065  45.735 -28.876  1.00 94.58           C  
ANISOU 2669  C   VAL A 281    14523  10604  10808    384   -506   -870       C  
ATOM   2670  O   VAL A 281     -26.702  46.308 -27.843  1.00 94.85           O  
ANISOU 2670  O   VAL A 281    14562  10618  10859    389   -501   -903       O  
ATOM   2671  CB  VAL A 281     -25.158  44.764 -30.352  1.00 92.57           C  
ANISOU 2671  CB  VAL A 281    14302  10362  10507    235   -433   -802       C  
ATOM   2672  CG1 VAL A 281     -24.265  45.903 -29.870  1.00 92.04           C  
ANISOU 2672  CG1 VAL A 281    14284  10241  10447    194   -438   -805       C  
ATOM   2673  CG2 VAL A 281     -24.320  43.505 -30.611  1.00 91.86           C  
ANISOU 2673  CG2 VAL A 281    14172  10334  10397    189   -365   -785       C  
ATOM   2674  N   ILE A 282     -28.134  46.140 -29.589  1.00 91.50           N  
ANISOU 2674  N   ILE A 282    14159  10198  10409    446   -559   -856       N  
ATOM   2675  CA  ILE A 282     -28.927  47.310 -29.188  1.00 91.18           C  
ANISOU 2675  CA  ILE A 282    14157  10106  10381    544   -609   -876       C  
ATOM   2676  C   ILE A 282     -29.733  46.982 -27.901  1.00 95.00           C  
ANISOU 2676  C   ILE A 282    14541  10667  10887    616   -598   -931       C  
ATOM   2677  O   ILE A 282     -29.697  47.768 -26.962  1.00 94.91           O  
ANISOU 2677  O   ILE A 282    14557  10615  10890    661   -600   -969       O  
ATOM   2678  CB  ILE A 282     -29.777  47.912 -30.352  1.00 93.95           C  
ANISOU 2678  CB  ILE A 282    14564  10423  10708    607   -671   -835       C  
ATOM   2679  CG1 ILE A 282     -28.889  48.240 -31.585  1.00 92.93           C  
ANISOU 2679  CG1 ILE A 282    14542  10218  10549    524   -674   -778       C  
ATOM   2680  CG2 ILE A 282     -30.531  49.175 -29.881  1.00 95.71           C  
ANISOU 2680  CG2 ILE A 282    14841  10583  10941    734   -716   -853       C  
ATOM   2681  CD1 ILE A 282     -29.602  48.167 -32.978  1.00 92.81           C  
ANISOU 2681  CD1 ILE A 282    14550  10220  10493    547   -723   -726       C  
ATOM   2682  N   VAL A 283     -30.384  45.805 -27.832  1.00 91.89           N  
ANISOU 2682  N   VAL A 283    14042  10383  10488    611   -581   -936       N  
ATOM   2683  CA  VAL A 283     -31.133  45.397 -26.639  1.00 92.40           C  
ANISOU 2683  CA  VAL A 283    14007  10535  10565    662   -564   -981       C  
ATOM   2684  C   VAL A 283     -30.177  45.172 -25.441  1.00100.22           C  
ANISOU 2684  C   VAL A 283    14985  11522  11570    619   -512  -1012       C  
ATOM   2685  O   VAL A 283     -30.472  45.675 -24.347  1.00101.95           O  
ANISOU 2685  O   VAL A 283    15187  11752  11799    678   -510  -1057       O  
ATOM   2686  CB  VAL A 283     -32.112  44.217 -26.868  1.00 95.38           C  
ANISOU 2686  CB  VAL A 283    14282  11032  10925    649   -561   -976       C  
ATOM   2687  CG1 VAL A 283     -32.822  43.828 -25.574  1.00 94.92           C  
ANISOU 2687  CG1 VAL A 283    14123  11069  10873    688   -536  -1019       C  
ATOM   2688  CG2 VAL A 283     -33.138  44.564 -27.943  1.00 95.89           C  
ANISOU 2688  CG2 VAL A 283    14343  11124  10966    699   -623   -948       C  
ATOM   2689  N   TRP A 284     -29.011  44.498 -25.660  1.00 96.19           N  
ANISOU 2689  N   TRP A 284    14490  11003  11055    525   -472   -989       N  
ATOM   2690  CA  TRP A 284     -27.997  44.257 -24.622  1.00 95.49           C  
ANISOU 2690  CA  TRP A 284    14383  10929  10971    484   -428  -1007       C  
ATOM   2691  C   TRP A 284     -27.530  45.532 -23.909  1.00103.26           C  
ANISOU 2691  C   TRP A 284    15423  11849  11961    497   -446  -1039       C  
ATOM   2692  O   TRP A 284     -27.307  45.508 -22.694  1.00104.21           O  
ANISOU 2692  O   TRP A 284    15508  12006  12081    501   -426  -1076       O  
ATOM   2693  CB  TRP A 284     -26.780  43.501 -25.170  1.00 93.22           C  
ANISOU 2693  CB  TRP A 284    14104  10644  10670    402   -387   -967       C  
ATOM   2694  CG  TRP A 284     -25.854  43.025 -24.084  1.00 94.00           C  
ANISOU 2694  CG  TRP A 284    14158  10792  10765    375   -342   -977       C  
ATOM   2695  CD1 TRP A 284     -26.182  42.258 -23.000  1.00 96.66           C  
ANISOU 2695  CD1 TRP A 284    14427  11199  11101    400   -314   -997       C  
ATOM   2696  CD2 TRP A 284     -24.460  43.323 -23.955  1.00 93.89           C  
ANISOU 2696  CD2 TRP A 284    14159  10774  10740    317   -324   -963       C  
ATOM   2697  NE1 TRP A 284     -25.071  42.034 -22.221  1.00 95.62           N  
ANISOU 2697  NE1 TRP A 284    14270  11104  10958    372   -282   -993       N  
ATOM   2698  CE2 TRP A 284     -24.001  42.687 -22.777  1.00 97.28           C  
ANISOU 2698  CE2 TRP A 284    14521  11279  11161    320   -289   -974       C  
ATOM   2699  CE3 TRP A 284     -23.546  44.052 -24.732  1.00 95.69           C  
ANISOU 2699  CE3 TRP A 284    14446  10954  10958    256   -334   -937       C  
ATOM   2700  CZ2 TRP A 284     -22.671  42.779 -22.343  1.00 96.77           C  
ANISOU 2700  CZ2 TRP A 284    14436  11256  11078    271   -269   -961       C  
ATOM   2701  CZ3 TRP A 284     -22.230  44.140 -24.301  1.00 97.62           C  
ANISOU 2701  CZ3 TRP A 284    14666  11241  11184    194   -309   -927       C  
ATOM   2702  CH2 TRP A 284     -21.802  43.503 -23.123  1.00 97.95           C  
ANISOU 2702  CH2 TRP A 284    14629  11370  11217    205   -280   -939       C  
ATOM   2703  N   THR A 285     -27.393  46.633 -24.667  1.00100.78           N  
ANISOU 2703  N   THR A 285    15209  11437  11645    497   -484  -1026       N  
ATOM   2704  CA  THR A 285     -26.915  47.935 -24.198  1.00101.55           C  
ANISOU 2704  CA  THR A 285    15400  11444  11741    489   -504  -1054       C  
ATOM   2705  C   THR A 285     -27.943  48.744 -23.412  1.00105.31           C  
ANISOU 2705  C   THR A 285    15899  11891  12223    602   -529  -1108       C  
ATOM   2706  O   THR A 285     -27.556  49.524 -22.538  1.00103.85           O  
ANISOU 2706  O   THR A 285    15772  11656  12031    594   -528  -1153       O  
ATOM   2707  CB  THR A 285     -26.371  48.752 -25.388  1.00110.84           C  
ANISOU 2707  CB  THR A 285    16693  12515  12905    436   -530  -1010       C  
ATOM   2708  OG1 THR A 285     -27.242  48.598 -26.503  1.00111.08           O  
ANISOU 2708  OG1 THR A 285    16731  12539  12934    492   -558   -972       O  
ATOM   2709  CG2 THR A 285     -25.016  48.302 -25.813  1.00107.12           C  
ANISOU 2709  CG2 THR A 285    16213  12070  12420    312   -495   -973       C  
ATOM   2710  N   LEU A 286     -29.244  48.577 -23.738  1.00102.50           N  
ANISOU 2710  N   LEU A 286    15499  11573  11873    706   -550  -1104       N  
ATOM   2711  CA  LEU A 286     -30.345  49.339 -23.130  1.00102.84           C  
ANISOU 2711  CA  LEU A 286    15553  11605  11917    842   -571  -1149       C  
ATOM   2712  C   LEU A 286     -31.119  48.598 -22.018  1.00106.60           C  
ANISOU 2712  C   LEU A 286    15897  12213  12393    895   -541  -1191       C  
ATOM   2713  O   LEU A 286     -31.728  49.237 -21.151  1.00105.78           O  
ANISOU 2713  O   LEU A 286    15800  12109  12284    993   -541  -1244       O  
ATOM   2714  CB  LEU A 286     -31.323  49.821 -24.235  1.00103.10           C  
ANISOU 2714  CB  LEU A 286    15619  11609  11946    939   -621  -1112       C  
ATOM   2715  CG  LEU A 286     -30.718  50.537 -25.457  1.00107.33           C  
ANISOU 2715  CG  LEU A 286    16290  12018  12472    894   -654  -1058       C  
ATOM   2716  CD1 LEU A 286     -31.745  50.702 -26.569  1.00107.83           C  
ANISOU 2716  CD1 LEU A 286    16354  12094  12524    988   -704  -1011       C  
ATOM   2717  CD2 LEU A 286     -30.087  51.871 -25.084  1.00109.60           C  
ANISOU 2717  CD2 LEU A 286    16740  12149  12753    889   -662  -1084       C  
ATOM   2718  N   VAL A 287     -31.097  47.255 -22.062  1.00103.25           N  
ANISOU 2718  N   VAL A 287    15364  11896  11969    830   -511  -1167       N  
ATOM   2719  CA  VAL A 287     -31.842  46.378 -21.163  1.00103.05           C  
ANISOU 2719  CA  VAL A 287    15215  12002  11938    855   -479  -1193       C  
ATOM   2720  C   VAL A 287     -30.936  45.348 -20.482  1.00107.26           C  
ANISOU 2720  C   VAL A 287    15705  12581  12466    756   -430  -1189       C  
ATOM   2721  O   VAL A 287     -29.909  44.949 -21.040  1.00105.97           O  
ANISOU 2721  O   VAL A 287    15575  12383  12305    669   -419  -1152       O  
ATOM   2722  CB  VAL A 287     -33.031  45.742 -21.960  1.00107.19           C  
ANISOU 2722  CB  VAL A 287    15654  12616  12456    886   -498  -1162       C  
ATOM   2723  CG1 VAL A 287     -33.612  44.505 -21.289  1.00106.87           C  
ANISOU 2723  CG1 VAL A 287    15490  12713  12402    854   -458  -1170       C  
ATOM   2724  CG2 VAL A 287     -34.131  46.766 -22.215  1.00108.12           C  
ANISOU 2724  CG2 VAL A 287    15780  12731  12569   1024   -544  -1173       C  
ATOM   2725  N   ASP A 288     -31.323  44.943 -19.253  1.00105.70           N  
ANISOU 2725  N   ASP A 288    15435  12471  12256    779   -397  -1225       N  
ATOM   2726  CA  ASP A 288     -30.666  43.901 -18.464  1.00105.64           C  
ANISOU 2726  CA  ASP A 288    15379  12524  12236    708   -349  -1218       C  
ATOM   2727  C   ASP A 288     -31.171  42.544 -18.953  1.00108.25           C  
ANISOU 2727  C   ASP A 288    15642  12926  12560    666   -327  -1176       C  
ATOM   2728  O   ASP A 288     -32.383  42.290 -18.946  1.00107.91           O  
ANISOU 2728  O   ASP A 288    15533  12959  12510    701   -330  -1184       O  
ATOM   2729  CB  ASP A 288     -30.939  44.079 -16.960  1.00108.36           C  
ANISOU 2729  CB  ASP A 288    15684  12930  12558    750   -325  -1271       C  
ATOM   2730  CG  ASP A 288     -29.753  44.618 -16.192  1.00120.78           C  
ANISOU 2730  CG  ASP A 288    17314  14460  14118    712   -321  -1297       C  
ATOM   2731  OD1 ASP A 288     -28.667  43.997 -16.262  1.00120.64           O  
ANISOU 2731  OD1 ASP A 288    17296  14446  14095    633   -305  -1259       O  
ATOM   2732  OD2 ASP A 288     -29.910  45.656 -15.516  1.00129.53           O1-
ANISOU 2732  OD2 ASP A 288    18467  15536  15214    764   -334  -1355       O1-
ATOM   2733  N   ILE A 289     -30.239  41.703 -19.427  1.00103.62           N  
ANISOU 2733  N   ILE A 289    15080  12318  11973    588   -304  -1132       N  
ATOM   2734  CA  ILE A 289     -30.521  40.383 -19.995  1.00102.76           C  
ANISOU 2734  CA  ILE A 289    14947  12244  11853    534   -277  -1093       C  
ATOM   2735  C   ILE A 289     -29.922  39.311 -19.105  1.00106.14           C  
ANISOU 2735  C   ILE A 289    15357  12710  12262    497   -222  -1077       C  
ATOM   2736  O   ILE A 289     -28.775  39.460 -18.667  1.00106.88           O  
ANISOU 2736  O   ILE A 289    15474  12782  12353    491   -209  -1071       O  
ATOM   2737  CB  ILE A 289     -30.019  40.331 -21.473  1.00105.42           C  
ANISOU 2737  CB  ILE A 289    15347  12509  12197    495   -295  -1054       C  
ATOM   2738  CG1 ILE A 289     -30.861  41.288 -22.347  1.00106.67           C  
ANISOU 2738  CG1 ILE A 289    15519  12645  12366    540   -353  -1061       C  
ATOM   2739  CG2 ILE A 289     -30.023  38.908 -22.054  1.00105.70           C  
ANISOU 2739  CG2 ILE A 289    15389  12559  12213    430   -258  -1018       C  
ATOM   2740  CD1 ILE A 289     -30.244  41.722 -23.638  1.00117.78           C  
ANISOU 2740  CD1 ILE A 289    17005  13969  13777    515   -379  -1029       C  
ATOM   2741  N   ASP A 290     -30.705  38.242 -18.820  1.00100.90           N  
ANISOU 2741  N   ASP A 290    14652  12109  11576    469   -191  -1068       N  
ATOM   2742  CA  ASP A 290     -30.265  37.110 -17.994  1.00 99.86           C  
ANISOU 2742  CA  ASP A 290    14519  12006  11417    438   -135  -1044       C  
ATOM   2743  C   ASP A 290     -29.169  36.291 -18.707  1.00103.00           C  
ANISOU 2743  C   ASP A 290    14986  12340  11810    404   -106   -995       C  
ATOM   2744  O   ASP A 290     -29.478  35.322 -19.409  1.00102.81           O  
ANISOU 2744  O   ASP A 290    14997  12295  11771    357    -83   -970       O  
ATOM   2745  CB  ASP A 290     -31.470  36.224 -17.575  1.00101.65           C  
ANISOU 2745  CB  ASP A 290    14697  12308  11615    403   -108  -1045       C  
ATOM   2746  CG  ASP A 290     -31.194  35.148 -16.522  1.00103.91           C  
ANISOU 2746  CG  ASP A 290    14989  12625  11866    375    -50  -1019       C  
ATOM   2747  OD1 ASP A 290     -30.136  35.231 -15.836  1.00101.96           O  
ANISOU 2747  OD1 ASP A 290    14760  12367  11615    407    -35  -1008       O  
ATOM   2748  OD2 ASP A 290     -32.038  34.229 -16.377  1.00106.12           O  
ANISOU 2748  OD2 ASP A 290    15258  12946  12117    317    -21  -1006       O  
ATOM   2749  N   ARG A 291     -27.888  36.697 -18.518  1.00 98.96           N  
ANISOU 2749  N   ARG A 291    14492  11803  11304    425   -105   -984       N  
ATOM   2750  CA  ARG A 291     -26.669  36.076 -19.073  1.00 98.62           C  
ANISOU 2750  CA  ARG A 291    14497  11721  11252    417    -74   -938       C  
ATOM   2751  C   ARG A 291     -26.608  34.547 -18.874  1.00102.06           C  
ANISOU 2751  C   ARG A 291    14966  12155  11655    407    -13   -898       C  
ATOM   2752  O   ARG A 291     -25.955  33.856 -19.656  1.00101.40           O  
ANISOU 2752  O   ARG A 291    14942  12025  11561    404     18   -863       O  
ATOM   2753  CB  ARG A 291     -25.413  36.690 -18.425  1.00100.21           C  
ANISOU 2753  CB  ARG A 291    14675  11949  11450    440    -78   -935       C  
ATOM   2754  CG  ARG A 291     -25.040  38.089 -18.899  1.00117.62           C  
ANISOU 2754  CG  ARG A 291    16886  14124  13679    430   -128   -961       C  
ATOM   2755  CD  ARG A 291     -23.525  38.295 -18.977  1.00135.24           C  
ANISOU 2755  CD  ARG A 291    19115  16373  15898    417   -119   -933       C  
ATOM   2756  NE  ARG A 291     -22.853  37.251 -19.767  1.00145.41           N  
ANISOU 2756  NE  ARG A 291    20426  17651  17171    422    -73   -879       N  
ATOM   2757  CZ  ARG A 291     -21.639  37.357 -20.305  1.00151.41           C  
ANISOU 2757  CZ  ARG A 291    21183  18427  17920    413    -60   -847       C  
ATOM   2758  NH1 ARG A 291     -20.941  38.483 -20.177  1.00133.33           N  
ANISOU 2758  NH1 ARG A 291    18869  16160  15631    376    -94   -861       N  
ATOM   2759  NH2 ARG A 291     -21.119  36.344 -20.989  1.00128.69           N  
ANISOU 2759  NH2 ARG A 291    18331  15542  15024    438     -9   -803       N  
ATOM   2760  N   ARG A 292     -27.264  34.042 -17.810  1.00 98.85           N  
ANISOU 2760  N   ARG A 292    14534  11797  11228    404      8   -902       N  
ATOM   2761  CA  ARG A 292     -27.279  32.634 -17.409  1.00 99.23           C  
ANISOU 2761  CA  ARG A 292    14630  11836  11238    391     67   -862       C  
ATOM   2762  C   ARG A 292     -28.331  31.781 -18.136  1.00102.53           C  
ANISOU 2762  C   ARG A 292    15099  12215  11641    320     83   -860       C  
ATOM   2763  O   ARG A 292     -28.056  30.609 -18.406  1.00102.82           O  
ANISOU 2763  O   ARG A 292    15225  12193  11648    303    134   -823       O  
ATOM   2764  CB  ARG A 292     -27.454  32.505 -15.882  1.00102.06           C  
ANISOU 2764  CB  ARG A 292    14942  12267  11568    409     82   -861       C  
ATOM   2765  CG  ARG A 292     -26.334  33.101 -15.028  1.00114.94           C  
ANISOU 2765  CG  ARG A 292    16531  13946  13193    468     71   -856       C  
ATOM   2766  CD  ARG A 292     -26.665  32.945 -13.547  1.00132.42           C  
ANISOU 2766  CD  ARG A 292    18706  16238  15371    478     85   -860       C  
ATOM   2767  NE  ARG A 292     -25.672  33.572 -12.667  1.00139.34           N  
ANISOU 2767  NE  ARG A 292    19537  17176  16231    521     66   -862       N  
ATOM   2768  CZ  ARG A 292     -24.573  32.971 -12.219  1.00150.29           C  
ANISOU 2768  CZ  ARG A 292    20932  18589  17582    563     90   -807       C  
ATOM   2769  NH1 ARG A 292     -24.299  31.720 -12.573  1.00143.33           N  
ANISOU 2769  NH1 ARG A 292    20118  17660  16681    583    139   -745       N  
ATOM   2770  NH2 ARG A 292     -23.732  33.620 -11.428  1.00130.11           N  
ANISOU 2770  NH2 ARG A 292    18321  16110  15004    586     63   -815       N  
ATOM   2771  N   ASP A 293     -29.533  32.346 -18.420  1.00 98.01           N  
ANISOU 2771  N   ASP A 293    14476  11681  11083    279     42   -901       N  
ATOM   2772  CA  ASP A 293     -30.647  31.670 -19.109  1.00 98.03           C  
ANISOU 2772  CA  ASP A 293    14502  11678  11065    193     45   -905       C  
ATOM   2773  C   ASP A 293     -30.166  30.975 -20.395  1.00102.97           C  
ANISOU 2773  C   ASP A 293    15236  12208  11679    160     64   -883       C  
ATOM   2774  O   ASP A 293     -29.587  31.640 -21.260  1.00102.12           O  
ANISOU 2774  O   ASP A 293    15138  12066  11596    194     36   -886       O  
ATOM   2775  CB  ASP A 293     -31.776  32.678 -19.422  1.00100.00           C  
ANISOU 2775  CB  ASP A 293    14660  12001  11335    185    -16   -949       C  
ATOM   2776  CG  ASP A 293     -33.104  32.118 -19.928  1.00110.72           C  
ANISOU 2776  CG  ASP A 293    15998  13407  12662     89    -24   -957       C  
ATOM   2777  OD1 ASP A 293     -33.089  31.135 -20.696  1.00111.24           O  
ANISOU 2777  OD1 ASP A 293    16152  13414  12699     11     -1   -938       O  
ATOM   2778  OD2 ASP A 293     -34.154  32.694 -19.591  1.00117.67           O  
ANISOU 2778  OD2 ASP A 293    16774  14391  13543     94    -55   -986       O  
ATOM   2779  N   PRO A 294     -30.395  29.640 -20.534  1.00100.86           N  
ANISOU 2779  N   PRO A 294    15064  11891  11367     92    115   -860       N  
ATOM   2780  CA  PRO A 294     -29.938  28.922 -21.751  1.00100.46           C  
ANISOU 2780  CA  PRO A 294    15136  11738  11295     65    141   -846       C  
ATOM   2781  C   PRO A 294     -30.594  29.345 -23.068  1.00103.51           C  
ANISOU 2781  C   PRO A 294    15516  12129  11684      4     89   -876       C  
ATOM   2782  O   PRO A 294     -30.059  29.039 -24.128  1.00102.56           O  
ANISOU 2782  O   PRO A 294    15485  11932  11550      0    102   -869       O  
ATOM   2783  CB  PRO A 294     -30.217  27.447 -21.430  1.00102.80           C  
ANISOU 2783  CB  PRO A 294    15546  11977  11536     -6    205   -823       C  
ATOM   2784  CG  PRO A 294     -30.502  27.396 -19.968  1.00107.33           C  
ANISOU 2784  CG  PRO A 294    16057  12619  12105      6    220   -810       C  
ATOM   2785  CD  PRO A 294     -31.062  28.718 -19.592  1.00102.55           C  
ANISOU 2785  CD  PRO A 294    15293  12130  11541     31    156   -847       C  
ATOM   2786  N   LEU A 295     -31.753  30.021 -23.002  1.00101.09           N  
ANISOU 2786  N   LEU A 295    15103  11918  11389    -34     32   -905       N  
ATOM   2787  CA  LEU A 295     -32.460  30.521 -24.174  1.00101.78           C  
ANISOU 2787  CA  LEU A 295    15167  12032  11473    -80    -27   -927       C  
ATOM   2788  C   LEU A 295     -31.679  31.689 -24.745  1.00104.36           C  
ANISOU 2788  C   LEU A 295    15475  12336  11842     10    -67   -927       C  
ATOM   2789  O   LEU A 295     -31.510  31.747 -25.964  1.00104.42           O  
ANISOU 2789  O   LEU A 295    15537  12301  11837    -13    -86   -926       O  
ATOM   2790  CB  LEU A 295     -33.889  31.000 -23.817  1.00102.97           C  
ANISOU 2790  CB  LEU A 295    15189  12315  11620   -120    -77   -952       C  
ATOM   2791  CG  LEU A 295     -35.081  30.022 -23.943  1.00109.24           C  
ANISOU 2791  CG  LEU A 295    15985  13165  12354   -265    -69   -959       C  
ATOM   2792  CD1 LEU A 295     -35.058  29.243 -25.261  1.00109.97           C  
ANISOU 2792  CD1 LEU A 295    16197  13184  12401   -364    -67   -959       C  
ATOM   2793  CD2 LEU A 295     -35.212  29.115 -22.716  1.00111.81           C  
ANISOU 2793  CD2 LEU A 295    16325  13501  12656   -309     -5   -946       C  
ATOM   2794  N   VAL A 296     -31.194  32.623 -23.866  1.00 98.34           N  
ANISOU 2794  N   VAL A 296    14643  11599  11122    101    -78   -929       N  
ATOM   2795  CA  VAL A 296     -30.429  33.797 -24.308  1.00 96.22           C  
ANISOU 2795  CA  VAL A 296    14365  11305  10889    170   -114   -929       C  
ATOM   2796  C   VAL A 296     -29.040  33.354 -24.826  1.00 99.15           C  
ANISOU 2796  C   VAL A 296    14825  11595  11253    188    -67   -900       C  
ATOM   2797  O   VAL A 296     -28.587  33.890 -25.830  1.00100.51           O  
ANISOU 2797  O   VAL A 296    15025  11732  11430    195    -89   -894       O  
ATOM   2798  CB  VAL A 296     -30.377  35.015 -23.325  1.00 98.78           C  
ANISOU 2798  CB  VAL A 296    14605  11674  11252    246   -145   -949       C  
ATOM   2799  CG1 VAL A 296     -31.507  34.991 -22.308  1.00 98.52           C  
ANISOU 2799  CG1 VAL A 296    14489  11730  11213    244   -149   -973       C  
ATOM   2800  CG2 VAL A 296     -29.020  35.194 -22.653  1.00 98.14           C  
ANISOU 2800  CG2 VAL A 296    14539  11564  11186    296   -115   -935       C  
ATOM   2801  N   VAL A 297     -28.420  32.341 -24.210  1.00 93.37           N  
ANISOU 2801  N   VAL A 297    14138  10837  10501    196     -2   -878       N  
ATOM   2802  CA  VAL A 297     -27.120  31.823 -24.640  1.00 92.26           C  
ANISOU 2802  CA  VAL A 297    14072  10637  10346    233     51   -847       C  
ATOM   2803  C   VAL A 297     -27.227  31.175 -26.036  1.00 95.16           C  
ANISOU 2803  C   VAL A 297    14541  10938  10677    182     67   -847       C  
ATOM   2804  O   VAL A 297     -26.436  31.519 -26.918  1.00 95.83           O  
ANISOU 2804  O   VAL A 297    14655  10996  10760    206     70   -836       O  
ATOM   2805  CB  VAL A 297     -26.480  30.898 -23.568  1.00 96.11           C  
ANISOU 2805  CB  VAL A 297    14583  11119  10816    279    115   -818       C  
ATOM   2806  CG1 VAL A 297     -25.146  30.328 -24.041  1.00 96.07           C  
ANISOU 2806  CG1 VAL A 297    14647  11067  10789    340    172   -782       C  
ATOM   2807  CG2 VAL A 297     -26.297  31.642 -22.243  1.00 95.74           C  
ANISOU 2807  CG2 VAL A 297    14435  11147  10795    326     94   -821       C  
ATOM   2808  N   ALA A 298     -28.226  30.283 -26.241  1.00 89.37           N  
ANISOU 2808  N   ALA A 298    13861  10187   9908    101     75   -860       N  
ATOM   2809  CA  ALA A 298     -28.497  29.611 -27.514  1.00 88.34           C  
ANISOU 2809  CA  ALA A 298    13839   9997   9731     30     87   -870       C  
ATOM   2810  C   ALA A 298     -28.682  30.646 -28.619  1.00 91.57           C  
ANISOU 2810  C   ALA A 298    14213  10429  10149     18     21   -882       C  
ATOM   2811  O   ALA A 298     -28.010  30.574 -29.651  1.00 91.63           O  
ANISOU 2811  O   ALA A 298    14295  10387  10133     24     40   -875       O  
ATOM   2812  CB  ALA A 298     -29.755  28.766 -27.396  1.00 89.36           C  
ANISOU 2812  CB  ALA A 298    13999  10134   9821    -83     85   -889       C  
ATOM   2813  N   ALA A 299     -29.559  31.645 -28.364  1.00 86.52           N  
ANISOU 2813  N   ALA A 299    13464   9868   9541     12    -52   -897       N  
ATOM   2814  CA  ALA A 299     -29.882  32.722 -29.291  1.00 85.18           C  
ANISOU 2814  CA  ALA A 299    13260   9725   9380     13   -123   -901       C  
ATOM   2815  C   ALA A 299     -28.683  33.633 -29.564  1.00 86.50           C  
ANISOU 2815  C   ALA A 299    13430   9860   9576     85   -123   -881       C  
ATOM   2816  O   ALA A 299     -28.495  34.027 -30.710  1.00 86.36           O  
ANISOU 2816  O   ALA A 299    13454   9820   9540     71   -146   -873       O  
ATOM   2817  CB  ALA A 299     -31.073  33.522 -28.782  1.00 85.83           C  
ANISOU 2817  CB  ALA A 299    13227   9898   9486     17   -192   -918       C  
ATOM   2818  N   LEU A 300     -27.852  33.922 -28.547  1.00 80.78           N  
ANISOU 2818  N   LEU A 300    12665   9140   8887    149    -96   -871       N  
ATOM   2819  CA  LEU A 300     -26.690  34.787 -28.730  1.00 80.18           C  
ANISOU 2819  CA  LEU A 300    12583   9049   8831    195    -95   -852       C  
ATOM   2820  C   LEU A 300     -25.672  34.201 -29.687  1.00 86.16           C  
ANISOU 2820  C   LEU A 300    13422   9763   9553    193    -39   -830       C  
ATOM   2821  O   LEU A 300     -25.280  34.887 -30.629  1.00 87.68           O  
ANISOU 2821  O   LEU A 300    13635   9942   9738    184    -60   -818       O  
ATOM   2822  CB  LEU A 300     -26.027  35.179 -27.394  1.00 79.66           C  
ANISOU 2822  CB  LEU A 300    12451   9015   8801    249    -81   -850       C  
ATOM   2823  CG  LEU A 300     -24.748  36.020 -27.478  1.00 83.58           C  
ANISOU 2823  CG  LEU A 300    12935   9513   9309    275    -78   -830       C  
ATOM   2824  CD1 LEU A 300     -25.000  37.367 -28.146  1.00 84.21           C  
ANISOU 2824  CD1 LEU A 300    13016   9574   9405    258   -143   -835       C  
ATOM   2825  CD2 LEU A 300     -24.129  36.198 -26.123  1.00 84.31           C  
ANISOU 2825  CD2 LEU A 300    12963   9650   9420    313    -63   -830       C  
ATOM   2826  N   HIS A 301     -25.247  32.947 -29.453  1.00 82.24           N  
ANISOU 2826  N   HIS A 301    12979   9241   9029    207     34   -822       N  
ATOM   2827  CA  HIS A 301     -24.250  32.269 -30.277  1.00 82.33           C  
ANISOU 2827  CA  HIS A 301    13073   9213   8998    228    101   -802       C  
ATOM   2828  C   HIS A 301     -24.758  31.921 -31.687  1.00 87.99           C  
ANISOU 2828  C   HIS A 301    13884   9884   9665    164     95   -817       C  
ATOM   2829  O   HIS A 301     -23.945  31.854 -32.614  1.00 87.68           O  
ANISOU 2829  O   HIS A 301    13898   9823   9591    179    133   -804       O  
ATOM   2830  CB  HIS A 301     -23.687  31.058 -29.543  1.00 82.98           C  
ANISOU 2830  CB  HIS A 301    13194   9273   9060    283    181   -787       C  
ATOM   2831  CG  HIS A 301     -22.921  31.472 -28.329  1.00 85.58           C  
ANISOU 2831  CG  HIS A 301    13427   9664   9424    351    187   -765       C  
ATOM   2832  ND1 HIS A 301     -21.585  31.809 -28.403  1.00 87.06           N  
ANISOU 2832  ND1 HIS A 301    13576   9894   9609    410    217   -735       N  
ATOM   2833  CD2 HIS A 301     -23.354  31.677 -27.066  1.00 86.62           C  
ANISOU 2833  CD2 HIS A 301    13489   9835   9588    358    160   -771       C  
ATOM   2834  CE1 HIS A 301     -21.236  32.152 -27.180  1.00 86.23           C  
ANISOU 2834  CE1 HIS A 301    13383   9851   9531    446    205   -724       C  
ATOM   2835  NE2 HIS A 301     -22.274  32.107 -26.345  1.00 86.32           N  
ANISOU 2835  NE2 HIS A 301    13377   9857   9563    419    171   -747       N  
ATOM   2836  N   LEU A 302     -26.092  31.758 -31.858  1.00 84.90           N  
ANISOU 2836  N   LEU A 302    13503   9492   9263     90     46   -843       N  
ATOM   2837  CA  LEU A 302     -26.699  31.532 -33.162  1.00 85.23           C  
ANISOU 2837  CA  LEU A 302    13622   9512   9251     16     24   -859       C  
ATOM   2838  C   LEU A 302     -26.604  32.851 -33.944  1.00 88.94           C  
ANISOU 2838  C   LEU A 302    14050  10010   9733     20    -40   -845       C  
ATOM   2839  O   LEU A 302     -26.303  32.851 -35.147  1.00 88.88           O  
ANISOU 2839  O   LEU A 302    14113   9980   9677     -5    -33   -840       O  
ATOM   2840  CB  LEU A 302     -28.168  31.083 -33.028  1.00 85.93           C  
ANISOU 2840  CB  LEU A 302    13704   9623   9320    -73    -21   -888       C  
ATOM   2841  CG  LEU A 302     -28.887  30.800 -34.378  1.00 92.46           C  
ANISOU 2841  CG  LEU A 302    14606  10445  10078   -169    -54   -907       C  
ATOM   2842  CD1 LEU A 302     -28.791  29.337 -34.770  1.00 93.09           C  
ANISOU 2842  CD1 LEU A 302    14835  10445  10089   -229     19   -929       C  
ATOM   2843  CD2 LEU A 302     -30.340  31.274 -34.360  1.00 96.48           C  
ANISOU 2843  CD2 LEU A 302    15026  11043  10588   -234   -146   -921       C  
ATOM   2844  N   CYS A 303     -26.838  33.978 -33.228  1.00 84.10           N  
ANISOU 2844  N   CYS A 303    13335   9442   9178     53    -98   -838       N  
ATOM   2845  CA  CYS A 303     -26.799  35.327 -33.775  1.00 83.19           C  
ANISOU 2845  CA  CYS A 303    13191   9338   9078     63   -160   -821       C  
ATOM   2846  C   CYS A 303     -25.409  35.713 -34.246  1.00 86.30           C  
ANISOU 2846  C   CYS A 303    13615   9710   9465     87   -118   -792       C  
ATOM   2847  O   CYS A 303     -25.266  36.189 -35.385  1.00 88.13           O  
ANISOU 2847  O   CYS A 303    13894   9929   9663     60   -138   -774       O  
ATOM   2848  CB  CYS A 303     -27.373  36.340 -32.791  1.00 82.88           C  
ANISOU 2848  CB  CYS A 303    13058   9336   9097    102   -221   -827       C  
ATOM   2849  SG  CYS A 303     -29.179  36.321 -32.697  1.00 86.87           S  
ANISOU 2849  SG  CYS A 303    13509   9901   9596     76   -294   -851       S  
ATOM   2850  N   ILE A 304     -24.387  35.475 -33.391  1.00 78.96           N  
ANISOU 2850  N   ILE A 304    12654   8789   8559    132    -58   -783       N  
ATOM   2851  CA  ILE A 304     -22.975  35.720 -33.703  1.00 77.50           C  
ANISOU 2851  CA  ILE A 304    12473   8613   8362    153     -8   -753       C  
ATOM   2852  C   ILE A 304     -22.568  34.912 -34.936  1.00 86.02           C  
ANISOU 2852  C   ILE A 304    13644   9666   9372    139     50   -748       C  
ATOM   2853  O   ILE A 304     -21.981  35.470 -35.858  1.00 87.42           O  
ANISOU 2853  O   ILE A 304    13845   9849   9521    120     54   -725       O  
ATOM   2854  CB  ILE A 304     -22.081  35.429 -32.475  1.00 78.28           C  
ANISOU 2854  CB  ILE A 304    12506   8749   8487    210     42   -745       C  
ATOM   2855  CG1 ILE A 304     -22.299  36.506 -31.385  1.00 76.31           C  
ANISOU 2855  CG1 ILE A 304    12174   8527   8295    213    -17   -753       C  
ATOM   2856  CG2 ILE A 304     -20.599  35.306 -32.877  1.00 78.42           C  
ANISOU 2856  CG2 ILE A 304    12521   8802   8473    237    113   -713       C  
ATOM   2857  CD1 ILE A 304     -22.028  36.073 -29.997  1.00 71.22           C  
ANISOU 2857  CD1 ILE A 304    11467   7920   7674    259      9   -758       C  
ATOM   2858  N   ALA A 305     -22.935  33.617 -34.964  1.00 84.47           N  
ANISOU 2858  N   ALA A 305    13513   9438   9144    142     94   -770       N  
ATOM   2859  CA  ALA A 305     -22.646  32.670 -36.038  1.00 84.69           C  
ANISOU 2859  CA  ALA A 305    13653   9426   9099    134    158   -777       C  
ATOM   2860  C   ALA A 305     -23.242  33.045 -37.400  1.00 89.55           C  
ANISOU 2860  C   ALA A 305    14331  10029   9666     60    110   -784       C  
ATOM   2861  O   ALA A 305     -22.583  32.808 -38.421  1.00 90.66           O  
ANISOU 2861  O   ALA A 305    14542  10159   9747     60    160   -777       O  
ATOM   2862  CB  ALA A 305     -23.090  31.275 -35.638  1.00 85.16           C  
ANISOU 2862  CB  ALA A 305    13786   9435   9136    138    205   -804       C  
ATOM   2863  N   LEU A 306     -24.481  33.594 -37.433  1.00 84.68           N  
ANISOU 2863  N   LEU A 306    13686   9422   9065      6     16   -795       N  
ATOM   2864  CA  LEU A 306     -25.119  33.954 -38.711  1.00 84.57           C  
ANISOU 2864  CA  LEU A 306    13725   9410   8997    -58    -40   -795       C  
ATOM   2865  C   LEU A 306     -24.290  34.994 -39.500  1.00 89.00           C  
ANISOU 2865  C   LEU A 306    14289   9982   9545    -50    -45   -755       C  
ATOM   2866  O   LEU A 306     -24.152  34.860 -40.721  1.00 88.82           O  
ANISOU 2866  O   LEU A 306    14347   9951   9449    -87    -33   -751       O  
ATOM   2867  CB  LEU A 306     -26.566  34.429 -38.520  1.00 83.97           C  
ANISOU 2867  CB  LEU A 306    13595   9369   8942    -97   -143   -806       C  
ATOM   2868  CG  LEU A 306     -27.611  33.374 -38.242  1.00 86.73           C  
ANISOU 2868  CG  LEU A 306    13962   9724   9268   -152   -148   -845       C  
ATOM   2869  CD1 LEU A 306     -28.808  33.990 -37.588  1.00 86.03           C  
ANISOU 2869  CD1 LEU A 306    13768   9699   9222   -157   -236   -848       C  
ATOM   2870  CD2 LEU A 306     -28.031  32.692 -39.493  1.00 87.68           C  
ANISOU 2870  CD2 LEU A 306    14188   9833   9295   -236   -151   -866       C  
ATOM   2871  N   GLY A 307     -23.714  35.967 -38.776  1.00 84.98           N  
ANISOU 2871  N   GLY A 307    13700   9492   9098    -12    -58   -728       N  
ATOM   2872  CA  GLY A 307     -22.811  36.992 -39.299  1.00 84.81           C  
ANISOU 2872  CA  GLY A 307    13677   9480   9068    -19    -56   -686       C  
ATOM   2873  C   GLY A 307     -21.627  36.359 -40.011  1.00 89.64           C  
ANISOU 2873  C   GLY A 307    14336  10104   9619    -12     43   -676       C  
ATOM   2874  O   GLY A 307     -21.300  36.752 -41.133  1.00 90.64           O  
ANISOU 2874  O   GLY A 307    14516  10235   9689    -49     48   -651       O  
ATOM   2875  N   TYR A 308     -21.029  35.311 -39.400  1.00 84.80           N  
ANISOU 2875  N   TYR A 308    13713   9499   9010     42    126   -693       N  
ATOM   2876  CA  TYR A 308     -19.934  34.542 -40.004  1.00 84.45           C  
ANISOU 2876  CA  TYR A 308    13714   9471   8903     78    232   -687       C  
ATOM   2877  C   TYR A 308     -20.397  33.711 -41.194  1.00 89.77           C  
ANISOU 2877  C   TYR A 308    14517  10100   9492     47    255   -716       C  
ATOM   2878  O   TYR A 308     -19.657  33.605 -42.177  1.00 89.99           O  
ANISOU 2878  O   TYR A 308    14596  10146   9451     49    315   -704       O  
ATOM   2879  CB  TYR A 308     -19.267  33.651 -38.964  1.00 83.98           C  
ANISOU 2879  CB  TYR A 308    13613   9427   8867    166    307   -694       C  
ATOM   2880  CG  TYR A 308     -18.433  34.466 -38.017  1.00 83.55           C  
ANISOU 2880  CG  TYR A 308    13432   9445   8869    191    302   -660       C  
ATOM   2881  CD1 TYR A 308     -17.169  34.919 -38.387  1.00 85.80           C  
ANISOU 2881  CD1 TYR A 308    13668   9807   9126    198    353   -623       C  
ATOM   2882  CD2 TYR A 308     -18.925  34.842 -36.767  1.00 82.53           C  
ANISOU 2882  CD2 TYR A 308    13229   9316   8814    194    244   -668       C  
ATOM   2883  CE1 TYR A 308     -16.397  35.687 -37.519  1.00 86.61           C  
ANISOU 2883  CE1 TYR A 308    13651   9986   9269    197    342   -595       C  
ATOM   2884  CE2 TYR A 308     -18.163  35.618 -35.891  1.00 82.17           C  
ANISOU 2884  CE2 TYR A 308    13075   9336   8809    203    234   -644       C  
ATOM   2885  CZ  TYR A 308     -16.894  36.024 -36.270  1.00 88.62           C  
ANISOU 2885  CZ  TYR A 308    13845  10230   9595    199    282   -608       C  
ATOM   2886  OH  TYR A 308     -16.112  36.769 -35.438  1.00 87.60           O  
ANISOU 2886  OH  TYR A 308    13609  10179   9495    188    272   -586       O  
ATOM   2887  N   ILE A 309     -21.621  33.120 -41.108  1.00 86.53           N  
ANISOU 2887  N   ILE A 309    14157   9640   9078     11    210   -755       N  
ATOM   2888  CA  ILE A 309     -22.208  32.338 -42.204  1.00 87.14           C  
ANISOU 2888  CA  ILE A 309    14365   9676   9068    -44    219   -789       C  
ATOM   2889  C   ILE A 309     -22.287  33.224 -43.459  1.00 91.08           C  
ANISOU 2889  C   ILE A 309    14891  10202   9513   -103    171   -765       C  
ATOM   2890  O   ILE A 309     -21.919  32.763 -44.524  1.00 91.34           O  
ANISOU 2890  O   ILE A 309    15022  10226   9458   -119    225   -775       O  
ATOM   2891  CB  ILE A 309     -23.573  31.665 -41.829  1.00 89.93           C  
ANISOU 2891  CB  ILE A 309    14750   9994   9426   -101    166   -832       C  
ATOM   2892  CG1 ILE A 309     -23.348  30.438 -40.915  1.00 89.74           C  
ANISOU 2892  CG1 ILE A 309    14762   9919   9416    -50    245   -858       C  
ATOM   2893  CG2 ILE A 309     -24.386  31.262 -43.089  1.00 91.20           C  
ANISOU 2893  CG2 ILE A 309    15023  10138   9491   -197    133   -863       C  
ATOM   2894  CD1 ILE A 309     -24.519  30.071 -39.921  1.00 90.77           C  
ANISOU 2894  CD1 ILE A 309    14859  10038   9591    -94    191   -882       C  
ATOM   2895  N   ASN A 310     -22.676  34.501 -43.305  1.00 87.11           N  
ANISOU 2895  N   ASN A 310    14311   9729   9060   -126     78   -729       N  
ATOM   2896  CA  ASN A 310     -22.786  35.460 -44.398  1.00 87.76           C  
ANISOU 2896  CA  ASN A 310    14422   9829   9094   -176     24   -693       C  
ATOM   2897  C   ASN A 310     -21.422  35.835 -44.984  1.00 94.12           C  
ANISOU 2897  C   ASN A 310    15238  10660   9862   -163    100   -655       C  
ATOM   2898  O   ASN A 310     -21.254  35.796 -46.208  1.00 93.80           O  
ANISOU 2898  O   ASN A 310    15281  10627   9730   -202    119   -647       O  
ATOM   2899  CB  ASN A 310     -23.519  36.715 -43.925  1.00 85.79           C  
ANISOU 2899  CB  ASN A 310    14097   9588   8910   -181    -88   -662       C  
ATOM   2900  CG  ASN A 310     -23.842  37.676 -45.033  1.00104.19           C  
ANISOU 2900  CG  ASN A 310    16474  11925  11187   -224   -157   -619       C  
ATOM   2901  OD1 ASN A 310     -23.094  38.639 -45.306  1.00 96.78           O  
ANISOU 2901  OD1 ASN A 310    15536  10987  10250   -229   -153   -570       O  
ATOM   2902  ND2 ASN A 310     -24.970  37.428 -45.691  1.00 93.81           N  
ANISOU 2902  ND2 ASN A 310    15201  10623   9819   -264   -225   -634       N  
ATOM   2903  N   SER A 311     -20.460  36.204 -44.110  1.00 92.68           N  
ANISOU 2903  N   SER A 311    14968  10506   9742   -118    142   -632       N  
ATOM   2904  CA  SER A 311     -19.114  36.660 -44.482  1.00 93.93           C  
ANISOU 2904  CA  SER A 311    15102  10716   9870   -116    212   -591       C  
ATOM   2905  C   SER A 311     -18.293  35.597 -45.197  1.00 98.70           C  
ANISOU 2905  C   SER A 311    15766  11345  10391    -80    330   -609       C  
ATOM   2906  O   SER A 311     -17.498  35.941 -46.077  1.00 99.86           O  
ANISOU 2906  O   SER A 311    15931  11540  10472   -103    378   -577       O  
ATOM   2907  CB  SER A 311     -18.362  37.233 -43.277  1.00 98.50           C  
ANISOU 2907  CB  SER A 311    15561  11334  10530    -87    221   -568       C  
ATOM   2908  OG  SER A 311     -18.026  36.249 -42.308  1.00109.89           O  
ANISOU 2908  OG  SER A 311    16956  12790  12008     -7    282   -597       O  
ATOM   2909  N   SER A 312     -18.499  34.318 -44.840  1.00 94.57           N  
ANISOU 2909  N   SER A 312    15284  10786   9862    -22    380   -658       N  
ATOM   2910  CA  SER A 312     -17.805  33.191 -45.456  1.00 94.92           C  
ANISOU 2910  CA  SER A 312    15410  10832   9824     35    499   -684       C  
ATOM   2911  C   SER A 312     -18.606  32.488 -46.593  1.00 98.97           C  
ANISOU 2911  C   SER A 312    16079  11283  10242    -17    494   -730       C  
ATOM   2912  O   SER A 312     -17.984  31.852 -47.452  1.00 99.74           O  
ANISOU 2912  O   SER A 312    16264  11385  10246     12    588   -747       O  
ATOM   2913  CB  SER A 312     -17.351  32.195 -44.394  1.00 97.47           C  
ANISOU 2913  CB  SER A 312    15703  11145  10186    143    572   -705       C  
ATOM   2914  OG  SER A 312     -18.425  31.653 -43.645  1.00102.77           O  
ANISOU 2914  OG  SER A 312    16404  11741  10905    132    519   -742       O  
ATOM   2915  N   LEU A 313     -19.959  32.630 -46.626  1.00 94.32           N  
ANISOU 2915  N   LEU A 313    15521  10648   9666    -94    385   -750       N  
ATOM   2916  CA  LEU A 313     -20.784  31.993 -47.656  1.00 94.66           C  
ANISOU 2916  CA  LEU A 313    15703  10649   9614   -164    367   -795       C  
ATOM   2917  C   LEU A 313     -20.982  32.860 -48.905  1.00 98.75           C  
ANISOU 2917  C   LEU A 313    16255  11206  10059   -241    311   -763       C  
ATOM   2918  O   LEU A 313     -21.121  32.289 -49.986  1.00 98.98           O  
ANISOU 2918  O   LEU A 313    16409  11222   9977   -283    338   -795       O  
ATOM   2919  CB  LEU A 313     -22.126  31.455 -47.129  1.00 94.59           C  
ANISOU 2919  CB  LEU A 313    15716  10592   9633   -215    292   -838       C  
ATOM   2920  CG  LEU A 313     -22.375  29.935 -47.334  1.00100.95           C  
ANISOU 2920  CG  LEU A 313    16670  11320  10366   -227    361   -909       C  
ATOM   2921  CD1 LEU A 313     -21.470  29.070 -46.462  1.00100.85           C  
ANISOU 2921  CD1 LEU A 313    16665  11264  10388   -111    476   -920       C  
ATOM   2922  CD2 LEU A 313     -23.813  29.566 -47.056  1.00104.59           C  
ANISOU 2922  CD2 LEU A 313    17152  11757  10831   -323    271   -946       C  
ATOM   2923  N   ASN A 314     -20.941  34.211 -48.790  1.00 95.13           N  
ANISOU 2923  N   ASN A 314    15704  10789   9651   -260    238   -700       N  
ATOM   2924  CA  ASN A 314     -21.035  35.099 -49.969  1.00 95.49           C  
ANISOU 2924  CA  ASN A 314    15793  10866   9624   -326    189   -656       C  
ATOM   2925  C   ASN A 314     -19.880  34.811 -50.974  1.00101.23           C  
ANISOU 2925  C   ASN A 314    16589  11627  10247   -318    305   -650       C  
ATOM   2926  O   ASN A 314     -20.176  34.673 -52.164  1.00101.31           O  
ANISOU 2926  O   ASN A 314    16705  11643  10147   -374    297   -659       O  
ATOM   2927  CB  ASN A 314     -21.046  36.607 -49.601  1.00 92.00           C  
ANISOU 2927  CB  ASN A 314    15261  10441   9253   -338    106   -585       C  
ATOM   2928  CG  ASN A 314     -22.319  37.144 -48.995  1.00106.20           C  
ANISOU 2928  CG  ASN A 314    17012  12219  11121   -347    -22   -582       C  
ATOM   2929  OD1 ASN A 314     -23.429  36.853 -49.437  1.00 98.08           O  
ANISOU 2929  OD1 ASN A 314    16026  11189  10050   -384    -94   -605       O  
ATOM   2930  ND2 ASN A 314     -22.185  37.982 -47.979  1.00 98.57           N  
ANISOU 2930  ND2 ASN A 314    15951  11245  10257   -314    -56   -552       N  
ATOM   2931  N   PRO A 315     -18.581  34.703 -50.553  1.00 98.79           N  
ANISOU 2931  N   PRO A 315    16219  11357   9961   -249    414   -636       N  
ATOM   2932  CA  PRO A 315     -17.525  34.414 -51.548  1.00100.13           C  
ANISOU 2932  CA  PRO A 315    16444  11579  10022   -235    530   -631       C  
ATOM   2933  C   PRO A 315     -17.614  33.029 -52.184  1.00106.14           C  
ANISOU 2933  C   PRO A 315    17344  12300  10686   -205    611   -705       C  
ATOM   2934  O   PRO A 315     -17.451  32.936 -53.398  1.00107.45           O  
ANISOU 2934  O   PRO A 315    17608  12487  10732   -242    647   -710       O  
ATOM   2935  CB  PRO A 315     -16.209  34.588 -50.776  1.00101.61           C  
ANISOU 2935  CB  PRO A 315    16506  11837  10265   -161    619   -598       C  
ATOM   2936  CG  PRO A 315     -16.579  35.026 -49.408  1.00104.51           C  
ANISOU 2936  CG  PRO A 315    16764  12181  10766   -148    543   -587       C  
ATOM   2937  CD  PRO A 315     -18.021  34.815 -49.188  1.00 99.25           C  
ANISOU 2937  CD  PRO A 315    16149  11430  10132   -181    438   -623       C  
ATOM   2938  N   VAL A 316     -17.875  31.967 -51.384  1.00102.27           N  
ANISOU 2938  N   VAL A 316    16877  11745  10237   -141    642   -761       N  
ATOM   2939  CA  VAL A 316     -17.960  30.598 -51.894  1.00103.07           C  
ANISOU 2939  CA  VAL A 316    17135  11781  10245   -112    724   -837       C  
ATOM   2940  C   VAL A 316     -19.152  30.416 -52.840  1.00106.57           C  
ANISOU 2940  C   VAL A 316    17710  12181  10601   -232    642   -877       C  
ATOM   2941  O   VAL A 316     -18.956  29.869 -53.923  1.00107.02           O  
ANISOU 2941  O   VAL A 316    17903  12230  10531   -248    706   -915       O  
ATOM   2942  CB  VAL A 316     -17.894  29.496 -50.808  1.00107.34           C  
ANISOU 2942  CB  VAL A 316    17689  12252  10844    -16    783   -881       C  
ATOM   2943  CG1 VAL A 316     -16.534  29.493 -50.118  1.00107.12           C  
ANISOU 2943  CG1 VAL A 316    17549  12290  10863    120    887   -843       C  
ATOM   2944  CG2 VAL A 316     -19.018  29.634 -49.787  1.00106.45           C  
ANISOU 2944  CG2 VAL A 316    17519  12091  10835    -67    667   -885       C  
ATOM   2945  N   LEU A 317     -20.358  30.907 -52.467  1.00102.64           N  
ANISOU 2945  N   LEU A 317    17166  11670  10163   -315    501   -868       N  
ATOM   2946  CA  LEU A 317     -21.554  30.812 -53.315  1.00103.34           C  
ANISOU 2946  CA  LEU A 317    17350  11746  10167   -434    406   -898       C  
ATOM   2947  C   LEU A 317     -21.380  31.555 -54.632  1.00109.99           C  
ANISOU 2947  C   LEU A 317    18235  12652  10906   -490    385   -859       C  
ATOM   2948  O   LEU A 317     -21.767  31.023 -55.672  1.00111.73           O  
ANISOU 2948  O   LEU A 317    18591  12864  10997   -559    386   -903       O  
ATOM   2949  CB  LEU A 317     -22.825  31.280 -52.599  1.00102.50           C  
ANISOU 2949  CB  LEU A 317    17155  11644  10147   -492    262   -885       C  
ATOM   2950  CG  LEU A 317     -23.390  30.346 -51.526  1.00106.93           C  
ANISOU 2950  CG  LEU A 317    17714  12142  10773   -483    265   -938       C  
ATOM   2951  CD1 LEU A 317     -24.264  31.115 -50.554  1.00105.82           C  
ANISOU 2951  CD1 LEU A 317    17427  12033  10748   -497    146   -903       C  
ATOM   2952  CD2 LEU A 317     -24.172  29.171 -52.145  1.00110.40           C  
ANISOU 2952  CD2 LEU A 317    18315  12530  11101   -579    267  -1019       C  
ATOM   2953  N   TYR A 318     -20.752  32.752 -54.605  1.00106.05           N  
ANISOU 2953  N   TYR A 318    17631  12212  10450   -468    373   -777       N  
ATOM   2954  CA  TYR A 318     -20.484  33.518 -55.818  1.00106.48           C  
ANISOU 2954  CA  TYR A 318    17729  12325  10405   -522    361   -727       C  
ATOM   2955  C   TYR A 318     -19.514  32.750 -56.725  1.00110.16           C  
ANISOU 2955  C   TYR A 318    18305  12806  10745   -494    506   -765       C  
ATOM   2956  O   TYR A 318     -19.837  32.514 -57.886  1.00111.12           O  
ANISOU 2956  O   TYR A 318    18552  12938  10732   -561    499   -789       O  
ATOM   2957  CB  TYR A 318     -19.937  34.923 -55.500  1.00107.81           C  
ANISOU 2957  CB  TYR A 318    17775  12538  10647   -512    328   -632       C  
ATOM   2958  CG  TYR A 318     -20.008  35.865 -56.684  1.00112.16           C  
ANISOU 2958  CG  TYR A 318    18378  13134  11102   -588    277   -567       C  
ATOM   2959  CD1 TYR A 318     -19.152  35.714 -57.777  1.00115.85           C  
ANISOU 2959  CD1 TYR A 318    18925  13650  11442   -604    376   -561       C  
ATOM   2960  CD2 TYR A 318     -20.935  36.902 -56.722  1.00113.15           C  
ANISOU 2960  CD2 TYR A 318    18478  13256  11256   -634    132   -509       C  
ATOM   2961  CE1 TYR A 318     -19.239  36.553 -58.889  1.00117.99           C  
ANISOU 2961  CE1 TYR A 318    19256  13962  11613   -680    329   -497       C  
ATOM   2962  CE2 TYR A 318     -21.007  37.770 -57.813  1.00115.37           C  
ANISOU 2962  CE2 TYR A 318    18820  13572  11442   -695     82   -441       C  
ATOM   2963  CZ  TYR A 318     -20.159  37.588 -58.897  1.00124.45           C  
ANISOU 2963  CZ  TYR A 318    20055  14768  12464   -725    180   -434       C  
ATOM   2964  OH  TYR A 318     -20.225  38.430 -59.979  1.00126.31           O  
ANISOU 2964  OH  TYR A 318    20359  15038  12596   -791    133   -362       O  
ATOM   2965  N   ALA A 319     -18.339  32.367 -56.190  1.00105.93           N  
ANISOU 2965  N   ALA A 319    17721  12282  10246   -390    636   -769       N  
ATOM   2966  CA  ALA A 319     -17.282  31.636 -56.897  1.00106.53           C  
ANISOU 2966  CA  ALA A 319    17878  12385  10212   -328    793   -802       C  
ATOM   2967  C   ALA A 319     -17.756  30.301 -57.491  1.00110.16           C  
ANISOU 2967  C   ALA A 319    18528  12767  10562   -334    840   -902       C  
ATOM   2968  O   ALA A 319     -17.519  30.053 -58.673  1.00110.46           O  
ANISOU 2968  O   ALA A 319    18687  12828  10456   -362    896   -926       O  
ATOM   2969  CB  ALA A 319     -16.087  31.406 -55.973  1.00106.88           C  
ANISOU 2969  CB  ALA A 319    17812  12465  10334   -196    908   -788       C  
ATOM   2970  N   PHE A 320     -18.438  29.457 -56.692  1.00105.58           N  
ANISOU 2970  N   PHE A 320    17984  12091  10040   -320    816   -961       N  
ATOM   2971  CA  PHE A 320     -18.878  28.160 -57.186  1.00106.21           C  
ANISOU 2971  CA  PHE A 320    18262  12080  10015   -341    863  -1060       C  
ATOM   2972  C   PHE A 320     -20.086  28.263 -58.126  1.00110.99           C  
ANISOU 2972  C   PHE A 320    18968  12681  10520   -502    745  -1087       C  
ATOM   2973  O   PHE A 320     -20.469  27.264 -58.730  1.00112.41           O  
ANISOU 2973  O   PHE A 320    19330  12795  10586   -551    778  -1172       O  
ATOM   2974  CB  PHE A 320     -19.084  27.150 -56.049  1.00107.41           C  
ANISOU 2974  CB  PHE A 320    18439  12126  10247   -276    896  -1111       C  
ATOM   2975  CG  PHE A 320     -17.775  26.613 -55.509  1.00108.97           C  
ANISOU 2975  CG  PHE A 320    18613  12318  10472    -97   1052  -1109       C  
ATOM   2976  CD1 PHE A 320     -17.104  25.585 -56.161  1.00112.64           C  
ANISOU 2976  CD1 PHE A 320    19246  12736  10817    -11   1199  -1172       C  
ATOM   2977  CD2 PHE A 320     -17.195  27.160 -54.368  1.00110.00           C  
ANISOU 2977  CD2 PHE A 320    18553  12501  10741     -8   1052  -1044       C  
ATOM   2978  CE1 PHE A 320     -15.882  25.105 -55.675  1.00113.77           C  
ANISOU 2978  CE1 PHE A 320    19354  12892  10979    176   1344  -1163       C  
ATOM   2979  CE2 PHE A 320     -15.971  26.682 -53.884  1.00112.87           C  
ANISOU 2979  CE2 PHE A 320    18877  12887  11121    162   1190  -1035       C  
ATOM   2980  CZ  PHE A 320     -15.326  25.655 -54.540  1.00112.27           C  
ANISOU 2980  CZ  PHE A 320    18959  12772  10927    261   1335  -1092       C  
ATOM   2981  N   LEU A 321     -20.623  29.470 -58.329  1.00106.55           N  
ANISOU 2981  N   LEU A 321    18302  12196   9986   -581    614  -1013       N  
ATOM   2982  CA  LEU A 321     -21.690  29.672 -59.306  1.00106.90           C  
ANISOU 2982  CA  LEU A 321    18426  12268   9924   -721    498  -1024       C  
ATOM   2983  C   LEU A 321     -21.187  30.513 -60.520  1.00113.81           C  
ANISOU 2983  C   LEU A 321    19321  13232  10689   -750    505   -965       C  
ATOM   2984  O   LEU A 321     -21.930  30.699 -61.489  1.00114.64           O  
ANISOU 2984  O   LEU A 321    19504  13374  10680   -857    420   -967       O  
ATOM   2985  CB  LEU A 321     -22.986  30.209 -58.670  1.00105.34           C  
ANISOU 2985  CB  LEU A 321    18122  12086   9818   -793    328   -995       C  
ATOM   2986  CG  LEU A 321     -23.718  29.218 -57.754  1.00108.89           C  
ANISOU 2986  CG  LEU A 321    18592  12456  10325   -812    314  -1066       C  
ATOM   2987  CD1 LEU A 321     -24.734  29.913 -56.882  1.00107.50           C  
ANISOU 2987  CD1 LEU A 321    18261  12317  10269   -843    170  -1021       C  
ATOM   2988  CD2 LEU A 321     -24.363  28.080 -58.539  1.00113.25           C  
ANISOU 2988  CD2 LEU A 321    19336  12964  10730   -924    321  -1163       C  
ATOM   2989  N   ASP A 322     -19.894  30.942 -60.482  1.00111.20           N  
ANISOU 2989  N   ASP A 322    18927  12944  10382   -658    614   -915       N  
ATOM   2990  CA  ASP A 322     -19.175  31.681 -61.529  1.00112.57           C  
ANISOU 2990  CA  ASP A 322    19114  13203  10454   -676    654   -856       C  
ATOM   2991  C   ASP A 322     -18.756  30.642 -62.585  1.00120.78           C  
ANISOU 2991  C   ASP A 322    20336  14234  11320   -672    778   -939       C  
ATOM   2992  O   ASP A 322     -18.098  29.659 -62.233  1.00120.92           O  
ANISOU 2992  O   ASP A 322    20400  14202  11341   -570    911  -1004       O  
ATOM   2993  CB  ASP A 322     -17.938  32.392 -60.910  1.00113.53           C  
ANISOU 2993  CB  ASP A 322    19085  13379  10672   -587    734   -781       C  
ATOM   2994  CG  ASP A 322     -16.975  33.130 -61.839  1.00121.08           C  
ANISOU 2994  CG  ASP A 322    20035  14436  11533   -603    804   -714       C  
ATOM   2995  OD1 ASP A 322     -16.439  32.496 -62.769  1.00122.41           O1-
ANISOU 2995  OD1 ASP A 322    20320  14632  11556   -593    912   -759       O1-
ATOM   2996  OD2 ASP A 322     -16.703  34.322 -61.587  1.00125.07           O  
ANISOU 2996  OD2 ASP A 322    20422  14989  12108   -625    760   -619       O  
ATOM   2997  N   LYS A 323     -19.152  30.852 -63.868  1.00119.65           N  
ANISOU 2997  N   LYS A 323    20305  14136  11021   -773    735   -938       N  
ATOM   2998  CA  LYS A 323     -18.864  29.940 -64.991  1.00121.60           C  
ANISOU 2998  CA  LYS A 323    20745  14378  11081   -787    842  -1021       C  
ATOM   2999  C   LYS A 323     -17.366  29.649 -65.191  1.00125.78           C  
ANISOU 2999  C   LYS A 323    21279  14946  11567   -662   1038  -1026       C  
ATOM   3000  O   LYS A 323     -16.974  28.481 -65.291  1.00125.71           O  
ANISOU 3000  O   LYS A 323    21397  14877  11492   -586   1167  -1121       O  
ATOM   3001  CB  LYS A 323     -19.505  30.444 -66.297  1.00125.83           C  
ANISOU 3001  CB  LYS A 323    21371  14979  11458   -922    747   -998       C  
ATOM   3002  CG  LYS A 323     -21.022  30.261 -66.368  1.00144.21           C  
ANISOU 3002  CG  LYS A 323    23747  17279  13766  -1046    580  -1031       C  
ATOM   3003  CD  LYS A 323     -21.580  30.708 -67.724  1.00153.56           C  
ANISOU 3003  CD  LYS A 323    25023  18548  14775  -1169    491  -1005       C  
ATOM   3004  CE  LYS A 323     -23.088  30.669 -67.771  1.00162.92           C  
ANISOU 3004  CE  LYS A 323    26217  19744  15942  -1290    310  -1021       C  
ATOM   3005  NZ  LYS A 323     -23.614  31.048 -69.108  1.00171.97           N1+
ANISOU 3005  NZ  LYS A 323    27454  20984  16904  -1404    222   -995       N1+
ATOM   3006  N   ASN A 324     -16.542  30.715 -65.226  1.00122.50           N  
ANISOU 3006  N   ASN A 324    20727  14633  11185   -640   1062   -923       N  
ATOM   3007  CA  ASN A 324     -15.087  30.649 -65.384  1.00123.45           C  
ANISOU 3007  CA  ASN A 324    20803  14834  11268   -532   1239   -907       C  
ATOM   3008  C   ASN A 324     -14.428  29.854 -64.245  1.00125.87           C  
ANISOU 3008  C   ASN A 324    21041  15096  11688   -374   1346   -948       C  
ATOM   3009  O   ASN A 324     -13.657  28.934 -64.535  1.00126.51           O  
ANISOU 3009  O   ASN A 324    21205  15180  11685   -262   1506  -1012       O  
ATOM   3010  CB  ASN A 324     -14.493  32.071 -65.512  1.00127.99           C  
ANISOU 3010  CB  ASN A 324    21230  15527  11871   -578   1215   -777       C  
ATOM   3011  CG  ASN A 324     -12.977  32.159 -65.517  1.00165.62           C  
ANISOU 3011  CG  ASN A 324    25899  20409  16618   -484   1385   -743       C  
ATOM   3012  OD1 ASN A 324     -12.267  31.316 -66.087  1.00169.18           O  
ANISOU 3012  OD1 ASN A 324    26434  20896  16951   -400   1540   -806       O  
ATOM   3013  ND2 ASN A 324     -12.447  33.198 -64.887  1.00155.44           N  
ANISOU 3013  ND2 ASN A 324    24431  19189  15438   -497   1361   -644       N  
ATOM   3014  N   PHE A 325     -14.764  30.196 -62.961  1.00119.85           N  
ANISOU 3014  N   PHE A 325    20138  14292  11108   -358   1257   -912       N  
ATOM   3015  CA  PHE A 325     -14.269  29.560 -61.726  1.00118.09           C  
ANISOU 3015  CA  PHE A 325    19834  14028  11008   -217   1329   -937       C  
ATOM   3016  C   PHE A 325     -14.630  28.078 -61.658  1.00123.55           C  
ANISOU 3016  C   PHE A 325    20704  14589  11652   -153   1392  -1054       C  
ATOM   3017  O   PHE A 325     -13.794  27.273 -61.241  1.00122.98           O  
ANISOU 3017  O   PHE A 325    20639  14502  11584      3   1531  -1089       O  
ATOM   3018  CB  PHE A 325     -14.794  30.293 -60.474  1.00117.40           C  
ANISOU 3018  CB  PHE A 325    19584  13916  11107   -245   1196   -878       C  
ATOM   3019  CG  PHE A 325     -14.227  29.799 -59.159  1.00117.08           C  
ANISOU 3019  CG  PHE A 325    19438  13854  11194   -107   1260   -886       C  
ATOM   3020  CD1 PHE A 325     -14.790  28.709 -58.501  1.00118.75           C  
ANISOU 3020  CD1 PHE A 325    19735  13939  11445    -54   1262   -963       C  
ATOM   3021  CD2 PHE A 325     -13.127  30.419 -58.584  1.00118.11           C  
ANISOU 3021  CD2 PHE A 325    19387  14096  11395    -38   1318   -814       C  
ATOM   3022  CE1 PHE A 325     -14.256  28.243 -57.302  1.00118.92           C  
ANISOU 3022  CE1 PHE A 325    19668  13943  11575     80   1322   -963       C  
ATOM   3023  CE2 PHE A 325     -12.594  29.954 -57.386  1.00120.38           C  
ANISOU 3023  CE2 PHE A 325    19572  14379  11787     93   1373   -818       C  
ATOM   3024  CZ  PHE A 325     -13.166  28.872 -56.748  1.00118.20           C  
ANISOU 3024  CZ  PHE A 325    19388  13972  11549    159   1374   -890       C  
ATOM   3025  N   LYS A 326     -15.883  27.732 -62.024  1.00122.15           N  
ANISOU 3025  N   LYS A 326    20667  14318  11426   -275   1285  -1111       N  
ATOM   3026  CA  LYS A 326     -16.402  26.362 -62.054  1.00123.81           C  
ANISOU 3026  CA  LYS A 326    21078  14389  11574   -263   1325  -1227       C  
ATOM   3027  C   LYS A 326     -15.542  25.457 -62.962  1.00132.71           C  
ANISOU 3027  C   LYS A 326    22378  15506  12537   -167   1505  -1300       C  
ATOM   3028  O   LYS A 326     -15.227  24.329 -62.570  1.00133.07           O  
ANISOU 3028  O   LYS A 326    22535  15450  12577    -46   1616  -1372       O  
ATOM   3029  CB  LYS A 326     -17.860  26.353 -62.541  1.00126.05           C  
ANISOU 3029  CB  LYS A 326    21467  14623  11803   -449   1171  -1265       C  
ATOM   3030  CG  LYS A 326     -18.893  26.625 -61.460  1.00129.37           C  
ANISOU 3030  CG  LYS A 326    21779  15000  12375   -513   1021  -1241       C  
ATOM   3031  CD  LYS A 326     -20.328  26.433 -61.972  1.00135.39           C  
ANISOU 3031  CD  LYS A 326    22647  15731  13062   -693    881  -1288       C  
ATOM   3032  CE  LYS A 326     -20.890  27.622 -62.720  1.00141.17           C  
ANISOU 3032  CE  LYS A 326    23305  16578  13754   -808    743  -1213       C  
ATOM   3033  NZ  LYS A 326     -22.296  27.391 -63.143  1.00147.87           N1+
ANISOU 3033  NZ  LYS A 326    24234  17419  14529   -973    603  -1257       N1+
ATOM   3034  N   ARG A 327     -15.156  25.962 -64.162  1.00132.12           N  
ANISOU 3034  N   ARG A 327    22334  15538  12328   -213   1539  -1279       N  
ATOM   3035  CA  ARG A 327     -14.310  25.237 -65.120  1.00135.00           C  
ANISOU 3035  CA  ARG A 327    22853  15918  12523   -122   1714  -1343       C  
ATOM   3036  C   ARG A 327     -12.882  25.049 -64.573  1.00140.98           C  
ANISOU 3036  C   ARG A 327    23492  16745  13328     93   1883  -1314       C  
ATOM   3037  O   ARG A 327     -12.308  23.961 -64.715  1.00142.55           O  
ANISOU 3037  O   ARG A 327    23830  16885  13447    240   2038  -1393       O  
ATOM   3038  CB  ARG A 327     -14.274  25.956 -66.482  1.00136.44           C  
ANISOU 3038  CB  ARG A 327    23073  16217  12553   -237   1696  -1313       C  
ATOM   3039  N   CYS A 328     -12.328  26.102 -63.924  1.00136.16           N  
ANISOU 3039  N   CYS A 328    22630  16261  12845    112   1850  -1201       N  
ATOM   3040  CA  CYS A 328     -10.977  26.094 -63.355  1.00135.80           C  
ANISOU 3040  CA  CYS A 328    22426  16323  12849    294   1990  -1157       C  
ATOM   3041  C   CYS A 328     -10.834  25.204 -62.108  1.00138.21           C  
ANISOU 3041  C   CYS A 328    22717  16527  13268    453   2034  -1190       C  
ATOM   3042  O   CYS A 328      -9.727  24.730 -61.850  1.00138.41           O  
ANISOU 3042  O   CYS A 328    22690  16618  13282    646   2186  -1189       O  
ATOM   3043  CB  CYS A 328     -10.479  27.512 -63.103  1.00135.09           C  
ANISOU 3043  CB  CYS A 328    22087  16398  12842    230   1933  -1030       C  
ATOM   3044  SG  CYS A 328     -10.091  28.430 -64.616  1.00140.29           S  
ANISOU 3044  SG  CYS A 328    22757  17211  13335    107   1958   -977       S  
ATOM   3045  N   PHE A 329     -11.938  24.959 -61.356  1.00132.94           N  
ANISOU 3045  N   PHE A 329    22096  15712  12701    379   1907  -1217       N  
ATOM   3046  CA  PHE A 329     -11.938  24.084 -60.175  1.00145.98           C  
ANISOU 3046  CA  PHE A 329    23760  17251  14454    512   1939  -1248       C  
ATOM   3047  C   PHE A 329     -12.109  22.621 -60.598  1.00178.14           C  
ANISOU 3047  C   PHE A 329    28119  21158  18407    588   2044  -1368       C  
ATOM   3048  O   PHE A 329     -12.916  22.318 -61.475  1.00145.83           O  
ANISOU 3048  O   PHE A 329    24223  16982  14204    453   2003  -1439       O  
ATOM   3049  CB  PHE A 329     -13.013  24.501 -59.140  1.00145.43           C  
ANISOU 3049  CB  PHE A 329    23604  17109  14542    394   1763  -1219       C  
ATOM   3050  CG  PHE A 329     -13.220  23.533 -57.990  1.00146.10           C  
ANISOU 3050  CG  PHE A 329    23740  17057  14716    497   1782  -1257       C  
ATOM   3051  CD1 PHE A 329     -12.261  23.393 -56.991  1.00148.45           C  
ANISOU 3051  CD1 PHE A 329    23895  17406  15102    682   1864  -1211       C  
ATOM   3052  CD2 PHE A 329     -14.371  22.756 -57.910  1.00147.85           C  
ANISOU 3052  CD2 PHE A 329    24150  17104  14922    401   1718  -1334       C  
ATOM   3053  CE1 PHE A 329     -12.446  22.484 -55.940  1.00148.87           C  
ANISOU 3053  CE1 PHE A 329    24007  17328  15227    781   1883  -1239       C  
ATOM   3054  CE2 PHE A 329     -14.557  21.853 -56.854  1.00150.03           C  
ANISOU 3054  CE2 PHE A 329    24486  17247  15271    486   1740  -1364       C  
ATOM   3055  CZ  PHE A 329     -13.594  21.725 -55.876  1.00147.74           C  
ANISOU 3055  CZ  PHE A 329    24065  17000  15069    681   1823  -1314       C  
TER    3056      PHE A 329                                                      
ATOM   3057  N   ASP B1002     -24.509  27.472 -75.063  1.00179.14           N  
ANISOU 3057  N   ASP B1002    31416  18753  17898  -2173    287    568       N  
ATOM   3058  CA  ASP B1002     -24.190  27.131 -73.678  1.00177.36           C  
ANISOU 3058  CA  ASP B1002    30877  18629  17882  -2092    317    512       C  
ATOM   3059  C   ASP B1002     -25.339  26.364 -73.017  1.00179.71           C  
ANISOU 3059  C   ASP B1002    30983  19037  18261  -1884    182    466       C  
ATOM   3060  O   ASP B1002     -26.487  26.813 -73.086  1.00179.77           O  
ANISOU 3060  O   ASP B1002    31093  19005  18207  -1753    -25    492       O  
ATOM   3061  CB  ASP B1002     -23.843  28.395 -72.872  1.00179.46           C  
ANISOU 3061  CB  ASP B1002    31183  18797  18205  -2095    236    540       C  
ATOM   3062  N   LEU B1003     -25.026  25.208 -72.381  1.00174.28           N  
ANISOU 3062  N   LEU B1003    30014  18490  17713  -1856    299    402       N  
ATOM   3063  CA  LEU B1003     -25.987  24.336 -71.686  1.00172.30           C  
ANISOU 3063  CA  LEU B1003    29552  18360  17554  -1683    201    358       C  
ATOM   3064  C   LEU B1003     -26.691  25.037 -70.520  1.00175.01           C  
ANISOU 3064  C   LEU B1003    29807  18704  17987  -1510     20    359       C  
ATOM   3065  O   LEU B1003     -27.873  24.780 -70.287  1.00173.87           O  
ANISOU 3065  O   LEU B1003    29601  18615  17845  -1355   -131    358       O  
ATOM   3066  CB  LEU B1003     -25.311  23.048 -71.197  1.00171.06           C  
ANISOU 3066  CB  LEU B1003    29133  18334  17530  -1706    379    293       C  
ATOM   3067  N   GLU B1004     -25.964  25.919 -69.797  1.00171.48           N  
ANISOU 3067  N   GLU B1004    29354  18194  17606  -1538     37    364       N  
ATOM   3068  CA  GLU B1004     -26.478  26.701 -68.668  1.00170.68           C  
ANISOU 3068  CA  GLU B1004    29204  18070  17575  -1379   -120    362       C  
ATOM   3069  C   GLU B1004     -27.452  27.773 -69.165  1.00175.04           C  
ANISOU 3069  C   GLU B1004    30010  18503  17993  -1290   -318    418       C  
ATOM   3070  O   GLU B1004     -28.477  28.014 -68.521  1.00174.01           O  
ANISOU 3070  O   GLU B1004    29827  18399  17891  -1092   -479    416       O  
ATOM   3071  CB  GLU B1004     -25.325  27.343 -67.884  1.00172.14           C  
ANISOU 3071  CB  GLU B1004    29351  18204  17851  -1466    -45    352       C  
ATOM   3072  N   ASP B1005     -27.135  28.395 -70.324  1.00172.88           N  
ANISOU 3072  N   ASP B1005    30014  18103  17571  -1431   -303    471       N  
ATOM   3073  CA  ASP B1005     -27.959  29.415 -70.976  1.00173.78           C  
ANISOU 3073  CA  ASP B1005    30407  18085  17536  -1368   -486    533       C  
ATOM   3074  C   ASP B1005     -29.218  28.779 -71.580  1.00176.57           C  
ANISOU 3074  C   ASP B1005    30755  18512  17822  -1253   -603    544       C  
ATOM   3075  O   ASP B1005     -30.285  29.390 -71.531  1.00176.85           O  
ANISOU 3075  O   ASP B1005    30876  18508  17809  -1089   -801    577       O  
ATOM   3076  CB  ASP B1005     -27.157  30.165 -72.052  1.00177.39           C  
ANISOU 3076  CB  ASP B1005    31160  18389  17851  -1577   -416    590       C  
ATOM   3077  CG  ASP B1005     -27.589  31.607 -72.260  1.00190.63           C  
ANISOU 3077  CG  ASP B1005    33131  19885  19415  -1528   -595    651       C  
ATOM   3078  OD1 ASP B1005     -28.764  31.832 -72.631  1.00191.69           O  
ANISOU 3078  OD1 ASP B1005    33374  19996  19465  -1378   -775    681       O  
ATOM   3079  OD2 ASP B1005     -26.748  32.512 -72.065  1.00198.55           O1-
ANISOU 3079  OD2 ASP B1005    34259  20767  20414  -1641   -560    674       O1-
ATOM   3080  N   ASN B1006     -29.093  27.548 -72.130  1.00171.63           N  
ANISOU 3080  N   ASN B1006    30027  17990  17193  -1336   -485    518       N  
ATOM   3081  CA  ASN B1006     -30.212  26.792 -72.704  1.00170.84           C  
ANISOU 3081  CA  ASN B1006    29908  17969  17035  -1258   -590    526       C  
ATOM   3082  C   ASN B1006     -31.176  26.340 -71.602  1.00172.66           C  
ANISOU 3082  C   ASN B1006    29866  18336  17400  -1050   -701    497       C  
ATOM   3083  O   ASN B1006     -32.389  26.421 -71.794  1.00172.54           O  
ANISOU 3083  O   ASN B1006    29868  18348  17341   -916   -883    531       O  
ATOM   3084  CB  ASN B1006     -29.716  25.590 -73.525  1.00169.60           C  
ANISOU 3084  CB  ASN B1006    29733  17872  16837  -1411   -423    498       C  
ATOM   3085  CG  ASN B1006     -29.212  25.921 -74.913  1.00183.60           C  
ANISOU 3085  CG  ASN B1006    31811  19523  18424  -1587   -356    540       C  
ATOM   3086  OD1 ASN B1006     -28.086  25.579 -75.286  1.00174.17           O  
ANISOU 3086  OD1 ASN B1006    30640  18320  17218  -1751   -143    522       O  
ATOM   3087  ND2 ASN B1006     -30.039  26.573 -75.721  1.00175.53           N  
ANISOU 3087  ND2 ASN B1006    31031  18411  17251  -1552   -532    601       N  
ATOM   3088  N   TRP B1007     -30.627  25.901 -70.440  1.00167.39           N  
ANISOU 3088  N   TRP B1007    28950  17756  16896  -1024   -593    441       N  
ATOM   3089  CA  TRP B1007     -31.361  25.457 -69.243  1.00165.64           C  
ANISOU 3089  CA  TRP B1007    28456  17667  16811   -841   -662    411       C  
ATOM   3090  C   TRP B1007     -32.257  26.562 -68.692  1.00167.57           C  
ANISOU 3090  C   TRP B1007    28756  17867  17048   -643   -854    444       C  
ATOM   3091  O   TRP B1007     -33.363  26.282 -68.228  1.00166.32           O  
ANISOU 3091  O   TRP B1007    28446  17813  16933   -471   -973    450       O  
ATOM   3092  CB  TRP B1007     -30.377  25.045 -68.142  1.00163.45           C  
ANISOU 3092  CB  TRP B1007    27966  17448  16687   -872   -506    351       C  
ATOM   3093  CG  TRP B1007     -30.406  23.597 -67.759  1.00163.53           C  
ANISOU 3093  CG  TRP B1007    27719  17614  16800   -873   -414    304       C  
ATOM   3094  CD1 TRP B1007     -31.358  22.672 -68.083  1.00166.34           C  
ANISOU 3094  CD1 TRP B1007    27990  18072  17141   -825   -478    308       C  
ATOM   3095  CD2 TRP B1007     -29.456  22.921 -66.925  1.00162.35           C  
ANISOU 3095  CD2 TRP B1007    27367  17532  16785   -921   -254    248       C  
ATOM   3096  NE1 TRP B1007     -31.045  21.454 -67.523  1.00164.65           N  
ANISOU 3096  NE1 TRP B1007    27548  17974  17039   -846   -362    258       N  
ATOM   3097  CE2 TRP B1007     -29.882  21.578 -66.806  1.00165.44           C  
ANISOU 3097  CE2 TRP B1007    27570  18056  17232   -896   -223    220       C  
ATOM   3098  CE3 TRP B1007     -28.271  23.317 -66.278  1.00163.40           C  
ANISOU 3098  CE3 TRP B1007    27462  17625  16997   -989   -142    223       C  
ATOM   3099  CZ2 TRP B1007     -29.165  20.630 -66.065  1.00163.53           C  
ANISOU 3099  CZ2 TRP B1007    27114  17900  17118   -925    -81    166       C  
ATOM   3100  CZ3 TRP B1007     -27.564  22.376 -65.543  1.00163.73           C  
ANISOU 3100  CZ3 TRP B1007    27276  17763  17171  -1017     -6    172       C  
ATOM   3101  CH2 TRP B1007     -28.012  21.050 -65.440  1.00163.43           C  
ANISOU 3101  CH2 TRP B1007    27063  17850  17183   -978     25    143       C  
ATOM   3102  N   GLU B1008     -31.755  27.814 -68.727  1.00163.54           N  
ANISOU 3102  N   GLU B1008    28458  17198  16482   -668   -879    467       N  
ATOM   3103  CA  GLU B1008     -32.459  29.003 -68.264  1.00163.40           C  
ANISOU 3103  CA  GLU B1008    28547  17098  16437   -484  -1053    497       C  
ATOM   3104  C   GLU B1008     -33.601  29.377 -69.214  1.00166.79           C  
ANISOU 3104  C   GLU B1008    29146  17491  16736   -395  -1234    562       C  
ATOM   3105  O   GLU B1008     -34.712  29.608 -68.734  1.00166.58           O  
ANISOU 3105  O   GLU B1008    29039  17520  16734   -175  -1385    578       O  
ATOM   3106  CB  GLU B1008     -31.485  30.178 -68.075  1.00165.50           C  
ANISOU 3106  CB  GLU B1008    29017  17190  16676   -569  -1021    502       C  
ATOM   3107  N   THR B1009     -33.343  29.401 -70.556  1.00162.60           N  
ANISOU 3107  N   THR B1009    28841  16874  16066   -560  -1219    601       N  
ATOM   3108  CA  THR B1009     -34.345  29.748 -71.585  1.00162.89           C  
ANISOU 3108  CA  THR B1009    29067  16863  15962   -501  -1396    667       C  
ATOM   3109  C   THR B1009     -35.525  28.769 -71.598  1.00164.26           C  
ANISOU 3109  C   THR B1009    29025  17212  16174   -386  -1492    672       C  
ATOM   3110  O   THR B1009     -36.618  29.153 -72.009  1.00164.72           O  
ANISOU 3110  O   THR B1009    29157  17267  16163   -253  -1684    727       O  
ATOM   3111  CB  THR B1009     -33.726  29.941 -72.990  1.00169.58           C  
ANISOU 3111  CB  THR B1009    30212  17577  16642   -718  -1344    706       C  
ATOM   3112  OG1 THR B1009     -32.994  28.780 -73.381  1.00168.08           O  
ANISOU 3112  OG1 THR B1009    29926  17468  16471   -903  -1153    666       O  
ATOM   3113  CG2 THR B1009     -32.849  31.184 -73.087  1.00168.33           C  
ANISOU 3113  CG2 THR B1009    30316  17225  16417   -809  -1312    730       C  
ATOM   3114  N   LEU B1010     -35.311  27.521 -71.128  1.00157.97           N  
ANISOU 3114  N   LEU B1010    27962  16568  15492   -435  -1365    618       N  
ATOM   3115  CA  LEU B1010     -36.353  26.499 -71.023  1.00156.78           C  
ANISOU 3115  CA  LEU B1010    27583  16592  15395   -350  -1442    621       C  
ATOM   3116  C   LEU B1010     -37.287  26.850 -69.869  1.00160.17           C  
ANISOU 3116  C   LEU B1010    27812  17115  15930    -97  -1559    627       C  
ATOM   3117  O   LEU B1010     -38.504  26.715 -70.006  1.00160.06           O  
ANISOU 3117  O   LEU B1010    27715  17193  15908     35  -1720    672       O  
ATOM   3118  CB  LEU B1010     -35.734  25.106 -70.786  1.00155.08           C  
ANISOU 3118  CB  LEU B1010    27163  16491  15270   -482  -1260    559       C  
ATOM   3119  CG  LEU B1010     -35.206  24.363 -72.012  1.00159.88           C  
ANISOU 3119  CG  LEU B1010    27915  17061  15770   -696  -1165    554       C  
ATOM   3120  CD1 LEU B1010     -34.037  23.480 -71.645  1.00158.50           C  
ANISOU 3120  CD1 LEU B1010    27615  16925  15682   -831   -930    484       C  
ATOM   3121  CD2 LEU B1010     -36.303  23.529 -72.675  1.00162.83           C  
ANISOU 3121  CD2 LEU B1010    28248  17528  16093   -686  -1297    584       C  
ATOM   3122  N   ASN B1011     -36.704  27.319 -68.738  1.00156.14           N  
ANISOU 3122  N   ASN B1011    27229  16582  15515    -30  -1479    585       N  
ATOM   3123  CA  ASN B1011     -37.403  27.693 -67.506  1.00155.53           C  
ANISOU 3123  CA  ASN B1011    26977  16582  15535    210  -1553    578       C  
ATOM   3124  C   ASN B1011     -38.100  29.052 -67.612  1.00160.57           C  
ANISOU 3124  C   ASN B1011    27808  17109  16091    396  -1732    630       C  
ATOM   3125  O   ASN B1011     -39.294  29.135 -67.312  1.00160.74           O  
ANISOU 3125  O   ASN B1011    27707  17231  16136    607  -1868    665       O  
ATOM   3126  CB  ASN B1011     -36.443  27.657 -66.305  1.00154.82           C  
ANISOU 3126  CB  ASN B1011    26768  16496  15561    195  -1400    510       C  
ATOM   3127  CG  ASN B1011     -35.852  26.300 -65.971  1.00177.46           C  
ANISOU 3127  CG  ASN B1011    29408  19489  18531     62  -1234    458       C  
ATOM   3128  OD1 ASN B1011     -35.772  25.381 -66.801  1.00171.48           O  
ANISOU 3128  OD1 ASN B1011    28638  18775  17743    -83  -1187    461       O  
ATOM   3129  ND2 ASN B1011     -35.405  26.150 -64.733  1.00168.31           N  
ANISOU 3129  ND2 ASN B1011    28080  18381  17491    112  -1144    407       N  
ATOM   3130  N   ASP B1012     -37.367  30.105 -68.063  1.00157.68           N  
ANISOU 3130  N   ASP B1012    27745  16538  15628    317  -1731    641       N  
ATOM   3131  CA  ASP B1012     -37.849  31.492 -68.235  1.00159.14           C  
ANISOU 3131  CA  ASP B1012    28176  16573  15718    472  -1894    688       C  
ATOM   3132  C   ASP B1012     -38.985  31.632 -69.262  1.00163.93           C  
ANISOU 3132  C   ASP B1012    28879  17187  16219    555  -2083    766       C  
ATOM   3133  O   ASP B1012     -39.589  32.704 -69.371  1.00164.56           O  
ANISOU 3133  O   ASP B1012    29131  17166  16228    727  -2241    811       O  
ATOM   3134  CB  ASP B1012     -36.685  32.439 -68.589  1.00161.48           C  
ANISOU 3134  CB  ASP B1012    28783  16644  15929    311  -1835    686       C  
ATOM   3135  N   ASN B1013     -39.267  30.540 -70.001  1.00160.03           N  
ANISOU 3135  N   ASN B1013    28279  16810  15714    436  -2073    780       N  
ATOM   3136  CA  ASN B1013     -40.305  30.436 -71.024  1.00160.71           C  
ANISOU 3136  CA  ASN B1013    28429  16929  15706    475  -2250    852       C  
ATOM   3137  C   ASN B1013     -41.521  29.615 -70.538  1.00162.33           C  
ANISOU 3137  C   ASN B1013    28297  17365  16014    633  -2336    868       C  
ATOM   3138  O   ASN B1013     -42.623  29.796 -71.058  1.00162.95           O  
ANISOU 3138  O   ASN B1013    28384  17487  16043    754  -2527    937       O  
ATOM   3139  CB  ASN B1013     -39.709  29.881 -72.310  1.00162.16           C  
ANISOU 3139  CB  ASN B1013    28788  17051  15776    207  -2188    861       C  
ATOM   3140  CG  ASN B1013     -40.641  29.924 -73.475  1.00189.07           C  
ANISOU 3140  CG  ASN B1013    32332  20450  19056    221  -2382    937       C  
ATOM   3141  OD1 ASN B1013     -41.484  29.043 -73.626  1.00188.39           O  
ANISOU 3141  OD1 ASN B1013    32052  20523  19005    246  -2459    956       O  
ATOM   3142  ND2 ASN B1013     -40.516  30.948 -74.306  1.00179.78           N  
ANISOU 3142  ND2 ASN B1013    31495  19085  17729    200  -2473    987       N  
ATOM   3143  N   LEU B1014     -41.328  28.748 -69.520  1.00156.21           N  
ANISOU 3143  N   LEU B1014    27227  16739  15384    633  -2201    811       N  
ATOM   3144  CA  LEU B1014     -42.407  27.974 -68.899  1.00155.42           C  
ANISOU 3144  CA  LEU B1014    26792  16866  15395    774  -2259    826       C  
ATOM   3145  C   LEU B1014     -43.360  28.925 -68.146  1.00160.45           C  
ANISOU 3145  C   LEU B1014    27363  17535  16065   1086  -2391    861       C  
ATOM   3146  O   LEU B1014     -44.552  28.633 -68.029  1.00160.98           O  
ANISOU 3146  O   LEU B1014    27224  17766  16176   1236  -2513    913       O  
ATOM   3147  CB  LEU B1014     -41.836  26.918 -67.933  1.00153.23           C  
ANISOU 3147  CB  LEU B1014    26253  16712  15255    695  -2070    755       C  
ATOM   3148  CG  LEU B1014     -41.505  25.552 -68.541  1.00156.50           C  
ANISOU 3148  CG  LEU B1014    26592  17199  15673    460  -1983    736       C  
ATOM   3149  CD1 LEU B1014     -40.337  24.912 -67.834  1.00154.49           C  
ANISOU 3149  CD1 LEU B1014    26243  16949  15507    332  -1761    654       C  
ATOM   3150  CD2 LEU B1014     -42.706  24.619 -68.493  1.00158.60           C  
ANISOU 3150  CD2 LEU B1014    26595  17669  15996    516  -2087    780       C  
ATOM   3151  N   LYS B1015     -42.827  30.073 -67.669  1.00157.03           N  
ANISOU 3151  N   LYS B1015    27117  16942  15607   1179  -2368    836       N  
ATOM   3152  CA  LYS B1015     -43.569  31.115 -66.955  1.00158.03           C  
ANISOU 3152  CA  LYS B1015    27245  17055  15745   1483  -2477    857       C  
ATOM   3153  C   LYS B1015     -44.333  32.065 -67.900  1.00163.73           C  
ANISOU 3153  C   LYS B1015    28197  17672  16342   1605  -2691    938       C  
ATOM   3154  O   LYS B1015     -45.309  32.684 -67.467  1.00164.77           O  
ANISOU 3154  O   LYS B1015    28264  17852  16489   1887  -2815    975       O  
ATOM   3155  CB  LYS B1015     -42.646  31.896 -66.001  1.00159.86           C  
ANISOU 3155  CB  LYS B1015    27595  17147  15997   1522  -2367    790       C  
ATOM   3156  N   VAL B1016     -43.901  32.175 -69.182  1.00160.30           N  
ANISOU 3156  N   VAL B1016    28031  17097  15779   1402  -2731    967       N  
ATOM   3157  CA  VAL B1016     -44.555  33.011 -70.208  1.00162.14           C  
ANISOU 3157  CA  VAL B1016    28512  17217  15877   1485  -2939   1049       C  
ATOM   3158  C   VAL B1016     -45.931  32.391 -70.577  1.00168.26           C  
ANISOU 3158  C   VAL B1016    29054  18197  16680   1598  -3104   1121       C  
ATOM   3159  O   VAL B1016     -46.875  33.118 -70.906  1.00170.01           O  
ANISOU 3159  O   VAL B1016    29345  18403  16850   1804  -3301   1192       O  
ATOM   3160  CB  VAL B1016     -43.653  33.275 -71.458  1.00165.71           C  
ANISOU 3160  CB  VAL B1016    29325  17462  16174   1222  -2921   1061       C  
ATOM   3161  CG1 VAL B1016     -44.293  34.283 -72.415  1.00167.75           C  
ANISOU 3161  CG1 VAL B1016    29873  17580  16286   1326  -3142   1147       C  
ATOM   3162  CG2 VAL B1016     -42.261  33.752 -71.052  1.00164.34           C  
ANISOU 3162  CG2 VAL B1016    29329  17120  15994   1081  -2744    996       C  
ATOM   3163  N   ILE B1017     -46.038  31.047 -70.481  1.00164.22           N  
ANISOU 3163  N   ILE B1017    28263  17877  16255   1464  -3026   1103       N  
ATOM   3164  CA  ILE B1017     -47.264  30.291 -70.745  1.00165.06           C  
ANISOU 3164  CA  ILE B1017    28113  18197  16406   1525  -3166   1169       C  
ATOM   3165  C   ILE B1017     -48.280  30.521 -69.623  1.00169.52           C  
ANISOU 3165  C   ILE B1017    28383  18935  17093   1837  -3216   1191       C  
ATOM   3166  O   ILE B1017     -49.451  30.795 -69.903  1.00171.11           O  
ANISOU 3166  O   ILE B1017    28498  19228  17287   2020  -3409   1273       O  
ATOM   3167  CB  ILE B1017     -46.953  28.789 -70.944  1.00166.67           C  
ANISOU 3167  CB  ILE B1017    28140  18528  16659   1268  -3054   1137       C  
ATOM   3168  N   GLU B1018     -47.814  30.437 -68.358  1.00164.41           N  
ANISOU 3168  N   GLU B1018    27586  18331  16552   1901  -3043   1119       N  
ATOM   3169  CA  GLU B1018     -48.615  30.641 -67.152  1.00186.08           C  
ANISOU 3169  CA  GLU B1018    30062  21232  19408   2192  -3044   1125       C  
ATOM   3170  C   GLU B1018     -48.637  32.122 -66.758  1.00192.18           C  
ANISOU 3170  C   GLU B1018    31053  21841  20127   2449  -3099   1121       C  
ATOM   3171  O   GLU B1018     -48.951  32.987 -67.578  1.00145.90           O  
ANISOU 3171  O   GLU B1018    25434  15846  14155   2526  -3263   1176       O  
ATOM   3172  CB  GLU B1018     -48.067  29.781 -66.001  1.00185.20           C  
ANISOU 3172  CB  GLU B1018    29707  21237  19422   2122  -2831   1048       C  
ATOM   3173  N   ALA B1023     -52.854  31.596 -76.477  1.00177.61           N  
ANISOU 3173  N   ALA B1023    30117  19870  17496   1862  -4628   1741       N  
ATOM   3174  CA  ALA B1023     -53.053  30.709 -77.620  1.00177.96           C  
ANISOU 3174  CA  ALA B1023    30215  19949  17454   1612  -4742   1781       C  
ATOM   3175  C   ALA B1023     -51.886  30.800 -78.612  1.00180.88           C  
ANISOU 3175  C   ALA B1023    31018  20068  17640   1339  -4655   1737       C  
ATOM   3176  O   ALA B1023     -51.283  29.777 -78.943  1.00178.02           O  
ANISOU 3176  O   ALA B1023    30665  19718  17256   1066  -4529   1686       O  
ATOM   3177  CB  ALA B1023     -54.372  31.028 -78.310  1.00181.63           C  
ANISOU 3177  CB  ALA B1023    30639  20494  17879   1766  -5064   1906       C  
ATOM   3178  N   ALA B1024     -51.575  32.025 -79.078  1.00178.37           N  
ANISOU 3178  N   ALA B1024    31062  19521  17188   1418  -4718   1760       N  
ATOM   3179  CA  ALA B1024     -50.478  32.303 -80.005  1.00177.39           C  
ANISOU 3179  CA  ALA B1024    31371  19149  16881   1182  -4634   1731       C  
ATOM   3180  C   ALA B1024     -49.184  32.488 -79.216  1.00178.48           C  
ANISOU 3180  C   ALA B1024    31567  19182  17067   1107  -4339   1627       C  
ATOM   3181  O   ALA B1024     -48.122  32.064 -79.680  1.00176.44           O  
ANISOU 3181  O   ALA B1024    31490  18820  16729    839  -4167   1573       O  
ATOM   3182  CB  ALA B1024     -50.783  33.553 -80.819  1.00180.66           C  
ANISOU 3182  CB  ALA B1024    32141  19368  17133   1304  -4845   1813       C  
ATOM   3183  N   GLN B1025     -49.284  33.107 -78.016  1.00174.79           N  
ANISOU 3183  N   GLN B1025    30937  18746  16728   1348  -4282   1602       N  
ATOM   3184  CA  GLN B1025     -48.166  33.349 -77.103  1.00172.74           C  
ANISOU 3184  CA  GLN B1025    30699  18403  16533   1311  -4029   1508       C  
ATOM   3185  C   GLN B1025     -47.615  32.038 -76.545  1.00173.94           C  
ANISOU 3185  C   GLN B1025    30577  18706  16805   1127  -3809   1427       C  
ATOM   3186  O   GLN B1025     -46.396  31.891 -76.454  1.00172.02           O  
ANISOU 3186  O   GLN B1025    30453  18359  16545    935  -3595   1355       O  
ATOM   3187  CB  GLN B1025     -48.577  34.288 -75.956  1.00174.60           C  
ANISOU 3187  CB  GLN B1025    30825  18646  16867   1636  -4054   1505       C  
ATOM   3188  CG  GLN B1025     -48.594  35.760 -76.346  1.00200.32           C  
ANISOU 3188  CG  GLN B1025    34453  21667  19994   1784  -4189   1553       C  
ATOM   3189  CD  GLN B1025     -48.578  36.673 -75.145  1.00220.87           C  
ANISOU 3189  CD  GLN B1025    35913  24818  23188   1844  -3705   1569       C  
ATOM   3190  OE1 GLN B1025     -47.607  36.725 -74.381  1.00219.26           O  
ANISOU 3190  OE1 GLN B1025    36141  24323  22844   1848  -3678   1464       O  
ATOM   3191  NE2 GLN B1025     -49.650  37.427 -74.962  1.00218.89           N  
ANISOU 3191  NE2 GLN B1025    35873  24462  22835   2184  -3985   1630       N  
ATOM   3192  N   VAL B1026     -48.508  31.085 -76.191  1.00169.91           N  
ANISOU 3192  N   VAL B1026    29702  18442  16415   1180  -3866   1445       N  
ATOM   3193  CA  VAL B1026     -48.128  29.775 -75.652  1.00167.39           C  
ANISOU 3193  CA  VAL B1026    29111  18278  16213   1020  -3682   1377       C  
ATOM   3194  C   VAL B1026     -47.476  28.894 -76.728  1.00170.53           C  
ANISOU 3194  C   VAL B1026    29680  18615  16498    698  -3618   1355       C  
ATOM   3195  O   VAL B1026     -46.594  28.106 -76.401  1.00168.70           O  
ANISOU 3195  O   VAL B1026    29380  18402  16318    525  -3400   1276       O  
ATOM   3196  CB  VAL B1026     -49.267  29.038 -74.889  1.00171.31           C  
ANISOU 3196  CB  VAL B1026    29168  19052  16872   1167  -3754   1407       C  
ATOM   3197  CG1 VAL B1026     -49.697  29.818 -73.650  1.00171.29           C  
ANISOU 3197  CG1 VAL B1026    28985  19111  16986   1479  -3746   1406       C  
ATOM   3198  CG2 VAL B1026     -50.466  28.737 -75.786  1.00173.19           C  
ANISOU 3198  CG2 VAL B1026    29350  19393  17059   1181  -4017   1507       C  
ATOM   3199  N   LYS B1027     -47.897  29.048 -78.003  1.00168.18           N  
ANISOU 3199  N   LYS B1027    29618  18242  16042    627  -3806   1425       N  
ATOM   3200  CA  LYS B1027     -47.360  28.318 -79.155  1.00167.65           C  
ANISOU 3200  CA  LYS B1027    29766  18099  15834    338  -3768   1411       C  
ATOM   3201  C   LYS B1027     -45.952  28.818 -79.505  1.00169.79           C  
ANISOU 3201  C   LYS B1027    30373  18146  15993    177  -3569   1357       C  
ATOM   3202  O   LYS B1027     -45.049  27.997 -79.689  1.00167.78           O  
ANISOU 3202  O   LYS B1027    30150  17877  15723    -45  -3372   1290       O  
ATOM   3203  CB  LYS B1027     -48.298  28.451 -80.366  1.00172.97           C  
ANISOU 3203  CB  LYS B1027    30603  18754  16364    334  -4052   1509       C  
ATOM   3204  N   ASP B1028     -45.767  30.167 -79.573  1.00166.71           N  
ANISOU 3204  N   ASP B1028    30228  17584  15530    294  -3620   1388       N  
ATOM   3205  CA  ASP B1028     -44.492  30.851 -79.845  1.00165.78           C  
ANISOU 3205  CA  ASP B1028    30433  17248  15309    158  -3452   1353       C  
ATOM   3206  C   ASP B1028     -43.467  30.572 -78.730  1.00165.42           C  
ANISOU 3206  C   ASP B1028    30212  17233  15408    110  -3178   1257       C  
ATOM   3207  O   ASP B1028     -42.260  30.599 -78.978  1.00164.71           O  
ANISOU 3207  O   ASP B1028    30301  17021  15259    -84  -2982   1212       O  
ATOM   3208  CB  ASP B1028     -44.715  32.362 -80.000  1.00169.71           C  
ANISOU 3208  CB  ASP B1028    31194  17569  15717    327  -3601   1416       C  
ATOM   3209  CG  ASP B1028     -43.543  33.115 -80.606  1.00183.01           C  
ANISOU 3209  CG  ASP B1028    33275  19010  17251    155  -3480   1409       C  
ATOM   3210  OD1 ASP B1028     -42.571  33.398 -79.868  1.00184.88           O  
ANISOU 3210  OD1 ASP B1028    33501  19188  17559    114  -3280   1348       O  
ATOM   3211  OD2 ASP B1028     -43.608  33.444 -81.811  1.00187.40           O1-
ANISOU 3211  OD2 ASP B1028    34153  19435  17617     59  -3591   1470       O1-
ATOM   3212  N   ALA B1029     -43.957  30.312 -77.507  1.00158.61           N  
ANISOU 3212  N   ALA B1029    28996  16537  14732    289  -3167   1230       N  
ATOM   3213  CA  ALA B1029     -43.139  29.982 -76.350  1.00155.33           C  
ANISOU 3213  CA  ALA B1029    28378  16175  14466    269  -2936   1143       C  
ATOM   3214  C   ALA B1029     -42.673  28.519 -76.446  1.00155.01           C  
ANISOU 3214  C   ALA B1029    28175  16251  14472     58  -2775   1086       C  
ATOM   3215  O   ALA B1029     -41.492  28.231 -76.241  1.00152.42           O  
ANISOU 3215  O   ALA B1029    27876  15870  14164   -100  -2550   1018       O  
ATOM   3216  CB  ALA B1029     -43.939  30.205 -75.074  1.00155.83           C  
ANISOU 3216  CB  ALA B1029    28139  16379  14692    545  -2998   1143       C  
ATOM   3217  N   LEU B1030     -43.606  27.607 -76.777  1.00151.11           N  
ANISOU 3217  N   LEU B1030    27516  15909  13992     53  -2899   1117       N  
ATOM   3218  CA  LEU B1030     -43.382  26.170 -76.947  1.00149.17           C  
ANISOU 3218  CA  LEU B1030    27128  15772  13779   -133  -2790   1071       C  
ATOM   3219  C   LEU B1030     -42.356  25.868 -78.051  1.00152.00           C  
ANISOU 3219  C   LEU B1030    27787  15985  13979   -393  -2661   1043       C  
ATOM   3220  O   LEU B1030     -41.510  24.992 -77.852  1.00149.89           O  
ANISOU 3220  O   LEU B1030    27446  15747  13760   -541  -2451    970       O  
ATOM   3221  CB  LEU B1030     -44.720  25.465 -77.233  1.00150.02           C  
ANISOU 3221  CB  LEU B1030    27054  16044  13904    -83  -3003   1131       C  
ATOM   3222  CG  LEU B1030     -45.453  24.758 -76.076  1.00153.40           C  
ANISOU 3222  CG  LEU B1030    27058  16700  14527     42  -3010   1124       C  
ATOM   3223  CD1 LEU B1030     -45.339  25.507 -74.757  1.00152.76           C  
ANISOU 3223  CD1 LEU B1030    26816  16645  14580    255  -2932   1100       C  
ATOM   3224  CD2 LEU B1030     -46.911  24.593 -76.406  1.00157.30           C  
ANISOU 3224  CD2 LEU B1030    27414  17331  15023    142  -3275   1215       C  
ATOM   3225  N   THR B1031     -42.403  26.613 -79.191  1.00149.57           N  
ANISOU 3225  N   THR B1031    27824  15521  13484   -440  -2777   1100       N  
ATOM   3226  CA  THR B1031     -41.443  26.446 -80.294  1.00149.64           C  
ANISOU 3226  CA  THR B1031    28150  15385  13323   -678  -2651   1081       C  
ATOM   3227  C   THR B1031     -40.052  26.967 -79.881  1.00152.44           C  
ANISOU 3227  C   THR B1031    28599  15625  13698   -754  -2401   1027       C  
ATOM   3228  O   THR B1031     -39.047  26.341 -80.217  1.00151.05           O  
ANISOU 3228  O   THR B1031    28492  15416  13483   -947  -2190    973       O  
ATOM   3229  CB  THR B1031     -41.962  27.010 -81.642  1.00159.25           C  
ANISOU 3229  CB  THR B1031    29707  16478  14323   -713  -2856   1163       C  
ATOM   3230  OG1 THR B1031     -41.012  26.718 -82.665  1.00158.66           O  
ANISOU 3230  OG1 THR B1031    29923  16279  14083   -949  -2705   1139       O  
ATOM   3231  CG2 THR B1031     -42.230  28.506 -81.620  1.00159.28           C  
ANISOU 3231  CG2 THR B1031    29887  16355  14278   -552  -2996   1228       C  
ATOM   3232  N   LYS B1032     -40.006  28.079 -79.115  1.00149.67           N  
ANISOU 3232  N   LYS B1032    28237  15217  13413   -599  -2426   1040       N  
ATOM   3233  CA  LYS B1032     -38.772  28.675 -78.590  1.00148.92           C  
ANISOU 3233  CA  LYS B1032    28210  15017  13355   -659  -2221    997       C  
ATOM   3234  C   LYS B1032     -38.086  27.690 -77.633  1.00152.26           C  
ANISOU 3234  C   LYS B1032    28333  15570  13950   -713  -2000    909       C  
ATOM   3235  O   LYS B1032     -36.859  27.592 -77.645  1.00151.93           O  
ANISOU 3235  O   LYS B1032    28355  15465  13905   -871  -1781    864       O  
ATOM   3236  CB  LYS B1032     -39.068  30.008 -77.882  1.00151.29           C  
ANISOU 3236  CB  LYS B1032    28548  15238  13696   -456  -2333   1029       C  
ATOM   3237  N   MET B1033     -38.895  26.936 -76.844  1.00147.90           N  
ANISOU 3237  N   MET B1033    27453  15200  13541   -586  -2061    890       N  
ATOM   3238  CA  MET B1033     -38.466  25.912 -75.889  1.00145.76           C  
ANISOU 3238  CA  MET B1033    26878  15069  13437   -611  -1889    815       C  
ATOM   3239  C   MET B1033     -37.788  24.719 -76.568  1.00148.43           C  
ANISOU 3239  C   MET B1033    27246  15426  13727   -830  -1727    770       C  
ATOM   3240  O   MET B1033     -36.825  24.182 -76.012  1.00146.73           O  
ANISOU 3240  O   MET B1033    26909  15239  13603   -910  -1514    703       O  
ATOM   3241  CB  MET B1033     -39.669  25.401 -75.083  1.00147.83           C  
ANISOU 3241  CB  MET B1033    26819  15518  13831   -430  -2024    827       C  
ATOM   3242  CG  MET B1033     -39.923  26.168 -73.812  1.00151.22           C  
ANISOU 3242  CG  MET B1033    27086  15982  14389   -214  -2052    824       C  
ATOM   3243  SD  MET B1033     -41.347  25.534 -72.882  1.00155.25           S  
ANISOU 3243  SD  MET B1033    27208  16731  15050     -4  -2190    846       S  
ATOM   3244  CE  MET B1033     -40.604  24.146 -72.043  1.00149.53           C  
ANISOU 3244  CE  MET B1033    26209  16133  14472   -123  -1959    758       C  
ATOM   3245  N   ARG B1034     -38.317  24.283 -77.741  1.00144.96           N  
ANISOU 3245  N   ARG B1034    26965  14970  13142   -916  -1837    805       N  
ATOM   3246  CA  ARG B1034     -37.824  23.136 -78.508  1.00143.96           C  
ANISOU 3246  CA  ARG B1034    26907  14850  12941  -1111  -1710    765       C  
ATOM   3247  C   ARG B1034     -36.437  23.351 -79.113  1.00147.63           C  
ANISOU 3247  C   ARG B1034    27610  15178  13304  -1287  -1484    734       C  
ATOM   3248  O   ARG B1034     -35.617  22.434 -79.076  1.00145.50           O  
ANISOU 3248  O   ARG B1034    27274  14941  13068  -1404  -1278    669       O  
ATOM   3249  CB  ARG B1034     -38.833  22.726 -79.588  1.00145.33           C  
ANISOU 3249  CB  ARG B1034    27212  15033  12975  -1147  -1917    816       C  
ATOM   3250  N   ALA B1035     -36.175  24.554 -79.667  1.00146.54           N  
ANISOU 3250  N   ALA B1035    27749  14888  13043  -1304  -1521    784       N  
ATOM   3251  CA  ALA B1035     -34.886  24.908 -80.275  1.00147.39           C  
ANISOU 3251  CA  ALA B1035    28095  14863  13045  -1477  -1313    772       C  
ATOM   3252  C   ALA B1035     -33.774  24.944 -79.226  1.00150.50           C  
ANISOU 3252  C   ALA B1035    28299  15284  13601  -1494  -1089    714       C  
ATOM   3253  O   ALA B1035     -32.642  24.554 -79.520  1.00150.10           O  
ANISOU 3253  O   ALA B1035    28297  15207  13526  -1649   -857    675       O  
ATOM   3254  CB  ALA B1035     -34.987  26.245 -80.984  1.00150.06           C  
ANISOU 3254  CB  ALA B1035    28755  15035  13225  -1478  -1433    850       C  
ATOM   3255  N   ALA B1036     -34.112  25.388 -78.000  1.00146.35           N  
ANISOU 3255  N   ALA B1036    27551  14816  13238  -1328  -1162    709       N  
ATOM   3256  CA  ALA B1036     -33.201  25.416 -76.863  1.00145.10           C  
ANISOU 3256  CA  ALA B1036    27190  14695  13246  -1321   -989    655       C  
ATOM   3257  C   ALA B1036     -32.947  23.979 -76.421  1.00149.24           C  
ANISOU 3257  C   ALA B1036    27451  15364  13887  -1356   -848    584       C  
ATOM   3258  O   ALA B1036     -31.788  23.607 -76.258  1.00148.27           O  
ANISOU 3258  O   ALA B1036    27280  15244  13814  -1469   -624    536       O  
ATOM   3259  CB  ALA B1036     -33.806  26.217 -75.720  1.00145.29           C  
ANISOU 3259  CB  ALA B1036    27072  14741  13391  -1117  -1130    669       C  
ATOM   3260  N   ALA B1037     -34.028  23.159 -76.295  1.00146.77           N  
ANISOU 3260  N   ALA B1037    26983  15170  13612  -1267   -981    582       N  
ATOM   3261  CA  ALA B1037     -33.993  21.740 -75.900  1.00145.92           C  
ANISOU 3261  CA  ALA B1037    26641  15197  13606  -1291   -885    521       C  
ATOM   3262  C   ALA B1037     -33.188  20.861 -76.868  1.00151.70           C  
ANISOU 3262  C   ALA B1037    27513  15892  14234  -1477   -707    484       C  
ATOM   3263  O   ALA B1037     -32.618  19.852 -76.440  1.00149.46           O  
ANISOU 3263  O   ALA B1037    27061  15682  14044  -1518   -545    421       O  
ATOM   3264  CB  ALA B1037     -35.406  21.195 -75.752  1.00146.61           C  
ANISOU 3264  CB  ALA B1037    26581  15399  13724  -1179  -1095    547       C  
ATOM   3265  N   LEU B1038     -33.145  21.245 -78.166  1.00151.84           N  
ANISOU 3265  N   LEU B1038    27849  15792  14051  -1582   -735    523       N  
ATOM   3266  CA  LEU B1038     -32.381  20.545 -79.203  1.00153.02           C  
ANISOU 3266  CA  LEU B1038    28183  15889  14068  -1753   -561    492       C  
ATOM   3267  C   LEU B1038     -30.891  20.838 -78.999  1.00157.75           C  
ANISOU 3267  C   LEU B1038    28788  16443  14706  -1846   -294    461       C  
ATOM   3268  O   LEU B1038     -30.075  19.915 -79.015  1.00156.70           O  
ANISOU 3268  O   LEU B1038    28585  16350  14605  -1924    -85    401       O  
ATOM   3269  CB  LEU B1038     -32.840  20.975 -80.604  1.00155.18           C  
ANISOU 3269  CB  LEU B1038    28807  16048  14106  -1826   -686    551       C  
ATOM   3270  N   ASP B1039     -30.555  22.119 -78.739  1.00155.72           N  
ANISOU 3270  N   ASP B1039    28602  16108  14458  -1831   -310    503       N  
ATOM   3271  CA  ASP B1039     -29.193  22.580 -78.472  1.00155.81           C  
ANISOU 3271  CA  ASP B1039    28608  16075  14517  -1924    -89    490       C  
ATOM   3272  C   ASP B1039     -28.713  22.183 -77.056  1.00156.82           C  
ANISOU 3272  C   ASP B1039    28393  16314  14878  -1852      8    433       C  
ATOM   3273  O   ASP B1039     -27.507  22.205 -76.796  1.00156.42           O  
ANISOU 3273  O   ASP B1039    28281  16261  14889  -1940    216    409       O  
ATOM   3274  CB  ASP B1039     -29.100  24.098 -78.680  1.00159.47           C  
ANISOU 3274  CB  ASP B1039    29287  16405  14902  -1940   -172    560       C  
ATOM   3275  CG  ASP B1039     -27.687  24.611 -78.885  1.00175.83           C  
ANISOU 3275  CG  ASP B1039    31453  18404  16952  -2100     54    568       C  
ATOM   3276  OD1 ASP B1039     -26.992  24.097 -79.796  1.00178.01           O  
ANISOU 3276  OD1 ASP B1039    31855  18663  17118  -2243    237    558       O  
ATOM   3277  OD2 ASP B1039     -27.280  25.538 -78.147  1.00183.24           O  
ANISOU 3277  OD2 ASP B1039    32344  19302  17978  -2083     47    587       O  
ATOM   3278  N   ALA B1040     -29.654  21.818 -76.153  1.00150.99           N  
ANISOU 3278  N   ALA B1040    27429  15676  14263  -1696   -142    416       N  
ATOM   3279  CA  ALA B1040     -29.367  21.374 -74.783  1.00148.50           C  
ANISOU 3279  CA  ALA B1040    26793  15470  14159  -1613    -75    365       C  
ATOM   3280  C   ALA B1040     -28.924  19.902 -74.780  1.00151.12           C  
ANISOU 3280  C   ALA B1040    26980  15894  14545  -1665     89    299       C  
ATOM   3281  O   ALA B1040     -28.101  19.514 -73.950  1.00150.05           O  
ANISOU 3281  O   ALA B1040    26642  15817  14552  -1666    239    253       O  
ATOM   3282  CB  ALA B1040     -30.587  21.562 -73.890  1.00148.21           C  
ANISOU 3282  CB  ALA B1040    26594  15506  14214  -1426   -293    380       C  
ATOM   3283  N   GLN B1041     -29.470  19.089 -75.716  1.00147.14           N  
ANISOU 3283  N   GLN B1041    26593  15393  13920  -1708     52    296       N  
ATOM   3284  CA  GLN B1041     -29.137  17.673 -75.905  1.00145.73           C  
ANISOU 3284  CA  GLN B1041    26340  15274  13756  -1761    193    234       C  
ATOM   3285  C   GLN B1041     -27.715  17.574 -76.479  1.00149.67           C  
ANISOU 3285  C   GLN B1041    26944  15720  14203  -1896    460    207       C  
ATOM   3286  O   GLN B1041     -26.991  16.630 -76.153  1.00148.09           O  
ANISOU 3286  O   GLN B1041    26598  15579  14090  -1912    638    148       O  
ATOM   3287  CB  GLN B1041     -30.144  17.023 -76.870  1.00147.67           C  
ANISOU 3287  CB  GLN B1041    26742  15509  13855  -1784     53    247       C  
ATOM   3288  CG  GLN B1041     -30.207  15.504 -76.785  1.00156.90           C  
ANISOU 3288  CG  GLN B1041    27798  16752  15065  -1798    118    186       C  
ATOM   3289  CD  GLN B1041     -31.197  14.934 -77.769  1.00172.62           C  
ANISOU 3289  CD  GLN B1041    29964  18720  16902  -1838    -38    203       C  
ATOM   3290  OE1 GLN B1041     -30.955  14.902 -78.975  1.00170.19           O  
ANISOU 3290  OE1 GLN B1041    29936  18319  16408  -1944     10    206       O  
ATOM   3291  NE2 GLN B1041     -32.332  14.462 -77.276  1.00162.12           N  
ANISOU 3291  NE2 GLN B1041    28479  17478  15643  -1762   -229    217       N  
ATOM   3292  N   LYS B1042     -27.329  18.571 -77.330  1.00147.35           N  
ANISOU 3292  N   LYS B1042    26903  15315  13767  -1988    488    256       N  
ATOM   3293  CA  LYS B1042     -26.020  18.710 -77.980  1.00161.42           C  
ANISOU 3293  CA  LYS B1042    28810  17042  15479  -2127    736    251       C  
ATOM   3294  C   LYS B1042     -24.964  19.121 -76.950  1.00197.16           C  
ANISOU 3294  C   LYS B1042    33119  21609  20184  -2128    875    240       C  
ATOM   3295  O   LYS B1042     -23.771  19.153 -77.250  1.00161.34           O  
ANISOU 3295  O   LYS B1042    28602  17060  15638  -2235   1101    234       O  
ATOM   3296  CB  LYS B1042     -26.088  19.758 -79.104  1.00165.12           C  
ANISOU 3296  CB  LYS B1042    29613  17380  15743  -2221    687    321       C  
ATOM   3297  CG  LYS B1042     -26.867  19.313 -80.334  1.00176.60           C  
ANISOU 3297  CG  LYS B1042    31327  18782  16989  -2256    592    332       C  
ATOM   3298  CD  LYS B1042     -26.913  20.419 -81.389  1.00183.63           C  
ANISOU 3298  CD  LYS B1042    32556  19538  17676  -2346    535    407       C  
ATOM   3299  CE  LYS B1042     -27.731  20.049 -82.603  1.00188.04           C  
ANISOU 3299  CE  LYS B1042    33387  20038  18020  -2380    414    423       C  
ATOM   3300  NZ  LYS B1042     -29.192  20.071 -82.329  1.00193.46           N  
ANISOU 3300  NZ  LYS B1042    34023  20753  18729  -2256    106    448       N  
ATOM   3301  N   MET B1058     -23.892   9.862 -69.846  1.00163.62           N  
ANISOU 3301  N   MET B1058    26916  18115  17138  -1526   1319   -223       N  
ATOM   3302  CA  MET B1058     -24.070  10.960 -70.795  1.00164.64           C  
ANISOU 3302  CA  MET B1058    27264  18170  17122  -1602   1275   -177       C  
ATOM   3303  C   MET B1058     -25.257  10.730 -71.738  1.00169.65           C  
ANISOU 3303  C   MET B1058    28107  18759  17592  -1629   1124   -160       C  
ATOM   3304  O   MET B1058     -25.972  11.684 -72.050  1.00169.33           O  
ANISOU 3304  O   MET B1058    28178  18685  17475  -1638    970   -107       O  
ATOM   3305  CB  MET B1058     -22.782  11.214 -71.591  1.00168.22           C  
ANISOU 3305  CB  MET B1058    27824  18576  17514  -1695   1502   -185       C  
ATOM   3306  N   LYS B1059     -25.466   9.466 -72.185  1.00166.92           N  
ANISOU 3306  N   LYS B1059    27820  18408  17193  -1642   1158   -202       N  
ATOM   3307  CA  LYS B1059     -26.564   9.062 -73.075  1.00167.39           C  
ANISOU 3307  CA  LYS B1059    28076  18425  17099  -1681   1010   -190       C  
ATOM   3308  C   LYS B1059     -27.930   9.150 -72.377  1.00170.57           C  
ANISOU 3308  C   LYS B1059    28354  18893  17563  -1614    758   -149       C  
ATOM   3309  O   LYS B1059     -28.944   9.327 -73.053  1.00171.17           O  
ANISOU 3309  O   LYS B1059    28575  18943  17519  -1644    586   -111       O  
ATOM   3310  CB  LYS B1059     -26.329   7.648 -73.632  1.00170.13           C  
ANISOU 3310  CB  LYS B1059    28518  18742  17383  -1713   1120   -251       C  
ATOM   3311  N   ASP B1060     -27.946   9.036 -71.027  1.00165.29           N  
ANISOU 3311  N   ASP B1060    27415  18312  17075  -1523    738   -154       N  
ATOM   3312  CA  ASP B1060     -29.144   9.116 -70.177  1.00163.97           C  
ANISOU 3312  CA  ASP B1060    27086  18227  16987  -1443    531   -115       C  
ATOM   3313  C   ASP B1060     -29.686  10.550 -70.126  1.00166.27           C  
ANISOU 3313  C   ASP B1060    27405  18514  17255  -1403    390    -53       C  
ATOM   3314  O   ASP B1060     -30.904  10.748 -70.097  1.00165.61           O  
ANISOU 3314  O   ASP B1060    27307  18469  17147  -1363    192     -6       O  
ATOM   3315  CB  ASP B1060     -28.841   8.599 -68.762  1.00164.58           C  
ANISOU 3315  CB  ASP B1060    26889  18392  17253  -1358    583   -141       C  
ATOM   3316  CG  ASP B1060     -28.082   7.288 -68.755  1.00175.94           C  
ANISOU 3316  CG  ASP B1060    28303  19820  18724  -1383    746   -204       C  
ATOM   3317  OD1 ASP B1060     -28.731   6.225 -68.881  1.00176.36           O  
ANISOU 3317  OD1 ASP B1060    28373  19884  18753  -1402    683   -215       O  
ATOM   3318  OD2 ASP B1060     -26.837   7.326 -68.643  1.00182.87           O  
ANISOU 3318  OD2 ASP B1060    29151  20679  19652  -1385    934   -240       O  
ATOM   3319  N   PHE B1061     -28.774  11.543 -70.117  1.00162.02           N  
ANISOU 3319  N   PHE B1061    26905  17929  16724  -1413    491    -50       N  
ATOM   3320  CA  PHE B1061     -29.101  12.967 -70.145  1.00161.85           C  
ANISOU 3320  CA  PHE B1061    26953  17874  16669  -1383    378      4       C  
ATOM   3321  C   PHE B1061     -29.732  13.293 -71.511  1.00166.41           C  
ANISOU 3321  C   PHE B1061    27800  18374  17054  -1452    276     42       C  
ATOM   3322  O   PHE B1061     -30.733  14.011 -71.553  1.00166.60           O  
ANISOU 3322  O   PHE B1061    27860  18401  17039  -1397     84     96       O  
ATOM   3323  CB  PHE B1061     -27.833  13.817 -69.889  1.00163.67           C  
ANISOU 3323  CB  PHE B1061    27182  18060  16946  -1410    528     -5       C  
ATOM   3324  CG  PHE B1061     -27.947  15.301 -70.179  1.00165.96           C  
ANISOU 3324  CG  PHE B1061    27617  18276  17166  -1414    441     49       C  
ATOM   3325  CD1 PHE B1061     -28.423  16.181 -69.212  1.00168.48           C  
ANISOU 3325  CD1 PHE B1061    27830  18618  17566  -1304    311     76       C  
ATOM   3326  CD2 PHE B1061     -27.543  15.821 -71.405  1.00169.16           C  
ANISOU 3326  CD2 PHE B1061    28279  18578  17416  -1526    497     71       C  
ATOM   3327  CE1 PHE B1061     -28.521  17.551 -69.478  1.00170.04           C  
ANISOU 3327  CE1 PHE B1061    28184  18731  17693  -1302    226    124       C  
ATOM   3328  CE2 PHE B1061     -27.643  17.189 -71.672  1.00172.62           C  
ANISOU 3328  CE2 PHE B1061    28869  18936  17785  -1534    412    124       C  
ATOM   3329  CZ  PHE B1061     -28.131  18.044 -70.706  1.00170.25           C  
ANISOU 3329  CZ  PHE B1061    28467  18652  17569  -1420    273    149       C  
ATOM   3330  N   ARG B1062     -29.153  12.741 -72.616  1.00162.76           N  
ANISOU 3330  N   ARG B1062    27530  17843  16468  -1566    404     15       N  
ATOM   3331  CA  ARG B1062     -29.619  12.920 -74.003  1.00163.42           C  
ANISOU 3331  CA  ARG B1062    27901  17842  16349  -1649    329     44       C  
ATOM   3332  C   ARG B1062     -31.016  12.329 -74.225  1.00165.42           C  
ANISOU 3332  C   ARG B1062    28162  18135  16555  -1629    112     68       C  
ATOM   3333  O   ARG B1062     -31.761  12.835 -75.067  1.00166.02           O  
ANISOU 3333  O   ARG B1062    28423  18162  16494  -1655    -44    118       O  
ATOM   3334  CB  ARG B1062     -28.613  12.333 -75.008  1.00164.72           C  
ANISOU 3334  CB  ARG B1062    28253  17933  16399  -1763    543     -1       C  
ATOM   3335  N   HIS B1063     -31.362  11.264 -73.461  1.00159.42           N  
ANISOU 3335  N   HIS B1063    27199  17464  15910  -1587     95     39       N  
ATOM   3336  CA  HIS B1063     -32.669  10.597 -73.476  1.00158.61           C  
ANISOU 3336  CA  HIS B1063    27049  17421  15795  -1576   -106     66       C  
ATOM   3337  C   HIS B1063     -33.730  11.529 -72.871  1.00160.48           C  
ANISOU 3337  C   HIS B1063    27156  17729  16091  -1467   -316    136       C  
ATOM   3338  O   HIS B1063     -34.857  11.552 -73.366  1.00161.11           O  
ANISOU 3338  O   HIS B1063    27292  17826  16095  -1473   -517    188       O  
ATOM   3339  CB  HIS B1063     -32.611   9.251 -72.714  1.00158.31           C  
ANISOU 3339  CB  HIS B1063    26823  17455  15875  -1567    -43     19       C  
ATOM   3340  CG  HIS B1063     -33.934   8.550 -72.561  1.00161.64           C  
ANISOU 3340  CG  HIS B1063    27157  17952  16308  -1565   -246     54       C  
ATOM   3341  ND1 HIS B1063     -34.664   8.135 -73.666  1.00162.01           N  
ANISOU 3341  ND1 HIS B1063    26921  18120  16517  -1477   -310     72       N  
ATOM   3342  CD2 HIS B1063     -34.614   8.209 -71.440  1.00164.40           C  
ANISOU 3342  CD2 HIS B1063    27666  18273  16524  -1651   -396     79       C  
ATOM   3343  CE1 HIS B1063     -35.759   7.569 -73.183  1.00161.88           C  
ANISOU 3343  CE1 HIS B1063    26888  18153  16467  -1516   -488    110       C  
ATOM   3344  NE2 HIS B1063     -35.770   7.583 -71.851  1.00163.69           N  
ANISOU 3344  NE2 HIS B1063    27377  18294  16523  -1622   -555    116       N  
ATOM   3345  N   GLY B1064     -33.345  12.286 -71.835  1.00154.20           N  
ANISOU 3345  N   GLY B1064    26194  16970  15425  -1368   -267    138       N  
ATOM   3346  CA  GLY B1064     -34.195  13.255 -71.145  1.00152.95           C  
ANISOU 3346  CA  GLY B1064    25914  16871  15328  -1239   -433    195       C  
ATOM   3347  C   GLY B1064     -34.747  14.336 -72.056  1.00155.93           C  
ANISOU 3347  C   GLY B1064    26505  17175  15567  -1237   -580    256       C  
ATOM   3348  O   GLY B1064     -35.926  14.686 -71.959  1.00155.86           O  
ANISOU 3348  O   GLY B1064    26440  17224  15556  -1153   -782    314       O  
ATOM   3349  N   PHE B1065     -33.900  14.855 -72.967  1.00151.76           N  
ANISOU 3349  N   PHE B1065    26222  16521  14917  -1330   -478    246       N  
ATOM   3350  CA  PHE B1065     -34.286  15.868 -73.949  1.00152.25           C  
ANISOU 3350  CA  PHE B1065    26532  16491  14826  -1347   -603    303       C  
ATOM   3351  C   PHE B1065     -35.154  15.271 -75.077  1.00155.65           C  
ANISOU 3351  C   PHE B1065    27123  16907  15109  -1423   -748    331       C  
ATOM   3352  O   PHE B1065     -35.945  16.001 -75.664  1.00156.08           O  
ANISOU 3352  O   PHE B1065    27309  16929  15066  -1395   -933    394       O  
ATOM   3353  CB  PHE B1065     -33.059  16.610 -74.498  1.00154.47           C  
ANISOU 3353  CB  PHE B1065    27018  16645  15027  -1432   -436    289       C  
ATOM   3354  N   ASP B1066     -35.036  13.949 -75.354  1.00151.19           N  
ANISOU 3354  N   ASP B1066    26552  16364  14529  -1514   -678    285       N  
ATOM   3355  CA  ASP B1066     -35.857  13.244 -76.352  1.00151.87           C  
ANISOU 3355  CA  ASP B1066    26787  16437  14480  -1600   -823    305       C  
ATOM   3356  C   ASP B1066     -37.311  13.108 -75.848  1.00155.33           C  
ANISOU 3356  C   ASP B1066    27026  16999  14993  -1514  -1071    365       C  
ATOM   3357  O   ASP B1066     -38.241  13.228 -76.648  1.00156.15           O  
ANISOU 3357  O   ASP B1066    27255  17093  14984  -1542  -1274    421       O  
ATOM   3358  CB  ASP B1066     -35.255  11.874 -76.719  1.00153.34           C  
ANISOU 3358  CB  ASP B1066    27034  16599  14631  -1715   -668    233       C  
ATOM   3359  N   ILE B1067     -37.498  12.889 -74.515  1.00150.34           N  
ANISOU 3359  N   ILE B1067    26081  16490  14551  -1408  -1054    358       N  
ATOM   3360  CA  ILE B1067     -38.814  12.816 -73.849  1.00149.83           C  
ANISOU 3360  CA  ILE B1067    25780  16566  14581  -1310  -1257    419       C  
ATOM   3361  C   ILE B1067     -39.384  14.245 -73.799  1.00153.23           C  
ANISOU 3361  C   ILE B1067    26225  16995  14999  -1177  -1402    487       C  
ATOM   3362  O   ILE B1067     -40.585  14.437 -74.014  1.00154.28           O  
ANISOU 3362  O   ILE B1067    26314  17195  15110  -1126  -1624    559       O  
ATOM   3363  CB  ILE B1067     -38.752  12.210 -72.413  1.00151.34           C  
ANISOU 3363  CB  ILE B1067    25651  16883  14969  -1234  -1170    391       C  
ATOM   3364  CG1 ILE B1067     -37.904  10.931 -72.342  1.00151.15           C  
ANISOU 3364  CG1 ILE B1067    25627  16835  14969  -1343   -987    314       C  
ATOM   3365  CG2 ILE B1067     -40.164  11.960 -71.857  1.00152.40           C  
ANISOU 3365  CG2 ILE B1067    25548  17174  15185  -1158  -1372    460       C  
ATOM   3366  CD1 ILE B1067     -37.188  10.749 -70.981  1.00158.20           C  
ANISOU 3366  CD1 ILE B1067    26285  17787  16035  -1262   -818    267       C  
ATOM   3367  N   LEU B1068     -38.509  15.237 -73.505  1.00147.53           N  
ANISOU 3367  N   LEU B1068    25566  16196  14292  -1121  -1278    466       N  
ATOM   3368  CA  LEU B1068     -38.851  16.658 -73.442  1.00146.96           C  
ANISOU 3368  CA  LEU B1068    25550  16090  14200   -994  -1389    520       C  
ATOM   3369  C   LEU B1068     -39.301  17.190 -74.814  1.00149.73           C  
ANISOU 3369  C   LEU B1068    26189  16341  14361  -1051  -1544    575       C  
ATOM   3370  O   LEU B1068     -40.348  17.829 -74.873  1.00151.22           O  
ANISOU 3370  O   LEU B1068    26352  16568  14536   -940  -1753    646       O  
ATOM   3371  CB  LEU B1068     -37.695  17.491 -72.861  1.00146.12           C  
ANISOU 3371  CB  LEU B1068    25471  15905  14143   -958  -1214    479       C  
ATOM   3372  N   VAL B1069     -38.558  16.885 -75.910  1.00143.22           N  
ANISOU 3372  N   VAL B1069    25632  15395  13389  -1217  -1445    544       N  
ATOM   3373  CA  VAL B1069     -38.907  17.301 -77.278  1.00143.39           C  
ANISOU 3373  CA  VAL B1069    25961  15312  13211  -1292  -1579    592       C  
ATOM   3374  C   VAL B1069     -40.279  16.730 -77.658  1.00146.35           C  
ANISOU 3374  C   VAL B1069    26275  15776  13554  -1289  -1828    649       C  
ATOM   3375  O   VAL B1069     -41.147  17.488 -78.096  1.00146.62           O  
ANISOU 3375  O   VAL B1069    26387  15801  13520  -1220  -2043    725       O  
ATOM   3376  CB  VAL B1069     -37.796  16.957 -78.317  1.00147.10           C  
ANISOU 3376  CB  VAL B1069    26719  15645  13526  -1471  -1395    542       C  
ATOM   3377  CG1 VAL B1069     -38.321  17.008 -79.747  1.00148.67           C  
ANISOU 3377  CG1 VAL B1069    27224  15756  13509  -1567  -1550    588       C  
ATOM   3378  CG2 VAL B1069     -36.595  17.883 -78.168  1.00146.44           C  
ANISOU 3378  CG2 VAL B1069    26738  15462  13442  -1476  -1204    520       C  
ATOM   3379  N   GLY B1070     -40.459  15.426 -77.414  1.00141.60           N  
ANISOU 3379  N   GLY B1070    25525  15263  13015  -1359  -1800    614       N  
ATOM   3380  CA  GLY B1070     -41.678  14.668 -77.685  1.00142.02           C  
ANISOU 3380  CA  GLY B1070    25492  15413  13057  -1392  -2018    663       C  
ATOM   3381  C   GLY B1070     -42.924  15.177 -76.987  1.00145.28           C  
ANISOU 3381  C   GLY B1070    25647  15969  13583  -1226  -2229    745       C  
ATOM   3382  O   GLY B1070     -44.005  15.188 -77.585  1.00146.17           O  
ANISOU 3382  O   GLY B1070    25783  16124  13631  -1231  -2470    819       O  
ATOM   3383  N   GLN B1071     -42.781  15.598 -75.716  1.00140.17           N  
ANISOU 3383  N   GLN B1071    24753  15402  13102  -1074  -2140    733       N  
ATOM   3384  CA  GLN B1071     -43.870  16.152 -74.906  1.00140.33           C  
ANISOU 3384  CA  GLN B1071    24514  15565  13240   -885  -2300    804       C  
ATOM   3385  C   GLN B1071     -44.259  17.548 -75.424  1.00145.82           C  
ANISOU 3385  C   GLN B1071    25375  16185  13844   -768  -2451    868       C  
ATOM   3386  O   GLN B1071     -45.451  17.852 -75.535  1.00147.30           O  
ANISOU 3386  O   GLN B1071    25467  16464  14037   -669  -2678    952       O  
ATOM   3387  CB  GLN B1071     -43.472  16.204 -73.424  1.00139.95           C  
ANISOU 3387  CB  GLN B1071    24199  15601  13374   -761  -2139    763       C  
ATOM   3388  N   ILE B1072     -43.244  18.377 -75.782  1.00141.31           N  
ANISOU 3388  N   ILE B1072    25059  15447  13185   -786  -2328    833       N  
ATOM   3389  CA  ILE B1072     -43.402  19.720 -76.360  1.00141.58           C  
ANISOU 3389  CA  ILE B1072    25315  15369  13111   -700  -2446    887       C  
ATOM   3390  C   ILE B1072     -44.186  19.602 -77.679  1.00147.61           C  
ANISOU 3390  C   ILE B1072    26275  16098  13711   -784  -2668    952       C  
ATOM   3391  O   ILE B1072     -45.067  20.426 -77.931  1.00149.09           O  
ANISOU 3391  O   ILE B1072    26491  16295  13863   -657  -2881   1033       O  
ATOM   3392  CB  ILE B1072     -42.022  20.444 -76.501  1.00143.30           C  
ANISOU 3392  CB  ILE B1072    25771  15411  13266   -753  -2241    833       C  
ATOM   3393  CG1 ILE B1072     -41.536  20.970 -75.127  1.00141.20           C  
ANISOU 3393  CG1 ILE B1072    25309  15178  13160   -613  -2105    795       C  
ATOM   3394  CG2 ILE B1072     -42.059  21.585 -77.530  1.00145.73           C  
ANISOU 3394  CG2 ILE B1072    26411  15561  13399   -750  -2359    888       C  
ATOM   3395  CD1 ILE B1072     -40.025  21.216 -75.008  1.00141.51           C  
ANISOU 3395  CD1 ILE B1072    25481  15093  13192   -711  -1855    724       C  
ATOM   3396  N   ASP B1073     -43.909  18.538 -78.471  1.00143.81           N  
ANISOU 3396  N   ASP B1073    25921  15584  13136   -989  -2627    919       N  
ATOM   3397  CA  ASP B1073     -44.587  18.239 -79.738  1.00145.30           C  
ANISOU 3397  CA  ASP B1073    26312  15736  13159  -1100  -2831    971       C  
ATOM   3398  C   ASP B1073     -46.099  18.029 -79.529  1.00150.53           C  
ANISOU 3398  C   ASP B1073    26729  16570  13897  -1009  -3105   1058       C  
ATOM   3399  O   ASP B1073     -46.905  18.495 -80.344  1.00151.41           O  
ANISOU 3399  O   ASP B1073    26969  16660  13899   -988  -3344   1138       O  
ATOM   3400  CB  ASP B1073     -43.970  16.992 -80.407  1.00146.36           C  
ANISOU 3400  CB  ASP B1073    26595  15816  13200  -1325  -2709    904       C  
ATOM   3401  CG  ASP B1073     -42.531  17.128 -80.869  1.00152.50           C  
ANISOU 3401  CG  ASP B1073    27643  16427  13872  -1434  -2452    829       C  
ATOM   3402  OD1 ASP B1073     -42.174  18.199 -81.410  1.00153.50           O  
ANISOU 3402  OD1 ASP B1073    28009  16428  13886  -1413  -2452    853       O  
ATOM   3403  OD2 ASP B1073     -41.766  16.158 -80.711  1.00157.03           O  
ANISOU 3403  OD2 ASP B1073    28192  16998  14473  -1541  -2251    749       O  
ATOM   3404  N   ASP B1074     -46.472  17.336 -78.422  1.00145.93           N  
ANISOU 3404  N   ASP B1074    25785  16160  13501   -954  -3067   1048       N  
ATOM   3405  CA  ASP B1074     -47.865  17.057 -78.060  1.00146.39           C  
ANISOU 3405  CA  ASP B1074    25552  16411  13660   -870  -3293   1133       C  
ATOM   3406  C   ASP B1074     -48.576  18.323 -77.560  1.00149.29           C  
ANISOU 3406  C   ASP B1074    25791  16839  14093   -615  -3422   1207       C  
ATOM   3407  O   ASP B1074     -49.785  18.479 -77.763  1.00150.41           O  
ANISOU 3407  O   ASP B1074    25811  17093  14246   -536  -3669   1302       O  
ATOM   3408  CB  ASP B1074     -47.941  15.919 -77.029  1.00146.97           C  
ANISOU 3408  CB  ASP B1074    25300  16639  13901   -903  -3185   1099       C  
ATOM   3409  CG  ASP B1074     -47.269  14.618 -77.456  1.00159.13           C  
ANISOU 3409  CG  ASP B1074    26961  18117  15383  -1137  -3060   1024       C  
ATOM   3410  OD1 ASP B1074     -47.351  14.267 -78.661  1.00160.43           O  
ANISOU 3410  OD1 ASP B1074    27386  18187  15381  -1295  -3167   1033       O  
ATOM   3411  OD2 ASP B1074     -46.680  13.937 -76.580  1.00165.73           O  
ANISOU 3411  OD2 ASP B1074    27638  18996  16336  -1157  -2861    958       O  
ATOM   3412  N   ALA B1075     -47.809  19.236 -76.933  1.00143.13           N  
ANISOU 3412  N   ALA B1075    25051  15980  13352   -487  -3257   1163       N  
ATOM   3413  CA  ALA B1075     -48.297  20.520 -76.429  1.00142.67           C  
ANISOU 3413  CA  ALA B1075    24925  15941  13342   -234  -3347   1216       C  
ATOM   3414  C   ALA B1075     -48.502  21.515 -77.578  1.00145.67           C  
ANISOU 3414  C   ALA B1075    25629  16172  13546   -212  -3523   1275       C  
ATOM   3415  O   ALA B1075     -49.417  22.336 -77.510  1.00145.85           O  
ANISOU 3415  O   ALA B1075    25586  16244  13584    -16  -3713   1355       O  
ATOM   3416  CB  ALA B1075     -47.330  21.078 -75.403  1.00141.63           C  
ANISOU 3416  CB  ALA B1075    24760  15755  13299   -135  -3113   1143       C  
ATOM   3417  N   LEU B1076     -47.656  21.429 -78.636  1.00141.58           N  
ANISOU 3417  N   LEU B1076    25464  15473  12856   -407  -3456   1237       N  
ATOM   3418  CA  LEU B1076     -47.743  22.250 -79.857  1.00142.67           C  
ANISOU 3418  CA  LEU B1076    25959  15451  12799   -430  -3610   1290       C  
ATOM   3419  C   LEU B1076     -49.005  21.858 -80.639  1.00147.88           C  
ANISOU 3419  C   LEU B1076    26589  16202  13399   -454  -3908   1382       C  
ATOM   3420  O   LEU B1076     -49.627  22.707 -81.279  1.00149.03           O  
ANISOU 3420  O   LEU B1076    26882  16294  13448   -360  -4124   1462       O  
ATOM   3421  CB  LEU B1076     -46.498  22.059 -80.742  1.00142.13           C  
ANISOU 3421  CB  LEU B1076    26249  15189  12564   -653  -3434   1224       C  
ATOM   3422  CG  LEU B1076     -45.213  22.755 -80.295  1.00145.10           C  
ANISOU 3422  CG  LEU B1076    26746  15433  12952   -642  -3180   1157       C  
ATOM   3423  CD1 LEU B1076     -43.990  22.003 -80.779  1.00144.27           C  
ANISOU 3423  CD1 LEU B1076    26820  15232  12765   -874  -2941   1074       C  
ATOM   3424  CD2 LEU B1076     -45.168  24.187 -80.776  1.00148.78           C  
ANISOU 3424  CD2 LEU B1076    27487  15741  13301   -546  -3273   1211       C  
ATOM   3425  N   LYS B1077     -49.377  20.558 -80.568  1.00143.88           N  
ANISOU 3425  N   LYS B1077    25890  15829  12950   -586  -3927   1372       N  
ATOM   3426  CA  LYS B1077     -50.586  19.984 -81.155  1.00145.10           C  
ANISOU 3426  CA  LYS B1077    25954  16099  13077   -637  -4206   1457       C  
ATOM   3427  C   LYS B1077     -51.790  20.547 -80.386  1.00149.83           C  
ANISOU 3427  C   LYS B1077    26214  16885  13828   -384  -4385   1549       C  
ATOM   3428  O   LYS B1077     -52.751  21.014 -81.001  1.00151.30           O  
ANISOU 3428  O   LYS B1077    26430  17101  13956   -310  -4657   1647       O  
ATOM   3429  CB  LYS B1077     -50.547  18.448 -81.051  1.00146.23           C  
ANISOU 3429  CB  LYS B1077    25958  16334  13268   -839  -4140   1412       C  
ATOM   3430  N   LEU B1078     -51.693  20.555 -79.030  1.00145.03           N  
ANISOU 3430  N   LEU B1078    25295  16397  13411   -241  -4223   1515       N  
ATOM   3431  CA  LEU B1078     -52.707  21.057 -78.105  1.00156.18           C  
ANISOU 3431  CA  LEU B1078    26362  17996  14982     18  -4329   1587       C  
ATOM   3432  C   LEU B1078     -52.604  22.575 -77.938  1.00169.88           C  
ANISOU 3432  C   LEU B1078    28231  19625  16690    261  -4344   1605       C  
ATOM   3433  O   LEU B1078     -52.283  23.292 -78.888  1.00126.41           O  
ANISOU 3433  O   LEU B1078    23080  13932  11019    232  -4414   1616       O  
ATOM   3434  CB  LEU B1078     -52.565  20.354 -76.747  1.00154.04           C  
ANISOU 3434  CB  LEU B1078    25738  17884  14905     50  -4131   1537       C  
ATOM   3435  N   ALA B1090     -49.489  17.543 -70.277  1.00185.09           N  
ANISOU 3435  N   ALA B1090    28587  22173  19565     98  -2881   1152       N  
ATOM   3436  CA  ALA B1090     -48.679  18.321 -71.211  1.00184.95           C  
ANISOU 3436  CA  ALA B1090    28942  21931  19401     51  -2868   1115       C  
ATOM   3437  C   ALA B1090     -48.360  19.720 -70.681  1.00188.47           C  
ANISOU 3437  C   ALA B1090    29463  22294  19853    271  -2820   1101       C  
ATOM   3438  O   ALA B1090     -47.249  20.207 -70.896  1.00186.82           O  
ANISOU 3438  O   ALA B1090    29503  21904  19576    219  -2691   1035       O  
ATOM   3439  CB  ALA B1090     -49.378  18.417 -72.557  1.00187.70           C  
ANISOU 3439  CB  ALA B1090    29460  22242  19616    -26  -3103   1188       C  
ATOM   3440  N   ALA B1091     -49.336  20.359 -69.997  1.00186.35           N  
ANISOU 3440  N   ALA B1091    28982  22158  19664    515  -2923   1165       N  
ATOM   3441  CA  ALA B1091     -49.238  21.706 -69.426  1.00186.66           C  
ANISOU 3441  CA  ALA B1091    29081  22132  19711    758  -2905   1159       C  
ATOM   3442  C   ALA B1091     -48.088  21.853 -68.426  1.00189.43           C  
ANISOU 3442  C   ALA B1091    29446  22407  20121    774  -2664   1061       C  
ATOM   3443  O   ALA B1091     -47.268  22.761 -68.573  1.00188.71           O  
ANISOU 3443  O   ALA B1091    29610  22131  19961    794  -2604   1019       O  
ATOM   3444  CB  ALA B1091     -50.560  22.101 -68.783  1.00188.78           C  
ANISOU 3444  CB  ALA B1091    29067  22592  20068   1016  -3040   1244       C  
ATOM   3445  N   GLU B1092     -48.025  20.953 -67.427  1.00185.42           N  
ANISOU 3445  N   GLU B1092    28674  22039  19739    752  -2534   1029       N  
ATOM   3446  CA  GLU B1092     -46.984  20.929 -66.395  1.00183.55           C  
ANISOU 3446  CA  GLU B1092    28415  21756  19572    759  -2314    940       C  
ATOM   3447  C   GLU B1092     -46.228  19.586 -66.391  1.00186.42           C  
ANISOU 3447  C   GLU B1092    28735  22129  19968    517  -2167    881       C  
ATOM   3448  O   GLU B1092     -45.344  19.384 -65.552  1.00184.58           O  
ANISOU 3448  O   GLU B1092    28463  21869  19800    500  -1987    809       O  
ATOM   3449  CB  GLU B1092     -47.579  21.250 -65.012  1.00184.85           C  
ANISOU 3449  CB  GLU B1092    28312  22069  19853   1004  -2284    953       C  
ATOM   3450  N   GLN B1093     -46.557  18.684 -67.355  1.00183.75           N  
ANISOU 3450  N   GLN B1093    28423  21816  19579    333  -2253    911       N  
ATOM   3451  CA  GLN B1093     -45.933  17.364 -67.523  1.00182.45           C  
ANISOU 3451  CA  GLN B1093    28251  21647  19426    103  -2137    861       C  
ATOM   3452  C   GLN B1093     -44.473  17.473 -67.970  1.00185.79           C  
ANISOU 3452  C   GLN B1093    28946  21870  19775    -33  -1975    774       C  
ATOM   3453  O   GLN B1093     -43.705  16.529 -67.775  1.00184.08           O  
ANISOU 3453  O   GLN B1093    28708  21641  19594   -172  -1824    713       O  
ATOM   3454  CB  GLN B1093     -46.736  16.490 -68.501  1.00184.91           C  
ANISOU 3454  CB  GLN B1093    28555  22021  19682    -48  -2296    919       C  
ATOM   3455  N   LEU B1094     -44.094  18.624 -68.564  1.00183.38           N  
ANISOU 3455  N   LEU B1094    28894  21411  19370      9  -2005    774       N  
ATOM   3456  CA  LEU B1094     -42.731  18.909 -69.010  1.00182.56           C  
ANISOU 3456  CA  LEU B1094    29050  21122  19194   -113  -1854    706       C  
ATOM   3457  C   LEU B1094     -41.816  19.152 -67.806  1.00185.14           C  
ANISOU 3457  C   LEU B1094    29287  21433  19625    -47  -1670    639       C  
ATOM   3458  O   LEU B1094     -40.622  18.872 -67.897  1.00183.74           O  
ANISOU 3458  O   LEU B1094    29214  21161  19440   -180  -1502    574       O  
ATOM   3459  CB  LEU B1094     -42.702  20.105 -69.971  1.00184.00           C  
ANISOU 3459  CB  LEU B1094    29525  21151  19236    -88  -1958    740       C  
ATOM   3460  N   LYS B1095     -42.379  19.651 -66.678  1.00182.01           N  
ANISOU 3460  N   LYS B1095    28696  21134  19325    160  -1701    657       N  
ATOM   3461  CA  LYS B1095     -41.654  19.907 -65.425  1.00180.62           C  
ANISOU 3461  CA  LYS B1095    28424  20955  19247    242  -1551    598       C  
ATOM   3462  C   LYS B1095     -41.284  18.595 -64.735  1.00183.43           C  
ANISOU 3462  C   LYS B1095    28576  21413  19708    148  -1414    554       C  
ATOM   3463  O   LYS B1095     -40.240  18.526 -64.084  1.00181.65           O  
ANISOU 3463  O   LYS B1095    28346  21138  19536    116  -1256    488       O  
ATOM   3464  CB  LYS B1095     -42.473  20.800 -64.481  1.00183.65           C  
ANISOU 3464  CB  LYS B1095    28680  21414  19683    502  -1634    633       C  
ATOM   3465  N   THR B1096     -42.135  17.555 -64.889  1.00180.75           N  
ANISOU 3465  N   THR B1096    28072  21210  19394     98  -1483    592       N  
ATOM   3466  CA  THR B1096     -41.908  16.214 -64.336  1.00179.61           C  
ANISOU 3466  CA  THR B1096    27747  21158  19337     -2  -1375    560       C  
ATOM   3467  C   THR B1096     -40.840  15.474 -65.159  1.00183.02           C  
ANISOU 3467  C   THR B1096    28357  21472  19713   -221  -1261    502       C  
ATOM   3468  O   THR B1096     -40.053  14.713 -64.591  1.00181.25           O  
ANISOU 3468  O   THR B1096    28058  21251  19557   -287  -1109    445       O  
ATOM   3469  CB  THR B1096     -43.221  15.417 -64.192  1.00189.16           C  
ANISOU 3469  CB  THR B1096    28727  22552  20593     15  -1497    630       C  
ATOM   3470  OG1 THR B1096     -43.745  15.090 -65.480  1.00190.32           O  
ANISOU 3470  OG1 THR B1096    28993  22677  20642   -109  -1633    674       O  
ATOM   3471  CG2 THR B1096     -44.272  16.143 -63.348  1.00188.50           C  
ANISOU 3471  CG2 THR B1096    28449  22603  20570    248  -1589    690       C  
ATOM   3472  N   THR B1097     -40.807  15.712 -66.494  1.00180.67           N  
ANISOU 3472  N   THR B1097    28297  21067  19283   -322  -1332    518       N  
ATOM   3473  CA  THR B1097     -39.807  15.125 -67.398  1.00180.14           C  
ANISOU 3473  CA  THR B1097    28430  20877  19136   -516  -1219    466       C  
ATOM   3474  C   THR B1097     -38.466  15.870 -67.257  1.00182.76           C  
ANISOU 3474  C   THR B1097    28903  21076  19462   -525  -1059    408       C  
ATOM   3475  O   THR B1097     -37.419  15.294 -67.557  1.00182.16           O  
ANISOU 3475  O   THR B1097    28911  20930  19372   -658   -904    351       O  
ATOM   3476  CB  THR B1097     -40.307  15.032 -68.860  1.00188.91           C  
ANISOU 3476  CB  THR B1097    29750  21930  20099   -627  -1354    506       C  
ATOM   3477  OG1 THR B1097     -40.554  16.337 -69.378  1.00190.13           O  
ANISOU 3477  OG1 THR B1097    30069  22005  20166   -545  -1462    549       O  
ATOM   3478  CG2 THR B1097     -41.545  14.157 -69.013  1.00187.67           C  
ANISOU 3478  CG2 THR B1097    29448  21904  19953   -654  -1512    562       C  
ATOM   3479  N   ARG B1098     -38.502  17.136 -66.768  1.00178.46           N  
ANISOU 3479  N   ARG B1098    28377  20499  18930   -382  -1097    425       N  
ATOM   3480  CA  ARG B1098     -37.326  17.982 -66.525  1.00177.35           C  
ANISOU 3480  CA  ARG B1098    28358  20236  18791   -385   -973    381       C  
ATOM   3481  C   ARG B1098     -36.478  17.427 -65.380  1.00178.72           C  
ANISOU 3481  C   ARG B1098    28355  20454  19095   -386   -806    319       C  
ATOM   3482  O   ARG B1098     -35.285  17.725 -65.301  1.00177.47           O  
ANISOU 3482  O   ARG B1098    28282  20202  18946   -452   -671    274       O  
ATOM   3483  CB  ARG B1098     -37.748  19.426 -66.220  1.00178.34           C  
ANISOU 3483  CB  ARG B1098    28548  20317  18896   -220  -1084    419       C  
ATOM   3484  N   ASN B1099     -37.100  16.599 -64.511  1.00174.32           N  
ANISOU 3484  N   ASN B1099    27552  20043  18640   -321   -820    322       N  
ATOM   3485  CA  ASN B1099     -36.478  15.914 -63.375  1.00172.36           C  
ANISOU 3485  CA  ASN B1099    27117  19855  18516   -313   -685    271       C  
ATOM   3486  C   ASN B1099     -35.619  14.707 -63.832  1.00174.88           C  
ANISOU 3486  C   ASN B1099    27461  20147  18838   -486   -545    223       C  
ATOM   3487  O   ASN B1099     -35.080  13.981 -62.991  1.00173.03           O  
ANISOU 3487  O   ASN B1099    27081  19960  18704   -492   -434    182       O  
ATOM   3488  CB  ASN B1099     -37.547  15.487 -62.369  1.00172.33           C  
ANISOU 3488  CB  ASN B1099    26861  20016  18601   -185   -757    304       C  
ATOM   3489  N   ALA B1100     -35.489  14.509 -65.165  1.00171.82           N  
ANISOU 3489  N   ALA B1100    27271  19678  18334   -618   -552    227       N  
ATOM   3490  CA  ALA B1100     -34.669  13.472 -65.799  1.00171.08           C  
ANISOU 3490  CA  ALA B1100    27253  19537  18213   -773   -417    179       C  
ATOM   3491  C   ALA B1100     -33.438  14.113 -66.494  1.00174.62           C  
ANISOU 3491  C   ALA B1100    27909  19847  18592   -861   -291    148       C  
ATOM   3492  O   ALA B1100     -32.710  13.427 -67.220  1.00174.30           O  
ANISOU 3492  O   ALA B1100    27972  19752  18503   -985   -170    112       O  
ATOM   3493  CB  ALA B1100     -35.502  12.683 -66.802  1.00172.64           C  
ANISOU 3493  CB  ALA B1100    27529  19751  18317   -861   -519    207       C  
ATOM   3494  N   TYR B1101     -33.206  15.428 -66.242  1.00170.87           N  
ANISOU 3494  N   TYR B1101    27494  19316  18114   -794   -316    165       N  
ATOM   3495  CA  TYR B1101     -32.100  16.212 -66.805  1.00170.98           C  
ANISOU 3495  CA  TYR B1101    27695  19202  18066   -878   -212    151       C  
ATOM   3496  C   TYR B1101     -31.475  17.219 -65.818  1.00174.26           C  
ANISOU 3496  C   TYR B1101    28057  19591  18565   -805   -178    141       C  
ATOM   3497  O   TYR B1101     -30.326  17.614 -66.025  1.00174.05           O  
ANISOU 3497  O   TYR B1101    28119  19481  18530   -895    -52    120       O  
ATOM   3498  CB  TYR B1101     -32.547  16.936 -68.087  1.00173.44           C  
ANISOU 3498  CB  TYR B1101    28264  19422  18215   -924   -316    199       C  
ATOM   3499  N   ILE B1102     -32.224  17.635 -64.763  1.00170.16           N  
ANISOU 3499  N   ILE B1102    27396  19139  18118   -647   -287    158       N  
ATOM   3500  CA  ILE B1102     -31.793  18.620 -63.753  1.00169.65           C  
ANISOU 3500  CA  ILE B1102    27295  19043  18121   -559   -283    148       C  
ATOM   3501  C   ILE B1102     -30.629  18.138 -62.874  1.00172.33           C  
ANISOU 3501  C   ILE B1102    27492  19404  18579   -602   -126     93       C  
ATOM   3502  O   ILE B1102     -29.704  18.917 -62.627  1.00171.97           O  
ANISOU 3502  O   ILE B1102    27510  19279  18551   -638    -69     80       O  
ATOM   3503  CB  ILE B1102     -32.979  19.110 -62.891  1.00172.75           C  
ANISOU 3503  CB  ILE B1102    27581  19509  18546   -363   -435    178       C  
ATOM   3504  N   GLN B1103     -30.690  16.872 -62.391  1.00167.76           N  
ANISOU 3504  N   GLN B1103    26727  18931  18083   -600    -67     65       N  
ATOM   3505  CA  GLN B1103     -29.662  16.233 -61.556  1.00166.41           C  
ANISOU 3505  CA  GLN B1103    26406  18794  18030   -630     73     16       C  
ATOM   3506  C   GLN B1103     -28.348  16.010 -62.334  1.00170.84           C  
ANISOU 3506  C   GLN B1103    27061  19280  18571   -788    234    -11       C  
ATOM   3507  O   GLN B1103     -27.270  16.105 -61.741  1.00169.94           O  
ANISOU 3507  O   GLN B1103    26877  19152  18539   -818    336    -40       O  
ATOM   3508  CB  GLN B1103     -30.181  14.904 -60.978  1.00166.75           C  
ANISOU 3508  CB  GLN B1103    26254  18957  18147   -590     82      2       C  
ATOM   3509  N   LYS B1104     -28.449  15.725 -63.663  1.00168.18           N  
ANISOU 3509  N   LYS B1104    26882  18897  18120   -887    255      1       N  
ATOM   3510  CA  LYS B1104     -27.329  15.495 -64.590  1.00180.11           C  
ANISOU 3510  CA  LYS B1104    28508  20340  19584  -1033    416    -19       C  
ATOM   3511  C   LYS B1104     -26.979  16.772 -65.356  1.00177.22           C  
ANISOU 3511  C   LYS B1104    28357  19860  19116  -1103    405     15       C  
ATOM   3512  O   LYS B1104     -26.422  17.707 -64.783  1.00129.86           O  
ANISOU 3512  O   LYS B1104    22354  13823  13165  -1096    407     21       O  
ATOM   3513  CB  LYS B1104     -27.665  14.367 -65.580  1.00182.64           C  
ANISOU 3513  CB  LYS B1104    28896  20673  19825  -1098    450    -30       C  
ATOM   3514  N   ARG B  41     -31.519  21.638 -59.037  1.00150.05           N  
ANISOU 3514  N   ARG B  41    24592  16538  15885    -67   -413     99       N  
ATOM   3515  CA  ARG B  41     -31.127  22.918 -59.628  1.00150.92           C  
ANISOU 3515  CA  ARG B  41    24950  16487  15906   -110   -459    117       C  
ATOM   3516  C   ARG B  41     -29.633  23.252 -59.407  1.00153.41           C  
ANISOU 3516  C   ARG B  41    25320  16708  16261   -256   -352     85       C  
ATOM   3517  O   ARG B  41     -28.931  22.511 -58.709  1.00152.34           O  
ANISOU 3517  O   ARG B  41    25017  16638  16228   -301   -250     46       O  
ATOM   3518  CB  ARG B  41     -32.043  24.052 -59.127  1.00152.46           C  
ANISOU 3518  CB  ARG B  41    25229  16643  16055     91   -608    140       C  
ATOM   3519  N   SER B  42     -29.157  24.367 -60.019  1.00149.10           N  
ANISOU 3519  N   SER B  42    25009  16010  15633   -334   -381    107       N  
ATOM   3520  CA  SER B  42     -27.773  24.860 -59.963  1.00147.77           C  
ANISOU 3520  CA  SER B  42    24918  15741  15488   -494   -296     94       C  
ATOM   3521  C   SER B  42     -27.265  25.096 -58.528  1.00146.72           C  
ANISOU 3521  C   SER B  42    24677  15614  15454   -436   -297     54       C  
ATOM   3522  O   SER B  42     -26.463  24.296 -58.037  1.00145.26           O  
ANISOU 3522  O   SER B  42    24317  15502  15372   -509   -187     22       O  
ATOM   3523  CB  SER B  42     -27.614  26.114 -60.825  1.00152.72           C  
ANISOU 3523  CB  SER B  42    25833  16199  15994   -567   -359    137       C  
ATOM   3524  OG  SER B  42     -28.044  25.884 -62.157  1.00161.29           O  
ANISOU 3524  OG  SER B  42    27031  17274  16978   -627   -360    174       O  
ATOM   3525  N   ALA B  43     -27.757  26.165 -57.859  1.00140.54           N  
ANISOU 3525  N   ALA B  43    24006  14756  14636   -293   -425     57       N  
ATOM   3526  CA  ALA B  43     -27.404  26.544 -56.486  1.00138.39           C  
ANISOU 3526  CA  ALA B  43    23681  14469  14431   -219   -453     19       C  
ATOM   3527  C   ALA B  43     -27.889  25.520 -55.434  1.00137.12           C  
ANISOU 3527  C   ALA B  43    23262  14473  14363    -83   -427    -15       C  
ATOM   3528  O   ALA B  43     -27.251  25.374 -54.394  1.00135.27           O  
ANISOU 3528  O   ALA B  43    22928  14259  14210    -87   -395    -51       O  
ATOM   3529  CB  ALA B  43     -27.949  27.931 -56.174  1.00140.08           C  
ANISOU 3529  CB  ALA B  43    24114  14550  14559    -82   -601     30       C  
ATOM   3530  N   SER B  44     -29.006  24.809 -55.721  1.00131.31           N  
ANISOU 3530  N   SER B  44    22425  13855  13614     26   -444      2       N  
ATOM   3531  CA  SER B  44     -29.625  23.768 -54.878  1.00128.96           C  
ANISOU 3531  CA  SER B  44    21886  13722  13391    145   -419    -17       C  
ATOM   3532  C   SER B  44     -28.654  22.599 -54.602  1.00126.53           C  
ANISOU 3532  C   SER B  44    21395  13491  13191     11   -284    -48       C  
ATOM   3533  O   SER B  44     -28.672  22.027 -53.514  1.00124.61           O  
ANISOU 3533  O   SER B  44    20986  13336  13023     86   -261    -75       O  
ATOM   3534  CB  SER B  44     -30.897  23.242 -55.541  1.00133.96           C  
ANISOU 3534  CB  SER B  44    22465  14453  13983    229   -464     21       C  
ATOM   3535  OG  SER B  44     -31.782  24.295 -55.890  1.00145.56           O  
ANISOU 3535  OG  SER B  44    24097  15854  15355    357   -591     56       O  
ATOM   3536  N   SER B  45     -27.813  22.265 -55.600  1.00119.53           N  
ANISOU 3536  N   SER B  45    20547  12566  12302   -180   -193    -43       N  
ATOM   3537  CA  SER B  45     -26.762  21.256 -55.546  1.00116.75           C  
ANISOU 3537  CA  SER B  45    20051  12267  12043   -316    -56    -69       C  
ATOM   3538  C   SER B  45     -25.624  21.753 -54.648  1.00115.46           C  
ANISOU 3538  C   SER B  45    19874  12048  11948   -368    -36    -96       C  
ATOM   3539  O   SER B  45     -25.095  20.983 -53.856  1.00114.18           O  
ANISOU 3539  O   SER B  45    19538  11961  11885   -373     25   -125       O  
ATOM   3540  CB  SER B  45     -26.226  20.993 -56.951  1.00121.91           C  
ANISOU 3540  CB  SER B  45    20791  12880  12651   -489     33    -51       C  
ATOM   3541  OG  SER B  45     -25.109  20.118 -56.943  1.00133.47           O  
ANISOU 3541  OG  SER B  45    22128  14385  14202   -613    176    -77       O  
ATOM   3542  N   LEU B  46     -25.244  23.037 -54.791  1.00109.95           N  
ANISOU 3542  N   LEU B  46    19368  11214  11195   -413    -98    -83       N  
ATOM   3543  CA  LEU B  46     -24.184  23.698 -54.029  1.00108.33           C  
ANISOU 3543  CA  LEU B  46    19188  10933  11039   -484   -107   -100       C  
ATOM   3544  C   LEU B  46     -24.572  23.848 -52.555  1.00108.90           C  
ANISOU 3544  C   LEU B  46    19195  11035  11147   -317   -188   -132       C  
ATOM   3545  O   LEU B  46     -23.734  23.619 -51.689  1.00108.54           O  
ANISOU 3545  O   LEU B  46    19044  11008  11188   -360   -162   -158       O  
ATOM   3546  CB  LEU B  46     -23.850  25.062 -54.666  1.00109.47           C  
ANISOU 3546  CB  LEU B  46    19587  10911  11095   -578   -167    -70       C  
ATOM   3547  CG  LEU B  46     -22.660  25.849 -54.111  1.00114.62           C  
ANISOU 3547  CG  LEU B  46    20297  11465  11788   -703   -182    -75       C  
ATOM   3548  CD1 LEU B  46     -21.373  25.021 -54.111  1.00114.50           C  
ANISOU 3548  CD1 LEU B  46    20094  11523  11889   -872    -44    -83       C  
ATOM   3549  CD2 LEU B  46     -22.479  27.146 -54.863  1.00117.39           C  
ANISOU 3549  CD2 LEU B  46    20917  11648  12037   -802   -244    -37       C  
ATOM   3550  N   ALA B  47     -25.847  24.194 -52.280  1.00102.94           N  
ANISOU 3550  N   ALA B  47    18496  10292  10325   -123   -285   -127       N  
ATOM   3551  CA  ALA B  47     -26.412  24.340 -50.943  1.00101.33           C  
ANISOU 3551  CA  ALA B  47    18242  10125  10132     64   -354   -155       C  
ATOM   3552  C   ALA B  47     -26.313  23.016 -50.221  1.00104.23           C  
ANISOU 3552  C   ALA B  47    18359  10643  10600     85   -273   -177       C  
ATOM   3553  O   ALA B  47     -25.949  22.983 -49.048  1.00104.55           O  
ANISOU 3553  O   ALA B  47    18338  10698  10689    133   -287   -208       O  
ATOM   3554  CB  ALA B  47     -27.869  24.747 -51.041  1.00102.19           C  
ANISOU 3554  CB  ALA B  47    18423  10252  10154    266   -441   -135       C  
ATOM   3555  N   LEU B  48     -26.606  21.919 -50.941  1.00 99.28           N  
ANISOU 3555  N   LEU B  48    17604  10119   9999     44   -193   -161       N  
ATOM   3556  CA  LEU B  48     -26.577  20.554 -50.439  1.00 97.29           C  
ANISOU 3556  CA  LEU B  48    17128  10003   9833     53   -114   -176       C  
ATOM   3557  C   LEU B  48     -25.147  20.137 -50.097  1.00100.34           C  
ANISOU 3557  C   LEU B  48    17429  10380  10317    -87    -35   -201       C  
ATOM   3558  O   LEU B  48     -24.906  19.704 -48.961  1.00100.38           O  
ANISOU 3558  O   LEU B  48    17315  10438  10387    -33    -33   -225       O  
ATOM   3559  CB  LEU B  48     -27.240  19.606 -51.454  1.00 96.87           C  
ANISOU 3559  CB  LEU B  48    17008  10032   9765     25    -63   -150       C  
ATOM   3560  CG  LEU B  48     -27.884  18.326 -50.917  1.00101.44           C  
ANISOU 3560  CG  LEU B  48    17389  10758  10396    102    -29   -151       C  
ATOM   3561  CD1 LEU B  48     -28.704  18.576 -49.646  1.00101.80           C  
ANISOU 3561  CD1 LEU B  48    17381  10862  10436    292    -99   -154       C  
ATOM   3562  CD2 LEU B  48     -28.754  17.680 -51.972  1.00103.43           C  
ANISOU 3562  CD2 LEU B  48    17626  11067  10605     84    -22   -119       C  
ATOM   3563  N   ALA B  49     -24.189  20.344 -51.033  1.00 95.59           N  
ANISOU 3563  N   ALA B  49    16891   9707   9721   -263     25   -192       N  
ATOM   3564  CA  ALA B  49     -22.774  20.030 -50.816  1.00 94.88           C  
ANISOU 3564  CA  ALA B  49    16710   9612   9728   -403    103   -207       C  
ATOM   3565  C   ALA B  49     -22.221  20.787 -49.606  1.00 99.67           C  
ANISOU 3565  C   ALA B  49    17340  10163  10366   -382     21   -227       C  
ATOM   3566  O   ALA B  49     -21.472  20.196 -48.832  1.00 98.75           O  
ANISOU 3566  O   ALA B  49    17078  10097  10345   -408     54   -246       O  
ATOM   3567  CB  ALA B  49     -21.957  20.333 -52.054  1.00 96.10           C  
ANISOU 3567  CB  ALA B  49    16951   9698   9865   -585    177   -185       C  
ATOM   3568  N   ILE B  50     -22.645  22.058 -49.402  1.00 97.80           N  
ANISOU 3568  N   ILE B  50    17294   9821  10044   -321    -94   -223       N  
ATOM   3569  CA  ILE B  50     -22.244  22.869 -48.245  1.00 98.86           C  
ANISOU 3569  CA  ILE B  50    17495   9884  10184   -290   -192   -245       C  
ATOM   3570  C   ILE B  50     -22.797  22.271 -46.935  1.00104.41           C  
ANISOU 3570  C   ILE B  50    18076  10680  10915   -118   -219   -275       C  
ATOM   3571  O   ILE B  50     -22.021  22.051 -45.997  1.00103.89           O  
ANISOU 3571  O   ILE B  50    17926  10628  10920   -148   -228   -296       O  
ATOM   3572  CB  ILE B  50     -22.572  24.381 -48.411  1.00102.88           C  
ANISOU 3572  CB  ILE B  50    18269  10239  10583   -264   -309   -236       C  
ATOM   3573  CG1 ILE B  50     -21.836  25.030 -49.621  1.00103.88           C  
ANISOU 3573  CG1 ILE B  50    18527  10259  10683   -464   -282   -201       C  
ATOM   3574  CG2 ILE B  50     -22.298  25.157 -47.109  1.00104.56           C  
ANISOU 3574  CG2 ILE B  50    18568  10374  10788   -204   -420   -267       C  
ATOM   3575  CD1 ILE B  50     -20.313  24.586 -49.883  1.00111.73           C  
ANISOU 3575  CD1 ILE B  50    19392  11274  11786   -693   -181   -191       C  
ATOM   3576  N   ALA B  51     -24.127  21.971 -46.907  1.00101.16           N  
ANISOU 3576  N   ALA B  51    17647  10341  10448     52   -230   -270       N  
ATOM   3577  CA  ALA B  51     -24.851  21.355 -45.790  1.00100.09           C  
ANISOU 3577  CA  ALA B  51    17396  10311  10324    221   -240   -286       C  
ATOM   3578  C   ALA B  51     -24.191  20.053 -45.343  1.00103.93           C  
ANISOU 3578  C   ALA B  51    17668  10899  10921    160   -156   -297       C  
ATOM   3579  O   ALA B  51     -24.030  19.845 -44.138  1.00104.50           O  
ANISOU 3579  O   ALA B  51    17681  11001  11022    228   -183   -319       O  
ATOM   3580  CB  ALA B  51     -26.293  21.090 -46.183  1.00100.44           C  
ANISOU 3580  CB  ALA B  51    17419  10435  10307    364   -240   -262       C  
ATOM   3581  N   ILE B  52     -23.783  19.195 -46.304  1.00 99.59           N  
ANISOU 3581  N   ILE B  52    17019  10395  10427     35    -56   -282       N  
ATOM   3582  CA  ILE B  52     -23.121  17.917 -46.011  1.00 98.69           C  
ANISOU 3582  CA  ILE B  52    16712  10368  10418    -21     30   -291       C  
ATOM   3583  C   ILE B  52     -21.724  18.170 -45.432  1.00100.81           C  
ANISOU 3583  C   ILE B  52    16954  10586  10764   -126     20   -308       C  
ATOM   3584  O   ILE B  52     -21.394  17.584 -44.395  1.00 99.47           O  
ANISOU 3584  O   ILE B  52    16670  10468  10655    -85     14   -324       O  
ATOM   3585  CB  ILE B  52     -23.153  16.955 -47.239  1.00101.89           C  
ANISOU 3585  CB  ILE B  52    17046  10824  10843   -106    139   -273       C  
ATOM   3586  CG1 ILE B  52     -24.517  16.228 -47.313  1.00101.73           C  
ANISOU 3586  CG1 ILE B  52    16973  10899  10782     11    141   -258       C  
ATOM   3587  CG2 ILE B  52     -22.015  15.936 -47.210  1.00102.90           C  
ANISOU 3587  CG2 ILE B  52    17022  10993  11082   -207    236   -285       C  
ATOM   3588  CD1 ILE B  52     -25.073  16.008 -48.729  1.00108.87           C  
ANISOU 3588  CD1 ILE B  52    17929  11804  11632    -43    178   -233       C  
ATOM   3589  N   THR B  53     -20.950  19.100 -46.055  1.00 97.18           N  
ANISOU 3589  N   THR B  53    16606  10023  10294   -259      5   -299       N  
ATOM   3590  CA  THR B  53     -19.611  19.517 -45.603  1.00 97.23           C  
ANISOU 3590  CA  THR B  53    16596   9976  10372   -383    -20   -305       C  
ATOM   3591  C   THR B  53     -19.684  20.033 -44.156  1.00100.24           C  
ANISOU 3591  C   THR B  53    17024  10325  10736   -284   -143   -331       C  
ATOM   3592  O   THR B  53     -18.844  19.660 -43.335  1.00100.26           O  
ANISOU 3592  O   THR B  53    16918  10355  10822   -320   -157   -342       O  
ATOM   3593  CB  THR B  53     -18.975  20.530 -46.580  1.00104.66           C  
ANISOU 3593  CB  THR B  53    17673  10810  11285   -545    -21   -282       C  
ATOM   3594  OG1 THR B  53     -18.959  19.965 -47.885  1.00101.96           O  
ANISOU 3594  OG1 THR B  53    17292  10504  10945   -622    102   -261       O  
ATOM   3595  CG2 THR B  53     -17.544  20.895 -46.205  1.00105.18           C  
ANISOU 3595  CG2 THR B  53    17693  10835  11437   -700    -40   -277       C  
ATOM   3596  N   ALA B  54     -20.726  20.839 -43.846  1.00 95.28           N  
ANISOU 3596  N   ALA B  54    16558   9645   9997   -147   -229   -339       N  
ATOM   3597  CA  ALA B  54     -21.012  21.390 -42.523  1.00 94.29           C  
ANISOU 3597  CA  ALA B  54    16516   9484   9824    -21   -339   -367       C  
ATOM   3598  C   ALA B  54     -21.366  20.288 -41.515  1.00 95.37           C  
ANISOU 3598  C   ALA B  54    16492   9744   9999    101   -311   -381       C  
ATOM   3599  O   ALA B  54     -20.860  20.321 -40.392  1.00 94.53           O  
ANISOU 3599  O   ALA B  54    16376   9626   9915    118   -374   -402       O  
ATOM   3600  CB  ALA B  54     -22.129  22.411 -42.616  1.00 95.58           C  
ANISOU 3600  CB  ALA B  54    16885   9574   9857    116   -412   -370       C  
ATOM   3601  N   LEU B  55     -22.198  19.299 -41.928  1.00 91.05           N  
ANISOU 3601  N   LEU B  55    15828   9310   9458    172   -223   -366       N  
ATOM   3602  CA  LEU B  55     -22.576  18.136 -41.107  1.00 89.86           C  
ANISOU 3602  CA  LEU B  55    15520   9279   9342    270   -184   -369       C  
ATOM   3603  C   LEU B  55     -21.361  17.245 -40.791  1.00 93.18           C  
ANISOU 3603  C   LEU B  55    15785   9736   9885    160   -144   -373       C  
ATOM   3604  O   LEU B  55     -21.202  16.862 -39.633  1.00 91.55           O  
ANISOU 3604  O   LEU B  55    15524   9564   9699    223   -178   -386       O  
ATOM   3605  CB  LEU B  55     -23.697  17.304 -41.774  1.00 88.73           C  
ANISOU 3605  CB  LEU B  55    15295   9238   9179    336   -106   -343       C  
ATOM   3606  CG  LEU B  55     -24.169  16.025 -41.047  1.00 90.92           C  
ANISOU 3606  CG  LEU B  55    15413   9641   9490    419    -57   -336       C  
ATOM   3607  CD1 LEU B  55     -24.822  16.342 -39.717  1.00 91.00           C  
ANISOU 3607  CD1 LEU B  55    15465   9676   9437    583   -119   -347       C  
ATOM   3608  CD2 LEU B  55     -25.133  15.233 -41.909  1.00 90.61           C  
ANISOU 3608  CD2 LEU B  55    15300   9688   9439    435     12   -305       C  
ATOM   3609  N   TYR B  56     -20.511  16.925 -41.807  1.00 90.51           N  
ANISOU 3609  N   TYR B  56    15377   9390   9620      6    -69   -360       N  
ATOM   3610  CA  TYR B  56     -19.313  16.099 -41.593  1.00 90.61           C  
ANISOU 3610  CA  TYR B  56    15230   9441   9755    -89    -24   -361       C  
ATOM   3611  C   TYR B  56     -18.288  16.818 -40.710  1.00 94.07           C  
ANISOU 3611  C   TYR B  56    15699   9814  10229   -148   -125   -373       C  
ATOM   3612  O   TYR B  56     -17.683  16.187 -39.845  1.00 92.14           O  
ANISOU 3612  O   TYR B  56    15341   9612  10056   -140   -143   -379       O  
ATOM   3613  CB  TYR B  56     -18.655  15.653 -42.916  1.00 92.62           C  
ANISOU 3613  CB  TYR B  56    15413   9706  10073   -227     91   -344       C  
ATOM   3614  CG  TYR B  56     -19.236  14.405 -43.549  1.00 95.33           C  
ANISOU 3614  CG  TYR B  56    15661  10133  10427   -191    201   -336       C  
ATOM   3615  CD1 TYR B  56     -19.243  13.189 -42.868  1.00 97.48           C  
ANISOU 3615  CD1 TYR B  56    15795  10485  10757   -126    232   -341       C  
ATOM   3616  CD2 TYR B  56     -19.682  14.412 -44.864  1.00 96.59           C  
ANISOU 3616  CD2 TYR B  56    15878  10283  10540   -237    270   -323       C  
ATOM   3617  CE1 TYR B  56     -19.766  12.033 -43.451  1.00 96.73           C  
ANISOU 3617  CE1 TYR B  56    15632  10453  10668   -104    323   -333       C  
ATOM   3618  CE2 TYR B  56     -20.190  13.259 -45.464  1.00 97.08           C  
ANISOU 3618  CE2 TYR B  56    15869  10410  10605   -216    359   -318       C  
ATOM   3619  CZ  TYR B  56     -20.239  12.074 -44.751  1.00104.29           C  
ANISOU 3619  CZ  TYR B  56    16654  11398  11575   -152    384   -323       C  
ATOM   3620  OH  TYR B  56     -20.734  10.942 -45.349  1.00108.80           O  
ANISOU 3620  OH  TYR B  56    17175  12020  12145   -143    464   -317       O  
ATOM   3621  N   SER B  57     -18.112  18.140 -40.913  1.00 92.06           N  
ANISOU 3621  N   SER B  57    15609   9449   9918   -210   -202   -374       N  
ATOM   3622  CA  SER B  57     -17.164  18.942 -40.128  1.00 92.83           C  
ANISOU 3622  CA  SER B  57    15763   9469  10039   -287   -318   -383       C  
ATOM   3623  C   SER B  57     -17.610  19.174 -38.678  1.00 96.73           C  
ANISOU 3623  C   SER B  57    16335   9946  10470   -146   -431   -412       C  
ATOM   3624  O   SER B  57     -16.752  19.263 -37.798  1.00 95.98           O  
ANISOU 3624  O   SER B  57    16215   9831  10423   -195   -515   -420       O  
ATOM   3625  CB  SER B  57     -16.834  20.253 -40.826  1.00 95.04           C  
ANISOU 3625  CB  SER B  57    16211   9625  10274   -410   -367   -372       C  
ATOM   3626  OG  SER B  57     -18.024  20.963 -41.104  1.00103.52           O  
ANISOU 3626  OG  SER B  57    17472  10643  11219   -299   -396   -380       O  
ATOM   3627  N   ALA B  58     -18.939  19.237 -38.425  1.00 93.18           N  
ANISOU 3627  N   ALA B  58    15974   9516   9915     29   -431   -424       N  
ATOM   3628  CA  ALA B  58     -19.483  19.377 -37.071  1.00 93.11           C  
ANISOU 3628  CA  ALA B  58    16040   9507   9832    185   -512   -450       C  
ATOM   3629  C   ALA B  58     -19.299  18.052 -36.326  1.00 95.97           C  
ANISOU 3629  C   ALA B  58    16215   9982  10266    227   -469   -446       C  
ATOM   3630  O   ALA B  58     -18.850  18.064 -35.178  1.00 96.26           O  
ANISOU 3630  O   ALA B  58    16266  10005  10304    251   -553   -463       O  
ATOM   3631  CB  ALA B  58     -20.955  19.768 -37.116  1.00 93.56           C  
ANISOU 3631  CB  ALA B  58    16215   9570   9764    363   -502   -456       C  
ATOM   3632  N   VAL B  59     -19.599  16.913 -37.002  1.00 91.09           N  
ANISOU 3632  N   VAL B  59    15438   9467   9706    227   -346   -424       N  
ATOM   3633  CA  VAL B  59     -19.450  15.553 -36.467  1.00 89.80           C  
ANISOU 3633  CA  VAL B  59    15101   9405   9614    259   -294   -415       C  
ATOM   3634  C   VAL B  59     -17.971  15.230 -36.243  1.00 93.63           C  
ANISOU 3634  C   VAL B  59    15474   9880  10221    131   -320   -412       C  
ATOM   3635  O   VAL B  59     -17.629  14.666 -35.203  1.00 93.67           O  
ANISOU 3635  O   VAL B  59    15415   9918  10256    172   -362   -415       O  
ATOM   3636  CB  VAL B  59     -20.196  14.489 -37.313  1.00 92.98           C  
ANISOU 3636  CB  VAL B  59    15392   9901  10034    285   -166   -392       C  
ATOM   3637  CG1 VAL B  59     -19.880  13.065 -36.850  1.00 92.19           C  
ANISOU 3637  CG1 VAL B  59    15126   9885  10015    297   -114   -380       C  
ATOM   3638  CG2 VAL B  59     -21.702  14.725 -37.265  1.00 92.80           C  
ANISOU 3638  CG2 VAL B  59    15451   9911   9897    428   -158   -386       C  
ATOM   3639  N   CYS B  60     -17.095  15.638 -37.184  1.00 89.98           N  
ANISOU 3639  N   CYS B  60    14991   9375   9825    -22   -299   -403       N  
ATOM   3640  CA  CYS B  60     -15.649  15.440 -37.079  1.00 89.70           C  
ANISOU 3640  CA  CYS B  60    14831   9338   9914   -153   -320   -393       C  
ATOM   3641  C   CYS B  60     -14.999  16.282 -35.967  1.00 94.40           C  
ANISOU 3641  C   CYS B  60    15509   9861  10496   -183   -481   -406       C  
ATOM   3642  O   CYS B  60     -14.224  15.744 -35.178  1.00 93.83           O  
ANISOU 3642  O   CYS B  60    15327   9822  10501   -197   -531   -401       O  
ATOM   3643  CB  CYS B  60     -14.961  15.655 -38.421  1.00 89.80           C  
ANISOU 3643  CB  CYS B  60    14794   9335   9991   -308   -237   -373       C  
ATOM   3644  SG  CYS B  60     -13.182  15.332 -38.395  1.00 94.57           S  
ANISOU 3644  SG  CYS B  60    15203   9968  10764   -464   -238   -350       S  
ATOM   3645  N   ALA B  61     -15.311  17.588 -35.905  1.00 92.47           N  
ANISOU 3645  N   ALA B  61    15470   9512  10153   -193   -571   -421       N  
ATOM   3646  CA  ALA B  61     -14.735  18.484 -34.906  1.00 93.91           C  
ANISOU 3646  CA  ALA B  61    15771   9604  10305   -232   -736   -437       C  
ATOM   3647  C   ALA B  61     -15.200  18.224 -33.481  1.00 98.76           C  
ANISOU 3647  C   ALA B  61    16443  10231  10850    -80   -817   -462       C  
ATOM   3648  O   ALA B  61     -14.396  18.377 -32.565  1.00 99.57           O  
ANISOU 3648  O   ALA B  61    16550  10304  10980   -127   -939   -467       O  
ATOM   3649  CB  ALA B  61     -14.973  19.921 -35.284  1.00 95.53           C  
ANISOU 3649  CB  ALA B  61    16204   9680  10415   -280   -806   -447       C  
ATOM   3650  N   VAL B  62     -16.474  17.834 -33.280  1.00 94.84           N  
ANISOU 3650  N   VAL B  62    15989   9784  10261     96   -753   -473       N  
ATOM   3651  CA  VAL B  62     -16.980  17.522 -31.937  1.00 94.77           C  
ANISOU 3651  CA  VAL B  62    16032   9799  10176    247   -807   -492       C  
ATOM   3652  C   VAL B  62     -16.490  16.104 -31.543  1.00 98.44           C  
ANISOU 3652  C   VAL B  62    16284  10372  10748    247   -762   -470       C  
ATOM   3653  O   VAL B  62     -16.137  15.871 -30.383  1.00 99.73           O  
ANISOU 3653  O   VAL B  62    16456  10535  10902    284   -851   -477       O  
ATOM   3654  CB  VAL B  62     -18.514  17.758 -31.783  1.00 97.98           C  
ANISOU 3654  CB  VAL B  62    16567  10223  10440    436   -760   -506       C  
ATOM   3655  CG1 VAL B  62     -19.033  17.291 -30.431  1.00 97.65           C  
ANISOU 3655  CG1 VAL B  62    16556  10227  10321    589   -786   -518       C  
ATOM   3656  CG2 VAL B  62     -18.849  19.227 -31.968  1.00 98.79           C  
ANISOU 3656  CG2 VAL B  62    16904  10200  10433    451   -834   -532       C  
ATOM   3657  N   GLY B  63     -16.393  15.216 -32.528  1.00 91.88           N  
ANISOU 3657  N   GLY B  63    15280   9617  10015    199   -633   -444       N  
ATOM   3658  CA  GLY B  63     -15.903  13.860 -32.341  1.00 90.60           C  
ANISOU 3658  CA  GLY B  63    14922   9543   9959    197   -580   -422       C  
ATOM   3659  C   GLY B  63     -14.459  13.820 -31.894  1.00 95.36           C  
ANISOU 3659  C   GLY B  63    15432  10128  10673     87   -674   -414       C  
ATOM   3660  O   GLY B  63     -14.174  13.289 -30.825  1.00 94.58           O  
ANISOU 3660  O   GLY B  63    15301  10052  10584    139   -744   -412       O  
ATOM   3661  N   LEU B  64     -13.540  14.417 -32.686  1.00 94.34           N  
ANISOU 3661  N   LEU B  64    15262   9960  10623    -69   -683   -405       N  
ATOM   3662  CA  LEU B  64     -12.101  14.454 -32.374  1.00 95.83           C  
ANISOU 3662  CA  LEU B  64    15334  10143  10933   -196   -772   -387       C  
ATOM   3663  C   LEU B  64     -11.814  15.113 -31.024  1.00103.64           C  
ANISOU 3663  C   LEU B  64    16450  11065  11863   -187   -964   -403       C  
ATOM   3664  O   LEU B  64     -11.163  14.516 -30.166  1.00103.93           O  
ANISOU 3664  O   LEU B  64    16392  11135  11960   -177  -1040   -391       O  
ATOM   3665  CB  LEU B  64     -11.278  15.140 -33.488  1.00 96.24           C  
ANISOU 3665  CB  LEU B  64    15338  10165  11064   -375   -743   -368       C  
ATOM   3666  CG  LEU B  64     -11.244  14.459 -34.869  1.00100.16           C  
ANISOU 3666  CG  LEU B  64    15693  10729  11636   -410   -555   -349       C  
ATOM   3667  CD1 LEU B  64     -10.468  15.286 -35.868  1.00101.00           C  
ANISOU 3667  CD1 LEU B  64    15783  10798  11795   -589   -532   -328       C  
ATOM   3668  CD2 LEU B  64     -10.650  13.071 -34.804  1.00102.53           C  
ANISOU 3668  CD2 LEU B  64    15769  11126  12060   -376   -481   -330       C  
ATOM   3669  N   LEU B  65     -12.356  16.312 -30.819  1.00102.02           N  
ANISOU 3669  N   LEU B  65    16474  10761  11529   -177  -1043   -431       N  
ATOM   3670  CA  LEU B  65     -12.135  17.076 -29.608  1.00103.75           C  
ANISOU 3670  CA  LEU B  65    16859  10894  11667   -172  -1228   -453       C  
ATOM   3671  C   LEU B  65     -12.810  16.470 -28.353  1.00106.86           C  
ANISOU 3671  C   LEU B  65    17316  11318  11968      5  -1261   -471       C  
ATOM   3672  O   LEU B  65     -12.210  16.508 -27.277  1.00107.22           O  
ANISOU 3672  O   LEU B  65    17393  11336  12008     -6  -1406   -474       O  
ATOM   3673  CB  LEU B  65     -12.520  18.557 -29.826  1.00105.10           C  
ANISOU 3673  CB  LEU B  65    17279  10934  11720   -207  -1298   -480       C  
ATOM   3674  CG  LEU B  65     -11.444  19.526 -30.431  1.00112.04           C  
ANISOU 3674  CG  LEU B  65    18167  11732  12670   -430  -1378   -461       C  
ATOM   3675  CD1 LEU B  65     -10.175  19.619 -29.553  1.00114.35           C  
ANISOU 3675  CD1 LEU B  65    18400  12006  13042   -554  -1552   -445       C  
ATOM   3676  CD2 LEU B  65     -11.125  19.241 -31.914  1.00113.21           C  
ANISOU 3676  CD2 LEU B  65    18143  11940  12932   -540  -1222   -425       C  
ATOM   3677  N   GLY B  66     -14.005  15.898 -28.499  1.00101.64           N  
ANISOU 3677  N   GLY B  66    16665  10718  11237    156  -1131   -477       N  
ATOM   3678  CA  GLY B  66     -14.720  15.274 -27.384  1.00100.90           C  
ANISOU 3678  CA  GLY B  66    16621  10665  11051    320  -1136   -485       C  
ATOM   3679  C   GLY B  66     -14.018  14.033 -26.853  1.00104.50           C  
ANISOU 3679  C   GLY B  66    16895  11198  11613    315  -1146   -455       C  
ATOM   3680  O   GLY B  66     -13.858  13.878 -25.638  1.00104.53           O  
ANISOU 3680  O   GLY B  66    16964  11189  11564    370  -1254   -460       O  
ATOM   3681  N   ASN B  67     -13.560  13.162 -27.781  1.00 99.70           N  
ANISOU 3681  N   ASN B  67    16070  10663  11149    250  -1036   -425       N  
ATOM   3682  CA  ASN B  67     -12.838  11.927 -27.496  1.00 98.72           C  
ANISOU 3682  CA  ASN B  67    15756  10609  11144    248  -1029   -394       C  
ATOM   3683  C   ASN B  67     -11.427  12.176 -26.988  1.00104.06           C  
ANISOU 3683  C   ASN B  67    16364  11255  11917    135  -1185   -382       C  
ATOM   3684  O   ASN B  67     -11.021  11.505 -26.035  1.00104.35           O  
ANISOU 3684  O   ASN B  67    16356  11317  11977    180  -1265   -367       O  
ATOM   3685  CB  ASN B  67     -12.823  11.015 -28.705  1.00 96.23           C  
ANISOU 3685  CB  ASN B  67    15258  10366  10938    223   -860   -372       C  
ATOM   3686  CG  ASN B  67     -14.159  10.396 -28.993  1.00111.57           C  
ANISOU 3686  CG  ASN B  67    17235  12358  12801    339   -724   -372       C  
ATOM   3687  OD1 ASN B  67     -14.792   9.775 -28.133  1.00110.85           O  
ANISOU 3687  OD1 ASN B  67    17183  12297  12638    452   -726   -365       O  
ATOM   3688  ND2 ASN B  67     -14.616  10.546 -30.218  1.00 97.07           N  
ANISOU 3688  ND2 ASN B  67    15381  10530  10971    305   -605   -374       N  
ATOM   3689  N   VAL B  68     -10.673  13.128 -27.602  1.00101.12           N  
ANISOU 3689  N   VAL B  68    15983  10834  11604    -16  -1236   -382       N  
ATOM   3690  CA  VAL B  68      -9.316  13.468 -27.131  1.00102.45           C  
ANISOU 3690  CA  VAL B  68    16078  10978  11869   -145  -1399   -363       C  
ATOM   3691  C   VAL B  68      -9.409  13.988 -25.681  1.00107.73           C  
ANISOU 3691  C   VAL B  68    16945  11573  12413    -97  -1591   -386       C  
ATOM   3692  O   VAL B  68      -8.661  13.518 -24.809  1.00108.49           O  
ANISOU 3692  O   VAL B  68    16972  11689  12562   -102  -1712   -367       O  
ATOM   3693  CB  VAL B  68      -8.529  14.419 -28.084  1.00106.60           C  
ANISOU 3693  CB  VAL B  68    16559  11467  12477   -334  -1411   -351       C  
ATOM   3694  CG1 VAL B  68      -7.275  14.981 -27.414  1.00107.95           C  
ANISOU 3694  CG1 VAL B  68    16699  11600  12717   -475  -1615   -331       C  
ATOM   3695  CG2 VAL B  68      -8.157  13.708 -29.385  1.00105.68           C  
ANISOU 3695  CG2 VAL B  68    16213  11438  12502   -383  -1230   -321       C  
ATOM   3696  N   LEU B  69     -10.393  14.883 -25.423  1.00103.27           N  
ANISOU 3696  N   LEU B  69    16635  10928  11675    -30  -1608   -428       N  
ATOM   3697  CA  LEU B  69     -10.671  15.453 -24.103  1.00103.28           C  
ANISOU 3697  CA  LEU B  69    16871  10848  11522     39  -1766   -459       C  
ATOM   3698  C   LEU B  69     -11.004  14.372 -23.077  1.00105.74           C  
ANISOU 3698  C   LEU B  69    17166  11222  11791    184  -1766   -451       C  
ATOM   3699  O   LEU B  69     -10.458  14.416 -21.976  1.00107.71           O  
ANISOU 3699  O   LEU B  69    17481  11435  12009    178  -1934   -451       O  
ATOM   3700  CB  LEU B  69     -11.806  16.486 -24.179  1.00102.87           C  
ANISOU 3700  CB  LEU B  69    17080  10714  11294    119  -1737   -505       C  
ATOM   3701  CG  LEU B  69     -11.988  17.392 -22.977  1.00108.43           C  
ANISOU 3701  CG  LEU B  69    18067  11303  11829    169  -1907   -547       C  
ATOM   3702  CD1 LEU B  69     -10.873  18.412 -22.903  1.00110.60           C  
ANISOU 3702  CD1 LEU B  69    18409  11469  12143    -21  -2097   -549       C  
ATOM   3703  CD2 LEU B  69     -13.340  18.082 -23.022  1.00109.19           C  
ANISOU 3703  CD2 LEU B  69    18391  11349  11746    316  -1830   -589       C  
ATOM   3704  N   VAL B  70     -11.884  13.411 -23.423  1.00 98.66           N  
ANISOU 3704  N   VAL B  70    16189  10411  10885    304  -1588   -440       N  
ATOM   3705  CA  VAL B  70     -12.232  12.331 -22.502  1.00 97.53           C  
ANISOU 3705  CA  VAL B  70    16030  10327  10701    431  -1575   -423       C  
ATOM   3706  C   VAL B  70     -10.949  11.592 -22.108  1.00105.21           C  
ANISOU 3706  C   VAL B  70    16828  11330  11818    361  -1681   -386       C  
ATOM   3707  O   VAL B  70     -10.649  11.520 -20.911  1.00106.09           O  
ANISOU 3707  O   VAL B  70    17026  11413  11870    395  -1828   -385       O  
ATOM   3708  CB  VAL B  70     -13.350  11.401 -23.044  1.00 98.24           C  
ANISOU 3708  CB  VAL B  70    16050  10505  10773    543  -1368   -409       C  
ATOM   3709  CG1 VAL B  70     -13.338  10.037 -22.365  1.00 97.44           C  
ANISOU 3709  CG1 VAL B  70    15858  10472  10695    623  -1348   -374       C  
ATOM   3710  CG2 VAL B  70     -14.717  12.052 -22.906  1.00 97.15           C  
ANISOU 3710  CG2 VAL B  70    16109  10346  10457    658  -1302   -440       C  
ATOM   3711  N   MET B  71     -10.152  11.141 -23.120  1.00102.90           N  
ANISOU 3711  N   MET B  71    16298  11090  11710    262  -1615   -357       N  
ATOM   3712  CA  MET B  71      -8.872  10.440 -22.937  1.00103.91           C  
ANISOU 3712  CA  MET B  71    16220  11260  12001    200  -1697   -317       C  
ATOM   3713  C   MET B  71      -7.921  11.227 -22.026  1.00111.50           C  
ANISOU 3713  C   MET B  71    17250  12156  12959    106  -1939   -317       C  
ATOM   3714  O   MET B  71      -7.320  10.633 -21.131  1.00112.17           O  
ANISOU 3714  O   MET B  71    17286  12257  13077    132  -2061   -292       O  
ATOM   3715  CB  MET B  71      -8.207  10.133 -24.289  1.00105.72           C  
ANISOU 3715  CB  MET B  71    16210  11548  12412    104  -1576   -293       C  
ATOM   3716  CG  MET B  71      -8.736   8.884 -24.966  1.00107.52           C  
ANISOU 3716  CG  MET B  71    16315  11851  12685    198  -1377   -279       C  
ATOM   3717  SD  MET B  71      -8.358   8.825 -26.738  1.00111.03           S  
ANISOU 3717  SD  MET B  71    16569  12342  13275     99  -1194   -270       S  
ATOM   3718  CE  MET B  71      -6.721   8.213 -26.703  1.00109.21           C  
ANISOU 3718  CE  MET B  71    16072  12169  13253     33  -1262   -225       C  
ATOM   3719  N   PHE B  72      -7.837  12.567 -22.221  1.00110.10           N  
ANISOU 3719  N   PHE B  72    17207  11895  12730      0  -2016   -345       N  
ATOM   3720  CA  PHE B  72      -7.021  13.496 -21.423  1.00112.07           C  
ANISOU 3720  CA  PHE B  72    17562  12062  12957   -113  -2256   -349       C  
ATOM   3721  C   PHE B  72      -7.460  13.482 -19.955  1.00113.63           C  
ANISOU 3721  C   PHE B  72    17985  12206  12984      3  -2390   -372       C  
ATOM   3722  O   PHE B  72      -6.612  13.335 -19.078  1.00114.08           O  
ANISOU 3722  O   PHE B  72    18020  12253  13073    -38  -2576   -351       O  
ATOM   3723  CB  PHE B  72      -7.101  14.914 -22.004  1.00115.16           C  
ANISOU 3723  CB  PHE B  72    18100  12359  13296   -232  -2284   -379       C  
ATOM   3724  CG  PHE B  72      -6.178  15.922 -21.365  1.00120.27           C  
ANISOU 3724  CG  PHE B  72    18849  12912  13936   -386  -2533   -379       C  
ATOM   3725  CD1 PHE B  72      -6.561  16.615 -20.219  1.00125.49           C  
ANISOU 3725  CD1 PHE B  72    19811  13461  14409   -335  -2694   -421       C  
ATOM   3726  CD2 PHE B  72      -4.949  16.225 -21.940  1.00125.01           C  
ANISOU 3726  CD2 PHE B  72    19255  13532  14709   -587  -2604   -336       C  
ATOM   3727  CE1 PHE B  72      -5.711  17.558 -19.636  1.00128.97           C  
ANISOU 3727  CE1 PHE B  72    20367  13801  14834   -489  -2938   -423       C  
ATOM   3728  CE2 PHE B  72      -4.104  17.180 -21.366  1.00130.43           C  
ANISOU 3728  CE2 PHE B  72    20037  14131  15390   -750  -2845   -330       C  
ATOM   3729  CZ  PHE B  72      -4.493  17.843 -20.220  1.00129.62           C  
ANISOU 3729  CZ  PHE B  72    20247  13906  15097   -704  -3018   -376       C  
ATOM   3730  N   VAL B  73      -8.781  13.608 -19.697  1.00107.99           N  
ANISOU 3730  N   VAL B  73    17479  11465  12088    150  -2292   -411       N  
ATOM   3731  CA  VAL B  73      -9.388  13.569 -18.357  1.00107.86           C  
ANISOU 3731  CA  VAL B  73    17693  11405  11882    284  -2374   -435       C  
ATOM   3732  C   VAL B  73      -8.998  12.265 -17.641  1.00111.22           C  
ANISOU 3732  C   VAL B  73    17989  11904  12365    348  -2407   -391       C  
ATOM   3733  O   VAL B  73      -8.587  12.309 -16.486  1.00111.29           O  
ANISOU 3733  O   VAL B  73    18112  11868  12304    357  -2589   -390       O  
ATOM   3734  CB  VAL B  73     -10.931  13.771 -18.422  1.00110.31           C  
ANISOU 3734  CB  VAL B  73    18185  11711  12017    442  -2209   -472       C  
ATOM   3735  CG1 VAL B  73     -11.624  13.342 -17.131  1.00109.96           C  
ANISOU 3735  CG1 VAL B  73    18315  11667  11798    603  -2231   -480       C  
ATOM   3736  CG2 VAL B  73     -11.280  15.216 -18.765  1.00110.68           C  
ANISOU 3736  CG2 VAL B  73    18436  11651  11965    402  -2238   -522       C  
ATOM   3737  N   ILE B  74      -9.095  11.123 -18.346  1.00107.34           N  
ANISOU 3737  N   ILE B  74    17271  11516  11997    389  -2239   -355       N  
ATOM   3738  CA  ILE B  74      -8.756   9.808 -17.812  1.00107.59           C  
ANISOU 3738  CA  ILE B  74    17173  11613  12092    456  -2250   -310       C  
ATOM   3739  C   ILE B  74      -7.236   9.689 -17.547  1.00116.50           C  
ANISOU 3739  C   ILE B  74    18140  12745  13379    342  -2442   -273       C  
ATOM   3740  O   ILE B  74      -6.857   9.323 -16.433  1.00117.04           O  
ANISOU 3740  O   ILE B  74    18266  12798  13407    380  -2598   -255       O  
ATOM   3741  CB  ILE B  74      -9.341   8.673 -18.700  1.00108.22           C  
ANISOU 3741  CB  ILE B  74    17085  11785  12250    529  -2017   -286       C  
ATOM   3742  CG1 ILE B  74     -10.839   8.486 -18.402  1.00106.84           C  
ANISOU 3742  CG1 ILE B  74    17081  11619  11893    670  -1881   -303       C  
ATOM   3743  CG2 ILE B  74      -8.594   7.355 -18.506  1.00108.71           C  
ANISOU 3743  CG2 ILE B  74    16952  11907  12447    556  -2036   -234       C  
ATOM   3744  CD1 ILE B  74     -11.640   7.737 -19.443  1.00108.53           C  
ANISOU 3744  CD1 ILE B  74    17177  11907  12153    716  -1650   -290       C  
ATOM   3745  N   VAL B  75      -6.383  10.036 -18.537  1.00116.06           N  
ANISOU 3745  N   VAL B  75    17891  12712  13496    201  -2435   -260       N  
ATOM   3746  CA  VAL B  75      -4.917   9.966 -18.404  1.00118.86           C  
ANISOU 3746  CA  VAL B  75    18050  13089  14020     83  -2604   -217       C  
ATOM   3747  C   VAL B  75      -4.388  10.917 -17.293  1.00129.27           C  
ANISOU 3747  C   VAL B  75    19550  14317  15251      0  -2879   -229       C  
ATOM   3748  O   VAL B  75      -3.679  10.452 -16.391  1.00130.36           O  
ANISOU 3748  O   VAL B  75    19647  14464  15421      8  -3052   -195       O  
ATOM   3749  CB  VAL B  75      -4.190  10.161 -19.772  1.00122.01           C  
ANISOU 3749  CB  VAL B  75    18197  13544  14616    -51  -2508   -196       C  
ATOM   3750  CG1 VAL B  75      -2.688  10.386 -19.602  1.00123.56           C  
ANISOU 3750  CG1 VAL B  75    18207  13764  14977   -197  -2700   -150       C  
ATOM   3751  CG2 VAL B  75      -4.436   8.971 -20.688  1.00120.40           C  
ANISOU 3751  CG2 VAL B  75    17794  13433  14518     38  -2276   -176       C  
ATOM   3752  N   ARG B  76      -4.761  12.219 -17.343  1.00128.81           N  
ANISOU 3752  N   ARG B  76    19709  14163  15072    -72  -2925   -276       N  
ATOM   3753  CA  ARG B  76      -4.294  13.237 -16.394  1.00131.80           C  
ANISOU 3753  CA  ARG B  76    20292  14433  15352   -167  -3186   -294       C  
ATOM   3754  C   ARG B  76      -4.969  13.210 -15.011  1.00138.08           C  
ANISOU 3754  C   ARG B  76    21385  15158  15922    -31  -3287   -326       C  
ATOM   3755  O   ARG B  76      -4.258  13.162 -14.006  1.00139.78           O  
ANISOU 3755  O   ARG B  76    21647  15341  16121    -67  -3514   -308       O  
ATOM   3756  CB  ARG B  76      -4.382  14.662 -16.992  1.00133.87           C  
ANISOU 3756  CB  ARG B  76    20692  14603  15571   -302  -3205   -331       C  
ATOM   3757  CG  ARG B  76      -3.576  14.878 -18.281  1.00148.70           C  
ANISOU 3757  CG  ARG B  76    22301  16538  17659   -472  -3139   -294       C  
ATOM   3758  CD  ARG B  76      -2.093  15.115 -18.050  1.00165.43           C  
ANISOU 3758  CD  ARG B  76    24253  18669  19932   -662  -3362   -242       C  
ATOM   3759  NE  ARG B  76      -1.279  14.114 -18.742  1.00178.46           N  
ANISOU 3759  NE  ARG B  76    25523  20465  21819   -683  -3268   -178       N  
ATOM   3760  CZ  ARG B  76       0.045  14.166 -18.859  1.00196.90           C  
ANISOU 3760  CZ  ARG B  76    27617  22856  24340   -843  -3401   -119       C  
ATOM   3761  NH1 ARG B  76       0.727  15.179 -18.337  1.00186.20           N  
ANISOU 3761  NH1 ARG B  76    26359  21421  22966  -1021  -3647   -111       N  
ATOM   3762  NH2 ARG B  76       0.697  13.208 -19.504  1.00184.81           N1+
ANISOU 3762  NH2 ARG B  76    25746  21461  23013   -828  -3288    -65       N1+
ATOM   3763  N   TYR B  77      -6.311  13.251 -14.946  1.00134.38           N  
ANISOU 3763  N   TYR B  77    21113  14668  15277    120  -3125   -370       N  
ATOM   3764  CA  TYR B  77      -7.020  13.344 -13.670  1.00135.38           C  
ANISOU 3764  CA  TYR B  77    21540  14729  15170    252  -3198   -403       C  
ATOM   3765  C   TYR B  77      -7.500  12.003 -13.057  1.00139.61           C  
ANISOU 3765  C   TYR B  77    22039  15343  15666    416  -3111   -372       C  
ATOM   3766  O   TYR B  77      -7.075  11.700 -11.941  1.00140.52           O  
ANISOU 3766  O   TYR B  77    22240  15432  15721    439  -3285   -355       O  
ATOM   3767  CB  TYR B  77      -8.185  14.341 -13.778  1.00136.64           C  
ANISOU 3767  CB  TYR B  77    21974  14808  15134    325  -3101   -470       C  
ATOM   3768  CG  TYR B  77      -7.736  15.762 -14.059  1.00140.86           C  
ANISOU 3768  CG  TYR B  77    22639  15227  15656    172  -3237   -505       C  
ATOM   3769  CD1 TYR B  77      -7.398  16.627 -13.020  1.00145.18           C  
ANISOU 3769  CD1 TYR B  77    23460  15642  16058    126  -3477   -539       C  
ATOM   3770  CD2 TYR B  77      -7.649  16.244 -15.364  1.00141.21           C  
ANISOU 3770  CD2 TYR B  77    22550  15282  15823     67  -3131   -504       C  
ATOM   3771  CE1 TYR B  77      -6.982  17.936 -13.271  1.00147.61           C  
ANISOU 3771  CE1 TYR B  77    23908  15829  16349    -26  -3613   -569       C  
ATOM   3772  CE2 TYR B  77      -7.230  17.550 -15.627  1.00143.58           C  
ANISOU 3772  CE2 TYR B  77    22981  15467  16107    -85  -3258   -530       C  
ATOM   3773  CZ  TYR B  77      -6.901  18.394 -14.576  1.00153.99           C  
ANISOU 3773  CZ  TYR B  77    24575  16651  17284   -133  -3502   -563       C  
ATOM   3774  OH  TYR B  77      -6.495  19.687 -14.819  1.00157.18           O  
ANISOU 3774  OH  TYR B  77    25131  16926  17665   -292  -3638   -588       O  
ATOM   3775  N   THR B  78      -8.384  11.227 -13.741  1.00135.16           N  
ANISOU 3775  N   THR B  78    21366  14865  15124    523  -2858   -361       N  
ATOM   3776  CA  THR B  78      -8.962   9.968 -13.214  1.00134.44           C  
ANISOU 3776  CA  THR B  78    21257  14841  14982    670  -2758   -328       C  
ATOM   3777  C   THR B  78      -7.903   8.890 -12.863  1.00140.38           C  
ANISOU 3777  C   THR B  78    21813  15641  15883    647  -2871   -266       C  
ATOM   3778  O   THR B  78      -8.001   8.273 -11.796  1.00140.55           O  
ANISOU 3778  O   THR B  78    21941  15656  15804    735  -2945   -245       O  
ATOM   3779  CB  THR B  78     -10.053   9.421 -14.140  1.00135.51           C  
ANISOU 3779  CB  THR B  78    21304  15055  15130    755  -2478   -326       C  
ATOM   3780  OG1 THR B  78     -10.878  10.500 -14.574  1.00132.45           O  
ANISOU 3780  OG1 THR B  78    21068  14625  14633    766  -2395   -379       O  
ATOM   3781  CG2 THR B  78     -10.932   8.410 -13.448  1.00133.03           C  
ANISOU 3781  CG2 THR B  78    21058  14788  14698    906  -2376   -300       C  
ATOM   3782  N   LYS B  79      -6.903   8.691 -13.747  1.00137.76           N  
ANISOU 3782  N   LYS B  79    21203  15356  15782    536  -2883   -236       N  
ATOM   3783  CA  LYS B  79      -5.758   7.775 -13.621  1.00138.82           C  
ANISOU 3783  CA  LYS B  79    21105  15543  16096    508  -2987   -177       C  
ATOM   3784  C   LYS B  79      -6.133   6.259 -13.697  1.00142.60           C  
ANISOU 3784  C   LYS B  79    21468  16097  16619    640  -2836   -134       C  
ATOM   3785  O   LYS B  79      -5.485   5.430 -13.039  1.00143.81           O  
ANISOU 3785  O   LYS B  79    21552  16265  16826    678  -2953    -87       O  
ATOM   3786  CB  LYS B  79      -4.905   8.093 -12.371  1.00143.21           C  
ANISOU 3786  CB  LYS B  79    21772  16038  16602    463  -3285   -163       C  
ATOM   3787  N   MET B  80      -7.137   5.913 -14.552  1.00136.53           N  
ANISOU 3787  N   MET B  80    20674  15368  15833    701  -2584   -148       N  
ATOM   3788  CA  MET B  80      -7.631   4.560 -14.902  1.00134.85           C  
ANISOU 3788  CA  MET B  80    20354  15219  15665    803  -2406   -113       C  
ATOM   3789  C   MET B  80      -7.609   3.470 -13.770  1.00138.71           C  
ANISOU 3789  C   MET B  80    20909  15704  16090    910  -2486    -67       C  
ATOM   3790  O   MET B  80      -7.258   2.313 -14.033  1.00137.67           O  
ANISOU 3790  O   MET B  80    20614  15613  16081    954  -2437    -22       O  
ATOM   3791  CB  MET B  80      -6.868   4.037 -16.141  1.00136.73           C  
ANISOU 3791  CB  MET B  80    20293  15518  16140    748  -2314    -91       C  
ATOM   3792  CG  MET B  80      -7.670   4.126 -17.428  1.00138.53           C  
ANISOU 3792  CG  MET B  80    20469  15779  16388    739  -2076   -117       C  
ATOM   3793  SD  MET B  80      -6.811   3.557 -18.926  1.00142.21           S  
ANISOU 3793  SD  MET B  80    20613  16312  17109    680  -1949    -97       S  
ATOM   3794  CE  MET B  80      -5.704   4.919 -19.220  1.00140.12           C  
ANISOU 3794  CE  MET B  80    20267  16031  16941    511  -2094   -112       C  
ATOM   3795  N   LYS B  81      -8.037   3.827 -12.543  1.00135.78           N  
ANISOU 3795  N   LYS B  81    20792  15280  15518    957  -2598    -77       N  
ATOM   3796  CA  LYS B  81      -8.070   2.878 -11.421  1.00136.09           C  
ANISOU 3796  CA  LYS B  81    20928  15309  15472   1053  -2676    -31       C  
ATOM   3797  C   LYS B  81      -9.296   1.950 -11.463  1.00137.77           C  
ANISOU 3797  C   LYS B  81    21201  15558  15587   1160  -2463     -9       C  
ATOM   3798  O   LYS B  81      -9.187   0.781 -11.091  1.00137.92           O  
ANISOU 3798  O   LYS B  81    21187  15587  15627   1224  -2465     44       O  
ATOM   3799  CB  LYS B  81      -7.952   3.601 -10.066  1.00139.96           C  
ANISOU 3799  CB  LYS B  81    21674  15725  15780   1056  -2890    -47       C  
ATOM   3800  N   THR B  82     -10.453   2.468 -11.910  1.00131.92           N  
ANISOU 3800  N   THR B  82    20549  14835  14741   1176  -2286    -46       N  
ATOM   3801  CA  THR B  82     -11.698   1.700 -12.011  1.00130.14           C  
ANISOU 3801  CA  THR B  82    20370  14654  14422   1259  -2079    -23       C  
ATOM   3802  C   THR B  82     -11.792   1.032 -13.383  1.00130.31           C  
ANISOU 3802  C   THR B  82    20167  14730  14614   1231  -1902    -11       C  
ATOM   3803  O   THR B  82     -11.248   1.560 -14.362  1.00129.58           O  
ANISOU 3803  O   THR B  82    19927  14643  14662   1153  -1892    -41       O  
ATOM   3804  CB  THR B  82     -12.932   2.602 -11.786  1.00140.98           C  
ANISOU 3804  CB  THR B  82    21941  16030  15593   1300  -1979    -64       C  
ATOM   3805  OG1 THR B  82     -12.588   3.751 -11.009  1.00143.55           O  
ANISOU 3805  OG1 THR B  82    22446  16287  15808   1285  -2150   -107       O  
ATOM   3806  CG2 THR B  82     -14.102   1.854 -11.145  1.00140.00           C  
ANISOU 3806  CG2 THR B  82    21945  15945  15305   1400  -1849    -24       C  
ATOM   3807  N   ALA B  83     -12.512  -0.113 -13.450  1.00123.85           N  
ANISOU 3807  N   ALA B  83    19338  13947  13772   1290  -1763     34       N  
ATOM   3808  CA  ALA B  83     -12.766  -0.879 -14.671  1.00121.38           C  
ANISOU 3808  CA  ALA B  83    18854  13676  13588   1273  -1589     47       C  
ATOM   3809  C   ALA B  83     -13.568  -0.036 -15.680  1.00122.59           C  
ANISOU 3809  C   ALA B  83    18987  13863  13727   1232  -1440      1       C  
ATOM   3810  O   ALA B  83     -13.240  -0.044 -16.865  1.00121.44           O  
ANISOU 3810  O   ALA B  83    18679  13734  13729   1176  -1367    -16       O  
ATOM   3811  CB  ALA B  83     -13.514  -2.165 -14.338  1.00121.74           C  
ANISOU 3811  CB  ALA B  83    18950  13738  13567   1335  -1490    106       C  
ATOM   3812  N   THR B  84     -14.569   0.740 -15.189  1.00117.77           N  
ANISOU 3812  N   THR B  84    18548  13263  12937   1267  -1402    -21       N  
ATOM   3813  CA  THR B  84     -15.441   1.638 -15.968  1.00115.67           C  
ANISOU 3813  CA  THR B  84    18297  13026  12627   1252  -1277    -62       C  
ATOM   3814  C   THR B  84     -14.666   2.653 -16.811  1.00116.49           C  
ANISOU 3814  C   THR B  84    18314  13099  12846   1165  -1332   -114       C  
ATOM   3815  O   THR B  84     -15.058   2.907 -17.949  1.00115.21           O  
ANISOU 3815  O   THR B  84    18067  12964  12742   1127  -1208   -133       O  
ATOM   3816  CB  THR B  84     -16.474   2.358 -15.070  1.00125.56           C  
ANISOU 3816  CB  THR B  84    19764  14287  13658   1329  -1257    -76       C  
ATOM   3817  OG1 THR B  84     -16.432   1.862 -13.724  1.00127.91           O  
ANISOU 3817  OG1 THR B  84    20199  14565  13835   1391  -1347    -42       O  
ATOM   3818  CG2 THR B  84     -17.885   2.254 -15.616  1.00123.97           C  
ANISOU 3818  CG2 THR B  84    19557  14161  13386   1366  -1054    -63       C  
ATOM   3819  N   ASN B  85     -13.565   3.212 -16.261  1.00112.11           N  
ANISOU 3819  N   ASN B  85    17783  12488  12325   1125  -1523   -130       N  
ATOM   3820  CA  ASN B  85     -12.719   4.208 -16.929  1.00111.38           C  
ANISOU 3820  CA  ASN B  85    17616  12364  12341   1024  -1599   -170       C  
ATOM   3821  C   ASN B  85     -11.830   3.616 -18.014  1.00113.75           C  
ANISOU 3821  C   ASN B  85    17668  12690  12860    953  -1558   -153       C  
ATOM   3822  O   ASN B  85     -11.400   4.354 -18.903  1.00113.71           O  
ANISOU 3822  O   ASN B  85    17578  12678  12946    865  -1548   -181       O  
ATOM   3823  CB  ASN B  85     -11.903   5.019 -15.925  1.00113.76           C  
ANISOU 3823  CB  ASN B  85    18035  12596  12592    994  -1825   -188       C  
ATOM   3824  CG  ASN B  85     -12.746   5.736 -14.890  1.00131.56           C  
ANISOU 3824  CG  ASN B  85    20559  14812  14615   1070  -1862   -216       C  
ATOM   3825  OD1 ASN B  85     -13.645   6.531 -15.204  1.00114.36           O  
ANISOU 3825  OD1 ASN B  85    18484  12631  12336   1095  -1766   -253       O  
ATOM   3826  ND2 ASN B  85     -12.474   5.465 -13.623  1.00126.95           N  
ANISOU 3826  ND2 ASN B  85    20102  14198  13937   1116  -2000   -197       N  
ATOM   3827  N   ILE B  86     -11.569   2.291 -17.961  1.00108.73           N  
ANISOU 3827  N   ILE B  86    16927  12081  12303    995  -1528   -107       N  
ATOM   3828  CA  ILE B  86     -10.793   1.581 -18.987  1.00107.56           C  
ANISOU 3828  CA  ILE B  86    16554  11961  12355    956  -1466    -91       C  
ATOM   3829  C   ILE B  86     -11.693   1.392 -20.225  1.00109.00           C  
ANISOU 3829  C   ILE B  86    16689  12179  12547    947  -1251   -104       C  
ATOM   3830  O   ILE B  86     -11.265   1.668 -21.352  1.00108.69           O  
ANISOU 3830  O   ILE B  86    16517  12152  12627    877  -1186   -122       O  
ATOM   3831  CB  ILE B  86     -10.170   0.270 -18.437  1.00111.12           C  
ANISOU 3831  CB  ILE B  86    16933  12412  12876   1019  -1526    -40       C  
ATOM   3832  CG1 ILE B  86      -8.953   0.594 -17.544  1.00112.91           C  
ANISOU 3832  CG1 ILE B  86    17141  12610  13151    999  -1756    -28       C  
ATOM   3833  CG2 ILE B  86      -9.772  -0.687 -19.566  1.00111.41           C  
ANISOU 3833  CG2 ILE B  86    16774  12477  13081   1019  -1400    -24       C  
ATOM   3834  CD1 ILE B  86      -8.778  -0.288 -16.366  1.00119.61           C  
ANISOU 3834  CD1 ILE B  86    18063  13437  13946   1083  -1869     18       C  
ATOM   3835  N   TYR B  87     -12.965   1.002 -19.987  1.00103.23           N  
ANISOU 3835  N   TYR B  87    16075  11467  11682   1011  -1147    -92       N  
ATOM   3836  CA  TYR B  87     -14.011   0.850 -21.001  1.00100.81           C  
ANISOU 3836  CA  TYR B  87    15751  11198  11355   1004   -961    -98       C  
ATOM   3837  C   TYR B  87     -14.361   2.204 -21.640  1.00103.13           C  
ANISOU 3837  C   TYR B  87    16082  11489  11613    951   -932   -146       C  
ATOM   3838  O   TYR B  87     -14.809   2.236 -22.787  1.00102.78           O  
ANISOU 3838  O   TYR B  87    15976  11468  11606    916   -802   -158       O  
ATOM   3839  CB  TYR B  87     -15.263   0.235 -20.383  1.00101.29           C  
ANISOU 3839  CB  TYR B  87    15930  11286  11268   1078   -885    -66       C  
ATOM   3840  CG  TYR B  87     -15.175  -1.255 -20.120  1.00103.37           C  
ANISOU 3840  CG  TYR B  87    16156  11550  11568   1116   -862    -13       C  
ATOM   3841  CD1 TYR B  87     -15.462  -2.183 -21.125  1.00104.36           C  
ANISOU 3841  CD1 TYR B  87    16190  11692  11771   1096   -728      4       C  
ATOM   3842  CD2 TYR B  87     -14.885  -1.741 -18.849  1.00104.83           C  
ANISOU 3842  CD2 TYR B  87    16426  11712  11695   1172   -976     22       C  
ATOM   3843  CE1 TYR B  87     -15.415  -3.556 -20.876  1.00104.48           C  
ANISOU 3843  CE1 TYR B  87    16196  11691  11810   1132   -711     52       C  
ATOM   3844  CE2 TYR B  87     -14.823  -3.110 -18.593  1.00105.78           C  
ANISOU 3844  CE2 TYR B  87    16531  11820  11841   1209   -960     74       C  
ATOM   3845  CZ  TYR B  87     -15.100  -4.013 -19.604  1.00109.26           C  
ANISOU 3845  CZ  TYR B  87    16882  12270  12361   1189   -826     89       C  
ATOM   3846  OH  TYR B  87     -15.062  -5.351 -19.314  1.00107.54           O  
ANISOU 3846  OH  TYR B  87    16676  12026  12159   1227   -818    140       O  
ATOM   3847  N   ILE B  88     -14.162   3.319 -20.911  1.00 98.06           N  
ANISOU 3847  N   ILE B  88    15557  10809  10892    946  -1059   -174       N  
ATOM   3848  CA  ILE B  88     -14.419   4.637 -21.484  1.00 96.91           C  
ANISOU 3848  CA  ILE B  88    15467  10643  10711    897  -1047   -219       C  
ATOM   3849  C   ILE B  88     -13.206   5.079 -22.331  1.00100.19           C  
ANISOU 3849  C   ILE B  88    15742  11035  11289    783  -1094   -234       C  
ATOM   3850  O   ILE B  88     -13.416   5.621 -23.416  1.00 99.35           O  
ANISOU 3850  O   ILE B  88    15600  10933  11216    726  -1005   -255       O  
ATOM   3851  CB  ILE B  88     -14.900   5.702 -20.450  1.00100.25           C  
ANISOU 3851  CB  ILE B  88    16105  11026  10959    947  -1143   -247       C  
ATOM   3852  CG1 ILE B  88     -16.258   5.299 -19.848  1.00 99.85           C  
ANISOU 3852  CG1 ILE B  88    16170  11020  10748   1062  -1046   -228       C  
ATOM   3853  CG2 ILE B  88     -15.009   7.090 -21.092  1.00100.31           C  
ANISOU 3853  CG2 ILE B  88    16176  10992  10944    893  -1149   -294       C  
ATOM   3854  CD1 ILE B  88     -16.572   5.949 -18.556  1.00107.15           C  
ANISOU 3854  CD1 ILE B  88    17305  11911  11498   1138  -1142   -245       C  
ATOM   3855  N   PHE B  89     -11.953   4.821 -21.863  1.00 96.46           N  
ANISOU 3855  N   PHE B  89    15183  10547  10920    748  -1228   -218       N  
ATOM   3856  CA  PHE B  89     -10.738   5.197 -22.606  1.00 95.91           C  
ANISOU 3856  CA  PHE B  89    14956  10473  11014    636  -1271   -221       C  
ATOM   3857  C   PHE B  89     -10.694   4.516 -23.979  1.00 99.43           C  
ANISOU 3857  C   PHE B  89    15232  10964  11584    611  -1096   -213       C  
ATOM   3858  O   PHE B  89     -10.364   5.158 -24.979  1.00 98.38           O  
ANISOU 3858  O   PHE B  89    15030  10830  11519    520  -1047   -229       O  
ATOM   3859  CB  PHE B  89      -9.462   4.889 -21.800  1.00 98.48           C  
ANISOU 3859  CB  PHE B  89    15195  10790  11433    618  -1445   -194       C  
ATOM   3860  CG  PHE B  89      -8.187   5.334 -22.490  1.00100.28           C  
ANISOU 3860  CG  PHE B  89    15243  11028  11832    496  -1495   -189       C  
ATOM   3861  CD1 PHE B  89      -7.564   4.520 -23.437  1.00102.32           C  
ANISOU 3861  CD1 PHE B  89    15281  11340  12257    484  -1385   -166       C  
ATOM   3862  CD2 PHE B  89      -7.613   6.567 -22.198  1.00102.76           C  
ANISOU 3862  CD2 PHE B  89    15612  11296  12136    391  -1648   -205       C  
ATOM   3863  CE1 PHE B  89      -6.407   4.944 -24.095  1.00103.74           C  
ANISOU 3863  CE1 PHE B  89    15281  11542  12592    372  -1413   -156       C  
ATOM   3864  CE2 PHE B  89      -6.442   6.980 -22.843  1.00106.27           C  
ANISOU 3864  CE2 PHE B  89    15878  11760  12741    263  -1689   -190       C  
ATOM   3865  CZ  PHE B  89      -5.844   6.163 -23.781  1.00104.08           C  
ANISOU 3865  CZ  PHE B  89    15365  11551  12632    256  -1567   -164       C  
ATOM   3866  N   SER B  90     -11.015   3.211 -24.008  1.00 96.25           N  
ANISOU 3866  N   SER B  90    14778  10593  11200    690  -1006   -186       N  
ATOM   3867  CA  SER B  90     -11.052   2.399 -25.218  1.00 95.24           C  
ANISOU 3867  CA  SER B  90    14521  10497  11168    683   -842   -179       C  
ATOM   3868  C   SER B  90     -12.131   2.913 -26.172  1.00 98.31           C  
ANISOU 3868  C   SER B  90    14978  10892  11481    656   -705   -205       C  
ATOM   3869  O   SER B  90     -11.860   3.053 -27.365  1.00 98.14           O  
ANISOU 3869  O   SER B  90    14865  10880  11542    591   -610   -217       O  
ATOM   3870  CB  SER B  90     -11.299   0.941 -24.855  1.00 98.12           C  
ANISOU 3870  CB  SER B  90    14871  10874  11536    777   -798   -145       C  
ATOM   3871  OG  SER B  90     -11.257   0.097 -25.992  1.00107.24           O  
ANISOU 3871  OG  SER B  90    15917  12046  12782    775   -650   -142       O  
ATOM   3872  N   LEU B  91     -13.333   3.237 -25.640  1.00 94.10           N  
ANISOU 3872  N   LEU B  91    14605  10358  10791    708   -698   -211       N  
ATOM   3873  CA  LEU B  91     -14.451   3.765 -26.419  1.00 93.29           C  
ANISOU 3873  CA  LEU B  91    14572  10267  10606    699   -586   -230       C  
ATOM   3874  C   LEU B  91     -14.113   5.158 -27.006  1.00 98.95           C  
ANISOU 3874  C   LEU B  91    15313  10950  11333    613   -620   -264       C  
ATOM   3875  O   LEU B  91     -14.538   5.469 -28.119  1.00 99.19           O  
ANISOU 3875  O   LEU B  91    15332  10987  11368    571   -517   -277       O  
ATOM   3876  CB  LEU B  91     -15.749   3.776 -25.570  1.00 93.02           C  
ANISOU 3876  CB  LEU B  91    14687  10251  10405    789   -577   -221       C  
ATOM   3877  CG  LEU B  91     -17.074   4.152 -26.289  1.00 97.21           C  
ANISOU 3877  CG  LEU B  91    15276  10813  10846    802   -459   -229       C  
ATOM   3878  CD1 LEU B  91     -17.559   3.041 -27.235  1.00 96.48           C  
ANISOU 3878  CD1 LEU B  91    15094  10761  10804    789   -319   -205       C  
ATOM   3879  CD2 LEU B  91     -18.166   4.501 -25.290  1.00100.16           C  
ANISOU 3879  CD2 LEU B  91    15794  11208  11055    896   -474   -223       C  
ATOM   3880  N   ALA B  92     -13.314   5.968 -26.273  1.00 96.05           N  
ANISOU 3880  N   ALA B  92    14983  10541  10969    578   -772   -276       N  
ATOM   3881  CA  ALA B  92     -12.868   7.301 -26.699  1.00 95.73           C  
ANISOU 3881  CA  ALA B  92    14979  10454  10939    481   -830   -303       C  
ATOM   3882  C   ALA B  92     -11.774   7.197 -27.774  1.00 99.88           C  
ANISOU 3882  C   ALA B  92    15324  10993  11632    370   -785   -294       C  
ATOM   3883  O   ALA B  92     -11.772   7.988 -28.717  1.00 99.64           O  
ANISOU 3883  O   ALA B  92    15302  10944  11612    288   -736   -309       O  
ATOM   3884  CB  ALA B  92     -12.368   8.105 -25.504  1.00 97.18           C  
ANISOU 3884  CB  ALA B  92    15274  10583  11067    471  -1019   -314       C  
ATOM   3885  N   LEU B  93     -10.858   6.217 -27.637  1.00 96.40           N  
ANISOU 3885  N   LEU B  93    14723  10587  11318    375   -795   -267       N  
ATOM   3886  CA  LEU B  93      -9.770   5.982 -28.585  1.00 96.37           C  
ANISOU 3886  CA  LEU B  93    14527  10611  11478    292   -739   -254       C  
ATOM   3887  C   LEU B  93     -10.347   5.553 -29.933  1.00 99.85           C  
ANISOU 3887  C   LEU B  93    14933  11076  11931    290   -545   -261       C  
ATOM   3888  O   LEU B  93      -9.905   6.059 -30.975  1.00100.14           O  
ANISOU 3888  O   LEU B  93    14904  11114  12030    194   -478   -266       O  
ATOM   3889  CB  LEU B  93      -8.789   4.927 -28.015  1.00 97.08           C  
ANISOU 3889  CB  LEU B  93    14465  10734  11687    337   -795   -222       C  
ATOM   3890  CG  LEU B  93      -7.575   4.512 -28.873  1.00102.03           C  
ANISOU 3890  CG  LEU B  93    14864  11406  12496    282   -732   -202       C  
ATOM   3891  CD1 LEU B  93      -6.808   5.724 -29.432  1.00102.86           C  
ANISOU 3891  CD1 LEU B  93    14914  11506  12662    131   -768   -204       C  
ATOM   3892  CD2 LEU B  93      -6.655   3.571 -28.106  1.00103.26           C  
ANISOU 3892  CD2 LEU B  93    14887  11590  12757    348   -819   -168       C  
ATOM   3893  N   ALA B  94     -11.362   4.645 -29.892  1.00 94.71           N  
ANISOU 3893  N   ALA B  94    14337  10441  11209    387   -459   -259       N  
ATOM   3894  CA  ALA B  94     -12.098   4.113 -31.042  1.00 92.65           C  
ANISOU 3894  CA  ALA B  94    14071  10196  10934    393   -291   -264       C  
ATOM   3895  C   ALA B  94     -12.856   5.235 -31.766  1.00 94.59           C  
ANISOU 3895  C   ALA B  94    14426  10422  11093    337   -251   -287       C  
ATOM   3896  O   ALA B  94     -12.847   5.277 -32.994  1.00 94.56           O  
ANISOU 3896  O   ALA B  94    14385  10422  11122    280   -139   -294       O  
ATOM   3897  CB  ALA B  94     -13.060   3.028 -30.589  1.00 92.45           C  
ANISOU 3897  CB  ALA B  94    14101  10187  10837    495   -249   -250       C  
ATOM   3898  N   GLY B  95     -13.444   6.151 -30.998  1.00 89.60           N  
ANISOU 3898  N   GLY B  95    13934   9763  10348    358   -347   -299       N  
ATOM   3899  CA  GLY B  95     -14.166   7.313 -31.508  1.00 88.72           C  
ANISOU 3899  CA  GLY B  95    13946   9620  10143    325   -335   -320       C  
ATOM   3900  C   GLY B  95     -13.286   8.348 -32.187  1.00 92.44           C  
ANISOU 3900  C   GLY B  95    14395  10052  10675    199   -361   -330       C  
ATOM   3901  O   GLY B  95     -13.703   8.949 -33.180  1.00 91.60           O  
ANISOU 3901  O   GLY B  95    14339   9928  10536    150   -292   -340       O  
ATOM   3902  N   ALA B  96     -12.069   8.579 -31.655  1.00 89.92           N  
ANISOU 3902  N   ALA B  96    14002   9721  10444    139   -469   -322       N  
ATOM   3903  CA  ALA B  96     -11.102   9.518 -32.238  1.00 90.53           C  
ANISOU 3903  CA  ALA B  96    14037   9768  10593     -3   -501   -321       C  
ATOM   3904  C   ALA B  96     -10.546   8.939 -33.564  1.00 95.56           C  
ANISOU 3904  C   ALA B  96    14515  10449  11345    -66   -347   -306       C  
ATOM   3905  O   ALA B  96     -10.321   9.689 -34.519  1.00 94.01           O  
ANISOU 3905  O   ALA B  96    14326  10231  11160   -172   -298   -307       O  
ATOM   3906  CB  ALA B  96      -9.977   9.812 -31.253  1.00 92.13           C  
ANISOU 3906  CB  ALA B  96    14187   9956  10862    -53   -666   -308       C  
ATOM   3907  N   LEU B  97     -10.370   7.600 -33.633  1.00 94.24           N  
ANISOU 3907  N   LEU B  97    14221  10336  11249      5   -266   -294       N  
ATOM   3908  CA  LEU B  97      -9.909   6.961 -34.872  1.00 95.22           C  
ANISOU 3908  CA  LEU B  97    14216  10498  11467    -30   -107   -287       C  
ATOM   3909  C   LEU B  97     -11.026   6.994 -35.926  1.00 98.76           C  
ANISOU 3909  C   LEU B  97    14772  10932  11820    -25     20   -304       C  
ATOM   3910  O   LEU B  97     -10.763   7.351 -37.078  1.00 98.12           O  
ANISOU 3910  O   LEU B  97    14670  10848  11762   -111    116   -305       O  
ATOM   3911  CB  LEU B  97      -9.389   5.531 -34.635  1.00 95.58           C  
ANISOU 3911  CB  LEU B  97    14117  10590  11610     55    -63   -272       C  
ATOM   3912  CG  LEU B  97      -8.018   5.412 -33.954  1.00102.05           C  
ANISOU 3912  CG  LEU B  97    14772  11438  12562     37   -162   -247       C  
ATOM   3913  CD1 LEU B  97      -7.728   3.992 -33.594  1.00102.75           C  
ANISOU 3913  CD1 LEU B  97    14759  11560  12722    152   -132   -233       C  
ATOM   3914  CD2 LEU B  97      -6.897   5.902 -34.852  1.00105.39           C  
ANISOU 3914  CD2 LEU B  97    15050  11891  13101    -84   -104   -231       C  
ATOM   3915  N   ALA B  98     -12.282   6.701 -35.495  1.00 94.51           N  
ANISOU 3915  N   ALA B  98    14355  10388  11168     70     11   -313       N  
ATOM   3916  CA  ALA B  98     -13.487   6.719 -36.323  1.00 93.45           C  
ANISOU 3916  CA  ALA B  98    14324  10247  10934     86    104   -324       C  
ATOM   3917  C   ALA B  98     -13.714   8.075 -37.002  1.00 99.11           C  
ANISOU 3917  C   ALA B  98    15145  10921  11591      1     95   -334       C  
ATOM   3918  O   ALA B  98     -13.888   8.110 -38.220  1.00 98.92           O  
ANISOU 3918  O   ALA B  98    15133  10894  11559    -51    202   -336       O  
ATOM   3919  CB  ALA B  98     -14.703   6.335 -35.496  1.00 93.14           C  
ANISOU 3919  CB  ALA B  98    14377  10221  10791    196     68   -322       C  
ATOM   3920  N   THR B  99     -13.652   9.186 -36.232  1.00 96.78           N  
ANISOU 3920  N   THR B  99    14939  10584  11250    -15    -36   -340       N  
ATOM   3921  CA  THR B  99     -13.874  10.544 -36.751  1.00 96.72           C  
ANISOU 3921  CA  THR B  99    15057  10516  11175    -89    -66   -349       C  
ATOM   3922  C   THR B  99     -12.719  11.074 -37.587  1.00101.95           C  
ANISOU 3922  C   THR B  99    15650  11161  11927   -238    -36   -337       C  
ATOM   3923  O   THR B  99     -12.925  12.031 -38.329  1.00103.29           O  
ANISOU 3923  O   THR B  99    15923  11281  12043   -311    -26   -339       O  
ATOM   3924  CB  THR B  99     -14.264  11.553 -35.640  1.00102.65           C  
ANISOU 3924  CB  THR B  99    15958  11214  11831    -46   -216   -363       C  
ATOM   3925  OG1 THR B  99     -13.548  11.308 -34.435  1.00100.52           O  
ANISOU 3925  OG1 THR B  99    15632  10951  11610    -27   -324   -360       O  
ATOM   3926  CG2 THR B  99     -15.732  11.543 -35.348  1.00100.53           C  
ANISOU 3926  CG2 THR B  99    15812  10954  11432     82   -208   -373       C  
ATOM   3927  N   SER B 100     -11.520  10.475 -37.490  1.00 98.17           N  
ANISOU 3927  N   SER B 100    14996  10724  11582   -282    -21   -321       N  
ATOM   3928  CA  SER B 100     -10.357  10.960 -38.242  1.00 98.52           C  
ANISOU 3928  CA  SER B 100    14944  10767  11720   -429     16   -301       C  
ATOM   3929  C   SER B 100     -10.420  10.679 -39.770  1.00101.10           C  
ANISOU 3929  C   SER B 100    15247  11111  12054   -478    196   -297       C  
ATOM   3930  O   SER B 100      -9.684  11.323 -40.519  1.00101.56           O  
ANISOU 3930  O   SER B 100    15274  11160  12155   -609    237   -279       O  
ATOM   3931  CB  SER B 100      -9.056  10.443 -37.635  1.00102.14           C  
ANISOU 3931  CB  SER B 100    15207  11277  12324   -452    -27   -279       C  
ATOM   3932  OG  SER B 100      -8.875   9.060 -37.887  1.00108.60           O  
ANISOU 3932  OG  SER B 100    15886  12161  13217   -368     88   -276       O  
ATOM   3933  N   THR B 101     -11.287   9.750 -40.229  1.00 96.01           N  
ANISOU 3933  N   THR B 101    14626  10489  11362   -383    299   -312       N  
ATOM   3934  CA  THR B 101     -11.426   9.433 -41.665  1.00 95.58           C  
ANISOU 3934  CA  THR B 101    14577  10443  11295   -423    462   -312       C  
ATOM   3935  C   THR B 101     -12.353  10.432 -42.378  1.00 99.59           C  
ANISOU 3935  C   THR B 101    15270  10892  11676   -467    458   -318       C  
ATOM   3936  O   THR B 101     -12.276  10.563 -43.606  1.00 99.87           O  
ANISOU 3936  O   THR B 101    15334  10919  11695   -541    570   -312       O  
ATOM   3937  CB  THR B 101     -11.904   7.983 -41.904  1.00 99.75           C  
ANISOU 3937  CB  THR B 101    15063  11011  11827   -318    564   -324       C  
ATOM   3938  OG1 THR B 101     -13.160   7.763 -41.261  1.00 96.03           O  
ANISOU 3938  OG1 THR B 101    14696  10531  11260   -217    498   -335       O  
ATOM   3939  CG2 THR B 101     -10.898   6.938 -41.447  1.00101.69           C  
ANISOU 3939  CG2 THR B 101    15128  11307  12202   -272    592   -317       C  
ATOM   3940  N   LEU B 102     -13.221  11.144 -41.601  1.00 93.89           N  
ANISOU 3940  N   LEU B 102    14683  10129  10861   -413    331   -327       N  
ATOM   3941  CA  LEU B 102     -14.215  12.093 -42.120  1.00 91.97           C  
ANISOU 3941  CA  LEU B 102    14624   9829  10493   -421    307   -332       C  
ATOM   3942  C   LEU B 102     -13.624  13.178 -43.051  1.00 94.36           C  
ANISOU 3942  C   LEU B 102    14990  10075  10790   -570    327   -316       C  
ATOM   3943  O   LEU B 102     -14.210  13.353 -44.123  1.00 93.36           O  
ANISOU 3943  O   LEU B 102    14955   9926  10591   -592    400   -314       O  
ATOM   3944  CB  LEU B 102     -15.088  12.712 -41.012  1.00 91.33           C  
ANISOU 3944  CB  LEU B 102    14665   9716  10321   -324    168   -344       C  
ATOM   3945  CG  LEU B 102     -15.964  11.708 -40.228  1.00 95.35           C  
ANISOU 3945  CG  LEU B 102    15143  10283  10803   -177    164   -352       C  
ATOM   3946  CD1 LEU B 102     -16.654  12.366 -39.048  1.00 95.15           C  
ANISOU 3946  CD1 LEU B 102    15229  10232  10692    -81     36   -363       C  
ATOM   3947  CD2 LEU B 102     -16.982  11.005 -41.128  1.00 96.80           C  
ANISOU 3947  CD2 LEU B 102    15344  10500  10934   -134    267   -349       C  
ATOM   3948  N   PRO B 103     -12.476  13.868 -42.764  1.00 90.56           N  
ANISOU 3948  N   PRO B 103    14459   9570  10380   -684    271   -300       N  
ATOM   3949  CA  PRO B 103     -11.978  14.870 -43.737  1.00 90.50           C  
ANISOU 3949  CA  PRO B 103    14520   9508  10358   -840    302   -277       C  
ATOM   3950  C   PRO B 103     -11.851  14.309 -45.159  1.00 93.25           C  
ANISOU 3950  C   PRO B 103    14825   9890  10715   -890    484   -267       C  
ATOM   3951  O   PRO B 103     -12.242  14.973 -46.116  1.00 91.89           O  
ANISOU 3951  O   PRO B 103    14791   9665  10458   -953    520   -257       O  
ATOM   3952  CB  PRO B 103     -10.623  15.288 -43.159  1.00 93.03           C  
ANISOU 3952  CB  PRO B 103    14726   9832  10789   -957    233   -255       C  
ATOM   3953  CG  PRO B 103     -10.740  15.031 -41.705  1.00 96.77           C  
ANISOU 3953  CG  PRO B 103    15173  10316  11279   -852     99   -274       C  
ATOM   3954  CD  PRO B 103     -11.626  13.838 -41.550  1.00 91.54           C  
ANISOU 3954  CD  PRO B 103    14479   9712  10592   -688    163   -297       C  
ATOM   3955  N   PHE B 104     -11.395  13.049 -45.270  1.00 89.62           N  
ANISOU 3955  N   PHE B 104    14194   9512  10343   -845    593   -271       N  
ATOM   3956  CA  PHE B 104     -11.183  12.323 -46.524  1.00 89.75           C  
ANISOU 3956  CA  PHE B 104    14164   9566  10372   -873    775   -267       C  
ATOM   3957  C   PHE B 104     -12.494  11.935 -47.236  1.00 93.54           C  
ANISOU 3957  C   PHE B 104    14785  10026  10731   -797    823   -287       C  
ATOM   3958  O   PHE B 104     -12.612  12.117 -48.460  1.00 92.79           O  
ANISOU 3958  O   PHE B 104    14773   9907  10576   -864    922   -280       O  
ATOM   3959  CB  PHE B 104     -10.276  11.098 -46.277  1.00 91.58           C  
ANISOU 3959  CB  PHE B 104    14179   9882  10736   -827    861   -269       C  
ATOM   3960  CG  PHE B 104      -9.000  11.428 -45.530  1.00 93.96           C  
ANISOU 3960  CG  PHE B 104    14319  10216  11166   -897    797   -243       C  
ATOM   3961  CD1 PHE B 104      -7.860  11.839 -46.212  1.00 97.95           C  
ANISOU 3961  CD1 PHE B 104    14726  10747  11745  -1038    884   -208       C  
ATOM   3962  CD2 PHE B 104      -8.941  11.334 -44.143  1.00 96.10           C  
ANISOU 3962  CD2 PHE B 104    14537  10496  11482   -828    649   -249       C  
ATOM   3963  CE1 PHE B 104      -6.680  12.141 -45.525  1.00 99.99           C  
ANISOU 3963  CE1 PHE B 104    14817  11045  12128  -1113    815   -176       C  
ATOM   3964  CE2 PHE B 104      -7.763  11.649 -43.452  1.00 99.99           C  
ANISOU 3964  CE2 PHE B 104    14883  11018  12092   -901    572   -222       C  
ATOM   3965  CZ  PHE B 104      -6.641  12.048 -44.149  1.00 99.26           C  
ANISOU 3965  CZ  PHE B 104    14678  10957  12081  -1046    651   -184       C  
ATOM   3966  N   GLN B 105     -13.472  11.413 -46.459  1.00 90.03           N  
ANISOU 3966  N   GLN B 105    14366   9593  10249   -663    748   -308       N  
ATOM   3967  CA  GLN B 105     -14.799  10.998 -46.922  1.00 89.43           C  
ANISOU 3967  CA  GLN B 105    14402   9511  10067   -586    766   -320       C  
ATOM   3968  C   GLN B 105     -15.617  12.163 -47.455  1.00 96.92           C  
ANISOU 3968  C   GLN B 105    15536  10393  10895   -620    708   -311       C  
ATOM   3969  O   GLN B 105     -16.372  11.968 -48.411  1.00 97.10           O  
ANISOU 3969  O   GLN B 105    15650  10406  10836   -616    762   -311       O  
ATOM   3970  CB  GLN B 105     -15.582  10.316 -45.801  1.00 89.25           C  
ANISOU 3970  CB  GLN B 105    14348   9523  10038   -449    687   -333       C  
ATOM   3971  CG  GLN B 105     -15.153   8.902 -45.504  1.00 93.70           C  
ANISOU 3971  CG  GLN B 105    14770  10144  10689   -392    756   -341       C  
ATOM   3972  CD  GLN B 105     -15.930   8.359 -44.340  1.00 99.31           C  
ANISOU 3972  CD  GLN B 105    15467  10883  11384   -273    670   -346       C  
ATOM   3973  OE1 GLN B 105     -17.144   8.139 -44.428  1.00 94.79           O  
ANISOU 3973  OE1 GLN B 105    14974  10316  10725   -215    653   -345       O  
ATOM   3974  NE2 GLN B 105     -15.245   8.135 -43.221  1.00 77.71           N  
ANISOU 3974  NE2 GLN B 105    12627   8168   8729   -237    610   -345       N  
ATOM   3975  N   SER B 106     -15.504  13.355 -46.804  1.00 95.73           N  
ANISOU 3975  N   SER B 106    15454  10192  10728   -645    587   -304       N  
ATOM   3976  CA  SER B 106     -16.200  14.605 -47.183  1.00 96.32           C  
ANISOU 3976  CA  SER B 106    15720  10186  10689   -668    513   -295       C  
ATOM   3977  C   SER B 106     -15.532  15.347 -48.365  1.00100.77           C  
ANISOU 3977  C   SER B 106    16357  10696  11236   -825    580   -271       C  
ATOM   3978  O   SER B 106     -16.220  16.051 -49.098  1.00100.36           O  
ANISOU 3978  O   SER B 106    16471  10584  11079   -842    562   -261       O  
ATOM   3979  CB  SER B 106     -16.390  15.535 -45.980  1.00 98.41           C  
ANISOU 3979  CB  SER B 106    16054  10405  10931   -617    355   -302       C  
ATOM   3980  OG  SER B 106     -15.253  16.336 -45.717  1.00101.96           O  
ANISOU 3980  OG  SER B 106    16496  10808  11437   -738    309   -290       O  
ATOM   3981  N   ALA B 107     -14.201  15.196 -48.526  1.00 97.87           N  
ANISOU 3981  N   ALA B 107    15862  10352  10971   -937    657   -258       N  
ATOM   3982  CA  ALA B 107     -13.420  15.755 -49.630  1.00 98.64           C  
ANISOU 3982  CA  ALA B 107    15995  10418  11066  -1097    749   -228       C  
ATOM   3983  C   ALA B 107     -13.784  14.988 -50.904  1.00104.11           C  
ANISOU 3983  C   ALA B 107    16716  11135  11705  -1093    898   -232       C  
ATOM   3984  O   ALA B 107     -14.004  15.614 -51.947  1.00104.26           O  
ANISOU 3984  O   ALA B 107    16884  11098  11633  -1172    934   -212       O  
ATOM   3985  CB  ALA B 107     -11.934  15.605 -49.345  1.00100.13           C  
ANISOU 3985  CB  ALA B 107    15996  10655  11393  -1197    798   -210       C  
ATOM   3986  N   ASP B 108     -13.872  13.632 -50.796  1.00101.30           N  
ANISOU 3986  N   ASP B 108    16237  10854  11399  -1000    976   -256       N  
ATOM   3987  CA  ASP B 108     -14.233  12.701 -51.875  1.00101.69           C  
ANISOU 3987  CA  ASP B 108    16314  10925  11399   -980   1109   -268       C  
ATOM   3988  C   ASP B 108     -15.614  13.069 -52.429  1.00104.95           C  
ANISOU 3988  C   ASP B 108    16921  11286  11668   -943   1046   -268       C  
ATOM   3989  O   ASP B 108     -15.769  13.139 -53.649  1.00105.27           O  
ANISOU 3989  O   ASP B 108    17074  11298  11627  -1005   1127   -259       O  
ATOM   3990  CB  ASP B 108     -14.206  11.233 -51.364  1.00103.09           C  
ANISOU 3990  CB  ASP B 108    16344  11174  11652   -869   1157   -296       C  
ATOM   3991  CG  ASP B 108     -14.470  10.123 -52.384  1.00114.17           C  
ANISOU 3991  CG  ASP B 108    17774  12593  13013   -845   1294   -314       C  
ATOM   3992  OD1 ASP B 108     -15.503  10.182 -53.079  1.00114.41           O1-
ANISOU 3992  OD1 ASP B 108    17957  12588  12926   -838   1277   -315       O1-
ATOM   3993  OD2 ASP B 108     -13.671   9.165 -52.441  1.00122.91           O  
ANISOU 3993  OD2 ASP B 108    18752  13744  14202   -825   1408   -326       O  
ATOM   3994  N   TYR B 109     -16.603  13.317 -51.533  1.00 99.83           N  
ANISOU 3994  N   TYR B 109    16311  10632  10987   -838    902   -275       N  
ATOM   3995  CA  TYR B 109     -17.971  13.697 -51.892  1.00 99.01           C  
ANISOU 3995  CA  TYR B 109    16365  10495  10760   -781    823   -270       C  
ATOM   3996  C   TYR B 109     -17.942  14.989 -52.728  1.00103.93           C  
ANISOU 3996  C   TYR B 109    17162  11029  11296   -880    800   -244       C  
ATOM   3997  O   TYR B 109     -18.515  15.042 -53.823  1.00104.47           O  
ANISOU 3997  O   TYR B 109    17358  11070  11267   -907    832   -233       O  
ATOM   3998  CB  TYR B 109     -18.851  13.855 -50.619  1.00 99.52           C  
ANISOU 3998  CB  TYR B 109    16415  10578  10819   -647    682   -278       C  
ATOM   3999  CG  TYR B 109     -20.174  14.546 -50.873  1.00101.27           C  
ANISOU 3999  CG  TYR B 109    16791  10766  10922   -582    585   -265       C  
ATOM   4000  CD1 TYR B 109     -21.191  13.909 -51.573  1.00102.89           C  
ANISOU 4000  CD1 TYR B 109    17031  11001  11060   -541    604   -260       C  
ATOM   4001  CD2 TYR B 109     -20.388  15.860 -50.462  1.00102.71           C  
ANISOU 4001  CD2 TYR B 109    17088  10880  11056   -564    472   -256       C  
ATOM   4002  CE1 TYR B 109     -22.391  14.557 -51.858  1.00105.04           C  
ANISOU 4002  CE1 TYR B 109    17429  11251  11229   -480    510   -241       C  
ATOM   4003  CE2 TYR B 109     -21.583  16.522 -50.746  1.00103.89           C  
ANISOU 4003  CE2 TYR B 109    17378  10997  11097   -490    385   -242       C  
ATOM   4004  CZ  TYR B 109     -22.585  15.864 -51.441  1.00113.42           C  
ANISOU 4004  CZ  TYR B 109    18597  12250  12247   -446    405   -232       C  
ATOM   4005  OH  TYR B 109     -23.772  16.492 -51.735  1.00115.95           O  
ANISOU 4005  OH  TYR B 109    19037  12550  12468   -367    314   -212       O  
ATOM   4006  N   LEU B 110     -17.228  16.008 -52.214  1.00 99.75           N  
ANISOU 4006  N   LEU B 110    16646  10453  10801   -944    742   -231       N  
ATOM   4007  CA  LEU B 110     -17.068  17.311 -52.845  1.00 99.51           C  
ANISOU 4007  CA  LEU B 110    16787  10326  10697  -1050    707   -202       C  
ATOM   4008  C   LEU B 110     -16.414  17.241 -54.229  1.00105.92           C  
ANISOU 4008  C   LEU B 110    17641  11124  11481  -1192    855   -179       C  
ATOM   4009  O   LEU B 110     -16.939  17.824 -55.173  1.00106.13           O  
ANISOU 4009  O   LEU B 110    17848  11085  11392  -1231    847   -159       O  
ATOM   4010  CB  LEU B 110     -16.295  18.265 -51.923  1.00 99.01           C  
ANISOU 4010  CB  LEU B 110    16713  10215  10689  -1106    616   -194       C  
ATOM   4011  CG  LEU B 110     -17.028  18.840 -50.706  1.00100.97           C  
ANISOU 4011  CG  LEU B 110    17019  10432  10913   -980    447   -211       C  
ATOM   4012  CD1 LEU B 110     -16.125  19.808 -49.954  1.00101.27           C  
ANISOU 4012  CD1 LEU B 110    17076  10406  10997  -1068    360   -202       C  
ATOM   4013  CD2 LEU B 110     -18.347  19.526 -51.091  1.00 99.81           C  
ANISOU 4013  CD2 LEU B 110    17074  10221  10630   -893    361   -205       C  
ATOM   4014  N   MET B 111     -15.311  16.495 -54.354  1.00103.77           N  
ANISOU 4014  N   MET B 111    17205  10915  11308  -1256    992   -182       N  
ATOM   4015  CA  MET B 111     -14.542  16.367 -55.590  1.00105.22           C  
ANISOU 4015  CA  MET B 111    17404  11101  11475  -1385   1158   -161       C  
ATOM   4016  C   MET B 111     -15.041  15.326 -56.596  1.00109.25           C  
ANISOU 4016  C   MET B 111    17952  11641  11919  -1344   1275   -180       C  
ATOM   4017  O   MET B 111     -14.636  15.379 -57.762  1.00109.56           O  
ANISOU 4017  O   MET B 111    18068  11660  11899  -1444   1402   -162       O  
ATOM   4018  CB  MET B 111     -13.082  16.094 -55.256  1.00108.72           C  
ANISOU 4018  CB  MET B 111    17642  11606  12059  -1465   1257   -152       C  
ATOM   4019  CG  MET B 111     -12.362  17.306 -54.768  1.00113.85           C  
ANISOU 4019  CG  MET B 111    18300  12209  12748  -1584   1174   -116       C  
ATOM   4020  SD  MET B 111     -10.672  16.887 -54.343  1.00119.99           S  
ANISOU 4020  SD  MET B 111    18801  13084  13708  -1674   1280    -98       S  
ATOM   4021  CE  MET B 111     -10.831  16.719 -52.630  1.00116.16           C  
ANISOU 4021  CE  MET B 111    18199  12621  13315  -1554   1104   -127       C  
ATOM   4022  N   GLU B 112     -15.881  14.368 -56.148  1.00105.44           N  
ANISOU 4022  N   GLU B 112    17420  11202  11442  -1205   1235   -214       N  
ATOM   4023  CA  GLU B 112     -16.429  13.263 -56.962  1.00105.00           C  
ANISOU 4023  CA  GLU B 112    17400  11169  11325  -1161   1322   -236       C  
ATOM   4024  C   GLU B 112     -15.336  12.318 -57.499  1.00109.65           C  
ANISOU 4024  C   GLU B 112    17880  11805  11975  -1203   1518   -250       C  
ATOM   4025  O   GLU B 112     -15.543  11.647 -58.511  1.00109.36           O  
ANISOU 4025  O   GLU B 112    17927  11761  11862  -1210   1620   -263       O  
ATOM   4026  CB  GLU B 112     -17.347  13.776 -58.089  1.00106.56           C  
ANISOU 4026  CB  GLU B 112    17826  11298  11363  -1197   1290   -217       C  
ATOM   4027  CG  GLU B 112     -18.679  14.312 -57.598  1.00116.89           C  
ANISOU 4027  CG  GLU B 112    19220  12581  12610  -1104   1105   -211       C  
ATOM   4028  CD  GLU B 112     -19.538  14.983 -58.651  1.00136.91           C  
ANISOU 4028  CD  GLU B 112    21978  15047  14995  -1135   1051   -184       C  
ATOM   4029  OE1 GLU B 112     -19.050  15.936 -59.305  1.00131.43           O  
ANISOU 4029  OE1 GLU B 112    21407  14284  14247  -1245   1077   -155       O  
ATOM   4030  OE2 GLU B 112     -20.708  14.563 -58.813  1.00127.40           O1-
ANISOU 4030  OE2 GLU B 112    20822  13858  13727  -1055    977   -188       O1-
ATOM   4031  N   THR B 113     -14.175  12.268 -56.805  1.00107.24           N  
ANISOU 4031  N   THR B 113    17391  11548  11807  -1225   1566   -246       N  
ATOM   4032  CA  THR B 113     -12.986  11.461 -57.126  1.00108.32           C  
ANISOU 4032  CA  THR B 113    17382  11744  12029  -1248   1750   -254       C  
ATOM   4033  C   THR B 113     -12.150  11.250 -55.837  1.00111.25           C  
ANISOU 4033  C   THR B 113    17522  12180  12567  -1207   1713   -256       C  
ATOM   4034  O   THR B 113     -12.209  12.095 -54.931  1.00110.46           O  
ANISOU 4034  O   THR B 113    17404  12064  12503  -1221   1566   -239       O  
ATOM   4035  CB  THR B 113     -12.148  12.206 -58.205  1.00123.04           C  
ANISOU 4035  CB  THR B 113    19311  13587  13852  -1401   1880   -217       C  
ATOM   4036  OG1 THR B 113     -12.959  12.430 -59.354  1.00129.58           O  
ANISOU 4036  OG1 THR B 113    20371  14348  14515  -1436   1896   -214       O  
ATOM   4037  CG2 THR B 113     -10.896  11.450 -58.641  1.00123.19           C  
ANISOU 4037  CG2 THR B 113    19178  13677  13952  -1423   2092   -220       C  
ATOM   4038  N   TRP B 114     -11.375  10.129 -55.761  1.00106.25           N  
ANISOU 4038  N   TRP B 114    16726  11614  12031  -1151   1840   -275       N  
ATOM   4039  CA  TRP B 114     -10.455   9.883 -54.646  1.00104.88           C  
ANISOU 4039  CA  TRP B 114    16325  11507  12019  -1116   1814   -271       C  
ATOM   4040  C   TRP B 114      -9.073  10.479 -55.021  1.00110.82           C  
ANISOU 4040  C   TRP B 114    16961  12298  12848  -1247   1926   -229       C  
ATOM   4041  O   TRP B 114      -8.366   9.931 -55.880  1.00112.00           O  
ANISOU 4041  O   TRP B 114    17059  12487  13009  -1263   2118   -229       O  
ATOM   4042  CB  TRP B 114     -10.373   8.399 -54.231  1.00102.09           C  
ANISOU 4042  CB  TRP B 114    15851  11202  11737   -975   1867   -308       C  
ATOM   4043  CG  TRP B 114      -9.440   8.154 -53.073  1.00102.79           C  
ANISOU 4043  CG  TRP B 114    15710  11357  11990   -933   1827   -299       C  
ATOM   4044  CD1 TRP B 114      -8.140   7.754 -53.147  1.00106.90           C  
ANISOU 4044  CD1 TRP B 114    16039  11947  12630   -940   1955   -286       C  
ATOM   4045  CD2 TRP B 114      -9.715   8.361 -51.671  1.00101.43           C  
ANISOU 4045  CD2 TRP B 114    15477  11189  11874   -879   1642   -298       C  
ATOM   4046  NE1 TRP B 114      -7.598   7.656 -51.884  1.00106.03           N  
ANISOU 4046  NE1 TRP B 114    15750  11884  12653   -895   1849   -276       N  
ATOM   4047  CE2 TRP B 114      -8.538   8.034 -50.961  1.00105.84           C  
ANISOU 4047  CE2 TRP B 114    15812  11816  12587   -861   1657   -284       C  
ATOM   4048  CE3 TRP B 114     -10.839   8.797 -50.947  1.00100.98           C  
ANISOU 4048  CE3 TRP B 114    15533  11087  11749   -840   1468   -305       C  
ATOM   4049  CZ2 TRP B 114      -8.450   8.134 -49.565  1.00104.38           C  
ANISOU 4049  CZ2 TRP B 114    15530  11647  12481   -814   1495   -279       C  
ATOM   4050  CZ3 TRP B 114     -10.754   8.881 -49.564  1.00101.65           C  
ANISOU 4050  CZ3 TRP B 114    15523  11191  11909   -786   1324   -303       C  
ATOM   4051  CH2 TRP B 114      -9.572   8.551 -48.888  1.00102.99           C  
ANISOU 4051  CH2 TRP B 114    15488  11420  12223   -777   1334   -291       C  
ATOM   4052  N   PRO B 115      -8.701  11.626 -54.406  1.00106.81           N  
ANISOU 4052  N   PRO B 115    16421  11778  12385  -1345   1808   -192       N  
ATOM   4053  CA  PRO B 115      -7.430  12.277 -54.755  1.00108.22           C  
ANISOU 4053  CA  PRO B 115    16489  11995  12634  -1496   1900   -142       C  
ATOM   4054  C   PRO B 115      -6.261  12.018 -53.786  1.00111.77           C  
ANISOU 4054  C   PRO B 115    16664  12535  13269  -1491   1885   -123       C  
ATOM   4055  O   PRO B 115      -5.279  12.772 -53.825  1.00113.61           O  
ANISOU 4055  O   PRO B 115    16796  12799  13571  -1635   1905    -71       O  
ATOM   4056  CB  PRO B 115      -7.820  13.755 -54.715  1.00110.31           C  
ANISOU 4056  CB  PRO B 115    16922  12171  12820  -1621   1759   -109       C  
ATOM   4057  CG  PRO B 115      -8.855  13.824 -53.589  1.00113.40           C  
ANISOU 4057  CG  PRO B 115    17382  12517  13189  -1505   1549   -142       C  
ATOM   4058  CD  PRO B 115      -9.442  12.435 -53.415  1.00107.66           C  
ANISOU 4058  CD  PRO B 115    16610  11830  12467  -1332   1588   -192       C  
ATOM   4059  N   PHE B 116      -6.361  10.999 -52.903  1.00105.07           N  
ANISOU 4059  N   PHE B 116    15696  11728  12498  -1336   1838   -158       N  
ATOM   4060  CA  PHE B 116      -5.316  10.727 -51.908  1.00104.27           C  
ANISOU 4060  CA  PHE B 116    15340  11709  12569  -1316   1797   -140       C  
ATOM   4061  C   PHE B 116      -4.527   9.425 -52.160  1.00109.19           C  
ANISOU 4061  C   PHE B 116    15771  12425  13292  -1211   1973   -151       C  
ATOM   4062  O   PHE B 116      -3.695   9.057 -51.322  1.00110.54           O  
ANISOU 4062  O   PHE B 116    15721  12668  13610  -1169   1937   -137       O  
ATOM   4063  CB  PHE B 116      -5.888  10.763 -50.468  1.00103.73           C  
ANISOU 4063  CB  PHE B 116    15276  11612  12524  -1231   1573   -160       C  
ATOM   4064  CG  PHE B 116      -6.828  11.910 -50.171  1.00103.32           C  
ANISOU 4064  CG  PHE B 116    15435  11461  12359  -1287   1404   -160       C  
ATOM   4065  CD1 PHE B 116      -6.346  13.201 -49.999  1.00106.55           C  
ANISOU 4065  CD1 PHE B 116    15867  11838  12779  -1445   1313   -118       C  
ATOM   4066  CD2 PHE B 116      -8.195  11.695 -50.050  1.00103.22           C  
ANISOU 4066  CD2 PHE B 116    15600  11390  12230  -1179   1332   -200       C  
ATOM   4067  CE1 PHE B 116      -7.215  14.262 -49.733  1.00106.39           C  
ANISOU 4067  CE1 PHE B 116    16060  11715  12647  -1479   1157   -122       C  
ATOM   4068  CE2 PHE B 116      -9.064  12.755 -49.773  1.00105.34           C  
ANISOU 4068  CE2 PHE B 116    16056  11573  12395  -1209   1182   -199       C  
ATOM   4069  CZ  PHE B 116      -8.567  14.033 -49.621  1.00104.15           C  
ANISOU 4069  CZ  PHE B 116    15943  11379  12251  -1351   1097   -163       C  
ATOM   4070  N   GLY B 117      -4.768   8.759 -53.299  1.00104.02           N  
ANISOU 4070  N   GLY B 117    15206  11762  12555  -1167   2155   -177       N  
ATOM   4071  CA  GLY B 117      -4.070   7.526 -53.654  1.00104.46           C  
ANISOU 4071  CA  GLY B 117    15116  11890  12685  -1053   2338   -194       C  
ATOM   4072  C   GLY B 117      -4.447   6.279 -52.863  1.00108.11           C  
ANISOU 4072  C   GLY B 117    15536  12352  13190   -864   2280   -240       C  
ATOM   4073  O   GLY B 117      -5.134   6.359 -51.838  1.00106.47           O  
ANISOU 4073  O   GLY B 117    15369  12107  12979   -821   2089   -253       O  
ATOM   4074  N   GLU B 118      -3.957   5.105 -53.327  1.00105.46           N  
ANISOU 4074  N   GLU B 118    15121  12056  12893   -745   2454   -264       N  
ATOM   4075  CA  GLU B 118      -4.238   3.778 -52.767  1.00104.24           C  
ANISOU 4075  CA  GLU B 118    14947  11891  12770   -561   2435   -308       C  
ATOM   4076  C   GLU B 118      -3.830   3.568 -51.309  1.00107.73           C  
ANISOU 4076  C   GLU B 118    15202  12377  13355   -491   2275   -292       C  
ATOM   4077  O   GLU B 118      -4.627   3.009 -50.557  1.00106.22           O  
ANISOU 4077  O   GLU B 118    15086  12137  13136   -397   2149   -320       O  
ATOM   4078  CB  GLU B 118      -3.628   2.679 -53.635  1.00106.95           C  
ANISOU 4078  CB  GLU B 118    15248  12263  13126   -454   2667   -333       C  
ATOM   4079  CG  GLU B 118      -4.375   1.368 -53.509  1.00115.52           C  
ANISOU 4079  CG  GLU B 118    16453  13281  14157   -292   2659   -391       C  
ATOM   4080  CD  GLU B 118      -3.936   0.297 -54.474  1.00135.64           C  
ANISOU 4080  CD  GLU B 118    19027  15827  16682   -183   2886   -426       C  
ATOM   4081  OE1 GLU B 118      -2.738  -0.065 -54.462  1.00136.89           O  
ANISOU 4081  OE1 GLU B 118    18974  16071  16967   -114   3011   -410       O  
ATOM   4082  OE2 GLU B 118      -4.798  -0.192 -55.236  1.00133.05           O1-
ANISOU 4082  OE2 GLU B 118    18934  15413  16207   -163   2936   -471       O1-
ATOM   4083  N   LEU B 119      -2.596   3.948 -50.924  1.00105.55           N  
ANISOU 4083  N   LEU B 119    14683  12194  13228   -537   2282   -244       N  
ATOM   4084  CA  LEU B 119      -2.085   3.793 -49.558  1.00105.55           C  
ANISOU 4084  CA  LEU B 119    14495  12240  13369   -480   2123   -223       C  
ATOM   4085  C   LEU B 119      -2.991   4.473 -48.520  1.00106.91           C  
ANISOU 4085  C   LEU B 119    14787  12348  13487   -524   1879   -225       C  
ATOM   4086  O   LEU B 119      -3.292   3.864 -47.489  1.00104.58           O  
ANISOU 4086  O   LEU B 119    14475  12039  13222   -412   1753   -240       O  
ATOM   4087  CB  LEU B 119      -0.616   4.272 -49.459  1.00108.22           C  
ANISOU 4087  CB  LEU B 119    14555  12695  13869   -560   2166   -161       C  
ATOM   4088  CG  LEU B 119       0.115   4.164 -48.100  1.00114.27           C  
ANISOU 4088  CG  LEU B 119    15095  13524  14796   -516   2000   -129       C  
ATOM   4089  CD1 LEU B 119       0.086   2.743 -47.544  1.00114.97           C  
ANISOU 4089  CD1 LEU B 119    15134  13613  14936   -297   1999   -162       C  
ATOM   4090  CD2 LEU B 119       1.554   4.599 -48.229  1.00118.63           C  
ANISOU 4090  CD2 LEU B 119    15368  14203  15505   -607   2068    -62       C  
ATOM   4091  N   LEU B 120      -3.468   5.704 -48.825  1.00104.08           N  
ANISOU 4091  N   LEU B 120    14566  11943  13035   -677   1821   -211       N  
ATOM   4092  CA  LEU B 120      -4.391   6.463 -47.967  1.00102.73           C  
ANISOU 4092  CA  LEU B 120    14535  11704  12792   -713   1607   -216       C  
ATOM   4093  C   LEU B 120      -5.824   5.940 -48.053  1.00104.73           C  
ANISOU 4093  C   LEU B 120    15007  11880  12907   -619   1579   -264       C  
ATOM   4094  O   LEU B 120      -6.600   6.147 -47.119  1.00103.10           O  
ANISOU 4094  O   LEU B 120    14879  11633  12659   -584   1412   -274       O  
ATOM   4095  CB  LEU B 120      -4.345   7.974 -48.243  1.00103.24           C  
ANISOU 4095  CB  LEU B 120    14676  11740  12811   -899   1549   -183       C  
ATOM   4096  CG  LEU B 120      -3.695   8.829 -47.162  1.00108.44           C  
ANISOU 4096  CG  LEU B 120    15221  12418  13563   -986   1371   -144       C  
ATOM   4097  CD1 LEU B 120      -3.415  10.224 -47.678  1.00109.26           C  
ANISOU 4097  CD1 LEU B 120    15388  12495  13632  -1187   1357   -104       C  
ATOM   4098  CD2 LEU B 120      -4.554   8.891 -45.907  1.00109.50           C  
ANISOU 4098  CD2 LEU B 120    15456  12496  13652   -906   1161   -169       C  
ATOM   4099  N   CYS B 121      -6.168   5.260 -49.167  1.00101.25           N  
ANISOU 4099  N   CYS B 121    14661  11420  12391   -580   1744   -292       N  
ATOM   4100  CA  CYS B 121      -7.466   4.612 -49.369  1.00 99.49           C  
ANISOU 4100  CA  CYS B 121    14627  11131  12044   -498   1732   -332       C  
ATOM   4101  C   CYS B 121      -7.521   3.382 -48.468  1.00102.46           C  
ANISOU 4101  C   CYS B 121    14929  11519  12483   -344   1687   -351       C  
ATOM   4102  O   CYS B 121      -8.560   3.114 -47.856  1.00101.37           O  
ANISOU 4102  O   CYS B 121    14896  11340  12280   -287   1574   -367       O  
ATOM   4103  CB  CYS B 121      -7.671   4.238 -50.834  1.00100.23           C  
ANISOU 4103  CB  CYS B 121    14842  11198  12042   -514   1916   -354       C  
ATOM   4104  SG  CYS B 121      -9.080   3.139 -51.133  1.00102.78           S  
ANISOU 4104  SG  CYS B 121    15367  11449  12235   -411   1913   -401       S  
ATOM   4105  N   LYS B 122      -6.387   2.647 -48.388  1.00 98.79           N  
ANISOU 4105  N   LYS B 122    14279  11112  12145   -276   1779   -345       N  
ATOM   4106  CA  LYS B 122      -6.216   1.473 -47.537  1.00 97.60           C  
ANISOU 4106  CA  LYS B 122    14042  10971  12071   -126   1741   -357       C  
ATOM   4107  C   LYS B 122      -6.310   1.900 -46.084  1.00100.46           C  
ANISOU 4107  C   LYS B 122    14346  11344  12482   -122   1530   -335       C  
ATOM   4108  O   LYS B 122      -7.002   1.238 -45.314  1.00 99.25           O  
ANISOU 4108  O   LYS B 122    14254  11158  12299    -29   1437   -348       O  
ATOM   4109  CB  LYS B 122      -4.868   0.783 -47.796  1.00100.79           C  
ANISOU 4109  CB  LYS B 122    14245  11442  12608    -54   1881   -348       C  
ATOM   4110  CG  LYS B 122      -4.845  -0.031 -49.072  1.00106.64           C  
ANISOU 4110  CG  LYS B 122    15066  12160  13293      1   2094   -382       C  
ATOM   4111  CD  LYS B 122      -3.535  -0.769 -49.258  1.00107.76           C  
ANISOU 4111  CD  LYS B 122    15005  12372  13568    102   2239   -375       C  
ATOM   4112  CE  LYS B 122      -3.533  -1.576 -50.516  1.00102.52           C  
ANISOU 4112  CE  LYS B 122    14448  11675  12831    167   2456   -415       C  
ATOM   4113  NZ  LYS B 122      -4.501  -2.693 -50.438  1.00109.82           N1+
ANISOU 4113  NZ  LYS B 122    15562  12501  13665    277   2427   -461       N1+
ATOM   4114  N   ALA B 123      -5.651   3.032 -45.724  1.00 96.22           N  
ANISOU 4114  N   ALA B 123    13707  10846  12006   -231   1452   -299       N  
ATOM   4115  CA  ALA B 123      -5.659   3.566 -44.366  1.00 95.17           C  
ANISOU 4115  CA  ALA B 123    13534  10717  11910   -241   1246   -279       C  
ATOM   4116  C   ALA B 123      -7.054   3.981 -43.936  1.00 96.35           C  
ANISOU 4116  C   ALA B 123    13890  10798  11921   -244   1124   -298       C  
ATOM   4117  O   ALA B 123      -7.452   3.611 -42.840  1.00 95.41           O  
ANISOU 4117  O   ALA B 123    13784  10668  11799   -162    999   -301       O  
ATOM   4118  CB  ALA B 123      -4.694   4.730 -44.239  1.00 97.14           C  
ANISOU 4118  CB  ALA B 123    13659  11009  12239   -379   1194   -239       C  
ATOM   4119  N   VAL B 124      -7.814   4.691 -44.813  1.00 91.79           N  
ANISOU 4119  N   VAL B 124    13473  10177  11225   -327   1167   -308       N  
ATOM   4120  CA  VAL B 124      -9.184   5.170 -44.547  1.00 89.58           C  
ANISOU 4120  CA  VAL B 124    13385   9841  10812   -325   1063   -322       C  
ATOM   4121  C   VAL B 124     -10.177   3.996 -44.394  1.00 92.63           C  
ANISOU 4121  C   VAL B 124    13851  10207  11135   -205   1075   -346       C  
ATOM   4122  O   VAL B 124     -10.866   3.921 -43.374  1.00 91.70           O  
ANISOU 4122  O   VAL B 124    13779  10080  10983   -146    951   -345       O  
ATOM   4123  CB  VAL B 124      -9.642   6.238 -45.576  1.00 92.40           C  
ANISOU 4123  CB  VAL B 124    13883  10157  11066   -442   1102   -320       C  
ATOM   4124  CG1 VAL B 124     -11.169   6.363 -45.650  1.00 90.54           C  
ANISOU 4124  CG1 VAL B 124    13841   9873  10688   -407   1047   -338       C  
ATOM   4125  CG2 VAL B 124      -9.010   7.586 -45.257  1.00 92.88           C  
ANISOU 4125  CG2 VAL B 124    13914  10214  11160   -561   1010   -293       C  
ATOM   4126  N   LEU B 125     -10.228   3.089 -45.382  1.00 88.81           N  
ANISOU 4126  N   LEU B 125    13392   9716  10635   -174   1224   -364       N  
ATOM   4127  CA  LEU B 125     -11.118   1.933 -45.340  1.00 87.66           C  
ANISOU 4127  CA  LEU B 125    13332   9544  10432    -81   1238   -383       C  
ATOM   4128  C   LEU B 125     -10.809   0.993 -44.176  1.00 91.34           C  
ANISOU 4128  C   LEU B 125    13700  10026  10978     31   1172   -377       C  
ATOM   4129  O   LEU B 125     -11.750   0.542 -43.525  1.00 89.41           O  
ANISOU 4129  O   LEU B 125    13532   9763  10675     86   1093   -377       O  
ATOM   4130  CB  LEU B 125     -11.174   1.173 -46.694  1.00 87.69           C  
ANISOU 4130  CB  LEU B 125    13406   9522  10391    -79   1407   -407       C  
ATOM   4131  CG  LEU B 125     -11.880   1.900 -47.865  1.00 91.10           C  
ANISOU 4131  CG  LEU B 125    13993   9921  10702   -177   1456   -414       C  
ATOM   4132  CD1 LEU B 125     -11.790   1.106 -49.129  1.00 91.36           C  
ANISOU 4132  CD1 LEU B 125    14095   9925  10692   -172   1621   -440       C  
ATOM   4133  CD2 LEU B 125     -13.351   2.151 -47.575  1.00 91.44           C  
ANISOU 4133  CD2 LEU B 125    14174   9937  10630   -179   1340   -411       C  
ATOM   4134  N   SER B 126      -9.514   0.716 -43.895  1.00 90.14           N  
ANISOU 4134  N   SER B 126    13378   9914  10959     63   1200   -367       N  
ATOM   4135  CA  SER B 126      -9.120  -0.171 -42.786  1.00 91.02           C  
ANISOU 4135  CA  SER B 126    13394  10038  11151    175   1128   -358       C  
ATOM   4136  C   SER B 126      -9.461   0.444 -41.420  1.00 94.95           C  
ANISOU 4136  C   SER B 126    13897  10543  11637    173    940   -338       C  
ATOM   4137  O   SER B 126     -10.049  -0.241 -40.585  1.00 93.88           O  
ANISOU 4137  O   SER B 126    13810  10389  11470    253    866   -334       O  
ATOM   4138  CB  SER B 126      -7.646  -0.567 -42.862  1.00 96.49           C  
ANISOU 4138  CB  SER B 126    13892  10779  11992    217   1200   -347       C  
ATOM   4139  OG  SER B 126      -6.790   0.553 -42.687  1.00107.99           O  
ANISOU 4139  OG  SER B 126    15223  12285  13522    122   1153   -321       O  
ATOM   4140  N   ILE B 127      -9.135   1.736 -41.212  1.00 91.45           N  
ANISOU 4140  N   ILE B 127    13424  10118  11206     79    865   -324       N  
ATOM   4141  CA  ILE B 127      -9.455   2.424 -39.965  1.00 91.14           C  
ANISOU 4141  CA  ILE B 127    13416  10074  11139     76    688   -311       C  
ATOM   4142  C   ILE B 127     -10.977   2.523 -39.777  1.00 94.23           C  
ANISOU 4142  C   ILE B 127    13987  10430  11385     98    644   -322       C  
ATOM   4143  O   ILE B 127     -11.444   2.308 -38.665  1.00 94.60           O  
ANISOU 4143  O   ILE B 127    14067  10474  11400    163    537   -314       O  
ATOM   4144  CB  ILE B 127      -8.711   3.779 -39.821  1.00 95.07           C  
ANISOU 4144  CB  ILE B 127    13858  10586  11679    -38    612   -295       C  
ATOM   4145  CG1 ILE B 127      -7.215   3.532 -39.474  1.00 97.04           C  
ANISOU 4145  CG1 ILE B 127    13893  10888  12089    -37    599   -270       C  
ATOM   4146  CG2 ILE B 127      -9.380   4.701 -38.791  1.00 94.85           C  
ANISOU 4146  CG2 ILE B 127    13944  10528  11568    -52    443   -294       C  
ATOM   4147  CD1 ILE B 127      -6.238   4.702 -39.842  1.00105.58           C  
ANISOU 4147  CD1 ILE B 127    14880  11997  13239   -182    588   -247       C  
ATOM   4148  N   ASP B 128     -11.741   2.788 -40.851  1.00 89.24           N  
ANISOU 4148  N   ASP B 128    13465   9777  10666     49    730   -336       N  
ATOM   4149  CA  ASP B 128     -13.205   2.884 -40.796  1.00 87.41           C  
ANISOU 4149  CA  ASP B 128    13384   9525  10303     68    696   -341       C  
ATOM   4150  C   ASP B 128     -13.848   1.546 -40.349  1.00 91.41           C  
ANISOU 4150  C   ASP B 128    13912  10032  10789    162    703   -337       C  
ATOM   4151  O   ASP B 128     -14.669   1.556 -39.423  1.00 91.63           O  
ANISOU 4151  O   ASP B 128    13995  10066  10754    208    612   -325       O  
ATOM   4152  CB  ASP B 128     -13.776   3.434 -42.128  1.00 88.40           C  
ANISOU 4152  CB  ASP B 128    13611   9628  10349    -10    780   -352       C  
ATOM   4153  CG  ASP B 128     -15.284   3.457 -42.282  1.00 96.03           C  
ANISOU 4153  CG  ASP B 128    14715  10584  11189      9    757   -351       C  
ATOM   4154  OD1 ASP B 128     -15.983   3.636 -41.264  1.00 96.46           O  
ANISOU 4154  OD1 ASP B 128    14801  10651  11197     62    655   -340       O  
ATOM   4155  OD2 ASP B 128     -15.766   3.303 -43.427  1.00103.10           O1-
ANISOU 4155  OD2 ASP B 128    15683  11463  12028    -30    842   -359       O1-
ATOM   4156  N   TYR B 129     -13.427   0.402 -40.939  1.00 87.51           N  
ANISOU 4156  N   TYR B 129    13376   9528  10344    194    809   -345       N  
ATOM   4157  CA  TYR B 129     -13.944  -0.927 -40.561  1.00 86.23           C  
ANISOU 4157  CA  TYR B 129    13247   9352  10165    274    814   -339       C  
ATOM   4158  C   TYR B 129     -13.468  -1.370 -39.180  1.00 91.55           C  
ANISOU 4158  C   TYR B 129    13846  10038  10900    354    715   -320       C  
ATOM   4159  O   TYR B 129     -14.283  -1.788 -38.359  1.00 92.01           O  
ANISOU 4159  O   TYR B 129    13965  10095  10900    398    647   -301       O  
ATOM   4160  CB  TYR B 129     -13.618  -1.984 -41.619  1.00 86.40           C  
ANISOU 4160  CB  TYR B 129    13276   9341  10211    289    953   -359       C  
ATOM   4161  CG  TYR B 129     -14.624  -2.024 -42.748  1.00 85.89           C  
ANISOU 4161  CG  TYR B 129    13346   9250  10040    230   1022   -372       C  
ATOM   4162  CD1 TYR B 129     -14.595  -1.076 -43.769  1.00 86.60           C  
ANISOU 4162  CD1 TYR B 129    13469   9341  10095    145   1077   -385       C  
ATOM   4163  CD2 TYR B 129     -15.596  -3.017 -42.808  1.00 86.06           C  
ANISOU 4163  CD2 TYR B 129    13466   9241   9991    251   1025   -367       C  
ATOM   4164  CE1 TYR B 129     -15.508  -1.116 -44.821  1.00 84.45           C  
ANISOU 4164  CE1 TYR B 129    13326   9041   9719     91   1129   -395       C  
ATOM   4165  CE2 TYR B 129     -16.532  -3.053 -43.844  1.00 86.62           C  
ANISOU 4165  CE2 TYR B 129    13659   9289   9963    188   1071   -375       C  
ATOM   4166  CZ  TYR B 129     -16.484  -2.095 -44.850  1.00 91.42           C  
ANISOU 4166  CZ  TYR B 129    14299   9899  10536    113   1120   -390       C  
ATOM   4167  OH  TYR B 129     -17.381  -2.127 -45.896  1.00 90.44           O  
ANISOU 4167  OH  TYR B 129    14300   9750  10311     50   1155   -396       O  
ATOM   4168  N   TYR B 130     -12.162  -1.235 -38.912  1.00 88.09           N  
ANISOU 4168  N   TYR B 130    13275   9617  10578    368    701   -318       N  
ATOM   4169  CA  TYR B 130     -11.542  -1.596 -37.642  1.00 87.93           C  
ANISOU 4169  CA  TYR B 130    13174   9609  10627    441    596   -297       C  
ATOM   4170  C   TYR B 130     -12.168  -0.866 -36.459  1.00 90.21           C  
ANISOU 4170  C   TYR B 130    13524   9908  10844    439    451   -281       C  
ATOM   4171  O   TYR B 130     -12.580  -1.528 -35.515  1.00 89.28           O  
ANISOU 4171  O   TYR B 130    13445   9783  10694    508    387   -263       O  
ATOM   4172  CB  TYR B 130     -10.025  -1.364 -37.709  1.00 90.39           C  
ANISOU 4172  CB  TYR B 130    13316   9951  11079    434    602   -293       C  
ATOM   4173  CG  TYR B 130      -9.268  -1.737 -36.457  1.00 92.54           C  
ANISOU 4173  CG  TYR B 130    13489  10238  11433    509    483   -268       C  
ATOM   4174  CD1 TYR B 130      -8.938  -3.062 -36.186  1.00 94.48           C  
ANISOU 4174  CD1 TYR B 130    13700  10467  11733    620    504   -259       C  
ATOM   4175  CD2 TYR B 130      -8.806  -0.758 -35.585  1.00 93.93           C  
ANISOU 4175  CD2 TYR B 130    13615  10439  11636    467    343   -253       C  
ATOM   4176  CE1 TYR B 130      -8.210  -3.407 -35.049  1.00 95.48           C  
ANISOU 4176  CE1 TYR B 130    13737  10605  11935    693    384   -232       C  
ATOM   4177  CE2 TYR B 130      -8.070  -1.090 -34.453  1.00 95.59           C  
ANISOU 4177  CE2 TYR B 130    13738  10662  11919    531    220   -227       C  
ATOM   4178  CZ  TYR B 130      -7.787  -2.416 -34.182  1.00101.93           C  
ANISOU 4178  CZ  TYR B 130    14502  11453  12774    646    240   -216       C  
ATOM   4179  OH  TYR B 130      -7.067  -2.723 -33.060  1.00104.04           O  
ANISOU 4179  OH  TYR B 130    14689  11731  13110    712    107   -187       O  
ATOM   4180  N   SER B 131     -12.245   0.488 -36.514  1.00 86.74           N  
ANISOU 4180  N   SER B 131    13108   9478  10372    362    403   -288       N  
ATOM   4181  CA  SER B 131     -12.817   1.342 -35.458  1.00 85.73           C  
ANISOU 4181  CA  SER B 131    13058   9352  10164    365    271   -281       C  
ATOM   4182  C   SER B 131     -14.323   1.121 -35.258  1.00 89.40           C  
ANISOU 4182  C   SER B 131    13655   9817  10498    402    276   -275       C  
ATOM   4183  O   SER B 131     -14.816   1.372 -34.167  1.00 88.47           O  
ANISOU 4183  O   SER B 131    13595   9706  10315    446    180   -263       O  
ATOM   4184  CB  SER B 131     -12.526   2.815 -35.720  1.00 88.12           C  
ANISOU 4184  CB  SER B 131    13374   9649  10459    274    229   -292       C  
ATOM   4185  OG  SER B 131     -13.196   3.286 -36.881  1.00 94.00           O  
ANISOU 4185  OG  SER B 131    14194  10382  11140    216    320   -307       O  
ATOM   4186  N   MET B 132     -15.052   0.675 -36.303  1.00 86.70           N  
ANISOU 4186  N   MET B 132    13359   9470  10113    382    386   -281       N  
ATOM   4187  CA  MET B 132     -16.486   0.403 -36.191  1.00 85.97           C  
ANISOU 4187  CA  MET B 132    13367   9389   9907    405    392   -267       C  
ATOM   4188  C   MET B 132     -16.690  -0.742 -35.193  1.00 92.37           C  
ANISOU 4188  C   MET B 132    14178  10205  10714    481    358   -239       C  
ATOM   4189  O   MET B 132     -17.499  -0.613 -34.285  1.00 92.16           O  
ANISOU 4189  O   MET B 132    14208  10202  10606    518    298   -218       O  
ATOM   4190  CB  MET B 132     -17.118   0.069 -37.562  1.00 87.55           C  
ANISOU 4190  CB  MET B 132    13613   9581  10073    356    504   -276       C  
ATOM   4191  CG  MET B 132     -18.640  -0.013 -37.508  1.00 90.39           C  
ANISOU 4191  CG  MET B 132    14060   9967  10318    363    498   -254       C  
ATOM   4192  SD  MET B 132     -19.431  -0.834 -38.908  1.00 94.94           S  
ANISOU 4192  SD  MET B 132    14693  10529  10853    308    603   -254       S  
ATOM   4193  CE  MET B 132     -21.136  -0.658 -38.451  1.00 91.16           C  
ANISOU 4193  CE  MET B 132    14277  10108  10254    321    556   -215       C  
ATOM   4194  N   PHE B 133     -15.920  -1.832 -35.336  1.00 91.26           N  
ANISOU 4194  N   PHE B 133    13977  10039  10659    508    399   -238       N  
ATOM   4195  CA  PHE B 133     -15.997  -3.007 -34.462  1.00 91.39           C  
ANISOU 4195  CA  PHE B 133    14003  10044  10678    578    367   -209       C  
ATOM   4196  C   PHE B 133     -15.437  -2.764 -33.056  1.00 95.35           C  
ANISOU 4196  C   PHE B 133    14474  10555  11199    633    242   -193       C  
ATOM   4197  O   PHE B 133     -16.070  -3.196 -32.100  1.00 95.04           O  
ANISOU 4197  O   PHE B 133    14496  10523  11093    677    192   -162       O  
ATOM   4198  CB  PHE B 133     -15.350  -4.228 -35.129  1.00 93.51           C  
ANISOU 4198  CB  PHE B 133    14236  10269  11026    602    450   -216       C  
ATOM   4199  CG  PHE B 133     -16.174  -4.767 -36.283  1.00 94.65           C  
ANISOU 4199  CG  PHE B 133    14456  10390  11115    555    554   -225       C  
ATOM   4200  CD1 PHE B 133     -16.014  -4.263 -37.571  1.00 97.04           C  
ANISOU 4200  CD1 PHE B 133    14754  10688  11427    493    641   -258       C  
ATOM   4201  CD2 PHE B 133     -17.110  -5.781 -36.078  1.00 95.95           C  
ANISOU 4201  CD2 PHE B 133    14708  10536  11214    563    560   -196       C  
ATOM   4202  CE1 PHE B 133     -16.770  -4.764 -38.633  1.00 97.51           C  
ANISOU 4202  CE1 PHE B 133    14900  10721  11427    447    725   -266       C  
ATOM   4203  CE2 PHE B 133     -17.868  -6.279 -37.138  1.00 98.11           C  
ANISOU 4203  CE2 PHE B 133    15058  10785  11435    507    639   -202       C  
ATOM   4204  CZ  PHE B 133     -17.693  -5.769 -38.407  1.00 96.63           C  
ANISOU 4204  CZ  PHE B 133    14871  10590  11254    452    717   -239       C  
ATOM   4205  N   THR B 134     -14.296  -2.047 -32.919  1.00 92.20           N  
ANISOU 4205  N   THR B 134    13989  10159  10884    622    189   -209       N  
ATOM   4206  CA  THR B 134     -13.707  -1.770 -31.606  1.00 93.06           C  
ANISOU 4206  CA  THR B 134    14076  10273  11011    664     53   -193       C  
ATOM   4207  C   THR B 134     -14.634  -0.894 -30.758  1.00 97.69           C  
ANISOU 4207  C   THR B 134    14772  10876  11471    667    -25   -188       C  
ATOM   4208  O   THR B 134     -14.747  -1.120 -29.557  1.00 97.12           O  
ANISOU 4208  O   THR B 134    14744  10804  11354    724   -114   -165       O  
ATOM   4209  CB  THR B 134     -12.267  -1.219 -31.683  1.00101.92           C  
ANISOU 4209  CB  THR B 134    15069  11398  12257    637      4   -205       C  
ATOM   4210  OG1 THR B 134     -12.252   0.097 -32.229  1.00101.99           O  
ANISOU 4210  OG1 THR B 134    15085  11416  12251    550      6   -228       O  
ATOM   4211  CG2 THR B 134     -11.318  -2.132 -32.433  1.00100.87           C  
ANISOU 4211  CG2 THR B 134    14816  11259  12251    660     90   -207       C  
ATOM   4212  N   SER B 135     -15.324   0.062 -31.397  1.00 94.65           N  
ANISOU 4212  N   SER B 135    14440  10503  11021    614     13   -208       N  
ATOM   4213  CA  SER B 135     -16.286   0.966 -30.773  1.00 94.45           C  
ANISOU 4213  CA  SER B 135    14524  10494  10870    630    -39   -209       C  
ATOM   4214  C   SER B 135     -17.493   0.173 -30.281  1.00 97.78           C  
ANISOU 4214  C   SER B 135    15013  10943  11194    685     -7   -175       C  
ATOM   4215  O   SER B 135     -17.778   0.177 -29.076  1.00 98.62           O  
ANISOU 4215  O   SER B 135    15179  11062  11230    743    -79   -156       O  
ATOM   4216  CB  SER B 135     -16.742   2.029 -31.775  1.00 98.31           C  
ANISOU 4216  CB  SER B 135    15047  10982  11322    569      9   -234       C  
ATOM   4217  OG  SER B 135     -17.753   2.874 -31.249  1.00111.25           O  
ANISOU 4217  OG  SER B 135    16795  12638  12837    603    -29   -235       O  
ATOM   4218  N   ILE B 136     -18.183  -0.521 -31.218  1.00 91.65           N  
ANISOU 4218  N   ILE B 136    14233  10178  10411    658    101   -166       N  
ATOM   4219  CA  ILE B 136     -19.397  -1.300 -30.974  1.00 90.08           C  
ANISOU 4219  CA  ILE B 136    14085  10013  10126    681    143   -127       C  
ATOM   4220  C   ILE B 136     -19.174  -2.407 -29.914  1.00 95.59           C  
ANISOU 4220  C   ILE B 136    14792  10700  10829    735    102    -90       C  
ATOM   4221  O   ILE B 136     -19.988  -2.530 -28.987  1.00 95.16           O  
ANISOU 4221  O   ILE B 136    14797  10681  10678    775     79    -54       O  
ATOM   4222  CB  ILE B 136     -19.991  -1.811 -32.311  1.00 91.35           C  
ANISOU 4222  CB  ILE B 136    14239  10176  10293    621    249   -126       C  
ATOM   4223  CG1 ILE B 136     -20.615  -0.628 -33.094  1.00 89.85           C  
ANISOU 4223  CG1 ILE B 136    14075  10011  10053    583    273   -148       C  
ATOM   4224  CG2 ILE B 136     -21.026  -2.902 -32.076  1.00 91.20           C  
ANISOU 4224  CG2 ILE B 136    14257  10182  10213    625    284    -78       C  
ATOM   4225  CD1 ILE B 136     -20.766  -0.813 -34.570  1.00 88.23           C  
ANISOU 4225  CD1 ILE B 136    13861   9790   9873    512    359   -163       C  
ATOM   4226  N   PHE B 137     -18.051  -3.137 -29.996  1.00 93.06           N  
ANISOU 4226  N   PHE B 137    14411  10332  10614    744     90    -95       N  
ATOM   4227  CA  PHE B 137     -17.778  -4.187 -29.017  1.00 93.49           C  
ANISOU 4227  CA  PHE B 137    14483  10364  10676    801     42    -59       C  
ATOM   4228  C   PHE B 137     -17.360  -3.643 -27.651  1.00 97.76           C  
ANISOU 4228  C   PHE B 137    15050  10911  11185    855    -82    -51       C  
ATOM   4229  O   PHE B 137     -17.779  -4.229 -26.654  1.00 98.77           O  
ANISOU 4229  O   PHE B 137    15243  11043  11242    899   -118    -10       O  
ATOM   4230  CB  PHE B 137     -16.812  -5.244 -29.551  1.00 95.84           C  
ANISOU 4230  CB  PHE B 137    14718  10607  11091    813     73    -64       C  
ATOM   4231  CG  PHE B 137     -17.582  -6.143 -30.480  1.00 97.59           C  
ANISOU 4231  CG  PHE B 137    14978  10812  11291    774    180    -53       C  
ATOM   4232  CD1 PHE B 137     -18.469  -7.096 -29.977  1.00102.03           C  
ANISOU 4232  CD1 PHE B 137    15620  11369  11777    778    186     -4       C  
ATOM   4233  CD2 PHE B 137     -17.513  -5.968 -31.857  1.00 99.96           C  
ANISOU 4233  CD2 PHE B 137    15248  11102  11631    719    270    -90       C  
ATOM   4234  CE1 PHE B 137     -19.242  -7.878 -30.840  1.00103.55           C  
ANISOU 4234  CE1 PHE B 137    15858  11544  11943    723    271      9       C  
ATOM   4235  CE2 PHE B 137     -18.265  -6.768 -32.724  1.00103.22           C  
ANISOU 4235  CE2 PHE B 137    15714  11493  12011    674    355    -82       C  
ATOM   4236  CZ  PHE B 137     -19.126  -7.715 -32.212  1.00102.20           C  
ANISOU 4236  CZ  PHE B 137    15662  11357  11813    672    350    -33       C  
ATOM   4237  N   THR B 138     -16.623  -2.504 -27.582  1.00 92.66           N  
ANISOU 4237  N   THR B 138    14369  10262  10574    843   -151    -87       N  
ATOM   4238  CA  THR B 138     -16.266  -1.882 -26.294  1.00 91.99           C  
ANISOU 4238  CA  THR B 138    14332  10175  10444    884   -283    -84       C  
ATOM   4239  C   THR B 138     -17.560  -1.438 -25.597  1.00 94.97           C  
ANISOU 4239  C   THR B 138    14832  10592  10661    915   -277    -68       C  
ATOM   4240  O   THR B 138     -17.705  -1.639 -24.400  1.00 94.38           O  
ANISOU 4240  O   THR B 138    14831  10519  10510    971   -345    -41       O  
ATOM   4241  CB  THR B 138     -15.266  -0.734 -26.500  1.00 93.36           C  
ANISOU 4241  CB  THR B 138    14452  10333  10687    842   -356   -124       C  
ATOM   4242  OG1 THR B 138     -14.050  -1.269 -27.026  1.00 94.70           O  
ANISOU 4242  OG1 THR B 138    14490  10483  11009    826   -355   -127       O  
ATOM   4243  CG2 THR B 138     -14.966   0.018 -25.233  1.00 87.57           C  
ANISOU 4243  CG2 THR B 138    13793   9588   9893    872   -503   -126       C  
ATOM   4244  N   LEU B 139     -18.513  -0.886 -26.370  1.00 91.69           N  
ANISOU 4244  N   LEU B 139    14434  10212  10193    885   -190    -81       N  
ATOM   4245  CA  LEU B 139     -19.819  -0.458 -25.881  1.00 90.93           C  
ANISOU 4245  CA  LEU B 139    14429  10168   9953    923   -162    -63       C  
ATOM   4246  C   LEU B 139     -20.638  -1.666 -25.397  1.00 94.50           C  
ANISOU 4246  C   LEU B 139    14905  10653  10346    947   -110     -3       C  
ATOM   4247  O   LEU B 139     -21.232  -1.588 -24.325  1.00 94.81           O  
ANISOU 4247  O   LEU B 139    15025  10727  10273   1004   -132     25       O  
ATOM   4248  CB  LEU B 139     -20.567   0.309 -26.984  1.00 90.12           C  
ANISOU 4248  CB  LEU B 139    14317  10095   9831    885    -84    -86       C  
ATOM   4249  CG  LEU B 139     -21.919   0.921 -26.604  1.00 94.07           C  
ANISOU 4249  CG  LEU B 139    14892  10658  10191    937    -50    -71       C  
ATOM   4250  CD1 LEU B 139     -21.749   2.183 -25.764  1.00 94.46           C  
ANISOU 4250  CD1 LEU B 139    15036  10689  10164    996   -138   -104       C  
ATOM   4251  CD2 LEU B 139     -22.725   1.222 -27.828  1.00 94.80           C  
ANISOU 4251  CD2 LEU B 139    14952  10785  10283    895     37    -76       C  
ATOM   4252  N   THR B 140     -20.657  -2.776 -26.170  1.00 90.18           N  
ANISOU 4252  N   THR B 140    14302  10094   9869    902    -41     17       N  
ATOM   4253  CA  THR B 140     -21.388  -4.001 -25.802  1.00 89.76           C  
ANISOU 4253  CA  THR B 140    14279  10059   9768    902      4     79       C  
ATOM   4254  C   THR B 140     -20.844  -4.562 -24.474  1.00 94.06           C  
ANISOU 4254  C   THR B 140    14877  10572  10288    960    -82    110       C  
ATOM   4255  O   THR B 140     -21.626  -4.863 -23.568  1.00 93.70           O  
ANISOU 4255  O   THR B 140    14902  10566  10133    988    -75    160       O  
ATOM   4256  CB  THR B 140     -21.369  -5.047 -26.954  1.00 93.15           C  
ANISOU 4256  CB  THR B 140    14660  10455  10278    837     80     86       C  
ATOM   4257  OG1 THR B 140     -21.733  -4.446 -28.203  1.00 87.24           O  
ANISOU 4257  OG1 THR B 140    13871   9726   9551    782    145     52       O  
ATOM   4258  CG2 THR B 140     -22.290  -6.217 -26.688  1.00 92.51           C  
ANISOU 4258  CG2 THR B 140    14622  10391  10136    813    127    153       C  
ATOM   4259  N   MET B 141     -19.501  -4.636 -24.356  1.00 91.24           N  
ANISOU 4259  N   MET B 141    14483  10152  10032    979   -165     83       N  
ATOM   4260  CA  MET B 141     -18.778  -5.141 -23.190  1.00 92.04           C  
ANISOU 4260  CA  MET B 141    14626  10214  10131   1035   -269    109       C  
ATOM   4261  C   MET B 141     -18.938  -4.272 -21.965  1.00 98.51           C  
ANISOU 4261  C   MET B 141    15537  11057  10836   1086   -354    109       C  
ATOM   4262  O   MET B 141     -18.954  -4.815 -20.863  1.00 99.55           O  
ANISOU 4262  O   MET B 141    15748  11177  10899   1131   -409    151       O  
ATOM   4263  CB  MET B 141     -17.301  -5.406 -23.499  1.00 94.76           C  
ANISOU 4263  CB  MET B 141    14881  10497  10627   1044   -335     82       C  
ATOM   4264  CG  MET B 141     -17.095  -6.623 -24.383  1.00 98.85           C  
ANISOU 4264  CG  MET B 141    15348  10974  11238   1026   -259     94       C  
ATOM   4265  SD  MET B 141     -17.663  -8.212 -23.671  1.00104.40           S  
ANISOU 4265  SD  MET B 141    16151  11641  11876   1054   -249    170       S  
ATOM   4266  CE  MET B 141     -18.236  -9.017 -25.168  1.00101.06           C  
ANISOU 4266  CE  MET B 141    15704  11199  11496    984   -106    166       C  
ATOM   4267  N   MET B 142     -19.086  -2.944 -22.146  1.00 96.37           N  
ANISOU 4267  N   MET B 142    15273  10810  10531   1081   -364     62       N  
ATOM   4268  CA  MET B 142     -19.337  -1.987 -21.065  1.00 98.19           C  
ANISOU 4268  CA  MET B 142    15616  11057  10635   1135   -435     52       C  
ATOM   4269  C   MET B 142     -20.660  -2.341 -20.397  1.00106.03           C  
ANISOU 4269  C   MET B 142    16696  12113  11478   1175   -359    104       C  
ATOM   4270  O   MET B 142     -20.742  -2.390 -19.166  1.00107.01           O  
ANISOU 4270  O   MET B 142    16926  12236  11494   1232   -416    130       O  
ATOM   4271  CB  MET B 142     -19.502  -0.585 -21.632  1.00100.37           C  
ANISOU 4271  CB  MET B 142    15894  11344  10898   1119   -428     -4       C  
ATOM   4272  CG  MET B 142     -18.273   0.223 -21.619  1.00104.51           C  
ANISOU 4272  CG  MET B 142    16400  11811  11500   1095   -549    -51       C  
ATOM   4273  SD  MET B 142     -18.733   1.948 -21.472  1.00108.62           S  
ANISOU 4273  SD  MET B 142    17030  12329  11910   1114   -580   -103       S  
ATOM   4274  CE  MET B 142     -18.496   2.183 -19.672  1.00106.74           C  
ANISOU 4274  CE  MET B 142    16959  12062  11537   1194   -722    -96       C  
ATOM   4275  N   CYS B 143     -21.705  -2.564 -21.229  1.00103.35           N  
ANISOU 4275  N   CYS B 143    16309  11832  11127   1140   -229    123       N  
ATOM   4276  CA  CYS B 143     -23.049  -2.941 -20.804  1.00103.39           C  
ANISOU 4276  CA  CYS B 143    16358  11918  11009   1158   -135    182       C  
ATOM   4277  C   CYS B 143     -23.021  -4.295 -20.100  1.00106.69           C  
ANISOU 4277  C   CYS B 143    16812  12319  11408   1153   -141    251       C  
ATOM   4278  O   CYS B 143     -23.703  -4.456 -19.091  1.00107.21           O  
ANISOU 4278  O   CYS B 143    16962  12430  11342   1195   -123    300       O  
ATOM   4279  CB  CYS B 143     -24.009  -2.925 -21.989  1.00103.11           C  
ANISOU 4279  CB  CYS B 143    16239  11943  10994   1104    -17    189       C  
ATOM   4280  SG  CYS B 143     -24.209  -1.291 -22.748  1.00106.61           S  
ANISOU 4280  SG  CYS B 143    16667  12408  11434   1122     -9    119       S  
ATOM   4281  N   VAL B 144     -22.188  -5.238 -20.595  1.00102.13           N  
ANISOU 4281  N   VAL B 144    16181  11670  10955   1111   -170    254       N  
ATOM   4282  CA  VAL B 144     -21.992  -6.559 -19.991  1.00102.54           C  
ANISOU 4282  CA  VAL B 144    16279  11679  11003   1109   -193    315       C  
ATOM   4283  C   VAL B 144     -21.337  -6.368 -18.597  1.00108.45           C  
ANISOU 4283  C   VAL B 144    17128  12393  11684   1185   -316    321       C  
ATOM   4284  O   VAL B 144     -21.830  -6.917 -17.604  1.00108.28           O  
ANISOU 4284  O   VAL B 144    17204  12387  11548   1208   -314    383       O  
ATOM   4285  CB  VAL B 144     -21.194  -7.508 -20.941  1.00105.10           C  
ANISOU 4285  CB  VAL B 144    16529  11925  11481   1066   -194    305       C  
ATOM   4286  CG1 VAL B 144     -20.593  -8.706 -20.211  1.00104.85           C  
ANISOU 4286  CG1 VAL B 144    16556  11819  11462   1094   -262    353       C  
ATOM   4287  CG2 VAL B 144     -22.065  -7.971 -22.098  1.00104.31           C  
ANISOU 4287  CG2 VAL B 144    16376  11853  11403    986    -73    319       C  
ATOM   4288  N   ASP B 145     -20.269  -5.534 -18.534  1.00105.13           N  
ANISOU 4288  N   ASP B 145    16688  11930  11326   1213   -425    259       N  
ATOM   4289  CA  ASP B 145     -19.538  -5.209 -17.310  1.00105.60           C  
ANISOU 4289  CA  ASP B 145    16840  11951  11332   1274   -567    255       C  
ATOM   4290  C   ASP B 145     -20.473  -4.612 -16.259  1.00110.58           C  
ANISOU 4290  C   ASP B 145    17609  12638  11769   1325   -548    274       C  
ATOM   4291  O   ASP B 145     -20.462  -5.073 -15.121  1.00112.52           O  
ANISOU 4291  O   ASP B 145    17968  12868  11916   1367   -602    319       O  
ATOM   4292  CB  ASP B 145     -18.346  -4.288 -17.612  1.00106.79           C  
ANISOU 4292  CB  ASP B 145    16928  12059  11588   1271   -679    186       C  
ATOM   4293  CG  ASP B 145     -17.620  -3.783 -16.382  1.00109.50           C  
ANISOU 4293  CG  ASP B 145    17372  12363  11869   1320   -843    177       C  
ATOM   4294  OD1 ASP B 145     -16.660  -4.464 -15.933  1.00109.86           O1-
ANISOU 4294  OD1 ASP B 145    17407  12355  11981   1338   -955    200       O1-
ATOM   4295  OD2 ASP B 145     -18.000  -2.713 -15.876  1.00110.81           O  
ANISOU 4295  OD2 ASP B 145    17635  12548  11919   1346   -866    147       O  
ATOM   4296  N   ARG B 146     -21.311  -3.640 -16.655  1.00106.02           N  
ANISOU 4296  N   ARG B 146    17025  12125  11133   1329   -464    243       N  
ATOM   4297  CA  ARG B 146     -22.293  -2.998 -15.781  1.00106.15           C  
ANISOU 4297  CA  ARG B 146    17163  12206  10965   1395   -420    255       C  
ATOM   4298  C   ARG B 146     -23.425  -3.954 -15.390  1.00109.14           C  
ANISOU 4298  C   ARG B 146    17568  12656  11244   1391   -300    342       C  
ATOM   4299  O   ARG B 146     -23.873  -3.912 -14.246  1.00109.83           O  
ANISOU 4299  O   ARG B 146    17782  12774  11175   1451   -295    377       O  
ATOM   4300  CB  ARG B 146     -22.815  -1.673 -16.384  1.00106.92           C  
ANISOU 4300  CB  ARG B 146    17241  12345  11038   1413   -368    196       C  
ATOM   4301  CG  ARG B 146     -21.898  -0.462 -16.125  1.00122.21           C  
ANISOU 4301  CG  ARG B 146    19244  14212  12979   1441   -505    120       C  
ATOM   4302  CD  ARG B 146     -21.686  -0.213 -14.628  1.00143.61           C  
ANISOU 4302  CD  ARG B 146    22133  16892  15539   1517   -606    124       C  
ATOM   4303  NE  ARG B 146     -21.221   1.142 -14.321  1.00162.35           N  
ANISOU 4303  NE  ARG B 146    24609  19212  17864   1551   -713     52       N  
ATOM   4304  CZ  ARG B 146     -21.081   1.625 -13.087  1.00182.85           C  
ANISOU 4304  CZ  ARG B 146    27390  21773  20312   1620   -808     39       C  
ATOM   4305  NH1 ARG B 146     -21.363   0.868 -12.033  1.00171.96           N1+
ANISOU 4305  NH1 ARG B 146    26109  20412  18816   1666   -802     96       N1+
ATOM   4306  NH2 ARG B 146     -20.661   2.870 -12.899  1.00170.61           N  
ANISOU 4306  NH2 ARG B 146    25943  20162  18721   1639   -911    -30       N  
ATOM   4307  N   TYR B 147     -23.838  -4.855 -16.309  1.00104.21           N  
ANISOU 4307  N   TYR B 147    16835  12055  10707   1314   -208    381       N  
ATOM   4308  CA  TYR B 147     -24.854  -5.878 -16.042  1.00104.15           C  
ANISOU 4308  CA  TYR B 147    16840  12108  10624   1280   -103    472       C  
ATOM   4309  C   TYR B 147     -24.381  -6.779 -14.893  1.00108.49           C  
ANISOU 4309  C   TYR B 147    17507  12599  11114   1299   -179    528       C  
ATOM   4310  O   TYR B 147     -25.192  -7.207 -14.069  1.00108.60           O  
ANISOU 4310  O   TYR B 147    17601  12669  10992   1308   -116    601       O  
ATOM   4311  CB  TYR B 147     -25.145  -6.729 -17.310  1.00104.39           C  
ANISOU 4311  CB  TYR B 147    16747  12140  10776   1177    -26    495       C  
ATOM   4312  CG  TYR B 147     -25.557  -8.155 -17.004  1.00106.68           C  
ANISOU 4312  CG  TYR B 147    17071  12423  11040   1117     13    588       C  
ATOM   4313  CD1 TYR B 147     -26.868  -8.463 -16.651  1.00109.44           C  
ANISOU 4313  CD1 TYR B 147    17433  12877  11272   1087    126    669       C  
ATOM   4314  CD2 TYR B 147     -24.618  -9.185 -16.987  1.00107.29           C  
ANISOU 4314  CD2 TYR B 147    17177  12388  11202   1096    -67    601       C  
ATOM   4315  CE1 TYR B 147     -27.241  -9.762 -16.312  1.00110.73           C  
ANISOU 4315  CE1 TYR B 147    17642  13029  11402   1017    157    762       C  
ATOM   4316  CE2 TYR B 147     -24.975 -10.482 -16.630  1.00108.81           C  
ANISOU 4316  CE2 TYR B 147    17429  12556  11357   1043    -42    689       C  
ATOM   4317  CZ  TYR B 147     -26.290 -10.769 -16.303  1.00116.33           C  
ANISOU 4317  CZ  TYR B 147    18401  13609  12191    994     69    771       C  
ATOM   4318  OH  TYR B 147     -26.654 -12.051 -15.973  1.00117.27           O  
ANISOU 4318  OH  TYR B 147    18586  13698  12272    923     92    864       O  
ATOM   4319  N   ILE B 148     -23.070  -7.105 -14.898  1.00104.86           N  
ANISOU 4319  N   ILE B 148    17048  12030  10763   1303   -311    498       N  
ATOM   4320  CA  ILE B 148     -22.403  -7.952 -13.915  1.00105.42           C  
ANISOU 4320  CA  ILE B 148    17224  12027  10805   1328   -414    544       C  
ATOM   4321  C   ILE B 148     -22.442  -7.288 -12.533  1.00110.85           C  
ANISOU 4321  C   ILE B 148    18067  12727  11322   1409   -478    546       C  
ATOM   4322  O   ILE B 148     -22.719  -7.979 -11.560  1.00110.96           O  
ANISOU 4322  O   ILE B 148    18200  12738  11220   1424   -480    617       O  
ATOM   4323  CB  ILE B 148     -20.982  -8.362 -14.415  1.00107.92           C  
ANISOU 4323  CB  ILE B 148    17470  12235  11299   1324   -536    507       C  
ATOM   4324  CG1 ILE B 148     -21.115  -9.497 -15.466  1.00107.16           C  
ANISOU 4324  CG1 ILE B 148    17286  12112  11319   1253   -457    536       C  
ATOM   4325  CG2 ILE B 148     -20.044  -8.792 -13.263  1.00109.62           C  
ANISOU 4325  CG2 ILE B 148    17795  12370  11484   1382   -694    533       C  
ATOM   4326  CD1 ILE B 148     -20.050  -9.573 -16.493  1.00108.97           C  
ANISOU 4326  CD1 ILE B 148    17393  12276  11735   1244   -503    479       C  
ATOM   4327  N   ALA B 149     -22.250  -5.948 -12.465  1.00107.78           N  
ANISOU 4327  N   ALA B 149    17693  12353  10907   1458   -521    471       N  
ATOM   4328  CA  ALA B 149     -22.280  -5.164 -11.223  1.00108.59           C  
ANISOU 4328  CA  ALA B 149    17962  12459  10839   1540   -585    458       C  
ATOM   4329  C   ALA B 149     -23.666  -5.174 -10.574  1.00113.06           C  
ANISOU 4329  C   ALA B 149    18616  13127  11213   1574   -438    515       C  
ATOM   4330  O   ALA B 149     -23.779  -5.442  -9.372  1.00113.80           O  
ANISOU 4330  O   ALA B 149    18868  13216  11156   1620   -465    561       O  
ATOM   4331  CB  ALA B 149     -21.842  -3.729 -11.489  1.00108.89           C  
ANISOU 4331  CB  ALA B 149    17995  12480  10899   1571   -654    362       C  
ATOM   4332  N   VAL B 150     -24.712  -4.897 -11.376  1.00108.52           N  
ANISOU 4332  N   VAL B 150    17934  12650  10646   1552   -281    518       N  
ATOM   4333  CA  VAL B 150     -26.108  -4.835 -10.941  1.00108.58           C  
ANISOU 4333  CA  VAL B 150    17977  12783  10496   1584   -120    575       C  
ATOM   4334  C   VAL B 150     -26.645  -6.218 -10.510  1.00113.60           C  
ANISOU 4334  C   VAL B 150    18633  13449  11082   1524    -48    689       C  
ATOM   4335  O   VAL B 150     -27.210  -6.319  -9.422  1.00114.45           O  
ANISOU 4335  O   VAL B 150    18866  13606  11013   1571      3    744       O  
ATOM   4336  CB  VAL B 150     -27.003  -4.129 -12.017  1.00110.86           C  
ANISOU 4336  CB  VAL B 150    18124  13168  10830   1577      7    546       C  
ATOM   4337  CG1 VAL B 150     -28.496  -4.382 -11.806  1.00111.14           C  
ANISOU 4337  CG1 VAL B 150    18130  13351  10746   1583    189    629       C  
ATOM   4338  CG2 VAL B 150     -26.725  -2.631 -12.061  1.00110.29           C  
ANISOU 4338  CG2 VAL B 150    18098  13075  10732   1663    -47    447       C  
ATOM   4339  N   CYS B 151     -26.436  -7.271 -11.322  1.00110.17           N  
ANISOU 4339  N   CYS B 151    18094  12975  10790   1421    -47    723       N  
ATOM   4340  CA  CYS B 151     -27.004  -8.597 -11.072  1.00111.25           C  
ANISOU 4340  CA  CYS B 151    18249  13131  10891   1344     23    833       C  
ATOM   4341  C   CYS B 151     -26.122  -9.576 -10.285  1.00117.24           C  
ANISOU 4341  C   CYS B 151    19135  13771  11640   1339   -101    875       C  
ATOM   4342  O   CYS B 151     -26.673 -10.317  -9.474  1.00118.19           O  
ANISOU 4342  O   CYS B 151    19354  13915  11636   1317    -50    969       O  
ATOM   4343  CB  CYS B 151     -27.475  -9.213 -12.378  1.00110.85           C  
ANISOU 4343  CB  CYS B 151    18037  13106  10975   1232    106    855       C  
ATOM   4344  SG  CYS B 151     -28.593  -8.141 -13.310  1.00114.29           S  
ANISOU 4344  SG  CYS B 151    18320  13685  11419   1236    243    820       S  
ATOM   4345  N   HIS B 152     -24.799  -9.622 -10.518  1.00113.84           N  
ANISOU 4345  N   HIS B 152    18699  13218  11337   1358   -257    815       N  
ATOM   4346  CA  HIS B 152     -23.933 -10.538  -9.763  1.00114.82           C  
ANISOU 4346  CA  HIS B 152    18940  13229  11456   1370   -387    857       C  
ATOM   4347  C   HIS B 152     -22.879  -9.719  -8.980  1.00120.59           C  
ANISOU 4347  C   HIS B 152    19765  13898  12157   1464   -556    793       C  
ATOM   4348  O   HIS B 152     -21.734  -9.660  -9.426  1.00118.92           O  
ANISOU 4348  O   HIS B 152    19486  13603  12095   1474   -685    738       O  
ATOM   4349  CB  HIS B 152     -23.269 -11.603 -10.677  1.00115.11           C  
ANISOU 4349  CB  HIS B 152    18890  13171  11677   1308   -431    864       C  
ATOM   4350  CG  HIS B 152     -24.112 -12.087 -11.826  1.00117.71           C  
ANISOU 4350  CG  HIS B 152    19096  13549  12080   1208   -289    888       C  
ATOM   4351  ND1 HIS B 152     -25.103 -13.038 -11.651  1.00120.13           N  
ANISOU 4351  ND1 HIS B 152    19447  13891  12306   1127   -185    990       N  
ATOM   4352  CD2 HIS B 152     -24.052 -11.761 -13.140  1.00117.77           C  
ANISOU 4352  CD2 HIS B 152    18949  13567  12231   1171   -248    825       C  
ATOM   4353  CE1 HIS B 152     -25.624 -13.238 -12.852  1.00118.27           C  
ANISOU 4353  CE1 HIS B 152    19082  13689  12168   1041    -93    984       C  
ATOM   4354  NE2 HIS B 152     -25.021 -12.494 -13.777  1.00117.28           N  
ANISOU 4354  NE2 HIS B 152    18840  13548  12175   1069   -127    885       N  
ATOM   4355  N   PRO B 153     -23.228  -9.049  -7.844  1.00120.63           N  
ANISOU 4355  N   PRO B 153    19922  13943  11970   1533   -561    797       N  
ATOM   4356  CA  PRO B 153     -22.226  -8.228  -7.143  1.00121.84           C  
ANISOU 4356  CA  PRO B 153    20174  14028  12091   1610   -737    732       C  
ATOM   4357  C   PRO B 153     -21.116  -9.007  -6.438  1.00129.63           C  
ANISOU 4357  C   PRO B 153    21255  14897  13100   1627   -922    764       C  
ATOM   4358  O   PRO B 153     -20.001  -8.491  -6.334  1.00130.61           O  
ANISOU 4358  O   PRO B 153    21378  14952  13296   1661  -1095    703       O  
ATOM   4359  CB  PRO B 153     -23.056  -7.394  -6.162  1.00124.21           C  
ANISOU 4359  CB  PRO B 153    20630  14403  12161   1680   -669    732       C  
ATOM   4360  CG  PRO B 153     -24.484  -7.644  -6.516  1.00128.03           C  
ANISOU 4360  CG  PRO B 153    21048  15013  12584   1645   -444    790       C  
ATOM   4361  CD  PRO B 153     -24.527  -8.981  -7.149  1.00123.09           C  
ANISOU 4361  CD  PRO B 153    20323  14364  12080   1546   -406    861       C  
ATOM   4362  N   VAL B 154     -21.404 -10.236  -5.965  1.00127.68           N  
ANISOU 4362  N   VAL B 154    21090  14627  12795   1600   -894    862       N  
ATOM   4363  CA  VAL B 154     -20.403 -11.085  -5.295  1.00129.11           C  
ANISOU 4363  CA  VAL B 154    21371  14691  12993   1624  -1070    904       C  
ATOM   4364  C   VAL B 154     -19.358 -11.525  -6.339  1.00134.66           C  
ANISOU 4364  C   VAL B 154    21900  15318  13946   1605  -1158    867       C  
ATOM   4365  O   VAL B 154     -18.155 -11.499  -6.058  1.00134.83           O  
ANISOU 4365  O   VAL B 154    21927  15258  14044   1652  -1347    842       O  
ATOM   4366  CB  VAL B 154     -21.038 -12.275  -4.509  1.00133.34           C  
ANISOU 4366  CB  VAL B 154    22061  15215  13387   1598  -1012   1025       C  
ATOM   4367  CG1 VAL B 154     -19.974 -13.179  -3.892  1.00134.16           C  
ANISOU 4367  CG1 VAL B 154    22268  15187  13521   1630  -1204   1069       C  
ATOM   4368  CG2 VAL B 154     -22.002 -11.777  -3.432  1.00133.82           C  
ANISOU 4368  CG2 VAL B 154    22293  15359  13193   1627   -919   1061       C  
ATOM   4369  N   LYS B 155     -19.833 -11.857  -7.560  1.00131.86           N  
ANISOU 4369  N   LYS B 155    21387  14999  13715   1539  -1019    861       N  
ATOM   4370  CA  LYS B 155     -19.005 -12.250  -8.705  1.00131.46           C  
ANISOU 4370  CA  LYS B 155    21168  14890  13893   1522  -1058    822       C  
ATOM   4371  C   LYS B 155     -18.328 -11.037  -9.370  1.00135.00           C  
ANISOU 4371  C   LYS B 155    21473  15359  14461   1539  -1110    717       C  
ATOM   4372  O   LYS B 155     -17.248 -11.199  -9.944  1.00134.46           O  
ANISOU 4372  O   LYS B 155    21288  15232  14567   1553  -1205    681       O  
ATOM   4373  CB  LYS B 155     -19.828 -13.058  -9.728  1.00133.32           C  
ANISOU 4373  CB  LYS B 155    21318  15148  14189   1438   -890    857       C  
ATOM   4374  N   ALA B 156     -18.950  -9.827  -9.277  1.00131.58           N  
ANISOU 4374  N   ALA B 156    21054  15008  13931   1541  -1049    670       N  
ATOM   4375  CA  ALA B 156     -18.439  -8.560  -9.838  1.00130.79           C  
ANISOU 4375  CA  ALA B 156    20851  14926  13917   1547  -1095    574       C  
ATOM   4376  C   ALA B 156     -17.136  -8.120  -9.175  1.00136.26           C  
ANISOU 4376  C   ALA B 156    21581  15548  14643   1594  -1315    540       C  
ATOM   4377  O   ALA B 156     -16.270  -7.564  -9.847  1.00135.04           O  
ANISOU 4377  O   ALA B 156    21292  15377  14641   1581  -1388    478       O  
ATOM   4378  CB  ALA B 156     -19.481  -7.459  -9.710  1.00130.99           C  
ANISOU 4378  CB  ALA B 156    20927  15042  13802   1555   -985    543       C  
ATOM   4379  N   LEU B 157     -16.996  -8.399  -7.863  1.00135.16           N  
ANISOU 4379  N   LEU B 157    21624  15371  14361   1642  -1423    587       N  
ATOM   4380  CA  LEU B 157     -15.822  -8.105  -7.042  1.00136.55           C  
ANISOU 4380  CA  LEU B 157    21865  15477  14540   1684  -1655    572       C  
ATOM   4381  C   LEU B 157     -14.553  -8.758  -7.619  1.00141.75           C  
ANISOU 4381  C   LEU B 157    22362  16073  15423   1685  -1774    573       C  
ATOM   4382  O   LEU B 157     -13.482  -8.156  -7.577  1.00141.85           O  
ANISOU 4382  O   LEU B 157    22311  16058  15528   1693  -1939    530       O  
ATOM   4383  CB  LEU B 157     -16.074  -8.609  -5.613  1.00138.16           C  
ANISOU 4383  CB  LEU B 157    22305  15649  14541   1731  -1720    643       C  
ATOM   4384  CG  LEU B 157     -15.201  -8.002  -4.521  1.00144.64           C  
ANISOU 4384  CG  LEU B 157    23261  16413  15282   1775  -1950    623       C  
ATOM   4385  CD1 LEU B 157     -15.816  -6.714  -3.977  1.00145.16           C  
ANISOU 4385  CD1 LEU B 157    23473  16520  15163   1791  -1923    570       C  
ATOM   4386  CD2 LEU B 157     -14.963  -8.997  -3.400  1.00148.67           C  
ANISOU 4386  CD2 LEU B 157    23944  16858  15687   1818  -2062    708       C  
ATOM   4387  N   ASP B 158     -14.694  -9.975  -8.182  1.00138.89           N  
ANISOU 4387  N   ASP B 158    21933  15690  15148   1677  -1686    622       N  
ATOM   4388  CA  ASP B 158     -13.610 -10.762  -8.781  1.00139.19           C  
ANISOU 4388  CA  ASP B 158    21825  15669  15392   1699  -1765    629       C  
ATOM   4389  C   ASP B 158     -13.410 -10.512 -10.298  1.00140.38           C  
ANISOU 4389  C   ASP B 158    21751  15852  15736   1656  -1658    568       C  
ATOM   4390  O   ASP B 158     -12.322 -10.791 -10.812  1.00140.61           O  
ANISOU 4390  O   ASP B 158    21633  15847  15945   1682  -1737    553       O  
ATOM   4391  CB  ASP B 158     -13.829 -12.266  -8.514  1.00142.25           C  
ANISOU 4391  CB  ASP B 158    22301  15993  15754   1725  -1741    716       C  
ATOM   4392  CG  ASP B 158     -14.589 -12.595  -7.236  1.00160.10           C  
ANISOU 4392  CG  ASP B 158    24804  18245  17783   1736  -1747    788       C  
ATOM   4393  OD1 ASP B 158     -14.286 -11.980  -6.181  1.00162.39           O  
ANISOU 4393  OD1 ASP B 158    25216  18527  17958   1771  -1887    785       O  
ATOM   4394  OD2 ASP B 158     -15.484 -13.468  -7.286  1.00168.58           O1-
ANISOU 4394  OD2 ASP B 158    25952  19316  18784   1704  -1613    850       O1-
ATOM   4395  N   PHE B 159     -14.446 -10.003 -11.006  1.00133.60           N  
ANISOU 4395  N   PHE B 159    20863  15062  14836   1597  -1479    537       N  
ATOM   4396  CA  PHE B 159     -14.389  -9.761 -12.452  1.00131.45           C  
ANISOU 4396  CA  PHE B 159    20404  14820  14722   1550  -1366    483       C  
ATOM   4397  C   PHE B 159     -14.078  -8.306 -12.820  1.00132.28           C  
ANISOU 4397  C   PHE B 159    20425  14970  14866   1520  -1396    404       C  
ATOM   4398  O   PHE B 159     -13.210  -8.051 -13.660  1.00132.10           O  
ANISOU 4398  O   PHE B 159    20237  14943  15014   1504  -1423    362       O  
ATOM   4399  CB  PHE B 159     -15.695 -10.241 -13.138  1.00132.45           C  
ANISOU 4399  CB  PHE B 159    20542  14987  14797   1496  -1158    505       C  
ATOM   4400  CG  PHE B 159     -15.875  -9.889 -14.607  1.00132.96           C  
ANISOU 4400  CG  PHE B 159    20447  15089  14983   1440  -1029    450       C  
ATOM   4401  CD1 PHE B 159     -16.511  -8.710 -14.988  1.00133.95           C  
ANISOU 4401  CD1 PHE B 159    20546  15288  15060   1400   -954    400       C  
ATOM   4402  CD2 PHE B 159     -15.456 -10.763 -15.607  1.00136.02           C  
ANISOU 4402  CD2 PHE B 159    20729  15434  15520   1432   -980    449       C  
ATOM   4403  CE1 PHE B 159     -16.676  -8.387 -16.340  1.00135.33           C  
ANISOU 4403  CE1 PHE B 159    20587  15493  15338   1347   -843    353       C  
ATOM   4404  CE2 PHE B 159     -15.646 -10.448 -16.960  1.00135.43           C  
ANISOU 4404  CE2 PHE B 159    20526  15390  15540   1378   -859    398       C  
ATOM   4405  CZ  PHE B 159     -16.265  -9.268 -17.315  1.00132.97           C  
ANISOU 4405  CZ  PHE B 159    20189  15154  15181   1332   -794    354       C  
ATOM   4406  N   ARG B 160     -14.813  -7.359 -12.231  1.00125.48           N  
ANISOU 4406  N   ARG B 160    19682  14150  13843   1512  -1382    386       N  
ATOM   4407  CA  ARG B 160     -14.693  -5.939 -12.543  1.00123.08           C  
ANISOU 4407  CA  ARG B 160    19339  13878  13546   1482  -1402    313       C  
ATOM   4408  C   ARG B 160     -13.436  -5.259 -11.945  1.00126.25           C  
ANISOU 4408  C   ARG B 160    19739  14237  13994   1492  -1621    284       C  
ATOM   4409  O   ARG B 160     -13.509  -4.120 -11.477  1.00126.62           O  
ANISOU 4409  O   ARG B 160    19877  14288  13945   1484  -1686    243       O  
ATOM   4410  CB  ARG B 160     -15.980  -5.213 -12.140  1.00120.95           C  
ANISOU 4410  CB  ARG B 160    19208  13663  13083   1488  -1299    304       C  
ATOM   4411  CG  ARG B 160     -17.240  -5.781 -12.784  1.00124.51           C  
ANISOU 4411  CG  ARG B 160    19635  14173  13499   1464  -1090    336       C  
ATOM   4412  CD  ARG B 160     -18.482  -5.044 -12.330  1.00129.18           C  
ANISOU 4412  CD  ARG B 160    20346  14834  13903   1485   -991    334       C  
ATOM   4413  NE  ARG B 160     -18.616  -3.718 -12.944  1.00129.91           N  
ANISOU 4413  NE  ARG B 160    20395  14955  14009   1472   -965    259       N  
ATOM   4414  CZ  ARG B 160     -18.350  -2.568 -12.331  1.00133.81           C  
ANISOU 4414  CZ  ARG B 160    20992  15428  14420   1505  -1066    210       C  
ATOM   4415  NH1 ARG B 160     -17.925  -2.559 -11.074  1.00113.41           N1+
ANISOU 4415  NH1 ARG B 160    18560  12800  11728   1551  -1203    224       N1+
ATOM   4416  NH2 ARG B 160     -18.509  -1.418 -12.970  1.00119.12           N  
ANISOU 4416  NH2 ARG B 160    19100  13584  12577   1489  -1037    146       N  
ATOM   4417  N   THR B 161     -12.279  -5.940 -12.012  1.00121.66           N  
ANISOU 4417  N   THR B 161    19048  13614  13564   1508  -1735    306       N  
ATOM   4418  CA  THR B 161     -10.989  -5.430 -11.534  1.00121.70           C  
ANISOU 4418  CA  THR B 161    19010  13587  13644   1508  -1953    291       C  
ATOM   4419  C   THR B 161     -10.252  -4.766 -12.725  1.00123.54           C  
ANISOU 4419  C   THR B 161    19025  13846  14069   1443  -1938    237       C  
ATOM   4420  O   THR B 161     -10.397  -5.261 -13.849  1.00121.95           O  
ANISOU 4420  O   THR B 161    18687  13666  13980   1430  -1787    232       O  
ATOM   4421  CB  THR B 161     -10.188  -6.545 -10.849  1.00128.23           C  
ANISOU 4421  CB  THR B 161    19839  14364  14520   1574  -2091    353       C  
ATOM   4422  OG1 THR B 161      -9.849  -7.548 -11.807  1.00128.37           O  
ANISOU 4422  OG1 THR B 161    19689  14377  14707   1592  -2000    372       O  
ATOM   4423  CG2 THR B 161     -10.943  -7.177  -9.683  1.00125.88           C  
ANISOU 4423  CG2 THR B 161    19773  14037  14020   1627  -2101    411       C  
ATOM   4424  N   PRO B 162      -9.489  -3.653 -12.526  1.00119.75           N  
ANISOU 4424  N   PRO B 162    18519  13361  13619   1394  -2088    199       N  
ATOM   4425  CA  PRO B 162      -8.847  -2.964 -13.667  1.00118.77           C  
ANISOU 4425  CA  PRO B 162    18196  13266  13666   1316  -2060    155       C  
ATOM   4426  C   PRO B 162      -7.955  -3.811 -14.583  1.00122.36           C  
ANISOU 4426  C   PRO B 162    18412  13737  14343   1327  -2022    174       C  
ATOM   4427  O   PRO B 162      -7.861  -3.493 -15.772  1.00121.58           O  
ANISOU 4427  O   PRO B 162    18167  13672  14356   1273  -1903    141       O  
ATOM   4428  CB  PRO B 162      -8.051  -1.835 -13.003  1.00121.60           C  
ANISOU 4428  CB  PRO B 162    18590  13601  14010   1262  -2275    131       C  
ATOM   4429  CG  PRO B 162      -7.963  -2.201 -11.576  1.00127.49           C  
ANISOU 4429  CG  PRO B 162    19510  14304  14626   1324  -2439    170       C  
ATOM   4430  CD  PRO B 162      -9.239  -2.910 -11.278  1.00122.40           C  
ANISOU 4430  CD  PRO B 162    19023  13662  13822   1394  -2284    194       C  
ATOM   4431  N   ALA B 163      -7.320  -4.878 -14.050  1.00118.36           N  
ANISOU 4431  N   ALA B 163    17874  13206  13893   1404  -2117    228       N  
ATOM   4432  CA  ALA B 163      -6.466  -5.776 -14.828  1.00117.51           C  
ANISOU 4432  CA  ALA B 163    17554  13108  13987   1444  -2081    249       C  
ATOM   4433  C   ALA B 163      -7.309  -6.591 -15.815  1.00119.36           C  
ANISOU 4433  C   ALA B 163    17778  13344  14229   1466  -1846    245       C  
ATOM   4434  O   ALA B 163      -6.877  -6.813 -16.953  1.00118.31           O  
ANISOU 4434  O   ALA B 163    17469  13235  14250   1458  -1741    228       O  
ATOM   4435  CB  ALA B 163      -5.697  -6.697 -13.900  1.00119.66           C  
ANISOU 4435  CB  ALA B 163    17831  13342  14292   1537  -2251    309       C  
ATOM   4436  N   LYS B 164      -8.528  -7.004 -15.387  1.00114.78           N  
ANISOU 4436  N   LYS B 164    17391  12743  13477   1486  -1761    263       N  
ATOM   4437  CA  LYS B 164      -9.465  -7.770 -16.216  1.00112.86           C  
ANISOU 4437  CA  LYS B 164    17166  12499  13217   1489  -1554    266       C  
ATOM   4438  C   LYS B 164     -10.150  -6.901 -17.273  1.00113.87           C  
ANISOU 4438  C   LYS B 164    17251  12675  13339   1405  -1399    211       C  
ATOM   4439  O   LYS B 164     -10.406  -7.392 -18.365  1.00111.95           O  
ANISOU 4439  O   LYS B 164    16933  12438  13166   1392  -1246    200       O  
ATOM   4440  CB  LYS B 164     -10.470  -8.563 -15.368  1.00115.19           C  
ANISOU 4440  CB  LYS B 164    17665  12762  13342   1528  -1527    318       C  
ATOM   4441  CG  LYS B 164      -9.926  -9.923 -14.933  1.00129.84           C  
ANISOU 4441  CG  LYS B 164    19537  14553  15245   1616  -1597    378       C  
ATOM   4442  CD  LYS B 164     -10.948 -10.766 -14.168  1.00140.06           C  
ANISOU 4442  CD  LYS B 164    21037  15811  16368   1638  -1556    437       C  
ATOM   4443  CE  LYS B 164     -10.324 -12.022 -13.593  1.00147.91           C  
ANISOU 4443  CE  LYS B 164    22074  16727  17399   1729  -1658    500       C  
ATOM   4444  NZ  LYS B 164     -11.311 -12.853 -12.855  1.00152.79           N1+
ANISOU 4444  NZ  LYS B 164    22901  17305  17848   1735  -1617    565       N1+
ATOM   4445  N   ALA B 165     -10.391  -5.604 -16.975  1.00110.64           N  
ANISOU 4445  N   ALA B 165    16898  12293  12847   1350  -1445    175       N  
ATOM   4446  CA  ALA B 165     -10.963  -4.642 -17.934  1.00109.35           C  
ANISOU 4446  CA  ALA B 165    16702  12169  12677   1274  -1322    122       C  
ATOM   4447  C   ALA B 165      -9.921  -4.359 -19.032  1.00112.76           C  
ANISOU 4447  C   ALA B 165    16924  12617  13303   1228  -1307     92       C  
ATOM   4448  O   ALA B 165     -10.271  -4.285 -20.208  1.00110.94           O  
ANISOU 4448  O   ALA B 165    16624  12409  13119   1187  -1155     65       O  
ATOM   4449  CB  ALA B 165     -11.344  -3.346 -17.227  1.00110.02           C  
ANISOU 4449  CB  ALA B 165    16916  12261  12624   1243  -1400     93       C  
ATOM   4450  N   LYS B 166      -8.637  -4.252 -18.631  1.00110.35           N  
ANISOU 4450  N   LYS B 166    16516  12304  13107   1236  -1467    102       N  
ATOM   4451  CA  LYS B 166      -7.473  -4.050 -19.492  1.00110.43           C  
ANISOU 4451  CA  LYS B 166    16306  12341  13311   1200  -1473     88       C  
ATOM   4452  C   LYS B 166      -7.380  -5.217 -20.495  1.00113.02           C  
ANISOU 4452  C   LYS B 166    16523  12670  13750   1251  -1317     98       C  
ATOM   4453  O   LYS B 166      -7.273  -4.977 -21.697  1.00112.56           O  
ANISOU 4453  O   LYS B 166    16352  12639  13777   1203  -1188     67       O  
ATOM   4454  CB  LYS B 166      -6.206  -3.968 -18.611  1.00115.12           C  
ANISOU 4454  CB  LYS B 166    16822  12930  13986   1218  -1695    117       C  
ATOM   4455  CG  LYS B 166      -4.878  -3.843 -19.346  1.00137.16           C  
ANISOU 4455  CG  LYS B 166    19359  15765  16991   1187  -1719    118       C  
ATOM   4456  CD  LYS B 166      -3.730  -4.325 -18.458  1.00154.85           C  
ANISOU 4456  CD  LYS B 166    21510  18003  19322   1250  -1921    167       C  
ATOM   4457  CE  LYS B 166      -2.426  -4.492 -19.206  1.00170.51           C  
ANISOU 4457  CE  LYS B 166    23211  20042  21532   1250  -1920    180       C  
ATOM   4458  NZ  LYS B 166      -1.326  -4.944 -18.308  1.00180.72           N1+
ANISOU 4458  NZ  LYS B 166    24407  21341  22917   1318  -2130    234       N1+
ATOM   4459  N   LEU B 167      -7.469  -6.471 -19.995  1.00108.54           N  
ANISOU 4459  N   LEU B 167    16012  12062  13165   1349  -1329    140       N  
ATOM   4460  CA  LEU B 167      -7.394  -7.686 -20.804  1.00107.09           C  
ANISOU 4460  CA  LEU B 167    15765  11856  13068   1413  -1199    151       C  
ATOM   4461  C   LEU B 167      -8.527  -7.785 -21.832  1.00107.72           C  
ANISOU 4461  C   LEU B 167    15907  11938  13085   1364   -995    122       C  
ATOM   4462  O   LEU B 167      -8.232  -7.995 -23.010  1.00107.39           O  
ANISOU 4462  O   LEU B 167    15751  11905  13147   1356   -871     97       O  
ATOM   4463  CB  LEU B 167      -7.309  -8.941 -19.916  1.00107.68           C  
ANISOU 4463  CB  LEU B 167    15926  11871  13115   1522  -1277    206       C  
ATOM   4464  CG  LEU B 167      -7.022 -10.260 -20.642  1.00112.38           C  
ANISOU 4464  CG  LEU B 167    16466  12424  13810   1608  -1174    220       C  
ATOM   4465  CD1 LEU B 167      -5.558 -10.370 -21.039  1.00114.06           C  
ANISOU 4465  CD1 LEU B 167    16454  12662  14223   1669  -1222    218       C  
ATOM   4466  CD2 LEU B 167      -7.440 -11.451 -19.804  1.00113.75           C  
ANISOU 4466  CD2 LEU B 167    16803  12521  13894   1690  -1219    274       C  
ATOM   4467  N   ILE B 168      -9.804  -7.605 -21.396  1.00101.29           N  
ANISOU 4467  N   ILE B 168    15267  11120  12100   1332   -962    128       N  
ATOM   4468  CA  ILE B 168     -11.003  -7.641 -22.247  1.00 98.93           C  
ANISOU 4468  CA  ILE B 168    15032  10831  11725   1279   -791    109       C  
ATOM   4469  C   ILE B 168     -10.867  -6.621 -23.397  1.00101.78           C  
ANISOU 4469  C   ILE B 168    15286  11235  12151   1198   -708     55       C  
ATOM   4470  O   ILE B 168     -10.979  -6.995 -24.566  1.00100.04           O  
ANISOU 4470  O   ILE B 168    15011  11012  11989   1180   -571     35       O  
ATOM   4471  CB  ILE B 168     -12.301  -7.438 -21.401  1.00101.22           C  
ANISOU 4471  CB  ILE B 168    15503  11132  11824   1263   -792    132       C  
ATOM   4472  CG1 ILE B 168     -12.574  -8.653 -20.490  1.00102.01           C  
ANISOU 4472  CG1 ILE B 168    15719  11184  11856   1328   -832    194       C  
ATOM   4473  CG2 ILE B 168     -13.530  -7.129 -22.279  1.00100.72           C  
ANISOU 4473  CG2 ILE B 168    15478  11103  11689   1195   -635    111       C  
ATOM   4474  CD1 ILE B 168     -13.443  -8.362 -19.219  1.00104.46           C  
ANISOU 4474  CD1 ILE B 168    16198  11510  11982   1333   -889    227       C  
ATOM   4475  N   ASN B 169     -10.577  -5.352 -23.052  1.00 99.20           N  
ANISOU 4475  N   ASN B 169    14942  10938  11809   1150   -799     32       N  
ATOM   4476  CA  ASN B 169     -10.397  -4.260 -24.011  1.00 99.07           C  
ANISOU 4476  CA  ASN B 169    14842  10955  11844   1065   -744    -13       C  
ATOM   4477  C   ASN B 169      -9.256  -4.535 -25.002  1.00105.41           C  
ANISOU 4477  C   ASN B 169    15456  11767  12826   1060   -692    -25       C  
ATOM   4478  O   ASN B 169      -9.464  -4.358 -26.204  1.00105.16           O  
ANISOU 4478  O   ASN B 169    15380  11749  12825   1011   -554    -54       O  
ATOM   4479  CB  ASN B 169     -10.260  -2.896 -23.307  1.00 96.34           C  
ANISOU 4479  CB  ASN B 169    14543  10622  11440   1015   -875    -31       C  
ATOM   4480  CG  ASN B 169     -11.592  -2.382 -22.788  1.00100.90           C  
ANISOU 4480  CG  ASN B 169    15303  11202  11833   1012   -857    -36       C  
ATOM   4481  OD1 ASN B 169     -11.889  -2.421 -21.590  1.00 89.45           O  
ANISOU 4481  OD1 ASN B 169    13973   9739  10274   1058   -952    -14       O  
ATOM   4482  ND2 ASN B 169     -12.448  -1.916 -23.685  1.00 88.41           N  
ANISOU 4482  ND2 ASN B 169    13744   9640  10207    965   -729    -63       N  
ATOM   4483  N   ILE B 170      -8.092  -5.030 -24.516  1.00103.35           N  
ANISOU 4483  N   ILE B 170    15087  11502  12679   1120   -796      1       N  
ATOM   4484  CA  ILE B 170      -6.961  -5.395 -25.377  1.00104.16           C  
ANISOU 4484  CA  ILE B 170    14994  11624  12957   1140   -741     -3       C  
ATOM   4485  C   ILE B 170      -7.405  -6.494 -26.339  1.00107.98           C  
ANISOU 4485  C   ILE B 170    15497  12079  13451   1188   -565    -11       C  
ATOM   4486  O   ILE B 170      -7.142  -6.378 -27.537  1.00107.51           O  
ANISOU 4486  O   ILE B 170    15345  12040  13466   1155   -434    -39       O  
ATOM   4487  CB  ILE B 170      -5.680  -5.756 -24.569  1.00109.04           C  
ANISOU 4487  CB  ILE B 170    15488  12250  13692   1211   -900     35       C  
ATOM   4488  CG1 ILE B 170      -4.961  -4.474 -24.114  1.00110.55           C  
ANISOU 4488  CG1 ILE B 170    15602  12483  13921   1122  -1050     33       C  
ATOM   4489  CG2 ILE B 170      -4.717  -6.670 -25.357  1.00110.23           C  
ANISOU 4489  CG2 ILE B 170    15461  12412  14009   1291   -813     42       C  
ATOM   4490  CD1 ILE B 170      -4.055  -4.625 -22.876  1.00120.54           C  
ANISOU 4490  CD1 ILE B 170    16819  13747  15233   1173  -1269     76       C  
ATOM   4491  N   CYS B 171      -8.139  -7.517 -25.828  1.00104.79           N  
ANISOU 4491  N   CYS B 171    15233  11623  12960   1255   -560     15       N  
ATOM   4492  CA  CYS B 171      -8.663  -8.620 -26.653  1.00104.32           C  
ANISOU 4492  CA  CYS B 171    15229  11518  12891   1291   -410     10       C  
ATOM   4493  C   CYS B 171      -9.545  -8.135 -27.796  1.00105.32           C  
ANISOU 4493  C   CYS B 171    15398  11660  12959   1197   -260    -29       C  
ATOM   4494  O   CYS B 171      -9.454  -8.695 -28.887  1.00103.52           O  
ANISOU 4494  O   CYS B 171    15141  11411  12780   1207   -129    -50       O  
ATOM   4495  CB  CYS B 171      -9.363  -9.681 -25.814  1.00104.78           C  
ANISOU 4495  CB  CYS B 171    15446  11515  12851   1352   -449     52       C  
ATOM   4496  SG  CYS B 171      -8.231 -10.729 -24.869  1.00110.75           S  
ANISOU 4496  SG  CYS B 171    16157  12225  13700   1495   -585     99       S  
ATOM   4497  N   ILE B 172     -10.358  -7.065 -27.548  1.00100.15           N  
ANISOU 4497  N   ILE B 172    14814  11040  12197   1113   -286    -39       N  
ATOM   4498  CA  ILE B 172     -11.243  -6.435 -28.533  1.00 97.95           C  
ANISOU 4498  CA  ILE B 172    14579  10783  11856   1024   -168    -71       C  
ATOM   4499  C   ILE B 172     -10.389  -5.827 -29.653  1.00101.81           C  
ANISOU 4499  C   ILE B 172    14928  11297  12456    978    -97   -108       C  
ATOM   4500  O   ILE B 172     -10.597  -6.155 -30.827  1.00100.38           O  
ANISOU 4500  O   ILE B 172    14746  11105  12289    956     42   -130       O  
ATOM   4501  CB  ILE B 172     -12.248  -5.416 -27.889  1.00 99.59           C  
ANISOU 4501  CB  ILE B 172    14895  11021  11926    971   -223    -70       C  
ATOM   4502  CG1 ILE B 172     -13.223  -6.124 -26.917  1.00 98.94           C  
ANISOU 4502  CG1 ILE B 172    14951  10922  11720   1012   -255    -28       C  
ATOM   4503  CG2 ILE B 172     -13.039  -4.646 -28.972  1.00 99.49           C  
ANISOU 4503  CG2 ILE B 172    14907  11033  11864    886   -114   -103       C  
ATOM   4504  CD1 ILE B 172     -13.804  -5.257 -25.808  1.00101.21           C  
ANISOU 4504  CD1 ILE B 172    15331  11239  11887   1007   -351    -17       C  
ATOM   4505  N   TRP B 173      -9.403  -4.989 -29.277  1.00 99.54           N  
ANISOU 4505  N   TRP B 173    14530  11044  12247    958   -195   -109       N  
ATOM   4506  CA  TRP B 173      -8.506  -4.328 -30.215  1.00100.44           C  
ANISOU 4506  CA  TRP B 173    14499  11193  12471    901   -139   -132       C  
ATOM   4507  C   TRP B 173      -7.686  -5.327 -31.049  1.00106.32           C  
ANISOU 4507  C   TRP B 173    15127  11932  13338    968    -27   -135       C  
ATOM   4508  O   TRP B 173      -7.599  -5.149 -32.260  1.00106.33           O  
ANISOU 4508  O   TRP B 173    15087  11945  13369    922    110   -162       O  
ATOM   4509  CB  TRP B 173      -7.641  -3.284 -29.499  1.00100.47           C  
ANISOU 4509  CB  TRP B 173    14413  11232  12530    856   -289   -123       C  
ATOM   4510  CG  TRP B 173      -8.408  -2.019 -29.197  1.00101.00           C  
ANISOU 4510  CG  TRP B 173    14598  11301  12478    768   -348   -139       C  
ATOM   4511  CD1 TRP B 173      -9.332  -1.836 -28.207  1.00103.33           C  
ANISOU 4511  CD1 TRP B 173    15049  11575  12635    789   -431   -132       C  
ATOM   4512  CD2 TRP B 173      -8.385  -0.798 -29.952  1.00100.63           C  
ANISOU 4512  CD2 TRP B 173    14535  11270  12428    656   -312   -165       C  
ATOM   4513  NE1 TRP B 173      -9.884  -0.581 -28.300  1.00102.08           N  
ANISOU 4513  NE1 TRP B 173    14973  11420  12392    710   -449   -155       N  
ATOM   4514  CE2 TRP B 173      -9.318   0.080 -29.358  1.00103.83           C  
ANISOU 4514  CE2 TRP B 173    15098  11659  12694    625   -384   -175       C  
ATOM   4515  CE3 TRP B 173      -7.661  -0.355 -31.073  1.00102.41           C  
ANISOU 4515  CE3 TRP B 173    14637  11524  12752    581   -222   -177       C  
ATOM   4516  CZ2 TRP B 173      -9.534   1.379 -29.838  1.00103.11           C  
ANISOU 4516  CZ2 TRP B 173    15051  11566  12561    527   -380   -199       C  
ATOM   4517  CZ3 TRP B 173      -7.888   0.922 -31.558  1.00103.52           C  
ANISOU 4517  CZ3 TRP B 173    14822  11665  12848    469   -216   -197       C  
ATOM   4518  CH2 TRP B 173      -8.822   1.770 -30.951  1.00103.47           C  
ANISOU 4518  CH2 TRP B 173    14981  11629  12703    445   -299   -209       C  
ATOM   4519  N   VAL B 174      -7.193  -6.424 -30.443  1.00104.14           N  
ANISOU 4519  N   VAL B 174    14823  11629  13117   1083    -75   -108       N  
ATOM   4520  CA  VAL B 174      -6.446  -7.454 -31.187  1.00104.80           C  
ANISOU 4520  CA  VAL B 174    14812  11696  13309   1174     33   -113       C  
ATOM   4521  C   VAL B 174      -7.407  -8.319 -32.074  1.00106.49           C  
ANISOU 4521  C   VAL B 174    15173  11848  13440   1187    185   -136       C  
ATOM   4522  O   VAL B 174      -7.060  -8.636 -33.209  1.00104.71           O  
ANISOU 4522  O   VAL B 174    14901  11618  13267   1201    329   -163       O  
ATOM   4523  CB  VAL B 174      -5.491  -8.302 -30.283  1.00110.20           C  
ANISOU 4523  CB  VAL B 174    15410  12371  14092   1306    -77    -75       C  
ATOM   4524  CG1 VAL B 174      -6.248  -9.155 -29.276  1.00109.54           C  
ANISOU 4524  CG1 VAL B 174    15496  12218  13906   1370   -162    -46       C  
ATOM   4525  CG2 VAL B 174      -4.545  -9.167 -31.114  1.00111.42           C  
ANISOU 4525  CG2 VAL B 174    15436  12523  14377   1412     41    -82       C  
ATOM   4526  N   LEU B 175      -8.607  -8.658 -31.564  1.00102.79           N  
ANISOU 4526  N   LEU B 175    14881  11335  12838   1173    152   -123       N  
ATOM   4527  CA  LEU B 175      -9.601  -9.460 -32.275  1.00102.03           C  
ANISOU 4527  CA  LEU B 175    14932  11179  12654   1164    266   -136       C  
ATOM   4528  C   LEU B 175     -10.052  -8.759 -33.526  1.00103.70           C  
ANISOU 4528  C   LEU B 175    15156  11414  12831   1063    390   -176       C  
ATOM   4529  O   LEU B 175     -10.028  -9.376 -34.585  1.00103.83           O  
ANISOU 4529  O   LEU B 175    15200  11392  12858   1077    518   -201       O  
ATOM   4530  CB  LEU B 175     -10.806  -9.746 -31.377  1.00102.11           C  
ANISOU 4530  CB  LEU B 175    15102  11163  12530   1144    193   -103       C  
ATOM   4531  CG  LEU B 175     -11.650 -10.958 -31.717  1.00108.54           C  
ANISOU 4531  CG  LEU B 175    16067  11902  13272   1155    264    -94       C  
ATOM   4532  CD1 LEU B 175     -11.085 -12.228 -31.047  1.00110.77           C  
ANISOU 4532  CD1 LEU B 175    16375  12111  13600   1278    213    -63       C  
ATOM   4533  CD2 LEU B 175     -13.090 -10.735 -31.271  1.00111.20           C  
ANISOU 4533  CD2 LEU B 175    16534  12254  13463   1073    237    -68       C  
ATOM   4534  N   ALA B 176     -10.413  -7.452 -33.423  1.00 98.60           N  
ANISOU 4534  N   ALA B 176    14498  10824  12139    966    348   -182       N  
ATOM   4535  CA  ALA B 176     -10.858  -6.618 -34.547  1.00 96.84           C  
ANISOU 4535  CA  ALA B 176    14293  10625  11876    864    446   -214       C  
ATOM   4536  C   ALA B 176      -9.862  -6.533 -35.719  1.00101.95           C  
ANISOU 4536  C   ALA B 176    14826  11284  12624    860    567   -244       C  
ATOM   4537  O   ALA B 176     -10.277  -6.179 -36.821  1.00101.13           O  
ANISOU 4537  O   ALA B 176    14769  11180  12476    788    673   -271       O  
ATOM   4538  CB  ALA B 176     -11.233  -5.233 -34.065  1.00 96.61           C  
ANISOU 4538  CB  ALA B 176    14271  10644  11793    784    358   -212       C  
ATOM   4539  N   SER B 177      -8.569  -6.903 -35.504  1.00100.53           N  
ANISOU 4539  N   SER B 177    14499  11120  12577    941    556   -235       N  
ATOM   4540  CA  SER B 177      -7.548  -6.926 -36.564  1.00101.53           C  
ANISOU 4540  CA  SER B 177    14499  11270  12807    955    686   -257       C  
ATOM   4541  C   SER B 177      -7.856  -7.999 -37.641  1.00105.59           C  
ANISOU 4541  C   SER B 177    15114  11718  13285   1005    844   -287       C  
ATOM   4542  O   SER B 177      -7.303  -7.937 -38.743  1.00104.94           O  
ANISOU 4542  O   SER B 177    14976  11650  13245    999    984   -313       O  
ATOM   4543  CB  SER B 177      -6.146  -7.087 -35.985  1.00106.45           C  
ANISOU 4543  CB  SER B 177    14926  11937  13583   1040    628   -232       C  
ATOM   4544  OG  SER B 177      -5.888  -8.420 -35.573  1.00115.55           O  
ANISOU 4544  OG  SER B 177    16096  13038  14772   1185    619   -220       O  
ATOM   4545  N   GLY B 178      -8.775  -8.924 -37.318  1.00102.24           N  
ANISOU 4545  N   GLY B 178    14851  11222  12774   1041    819   -281       N  
ATOM   4546  CA  GLY B 178      -9.294  -9.943 -38.228  1.00102.58           C  
ANISOU 4546  CA  GLY B 178    15037  11185  12755   1066    938   -308       C  
ATOM   4547  C   GLY B 178     -10.262  -9.353 -39.249  1.00106.87           C  
ANISOU 4547  C   GLY B 178    15691  11727  13189    939   1015   -334       C  
ATOM   4548  O   GLY B 178     -10.690 -10.044 -40.176  1.00106.33           O  
ANISOU 4548  O   GLY B 178    15747  11593  13060    936   1116   -360       O  
ATOM   4549  N   VAL B 179     -10.619  -8.063 -39.073  1.00103.43           N  
ANISOU 4549  N   VAL B 179    15221  11357  12722    835    957   -325       N  
ATOM   4550  CA  VAL B 179     -11.483  -7.252 -39.937  1.00102.54           C  
ANISOU 4550  CA  VAL B 179    15193  11256  12513    715   1004   -343       C  
ATOM   4551  C   VAL B 179     -10.566  -6.218 -40.606  1.00106.78           C  
ANISOU 4551  C   VAL B 179    15604  11848  13118    666   1068   -359       C  
ATOM   4552  O   VAL B 179     -10.537  -6.125 -41.832  1.00106.78           O  
ANISOU 4552  O   VAL B 179    15643  11836  13093    624   1196   -388       O  
ATOM   4553  CB  VAL B 179     -12.625  -6.541 -39.136  1.00105.46           C  
ANISOU 4553  CB  VAL B 179    15629  11653  12789    649    883   -317       C  
ATOM   4554  CG1 VAL B 179     -13.526  -5.719 -40.054  1.00104.18           C  
ANISOU 4554  CG1 VAL B 179    15549  11503  12530    539    927   -332       C  
ATOM   4555  CG2 VAL B 179     -13.447  -7.535 -38.319  1.00105.15           C  
ANISOU 4555  CG2 VAL B 179    15689  11574  12690    691    817   -288       C  
ATOM   4556  N   GLY B 180      -9.834  -5.463 -39.779  1.00103.17           N  
ANISOU 4556  N   GLY B 180    15009  11449  12742    665    975   -338       N  
ATOM   4557  CA  GLY B 180      -8.914  -4.405 -40.186  1.00103.42           C  
ANISOU 4557  CA  GLY B 180    14907  11540  12848    602   1006   -339       C  
ATOM   4558  C   GLY B 180      -7.892  -4.806 -41.228  1.00108.88           C  
ANISOU 4558  C   GLY B 180    15505  12243  13622    636   1166   -358       C  
ATOM   4559  O   GLY B 180      -7.703  -4.072 -42.200  1.00109.33           O  
ANISOU 4559  O   GLY B 180    15549  12323  13668    550   1261   -370       O  
ATOM   4560  N   VAL B 181      -7.240  -5.985 -41.043  1.00105.67           N  
ANISOU 4560  N   VAL B 181    15041  11817  13292    770   1204   -358       N  
ATOM   4561  CA  VAL B 181      -6.213  -6.512 -41.954  1.00105.91           C  
ANISOU 4561  CA  VAL B 181    14975  11859  13405    839   1368   -375       C  
ATOM   4562  C   VAL B 181      -6.843  -6.957 -43.296  1.00110.41           C  
ANISOU 4562  C   VAL B 181    15717  12365  13867    819   1527   -418       C  
ATOM   4563  O   VAL B 181      -6.418  -6.388 -44.298  1.00111.72           O  
ANISOU 4563  O   VAL B 181    15844  12567  14039    759   1652   -432       O  
ATOM   4564  CB  VAL B 181      -5.272  -7.575 -41.329  1.00109.72           C  
ANISOU 4564  CB  VAL B 181    15340  12341  14008   1005   1353   -361       C  
ATOM   4565  CG1 VAL B 181      -4.260  -8.081 -42.351  1.00111.20           C  
ANISOU 4565  CG1 VAL B 181    15432  12547  14272   1091   1544   -382       C  
ATOM   4566  CG2 VAL B 181      -4.545  -7.010 -40.118  1.00109.53           C  
ANISOU 4566  CG2 VAL B 181    15134  12389  14093   1007   1194   -316       C  
ATOM   4567  N   PRO B 182      -7.856  -7.873 -43.397  1.00105.48           N  
ANISOU 4567  N   PRO B 182    15290  11651  13138    849   1524   -437       N  
ATOM   4568  CA  PRO B 182      -8.422  -8.184 -44.731  1.00104.54           C  
ANISOU 4568  CA  PRO B 182    15339  11472  12911    811   1663   -477       C  
ATOM   4569  C   PRO B 182      -8.965  -6.956 -45.487  1.00106.60           C  
ANISOU 4569  C   PRO B 182    15650  11764  13090    656   1686   -482       C  
ATOM   4570  O   PRO B 182      -8.749  -6.869 -46.691  1.00106.69           O  
ANISOU 4570  O   PRO B 182    15705  11766  13066    626   1833   -510       O  
ATOM   4571  CB  PRO B 182      -9.506  -9.226 -44.437  1.00105.40           C  
ANISOU 4571  CB  PRO B 182    15639  11485  12924    840   1603   -482       C  
ATOM   4572  CG  PRO B 182      -9.125  -9.814 -43.129  1.00110.25           C  
ANISOU 4572  CG  PRO B 182    16170  12099  13622    945   1489   -451       C  
ATOM   4573  CD  PRO B 182      -8.511  -8.688 -42.350  1.00106.15           C  
ANISOU 4573  CD  PRO B 182    15459  11680  13191    909   1397   -419       C  
ATOM   4574  N   ILE B 183      -9.596  -5.979 -44.782  1.00101.52           N  
ANISOU 4574  N   ILE B 183    15000  11158  12417    565   1546   -455       N  
ATOM   4575  CA  ILE B 183     -10.101  -4.716 -45.370  1.00100.47           C  
ANISOU 4575  CA  ILE B 183    14913  11051  12211    428   1546   -454       C  
ATOM   4576  C   ILE B 183      -8.926  -3.862 -45.947  1.00106.46           C  
ANISOU 4576  C   ILE B 183    15526  11872  13051    382   1639   -451       C  
ATOM   4577  O   ILE B 183      -9.061  -3.261 -47.019  1.00105.35           O  
ANISOU 4577  O   ILE B 183    15453  11730  12846    293   1731   -464       O  
ATOM   4578  CB  ILE B 183     -11.005  -3.925 -44.360  1.00101.47           C  
ANISOU 4578  CB  ILE B 183    15066  11197  12289    371   1372   -426       C  
ATOM   4579  CG1 ILE B 183     -12.347  -4.659 -44.045  1.00100.43           C  
ANISOU 4579  CG1 ILE B 183    15089  11015  12055    386   1307   -423       C  
ATOM   4580  CG2 ILE B 183     -11.254  -2.484 -44.787  1.00100.97           C  
ANISOU 4580  CG2 ILE B 183    15020  11165  12180    249   1355   -420       C  
ATOM   4581  CD1 ILE B 183     -13.372  -4.926 -45.215  1.00100.79           C  
ANISOU 4581  CD1 ILE B 183    15313  11010  11974    323   1377   -444       C  
ATOM   4582  N   MET B 184      -7.773  -3.849 -45.237  1.00104.99           N  
ANISOU 4582  N   MET B 184    15142  11743  13005    439   1613   -429       N  
ATOM   4583  CA  MET B 184      -6.550  -3.147 -45.633  1.00106.15           C  
ANISOU 4583  CA  MET B 184    15114  11965  13253    397   1693   -414       C  
ATOM   4584  C   MET B 184      -5.943  -3.785 -46.871  1.00110.17           C  
ANISOU 4584  C   MET B 184    15621  12470  13770    446   1908   -440       C  
ATOM   4585  O   MET B 184      -5.342  -3.092 -47.689  1.00111.49           O  
ANISOU 4585  O   MET B 184    15724  12683  13953    369   2020   -434       O  
ATOM   4586  CB  MET B 184      -5.524  -3.172 -44.502  1.00109.80           C  
ANISOU 4586  CB  MET B 184    15361  12490  13866    459   1597   -379       C  
ATOM   4587  CG  MET B 184      -4.553  -2.029 -44.577  1.00115.58           C  
ANISOU 4587  CG  MET B 184    15919  13306  14689    357   1598   -347       C  
ATOM   4588  SD  MET B 184      -3.441  -1.975 -43.166  1.00121.82           S  
ANISOU 4588  SD  MET B 184    16464  14171  15651    409   1443   -300       S  
ATOM   4589  CE  MET B 184      -2.275  -3.135 -43.672  1.00120.51           C  
ANISOU 4589  CE  MET B 184    16134  14047  15609    563   1611   -302       C  
ATOM   4590  N   VAL B 185      -6.092  -5.106 -46.996  1.00105.27           N  
ANISOU 4590  N   VAL B 185    15079  11788  13131    575   1966   -469       N  
ATOM   4591  CA  VAL B 185      -5.588  -5.884 -48.117  1.00105.84           C  
ANISOU 4591  CA  VAL B 185    15184  11835  13193    653   2170   -504       C  
ATOM   4592  C   VAL B 185      -6.442  -5.615 -49.372  1.00108.67           C  
ANISOU 4592  C   VAL B 185    15759  12138  13392    552   2264   -536       C  
ATOM   4593  O   VAL B 185      -5.888  -5.348 -50.439  1.00110.18           O  
ANISOU 4593  O   VAL B 185    15939  12354  13571    522   2430   -547       O  
ATOM   4594  CB  VAL B 185      -5.505  -7.388 -47.731  1.00110.05           C  
ANISOU 4594  CB  VAL B 185    15758  12303  13753    829   2177   -524       C  
ATOM   4595  CG1 VAL B 185      -5.173  -8.269 -48.927  1.00111.09           C  
ANISOU 4595  CG1 VAL B 185    15984  12383  13842    920   2386   -571       C  
ATOM   4596  CG2 VAL B 185      -4.499  -7.613 -46.602  1.00110.72           C  
ANISOU 4596  CG2 VAL B 185    15613  12452  14004    936   2097   -488       C  
ATOM   4597  N   MET B 186      -7.781  -5.639 -49.225  1.00102.14           N  
ANISOU 4597  N   MET B 186    15120  11243  12444    494   2152   -544       N  
ATOM   4598  CA  MET B 186      -8.742  -5.464 -50.316  1.00100.69           C  
ANISOU 4598  CA  MET B 186    15153  11000  12104    401   2203   -570       C  
ATOM   4599  C   MET B 186      -8.930  -4.024 -50.790  1.00105.21           C  
ANISOU 4599  C   MET B 186    15728  11617  12631    248   2194   -550       C  
ATOM   4600  O   MET B 186      -9.293  -3.829 -51.950  1.00104.97           O  
ANISOU 4600  O   MET B 186    15843  11551  12489    180   2288   -570       O  
ATOM   4601  CB  MET B 186     -10.095  -6.087 -49.955  1.00101.33           C  
ANISOU 4601  CB  MET B 186    15414  11004  12084    397   2082   -577       C  
ATOM   4602  CG  MET B 186      -9.999  -7.573 -49.655  1.00105.28           C  
ANISOU 4602  CG  MET B 186    15962  11435  12604    534   2098   -597       C  
ATOM   4603  SD  MET B 186     -11.573  -8.381 -49.298  1.00108.19           S  
ANISOU 4603  SD  MET B 186    16544  11712  12852    507   1964   -596       S  
ATOM   4604  CE  MET B 186     -12.068  -7.558 -47.751  1.00103.27           C  
ANISOU 4604  CE  MET B 186    15795  11164  12279    466   1759   -541       C  
ATOM   4605  N   ALA B 187      -8.708  -3.021 -49.909  1.00102.39           N  
ANISOU 4605  N   ALA B 187    15231  11325  12348    193   2073   -511       N  
ATOM   4606  CA  ALA B 187      -8.862  -1.593 -50.232  1.00101.42           C  
ANISOU 4606  CA  ALA B 187    15118  11232  12185     49   2042   -488       C  
ATOM   4607  C   ALA B 187      -7.967  -1.176 -51.410  1.00106.53           C  
ANISOU 4607  C   ALA B 187    15730  11910  12837     -7   2227   -490       C  
ATOM   4608  O   ALA B 187      -6.747  -1.357 -51.367  1.00107.40           O  
ANISOU 4608  O   ALA B 187    15659  12081  13067     41   2322   -479       O  
ATOM   4609  CB  ALA B 187      -8.565  -0.747 -49.009  1.00101.59           C  
ANISOU 4609  CB  ALA B 187    14992  11309  12299     19   1887   -450       C  
ATOM   4610  N   VAL B 188      -8.596  -0.691 -52.495  1.00102.73           N  
ANISOU 4610  N   VAL B 188    15423  11388  12222   -104   2283   -501       N  
ATOM   4611  CA  VAL B 188      -7.933  -0.294 -53.752  1.00103.66           C  
ANISOU 4611  CA  VAL B 188    15557  11522  12306   -170   2468   -502       C  
ATOM   4612  C   VAL B 188      -8.506   1.006 -54.317  1.00107.77           C  
ANISOU 4612  C   VAL B 188    16199  12026  12724   -326   2424   -480       C  
ATOM   4613  O   VAL B 188      -9.643   1.365 -54.010  1.00105.41           O  
ANISOU 4613  O   VAL B 188    16023  11684  12344   -362   2275   -479       O  
ATOM   4614  CB  VAL B 188      -7.982  -1.417 -54.857  1.00107.35           C  
ANISOU 4614  CB  VAL B 188    16169  11931  12686    -95   2643   -550       C  
ATOM   4615  CG1 VAL B 188      -7.250  -2.691 -54.437  1.00107.71           C  
ANISOU 4615  CG1 VAL B 188    16103  11986  12834     72   2713   -572       C  
ATOM   4616  CG2 VAL B 188      -9.408  -1.721 -55.316  1.00105.63           C  
ANISOU 4616  CG2 VAL B 188    16211  11619  12305   -124   2572   -578       C  
ATOM   4617  N   THR B 189      -7.732   1.665 -55.199  1.00107.42           N  
ANISOU 4617  N   THR B 189    16127  12015  12674   -414   2566   -462       N  
ATOM   4618  CA  THR B 189      -8.158   2.841 -55.961  1.00107.90           C  
ANISOU 4618  CA  THR B 189    16326  12048  12623   -563   2558   -440       C  
ATOM   4619  C   THR B 189      -8.261   2.426 -57.431  1.00114.84           C  
ANISOU 4619  C   THR B 189    17381  12883  13370   -576   2740   -469       C  
ATOM   4620  O   THR B 189      -7.251   2.045 -58.045  1.00115.46           O  
ANISOU 4620  O   THR B 189    17382  13002  13485   -548   2937   -473       O  
ATOM   4621  CB  THR B 189      -7.271   4.055 -55.730  1.00114.12           C  
ANISOU 4621  CB  THR B 189    16966  12898  13497   -680   2549   -387       C  
ATOM   4622  OG1 THR B 189      -5.910   3.669 -55.877  1.00118.80           O  
ANISOU 4622  OG1 THR B 189    17357  13573  14210   -646   2714   -374       O  
ATOM   4623  CG2 THR B 189      -7.498   4.677 -54.390  1.00109.59           C  
ANISOU 4623  CG2 THR B 189    16304  12336  12999   -693   2332   -363       C  
ATOM   4624  N   ARG B 190      -9.498   2.439 -57.967  1.00112.51           N  
ANISOU 4624  N   ARG B 190    17322  12506  12919   -607   2672   -488       N  
ATOM   4625  CA  ARG B 190      -9.802   2.024 -59.335  1.00114.23           C  
ANISOU 4625  CA  ARG B 190    17752  12664  12986   -624   2810   -519       C  
ATOM   4626  C   ARG B 190     -10.547   3.103 -60.144  1.00119.76           C  
ANISOU 4626  C   ARG B 190    18647  13317  13540   -762   2760   -496       C  
ATOM   4627  O   ARG B 190     -11.399   3.796 -59.587  1.00117.80           O  
ANISOU 4627  O   ARG B 190    18435  13052  13274   -804   2573   -475       O  
ATOM   4628  CB  ARG B 190     -10.562   0.687 -59.328  1.00114.90           C  
ANISOU 4628  CB  ARG B 190    17957  12686  13015   -515   2785   -569       C  
ATOM   4629  CG  ARG B 190      -9.821  -0.415 -60.079  1.00130.07           C  
ANISOU 4629  CG  ARG B 190    19903  14593  14924   -422   2999   -612       C  
ATOM   4630  CD  ARG B 190     -10.011  -1.770 -59.434  1.00142.27           C  
ANISOU 4630  CD  ARG B 190    21438  16105  16515   -280   2961   -651       C  
ATOM   4631  NE  ARG B 190      -8.852  -2.141 -58.624  1.00154.12           N  
ANISOU 4631  NE  ARG B 190    22688  17679  18192   -172   3018   -644       N  
ATOM   4632  CZ  ARG B 190      -8.063  -3.184 -58.863  1.00173.50           C  
ANISOU 4632  CZ  ARG B 190    25106  20130  20686    -42   3179   -678       C  
ATOM   4633  NH1 ARG B 190      -8.307  -3.987 -59.892  1.00166.85           N1+
ANISOU 4633  NH1 ARG B 190    24480  19205  19711     -3   3304   -728       N1+
ATOM   4634  NH2 ARG B 190      -7.032  -3.439 -58.070  1.00160.15           N  
ANISOU 4634  NH2 ARG B 190    23170  18515  19165     58   3210   -663       N  
ATOM   4635  N   PRO B 191     -10.241   3.269 -61.456  1.00119.57           N  
ANISOU 4635  N   PRO B 191    18757  13269  13404   -827   2927   -499       N  
ATOM   4636  CA  PRO B 191     -10.925   4.313 -62.239  1.00119.81           C  
ANISOU 4636  CA  PRO B 191    18985  13249  13291   -958   2873   -472       C  
ATOM   4637  C   PRO B 191     -12.274   3.904 -62.833  1.00125.16           C  
ANISOU 4637  C   PRO B 191    19914  13838  13804   -954   2782   -501       C  
ATOM   4638  O   PRO B 191     -12.362   2.901 -63.541  1.00125.81           O  
ANISOU 4638  O   PRO B 191    20118  13877  13805   -902   2885   -545       O  
ATOM   4639  CB  PRO B 191      -9.900   4.680 -63.317  1.00123.46           C  
ANISOU 4639  CB  PRO B 191    19466  13732  13710  -1035   3098   -455       C  
ATOM   4640  CG  PRO B 191      -8.892   3.549 -63.329  1.00128.80           C  
ANISOU 4640  CG  PRO B 191    20005  14459  14473   -916   3290   -489       C  
ATOM   4641  CD  PRO B 191      -9.248   2.550 -62.281  1.00122.97           C  
ANISOU 4641  CD  PRO B 191    19174  13720  13830   -779   3176   -524       C  
ATOM   4642  N   ARG B 192     -13.327   4.690 -62.533  1.00122.23           N  
ANISOU 4642  N   ARG B 192    19620  13438  13383  -1005   2583   -474       N  
ATOM   4643  CA  ARG B 192     -14.708   4.485 -63.002  1.00122.22           C  
ANISOU 4643  CA  ARG B 192    19832  13367  13237  -1015   2459   -486       C  
ATOM   4644  C   ARG B 192     -15.281   5.822 -63.521  1.00128.75           C  
ANISOU 4644  C   ARG B 192    20800  14159  13959  -1126   2364   -442       C  
ATOM   4645  O   ARG B 192     -15.487   6.756 -62.728  1.00127.45           O  
ANISOU 4645  O   ARG B 192    20553  14016  13855  -1144   2229   -407       O  
ATOM   4646  CB  ARG B 192     -15.614   3.913 -61.880  1.00120.59           C  
ANISOU 4646  CB  ARG B 192    19553  13173  13094   -929   2280   -496       C  
ATOM   4647  CG  ARG B 192     -15.076   2.685 -61.135  1.00130.67           C  
ANISOU 4647  CG  ARG B 192    20679  14481  14490   -815   2339   -530       C  
ATOM   4648  CD  ARG B 192     -15.465   1.361 -61.767  1.00142.73           C  
ANISOU 4648  CD  ARG B 192    22352  15948  15930   -767   2394   -577       C  
ATOM   4649  NE  ARG B 192     -15.144   0.227 -60.893  1.00150.87           N  
ANISOU 4649  NE  ARG B 192    23252  16998  17075   -652   2406   -604       N  
ATOM   4650  CZ  ARG B 192     -14.021  -0.485 -60.960  1.00164.30           C  
ANISOU 4650  CZ  ARG B 192    24870  18711  18846   -576   2576   -633       C  
ATOM   4651  NH1 ARG B 192     -13.093  -0.194 -61.864  1.00157.33           N  
ANISOU 4651  NH1 ARG B 192    24010  17835  17933   -606   2763   -638       N  
ATOM   4652  NH2 ARG B 192     -13.821  -1.497 -60.125  1.00143.50           N1+
ANISOU 4652  NH2 ARG B 192    22131  16083  16309   -466   2564   -653       N1+
ATOM   4653  N   ASP B 193     -15.513   5.907 -64.863  1.00127.83           N  
ANISOU 4653  N   ASP B 193    20911  13981  13676  -1196   2437   -444       N  
ATOM   4654  CA  ASP B 193     -16.033   7.074 -65.610  1.00128.25           C  
ANISOU 4654  CA  ASP B 193    21145  13984  13600  -1303   2367   -403       C  
ATOM   4655  C   ASP B 193     -15.085   8.288 -65.568  1.00130.78           C  
ANISOU 4655  C   ASP B 193    21391  14327  13971  -1392   2431   -356       C  
ATOM   4656  O   ASP B 193     -15.515   9.402 -65.240  1.00130.70           O  
ANISOU 4656  O   ASP B 193    21401  14300  13958  -1437   2286   -315       O  
ATOM   4657  CB  ASP B 193     -17.472   7.465 -65.172  1.00129.70           C  
ANISOU 4657  CB  ASP B 193    21391  14146  13743  -1285   2120   -383       C  
ATOM   4658  CG  ASP B 193     -18.534   6.409 -65.415  1.00145.39           C  
ANISOU 4658  CG  ASP B 193    23484  16106  15653  -1236   2041   -414       C  
ATOM   4659  OD1 ASP B 193     -18.984   6.272 -66.586  1.00146.84           O1-
ANISOU 4659  OD1 ASP B 193    23890  16226  15675  -1291   2057   -418       O1-
ATOM   4660  OD2 ASP B 193     -18.942   5.734 -64.430  1.00151.57           O  
ANISOU 4660  OD2 ASP B 193    24133  16927  16530  -1152   1955   -429       O  
ATOM   4661  N   GLY B 194     -13.805   8.059 -65.880  1.00125.87           N  
ANISOU 4661  N   GLY B 194    20681  13746  13400  -1413   2646   -361       N  
ATOM   4662  CA  GLY B 194     -12.781   9.104 -65.878  1.00125.37           C  
ANISOU 4662  CA  GLY B 194    20527  13714  13393  -1515   2729   -311       C  
ATOM   4663  C   GLY B 194     -12.303   9.544 -64.504  1.00125.06           C  
ANISOU 4663  C   GLY B 194    20240  13737  13540  -1496   2636   -290       C  
ATOM   4664  O   GLY B 194     -11.224  10.131 -64.386  1.00125.35           O  
ANISOU 4664  O   GLY B 194    20148  13818  13659  -1573   2726   -253       O  
ATOM   4665  N   ALA B 195     -13.108   9.277 -63.455  1.00117.67           N  
ANISOU 4665  N   ALA B 195    19238  12805  12667  -1401   2452   -309       N  
ATOM   4666  CA  ALA B 195     -12.804   9.582 -62.055  1.00115.23           C  
ANISOU 4666  CA  ALA B 195    18715  12547  12520  -1364   2340   -297       C  
ATOM   4667  C   ALA B 195     -12.209   8.344 -61.385  1.00114.97           C  
ANISOU 4667  C   ALA B 195    18482  12583  12620  -1250   2417   -335       C  
ATOM   4668  O   ALA B 195     -12.304   7.248 -61.930  1.00113.92           O  
ANISOU 4668  O   ALA B 195    18402  12441  12440  -1185   2519   -375       O  
ATOM   4669  CB  ALA B 195     -14.072  10.007 -61.326  1.00114.29           C  
ANISOU 4669  CB  ALA B 195    18658  12393  12374  -1318   2104   -294       C  
ATOM   4670  N   VAL B 196     -11.601   8.530 -60.205  1.00109.18           N  
ANISOU 4670  N   VAL B 196    17532  11907  12044  -1224   2358   -322       N  
ATOM   4671  CA  VAL B 196     -10.987   7.487 -59.372  1.00107.58           C  
ANISOU 4671  CA  VAL B 196    17120  11771  11985  -1112   2400   -348       C  
ATOM   4672  C   VAL B 196     -11.931   7.166 -58.184  1.00107.31           C  
ANISOU 4672  C   VAL B 196    17053  11731  11988  -1012   2202   -366       C  
ATOM   4673  O   VAL B 196     -12.574   8.077 -57.644  1.00105.46           O  
ANISOU 4673  O   VAL B 196    16862  11473  11734  -1041   2036   -344       O  
ATOM   4674  CB  VAL B 196      -9.571   7.948 -58.902  1.00112.17           C  
ANISOU 4674  CB  VAL B 196    17474  12427  12716  -1165   2470   -313       C  
ATOM   4675  CG1 VAL B 196      -8.935   6.972 -57.912  1.00111.72           C  
ANISOU 4675  CG1 VAL B 196    17189  12440  12819  -1043   2482   -333       C  
ATOM   4676  CG2 VAL B 196      -8.647   8.191 -60.094  1.00113.77           C  
ANISOU 4676  CG2 VAL B 196    17696  12650  12881  -1263   2687   -289       C  
ATOM   4677  N   VAL B 197     -12.032   5.875 -57.800  1.00102.53           N  
ANISOU 4677  N   VAL B 197    16385  11143  11428   -891   2224   -404       N  
ATOM   4678  CA  VAL B 197     -12.852   5.468 -56.650  1.00100.84           C  
ANISOU 4678  CA  VAL B 197    16130  10933  11253   -799   2055   -415       C  
ATOM   4679  C   VAL B 197     -12.033   4.645 -55.647  1.00102.89           C  
ANISOU 4679  C   VAL B 197    16177  11249  11666   -702   2077   -426       C  
ATOM   4680  O   VAL B 197     -11.228   3.810 -56.056  1.00103.57           O  
ANISOU 4680  O   VAL B 197    16202  11355  11795   -658   2233   -446       O  
ATOM   4681  CB  VAL B 197     -14.225   4.784 -56.983  1.00104.54           C  
ANISOU 4681  CB  VAL B 197    16768  11352  11602   -755   1988   -439       C  
ATOM   4682  CG1 VAL B 197     -15.141   5.703 -57.790  1.00104.57           C  
ANISOU 4682  CG1 VAL B 197    16967  11305  11462   -841   1922   -419       C  
ATOM   4683  CG2 VAL B 197     -14.063   3.433 -57.675  1.00105.09           C  
ANISOU 4683  CG2 VAL B 197    16890  11400  11640   -700   2126   -479       C  
ATOM   4684  N   CYS B 198     -12.241   4.898 -54.344  1.00 97.20           N  
ANISOU 4684  N   CYS B 198    15355  10553  11022   -662   1920   -413       N  
ATOM   4685  CA  CYS B 198     -11.646   4.146 -53.235  1.00 96.56           C  
ANISOU 4685  CA  CYS B 198    15091  10520  11078   -563   1898   -420       C  
ATOM   4686  C   CYS B 198     -12.681   3.049 -52.877  1.00 97.68           C  
ANISOU 4686  C   CYS B 198    15304  10634  11175   -464   1834   -446       C  
ATOM   4687  O   CYS B 198     -13.850   3.348 -52.615  1.00 96.27           O  
ANISOU 4687  O   CYS B 198    15226  10432  10919   -469   1706   -439       O  
ATOM   4688  CB  CYS B 198     -11.344   5.066 -52.052  1.00 96.85           C  
ANISOU 4688  CB  CYS B 198    15009  10588  11201   -586   1756   -390       C  
ATOM   4689  SG  CYS B 198     -10.720   4.218 -50.573  1.00100.91           S  
ANISOU 4689  SG  CYS B 198    15316  11156  11869   -466   1689   -392       S  
ATOM   4690  N   MET B 199     -12.273   1.778 -52.964  1.00 93.55           N  
ANISOU 4690  N   MET B 199    14741  10111  10693   -377   1931   -472       N  
ATOM   4691  CA  MET B 199     -13.187   0.646 -52.797  1.00 91.81           C  
ANISOU 4691  CA  MET B 199    14611   9852  10422   -302   1889   -495       C  
ATOM   4692  C   MET B 199     -12.508  -0.648 -52.393  1.00 94.07           C  
ANISOU 4692  C   MET B 199    14803  10141  10797   -187   1956   -516       C  
ATOM   4693  O   MET B 199     -11.307  -0.801 -52.588  1.00 93.36           O  
ANISOU 4693  O   MET B 199    14597  10081  10793   -157   2079   -521       O  
ATOM   4694  CB  MET B 199     -13.908   0.397 -54.132  1.00 94.44           C  
ANISOU 4694  CB  MET B 199    15151  10124  10607   -352   1958   -516       C  
ATOM   4695  CG  MET B 199     -12.964   0.372 -55.325  1.00 99.91           C  
ANISOU 4695  CG  MET B 199    15873  10808  11282   -382   2153   -534       C  
ATOM   4696  SD  MET B 199     -13.742  -0.252 -56.816  1.00105.17           S  
ANISOU 4696  SD  MET B 199    16804  11388  11769   -416   2234   -568       S  
ATOM   4697  CE  MET B 199     -13.338  -1.988 -56.670  1.00102.27           C  
ANISOU 4697  CE  MET B 199    16426  10986  11446   -281   2326   -613       C  
ATOM   4698  N   LEU B 200     -13.297  -1.604 -51.874  1.00 90.67           N  
ANISOU 4698  N   LEU B 200    14429   9678  10343   -121   1881   -525       N  
ATOM   4699  CA  LEU B 200     -12.792  -2.933 -51.537  1.00 91.17           C  
ANISOU 4699  CA  LEU B 200    14447   9722  10472     -6   1934   -546       C  
ATOM   4700  C   LEU B 200     -12.893  -3.757 -52.795  1.00 96.72           C  
ANISOU 4700  C   LEU B 200    15312  10354  11081      1   2070   -585       C  
ATOM   4701  O   LEU B 200     -13.918  -3.704 -53.483  1.00 95.13           O  
ANISOU 4701  O   LEU B 200    15286  10107  10751    -70   2041   -592       O  
ATOM   4702  CB  LEU B 200     -13.602  -3.626 -50.412  1.00 89.94           C  
ANISOU 4702  CB  LEU B 200    14297   9552  10322     50   1792   -533       C  
ATOM   4703  CG  LEU B 200     -13.747  -2.883 -49.075  1.00 92.91           C  
ANISOU 4703  CG  LEU B 200    14552   9988  10761     51   1639   -496       C  
ATOM   4704  CD1 LEU B 200     -14.850  -3.489 -48.239  1.00 91.35           C  
ANISOU 4704  CD1 LEU B 200    14411   9774  10523     81   1516   -480       C  
ATOM   4705  CD2 LEU B 200     -12.438  -2.839 -48.312  1.00 95.63           C  
ANISOU 4705  CD2 LEU B 200    14703  10380  11251    116   1652   -487       C  
ATOM   4706  N   GLN B 201     -11.809  -4.475 -53.118  1.00 96.44           N  
ANISOU 4706  N   GLN B 201    15220  10313  11108     87   2218   -611       N  
ATOM   4707  CA  GLN B 201     -11.739  -5.407 -54.234  1.00 98.14           C  
ANISOU 4707  CA  GLN B 201    15596  10452  11239    124   2363   -657       C  
ATOM   4708  C   GLN B 201     -11.841  -6.830 -53.645  1.00102.81           C  
ANISOU 4708  C   GLN B 201    16221  10984  11860    244   2335   -676       C  
ATOM   4709  O   GLN B 201     -10.850  -7.380 -53.155  1.00102.84           O  
ANISOU 4709  O   GLN B 201    16089  11007  11979    364   2393   -681       O  
ATOM   4710  CB  GLN B 201     -10.441  -5.211 -55.051  1.00101.35           C  
ANISOU 4710  CB  GLN B 201    15926  10895  11687    150   2567   -672       C  
ATOM   4711  CG  GLN B 201     -10.307  -6.109 -56.296  1.00115.68           C  
ANISOU 4711  CG  GLN B 201    17927  12629  13399    197   2739   -725       C  
ATOM   4712  CD  GLN B 201     -11.278  -5.753 -57.397  1.00131.69           C  
ANISOU 4712  CD  GLN B 201    20193  14596  15249     75   2737   -738       C  
ATOM   4713  OE1 GLN B 201     -10.974  -4.966 -58.299  1.00126.96           O  
ANISOU 4713  OE1 GLN B 201    19765  13923  14551     43   2626   -749       O  
ATOM   4714  NE2 GLN B 201     -12.465  -6.332 -57.345  1.00121.90           N  
ANISOU 4714  NE2 GLN B 201    18967  13387  13962     -2   2853   -733       N  
ATOM   4715  N   PHE B 202     -13.055  -7.389 -53.647  1.00 99.92           N  
ANISOU 4715  N   PHE B 202    16027  10546  11392    208   2234   -680       N  
ATOM   4716  CA  PHE B 202     -13.305  -8.745 -53.155  1.00101.23           C  
ANISOU 4716  CA  PHE B 202    16264  10637  11563    296   2195   -693       C  
ATOM   4717  C   PHE B 202     -12.810  -9.811 -54.158  1.00107.61           C  
ANISOU 4717  C   PHE B 202    17223  11349  12315    376   2356   -750       C  
ATOM   4718  O   PHE B 202     -12.875  -9.558 -55.371  1.00107.21           O  
ANISOU 4718  O   PHE B 202    17306  11269  12161    317   2458   -779       O  
ATOM   4719  CB  PHE B 202     -14.806  -8.949 -52.916  1.00102.30           C  
ANISOU 4719  CB  PHE B 202    16536  10733  11600    207   2037   -672       C  
ATOM   4720  CG  PHE B 202     -15.326  -8.167 -51.745  1.00103.01           C  
ANISOU 4720  CG  PHE B 202    16488  10908  11744    168   1880   -618       C  
ATOM   4721  CD1 PHE B 202     -15.068  -8.581 -50.443  1.00105.82           C  
ANISOU 4721  CD1 PHE B 202    16718  11287  12200    251   1803   -594       C  
ATOM   4722  CD2 PHE B 202     -16.078  -7.015 -51.940  1.00104.88           C  
ANISOU 4722  CD2 PHE B 202    16732  11196  11922     57   1807   -593       C  
ATOM   4723  CE1 PHE B 202     -15.534  -7.844 -49.356  1.00105.86           C  
ANISOU 4723  CE1 PHE B 202    16612  11368  12242    222   1666   -548       C  
ATOM   4724  CE2 PHE B 202     -16.542  -6.276 -50.852  1.00106.76           C  
ANISOU 4724  CE2 PHE B 202    16853  11508  12202     38   1671   -548       C  
ATOM   4725  CZ  PHE B 202     -16.281  -6.704 -49.567  1.00104.80           C  
ANISOU 4725  CZ  PHE B 202    16488  11283  12047    118   1604   -527       C  
ATOM   4726  N   PRO B 203     -12.383 -11.026 -53.699  1.00105.93           N  
ANISOU 4726  N   PRO B 203    17020  11074  12155    510   2377   -769       N  
ATOM   4727  CA  PRO B 203     -11.976 -12.076 -54.669  1.00108.09           C  
ANISOU 4727  CA  PRO B 203    17470  11239  12360    598   2530   -829       C  
ATOM   4728  C   PRO B 203     -13.154 -12.549 -55.534  1.00114.26           C  
ANISOU 4728  C   PRO B 203    18545  11906  12963    495   2490   -854       C  
ATOM   4729  O   PRO B 203     -14.297 -12.231 -55.203  1.00112.97           O  
ANISOU 4729  O   PRO B 203    18420  11752  12750    372   2331   -817       O  
ATOM   4730  CB  PRO B 203     -11.434 -13.205 -53.779  1.00110.00           C  
ANISOU 4730  CB  PRO B 203    17660  11435  12700    760   2516   -832       C  
ATOM   4731  CG  PRO B 203     -11.253 -12.594 -52.416  1.00112.64           C  
ANISOU 4731  CG  PRO B 203    17747  11879  13172    764   2386   -773       C  
ATOM   4732  CD  PRO B 203     -12.265 -11.514 -52.309  1.00106.46           C  
ANISOU 4732  CD  PRO B 203    16962  11155  12332    593   2263   -737       C  
ATOM   4733  N   SER B 204     -12.893 -13.270 -56.646  1.00113.87           N  
ANISOU 4733  N   SER B 204    18699  11752  12813    543   2632   -914       N  
ATOM   4734  CA  SER B 204     -13.980 -13.760 -57.515  1.00114.09           C  
ANISOU 4734  CA  SER B 204    19025  11660  12662    438   2585   -940       C  
ATOM   4735  C   SER B 204     -14.760 -14.917 -56.852  1.00115.24           C  
ANISOU 4735  C   SER B 204    19297  11701  12786    441   2442   -931       C  
ATOM   4736  O   SER B 204     -14.116 -15.837 -56.346  1.00115.80           O  
ANISOU 4736  O   SER B 204    19355  11716  12926    587   2481   -948       O  
ATOM   4737  CB  SER B 204     -13.462 -14.178 -58.888  1.00120.52           C  
ANISOU 4737  CB  SER B 204    20042  12386  13362    488   2777  -1010       C  
ATOM   4738  OG  SER B 204     -14.542 -14.388 -59.785  1.00129.83           O  
ANISOU 4738  OG  SER B 204    21502  13467  14362    355   2714  -1029       O  
ATOM   4739  N   PRO B 205     -16.121 -14.882 -56.804  1.00108.53           N  
ANISOU 4739  N   PRO B 205    18559  10830  11849    283   2274   -898       N  
ATOM   4740  CA  PRO B 205     -17.013 -13.824 -57.308  1.00106.47           C  
ANISOU 4740  CA  PRO B 205    18311  10634  11507    117   2198   -869       C  
ATOM   4741  C   PRO B 205     -17.142 -12.681 -56.305  1.00108.13           C  
ANISOU 4741  C   PRO B 205    18255  10999  11832     82   2103   -805       C  
ATOM   4742  O   PRO B 205     -17.450 -12.904 -55.132  1.00106.55           O  
ANISOU 4742  O   PRO B 205    17942  10831  11711     99   1988   -763       O  
ATOM   4743  CB  PRO B 205     -18.326 -14.568 -57.583  1.00107.97           C  
ANISOU 4743  CB  PRO B 205    18732  10722  11568     -7   2058   -860       C  
ATOM   4744  CG  PRO B 205     -18.294 -15.801 -56.697  1.00113.30           C  
ANISOU 4744  CG  PRO B 205    19436  11317  12295     71   2005   -854       C  
ATOM   4745  CD  PRO B 205     -16.891 -15.952 -56.140  1.00109.61           C  
ANISOU 4745  CD  PRO B 205    18806  10876  11966    264   2135   -877       C  
ATOM   4746  N   SER B 206     -16.821 -11.464 -56.755  1.00104.48           N  
ANISOU 4746  N   SER B 206    17699  10625  11374     42   2162   -801       N  
ATOM   4747  CA  SER B 206     -16.862 -10.266 -55.925  1.00102.94           C  
ANISOU 4747  CA  SER B 206    17276  10563  11273     10   2083   -748       C  
ATOM   4748  C   SER B 206     -18.253 -10.003 -55.348  1.00103.65           C  
ANISOU 4748  C   SER B 206    17369  10687  11328    -97   1889   -693       C  
ATOM   4749  O   SER B 206     -18.351  -9.734 -54.151  1.00102.52           O  
ANISOU 4749  O   SER B 206    17057  10617  11280    -71   1797   -651       O  
ATOM   4750  CB  SER B 206     -16.344  -9.059 -56.696  1.00108.55           C  
ANISOU 4750  CB  SER B 206    17939  11336  11969    -32   2181   -754       C  
ATOM   4751  OG  SER B 206     -17.053  -8.886 -57.913  1.00125.00           O  
ANISOU 4751  OG  SER B 206    20234  13365  13896   -139   2185   -769       O  
ATOM   4752  N   TRP B 207     -19.326 -10.160 -56.173  1.00 98.47           N  
ANISOU 4752  N   TRP B 207    16906   9976  10532   -212   1825   -693       N  
ATOM   4753  CA  TRP B 207     -20.721  -9.948 -55.760  1.00 96.45           C  
ANISOU 4753  CA  TRP B 207    16652   9760  10235   -319   1646   -636       C  
ATOM   4754  C   TRP B 207     -21.100 -10.815 -54.558  1.00 99.60           C  
ANISOU 4754  C   TRP B 207    16992  10154  10696   -287   1550   -602       C  
ATOM   4755  O   TRP B 207     -21.894 -10.386 -53.720  1.00 99.23           O  
ANISOU 4755  O   TRP B 207    16834  10192  10677   -328   1425   -544       O  
ATOM   4756  CB  TRP B 207     -21.706 -10.136 -56.941  1.00 95.50           C  
ANISOU 4756  CB  TRP B 207    16758   9572   9956   -446   1596   -643       C  
ATOM   4757  CG  TRP B 207     -21.877 -11.556 -57.404  1.00 97.74           C  
ANISOU 4757  CG  TRP B 207    17258   9718  10161   -455   1606   -677       C  
ATOM   4758  CD1 TRP B 207     -21.199 -12.178 -58.409  1.00101.80           C  
ANISOU 4758  CD1 TRP B 207    17959  10117  10601   -416   1740   -745       C  
ATOM   4759  CD2 TRP B 207     -22.750 -12.549 -56.833  1.00 97.82           C  
ANISOU 4759  CD2 TRP B 207    17327   9684  10158   -505   1479   -644       C  
ATOM   4760  NE1 TRP B 207     -21.592 -13.495 -58.503  1.00101.77           N  
ANISOU 4760  NE1 TRP B 207    18143   9989  10536   -433   1698   -762       N  
ATOM   4761  CE2 TRP B 207     -22.549 -13.746 -57.554  1.00102.58           C  
ANISOU 4761  CE2 TRP B 207    18169  10131  10675   -498   1535   -697       C  
ATOM   4762  CE3 TRP B 207     -23.664 -12.550 -55.757  1.00 97.98           C  
ANISOU 4762  CE3 TRP B 207    17223   9780  10226   -554   1331   -572       C  
ATOM   4763  CZ2 TRP B 207     -23.252 -14.919 -57.262  1.00102.55           C  
ANISOU 4763  CZ2 TRP B 207    18293  10038  10633   -554   1433   -679       C  
ATOM   4764  CZ3 TRP B 207     -24.347 -13.717 -55.463  1.00 99.68           C  
ANISOU 4764  CZ3 TRP B 207    17547   9921  10408   -610   1241   -549       C  
ATOM   4765  CH2 TRP B 207     -24.136 -14.885 -56.205  1.00101.71           C  
ANISOU 4765  CH2 TRP B 207    18050  10015  10581   -616   1286   -601       C  
ATOM   4766  N   TYR B 208     -20.523 -12.036 -54.492  1.00 95.26           N  
ANISOU 4766  N   TYR B 208    16528   9504  10163   -207   1613   -637       N  
ATOM   4767  CA  TYR B 208     -20.723 -13.025 -53.441  1.00 94.56           C  
ANISOU 4767  CA  TYR B 208    16420   9384  10126   -167   1540   -610       C  
ATOM   4768  C   TYR B 208     -20.105 -12.527 -52.139  1.00 97.32           C  
ANISOU 4768  C   TYR B 208    16528   9834  10617    -71   1527   -580       C  
ATOM   4769  O   TYR B 208     -20.829 -12.332 -51.155  1.00 95.89           O  
ANISOU 4769  O   TYR B 208    16249   9722  10462   -106   1407   -521       O  
ATOM   4770  CB  TYR B 208     -20.086 -14.368 -53.854  1.00 97.18           C  
ANISOU 4770  CB  TYR B 208    16926   9566  10433    -86   1629   -665       C  
ATOM   4771  CG  TYR B 208     -20.172 -15.453 -52.804  1.00 98.39           C  
ANISOU 4771  CG  TYR B 208    17082   9665  10635    -36   1560   -638       C  
ATOM   4772  CD1 TYR B 208     -21.325 -16.215 -52.658  1.00100.38           C  
ANISOU 4772  CD1 TYR B 208    17469   9858  10812   -151   1433   -599       C  
ATOM   4773  CD2 TYR B 208     -19.098 -15.724 -51.958  1.00 98.50           C  
ANISOU 4773  CD2 TYR B 208    16967   9687  10772    120   1616   -645       C  
ATOM   4774  CE1 TYR B 208     -21.425 -17.195 -51.677  1.00100.86           C  
ANISOU 4774  CE1 TYR B 208    17543   9866  10912   -116   1368   -566       C  
ATOM   4775  CE2 TYR B 208     -19.180 -16.720 -50.985  1.00 99.06           C  
ANISOU 4775  CE2 TYR B 208    17056   9700  10881    168   1547   -616       C  
ATOM   4776  CZ  TYR B 208     -20.348 -17.453 -50.853  1.00104.84           C  
ANISOU 4776  CZ  TYR B 208    17935  10370  11531     47   1426   -577       C  
ATOM   4777  OH  TYR B 208     -20.467 -18.455 -49.933  1.00106.22           O  
ANISOU 4777  OH  TYR B 208    18150  10479  11732     78   1357   -543       O  
ATOM   4778  N   TRP B 209     -18.765 -12.306 -52.148  1.00 93.68           N  
ANISOU 4778  N   TRP B 209    15968   9384  10241     49   1653   -618       N  
ATOM   4779  CA  TRP B 209     -17.995 -11.856 -50.995  1.00 92.52           C  
ANISOU 4779  CA  TRP B 209    15597   9323  10232    144   1644   -595       C  
ATOM   4780  C   TRP B 209     -18.426 -10.497 -50.516  1.00 97.39           C  
ANISOU 4780  C   TRP B 209    16068  10065  10871     80   1563   -553       C  
ATOM   4781  O   TRP B 209     -18.321 -10.226 -49.318  1.00 97.60           O  
ANISOU 4781  O   TRP B 209    15946  10158  10980    122   1491   -517       O  
ATOM   4782  CB  TRP B 209     -16.492 -11.938 -51.253  1.00 91.78           C  
ANISOU 4782  CB  TRP B 209    15430   9220  10223    273   1795   -640       C  
ATOM   4783  CG  TRP B 209     -16.018 -13.352 -51.446  1.00 93.99           C  
ANISOU 4783  CG  TRP B 209    15839   9376  10497    375   1864   -678       C  
ATOM   4784  CD1 TRP B 209     -15.529 -13.895 -52.592  1.00 98.33           C  
ANISOU 4784  CD1 TRP B 209    16540   9835  10986    418   2004   -738       C  
ATOM   4785  CD2 TRP B 209     -16.077 -14.424 -50.487  1.00 93.85           C  
ANISOU 4785  CD2 TRP B 209    15841   9299  10520    447   1792   -658       C  
ATOM   4786  NE1 TRP B 209     -15.248 -15.226 -52.403  1.00 98.94           N  
ANISOU 4786  NE1 TRP B 209    16729   9797  11068    522   2024   -761       N  
ATOM   4787  CE2 TRP B 209     -15.575 -15.578 -51.120  1.00 99.47           C  
ANISOU 4787  CE2 TRP B 209    16719   9878  11198    538   1891   -710       C  
ATOM   4788  CE3 TRP B 209     -16.480 -14.516 -49.140  1.00 94.28           C  
ANISOU 4788  CE3 TRP B 209    15797   9395  10630    448   1656   -600       C  
ATOM   4789  CZ2 TRP B 209     -15.473 -16.814 -50.460  1.00 99.74           C  
ANISOU 4789  CZ2 TRP B 209    16828   9812  11255    627   1851   -705       C  
ATOM   4790  CZ3 TRP B 209     -16.386 -15.735 -48.491  1.00 96.40           C  
ANISOU 4790  CZ3 TRP B 209    16136   9571  10919    527   1619   -591       C  
ATOM   4791  CH2 TRP B 209     -15.888 -16.870 -49.148  1.00 98.61           C  
ANISOU 4791  CH2 TRP B 209    16586   9713  11168    615   1711   -642       C  
ATOM   4792  N   ASP B 210     -18.991  -9.671 -51.425  1.00 93.41           N  
ANISOU 4792  N   ASP B 210    15625   9585  10282    -22   1564   -556       N  
ATOM   4793  CA  ASP B 210     -19.535  -8.364 -51.078  1.00 92.16           C  
ANISOU 4793  CA  ASP B 210    15361   9531  10127    -82   1480   -516       C  
ATOM   4794  C   ASP B 210     -20.824  -8.554 -50.260  1.00 92.70           C  
ANISOU 4794  C   ASP B 210    15424   9634  10164   -132   1332   -460       C  
ATOM   4795  O   ASP B 210     -21.003  -7.895 -49.238  1.00 91.20           O  
ANISOU 4795  O   ASP B 210    15098   9528  10024   -111   1257   -423       O  
ATOM   4796  CB  ASP B 210     -19.780  -7.514 -52.338  1.00 94.93           C  
ANISOU 4796  CB  ASP B 210    15799   9882  10387   -169   1521   -533       C  
ATOM   4797  CG  ASP B 210     -20.578  -6.249 -52.099  1.00112.90           C  
ANISOU 4797  CG  ASP B 210    18011  12246  12640   -234   1418   -491       C  
ATOM   4798  OD1 ASP B 210     -20.028  -5.306 -51.494  1.00115.33           O  
ANISOU 4798  OD1 ASP B 210    18178  12620  13023   -199   1414   -481       O  
ATOM   4799  OD2 ASP B 210     -21.757  -6.206 -52.509  1.00121.84           O1-
ANISOU 4799  OD2 ASP B 210    19238  13378  13678   -318   1337   -467       O1-
ATOM   4800  N   THR B 211     -21.687  -9.483 -50.685  1.00 88.41           N  
ANISOU 4800  N   THR B 211    15031   9026   9537   -198   1293   -453       N  
ATOM   4801  CA  THR B 211     -22.938  -9.788 -49.992  1.00 87.61           C  
ANISOU 4801  CA  THR B 211    14926   8961   9402   -260   1163   -392       C  
ATOM   4802  C   THR B 211     -22.633 -10.426 -48.582  1.00 91.13           C  
ANISOU 4802  C   THR B 211    15275   9417   9934   -177   1129   -364       C  
ATOM   4803  O   THR B 211     -23.251 -10.017 -47.594  1.00 89.42           O  
ANISOU 4803  O   THR B 211    14952   9288   9734   -182   1043   -311       O  
ATOM   4804  CB  THR B 211     -23.851 -10.580 -50.953  1.00 90.72           C  
ANISOU 4804  CB  THR B 211    15511   9276   9681   -372   1129   -391       C  
ATOM   4805  OG1 THR B 211     -24.343  -9.640 -51.918  1.00 90.96           O  
ANISOU 4805  OG1 THR B 211    15580   9342   9639   -450   1116   -393       O  
ATOM   4806  CG2 THR B 211     -25.033 -11.241 -50.269  1.00 84.17           C  
ANISOU 4806  CG2 THR B 211    14687   8468   8824   -445   1007   -324       C  
ATOM   4807  N   VAL B 212     -21.635 -11.347 -48.496  1.00 87.62           N  
ANISOU 4807  N   VAL B 212    14867   8885   9539    -89   1203   -401       N  
ATOM   4808  CA  VAL B 212     -21.190 -12.006 -47.258  1.00 86.59           C  
ANISOU 4808  CA  VAL B 212    14665   8746   9488      2   1176   -379       C  
ATOM   4809  C   VAL B 212     -20.711 -10.963 -46.239  1.00 89.82           C  
ANISOU 4809  C   VAL B 212    14877   9265   9986     68   1149   -360       C  
ATOM   4810  O   VAL B 212     -21.119 -11.013 -45.076  1.00 88.73           O  
ANISOU 4810  O   VAL B 212    14669   9176   9867     82   1065   -310       O  
ATOM   4811  CB  VAL B 212     -20.110 -13.085 -47.544  1.00 91.13           C  
ANISOU 4811  CB  VAL B 212    15322   9203  10101    103   1270   -429       C  
ATOM   4812  CG1 VAL B 212     -19.542 -13.664 -46.253  1.00 91.11           C  
ANISOU 4812  CG1 VAL B 212    15235   9195  10188    211   1236   -405       C  
ATOM   4813  CG2 VAL B 212     -20.664 -14.202 -48.417  1.00 91.63           C  
ANISOU 4813  CG2 VAL B 212    15612   9140  10064     37   1278   -447       C  
ATOM   4814  N   THR B 213     -19.880 -10.002 -46.697  1.00 86.72           N  
ANISOU 4814  N   THR B 213    14405   8908   9635     99   1218   -396       N  
ATOM   4815  CA  THR B 213     -19.342  -8.908 -45.881  1.00 86.12           C  
ANISOU 4815  CA  THR B 213    14160   8925   9637    146   1190   -383       C  
ATOM   4816  C   THR B 213     -20.460  -8.023 -45.332  1.00 87.76           C  
ANISOU 4816  C   THR B 213    14327   9221   9797     85   1086   -337       C  
ATOM   4817  O   THR B 213     -20.467  -7.759 -44.136  1.00 88.33           O  
ANISOU 4817  O   THR B 213    14305   9348   9909    130   1017   -305       O  
ATOM   4818  CB  THR B 213     -18.262  -8.135 -46.652  1.00 96.98           C  
ANISOU 4818  CB  THR B 213    15482  10310  11057    164   1292   -427       C  
ATOM   4819  OG1 THR B 213     -17.191  -9.038 -46.925  1.00103.31           O  
ANISOU 4819  OG1 THR B 213    16294  11044  11916    250   1390   -464       O  
ATOM   4820  CG2 THR B 213     -17.722  -6.930 -45.880  1.00 91.59           C  
ANISOU 4820  CG2 THR B 213    14638   9714  10449    189   1251   -413       C  
ATOM   4821  N   LYS B 214     -21.418  -7.613 -46.184  1.00 81.75           N  
ANISOU 4821  N   LYS B 214    13644   8473   8946    -10   1073   -331       N  
ATOM   4822  CA  LYS B 214     -22.567  -6.806 -45.786  1.00 80.04           C  
ANISOU 4822  CA  LYS B 214    13392   8342   8677    -57    980   -285       C  
ATOM   4823  C   LYS B 214     -23.453  -7.554 -44.766  1.00 84.99           C  
ANISOU 4823  C   LYS B 214    14010   8996   9286    -61    900   -228       C  
ATOM   4824  O   LYS B 214     -23.894  -6.941 -43.793  1.00 85.18           O  
ANISOU 4824  O   LYS B 214    13947   9103   9314    -35    836   -191       O  
ATOM   4825  CB  LYS B 214     -23.378  -6.361 -47.007  1.00 81.25           C  
ANISOU 4825  CB  LYS B 214    13637   8495   8739   -153    979   -287       C  
ATOM   4826  CG  LYS B 214     -22.703  -5.283 -47.850  1.00 83.80           C  
ANISOU 4826  CG  LYS B 214    13959   8817   9066   -159   1039   -327       C  
ATOM   4827  CD  LYS B 214     -23.554  -4.953 -49.060  1.00 90.14           C  
ANISOU 4827  CD  LYS B 214    14873   9609   9766   -254   1028   -325       C  
ATOM   4828  CE  LYS B 214     -22.796  -4.196 -50.105  1.00 96.01           C  
ANISOU 4828  CE  LYS B 214    15660  10323  10498   -273   1111   -367       C  
ATOM   4829  NZ  LYS B 214     -23.584  -4.056 -51.348  1.00 96.21           N1+
ANISOU 4829  NZ  LYS B 214    15822  10320  10412   -365   1099   -366       N1+
ATOM   4830  N   ILE B 215     -23.659  -8.877 -44.950  1.00 81.81           N  
ANISOU 4830  N   ILE B 215    13705   8519   8862    -90    908   -222       N  
ATOM   4831  CA  ILE B 215     -24.472  -9.690 -44.030  1.00 81.52           C  
ANISOU 4831  CA  ILE B 215    13673   8499   8804   -111    839   -161       C  
ATOM   4832  C   ILE B 215     -23.745  -9.892 -42.685  1.00 88.34           C  
ANISOU 4832  C   ILE B 215    14452   9372   9743     -6    825   -150       C  
ATOM   4833  O   ILE B 215     -24.397  -9.838 -41.631  1.00 88.14           O  
ANISOU 4833  O   ILE B 215    14372   9416   9703     -2    761    -94       O  
ATOM   4834  CB  ILE B 215     -24.982 -11.022 -44.664  1.00 84.20           C  
ANISOU 4834  CB  ILE B 215    14162   8743   9086   -195    837   -153       C  
ATOM   4835  CG1 ILE B 215     -25.871 -10.739 -45.893  1.00 82.85           C  
ANISOU 4835  CG1 ILE B 215    14072   8579   8830   -311    821   -152       C  
ATOM   4836  CG2 ILE B 215     -25.767 -11.864 -43.625  1.00 85.04           C  
ANISOU 4836  CG2 ILE B 215    14267   8867   9176   -226    765    -80       C  
ATOM   4837  CD1 ILE B 215     -25.983 -11.818 -46.821  1.00 82.97           C  
ANISOU 4837  CD1 ILE B 215    14258   8476   8791   -383    838   -174       C  
ATOM   4838  N   CYS B 216     -22.405 -10.084 -42.722  1.00 86.07           N  
ANISOU 4838  N   CYS B 216    14148   9023   9532     81    884   -199       N  
ATOM   4839  CA  CYS B 216     -21.590 -10.250 -41.513  1.00 85.60           C  
ANISOU 4839  CA  CYS B 216    14006   8968   9549    184    861   -190       C  
ATOM   4840  C   CYS B 216     -21.472  -8.968 -40.696  1.00 88.96           C  
ANISOU 4840  C   CYS B 216    14306   9495  10001    222    815   -179       C  
ATOM   4841  O   CYS B 216     -21.537  -9.050 -39.464  1.00 89.07           O  
ANISOU 4841  O   CYS B 216    14274   9543  10027    269    753   -141       O  
ATOM   4842  CB  CYS B 216     -20.228 -10.843 -41.840  1.00 86.36           C  
ANISOU 4842  CB  CYS B 216    14109   8979   9724    270    934   -240       C  
ATOM   4843  SG  CYS B 216     -20.285 -12.594 -42.296  1.00 91.04           S  
ANISOU 4843  SG  CYS B 216    14871   9431  10288    269    967   -246       S  
ATOM   4844  N   VAL B 217     -21.352  -7.785 -41.363  1.00 84.61           N  
ANISOU 4844  N   VAL B 217    13716   8984   9447    198    838   -208       N  
ATOM   4845  CA  VAL B 217     -21.305  -6.479 -40.664  1.00 83.69           C  
ANISOU 4845  CA  VAL B 217    13506   8949   9342    227    787   -201       C  
ATOM   4846  C   VAL B 217     -22.677  -6.198 -39.996  1.00 86.03           C  
ANISOU 4846  C   VAL B 217    13807   9323   9559    201    717   -146       C  
ATOM   4847  O   VAL B 217     -22.718  -5.853 -38.824  1.00 84.75           O  
ANISOU 4847  O   VAL B 217    13593   9209   9400    255    661   -122       O  
ATOM   4848  CB  VAL B 217     -20.804  -5.286 -41.531  1.00 87.36           C  
ANISOU 4848  CB  VAL B 217    13945   9426   9822    203    826   -242       C  
ATOM   4849  CG1 VAL B 217     -20.828  -3.977 -40.732  1.00 87.19           C  
ANISOU 4849  CG1 VAL B 217    13856   9472   9802    230    758   -233       C  
ATOM   4850  CG2 VAL B 217     -19.396  -5.539 -42.057  1.00 87.62           C  
ANISOU 4850  CG2 VAL B 217    13947   9403   9941    236    905   -287       C  
ATOM   4851  N   PHE B 218     -23.788  -6.401 -40.727  1.00 82.25           N  
ANISOU 4851  N   PHE B 218    13388   8857   9007    119    720   -125       N  
ATOM   4852  CA  PHE B 218     -25.133  -6.219 -40.192  1.00 81.37           C  
ANISOU 4852  CA  PHE B 218    13262   8831   8823     92    665    -65       C  
ATOM   4853  C   PHE B 218     -25.436  -7.169 -39.014  1.00 86.92           C  
ANISOU 4853  C   PHE B 218    13959   9546   9521    114    632    -13       C  
ATOM   4854  O   PHE B 218     -26.131  -6.772 -38.073  1.00 85.90           O  
ANISOU 4854  O   PHE B 218    13782   9503   9354    142    591     32       O  
ATOM   4855  CB  PHE B 218     -26.182  -6.389 -41.301  1.00 82.66           C  
ANISOU 4855  CB  PHE B 218    13484   9004   8920    -10    668    -48       C  
ATOM   4856  CG  PHE B 218     -27.610  -6.196 -40.841  1.00 84.03           C  
ANISOU 4856  CG  PHE B 218    13618   9283   9027    -40    615     21       C  
ATOM   4857  CD1 PHE B 218     -28.112  -4.924 -40.590  1.00 86.95           C  
ANISOU 4857  CD1 PHE B 218    13926   9743   9368      3    586     31       C  
ATOM   4858  CD2 PHE B 218     -28.453  -7.284 -40.664  1.00 86.50           C  
ANISOU 4858  CD2 PHE B 218    13956   9605   9304   -111    594     79       C  
ATOM   4859  CE1 PHE B 218     -29.431  -4.748 -40.168  1.00 88.04           C  
ANISOU 4859  CE1 PHE B 218    14012   9990   9448     -8    548     97       C  
ATOM   4860  CE2 PHE B 218     -29.770  -7.107 -40.242  1.00 89.40           C  
ANISOU 4860  CE2 PHE B 218    14264  10088   9617   -142    553    151       C  
ATOM   4861  CZ  PHE B 218     -30.253  -5.841 -40.007  1.00 87.54           C  
ANISOU 4861  CZ  PHE B 218    13952   9952   9357    -83    535    160       C  
ATOM   4862  N   LEU B 219     -24.947  -8.425 -39.080  1.00 85.52           N  
ANISOU 4862  N   LEU B 219    13842   9279   9373    106    653    -16       N  
ATOM   4863  CA  LEU B 219     -25.215  -9.414 -38.034  1.00 85.72           C  
ANISOU 4863  CA  LEU B 219    13884   9298   9387    117    621     38       C  
ATOM   4864  C   LEU B 219     -24.360  -9.179 -36.796  1.00 91.54           C  
ANISOU 4864  C   LEU B 219    14565  10043  10172    225    592     35       C  
ATOM   4865  O   LEU B 219     -24.910  -8.933 -35.723  1.00 91.24           O  
ANISOU 4865  O   LEU B 219    14495  10078  10095    250    551     82       O  
ATOM   4866  CB  LEU B 219     -25.111 -10.871 -38.562  1.00 85.96           C  
ANISOU 4866  CB  LEU B 219    14026   9216   9418     65    642     40       C  
ATOM   4867  CG  LEU B 219     -25.167 -12.057 -37.551  1.00 91.05           C  
ANISOU 4867  CG  LEU B 219    14718   9817  10057     77    610     93       C  
ATOM   4868  CD1 LEU B 219     -26.549 -12.226 -36.912  1.00 90.69           C  
ANISOU 4868  CD1 LEU B 219    14662   9860   9935     -2    569    180       C  
ATOM   4869  CD2 LEU B 219     -24.784 -13.378 -38.229  1.00 92.85           C  
ANISOU 4869  CD2 LEU B 219    15078   9905  10297     49    636     73       C  
ATOM   4870  N   PHE B 220     -23.030  -9.185 -36.951  1.00 89.25           N  
ANISOU 4870  N   PHE B 220    14260   9685   9964    291    613    -19       N  
ATOM   4871  CA  PHE B 220     -22.115  -9.082 -35.817  1.00 89.47           C  
ANISOU 4871  CA  PHE B 220    14237   9711  10046    389    571    -20       C  
ATOM   4872  C   PHE B 220     -21.941  -7.679 -35.242  1.00 91.97           C  
ANISOU 4872  C   PHE B 220    14476  10105  10364    431    531    -33       C  
ATOM   4873  O   PHE B 220     -21.758  -7.564 -34.032  1.00 92.15           O  
ANISOU 4873  O   PHE B 220    14479  10152  10383    492    472    -10       O  
ATOM   4874  CB  PHE B 220     -20.761  -9.716 -36.160  1.00 92.02           C  
ANISOU 4874  CB  PHE B 220    14559   9941  10464    447    604    -64       C  
ATOM   4875  CG  PHE B 220     -20.907 -11.189 -36.497  1.00 94.18           C  
ANISOU 4875  CG  PHE B 220    14937  10121  10726    427    631    -49       C  
ATOM   4876  CD1 PHE B 220     -21.207 -12.122 -35.508  1.00 96.57           C  
ANISOU 4876  CD1 PHE B 220    15293  10397  11003    444    581      6       C  
ATOM   4877  CD2 PHE B 220     -20.789 -11.635 -37.809  1.00 96.36           C  
ANISOU 4877  CD2 PHE B 220    15279  10328  11005    386    704    -89       C  
ATOM   4878  CE1 PHE B 220     -21.371 -13.468 -35.825  1.00 97.65           C  
ANISOU 4878  CE1 PHE B 220    15547  10433  11123    417    598     21       C  
ATOM   4879  CE2 PHE B 220     -20.944 -12.990 -38.121  1.00 99.13           C  
ANISOU 4879  CE2 PHE B 220    15754  10577  11335    366    721    -79       C  
ATOM   4880  CZ  PHE B 220     -21.231 -13.892 -37.127  1.00 97.13           C  
ANISOU 4880  CZ  PHE B 220    15552  10293  11062    380    665    -24       C  
ATOM   4881  N   ALA B 221     -22.013  -6.631 -36.067  1.00 87.63           N  
ANISOU 4881  N   ALA B 221    13901   9584   9810    400    556    -68       N  
ATOM   4882  CA  ALA B 221     -21.853  -5.258 -35.584  1.00 86.86           C  
ANISOU 4882  CA  ALA B 221    13753   9542   9706    435    513    -83       C  
ATOM   4883  C   ALA B 221     -23.179  -4.516 -35.342  1.00 92.38           C  
ANISOU 4883  C   ALA B 221    14465  10328  10309    419    491    -51       C  
ATOM   4884  O   ALA B 221     -23.145  -3.372 -34.885  1.00 92.98           O  
ANISOU 4884  O   ALA B 221    14523  10442  10365    459    452    -64       O  
ATOM   4885  CB  ALA B 221     -20.943  -4.464 -36.510  1.00 87.13           C  
ANISOU 4885  CB  ALA B 221    13754   9550   9802    419    546   -139       C  
ATOM   4886  N   PHE B 222     -24.345  -5.156 -35.597  1.00 88.81           N  
ANISOU 4886  N   PHE B 222    14043   9906   9794    366    512     -6       N  
ATOM   4887  CA  PHE B 222     -25.619  -4.483 -35.347  1.00 87.85           C  
ANISOU 4887  CA  PHE B 222    13911   9882   9588    363    496     32       C  
ATOM   4888  C   PHE B 222     -26.606  -5.329 -34.549  1.00 90.72           C  
ANISOU 4888  C   PHE B 222    14277  10300   9891    350    490    105       C  
ATOM   4889  O   PHE B 222     -26.906  -4.960 -33.418  1.00 90.11           O  
ANISOU 4889  O   PHE B 222    14185  10283   9769    415    463    134       O  
ATOM   4890  CB  PHE B 222     -26.255  -3.936 -36.634  1.00 89.50           C  
ANISOU 4890  CB  PHE B 222    14126  10109   9770    299    522     19       C  
ATOM   4891  CG  PHE B 222     -27.571  -3.219 -36.420  1.00 91.29           C  
ANISOU 4891  CG  PHE B 222    14327  10443   9916    311    504     61       C  
ATOM   4892  CD1 PHE B 222     -27.602  -1.906 -35.965  1.00 93.32           C  
ANISOU 4892  CD1 PHE B 222    14571  10741  10145    390    476     43       C  
ATOM   4893  CD2 PHE B 222     -28.782  -3.857 -36.682  1.00 94.15           C  
ANISOU 4893  CD2 PHE B 222    14679  10865  10230    245    513    121       C  
ATOM   4894  CE1 PHE B 222     -28.816  -1.246 -35.775  1.00 94.17           C  
ANISOU 4894  CE1 PHE B 222    14654  10949  10177    423    467     81       C  
ATOM   4895  CE2 PHE B 222     -29.999  -3.193 -36.484  1.00 96.59           C  
ANISOU 4895  CE2 PHE B 222    14940  11287  10471    268    500    166       C  
ATOM   4896  CZ  PHE B 222     -30.005  -1.894 -36.031  1.00 93.88           C  
ANISOU 4896  CZ  PHE B 222    14584  10986  10102    367    482    145       C  
ATOM   4897  N   VAL B 223     -27.111  -6.444 -35.108  1.00 87.68           N  
ANISOU 4897  N   VAL B 223    13923   9892   9499    264    514    139       N  
ATOM   4898  CA  VAL B 223     -28.116  -7.259 -34.406  1.00 87.68           C  
ANISOU 4898  CA  VAL B 223    13925   9949   9441    227    509    220       C  
ATOM   4899  C   VAL B 223     -27.541  -7.881 -33.096  1.00 91.19           C  
ANISOU 4899  C   VAL B 223    14393  10363   9893    289    486    242       C  
ATOM   4900  O   VAL B 223     -28.141  -7.667 -32.042  1.00 91.25           O  
ANISOU 4900  O   VAL B 223    14379  10452   9840    328    475    291       O  
ATOM   4901  CB  VAL B 223     -28.875  -8.298 -35.295  1.00 91.40           C  
ANISOU 4901  CB  VAL B 223    14433  10399   9894     99    524    258       C  
ATOM   4902  CG1 VAL B 223     -29.472  -7.653 -36.549  1.00 90.99           C  
ANISOU 4902  CG1 VAL B 223    14365  10381   9827     40    532    241       C  
ATOM   4903  CG2 VAL B 223     -28.008  -9.461 -35.679  1.00 91.33           C  
ANISOU 4903  CG2 VAL B 223    14509  10254   9936     69    534    232       C  
ATOM   4904  N   VAL B 224     -26.365  -8.562 -33.152  1.00 87.06           N  
ANISOU 4904  N   VAL B 224    13913   9726   9440    310    479    205       N  
ATOM   4905  CA  VAL B 224     -25.697  -9.190 -31.999  1.00 87.25           C  
ANISOU 4905  CA  VAL B 224    13966   9706   9479    373    445    224       C  
ATOM   4906  C   VAL B 224     -25.467  -8.158 -30.851  1.00 92.98           C  
ANISOU 4906  C   VAL B 224    14656  10494  10178    471    404    219       C  
ATOM   4907  O   VAL B 224     -25.930  -8.448 -29.742  1.00 93.36           O  
ANISOU 4907  O   VAL B 224    14726  10584  10163    494    386    276       O  
ATOM   4908  CB  VAL B 224     -24.418  -9.986 -32.392  1.00 91.02           C  
ANISOU 4908  CB  VAL B 224    14481  10055  10047    398    445    179       C  
ATOM   4909  CG1 VAL B 224     -23.627 -10.423 -31.158  1.00 90.87           C  
ANISOU 4909  CG1 VAL B 224    14481   9997  10049    483    391    196       C  
ATOM   4910  CG2 VAL B 224     -24.759 -11.200 -33.272  1.00 91.03           C  
ANISOU 4910  CG2 VAL B 224    14559   9981  10047    309    480    195       C  
ATOM   4911  N   PRO B 225     -24.858  -6.947 -31.075  1.00 90.13           N  
ANISOU 4911  N   PRO B 225    14254  10141   9850    521    388    157       N  
ATOM   4912  CA  PRO B 225     -24.734  -5.967 -29.974  1.00 90.02           C  
ANISOU 4912  CA  PRO B 225    14233  10176   9794    606    340    152       C  
ATOM   4913  C   PRO B 225     -26.087  -5.553 -29.371  1.00 94.69           C  
ANISOU 4913  C   PRO B 225    14825  10879  10274    617    358    205       C  
ATOM   4914  O   PRO B 225     -26.180  -5.504 -28.151  1.00 96.28           O  
ANISOU 4914  O   PRO B 225    15056  11111  10415    679    329    234       O  
ATOM   4915  CB  PRO B 225     -24.025  -4.776 -30.632  1.00 91.04           C  
ANISOU 4915  CB  PRO B 225    14329  10287   9975    623    327     81       C  
ATOM   4916  CG  PRO B 225     -23.377  -5.323 -31.822  1.00 94.97           C  
ANISOU 4916  CG  PRO B 225    14812  10713  10561    568    366     47       C  
ATOM   4917  CD  PRO B 225     -24.245  -6.413 -32.309  1.00 90.94           C  
ANISOU 4917  CD  PRO B 225    14330  10201  10020    497    413     91       C  
ATOM   4918  N   ILE B 226     -27.135  -5.299 -30.201  1.00 89.83           N  
ANISOU 4918  N   ILE B 226    14177  10328   9626    562    405    222       N  
ATOM   4919  CA  ILE B 226     -28.482  -4.948 -29.717  1.00 89.56           C  
ANISOU 4919  CA  ILE B 226    14117  10417   9493    577    432    280       C  
ATOM   4920  C   ILE B 226     -29.013  -6.061 -28.822  1.00 94.96           C  
ANISOU 4920  C   ILE B 226    14822  11133  10128    552    447    361       C  
ATOM   4921  O   ILE B 226     -29.392  -5.781 -27.686  1.00 95.58           O  
ANISOU 4921  O   ILE B 226    14912  11278  10128    621    448    395       O  
ATOM   4922  CB  ILE B 226     -29.492  -4.602 -30.853  1.00 92.07           C  
ANISOU 4922  CB  ILE B 226    14384  10800   9799    515    469    291       C  
ATOM   4923  CG1 ILE B 226     -29.114  -3.294 -31.544  1.00 91.19           C  
ANISOU 4923  CG1 ILE B 226    14267  10670   9709    557    453    220       C  
ATOM   4924  CG2 ILE B 226     -30.950  -4.531 -30.323  1.00 93.26           C  
ANISOU 4924  CG2 ILE B 226    14484  11093   9858    524    505    371       C  
ATOM   4925  CD1 ILE B 226     -29.652  -3.168 -32.858  1.00 93.15           C  
ANISOU 4925  CD1 ILE B 226    14489  10932   9972    483    474    216       C  
ATOM   4926  N   LEU B 227     -29.005  -7.317 -29.324  1.00 91.56           N  
ANISOU 4926  N   LEU B 227    14410  10645   9735    454    458    391       N  
ATOM   4927  CA  LEU B 227     -29.477  -8.506 -28.597  1.00 91.89           C  
ANISOU 4927  CA  LEU B 227    14487  10695   9733    405    467    474       C  
ATOM   4928  C   LEU B 227     -28.815  -8.643 -27.233  1.00 94.64           C  
ANISOU 4928  C   LEU B 227    14893  11014  10054    492    431    482       C  
ATOM   4929  O   LEU B 227     -29.521  -8.720 -26.227  1.00 95.06           O  
ANISOU 4929  O   LEU B 227    14954  11147  10016    512    450    548       O  
ATOM   4930  CB  LEU B 227     -29.299  -9.779 -29.437  1.00 91.98           C  
ANISOU 4930  CB  LEU B 227    14543  10608   9798    294    469    485       C  
ATOM   4931  CG  LEU B 227     -30.475 -10.215 -30.331  1.00 96.94           C  
ANISOU 4931  CG  LEU B 227    15140  11289  10404    162    500    536       C  
ATOM   4932  CD1 LEU B 227     -31.063  -9.057 -31.143  1.00 96.26           C  
ANISOU 4932  CD1 LEU B 227    14971  11291  10313    168    517    508       C  
ATOM   4933  CD2 LEU B 227     -30.044 -11.310 -31.289  1.00100.13           C  
ANISOU 4933  CD2 LEU B 227    15619  11562  10863     69    491    519       C  
ATOM   4934  N   ILE B 228     -27.473  -8.564 -27.190  1.00 88.68           N  
ANISOU 4934  N   ILE B 228    14171  10153   9370    551    378    417       N  
ATOM   4935  CA  ILE B 228     -26.722  -8.637 -25.941  1.00 87.62           C  
ANISOU 4935  CA  ILE B 228    14092   9981   9216    636    321    419       C  
ATOM   4936  C   ILE B 228     -27.094  -7.489 -24.997  1.00 92.39           C  
ANISOU 4936  C   ILE B 228    14697  10677   9730    725    314    418       C  
ATOM   4937  O   ILE B 228     -27.435  -7.771 -23.850  1.00 94.01           O  
ANISOU 4937  O   ILE B 228    14954  10918   9848    757    311    473       O  
ATOM   4938  CB  ILE B 228     -25.197  -8.765 -26.166  1.00 89.48           C  
ANISOU 4938  CB  ILE B 228    14340  10098   9562    678    260    353       C  
ATOM   4939  CG1 ILE B 228     -24.864 -10.060 -26.943  1.00 88.70           C  
ANISOU 4939  CG1 ILE B 228    14266   9901   9534    612    276    360       C  
ATOM   4940  CG2 ILE B 228     -24.438  -8.707 -24.824  1.00 90.50           C  
ANISOU 4940  CG2 ILE B 228    14522  10198   9667    769    181    357       C  
ATOM   4941  CD1 ILE B 228     -23.533 -10.036 -27.586  1.00 91.41           C  
ANISOU 4941  CD1 ILE B 228    14585  10150   9996    649    250    288       C  
ATOM   4942  N   ILE B 229     -27.077  -6.221 -25.472  1.00 87.59           N  
ANISOU 4942  N   ILE B 229    14047  10102   9131    764    314    358       N  
ATOM   4943  CA  ILE B 229     -27.397  -5.054 -24.633  1.00 87.29           C  
ANISOU 4943  CA  ILE B 229    14031  10134   9002    860    304    345       C  
ATOM   4944  C   ILE B 229     -28.873  -5.102 -24.142  1.00 93.80           C  
ANISOU 4944  C   ILE B 229    14839  11091   9710    864    382    423       C  
ATOM   4945  O   ILE B 229     -29.140  -4.734 -22.998  1.00 94.12           O  
ANISOU 4945  O   ILE B 229    14933  11181   9649    947    383    444       O  
ATOM   4946  CB  ILE B 229     -26.988  -3.716 -25.325  1.00 89.41           C  
ANISOU 4946  CB  ILE B 229    14275  10386   9309    895    280    263       C  
ATOM   4947  CG1 ILE B 229     -25.454  -3.663 -25.549  1.00 89.14           C  
ANISOU 4947  CG1 ILE B 229    14250  10236   9383    895    202    199       C  
ATOM   4948  CG2 ILE B 229     -27.444  -2.470 -24.526  1.00 90.74           C  
ANISOU 4948  CG2 ILE B 229    14487  10618   9370   1000    272    249       C  
ATOM   4949  CD1 ILE B 229     -24.974  -2.661 -26.633  1.00 91.12           C  
ANISOU 4949  CD1 ILE B 229    14462  10456   9705    877    193    128       C  
ATOM   4950  N   THR B 230     -29.799  -5.618 -24.977  1.00 92.29           N  
ANISOU 4950  N   THR B 230    14577  10957   9532    772    445    470       N  
ATOM   4951  CA  THR B 230     -31.228  -5.765 -24.674  1.00 93.38           C  
ANISOU 4951  CA  THR B 230    14665  11235   9580    753    523    555       C  
ATOM   4952  C   THR B 230     -31.440  -6.862 -23.636  1.00 99.81           C  
ANISOU 4952  C   THR B 230    15529  12060  10332    723    539    639       C  
ATOM   4953  O   THR B 230     -32.256  -6.674 -22.733  1.00101.18           O  
ANISOU 4953  O   THR B 230    15701  12343  10398    771    593    698       O  
ATOM   4954  CB  THR B 230     -32.020  -6.005 -25.964  1.00104.82           C  
ANISOU 4954  CB  THR B 230    16021  12729  11075    646    561    579       C  
ATOM   4955  OG1 THR B 230     -31.822  -4.889 -26.834  1.00104.30           O  
ANISOU 4955  OG1 THR B 230    15926  12654  11051    687    544    503       O  
ATOM   4956  CG2 THR B 230     -33.509  -6.222 -25.723  1.00106.03           C  
ANISOU 4956  CG2 THR B 230    16094  13041  11151    611    636    678       C  
ATOM   4957  N   VAL B 231     -30.718  -8.004 -23.756  1.00 97.06           N  
ANISOU 4957  N   VAL B 231    15234  11597  10047    649    498    648       N  
ATOM   4958  CA  VAL B 231     -30.805  -9.105 -22.787  1.00 98.21           C  
ANISOU 4958  CA  VAL B 231    15452  11727  10137    616    500    728       C  
ATOM   4959  C   VAL B 231     -30.223  -8.579 -21.472  1.00104.02           C  
ANISOU 4959  C   VAL B 231    16274  12450  10800    743    459    708       C  
ATOM   4960  O   VAL B 231     -30.811  -8.809 -20.413  1.00104.86           O  
ANISOU 4960  O   VAL B 231    16424  12625  10795    763    497    780       O  
ATOM   4961  CB  VAL B 231     -30.139 -10.427 -23.279  1.00102.51           C  
ANISOU 4961  CB  VAL B 231    16049  12133  10765    522    458    736       C  
ATOM   4962  CG1 VAL B 231     -30.051 -11.476 -22.161  1.00103.08           C  
ANISOU 4962  CG1 VAL B 231    16225  12166  10775    508    441    813       C  
ATOM   4963  CG2 VAL B 231     -30.874 -11.005 -24.495  1.00102.20           C  
ANISOU 4963  CG2 VAL B 231    15951  12109  10772    384    497    765       C  
ATOM   4964  N   CYS B 232     -29.127  -7.789 -21.561  1.00100.75           N  
ANISOU 4964  N   CYS B 232    15883  11956  10441    825    385    613       N  
ATOM   4965  CA  CYS B 232     -28.481  -7.152 -20.414  1.00100.95           C  
ANISOU 4965  CA  CYS B 232    15996  11959  10403    940    323    582       C  
ATOM   4966  C   CYS B 232     -29.468  -6.231 -19.708  1.00105.40           C  
ANISOU 4966  C   CYS B 232    16566  12650  10830   1021    387    602       C  
ATOM   4967  O   CYS B 232     -29.625  -6.355 -18.495  1.00107.20           O  
ANISOU 4967  O   CYS B 232    16882  12904  10944   1075    391    644       O  
ATOM   4968  CB  CYS B 232     -27.208  -6.413 -20.827  1.00100.51           C  
ANISOU 4968  CB  CYS B 232    15941  11805  10443    987    230    481       C  
ATOM   4969  SG  CYS B 232     -25.765  -7.488 -21.069  1.00104.33           S  
ANISOU 4969  SG  CYS B 232    16445  12135  11059    951    139    462       S  
ATOM   4970  N   TYR B 233     -30.182  -5.366 -20.469  1.00100.51           N  
ANISOU 4970  N   TYR B 233    15860  12113  10216   1033    443    578       N  
ATOM   4971  CA  TYR B 233     -31.180  -4.433 -19.932  1.00100.67           C  
ANISOU 4971  CA  TYR B 233    15875  12261  10115   1128    515    593       C  
ATOM   4972  C   TYR B 233     -32.286  -5.148 -19.133  1.00106.58           C  
ANISOU 4972  C   TYR B 233    16614  13129  10752   1109    613    706       C  
ATOM   4973  O   TYR B 233     -32.443  -4.881 -17.937  1.00105.56           O  
ANISOU 4973  O   TYR B 233    16574  13038  10495   1202    633    725       O  
ATOM   4974  CB  TYR B 233     -31.760  -3.520 -21.034  1.00100.78           C  
ANISOU 4974  CB  TYR B 233    15787  12335  10169   1137    553    556       C  
ATOM   4975  CG  TYR B 233     -32.831  -2.575 -20.525  1.00103.98           C  
ANISOU 4975  CG  TYR B 233    16179  12875  10452   1253    632    575       C  
ATOM   4976  CD1 TYR B 233     -32.512  -1.517 -19.671  1.00106.54           C  
ANISOU 4976  CD1 TYR B 233    16617  13180  10684   1397    602    518       C  
ATOM   4977  CD2 TYR B 233     -34.168  -2.756 -20.866  1.00105.34           C  
ANISOU 4977  CD2 TYR B 233    16228  13197  10598   1224    735    651       C  
ATOM   4978  CE1 TYR B 233     -33.500  -0.680 -19.150  1.00106.96           C  
ANISOU 4978  CE1 TYR B 233    16674  13352  10614   1525    685    533       C  
ATOM   4979  CE2 TYR B 233     -35.162  -1.906 -20.373  1.00107.33           C  
ANISOU 4979  CE2 TYR B 233    16457  13585  10740   1350    819    673       C  
ATOM   4980  CZ  TYR B 233     -34.823  -0.868 -19.516  1.00111.97           C  
ANISOU 4980  CZ  TYR B 233    17170  14144  11230   1509    799    610       C  
ATOM   4981  OH  TYR B 233     -35.796  -0.039 -19.011  1.00109.76           O  
ANISOU 4981  OH  TYR B 233    16881  13991  10832   1653    889    627       O  
ATOM   4982  N   GLY B 234     -32.980  -6.080 -19.791  1.00105.22           N  
ANISOU 4982  N   GLY B 234    16347  13006  10626    979    667    779       N  
ATOM   4983  CA  GLY B 234     -34.060  -6.878 -19.214  1.00106.86           C  
ANISOU 4983  CA  GLY B 234    16523  13331  10749    920    761    899       C  
ATOM   4984  C   GLY B 234     -33.731  -7.668 -17.957  1.00112.35           C  
ANISOU 4984  C   GLY B 234    17344  13984  11358    921    749    954       C  
ATOM   4985  O   GLY B 234     -34.615  -7.868 -17.122  1.00113.21           O  
ANISOU 4985  O   GLY B 234    17455  14212  11349    931    840   1042       O  
ATOM   4986  N   LEU B 235     -32.471  -8.152 -17.816  1.00108.57           N  
ANISOU 4986  N   LEU B 235    16971  13343  10937    912    639    910       N  
ATOM   4987  CA  LEU B 235     -32.027  -8.923 -16.644  1.00109.12           C  
ANISOU 4987  CA  LEU B 235    17179  13351  10931    919    604    958       C  
ATOM   4988  C   LEU B 235     -31.719  -8.005 -15.475  1.00116.83           C  
ANISOU 4988  C   LEU B 235    18266  14337  11786   1072    581    919       C  
ATOM   4989  O   LEU B 235     -32.063  -8.317 -14.331  1.00117.63           O  
ANISOU 4989  O   LEU B 235    18460  14480  11753   1099    620    987       O  
ATOM   4990  CB  LEU B 235     -30.833  -9.831 -16.968  1.00107.97           C  
ANISOU 4990  CB  LEU B 235    17095  13031  10897    861    491    932       C  
ATOM   4991  CG  LEU B 235     -31.129 -11.026 -17.876  1.00111.29           C  
ANISOU 4991  CG  LEU B 235    17464  13418  11405    706    511    986       C  
ATOM   4992  CD1 LEU B 235     -29.857 -11.672 -18.352  1.00110.57           C  
ANISOU 4992  CD1 LEU B 235    17425  13151  11435    689    404    932       C  
ATOM   4993  CD2 LEU B 235     -32.027 -12.038 -17.200  1.00113.46           C  
ANISOU 4993  CD2 LEU B 235    17775  13751  11581    614    579   1116       C  
ATOM   4994  N   MET B 236     -31.113  -6.841 -15.779  1.00115.21           N  
ANISOU 4994  N   MET B 236    18062  14093  11621   1165    520    812       N  
ATOM   4995  CA  MET B 236     -30.815  -5.761 -14.836  1.00116.02           C  
ANISOU 4995  CA  MET B 236    18276  14193  11612   1311    486    756       C  
ATOM   4996  C   MET B 236     -32.147  -5.218 -14.272  1.00122.03           C  
ANISOU 4996  C   MET B 236    19023  15122  12222   1386    628    807       C  
ATOM   4997  O   MET B 236     -32.225  -4.808 -13.111  1.00122.40           O  
ANISOU 4997  O   MET B 236    19197  15191  12119   1492    641    811       O  
ATOM   4998  CB  MET B 236     -30.036  -4.651 -15.564  1.00117.13           C  
ANISOU 4998  CB  MET B 236    18396  14261  11846   1361    401    638       C  
ATOM   4999  CG  MET B 236     -28.540  -4.880 -15.593  1.00120.03           C  
ANISOU 4999  CG  MET B 236    18821  14471  12315   1343    249    581       C  
ATOM   5000  SD  MET B 236     -27.626  -3.444 -16.212  1.00122.98           S  
ANISOU 5000  SD  MET B 236    19188  14770  12769   1400    150    452       S  
ATOM   5001  CE  MET B 236     -27.500  -3.869 -17.871  1.00118.27           C  
ANISOU 5001  CE  MET B 236    18429  14152  12356   1284    173    437       C  
ATOM   5002  N   LEU B 237     -33.195  -5.271 -15.113  1.00119.64           N  
ANISOU 5002  N   LEU B 237    18561  14938  11960   1329    733    851       N  
ATOM   5003  CA  LEU B 237     -34.566  -4.865 -14.842  1.00120.99           C  
ANISOU 5003  CA  LEU B 237    18658  15291  12022   1385    881    912       C  
ATOM   5004  C   LEU B 237     -35.239  -5.831 -13.856  1.00127.74           C  
ANISOU 5004  C   LEU B 237    19545  16231  12759   1339    973   1036       C  
ATOM   5005  O   LEU B 237     -35.880  -5.370 -12.909  1.00128.46           O  
ANISOU 5005  O   LEU B 237    19685  16429  12696   1449   1068   1068       O  
ATOM   5006  CB  LEU B 237     -35.334  -4.827 -16.175  1.00120.26           C  
ANISOU 5006  CB  LEU B 237    18371  15283  12040   1306    934    929       C  
ATOM   5007  CG  LEU B 237     -36.604  -4.006 -16.219  1.00125.52           C  
ANISOU 5007  CG  LEU B 237    18928  16130  12632   1399   1060    958       C  
ATOM   5008  CD1 LEU B 237     -36.304  -2.567 -16.604  1.00124.83           C  
ANISOU 5008  CD1 LEU B 237    18866  16006  12557   1538   1015    843       C  
ATOM   5009  CD2 LEU B 237     -37.591  -4.614 -17.189  1.00128.04           C  
ANISOU 5009  CD2 LEU B 237    19053  16564  13033   1264   1126   1040       C  
ATOM   5010  N   LEU B 238     -35.100  -7.162 -14.083  1.00125.43           N  
ANISOU 5010  N   LEU B 238    19235  15888  12533   1178    950   1107       N  
ATOM   5011  CA  LEU B 238     -35.681  -8.203 -13.221  1.00127.52           C  
ANISOU 5011  CA  LEU B 238    19540  16215  12696   1103   1027   1234       C  
ATOM   5012  C   LEU B 238     -35.062  -8.162 -11.830  1.00134.81           C  
ANISOU 5012  C   LEU B 238    20671  17071  13480   1201    987   1227       C  
ATOM   5013  O   LEU B 238     -35.783  -8.285 -10.837  1.00135.32           O  
ANISOU 5013  O   LEU B 238    20784  17243  13388   1234   1094   1310       O  
ATOM   5014  CB  LEU B 238     -35.544  -9.603 -13.845  1.00127.26           C  
ANISOU 5014  CB  LEU B 238    19475  16106  12770    910    986   1299       C  
ATOM   5015  CG  LEU B 238     -36.463  -9.888 -15.039  1.00132.10           C  
ANISOU 5015  CG  LEU B 238    19896  16815  13482    780   1047   1345       C  
ATOM   5016  CD1 LEU B 238     -35.837 -10.884 -16.005  1.00131.20           C  
ANISOU 5016  CD1 LEU B 238    19784  16554  13514    631    950   1335       C  
ATOM   5017  CD2 LEU B 238     -37.837 -10.353 -14.592  1.00136.95           C  
ANISOU 5017  CD2 LEU B 238    20421  17615  14000    704   1192   1488       C  
ATOM   5018  N   ARG B 239     -33.730  -7.935 -11.770  1.00133.28           N  
ANISOU 5018  N   ARG B 239    20594  16707  13340   1250    831   1130       N  
ATOM   5019  CA  ARG B 239     -32.941  -7.798 -10.546  1.00135.04           C  
ANISOU 5019  CA  ARG B 239    21021  16840  13448   1345    750   1105       C  
ATOM   5020  C   ARG B 239     -33.509  -6.659  -9.700  1.00142.97           C  
ANISOU 5020  C   ARG B 239    22093  17948  14279   1506    834   1083       C  
ATOM   5021  O   ARG B 239     -33.694  -6.838  -8.493  1.00144.79           O  
ANISOU 5021  O   ARG B 239    22467  18206  14342   1556    874   1135       O  
ATOM   5022  CB  ARG B 239     -31.450  -7.574 -10.892  1.00134.08           C  
ANISOU 5022  CB  ARG B 239    20958  16537  13448   1365    564    997       C  
ATOM   5023  CG  ARG B 239     -30.584  -6.956  -9.790  1.00142.40           C  
ANISOU 5023  CG  ARG B 239    22204  17505  14397   1488    453    937       C  
ATOM   5024  CD  ARG B 239     -30.040  -7.959  -8.787  1.00151.60           C  
ANISOU 5024  CD  ARG B 239    23527  18585  15491   1461    379   1001       C  
ATOM   5025  NE  ARG B 239     -29.255  -7.265  -7.763  1.00161.24           N  
ANISOU 5025  NE  ARG B 239    24931  19728  16603   1579    263    941       N  
ATOM   5026  CZ  ARG B 239     -28.495  -7.857  -6.849  1.00173.66           C  
ANISOU 5026  CZ  ARG B 239    26666  21200  18119   1584    146    968       C  
ATOM   5027  NH1 ARG B 239     -28.400  -9.179  -6.806  1.00160.17           N1+
ANISOU 5027  NH1 ARG B 239    24965  19446  16448   1486    134   1054       N1+
ATOM   5028  NH2 ARG B 239     -27.824  -7.128  -5.967  1.00158.75           N  
ANISOU 5028  NH2 ARG B 239    24943  19246  16128   1687     32    909       N  
ATOM   5029  N   LEU B 240     -33.829  -5.517 -10.345  1.00140.14           N  
ANISOU 5029  N   LEU B 240    21643  17648  13956   1588    867   1009       N  
ATOM   5030  CA  LEU B 240     -34.430  -4.340  -9.713  1.00141.76           C  
ANISOU 5030  CA  LEU B 240    21906  17949  14008   1758    953    976       C  
ATOM   5031  C   LEU B 240     -35.853  -4.620  -9.203  1.00149.96           C  
ANISOU 5031  C   LEU B 240    22875  19187  14915   1770   1155   1094       C  
ATOM   5032  O   LEU B 240     -36.213  -4.154  -8.121  1.00150.65           O  
ANISOU 5032  O   LEU B 240    23088  19336  14817   1900   1232   1105       O  
ATOM   5033  CB  LEU B 240     -34.452  -3.188 -10.714  1.00140.72           C  
ANISOU 5033  CB  LEU B 240    21677  17821  13968   1823    935    879       C  
ATOM   5034  CG  LEU B 240     -33.486  -2.047 -10.466  1.00145.11           C  
ANISOU 5034  CG  LEU B 240    22388  18249  14501   1942    804    751       C  
ATOM   5035  CD1 LEU B 240     -32.030  -2.490 -10.640  1.00144.23           C  
ANISOU 5035  CD1 LEU B 240    22341  17953  14508   1856    615    701       C  
ATOM   5036  CD2 LEU B 240     -33.798  -0.899 -11.393  1.00147.04           C  
ANISOU 5036  CD2 LEU B 240    22539  18523  14807   2012    821    676       C  
ATOM   5037  N   ARG B 241     -36.650  -5.387  -9.983  1.00148.91           N  
ANISOU 5037  N   ARG B 241    22545  19157  14877   1632   1240   1183       N  
ATOM   5038  CA  ARG B 241     -38.020  -5.777  -9.639  1.00151.26           C  
ANISOU 5038  CA  ARG B 241    22733  19659  15080   1607   1430   1312       C  
ATOM   5039  C   ARG B 241     -38.027  -6.765  -8.463  1.00158.67           C  
ANISOU 5039  C   ARG B 241    23809  20594  15884   1550   1466   1413       C  
ATOM   5040  O   ARG B 241     -38.939  -6.713  -7.634  1.00160.45           O  
ANISOU 5040  O   ARG B 241    24040  20973  15951   1609   1625   1495       O  
ATOM   5041  CB  ARG B 241     -38.742  -6.370 -10.860  1.00151.63           C  
ANISOU 5041  CB  ARG B 241    22539  19794  15279   1447   1474   1378       C  
ATOM   5042  CG  ARG B 241     -40.262  -6.342 -10.737  1.00166.35           C  
ANISOU 5042  CG  ARG B 241    24231  21903  17070   1453   1670   1492       C  
ATOM   5043  CD  ARG B 241     -40.958  -6.952 -11.939  1.00178.08           C  
ANISOU 5043  CD  ARG B 241    25485  23472  18707   1277   1690   1562       C  
ATOM   5044  NE  ARG B 241     -42.346  -7.304 -11.626  1.00188.91           N  
ANISOU 5044  NE  ARG B 241    26697  25075  20004   1230   1868   1707       N  
ATOM   5045  CZ  ARG B 241     -43.400  -6.543 -11.904  1.00202.19           C  
ANISOU 5045  CZ  ARG B 241    28197  26954  21674   1324   1988   1731       C  
ATOM   5046  NH1 ARG B 241     -43.244  -5.379 -12.524  1.00187.94           N1+
ANISOU 5046  NH1 ARG B 241    26360  25128  19919   1471   1945   1616       N1+
ATOM   5047  NH2 ARG B 241     -44.620  -6.945 -11.573  1.00189.14           N  
ANISOU 5047  NH2 ARG B 241    26386  25520  19958   1270   2151   1874       N  
ATOM   5048  N   SER B 242     -36.996  -7.638  -8.378  1.00155.69           N  
ANISOU 5048  N   SER B 242    23548  20041  15565   1447   1322   1409       N  
ATOM   5049  CA  SER B 242     -36.830  -8.627  -7.302  1.00157.24           C  
ANISOU 5049  CA  SER B 242    23903  20196  15643   1388   1323   1501       C  
ATOM   5050  C   SER B 242     -36.527  -7.991  -5.930  1.00163.53           C  
ANISOU 5050  C   SER B 242    24927  20972  16234   1556   1324   1467       C  
ATOM   5051  O   SER B 242     -36.710  -8.659  -4.909  1.00164.62           O  
ANISOU 5051  O   SER B 242    25194  21127  16227   1529   1375   1560       O  
ATOM   5052  CB  SER B 242     -35.755  -9.649  -7.664  1.00159.48           C  
ANISOU 5052  CB  SER B 242    24251  20286  16056   1257   1155   1493       C  
ATOM   5053  OG  SER B 242     -36.263 -10.674  -8.504  1.00166.32           O  
ANISOU 5053  OG  SER B 242    24973  21183  17040   1071   1190   1580       O  
ATOM   5054  N   VAL B 243     -36.077  -6.706  -5.908  1.00160.50           N  
ANISOU 5054  N   VAL B 243    24607  20546  15830   1722   1266   1338       N  
ATOM   5055  CA  VAL B 243     -35.750  -5.942  -4.691  1.00161.81           C  
ANISOU 5055  CA  VAL B 243    25006  20675  15798   1891   1248   1285       C  
ATOM   5056  C   VAL B 243     -37.003  -5.796  -3.802  1.00168.66           C  
ANISOU 5056  C   VAL B 243    25888  21738  16456   1974   1472   1376       C  
ATOM   5057  O   VAL B 243     -37.995  -5.191  -4.223  1.00168.75           O  
ANISOU 5057  O   VAL B 243    25738  21912  16469   2039   1620   1385       O  
ATOM   5058  CB  VAL B 243     -35.058  -4.573  -4.993  1.00164.61           C  
ANISOU 5058  CB  VAL B 243    25419  20938  16187   2032   1134   1128       C  
ATOM   5059  CG1 VAL B 243     -34.790  -3.779  -3.715  1.00165.71           C  
ANISOU 5059  CG1 VAL B 243    25820  21036  16106   2202   1113   1075       C  
ATOM   5060  CG2 VAL B 243     -33.763  -4.764  -5.781  1.00162.53           C  
ANISOU 5060  CG2 VAL B 243    25140  20490  16122   1944    920   1049       C  
ATOM   5061  N   ARG B 244     -36.937  -6.384  -2.584  1.00167.00           N  
ANISOU 5061  N   ARG B 244    25870  21511  16069   1972   1496   1448       N  
ATOM   5062  CA  ARG B 244     -37.981  -6.421  -1.545  1.00197.72           C  
ANISOU 5062  CA  ARG B 244    29818  25571  19734   2040   1707   1548       C  
ATOM   5063  C   ARG B 244     -39.258  -7.108  -2.022  1.00236.19           C  
ANISOU 5063  C   ARG B 244    34438  30649  24655   1915   1901   1688       C  
ATOM   5064  O   ARG B 244     -39.197  -8.218  -2.548  1.00198.48           O  
ANISOU 5064  O   ARG B 244    29566  25840  20007   1717   1858   1766       O  
ATOM   5065  CB  ARG B 244     -38.280  -5.024  -0.942  1.00198.36           C  
ANISOU 5065  CB  ARG B 244    30013  25711  19643   2282   1788   1461       C  
ATOM   5066  CG  ARG B 244     -37.055  -4.219  -0.478  1.00205.61           C  
ANISOU 5066  CG  ARG B 244    31190  26428  20506   2401   1586   1318       C  
ATOM   5067  CD  ARG B 244     -36.477  -4.677   0.855  1.00213.28           C  
ANISOU 5067  CD  ARG B 244    32455  27299  21285   2413   1517   1348       C  
ATOM   5068  NE  ARG B 244     -35.659  -5.885   0.722  1.00216.17           N  
ANISOU 5068  NE  ARG B 244    32835  27530  21768   2231   1360   1398       N  
ATOM   5069  CZ  ARG B 244     -34.359  -5.891   0.441  1.00226.28           C  
ANISOU 5069  CZ  ARG B 244    34189  28613  23173   2196   1115   1312       C  
ATOM   5070  NH1 ARG B 244     -33.704  -4.749   0.266  1.00212.66           N  
ANISOU 5070  NH1 ARG B 244    32532  26797  21473   2311    991   1172       N  
ATOM   5071  NH2 ARG B 244     -33.703  -7.038   0.335  1.00210.60           N  
ANISOU 5071  NH2 ARG B 244    32209  26520  21289   2047    992   1367       N  
ATOM   5072  N   LYS B 250     -31.726   2.975   0.443  1.00180.77           N  
ANISOU 5072  N   LYS B 250    29214  22325  17147   3088    526    425       N  
ATOM   5073  CA  LYS B 250     -32.657   3.908  -0.189  1.00180.57           C  
ANISOU 5073  CA  LYS B 250    29084  22401  17124   3212    683    385       C  
ATOM   5074  C   LYS B 250     -32.019   4.612  -1.385  1.00182.74           C  
ANISOU 5074  C   LYS B 250    29243  22577  17613   3159    538    290       C  
ATOM   5075  O   LYS B 250     -32.611   4.630  -2.466  1.00180.65           O  
ANISOU 5075  O   LYS B 250    28727  22410  17502   3131    639    309       O  
ATOM   5076  CB  LYS B 250     -33.183   4.929   0.830  1.00185.29           C  
ANISOU 5076  CB  LYS B 250    29958  23007  17437   3437    771    330       C  
ATOM   5077  N   GLU B 251     -30.813   5.189  -1.185  1.00179.84           N  
ANISOU 5077  N   GLU B 251    29060  22017  17254   3137    297    195       N  
ATOM   5078  CA  GLU B 251     -30.050   5.897  -2.218  1.00178.39           C  
ANISOU 5078  CA  GLU B 251    28799  21721  17261   3073    138    105       C  
ATOM   5079  C   GLU B 251     -29.171   4.920  -3.013  1.00180.60           C  
ANISOU 5079  C   GLU B 251    28866  21957  17796   2864     12    142       C  
ATOM   5080  O   GLU B 251     -29.059   5.058  -4.238  1.00178.52           O  
ANISOU 5080  O   GLU B 251    28396  21696  17737   2788      0    121       O  
ATOM   5081  CB  GLU B 251     -29.220   7.038  -1.600  1.00180.77           C  
ANISOU 5081  CB  GLU B 251    29402  21842  17440   3143    -57    -11       C  
ATOM   5082  CG  GLU B 251     -29.036   8.236  -2.523  1.00189.71           C  
ANISOU 5082  CG  GLU B 251    30511  22900  18671   3167   -123   -110       C  
ATOM   5083  CD  GLU B 251     -28.943   9.589  -1.839  1.00208.82           C  
ANISOU 5083  CD  GLU B 251    33257  25200  20886   3319   -198   -216       C  
ATOM   5084  OE1 GLU B 251     -28.128   9.734  -0.899  1.00203.01           O  
ANISOU 5084  OE1 GLU B 251    32774  24331  20029   3308   -374   -253       O  
ATOM   5085  OE2 GLU B 251     -29.680  10.513  -2.254  1.00200.67           O  
ANISOU 5085  OE2 GLU B 251    32234  24198  19811   3450    -90   -263       O  
ATOM   5086  N   LYS B 252     -28.577   3.915  -2.317  1.00177.28           N  
ANISOU 5086  N   LYS B 252    28504  21496  17357   2781    -75    201       N  
ATOM   5087  CA  LYS B 252     -27.745   2.857  -2.913  1.00175.49           C  
ANISOU 5087  CA  LYS B 252    28101  21228  17351   2605   -187    246       C  
ATOM   5088  C   LYS B 252     -28.613   1.890  -3.743  1.00177.17           C  
ANISOU 5088  C   LYS B 252    28041  21587  17690   2530      0    340       C  
ATOM   5089  O   LYS B 252     -28.118   1.255  -4.676  1.00174.87           O  
ANISOU 5089  O   LYS B 252    27555  21272  17615   2397    -57    357       O  
ATOM   5090  CB  LYS B 252     -26.992   2.088  -1.816  1.00179.10           C  
ANISOU 5090  CB  LYS B 252    28725  21603  17720   2566   -324    288       C  
ATOM   5091  N   ASP B 253     -29.910   1.796  -3.385  1.00174.00           N  
ANISOU 5091  N   ASP B 253    27630  21338  17144   2617    222    402       N  
ATOM   5092  CA  ASP B 253     -30.937   0.977  -4.029  1.00172.60           C  
ANISOU 5092  CA  ASP B 253    27213  21321  17047   2555    416    501       C  
ATOM   5093  C   ASP B 253     -31.342   1.593  -5.373  1.00171.99           C  
ANISOU 5093  C   ASP B 253    26925  21294  17128   2550    472    458       C  
ATOM   5094  O   ASP B 253     -31.564   0.853  -6.329  1.00170.22           O  
ANISOU 5094  O   ASP B 253    26474  21126  17075   2428    519    511       O  
ATOM   5095  CB  ASP B 253     -32.171   0.833  -3.105  1.00176.78           C  
ANISOU 5095  CB  ASP B 253    27810  22004  17353   2662    633    580       C  
ATOM   5096  CG  ASP B 253     -31.893   0.440  -1.651  1.00192.75           C  
ANISOU 5096  CG  ASP B 253    30090  23981  19166   2699    597    616       C  
ATOM   5097  OD1 ASP B 253     -30.757   0.001  -1.354  1.00194.36           O  
ANISOU 5097  OD1 ASP B 253    30393  24041  19415   2617    399    603       O  
ATOM   5098  OD2 ASP B 253     -32.816   0.570  -0.812  1.00199.68           O  
ANISOU 5098  OD2 ASP B 253    31068  24970  19830   2814    768    661       O  
ATOM   5099  N   ARG B 254     -31.436   2.939  -5.446  1.00166.88           N  
ANISOU 5099  N   ARG B 254    26370  20619  16419   2680    460    362       N  
ATOM   5100  CA  ARG B 254     -31.796   3.661  -6.673  1.00164.75           C  
ANISOU 5100  CA  ARG B 254    25934  20382  16281   2691    499    316       C  
ATOM   5101  C   ARG B 254     -30.566   4.077  -7.505  1.00165.06           C  
ANISOU 5101  C   ARG B 254    25953  20262  16501   2596    295    228       C  
ATOM   5102  O   ARG B 254     -30.726   4.528  -8.645  1.00163.47           O  
ANISOU 5102  O   ARG B 254    25603  20073  16433   2571    311    196       O  
ATOM   5103  CB  ARG B 254     -32.730   4.855  -6.387  1.00166.17           C  
ANISOU 5103  CB  ARG B 254    26208  20633  16297   2894    623    273       C  
ATOM   5104  CG  ARG B 254     -34.134   4.461  -5.901  1.00178.26           C  
ANISOU 5104  CG  ARG B 254    27670  22367  17693   2985    866    371       C  
ATOM   5105  CD  ARG B 254     -35.037   3.897  -6.993  1.00186.66           C  
ANISOU 5105  CD  ARG B 254    28422  23590  18911   2903   1003    452       C  
ATOM   5106  NE  ARG B 254     -35.675   4.950  -7.786  1.00194.40           N  
ANISOU 5106  NE  ARG B 254    29315  24624  19925   3014   1065    402       N  
ATOM   5107  CZ  ARG B 254     -36.539   4.731  -8.774  1.00204.71           C  
ANISOU 5107  CZ  ARG B 254    30362  26068  21351   2974   1175    459       C  
ATOM   5108  NH1 ARG B 254     -36.879   3.491  -9.106  1.00190.38           N  
ANISOU 5108  NH1 ARG B 254    28352  24350  19633   2815   1238    567       N  
ATOM   5109  NH2 ARG B 254     -37.070   5.751  -9.437  1.00188.14           N  
ANISOU 5109  NH2 ARG B 254    28208  24006  19272   3090   1215    410       N  
ATOM   5110  N   SER B 255     -29.343   3.887  -6.948  1.00159.73           N  
ANISOU 5110  N   SER B 255    25417  19443  15830   2537    105    197       N  
ATOM   5111  CA  SER B 255     -28.064   4.154  -7.628  1.00157.02           C  
ANISOU 5111  CA  SER B 255    25043  18956  15662   2432    -93    128       C  
ATOM   5112  C   SER B 255     -27.854   3.137  -8.766  1.00154.42           C  
ANISOU 5112  C   SER B 255    24453  18656  15563   2275    -79    178       C  
ATOM   5113  O   SER B 255     -27.228   3.460  -9.776  1.00152.37           O  
ANISOU 5113  O   SER B 255    24088  18333  15471   2199   -160    128       O  
ATOM   5114  CB  SER B 255     -26.904   4.083  -6.638  1.00162.03           C  
ANISOU 5114  CB  SER B 255    25875  19455  16236   2411   -292    101       C  
ATOM   5115  OG  SER B 255     -25.646   4.171  -7.289  1.00170.86           O  
ANISOU 5115  OG  SER B 255    26924  20454  17540   2294   -478     54       O  
ATOM   5116  N   LEU B 256     -28.378   1.911  -8.579  1.00147.71           N  
ANISOU 5116  N   LEU B 256    23516  17896  14710   2226     26    279       N  
ATOM   5117  CA  LEU B 256     -28.339   0.833  -9.559  1.00144.72           C  
ANISOU 5117  CA  LEU B 256    22918  17548  14520   2085     58    336       C  
ATOM   5118  C   LEU B 256     -29.435   1.071 -10.607  1.00144.80           C  
ANISOU 5118  C   LEU B 256    22747  17681  14588   2087    216    352       C  
ATOM   5119  O   LEU B 256     -29.271   0.648 -11.753  1.00142.96           O  
ANISOU 5119  O   LEU B 256    22341  17444  14533   1978    214    357       O  
ATOM   5120  CB  LEU B 256     -28.525  -0.543  -8.886  1.00145.28           C  
ANISOU 5120  CB  LEU B 256    22997  17656  14546   2030    102    441       C  
ATOM   5121  CG  LEU B 256     -27.498  -0.954  -7.813  1.00150.58           C  
ANISOU 5121  CG  LEU B 256    23845  18212  15155   2027    -57    443       C  
ATOM   5122  CD1 LEU B 256     -28.103  -1.947  -6.836  1.00151.79           C  
ANISOU 5122  CD1 LEU B 256    24076  18431  15168   2029     34    549       C  
ATOM   5123  CD2 LEU B 256     -26.220  -1.515  -8.431  1.00151.22           C  
ANISOU 5123  CD2 LEU B 256    23841  18177  15439   1916   -218    423       C  
ATOM   5124  N   ARG B 257     -30.535   1.770 -10.220  1.00139.66           N  
ANISOU 5124  N   ARG B 257    22142  17137  13785   2218    351    357       N  
ATOM   5125  CA  ARG B 257     -31.662   2.117 -11.099  1.00137.91           C  
ANISOU 5125  CA  ARG B 257    21756  17045  13600   2246    497    376       C  
ATOM   5126  C   ARG B 257     -31.283   3.161 -12.155  1.00138.10           C  
ANISOU 5126  C   ARG B 257    21739  16998  13735   2253    423    282       C  
ATOM   5127  O   ARG B 257     -31.980   3.295 -13.163  1.00136.48           O  
ANISOU 5127  O   ARG B 257    21370  16873  13611   2235    507    296       O  
ATOM   5128  CB  ARG B 257     -32.873   2.592 -10.282  1.00139.82           C  
ANISOU 5128  CB  ARG B 257    22062  17422  13641   2407    659    409       C  
ATOM   5129  N   ARG B 258     -30.186   3.904 -11.914  1.00133.31           N  
ANISOU 5129  N   ARG B 258    21285  16240  13126   2271    261    192       N  
ATOM   5130  CA  ARG B 258     -29.659   4.920 -12.823  1.00131.62           C  
ANISOU 5130  CA  ARG B 258    21062  15936  13010   2260    171    104       C  
ATOM   5131  C   ARG B 258     -28.825   4.223 -13.893  1.00132.03           C  
ANISOU 5131  C   ARG B 258    20953  15931  13280   2089     95    107       C  
ATOM   5132  O   ARG B 258     -28.920   4.573 -15.075  1.00130.76           O  
ANISOU 5132  O   ARG B 258    20673  15774  13237   2043    110     83       O  
ATOM   5133  CB  ARG B 258     -28.810   5.965 -12.064  1.00133.37           C  
ANISOU 5133  CB  ARG B 258    21521  16017  13135   2332     21     14       C  
ATOM   5134  CG  ARG B 258     -29.579   6.805 -11.029  1.00147.88           C  
ANISOU 5134  CG  ARG B 258    23557  17888  14741   2522     90     -7       C  
ATOM   5135  CD  ARG B 258     -30.353   7.957 -11.653  1.00156.99           C  
ANISOU 5135  CD  ARG B 258    24707  19076  15867   2636    165    -52       C  
ATOM   5136  NE  ARG B 258     -30.823   8.931 -10.662  1.00163.99           N  
ANISOU 5136  NE  ARG B 258    25828  19949  16531   2830    196    -97       N  
ATOM   5137  CZ  ARG B 258     -32.044   8.949 -10.132  1.00174.73           C  
ANISOU 5137  CZ  ARG B 258    27195  21450  17743   2982    376    -52       C  
ATOM   5138  NH1 ARG B 258     -32.937   8.024 -10.468  1.00161.17           N1+
ANISOU 5138  NH1 ARG B 258    25254  19903  16079   2946    533     46       N1+
ATOM   5139  NH2 ARG B 258     -32.382   9.890  -9.261  1.00159.85           N  
ANISOU 5139  NH2 ARG B 258    25543  19538  15655   3169    399   -104       N  
ATOM   5140  N   ILE B 259     -28.029   3.218 -13.470  1.00126.64           N  
ANISOU 5140  N   ILE B 259    20275  15197  12645   2001     18    140       N  
ATOM   5141  CA  ILE B 259     -27.159   2.398 -14.323  1.00124.46           C  
ANISOU 5141  CA  ILE B 259    19862  14864  12565   1854    -51    148       C  
ATOM   5142  C   ILE B 259     -27.982   1.615 -15.365  1.00123.79           C  
ANISOU 5142  C   ILE B 259    19579  14878  12576   1778     82    209       C  
ATOM   5143  O   ILE B 259     -27.583   1.560 -16.530  1.00121.89           O  
ANISOU 5143  O   ILE B 259    19219  14603  12489   1690     60    185       O  
ATOM   5144  CB  ILE B 259     -26.242   1.480 -13.451  1.00128.55           C  
ANISOU 5144  CB  ILE B 259    20449  15310  13084   1811   -157    177       C  
ATOM   5145  CG1 ILE B 259     -25.331   2.325 -12.517  1.00130.05           C  
ANISOU 5145  CG1 ILE B 259    20830  15390  13191   1869   -319    112       C  
ATOM   5146  CG2 ILE B 259     -25.411   0.503 -14.315  1.00128.86           C  
ANISOU 5146  CG2 ILE B 259    20340  15299  13323   1679   -208    193       C  
ATOM   5147  CD1 ILE B 259     -24.810   1.612 -11.250  1.00139.31           C  
ANISOU 5147  CD1 ILE B 259    22134  16521  14277   1881   -405    150       C  
ATOM   5148  N   THR B 260     -29.131   1.028 -14.945  1.00118.71           N  
ANISOU 5148  N   THR B 260    18907  14360  11838   1807    219    291       N  
ATOM   5149  CA  THR B 260     -30.026   0.261 -15.823  1.00116.69           C  
ANISOU 5149  CA  THR B 260    18473  14209  11656   1726    339    360       C  
ATOM   5150  C   THR B 260     -30.697   1.181 -16.826  1.00118.08           C  
ANISOU 5150  C   THR B 260    18558  14441  11866   1758    397    326       C  
ATOM   5151  O   THR B 260     -30.888   0.774 -17.974  1.00116.53           O  
ANISOU 5151  O   THR B 260    18218  14265  11794   1660    425    342       O  
ATOM   5152  CB  THR B 260     -31.039  -0.619 -15.055  1.00120.43           C  
ANISOU 5152  CB  THR B 260    18934  14803  12018   1731    462    466       C  
ATOM   5153  OG1 THR B 260     -32.121   0.173 -14.566  1.00121.18           O  
ANISOU 5153  OG1 THR B 260    19059  15017  11967   1864    573    477       O  
ATOM   5154  CG2 THR B 260     -30.405  -1.437 -13.941  1.00117.09           C  
ANISOU 5154  CG2 THR B 260    18635  14317  11535   1715    400    501       C  
ATOM   5155  N   ARG B 261     -31.033   2.427 -16.389  1.00113.89           N  
ANISOU 5155  N   ARG B 261    18130  13925  11219   1901    408    277       N  
ATOM   5156  CA  ARG B 261     -31.642   3.482 -17.210  1.00112.86           C  
ANISOU 5156  CA  ARG B 261    17948  13833  11099   1964    448    238       C  
ATOM   5157  C   ARG B 261     -30.662   3.927 -18.301  1.00115.42           C  
ANISOU 5157  C   ARG B 261    18249  14035  11571   1880    337    164       C  
ATOM   5158  O   ARG B 261     -31.070   4.161 -19.445  1.00113.97           O  
ANISOU 5158  O   ARG B 261    17952  13883  11468   1844    373    160       O  
ATOM   5159  CB  ARG B 261     -32.041   4.680 -16.342  1.00113.24           C  
ANISOU 5159  CB  ARG B 261    18156  13894  10978   2149    468    195       C  
ATOM   5160  N   MET B 262     -29.365   4.015 -17.942  1.00112.03           N  
ANISOU 5160  N   MET B 262    17922  13469  11174   1844    202    110       N  
ATOM   5161  CA  MET B 262     -28.284   4.382 -18.848  1.00111.04           C  
ANISOU 5161  CA  MET B 262    17775  13228  11190   1755     95     46       C  
ATOM   5162  C   MET B 262     -28.139   3.363 -19.970  1.00112.96           C  
ANISOU 5162  C   MET B 262    17847  13484  11591   1614    125     82       C  
ATOM   5163  O   MET B 262     -27.945   3.770 -21.121  1.00113.25           O  
ANISOU 5163  O   MET B 262    17815  13489  11725   1558    115     47       O  
ATOM   5164  CB  MET B 262     -26.960   4.529 -18.096  1.00114.18           C  
ANISOU 5164  CB  MET B 262    18295  13498  11588   1740    -55      0       C  
ATOM   5165  CG  MET B 262     -26.447   5.951 -18.071  1.00119.13           C  
ANISOU 5165  CG  MET B 262    19053  14030  12181   1789   -154    -84       C  
ATOM   5166  SD  MET B 262     -26.115   6.671 -19.703  1.00122.98           S  
ANISOU 5166  SD  MET B 262    19444  14467  12817   1701   -173   -133       S  
ATOM   5167  CE  MET B 262     -24.834   5.566 -20.278  1.00118.85           C  
ANISOU 5167  CE  MET B 262    18785  13888  12484   1537   -237   -119       C  
ATOM   5168  N   VAL B 263     -28.267   2.044 -19.642  1.00105.93           N  
ANISOU 5168  N   VAL B 263    16901  12633  10714   1558    165    152       N  
ATOM   5169  CA  VAL B 263     -28.197   0.923 -20.600  1.00102.77           C  
ANISOU 5169  CA  VAL B 263    16363  12239  10445   1429    198    191       C  
ATOM   5170  C   VAL B 263     -29.308   1.056 -21.660  1.00101.98           C  
ANISOU 5170  C   VAL B 263    16149  12234  10366   1406    299    216       C  
ATOM   5171  O   VAL B 263     -29.035   0.856 -22.839  1.00100.42           O  
ANISOU 5171  O   VAL B 263    15867  12002  10285   1314    293    199       O  
ATOM   5172  CB  VAL B 263     -28.157  -0.462 -19.884  1.00106.42           C  
ANISOU 5172  CB  VAL B 263    16828  12713  10895   1386    212    263       C  
ATOM   5173  CG1 VAL B 263     -28.312  -1.629 -20.861  1.00105.32           C  
ANISOU 5173  CG1 VAL B 263    16567  12582  10867   1261    259    309       C  
ATOM   5174  CG2 VAL B 263     -26.867  -0.611 -19.089  1.00106.42           C  
ANISOU 5174  CG2 VAL B 263    16925  12602  10910   1395     86    233       C  
ATOM   5175  N   LEU B 264     -30.521   1.472 -21.245  1.00 97.17           N  
ANISOU 5175  N   LEU B 264    15538  11743   9640   1498    386    252       N  
ATOM   5176  CA  LEU B 264     -31.651   1.702 -22.140  1.00 95.98           C  
ANISOU 5176  CA  LEU B 264    15273  11697   9499   1494    471    282       C  
ATOM   5177  C   LEU B 264     -31.368   2.855 -23.096  1.00 99.69           C  
ANISOU 5177  C   LEU B 264    15752  12107  10019   1513    424    206       C  
ATOM   5178  O   LEU B 264     -31.677   2.736 -24.282  1.00 99.45           O  
ANISOU 5178  O   LEU B 264    15622  12095  10070   1436    446    214       O  
ATOM   5179  CB  LEU B 264     -32.951   1.947 -21.354  1.00 96.80           C  
ANISOU 5179  CB  LEU B 264    15368  11948   9463   1610    575    340       C  
ATOM   5180  CG  LEU B 264     -34.248   2.129 -22.167  1.00101.00           C  
ANISOU 5180  CG  LEU B 264    15758  12616  10000   1617    665    388       C  
ATOM   5181  CD1 LEU B 264     -34.509   0.956 -23.112  1.00100.61           C  
ANISOU 5181  CD1 LEU B 264    15569  12598  10058   1446    686    450       C  
ATOM   5182  CD2 LEU B 264     -35.430   2.355 -21.261  1.00103.25           C  
ANISOU 5182  CD2 LEU B 264    16027  13056  10148   1745    774    449       C  
ATOM   5183  N   VAL B 265     -30.772   3.961 -22.594  1.00 96.08           N  
ANISOU 5183  N   VAL B 265    15429  11570   9509   1606    354    135       N  
ATOM   5184  CA  VAL B 265     -30.410   5.130 -23.418  1.00 95.21           C  
ANISOU 5184  CA  VAL B 265    15355  11383   9436   1619    298     63       C  
ATOM   5185  C   VAL B 265     -29.413   4.690 -24.530  1.00 98.96           C  
ANISOU 5185  C   VAL B 265    15766  11767  10068   1467    245     37       C  
ATOM   5186  O   VAL B 265     -29.572   5.101 -25.690  1.00 98.51           O  
ANISOU 5186  O   VAL B 265    15658  11703  10069   1425    254     20       O  
ATOM   5187  CB  VAL B 265     -29.841   6.298 -22.565  1.00 99.05           C  
ANISOU 5187  CB  VAL B 265    16021  11780   9833   1727    215     -7       C  
ATOM   5188  CG1 VAL B 265     -29.314   7.430 -23.445  1.00 98.09           C  
ANISOU 5188  CG1 VAL B 265    15949  11559   9762   1710    144    -78       C  
ATOM   5189  CG2 VAL B 265     -30.876   6.822 -21.570  1.00100.10           C  
ANISOU 5189  CG2 VAL B 265    16232  12001   9801   1897    283     11       C  
ATOM   5190  N   VAL B 266     -28.417   3.824 -24.154  1.00 93.31           N  
ANISOU 5190  N   VAL B 266    15052  10988   9413   1393    195     38       N  
ATOM   5191  CA  VAL B 266     -27.368   3.271 -25.015  1.00 90.77           C  
ANISOU 5191  CA  VAL B 266    14671  10583   9234   1267    154     17       C  
ATOM   5192  C   VAL B 266     -27.984   2.495 -26.177  1.00 95.02           C  
ANISOU 5192  C   VAL B 266    15089  11174   9841   1177    232     57       C  
ATOM   5193  O   VAL B 266     -27.613   2.745 -27.332  1.00 94.50           O  
ANISOU 5193  O   VAL B 266    14986  11061   9858   1108    225     24       O  
ATOM   5194  CB  VAL B 266     -26.342   2.414 -24.209  1.00 93.18           C  
ANISOU 5194  CB  VAL B 266    14998  10828   9577   1237     92     24       C  
ATOM   5195  CG1 VAL B 266     -25.417   1.624 -25.120  1.00 91.57           C  
ANISOU 5195  CG1 VAL B 266    14710  10560   9521   1122     77     15       C  
ATOM   5196  CG2 VAL B 266     -25.526   3.272 -23.260  1.00 93.64           C  
ANISOU 5196  CG2 VAL B 266    15179  10814   9588   1300    -15    -26       C  
ATOM   5197  N   VAL B 267     -28.943   1.586 -25.872  1.00 92.07           N  
ANISOU 5197  N   VAL B 267    14662  10897   9425   1172    305    131       N  
ATOM   5198  CA  VAL B 267     -29.566   0.707 -26.865  1.00 91.65           C  
ANISOU 5198  CA  VAL B 267    14505  10891   9427   1071    367    178       C  
ATOM   5199  C   VAL B 267     -30.499   1.493 -27.790  1.00 93.69           C  
ANISOU 5199  C   VAL B 267    14716  11214   9669   1085    403    178       C  
ATOM   5200  O   VAL B 267     -30.445   1.268 -29.002  1.00 91.84           O  
ANISOU 5200  O   VAL B 267    14432  10955   9510    992    409    170       O  
ATOM   5201  CB  VAL B 267     -30.203  -0.584 -26.268  1.00 96.63           C  
ANISOU 5201  CB  VAL B 267    15098  11592  10026   1033    419    264       C  
ATOM   5202  CG1 VAL B 267     -31.493  -0.317 -25.500  1.00 97.48           C  
ANISOU 5202  CG1 VAL B 267    15188  11838  10013   1117    486    323       C  
ATOM   5203  CG2 VAL B 267     -30.399  -1.659 -27.339  1.00 96.25           C  
ANISOU 5203  CG2 VAL B 267    14975  11538  10059    898    449    298       C  
ATOM   5204  N   VAL B 268     -31.266   2.462 -27.249  1.00 90.96           N  
ANISOU 5204  N   VAL B 268    14398  10939   9223   1208    421    180       N  
ATOM   5205  CA  VAL B 268     -32.144   3.310 -28.071  1.00 91.05           C  
ANISOU 5205  CA  VAL B 268    14370  11009   9215   1246    446    179       C  
ATOM   5206  C   VAL B 268     -31.309   4.150 -29.068  1.00 94.12           C  
ANISOU 5206  C   VAL B 268    14809  11283   9669   1212    384    104       C  
ATOM   5207  O   VAL B 268     -31.599   4.133 -30.268  1.00 93.59           O  
ANISOU 5207  O   VAL B 268    14687  11221   9651   1141    394    108       O  
ATOM   5208  CB  VAL B 268     -33.132   4.158 -27.228  1.00 95.81           C  
ANISOU 5208  CB  VAL B 268    14997  11712   9693   1410    485    198       C  
ATOM   5209  CG1 VAL B 268     -33.956   5.094 -28.112  1.00 95.34           C  
ANISOU 5209  CG1 VAL B 268    14901  11702   9621   1464    497    194       C  
ATOM   5210  CG2 VAL B 268     -34.050   3.257 -26.403  1.00 96.52           C  
ANISOU 5210  CG2 VAL B 268    15014  11937   9724   1423    566    287       C  
ATOM   5211  N   ALA B 269     -30.243   4.821 -28.575  1.00 90.09           N  
ANISOU 5211  N   ALA B 269    14405  10667   9159   1247    316     39       N  
ATOM   5212  CA  ALA B 269     -29.336   5.619 -29.403  1.00 88.86           C  
ANISOU 5212  CA  ALA B 269    14300  10398   9063   1201    256    -27       C  
ATOM   5213  C   ALA B 269     -28.625   4.744 -30.430  1.00 91.71           C  
ANISOU 5213  C   ALA B 269    14594  10707   9543   1054    263    -30       C  
ATOM   5214  O   ALA B 269     -28.434   5.195 -31.556  1.00 91.98           O  
ANISOU 5214  O   ALA B 269    14628  10699   9623    998    257    -57       O  
ATOM   5215  CB  ALA B 269     -28.320   6.337 -28.536  1.00 89.83           C  
ANISOU 5215  CB  ALA B 269    14540  10427   9165   1248    175    -83       C  
ATOM   5216  N   PHE B 270     -28.277   3.479 -30.066  1.00 86.42           N  
ANISOU 5216  N   PHE B 270    13877  10041   8918    998    279     -1       N  
ATOM   5217  CA  PHE B 270     -27.624   2.535 -30.979  1.00 84.46           C  
ANISOU 5217  CA  PHE B 270    13575   9741   8776    876    295     -3       C  
ATOM   5218  C   PHE B 270     -28.545   2.212 -32.163  1.00 90.01           C  
ANISOU 5218  C   PHE B 270    14220  10495   9485    811    349     28       C  
ATOM   5219  O   PHE B 270     -28.134   2.379 -33.316  1.00 88.85           O  
ANISOU 5219  O   PHE B 270    14073  10294   9394    740    351     -3       O  
ATOM   5220  CB  PHE B 270     -27.186   1.264 -30.242  1.00 85.42           C  
ANISOU 5220  CB  PHE B 270    13677   9853   8927    853    297     27       C  
ATOM   5221  CG  PHE B 270     -26.273   0.367 -31.045  1.00 86.01           C  
ANISOU 5221  CG  PHE B 270    13717   9852   9110    755    306     11       C  
ATOM   5222  CD1 PHE B 270     -24.894   0.550 -31.023  1.00 88.85           C  
ANISOU 5222  CD1 PHE B 270    14087  10124   9547    745    259    -38       C  
ATOM   5223  CD2 PHE B 270     -26.792  -0.663 -31.829  1.00 86.10           C  
ANISOU 5223  CD2 PHE B 270    13687   9881   9145    675    360     47       C  
ATOM   5224  CE1 PHE B 270     -24.054  -0.281 -31.775  1.00 88.89           C  
ANISOU 5224  CE1 PHE B 270    14054  10068   9653    673    281    -52       C  
ATOM   5225  CE2 PHE B 270     -25.952  -1.496 -32.565  1.00 87.70           C  
ANISOU 5225  CE2 PHE B 270    13877  10007   9438    601    375     27       C  
ATOM   5226  CZ  PHE B 270     -24.590  -1.296 -32.538  1.00 86.00           C  
ANISOU 5226  CZ  PHE B 270    13665   9712   9299    609    343    -22       C  
ATOM   5227  N   VAL B 271     -29.799   1.797 -31.876  1.00 88.62           N  
ANISOU 5227  N   VAL B 271    13997  10429   9247    833    390     93       N  
ATOM   5228  CA  VAL B 271     -30.822   1.491 -32.885  1.00 89.06           C  
ANISOU 5228  CA  VAL B 271    13989  10550   9301    769    425    135       C  
ATOM   5229  C   VAL B 271     -31.131   2.734 -33.737  1.00 93.37           C  
ANISOU 5229  C   VAL B 271    14556  11094   9827    801    407    104       C  
ATOM   5230  O   VAL B 271     -31.176   2.614 -34.959  1.00 93.24           O  
ANISOU 5230  O   VAL B 271    14529  11051   9848    715    410     98       O  
ATOM   5231  CB  VAL B 271     -32.112   0.889 -32.259  1.00 93.98           C  
ANISOU 5231  CB  VAL B 271    14540  11306   9860    787    468    220       C  
ATOM   5232  CG1 VAL B 271     -33.187   0.627 -33.317  1.00 94.02           C  
ANISOU 5232  CG1 VAL B 271    14471  11385   9868    711    487    268       C  
ATOM   5233  CG2 VAL B 271     -31.810  -0.383 -31.484  1.00 93.80           C  
ANISOU 5233  CG2 VAL B 271    14514  11274   9852    740    483    257       C  
ATOM   5234  N   VAL B 272     -31.326   3.916 -33.101  1.00 89.70           N  
ANISOU 5234  N   VAL B 272    14138  10646   9297    927    385     83       N  
ATOM   5235  CA  VAL B 272     -31.649   5.170 -33.805  1.00 89.77           C  
ANISOU 5235  CA  VAL B 272    14188  10643   9277    976    360     56       C  
ATOM   5236  C   VAL B 272     -30.549   5.584 -34.803  1.00 92.57           C  
ANISOU 5236  C   VAL B 272    14606  10870   9697    892    326     -6       C  
ATOM   5237  O   VAL B 272     -30.848   5.830 -35.971  1.00 92.07           O  
ANISOU 5237  O   VAL B 272    14542  10797   9645    839    326     -6       O  
ATOM   5238  CB  VAL B 272     -32.017   6.338 -32.832  1.00 94.40           C  
ANISOU 5238  CB  VAL B 272    14840  11254   9772   1142    341     41       C  
ATOM   5239  CG1 VAL B 272     -32.152   7.668 -33.574  1.00 94.11           C  
ANISOU 5239  CG1 VAL B 272    14877  11171   9708   1192    303      4       C  
ATOM   5240  CG2 VAL B 272     -33.294   6.038 -32.063  1.00 95.00           C  
ANISOU 5240  CG2 VAL B 272    14840  11480   9775   1233    395    109       C  
ATOM   5241  N   CYS B 273     -29.291   5.648 -34.333  1.00 88.46           N  
ANISOU 5241  N   CYS B 273    14135  10257   9218    876    298    -53       N  
ATOM   5242  CA  CYS B 273     -28.125   6.096 -35.091  1.00 87.94           C  
ANISOU 5242  CA  CYS B 273    14119  10078   9216    800    272   -107       C  
ATOM   5243  C   CYS B 273     -27.609   5.117 -36.131  1.00 92.14           C  
ANISOU 5243  C   CYS B 273    14603  10576   9831    670    313   -107       C  
ATOM   5244  O   CYS B 273     -27.000   5.564 -37.102  1.00 93.51           O  
ANISOU 5244  O   CYS B 273    14810  10680  10040    604    312   -140       O  
ATOM   5245  CB  CYS B 273     -27.010   6.500 -34.137  1.00 88.59           C  
ANISOU 5245  CB  CYS B 273    14254  10090   9315    828    219   -147       C  
ATOM   5246  SG  CYS B 273     -27.361   7.996 -33.179  1.00 93.42           S  
ANISOU 5246  SG  CYS B 273    14984  10691   9821    970    156   -172       S  
ATOM   5247  N   TRP B 274     -27.798   3.803 -35.929  1.00 87.51           N  
ANISOU 5247  N   TRP B 274    13952  10028   9270    633    350    -72       N  
ATOM   5248  CA  TRP B 274     -27.260   2.782 -36.823  1.00 86.22           C  
ANISOU 5248  CA  TRP B 274    13763   9820   9178    524    390    -76       C  
ATOM   5249  C   TRP B 274     -28.251   2.137 -37.802  1.00 89.17           C  
ANISOU 5249  C   TRP B 274    14112  10236   9530    456    424    -38       C  
ATOM   5250  O   TRP B 274     -27.819   1.720 -38.889  1.00 88.24           O  
ANISOU 5250  O   TRP B 274    14012  10062   9453    367    454    -58       O  
ATOM   5251  CB  TRP B 274     -26.557   1.698 -36.014  1.00 84.80           C  
ANISOU 5251  CB  TRP B 274    13552   9618   9048    521    398    -70       C  
ATOM   5252  CG  TRP B 274     -25.169   2.066 -35.591  1.00 85.36           C  
ANISOU 5252  CG  TRP B 274    13636   9616   9179    535    366   -117       C  
ATOM   5253  CD1 TRP B 274     -24.700   2.163 -34.313  1.00 88.36           C  
ANISOU 5253  CD1 TRP B 274    14022   9993   9558    601    317   -119       C  
ATOM   5254  CD2 TRP B 274     -24.050   2.333 -36.454  1.00 84.88           C  
ANISOU 5254  CD2 TRP B 274    13578   9479   9194    473    378   -161       C  
ATOM   5255  NE1 TRP B 274     -23.353   2.447 -34.324  1.00 87.94           N  
ANISOU 5255  NE1 TRP B 274    13964   9868   9580    580    287   -160       N  
ATOM   5256  CE2 TRP B 274     -22.930   2.568 -35.626  1.00 89.01           C  
ANISOU 5256  CE2 TRP B 274    14090   9963   9767    501    331   -185       C  
ATOM   5257  CE3 TRP B 274     -23.880   2.378 -37.853  1.00 85.53           C  
ANISOU 5257  CE3 TRP B 274    13671   9525   9301    392    428   -180       C  
ATOM   5258  CZ2 TRP B 274     -21.664   2.864 -36.147  1.00 88.26           C  
ANISOU 5258  CZ2 TRP B 274    13974   9806   9756    449    334   -221       C  
ATOM   5259  CZ3 TRP B 274     -22.626   2.661 -38.367  1.00 86.81           C  
ANISOU 5259  CZ3 TRP B 274    13825   9622   9537    346    444   -219       C  
ATOM   5260  CH2 TRP B 274     -21.540   2.920 -37.521  1.00 87.74           C  
ANISOU 5260  CH2 TRP B 274    13912   9713   9713    373    398   -237       C  
ATOM   5261  N   ALA B 275     -29.554   2.033 -37.428  1.00 85.05           N  
ANISOU 5261  N   ALA B 275    13551   9818   8945    494    421     18       N  
ATOM   5262  CA  ALA B 275     -30.584   1.455 -38.302  1.00 84.59           C  
ANISOU 5262  CA  ALA B 275    13460   9813   8866    419    435     64       C  
ATOM   5263  C   ALA B 275     -30.733   2.149 -39.690  1.00 88.73           C  
ANISOU 5263  C   ALA B 275    14029  10306   9380    372    422     43       C  
ATOM   5264  O   ALA B 275     -30.826   1.420 -40.678  1.00 87.87           O  
ANISOU 5264  O   ALA B 275    13933  10169   9284    268    437     49       O  
ATOM   5265  CB  ALA B 275     -31.931   1.391 -37.597  1.00 85.46           C  
ANISOU 5265  CB  ALA B 275    13498  10056   8915    474    432    135       C  
ATOM   5266  N   PRO B 276     -30.735   3.510 -39.821  1.00 86.10           N  
ANISOU 5266  N   PRO B 276    13738   9962   9016    441    392     16       N  
ATOM   5267  CA  PRO B 276     -30.944   4.111 -41.142  1.00 86.32           C  
ANISOU 5267  CA  PRO B 276    13817   9956   9024    392    376      5       C  
ATOM   5268  C   PRO B 276     -29.910   3.726 -42.211  1.00 91.36           C  
ANISOU 5268  C   PRO B 276    14516  10487   9709    280    410    -40       C  
ATOM   5269  O   PRO B 276     -30.314   3.369 -43.325  1.00 92.04           O  
ANISOU 5269  O   PRO B 276    14628  10565   9778    197    414    -28       O  
ATOM   5270  CB  PRO B 276     -30.967   5.609 -40.836  1.00 87.97           C  
ANISOU 5270  CB  PRO B 276    14077  10156   9192    499    337    -18       C  
ATOM   5271  CG  PRO B 276     -31.396   5.693 -39.407  1.00 92.31           C  
ANISOU 5271  CG  PRO B 276    14578  10781   9714    616    331      5       C  
ATOM   5272  CD  PRO B 276     -30.662   4.569 -38.790  1.00 87.85           C  
ANISOU 5272  CD  PRO B 276    13979  10196   9205    568    364      0       C  
ATOM   5273  N   ILE B 277     -28.598   3.741 -41.870  1.00 86.27           N  
ANISOU 5273  N   ILE B 277    13890   9766   9122    277    435    -87       N  
ATOM   5274  CA  ILE B 277     -27.536   3.388 -42.818  1.00 84.33           C  
ANISOU 5274  CA  ILE B 277    13687   9429   8926    186    484   -128       C  
ATOM   5275  C   ILE B 277     -27.616   1.904 -43.163  1.00 89.28           C  
ANISOU 5275  C   ILE B 277    14296  10051   9574    115    526   -113       C  
ATOM   5276  O   ILE B 277     -27.378   1.574 -44.318  1.00 90.77           O  
ANISOU 5276  O   ILE B 277    14540  10187   9761     34    563   -131       O  
ATOM   5277  CB  ILE B 277     -26.103   3.878 -42.401  1.00 86.24           C  
ANISOU 5277  CB  ILE B 277    13934   9603   9231    200    496   -175       C  
ATOM   5278  CG1 ILE B 277     -25.033   3.640 -43.509  1.00 86.48           C  
ANISOU 5278  CG1 ILE B 277    13997   9552   9308    109    563   -212       C  
ATOM   5279  CG2 ILE B 277     -25.641   3.318 -41.068  1.00 85.30           C  
ANISOU 5279  CG2 ILE B 277    13752   9501   9158    257    487   -173       C  
ATOM   5280  CD1 ILE B 277     -25.193   4.416 -44.832  1.00 88.72           C  
ANISOU 5280  CD1 ILE B 277    14367   9799   9543     47    573   -222       C  
ATOM   5281  N   HIS B 278     -28.021   1.024 -42.210  1.00 85.76           N  
ANISOU 5281  N   HIS B 278    13791   9657   9136    143    519    -78       N  
ATOM   5282  CA  HIS B 278     -28.153  -0.424 -42.468  1.00 84.74           C  
ANISOU 5282  CA  HIS B 278    13664   9513   9022     73    549    -59       C  
ATOM   5283  C   HIS B 278     -29.326  -0.732 -43.382  1.00 91.15           C  
ANISOU 5283  C   HIS B 278    14499  10360   9775     -4    529    -21       C  
ATOM   5284  O   HIS B 278     -29.167  -1.533 -44.305  1.00 91.38           O  
ANISOU 5284  O   HIS B 278    14589  10327   9803    -91    556    -34       O  
ATOM   5285  CB  HIS B 278     -28.189  -1.256 -41.182  1.00 84.13           C  
ANISOU 5285  CB  HIS B 278    13532   9468   8967    114    544    -28       C  
ATOM   5286  CG  HIS B 278     -26.838  -1.448 -40.575  1.00 86.52           C  
ANISOU 5286  CG  HIS B 278    13827   9706   9340    156    567    -69       C  
ATOM   5287  ND1 HIS B 278     -25.834  -2.109 -41.253  1.00 87.97           N  
ANISOU 5287  ND1 HIS B 278    14045   9802   9579    114    618   -108       N  
ATOM   5288  CD2 HIS B 278     -26.358  -1.037 -39.380  1.00 87.69           C  
ANISOU 5288  CD2 HIS B 278    13939   9870   9510    240    540    -73       C  
ATOM   5289  CE1 HIS B 278     -24.780  -2.082 -40.451  1.00 87.06           C  
ANISOU 5289  CE1 HIS B 278    13893   9659   9526    173    618   -131       C  
ATOM   5290  NE2 HIS B 278     -25.047  -1.454 -39.312  1.00 87.23           N  
ANISOU 5290  NE2 HIS B 278    13877   9737   9528    243    565   -111       N  
ATOM   5291  N   ILE B 279     -30.473  -0.039 -43.181  1.00 88.63           N  
ANISOU 5291  N   ILE B 279    14136  10137   9402     32    478     24       N  
ATOM   5292  CA  ILE B 279     -31.655  -0.165 -44.042  1.00 89.51           C  
ANISOU 5292  CA  ILE B 279    14252  10299   9460    -36    439     69       C  
ATOM   5293  C   ILE B 279     -31.299   0.423 -45.449  1.00 94.80           C  
ANISOU 5293  C   ILE B 279    15022  10891  10108    -90    441     27       C  
ATOM   5294  O   ILE B 279     -31.731  -0.139 -46.462  1.00 95.17           O  
ANISOU 5294  O   ILE B 279    15121  10917  10121   -188    428     39       O  
ATOM   5295  CB  ILE B 279     -32.925   0.478 -43.396  1.00 93.11           C  
ANISOU 5295  CB  ILE B 279    14614  10889   9873     39    389    131       C  
ATOM   5296  CG1 ILE B 279     -33.302  -0.200 -42.063  1.00 93.00           C  
ANISOU 5296  CG1 ILE B 279    14511  10955   9869     78    401    179       C  
ATOM   5297  CG2 ILE B 279     -34.130   0.466 -44.350  1.00 95.37           C  
ANISOU 5297  CG2 ILE B 279    14889  11236  10110    -29    335    182       C  
ATOM   5298  CD1 ILE B 279     -34.023   0.735 -41.094  1.00 97.87           C  
ANISOU 5298  CD1 ILE B 279    15050  11684  10451    209    385    213       C  
ATOM   5299  N   PHE B 280     -30.463   1.505 -45.501  1.00 90.30           N  
ANISOU 5299  N   PHE B 280    14489  10271   9551    -35    457    -22       N  
ATOM   5300  CA  PHE B 280     -29.990   2.093 -46.758  1.00 89.82           C  
ANISOU 5300  CA  PHE B 280    14529  10131   9467    -88    472    -60       C  
ATOM   5301  C   PHE B 280     -29.041   1.139 -47.522  1.00 95.01           C  
ANISOU 5301  C   PHE B 280    15255  10692  10152   -175    546   -102       C  
ATOM   5302  O   PHE B 280     -29.236   0.965 -48.733  1.00 95.52           O  
ANISOU 5302  O   PHE B 280    15410  10715  10169   -257    551   -108       O  
ATOM   5303  CB  PHE B 280     -29.326   3.465 -46.551  1.00 91.14           C  
ANISOU 5303  CB  PHE B 280    14721  10266   9641    -21    469    -94       C  
ATOM   5304  CG  PHE B 280     -29.447   4.452 -47.700  1.00 92.49           C  
ANISOU 5304  CG  PHE B 280    14989  10395   9756    -53    447   -103       C  
ATOM   5305  CD1 PHE B 280     -29.007   4.119 -48.980  1.00 95.17           C  
ANISOU 5305  CD1 PHE B 280    15423  10660  10076   -155    491   -127       C  
ATOM   5306  CD2 PHE B 280     -29.940   5.732 -47.487  1.00 94.78           C  
ANISOU 5306  CD2 PHE B 280    15294  10711  10008     26    385    -90       C  
ATOM   5307  CE1 PHE B 280     -29.122   5.022 -50.039  1.00 96.69           C  
ANISOU 5307  CE1 PHE B 280    15720  10810  10208   -189    470   -131       C  
ATOM   5308  CE2 PHE B 280     -30.032   6.647 -48.544  1.00 98.39           C  
ANISOU 5308  CE2 PHE B 280    15856  11118  10408     -3    359    -95       C  
ATOM   5309  CZ  PHE B 280     -29.616   6.286 -49.813  1.00 96.50           C  
ANISOU 5309  CZ  PHE B 280    15708  10809  10149   -115    401   -113       C  
ATOM   5310  N   VAL B 281     -28.028   0.530 -46.833  1.00 90.63           N  
ANISOU 5310  N   VAL B 281    14665  10101   9668   -150    602   -131       N  
ATOM   5311  CA  VAL B 281     -27.075  -0.416 -47.454  1.00 90.67           C  
ANISOU 5311  CA  VAL B 281    14726  10018   9705   -204    683   -171       C  
ATOM   5312  C   VAL B 281     -27.835  -1.582 -48.140  1.00 95.20           C  
ANISOU 5312  C   VAL B 281    15364  10576  10231   -289    674   -150       C  
ATOM   5313  O   VAL B 281     -27.529  -1.915 -49.287  1.00 95.52           O  
ANISOU 5313  O   VAL B 281    15510  10544  10240   -356    718   -180       O  
ATOM   5314  CB  VAL B 281     -25.941  -0.901 -46.486  1.00 93.52           C  
ANISOU 5314  CB  VAL B 281    15023  10355  10157   -145    730   -197       C  
ATOM   5315  CG1 VAL B 281     -25.159  -2.072 -47.077  1.00 93.17           C  
ANISOU 5315  CG1 VAL B 281    15032  10228  10140   -183    811   -230       C  
ATOM   5316  CG2 VAL B 281     -24.983   0.238 -46.139  1.00 92.98           C  
ANISOU 5316  CG2 VAL B 281    14917  10277  10133    -96    741   -226       C  
ATOM   5317  N   ILE B 282     -28.854  -2.138 -47.445  1.00 91.84           N  
ANISOU 5317  N   ILE B 282    14881  10222   9793   -291    613    -94       N  
ATOM   5318  CA  ILE B 282     -29.746  -3.212 -47.908  1.00 92.09           C  
ANISOU 5318  CA  ILE B 282    14958  10253   9778   -385    579    -58       C  
ATOM   5319  C   ILE B 282     -30.580  -2.731 -49.124  1.00 99.61           C  
ANISOU 5319  C   ILE B 282    15980  11214  10651   -461    527    -42       C  
ATOM   5320  O   ILE B 282     -30.582  -3.397 -50.157  1.00101.14           O  
ANISOU 5320  O   ILE B 282    16292  11335  10801   -552    536    -59       O  
ATOM   5321  CB  ILE B 282     -30.601  -3.771 -46.724  1.00 94.35           C  
ANISOU 5321  CB  ILE B 282    15142  10631  10078   -370    530      9       C  
ATOM   5322  CG1 ILE B 282     -29.722  -4.633 -45.775  1.00 93.79           C  
ANISOU 5322  CG1 ILE B 282    15052  10513  10070   -325    579     -8       C  
ATOM   5323  CG2 ILE B 282     -31.828  -4.549 -47.216  1.00 95.44           C  
ANISOU 5323  CG2 ILE B 282    15303  10801  10160   -483    465     68       C  
ATOM   5324  CD1 ILE B 282     -30.201  -4.778 -44.358  1.00 95.42           C  
ANISOU 5324  CD1 ILE B 282    15153  10808  10296   -270    550     46       C  
ATOM   5325  N   VAL B 283     -31.237  -1.560 -49.018  1.00 96.99           N  
ANISOU 5325  N   VAL B 283    15591  10965  10296   -415    470    -13       N  
ATOM   5326  CA  VAL B 283     -32.028  -0.968 -50.111  1.00 97.73           C  
ANISOU 5326  CA  VAL B 283    15745  11072  10316   -468    407      6       C  
ATOM   5327  C   VAL B 283     -31.150  -0.740 -51.374  1.00102.45           C  
ANISOU 5327  C   VAL B 283    16493  11554  10881   -518    464    -56       C  
ATOM   5328  O   VAL B 283     -31.572  -1.071 -52.476  1.00101.69           O  
ANISOU 5328  O   VAL B 283    16504  11419  10715   -611    434    -52       O  
ATOM   5329  CB  VAL B 283     -32.772   0.324 -49.646  1.00100.91           C  
ANISOU 5329  CB  VAL B 283    16058  11577  10705   -377    342     45       C  
ATOM   5330  CG1 VAL B 283     -33.239   1.180 -50.837  1.00100.98           C  
ANISOU 5330  CG1 VAL B 283    16152  11572  10643   -408    286     50       C  
ATOM   5331  CG2 VAL B 283     -33.944  -0.017 -48.724  1.00100.47           C  
ANISOU 5331  CG2 VAL B 283    15866  11653  10657   -352    284    120       C  
ATOM   5332  N   TRP B 284     -29.929  -0.198 -51.184  1.00 99.50           N  
ANISOU 5332  N   TRP B 284    16126  11128  10553   -460    545   -109       N  
ATOM   5333  CA  TRP B 284     -28.945   0.076 -52.227  1.00 98.94           C  
ANISOU 5333  CA  TRP B 284    16173  10958  10460   -496    624   -164       C  
ATOM   5334  C   TRP B 284     -28.504  -1.167 -52.967  1.00105.21           C  
ANISOU 5334  C   TRP B 284    17074  11666  11236   -570    691   -198       C  
ATOM   5335  O   TRP B 284     -28.351  -1.096 -54.192  1.00106.79           O  
ANISOU 5335  O   TRP B 284    17412  11799  11366   -635    719   -223       O  
ATOM   5336  CB  TRP B 284     -27.714   0.773 -51.644  1.00 96.60           C  
ANISOU 5336  CB  TRP B 284    15825  10641  10236   -425    696   -203       C  
ATOM   5337  CG  TRP B 284     -26.654   1.065 -52.662  1.00 97.63           C  
ANISOU 5337  CG  TRP B 284    16057  10686  10353   -467    791   -252       C  
ATOM   5338  CD1 TRP B 284     -26.776   1.848 -53.772  1.00100.85           C  
ANISOU 5338  CD1 TRP B 284    16578  11059  10683   -519    786   -255       C  
ATOM   5339  CD2 TRP B 284     -25.302   0.588 -52.652  1.00 97.50           C  
ANISOU 5339  CD2 TRP B 284    16032  10613  10400   -456    910   -299       C  
ATOM   5340  NE1 TRP B 284     -25.571   1.930 -54.430  1.00100.52           N  
ANISOU 5340  NE1 TRP B 284    16597  10946  10650   -547    904   -300       N  
ATOM   5341  CE2 TRP B 284     -24.654   1.146 -53.777  1.00101.74           C  
ANISOU 5341  CE2 TRP B 284    16671  11091  10895   -507    984   -328       C  
ATOM   5342  CE3 TRP B 284     -24.571  -0.256 -51.801  1.00 98.56           C  
ANISOU 5342  CE3 TRP B 284    16081  10744  10623   -405    961   -317       C  
ATOM   5343  CZ2 TRP B 284     -23.311   0.880 -54.076  1.00101.38           C  
ANISOU 5343  CZ2 TRP B 284    16628  10996  10897   -507   1117   -371       C  
ATOM   5344  CZ3 TRP B 284     -23.245  -0.524 -52.106  1.00100.41           C  
ANISOU 5344  CZ3 TRP B 284    16319  10925  10909   -397   1081   -361       C  
ATOM   5345  CH2 TRP B 284     -22.623   0.053 -53.221  1.00101.48           C  
ANISOU 5345  CH2 TRP B 284    16538  11014  11006   -446   1163   -387       C  
ATOM   5346  N   THR B 285     -28.249  -2.288 -52.242  1.00101.51           N  
ANISOU 5346  N   THR B 285    16559  11187  10821   -554    720   -202       N  
ATOM   5347  CA  THR B 285     -27.796  -3.525 -52.893  1.00102.00           C  
ANISOU 5347  CA  THR B 285    16739  11152  10864   -607    785   -238       C  
ATOM   5348  C   THR B 285     -28.937  -4.211 -53.668  1.00105.55           C  
ANISOU 5348  C   THR B 285    17296  11587  11221   -718    702   -207       C  
ATOM   5349  O   THR B 285     -28.676  -4.852 -54.690  1.00105.06           O  
ANISOU 5349  O   THR B 285    17393  11428  11098   -781    745   -244       O  
ATOM   5350  CB  THR B 285     -27.048  -4.486 -51.919  1.00109.42           C  
ANISOU 5350  CB  THR B 285    17616  12068  11891   -546    842   -254       C  
ATOM   5351  OG1 THR B 285     -26.746  -5.703 -52.606  1.00111.36           O  
ANISOU 5351  OG1 THR B 285    17999  12210  12104   -592    896   -288       O  
ATOM   5352  CG2 THR B 285     -27.833  -4.831 -50.689  1.00105.16           C  
ANISOU 5352  CG2 THR B 285    16962  11609  11386   -524    760   -197       C  
ATOM   5353  N   LEU B 286     -30.187  -4.045 -53.191  1.00102.39           N  
ANISOU 5353  N   LEU B 286    16809  11285  10809   -739    585   -138       N  
ATOM   5354  CA  LEU B 286     -31.385  -4.668 -53.753  1.00103.28           C  
ANISOU 5354  CA  LEU B 286    16986  11409  10848   -853    482    -91       C  
ATOM   5355  C   LEU B 286     -32.083  -3.893 -54.880  1.00112.23           C  
ANISOU 5355  C   LEU B 286    18198  12554  11892   -915    408    -75       C  
ATOM   5356  O   LEU B 286     -32.499  -4.498 -55.867  1.00112.86           O  
ANISOU 5356  O   LEU B 286    18419  12573  11889  -1024    363    -75       O  
ATOM   5357  CB  LEU B 286     -32.398  -4.974 -52.632  1.00102.24           C  
ANISOU 5357  CB  LEU B 286    16699  11392  10754   -852    398    -14       C  
ATOM   5358  CG  LEU B 286     -32.008  -6.018 -51.584  1.00105.08           C  
ANISOU 5358  CG  LEU B 286    17011  11735  11180   -826    440    -11       C  
ATOM   5359  CD1 LEU B 286     -33.151  -6.253 -50.619  1.00104.78           C  
ANISOU 5359  CD1 LEU B 286    16831  11820  11158   -845    356     77       C  
ATOM   5360  CD2 LEU B 286     -31.583  -7.330 -52.218  1.00106.60           C  
ANISOU 5360  CD2 LEU B 286    17371  11792  11341   -904    477    -50       C  
ATOM   5361  N   VAL B 287     -32.245  -2.576 -54.709  1.00111.84           N  
ANISOU 5361  N   VAL B 287    18067  12576  11851   -844    383    -58       N  
ATOM   5362  CA  VAL B 287     -32.949  -1.670 -55.619  1.00113.61           C  
ANISOU 5362  CA  VAL B 287    18346  12823  11997   -878    299    -33       C  
ATOM   5363  C   VAL B 287     -31.962  -0.752 -56.355  1.00121.57           C  
ANISOU 5363  C   VAL B 287    19461  13753  12978   -849    381    -90       C  
ATOM   5364  O   VAL B 287     -30.993  -0.278 -55.753  1.00120.73           O  
ANISOU 5364  O   VAL B 287    19297  13637  12938   -766    471   -125       O  
ATOM   5365  CB  VAL B 287     -34.022  -0.863 -54.812  1.00117.37           C  
ANISOU 5365  CB  VAL B 287    18649  13445  12501   -809    198     40       C  
ATOM   5366  CG1 VAL B 287     -34.680   0.235 -55.641  1.00117.69           C  
ANISOU 5366  CG1 VAL B 287    18735  13510  12471   -809    110     67       C  
ATOM   5367  CG2 VAL B 287     -35.085  -1.787 -54.224  1.00117.73           C  
ANISOU 5367  CG2 VAL B 287    18590  13579  12563   -861    119    109       C  
ATOM   5368  N   ASP B 288     -32.227  -0.485 -57.656  1.00121.40           N  
ANISOU 5368  N   ASP B 288    19597  13677  12853   -925    343    -93       N  
ATOM   5369  CA  ASP B 288     -31.429   0.447 -58.449  1.00122.12           C  
ANISOU 5369  CA  ASP B 288    19802  13699  12899   -915    412   -134       C  
ATOM   5370  C   ASP B 288     -31.753   1.850 -57.965  1.00125.44           C  
ANISOU 5370  C   ASP B 288    20125  14192  13343   -828    354   -100       C  
ATOM   5371  O   ASP B 288     -32.888   2.320 -58.102  1.00125.11           O  
ANISOU 5371  O   ASP B 288    20057  14217  13262   -827    224    -43       O  
ATOM   5372  CB  ASP B 288     -31.672   0.272 -59.956  1.00125.75           C  
ANISOU 5372  CB  ASP B 288    20476  14075  13228  -1024    386   -145       C  
ATOM   5373  CG  ASP B 288     -31.170  -1.055 -60.498  1.00145.68           C  
ANISOU 5373  CG  ASP B 288    23135  16500  15716  -1096    466   -195       C  
ATOM   5374  OD1 ASP B 288     -30.377  -1.733 -59.793  1.00146.78           O  
ANISOU 5374  OD1 ASP B 288    23210  16621  15938  -1048    570   -230       O  
ATOM   5375  OD2 ASP B 288     -31.565  -1.422 -61.624  1.00157.72           O1-
ANISOU 5375  OD2 ASP B 288    24841  17960  17125  -1193    421   -199       O1-
ATOM   5376  N   ILE B 289     -30.775   2.457 -57.278  1.00121.23           N  
ANISOU 5376  N   ILE B 289    19526  13653  12884   -748    443   -131       N  
ATOM   5377  CA  ILE B 289     -30.874   3.783 -56.665  1.00120.25           C  
ANISOU 5377  CA  ILE B 289    19323  13578  12789   -656    402   -110       C  
ATOM   5378  C   ILE B 289     -30.218   4.826 -57.573  1.00123.70           C  
ANISOU 5378  C   ILE B 289    19898  13934  13167   -679    442   -133       C  
ATOM   5379  O   ILE B 289     -29.089   4.618 -58.036  1.00124.33           O  
ANISOU 5379  O   ILE B 289    20054  13937  13249   -723    565   -181       O  
ATOM   5380  CB  ILE B 289     -30.269   3.749 -55.214  1.00122.15           C  
ANISOU 5380  CB  ILE B 289    19406  13862  13145   -562    455   -124       C  
ATOM   5381  CG1 ILE B 289     -31.025   2.776 -54.278  1.00122.48           C  
ANISOU 5381  CG1 ILE B 289    19317  13989  13232   -541    409    -90       C  
ATOM   5382  CG2 ILE B 289     -30.128   5.121 -54.576  1.00121.72           C  
ANISOU 5382  CG2 ILE B 289    19302  13830  13115   -469    428   -118       C  
ATOM   5383  CD1 ILE B 289     -32.554   2.945 -54.153  1.00129.80           C  
ANISOU 5383  CD1 ILE B 289    20178  15019  14123   -526    276    -19       C  
ATOM   5384  N   ASP B 290     -30.935   5.938 -57.837  1.00118.28           N  
ANISOU 5384  N   ASP B 290    19247  13268  12427   -648    340    -95       N  
ATOM   5385  CA  ASP B 290     -30.401   7.028 -58.644  1.00117.22           C  
ANISOU 5385  CA  ASP B 290    19254  13054  12231   -672    363   -107       C  
ATOM   5386  C   ASP B 290     -29.392   7.779 -57.770  1.00118.53           C  
ANISOU 5386  C   ASP B 290    19351  13206  12479   -609    434   -133       C  
ATOM   5387  O   ASP B 290     -29.781   8.548 -56.888  1.00116.34           O  
ANISOU 5387  O   ASP B 290    18990  12976  12236   -513    364   -111       O  
ATOM   5388  CB  ASP B 290     -31.535   7.943 -59.167  1.00119.19           C  
ANISOU 5388  CB  ASP B 290    19570  13323  12396   -649    217    -54       C  
ATOM   5389  CG  ASP B 290     -31.119   9.098 -60.079  1.00122.87           C  
ANISOU 5389  CG  ASP B 290    20210  13696  12778   -680    221    -55       C  
ATOM   5390  OD1 ASP B 290     -30.034   9.008 -60.712  1.00121.26           O  
ANISOU 5390  OD1 ASP B 290    20113  13409  12553   -760    343    -95       O  
ATOM   5391  OD2 ASP B 290     -31.884  10.081 -60.172  1.00128.19           O  
ANISOU 5391  OD2 ASP B 290    20916  14383  13406   -622    104    -13       O  
ATOM   5392  N   ARG B 291     -28.092   7.475 -57.976  1.00115.32           N  
ANISOU 5392  N   ARG B 291    18973  12738  12105   -662    574   -180       N  
ATOM   5393  CA  ARG B 291     -26.950   8.058 -57.260  1.00115.01           C  
ANISOU 5393  CA  ARG B 291    18869  12682  12150   -633    650   -205       C  
ATOM   5394  C   ARG B 291     -26.921   9.580 -57.405  1.00120.86           C  
ANISOU 5394  C   ARG B 291    19690  13382  12849   -620    595   -185       C  
ATOM   5395  O   ARG B 291     -26.503  10.257 -56.466  1.00120.79           O  
ANISOU 5395  O   ARG B 291    19608  13382  12906   -563    582   -189       O  
ATOM   5396  CB  ARG B 291     -25.619   7.465 -57.763  1.00115.58           C  
ANISOU 5396  CB  ARG B 291    18968  12699  12248   -705    813   -249       C  
ATOM   5397  CG  ARG B 291     -25.467   5.957 -57.580  1.00125.59           C  
ANISOU 5397  CG  ARG B 291    20170  13986  13561   -705    879   -276       C  
ATOM   5398  N   ARG B 292     -27.369  10.111 -58.578  1.00118.35           N  
ANISOU 5398  N   ARG B 292    19538  13013  12417   -675    554   -164       N  
ATOM   5399  CA  ARG B 292     -27.424  11.541 -58.902  1.00118.66           C  
ANISOU 5399  CA  ARG B 292    19693  12996  12397   -671    492   -140       C  
ATOM   5400  C   ARG B 292     -28.506  12.313 -58.142  1.00122.23           C  
ANISOU 5400  C   ARG B 292    20099  13495  12846   -547    342   -104       C  
ATOM   5401  O   ARG B 292     -28.229  13.426 -57.700  1.00121.79           O  
ANISOU 5401  O   ARG B 292    20075  13400  12799   -504    309   -100       O  
ATOM   5402  CB  ARG B 292     -27.564  11.762 -60.417  1.00120.52           C  
ANISOU 5402  CB  ARG B 292    20131  13158  12502   -767    495   -125       C  
ATOM   5403  N   ASP B 293     -29.728  11.732 -57.998  1.00119.43           N  
ANISOU 5403  N   ASP B 293    19677  13223  12479   -491    252    -77       N  
ATOM   5404  CA  ASP B 293     -30.903  12.312 -57.313  1.00119.87           C  
ANISOU 5404  CA  ASP B 293    19667  13347  12531   -359    118    -36       C  
ATOM   5405  C   ASP B 293     -30.492  13.102 -56.065  1.00125.50           C  
ANISOU 5405  C   ASP B 293    20311  14062  13310   -257    117    -51       C  
ATOM   5406  O   ASP B 293     -29.782  12.551 -55.217  1.00125.35           O  
ANISOU 5406  O   ASP B 293    20180  14068  13379   -256    194    -83       O  
ATOM   5407  CB  ASP B 293     -31.934  11.210 -56.955  1.00121.67           C  
ANISOU 5407  CB  ASP B 293    19754  13692  12784   -328     71    -11       C  
ATOM   5408  CG  ASP B 293     -33.368  11.660 -56.668  1.00133.23           C  
ANISOU 5408  CG  ASP B 293    21157  15244  14221   -213    -69     46       C  
ATOM   5409  OD1 ASP B 293     -33.553  12.587 -55.847  1.00134.69           O1-
ANISOU 5409  OD1 ASP B 293    21308  15445  14424    -86   -110     53       O1-
ATOM   5410  OD2 ASP B 293     -34.305  11.049 -57.227  1.00138.26           O  
ANISOU 5410  OD2 ASP B 293    21776  15938  14820   -247   -138     84       O  
ATOM   5411  N   PRO B 294     -30.882  14.399 -55.956  1.00123.26           N  
ANISOU 5411  N   PRO B 294    20110  13743  12981   -172     27    -31       N  
ATOM   5412  CA  PRO B 294     -30.452  15.209 -54.796  1.00122.74           C  
ANISOU 5412  CA  PRO B 294    20014  13658  12963    -81     19    -50       C  
ATOM   5413  C   PRO B 294     -30.868  14.681 -53.415  1.00124.58           C  
ANISOU 5413  C   PRO B 294    20065  14000  13270     35     13    -54       C  
ATOM   5414  O   PRO B 294     -29.992  14.497 -52.575  1.00123.58           O  
ANISOU 5414  O   PRO B 294    19873  13866  13215     28     75    -89       O  
ATOM   5415  CB  PRO B 294     -31.039  16.600 -55.088  1.00125.57           C  
ANISOU 5415  CB  PRO B 294    20520  13954  13238      0    -91    -22       C  
ATOM   5416  CG  PRO B 294     -31.292  16.614 -56.560  1.00130.75           C  
ANISOU 5416  CG  PRO B 294    21313  14562  13806    -96   -112      4       C  
ATOM   5417  CD  PRO B 294     -31.681  15.209 -56.901  1.00125.89           C  
ANISOU 5417  CD  PRO B 294    20588  14036  13209   -155    -77     10       C  
ATOM   5418  N   LEU B 295     -32.167  14.418 -53.183  1.00120.85           N  
ANISOU 5418  N   LEU B 295    19504  13632  12780    135    -60    -14       N  
ATOM   5419  CA  LEU B 295     -32.674  13.929 -51.897  1.00120.41           C  
ANISOU 5419  CA  LEU B 295    19278  13690  12781    246    -62     -8       C  
ATOM   5420  C   LEU B 295     -32.098  12.556 -51.472  1.00123.79           C  
ANISOU 5420  C   LEU B 295    19582  14164  13290    166     33    -30       C  
ATOM   5421  O   LEU B 295     -32.014  12.295 -50.265  1.00123.74           O  
ANISOU 5421  O   LEU B 295    19466  14212  13336    239     54    -40       O  
ATOM   5422  CB  LEU B 295     -34.207  13.917 -51.874  1.00121.07           C  
ANISOU 5422  CB  LEU B 295    19284  13889  12829    354   -151     51       C  
ATOM   5423  N   VAL B 296     -31.685  11.697 -52.453  1.00118.33           N  
ANISOU 5423  N   VAL B 296    18921  13441  12596     22     89    -39       N  
ATOM   5424  CA  VAL B 296     -31.061  10.383 -52.202  1.00116.05           C  
ANISOU 5424  CA  VAL B 296    18545  13173  12377    -55    181    -63       C  
ATOM   5425  C   VAL B 296     -29.670  10.600 -51.578  1.00118.71           C  
ANISOU 5425  C   VAL B 296    18879  13446  12780    -68    258   -112       C  
ATOM   5426  O   VAL B 296     -29.363  10.012 -50.535  1.00117.94           O  
ANISOU 5426  O   VAL B 296    18667  13392  12751    -31    292   -125       O  
ATOM   5427  CB  VAL B 296     -31.033   9.515 -53.485  1.00118.92           C  
ANISOU 5427  CB  VAL B 296    18977  13506  12704   -189    215    -63       C  
ATOM   5428  CG1 VAL B 296     -29.851   8.552 -53.506  1.00117.85           C  
ANISOU 5428  CG1 VAL B 296    18823  13326  12626   -275    336   -109       C  
ATOM   5429  CG2 VAL B 296     -32.343   8.762 -53.648  1.00118.87           C  
ANISOU 5429  CG2 VAL B 296    18902  13593  12669   -187    144    -14       C  
ATOM   5430  N   VAL B 297     -28.865  11.488 -52.205  1.00114.21           N  
ANISOU 5430  N   VAL B 297    18434  12776  12184   -124    278   -132       N  
ATOM   5431  CA  VAL B 297     -27.533  11.921 -51.783  1.00113.07           C  
ANISOU 5431  CA  VAL B 297    18299  12565  12096   -157    336   -169       C  
ATOM   5432  C   VAL B 297     -27.581  12.563 -50.374  1.00114.24           C  
ANISOU 5432  C   VAL B 297    18393  12736  12278    -38    278   -174       C  
ATOM   5433  O   VAL B 297     -26.753  12.234 -49.519  1.00113.60           O  
ANISOU 5433  O   VAL B 297    18230  12660  12273    -38    319   -199       O  
ATOM   5434  CB  VAL B 297     -26.937  12.837 -52.887  1.00117.81           C  
ANISOU 5434  CB  VAL B 297    19061  13061  12641   -250    352   -172       C  
ATOM   5435  CG1 VAL B 297     -26.149  14.029 -52.330  1.00118.00           C  
ANISOU 5435  CG1 VAL B 297    19137  13015  12684   -242    330   -186       C  
ATOM   5436  CG2 VAL B 297     -26.098  12.021 -53.857  1.00117.73           C  
ANISOU 5436  CG2 VAL B 297    19071  13020  12643   -381    471   -190       C  
ATOM   5437  N   ALA B 298     -28.582  13.425 -50.127  1.00108.59           N  
ANISOU 5437  N   ALA B 298    17723  12037  11501     72    182   -150       N  
ATOM   5438  CA  ALA B 298     -28.782  14.087 -48.843  1.00107.37           C  
ANISOU 5438  CA  ALA B 298    17544  11899  11353    204    126   -155       C  
ATOM   5439  C   ALA B 298     -29.020  13.039 -47.750  1.00108.60           C  
ANISOU 5439  C   ALA B 298    17537  12159  11567    263    153   -154       C  
ATOM   5440  O   ALA B 298     -28.326  13.042 -46.732  1.00108.59           O  
ANISOU 5440  O   ALA B 298    17496  12149  11616    289    165   -180       O  
ATOM   5441  CB  ALA B 298     -29.964  15.045 -48.931  1.00108.72           C  
ANISOU 5441  CB  ALA B 298    17790  12080  11439    327     29   -125       C  
ATOM   5442  N   ALA B 299     -29.952  12.105 -48.001  1.00102.35           N  
ANISOU 5442  N   ALA B 299    16660  11460  10768    269    159   -121       N  
ATOM   5443  CA  ALA B 299     -30.290  11.032 -47.074  1.00100.35           C  
ANISOU 5443  CA  ALA B 299    16260  11307  10560    310    185   -109       C  
ATOM   5444  C   ALA B 299     -29.116  10.065 -46.823  1.00 99.66           C  
ANISOU 5444  C   ALA B 299    16118  11194  10555    221    266   -142       C  
ATOM   5445  O   ALA B 299     -28.974   9.583 -45.698  1.00 98.63           O  
ANISOU 5445  O   ALA B 299    15899  11109  10468    273    279   -145       O  
ATOM   5446  CB  ALA B 299     -31.512  10.274 -47.575  1.00101.30           C  
ANISOU 5446  CB  ALA B 299    16315  11522  10653    303    166    -59       C  
ATOM   5447  N   LEU B 300     -28.262   9.806 -47.843  1.00 92.38           N  
ANISOU 5447  N   LEU B 300    15251  10199   9651     96    324   -164       N  
ATOM   5448  CA  LEU B 300     -27.131   8.891 -47.685  1.00 89.81           C  
ANISOU 5448  CA  LEU B 300    14868   9850   9405     27    407   -194       C  
ATOM   5449  C   LEU B 300     -26.095   9.373 -46.670  1.00 93.76           C  
ANISOU 5449  C   LEU B 300    15342  10318   9965     57    407   -222       C  
ATOM   5450  O   LEU B 300     -25.754   8.612 -45.753  1.00 92.81           O  
ANISOU 5450  O   LEU B 300    15126  10232   9904     86    426   -229       O  
ATOM   5451  CB  LEU B 300     -26.478   8.560 -49.034  1.00 89.14           C  
ANISOU 5451  CB  LEU B 300    14852   9700   9316    -98    481   -210       C  
ATOM   5452  CG  LEU B 300     -25.204   7.709 -49.015  1.00 91.85           C  
ANISOU 5452  CG  LEU B 300    15142  10013   9743   -160    580   -243       C  
ATOM   5453  CD1 LEU B 300     -25.414   6.361 -48.346  1.00 90.82           C  
ANISOU 5453  CD1 LEU B 300    14910   9939   9659   -130    600   -238       C  
ATOM   5454  CD2 LEU B 300     -24.668   7.529 -50.399  1.00 92.73           C  
ANISOU 5454  CD2 LEU B 300    15338  10064   9831   -266    660   -258       C  
ATOM   5455  N   HIS B 301     -25.610  10.634 -46.827  1.00 90.21           N  
ANISOU 5455  N   HIS B 301    14984   9797   9495     46    375   -236       N  
ATOM   5456  CA  HIS B 301     -24.582  11.224 -45.966  1.00 89.12           C  
ANISOU 5456  CA  HIS B 301    14840   9615   9408     51    357   -261       C  
ATOM   5457  C   HIS B 301     -25.098  11.572 -44.586  1.00 92.84           C  
ANISOU 5457  C   HIS B 301    15288  10124   9861    181    282   -259       C  
ATOM   5458  O   HIS B 301     -24.295  11.652 -43.647  1.00 92.53           O  
ANISOU 5458  O   HIS B 301    15215  10069   9873    192    265   -279       O  
ATOM   5459  CB  HIS B 301     -23.900  12.403 -46.647  1.00 90.10           C  
ANISOU 5459  CB  HIS B 301    15080   9643   9510    -26    345   -271       C  
ATOM   5460  CG  HIS B 301     -23.236  11.983 -47.918  1.00 93.82           C  
ANISOU 5460  CG  HIS B 301    15564  10082  10000   -155    441   -274       C  
ATOM   5461  ND1 HIS B 301     -21.991  11.386 -47.916  1.00 95.64           N  
ANISOU 5461  ND1 HIS B 301    15711  10308  10322   -230    523   -292       N  
ATOM   5462  CD2 HIS B 301     -23.712  11.996 -49.185  1.00 95.61           C  
ANISOU 5462  CD2 HIS B 301    15876  10289  10160   -208    468   -260       C  
ATOM   5463  CE1 HIS B 301     -21.730  11.103 -49.181  1.00 95.26           C  
ANISOU 5463  CE1 HIS B 301    15704  10234  10255   -322    609   -291       C  
ATOM   5464  NE2 HIS B 301     -22.743  11.438 -49.978  1.00 95.57           N  
ANISOU 5464  NE2 HIS B 301    15853  10261  10197   -317    576   -273       N  
ATOM   5465  N   LEU B 302     -26.436  11.724 -44.441  1.00 88.96           N  
ANISOU 5465  N   LEU B 302    14810   9691   9299    282    238   -233       N  
ATOM   5466  CA  LEU B 302     -27.051  11.983 -43.143  1.00 88.76           C  
ANISOU 5466  CA  LEU B 302    14762   9716   9245    420    185   -227       C  
ATOM   5467  C   LEU B 302     -26.953  10.684 -42.353  1.00 91.51           C  
ANISOU 5467  C   LEU B 302    14979  10139   9651    428    228   -220       C  
ATOM   5468  O   LEU B 302     -26.488  10.679 -41.216  1.00 91.03           O  
ANISOU 5468  O   LEU B 302    14895  10079   9615    476    208   -235       O  
ATOM   5469  CB  LEU B 302     -28.514  12.406 -43.295  1.00 89.31           C  
ANISOU 5469  CB  LEU B 302    14857   9845   9231    527    143   -193       C  
ATOM   5470  CG  LEU B 302     -29.103  13.066 -42.055  1.00 94.97           C  
ANISOU 5470  CG  LEU B 302    15592  10596   9898    689     92   -193       C  
ATOM   5471  CD1 LEU B 302     -29.363  14.533 -42.303  1.00 96.32           C  
ANISOU 5471  CD1 LEU B 302    15914  10690   9994    758     23   -203       C  
ATOM   5472  CD2 LEU B 302     -30.366  12.366 -41.605  1.00 97.56           C  
ANISOU 5472  CD2 LEU B 302    15808  11060  10200    783    107   -148       C  
ATOM   5473  N   CYS B 303     -27.349   9.585 -42.997  1.00 87.49           N  
ANISOU 5473  N   CYS B 303    14402   9681   9159    373    280   -197       N  
ATOM   5474  CA  CYS B 303     -27.303   8.235 -42.479  1.00 87.22           C  
ANISOU 5474  CA  CYS B 303    14261   9704   9175    362    324   -185       C  
ATOM   5475  C   CYS B 303     -25.871   7.856 -42.082  1.00 89.10           C  
ANISOU 5475  C   CYS B 303    14469   9887   9498    311    355   -219       C  
ATOM   5476  O   CYS B 303     -25.692   7.284 -41.002  1.00 89.12           O  
ANISOU 5476  O   CYS B 303    14409   9921   9530    358    350   -216       O  
ATOM   5477  CB  CYS B 303     -27.884   7.259 -43.498  1.00 88.32           C  
ANISOU 5477  CB  CYS B 303    14373   9875   9310    286    366   -159       C  
ATOM   5478  SG  CYS B 303     -29.690   7.329 -43.642  1.00 92.89           S  
ANISOU 5478  SG  CYS B 303    14926  10560   9807    351    320   -100       S  
ATOM   5479  N   ILE B 304     -24.857   8.190 -42.935  1.00 83.50           N  
ANISOU 5479  N   ILE B 304    13800   9099   8826    217    385   -246       N  
ATOM   5480  CA  ILE B 304     -23.435   7.923 -42.647  1.00 81.96           C  
ANISOU 5480  CA  ILE B 304    13559   8861   8721    167    415   -274       C  
ATOM   5481  C   ILE B 304     -22.984   8.667 -41.383  1.00 89.60           C  
ANISOU 5481  C   ILE B 304    14532   9814   9698    229    339   -287       C  
ATOM   5482  O   ILE B 304     -22.440   8.037 -40.487  1.00 90.24           O  
ANISOU 5482  O   ILE B 304    14541   9912   9834    253    334   -290       O  
ATOM   5483  CB  ILE B 304     -22.484   8.169 -43.848  1.00 83.19           C  
ANISOU 5483  CB  ILE B 304    13746   8952   8912     53    475   -293       C  
ATOM   5484  CG1 ILE B 304     -22.777   7.208 -44.996  1.00 82.07           C  
ANISOU 5484  CG1 ILE B 304    13605   8817   8760     -5    557   -287       C  
ATOM   5485  CG2 ILE B 304     -21.007   8.075 -43.418  1.00 82.78           C  
ANISOU 5485  CG2 ILE B 304    13623   8870   8959     13    495   -314       C  
ATOM   5486  CD1 ILE B 304     -22.342   7.712 -46.334  1.00 84.96           C  
ANISOU 5486  CD1 ILE B 304    14050   9126   9107   -102    610   -297       C  
ATOM   5487  N   ALA B 305     -23.230   9.992 -41.314  1.00 88.99           N  
ANISOU 5487  N   ALA B 305    14554   9697   9559    257    273   -293       N  
ATOM   5488  CA  ALA B 305     -22.871  10.847 -40.177  1.00 89.31           C  
ANISOU 5488  CA  ALA B 305    14640   9707   9588    313    189   -310       C  
ATOM   5489  C   ALA B 305     -23.590  10.387 -38.908  1.00 92.91           C  
ANISOU 5489  C   ALA B 305    15062  10232  10010    436    159   -297       C  
ATOM   5490  O   ALA B 305     -22.951  10.264 -37.867  1.00 92.15           O  
ANISOU 5490  O   ALA B 305    14941  10127   9943    459    120   -309       O  
ATOM   5491  CB  ALA B 305     -23.190  12.306 -40.484  1.00 90.27           C  
ANISOU 5491  CB  ALA B 305    14904   9762   9632    328    127   -318       C  
ATOM   5492  N   LEU B 306     -24.895  10.052 -39.022  1.00 89.49           N  
ANISOU 5492  N   LEU B 306    14616   9872   9515    506    182   -268       N  
ATOM   5493  CA  LEU B 306     -25.728   9.557 -37.923  1.00 89.14           C  
ANISOU 5493  CA  LEU B 306    14530   9911   9429    617    174   -245       C  
ATOM   5494  C   LEU B 306     -25.141   8.276 -37.271  1.00 92.58           C  
ANISOU 5494  C   LEU B 306    14867  10374   9935    592    204   -238       C  
ATOM   5495  O   LEU B 306     -25.294   8.090 -36.063  1.00 92.84           O  
ANISOU 5495  O   LEU B 306    14891  10442   9943    672    177   -230       O  
ATOM   5496  CB  LEU B 306     -27.182   9.379 -38.391  1.00 89.03           C  
ANISOU 5496  CB  LEU B 306    14495   9979   9352    667    201   -205       C  
ATOM   5497  CG  LEU B 306     -28.287   9.432 -37.344  1.00 94.31           C  
ANISOU 5497  CG  LEU B 306    15147  10739   9946    807    188   -176       C  
ATOM   5498  CD1 LEU B 306     -28.252  10.724 -36.535  1.00 94.86           C  
ANISOU 5498  CD1 LEU B 306    15332  10764   9949    918    124   -206       C  
ATOM   5499  CD2 LEU B 306     -29.632   9.324 -38.012  1.00 98.57           C  
ANISOU 5499  CD2 LEU B 306    15647  11365  10441    835    210   -131       C  
ATOM   5500  N   GLY B 307     -24.416   7.470 -38.060  1.00 87.19           N  
ANISOU 5500  N   GLY B 307    14127   9668   9334    488    258   -243       N  
ATOM   5501  CA  GLY B 307     -23.683   6.298 -37.589  1.00 86.17           C  
ANISOU 5501  CA  GLY B 307    13915   9545   9281    464    284   -240       C  
ATOM   5502  C   GLY B 307     -22.475   6.729 -36.768  1.00 89.91           C  
ANISOU 5502  C   GLY B 307    14390   9968   9805    465    225   -267       C  
ATOM   5503  O   GLY B 307     -22.206   6.175 -35.693  1.00 88.25           O  
ANISOU 5503  O   GLY B 307    14145   9776   9612    511    197   -260       O  
ATOM   5504  N   TYR B 308     -21.777   7.783 -37.250  1.00 87.98           N  
ANISOU 5504  N   TYR B 308    14195   9658   9576    411    197   -294       N  
ATOM   5505  CA  TYR B 308     -20.612   8.381 -36.592  1.00 88.48           C  
ANISOU 5505  CA  TYR B 308    14264   9667   9686    388    125   -317       C  
ATOM   5506  C   TYR B 308     -20.948   9.095 -35.292  1.00 94.24           C  
ANISOU 5506  C   TYR B 308    15076  10391  10339    482     28   -323       C  
ATOM   5507  O   TYR B 308     -20.070   9.231 -34.443  1.00 94.01           O  
ANISOU 5507  O   TYR B 308    15041  10332  10346    477    -44   -335       O  
ATOM   5508  CB  TYR B 308     -19.868   9.317 -37.536  1.00 88.85           C  
ANISOU 5508  CB  TYR B 308    14347   9648   9764    285    125   -335       C  
ATOM   5509  CG  TYR B 308     -18.982   8.569 -38.495  1.00 90.03           C  
ANISOU 5509  CG  TYR B 308    14397   9796  10015    189    214   -334       C  
ATOM   5510  CD1 TYR B 308     -17.731   8.105 -38.100  1.00 92.34           C  
ANISOU 5510  CD1 TYR B 308    14587  10085  10414    153    207   -338       C  
ATOM   5511  CD2 TYR B 308     -19.384   8.334 -39.807  1.00 90.48           C  
ANISOU 5511  CD2 TYR B 308    14465   9856  10056    140    305   -330       C  
ATOM   5512  CE1 TYR B 308     -16.906   7.418 -38.985  1.00 93.43           C  
ANISOU 5512  CE1 TYR B 308    14629  10226  10643     83    302   -337       C  
ATOM   5513  CE2 TYR B 308     -18.566   7.648 -40.702  1.00 91.18           C  
ANISOU 5513  CE2 TYR B 308    14479   9940  10226     62    399   -333       C  
ATOM   5514  CZ  TYR B 308     -17.326   7.198 -40.286  1.00 98.93           C  
ANISOU 5514  CZ  TYR B 308    15352  10921  11314     39    404   -338       C  
ATOM   5515  OH  TYR B 308     -16.517   6.526 -41.157  1.00103.25           O  
ANISOU 5515  OH  TYR B 308    15821  11470  11940    -18    508   -341       O  
ATOM   5516  N   ILE B 309     -22.209   9.548 -35.139  1.00 92.64           N  
ANISOU 5516  N   ILE B 309    14951  10219  10029    573     25   -315       N  
ATOM   5517  CA  ILE B 309     -22.694  10.222 -33.937  1.00 94.10           C  
ANISOU 5517  CA  ILE B 309    15230  10404  10119    687    -48   -322       C  
ATOM   5518  C   ILE B 309     -22.666   9.232 -32.771  1.00100.98           C  
ANISOU 5518  C   ILE B 309    16044  11328  10996    744    -53   -305       C  
ATOM   5519  O   ILE B 309     -22.215   9.585 -31.689  1.00100.92           O  
ANISOU 5519  O   ILE B 309    16095  11289  10962    785   -133   -321       O  
ATOM   5520  CB  ILE B 309     -24.069  10.917 -34.183  1.00 97.16           C  
ANISOU 5520  CB  ILE B 309    15697  10822  10396    782    -33   -313       C  
ATOM   5521  CG1 ILE B 309     -23.855  12.305 -34.834  1.00 97.34           C  
ANISOU 5521  CG1 ILE B 309    15842  10752  10389    751    -83   -341       C  
ATOM   5522  CG2 ILE B 309     -24.919  11.032 -32.896  1.00 98.78           C  
ANISOU 5522  CG2 ILE B 309    15954  11079  10499    934    -56   -305       C  
ATOM   5523  CD1 ILE B 309     -25.001  12.817 -35.639  1.00101.79           C  
ANISOU 5523  CD1 ILE B 309    16452  11338  10884    803    -53   -327       C  
ATOM   5524  N   ASN B 310     -23.054   7.977 -33.020  1.00100.03           N  
ANISOU 5524  N   ASN B 310    15822  11276  10910    734     25   -272       N  
ATOM   5525  CA  ASN B 310     -23.019   6.941 -31.990  1.00101.15           C  
ANISOU 5525  CA  ASN B 310    15915  11461  11057    777     24   -248       C  
ATOM   5526  C   ASN B 310     -21.601   6.529 -31.695  1.00107.60           C  
ANISOU 5526  C   ASN B 310    16681  12226  11975    716    -20   -262       C  
ATOM   5527  O   ASN B 310     -21.246   6.367 -30.538  1.00106.47           O  
ANISOU 5527  O   ASN B 310    16557  12079  11817    763    -84   -260       O  
ATOM   5528  CB  ASN B 310     -23.826   5.711 -32.406  1.00101.17           C  
ANISOU 5528  CB  ASN B 310    15835  11537  11066    767    114   -205       C  
ATOM   5529  CG  ASN B 310     -24.195   4.848 -31.229  1.00126.20           C  
ANISOU 5529  CG  ASN B 310    18990  14762  14200    832    115   -169       C  
ATOM   5530  OD1 ASN B 310     -23.778   3.684 -31.127  1.00128.08           O  
ANISOU 5530  OD1 ASN B 310    19165  15001  14500    795    136   -149       O  
ATOM   5531  ND2 ASN B 310     -24.976   5.403 -30.307  1.00112.94           N  
ANISOU 5531  ND2 ASN B 310    17376  13124  12411    935     94   -159       N  
ATOM   5532  N   SER B 311     -20.801   6.342 -32.755  1.00108.18           N  
ANISOU 5532  N   SER B 311    16688  12266  12149    616     15   -274       N  
ATOM   5533  CA  SER B 311     -19.408   5.891 -32.705  1.00109.47           C  
ANISOU 5533  CA  SER B 311    16769  12394  12430    556     -8   -283       C  
ATOM   5534  C   SER B 311     -18.493   6.779 -31.888  1.00115.07           C  
ANISOU 5534  C   SER B 311    17520  13054  13150    548   -127   -304       C  
ATOM   5535  O   SER B 311     -17.631   6.265 -31.173  1.00115.91           O  
ANISOU 5535  O   SER B 311    17569  13153  13319    550   -182   -298       O  
ATOM   5536  CB  SER B 311     -18.841   5.726 -34.118  1.00112.24           C  
ANISOU 5536  CB  SER B 311    17052  12726  12869    458     71   -292       C  
ATOM   5537  OG  SER B 311     -19.078   4.426 -34.633  1.00118.52           O  
ANISOU 5537  OG  SER B 311    17781  13551  13701    453    161   -273       O  
ATOM   5538  N   SER B 312     -18.686   8.094 -31.980  1.00111.75           N  
ANISOU 5538  N   SER B 312    17203  12591  12666    540   -176   -327       N  
ATOM   5539  CA  SER B 312     -17.795   9.048 -31.354  1.00113.26           C  
ANISOU 5539  CA  SER B 312    17451  12718  12864    507   -298   -349       C  
ATOM   5540  C   SER B 312     -18.434   9.971 -30.319  1.00118.78           C  
ANISOU 5540  C   SER B 312    18314  13388  13428    597   -388   -366       C  
ATOM   5541  O   SER B 312     -17.726  10.428 -29.416  1.00120.85           O  
ANISOU 5541  O   SER B 312    18630  13602  13684    590   -506   -380       O  
ATOM   5542  CB  SER B 312     -17.102   9.862 -32.437  1.00119.14           C  
ANISOU 5542  CB  SER B 312    18186  13411  13669    386   -292   -363       C  
ATOM   5543  OG  SER B 312     -16.627   9.009 -33.470  1.00130.76           O  
ANISOU 5543  OG  SER B 312    19520  14915  15249    317   -186   -350       O  
ATOM   5544  N   LEU B 313     -19.740  10.273 -30.445  1.00113.03           N  
ANISOU 5544  N   LEU B 313    17668  12689  12591    685   -336   -365       N  
ATOM   5545  CA  LEU B 313     -20.430  11.144 -29.481  1.00111.98           C  
ANISOU 5545  CA  LEU B 313    17697  12533  12318    797   -401   -383       C  
ATOM   5546  C   LEU B 313     -21.504  10.331 -28.725  1.00110.08           C  
ANISOU 5546  C   LEU B 313    17445  12382  11997    922   -342   -354       C  
ATOM   5547  O   LEU B 313     -22.681  10.705 -28.635  1.00109.44           O  
ANISOU 5547  O   LEU B 313    17432  12340  11810   1025   -299   -350       O  
ATOM   5548  CB  LEU B 313     -20.992  12.410 -30.179  1.00112.67           C  
ANISOU 5548  CB  LEU B 313    17905  12569  12335    808   -403   -405       C  
ATOM   5549  CG  LEU B 313     -19.986  13.438 -30.783  1.00118.65           C  
ANISOU 5549  CG  LEU B 313    18719  13221  13142    682   -478   -431       C  
ATOM   5550  CD1 LEU B 313     -18.761  13.655 -29.882  1.00119.62           C  
ANISOU 5550  CD1 LEU B 313    18863  13283  13305    619   -606   -446       C  
ATOM   5551  CD2 LEU B 313     -19.596  13.090 -32.245  1.00120.77           C  
ANISOU 5551  CD2 LEU B 313    18863  13502  13520    556   -391   -414       C  
ATOM   5552  N   ASN B 314     -21.054   9.203 -28.183  1.00102.96           N  
ANISOU 5552  N   ASN B 314    16452  11516  11152    910   -339   -331       N  
ATOM   5553  CA  ASN B 314     -21.859   8.204 -27.500  1.00101.58           C  
ANISOU 5553  CA  ASN B 314    16246  11425  10925    994   -281   -292       C  
ATOM   5554  C   ASN B 314     -22.462   8.657 -26.157  1.00106.16           C  
ANISOU 5554  C   ASN B 314    16963  12016  11359   1123   -325   -297       C  
ATOM   5555  O   ASN B 314     -21.746   9.312 -25.390  1.00106.50           O  
ANISOU 5555  O   ASN B 314    17108  11984  11371   1129   -438   -328       O  
ATOM   5556  CB  ASN B 314     -21.033   6.935 -27.320  1.00 95.92           C  
ANISOU 5556  CB  ASN B 314    15413  10719  10313    939   -281   -268       C  
ATOM   5557  CG  ASN B 314     -21.855   5.775 -26.894  1.00111.04           C  
ANISOU 5557  CG  ASN B 314    17287  12714  12191    994   -207   -220       C  
ATOM   5558  OD1 ASN B 314     -21.974   5.492 -25.701  1.00111.11           O  
ANISOU 5558  OD1 ASN B 314    17350  12737  12128   1063   -245   -204       O  
ATOM   5559  ND2 ASN B 314     -22.490   5.119 -27.856  1.00101.97           N  
ANISOU 5559  ND2 ASN B 314    16053  11615  11076    959   -103   -194       N  
ATOM   5560  N   PRO B 315     -23.729   8.232 -25.816  1.00101.47           N  
ANISOU 5560  N   PRO B 315    16367  11514  10673   1221   -236   -261       N  
ATOM   5561  CA  PRO B 315     -24.328   8.608 -24.508  1.00101.29           C  
ANISOU 5561  CA  PRO B 315    16474  11511  10500   1356   -257   -261       C  
ATOM   5562  C   PRO B 315     -23.520   8.258 -23.254  1.00103.69           C  
ANISOU 5562  C   PRO B 315    16840  11775  10781   1365   -350   -264       C  
ATOM   5563  O   PRO B 315     -23.790   8.837 -22.217  1.00104.34           O  
ANISOU 5563  O   PRO B 315    17070  11843  10733   1466   -392   -281       O  
ATOM   5564  CB  PRO B 315     -25.679   7.888 -24.513  1.00102.71           C  
ANISOU 5564  CB  PRO B 315    16581  11819  10624   1423   -128   -205       C  
ATOM   5565  CG  PRO B 315     -26.013   7.745 -25.952  1.00106.35           C  
ANISOU 5565  CG  PRO B 315    16928  12307  11172   1347    -61   -193       C  
ATOM   5566  CD  PRO B 315     -24.703   7.469 -26.630  1.00101.57           C  
ANISOU 5566  CD  PRO B 315    16264  11620  10707   1211   -114   -216       C  
ATOM   5567  N   VAL B 316     -22.544   7.335 -23.335  1.00 98.89           N  
ANISOU 5567  N   VAL B 316    16131  11149  10294   1269   -385   -248       N  
ATOM   5568  CA  VAL B 316     -21.663   7.005 -22.206  1.00 98.80           C  
ANISOU 5568  CA  VAL B 316    16170  11094  10276   1270   -495   -248       C  
ATOM   5569  C   VAL B 316     -20.622   8.142 -22.068  1.00103.23           C  
ANISOU 5569  C   VAL B 316    16824  11546  10852   1225   -640   -303       C  
ATOM   5570  O   VAL B 316     -20.350   8.595 -20.950  1.00102.66           O  
ANISOU 5570  O   VAL B 316    16894  11426  10684   1275   -746   -322       O  
ATOM   5571  CB  VAL B 316     -20.986   5.617 -22.362  1.00101.84           C  
ANISOU 5571  CB  VAL B 316    16411  11495  10788   1198   -485   -208       C  
ATOM   5572  CG1 VAL B 316     -19.941   5.382 -21.274  1.00102.20           C  
ANISOU 5572  CG1 VAL B 316    16504  11486  10840   1196   -623   -209       C  
ATOM   5573  CG2 VAL B 316     -22.015   4.492 -22.366  1.00101.33           C  
ANISOU 5573  CG2 VAL B 316    16286  11523  10692   1232   -359   -150       C  
ATOM   5574  N   LEU B 317     -20.054   8.597 -23.219  1.00100.84           N  
ANISOU 5574  N   LEU B 317    16448  11205  10664   1122   -646   -325       N  
ATOM   5575  CA  LEU B 317     -19.073   9.689 -23.310  1.00101.86           C  
ANISOU 5575  CA  LEU B 317    16644  11233  10824   1047   -774   -369       C  
ATOM   5576  C   LEU B 317     -19.683  11.024 -22.840  1.00104.30           C  
ANISOU 5576  C   LEU B 317    17166  11486  10976   1130   -821   -411       C  
ATOM   5577  O   LEU B 317     -18.989  11.815 -22.203  1.00104.31           O  
ANISOU 5577  O   LEU B 317    17297  11398  10940   1107   -963   -444       O  
ATOM   5578  CB  LEU B 317     -18.504   9.800 -24.739  1.00101.96           C  
ANISOU 5578  CB  LEU B 317    16525  11232  10982    920   -734   -373       C  
ATOM   5579  CG  LEU B 317     -17.608   8.637 -25.183  1.00108.08           C  
ANISOU 5579  CG  LEU B 317    17107  12039  11920    836   -710   -343       C  
ATOM   5580  CD1 LEU B 317     -17.643   8.448 -26.707  1.00108.63           C  
ANISOU 5580  CD1 LEU B 317    17053  12132  12090    758   -593   -338       C  
ATOM   5581  CD2 LEU B 317     -16.171   8.806 -24.681  1.00111.91           C  
ANISOU 5581  CD2 LEU B 317    17564  12467  12488    757   -859   -350       C  
ATOM   5582  N   TYR B 318     -20.993  11.235 -23.113  1.00 99.41           N  
ANISOU 5582  N   TYR B 318    16587  10922  10264   1233   -705   -407       N  
ATOM   5583  CA  TYR B 318     -21.774  12.383 -22.671  1.00100.07           C  
ANISOU 5583  CA  TYR B 318    16868  10968  10188   1352   -720   -442       C  
ATOM   5584  C   TYR B 318     -21.865  12.369 -21.128  1.00103.41           C  
ANISOU 5584  C   TYR B 318    17441  11379  10470   1459   -783   -450       C  
ATOM   5585  O   TYR B 318     -21.485  13.344 -20.483  1.00103.69           O  
ANISOU 5585  O   TYR B 318    17667  11313  10419   1480   -905   -496       O  
ATOM   5586  CB  TYR B 318     -23.185  12.345 -23.300  1.00101.95           C  
ANISOU 5586  CB  TYR B 318    17063  11298  10375   1448   -568   -420       C  
ATOM   5587  CG  TYR B 318     -24.091  13.480 -22.851  1.00107.30           C  
ANISOU 5587  CG  TYR B 318    17934  11951  10886   1603   -565   -453       C  
ATOM   5588  CD1 TYR B 318     -24.729  13.442 -21.614  1.00110.90           C  
ANISOU 5588  CD1 TYR B 318    18503  12444  11191   1752   -547   -451       C  
ATOM   5589  CD2 TYR B 318     -24.323  14.583 -23.671  1.00108.52           C  
ANISOU 5589  CD2 TYR B 318    18164  12042  11027   1609   -575   -484       C  
ATOM   5590  CE1 TYR B 318     -25.543  14.488 -21.188  1.00113.74           C  
ANISOU 5590  CE1 TYR B 318    19046  12779  11392   1914   -535   -485       C  
ATOM   5591  CE2 TYR B 318     -25.170  15.617 -23.269  1.00110.44           C  
ANISOU 5591  CE2 TYR B 318    18591  12256  11115   1770   -571   -515       C  
ATOM   5592  CZ  TYR B 318     -25.774  15.566 -22.022  1.00120.21           C  
ANISOU 5592  CZ  TYR B 318    19936  13532  12205   1928   -548   -517       C  
ATOM   5593  OH  TYR B 318     -26.591  16.577 -21.582  1.00125.57           O  
ANISOU 5593  OH  TYR B 318    20803  14182  12724   2107   -536   -551       O  
ATOM   5594  N   ALA B 319     -22.387  11.262 -20.558  1.00 99.34           N  
ANISOU 5594  N   ALA B 319    16853  10964   9927   1520   -702   -403       N  
ATOM   5595  CA  ALA B 319     -22.585  11.013 -19.126  1.00 99.68           C  
ANISOU 5595  CA  ALA B 319    17022  11018   9833   1622   -732   -396       C  
ATOM   5596  C   ALA B 319     -21.300  11.201 -18.297  1.00104.51           C  
ANISOU 5596  C   ALA B 319    17732  11525  10453   1556   -918   -422       C  
ATOM   5597  O   ALA B 319     -21.354  11.806 -17.216  1.00103.63           O  
ANISOU 5597  O   ALA B 319    17830  11357  10188   1641   -997   -453       O  
ATOM   5598  CB  ALA B 319     -23.163   9.621 -18.922  1.00 99.45           C  
ANISOU 5598  CB  ALA B 319    16857  11111   9818   1645   -615   -328       C  
ATOM   5599  N   PHE B 320     -20.149  10.712 -18.839  1.00101.91           N  
ANISOU 5599  N   PHE B 320    17252  11170  10299   1407   -987   -410       N  
ATOM   5600  CA  PHE B 320     -18.801  10.809 -18.262  1.00103.17           C  
ANISOU 5600  CA  PHE B 320    17446  11245  10511   1317  -1171   -424       C  
ATOM   5601  C   PHE B 320     -18.388  12.286 -18.100  1.00110.38           C  
ANISOU 5601  C   PHE B 320    18550  12034  11356   1291  -1309   -485       C  
ATOM   5602  O   PHE B 320     -17.867  12.663 -17.047  1.00111.83           O  
ANISOU 5602  O   PHE B 320    18894  12142  11455   1299  -1460   -507       O  
ATOM   5603  CB  PHE B 320     -17.773  10.036 -19.131  1.00104.18           C  
ANISOU 5603  CB  PHE B 320    17338  11390  10856   1174  -1182   -395       C  
ATOM   5604  CG  PHE B 320     -16.325  10.203 -18.720  1.00107.00           C  
ANISOU 5604  CG  PHE B 320    17685  11672  11296   1067  -1372   -403       C  
ATOM   5605  CD1 PHE B 320     -15.791   9.463 -17.669  1.00111.60           C  
ANISOU 5605  CD1 PHE B 320    18277  12258  11870   1085  -1470   -376       C  
ATOM   5606  CD2 PHE B 320     -15.499  11.108 -19.375  1.00109.89           C  
ANISOU 5606  CD2 PHE B 320    18034  11968  11750    944  -1460   -431       C  
ATOM   5607  CE1 PHE B 320     -14.458   9.637 -17.270  1.00113.61           C  
ANISOU 5607  CE1 PHE B 320    18511  12451  12205    987  -1660   -378       C  
ATOM   5608  CE2 PHE B 320     -14.172  11.295 -18.963  1.00114.07           C  
ANISOU 5608  CE2 PHE B 320    18543  12440  12360    836  -1644   -431       C  
ATOM   5609  CZ  PHE B 320     -13.661  10.553 -17.920  1.00112.98           C  
ANISOU 5609  CZ  PHE B 320    18401  12311  12217    861  -1746   -404       C  
ATOM   5610  N   LEU B 321     -18.605  13.107 -19.153  1.00106.69           N  
ANISOU 5610  N   LEU B 321    18077  11537  10924   1254  -1265   -510       N  
ATOM   5611  CA  LEU B 321     -18.275  14.534 -19.145  1.00107.39           C  
ANISOU 5611  CA  LEU B 321    18356  11497  10950   1220  -1387   -565       C  
ATOM   5612  C   LEU B 321     -19.217  15.289 -18.220  1.00114.46           C  
ANISOU 5612  C   LEU B 321    19516  12352  11621   1392  -1387   -604       C  
ATOM   5613  O   LEU B 321     -18.765  16.162 -17.483  1.00115.84           O  
ANISOU 5613  O   LEU B 321    19908  12409  11699   1388  -1541   -648       O  
ATOM   5614  CB  LEU B 321     -18.275  15.135 -20.568  1.00106.11           C  
ANISOU 5614  CB  LEU B 321    18118  11314  10884   1132  -1332   -573       C  
ATOM   5615  CG  LEU B 321     -17.160  14.647 -21.506  1.00109.04           C  
ANISOU 5615  CG  LEU B 321    18260  11702  11469    949  -1349   -544       C  
ATOM   5616  CD1 LEU B 321     -17.418  15.074 -22.931  1.00107.61           C  
ANISOU 5616  CD1 LEU B 321    18007  11521  11357    889  -1252   -545       C  
ATOM   5617  CD2 LEU B 321     -15.778  15.106 -21.038  1.00111.85           C  
ANISOU 5617  CD2 LEU B 321    18654  11964  11881    812  -1550   -556       C  
ATOM   5618  N   ASP B 322     -20.509  14.897 -18.212  1.00111.68           N  
ANISOU 5618  N   ASP B 322    19145  12104  11186   1543  -1216   -585       N  
ATOM   5619  CA  ASP B 322     -21.577  15.440 -17.368  1.00112.94           C  
ANISOU 5619  CA  ASP B 322    19518  12262  11133   1737  -1168   -612       C  
ATOM   5620  C   ASP B 322     -21.280  15.202 -15.873  1.00119.02           C  
ANISOU 5620  C   ASP B 322    20445  13002  11774   1794  -1264   -618       C  
ATOM   5621  O   ASP B 322     -21.704  15.982 -15.019  1.00120.14           O  
ANISOU 5621  O   ASP B 322    20841  13079  11727   1923  -1299   -663       O  
ATOM   5622  CB  ASP B 322     -22.907  14.768 -17.741  1.00114.18           C  
ANISOU 5622  CB  ASP B 322    19540  12573  11272   1855   -955   -566       C  
ATOM   5623  CG  ASP B 322     -24.130  15.654 -17.628  1.00127.78           C  
ANISOU 5623  CG  ASP B 322    21416  14304  12831   2042   -866   -594       C  
ATOM   5624  OD1 ASP B 322     -23.987  16.813 -17.183  1.00129.02           O  
ANISOU 5624  OD1 ASP B 322    21819  14334  12869   2100   -966   -655       O  
ATOM   5625  OD2 ASP B 322     -25.235  15.187 -17.985  1.00135.96           O1-
ANISOU 5625  OD2 ASP B 322    22328  15473  13859   2133   -699   -552       O1-
ATOM   5626  N   LYS B 323     -20.555  14.118 -15.571  1.00115.32           N  
ANISOU 5626  N   LYS B 323    19835  12576  11404   1704  -1307   -575       N  
ATOM   5627  CA  LYS B 323     -20.156  13.752 -14.220  1.00116.26           C  
ANISOU 5627  CA  LYS B 323    20082  12670  11423   1736  -1411   -571       C  
ATOM   5628  C   LYS B 323     -18.915  14.560 -13.797  1.00120.17           C  
ANISOU 5628  C   LYS B 323    20726  13013  11920   1625  -1652   -617       C  
ATOM   5629  O   LYS B 323     -18.937  15.196 -12.746  1.00120.66           O  
ANISOU 5629  O   LYS B 323    21053  12988  11805   1700  -1753   -658       O  
ATOM   5630  CB  LYS B 323     -19.884  12.229 -14.152  1.00118.23           C  
ANISOU 5630  CB  LYS B 323    20113  13022  11788   1684  -1365   -500       C  
ATOM   5631  CG  LYS B 323     -19.637  11.669 -12.754  1.00134.20           C  
ANISOU 5631  CG  LYS B 323    22257  15037  13697   1733  -1449   -482       C  
ATOM   5632  CD  LYS B 323     -19.178  10.217 -12.823  1.00146.14           C  
ANISOU 5632  CD  LYS B 323    23553  16625  15350   1661  -1430   -412       C  
ATOM   5633  CE  LYS B 323     -18.742   9.667 -11.482  1.00161.14           C  
ANISOU 5633  CE  LYS B 323    25572  18500  17153   1689  -1546   -390       C  
ATOM   5634  NZ  LYS B 323     -17.361  10.090 -11.123  1.00172.26           N1+
ANISOU 5634  NZ  LYS B 323    27034  19796  18620   1579  -1789   -416       N1+
ATOM   5635  N   ASN B 324     -17.841  14.518 -14.616  1.00115.84           N  
ANISOU 5635  N   ASN B 324    20008  12436  11572   1444  -1740   -606       N  
ATOM   5636  CA  ASN B 324     -16.545  15.146 -14.349  1.00116.46           C  
ANISOU 5636  CA  ASN B 324    20162  12391  11696   1299  -1972   -631       C  
ATOM   5637  C   ASN B 324     -16.533  16.663 -14.453  1.00120.32           C  
ANISOU 5637  C   ASN B 324    20886  12739  12089   1284  -2067   -697       C  
ATOM   5638  O   ASN B 324     -15.718  17.291 -13.775  1.00121.66           O  
ANISOU 5638  O   ASN B 324    21225  12791  12210   1209  -2275   -726       O  
ATOM   5639  CB  ASN B 324     -15.459  14.535 -15.221  1.00117.29           C  
ANISOU 5639  CB  ASN B 324    19981  12534  12049   1120  -2007   -589       C  
ATOM   5640  CG  ASN B 324     -15.099  13.144 -14.766  1.00144.09           C  
ANISOU 5640  CG  ASN B 324    23210  16017  15520   1123  -2002   -532       C  
ATOM   5641  OD1 ASN B 324     -14.323  12.957 -13.824  1.00138.95           O  
ANISOU 5641  OD1 ASN B 324    22619  15325  14851   1090  -2171   -524       O  
ATOM   5642  ND2 ASN B 324     -15.680  12.136 -15.399  1.00135.57           N  
ANISOU 5642  ND2 ASN B 324    21935  15055  14520   1164  -1815   -490       N  
ATOM   5643  N   PHE B 325     -17.421  17.254 -15.273  1.00115.52           N  
ANISOU 5643  N   PHE B 325    20301  12137  11452   1352  -1930   -718       N  
ATOM   5644  CA  PHE B 325     -17.539  18.715 -15.427  1.00115.93           C  
ANISOU 5644  CA  PHE B 325    20598  12048  11403   1358  -2006   -779       C  
ATOM   5645  C   PHE B 325     -18.902  19.231 -14.907  1.00121.85           C  
ANISOU 5645  C   PHE B 325    21576  12792  11927   1596  -1893   -818       C  
ATOM   5646  O   PHE B 325     -19.386  20.272 -15.342  1.00121.10           O  
ANISOU 5646  O   PHE B 325    21631  12619  11761   1652  -1874   -860       O  
ATOM   5647  CB  PHE B 325     -17.261  19.146 -16.883  1.00116.23           C  
ANISOU 5647  CB  PHE B 325    20491  12070  11600   1223  -1971   -772       C  
ATOM   5648  CG  PHE B 325     -15.857  18.881 -17.382  1.00116.95           C  
ANISOU 5648  CG  PHE B 325    20388  12152  11897    989  -2091   -739       C  
ATOM   5649  CD1 PHE B 325     -14.776  19.607 -16.890  1.00120.87           C  
ANISOU 5649  CD1 PHE B 325    21019  12517  12389    849  -2320   -761       C  
ATOM   5650  CD2 PHE B 325     -15.620  17.932 -18.367  1.00117.09           C  
ANISOU 5650  CD2 PHE B 325    20089  12290  12111    907  -1973   -685       C  
ATOM   5651  CE1 PHE B 325     -13.480  19.368 -17.357  1.00121.53           C  
ANISOU 5651  CE1 PHE B 325    20897  12609  12672    633  -2425   -722       C  
ATOM   5652  CE2 PHE B 325     -14.324  17.700 -18.837  1.00119.86           C  
ANISOU 5652  CE2 PHE B 325    20250  12641  12652    707  -2067   -654       C  
ATOM   5653  CZ  PHE B 325     -13.265  18.425 -18.334  1.00119.33           C  
ANISOU 5653  CZ  PHE B 325    20295  12459  12587    571  -2290   -669       C  
ATOM   5654  N   LYS B 326     -19.496  18.481 -13.951  1.00121.30           N  
ANISOU 5654  N   LYS B 326    21534  12810  11746   1739  -1817   -801       N  
ATOM   5655  CA  LYS B 326     -20.778  18.707 -13.272  1.00122.75           C  
ANISOU 5655  CA  LYS B 326    21899  13026  11714   1979  -1687   -823       C  
ATOM   5656  C   LYS B 326     -20.999  20.157 -12.920  1.00130.36           C  
ANISOU 5656  C   LYS B 326    23205  13828  12497   2071  -1774   -903       C  
ATOM   5657  O   LYS B 326     -22.001  20.711 -13.350  1.00130.27           O  
ANISOU 5657  O   LYS B 326    23250  13832  12414   2215  -1644   -922       O  
ATOM   5658  CB  LYS B 326     -20.876  17.847 -11.992  1.00125.77           C  
ANISOU 5658  CB  LYS B 326    22329  13470  11986   2060  -1682   -799       C  
ATOM   5659  CG  LYS B 326     -22.235  17.176 -11.787  1.00138.95           C  
ANISOU 5659  CG  LYS B 326    23930  15300  13566   2250  -1446   -760       C  
ATOM   5660  CD  LYS B 326     -22.247  16.246 -10.569  1.00150.95           C  
ANISOU 5660  CD  LYS B 326    25488  16879  14986   2303  -1442   -725       C  
ATOM   5661  CE  LYS B 326     -21.761  14.847 -10.884  1.00159.61           C  
ANISOU 5661  CE  LYS B 326    26293  18083  16270   2172  -1419   -648       C  
ATOM   5662  NZ  LYS B 326     -21.336  14.120  -9.660  1.00166.82           N  
ANISOU 5662  NZ  LYS B 326    27291  18995  17099   2177  -1503   -622       N  
ATOM   5663  N   ARG B 327     -20.050  20.772 -12.171  1.00129.65           N  
ANISOU 5663  N   ARG B 327    23344  13580  12339   1984  -2000   -947       N  
ATOM   5664  CA  ARG B 327     -20.090  22.168 -11.717  1.00131.74           C  
ANISOU 5664  CA  ARG B 327    23980  13657  12419   2050  -2123  -1028       C  
ATOM   5665  C   ARG B 327     -20.131  23.192 -12.857  1.00135.83           C  
ANISOU 5665  C   ARG B 327    24527  14082  13000   1995  -2131  -1055       C  
ATOM   5666  O   ARG B 327     -20.825  24.203 -12.720  1.00137.05           O  
ANISOU 5666  O   ARG B 327    24946  14140  12988   2152  -2110  -1112       O  
ATOM   5667  CB  ARG B 327     -18.930  22.475 -10.749  1.00134.51           C  
ANISOU 5667  CB  ARG B 327    24536  13860  12711   1921  -2388  -1058       C  
ATOM   5668  CG  ARG B 327     -19.156  22.015  -9.303  1.00149.35           C  
ANISOU 5668  CG  ARG B 327    26589  15758  14399   2056  -2403  -1066       C  
ATOM   5669  CD  ARG B 327     -18.675  20.593  -9.040  1.00163.03           C  
ANISOU 5669  CD  ARG B 327    28054  17631  16261   1970  -2394   -990       C  
ATOM   5670  NE  ARG B 327     -18.512  20.317  -7.610  1.00178.84           N  
ANISOU 5670  NE  ARG B 327    30268  19600  18085   2036  -2493  -1001       N  
ATOM   5671  CZ  ARG B 327     -18.237  19.118  -7.097  1.00197.62           C  
ANISOU 5671  CZ  ARG B 327    32491  22083  20511   2010  -2487   -940       C  
ATOM   5672  NH1 ARG B 327     -18.105  18.061  -7.891  1.00184.20           N  
ANISOU 5672  NH1 ARG B 327    30425  20529  19033   1925  -2384   -867       N  
ATOM   5673  NH2 ARG B 327     -18.101  18.966  -5.785  1.00187.22           N  
ANISOU 5673  NH2 ARG B 327    31402  20721  19012   2072  -2587   -952       N  
ATOM   5674  N   CYS B 328     -19.400  22.935 -13.971  1.00131.06           N  
ANISOU 5674  N   CYS B 328    23662  13507  12630   1782  -2157  -1012       N  
ATOM   5675  CA  CYS B 328     -19.342  23.814 -15.153  1.00130.81           C  
ANISOU 5675  CA  CYS B 328    23631  13394  12675   1698  -2163  -1025       C  
ATOM   5676  C   CYS B 328     -20.677  23.913 -15.870  1.00132.19           C  
ANISOU 5676  C   CYS B 328    23755  13656  12817   1885  -1945  -1021       C  
ATOM   5677  O   CYS B 328     -20.981  24.963 -16.436  1.00132.29           O  
ANISOU 5677  O   CYS B 328    23925  13560  12781   1919  -1958  -1056       O  
ATOM   5678  CB  CYS B 328     -18.244  23.375 -16.120  1.00130.74           C  
ANISOU 5678  CB  CYS B 328    23336  13420  12920   1433  -2219   -973       C  
ATOM   5679  SG  CYS B 328     -16.563  23.509 -15.460  1.00136.54           S  
ANISOU 5679  SG  CYS B 328    24122  14038  13719   1184  -2507   -973       S  
ATOM   5680  N   PHE B 329     -21.456  22.815 -15.875  1.00126.74           N  
ANISOU 5680  N   PHE B 329    22839  13160  12157   1997  -1754   -973       N  
ATOM   5681  CA  PHE B 329     -22.716  22.734 -16.607  1.00125.41           C  
ANISOU 5681  CA  PHE B 329    22561  13105  11983   2155  -1545   -952       C  
ATOM   5682  C   PHE B 329     -23.981  22.711 -15.726  1.00128.22           C  
ANISOU 5682  C   PHE B 329    23045  13535  12137   2437  -1408   -967       C  
ATOM   5683  O   PHE B 329     -25.065  22.982 -16.246  1.00127.33           O  
ANISOU 5683  O   PHE B 329    22905  13486  11987   2594  -1262   -961       O  
ATOM   5684  CB  PHE B 329     -22.676  21.552 -17.591  1.00125.49           C  
ANISOU 5684  CB  PHE B 329    22188  13285  12208   2040  -1422   -877       C  
ATOM   5685  CG  PHE B 329     -21.477  21.647 -18.514  1.00126.77           C  
ANISOU 5685  CG  PHE B 329    22226  13380  12559   1782  -1535   -864       C  
ATOM   5686  CD1 PHE B 329     -21.405  22.637 -19.491  1.00129.92           C  
ANISOU 5686  CD1 PHE B 329    22696  13678  12991   1719  -1567   -884       C  
ATOM   5687  CD2 PHE B 329     -20.391  20.794 -18.360  1.00128.72           C  
ANISOU 5687  CD2 PHE B 329    22302  13662  12945   1606  -1612   -829       C  
ATOM   5688  CE1 PHE B 329     -20.277  22.756 -20.309  1.00130.51           C  
ANISOU 5688  CE1 PHE B 329    22663  13694  13231   1474  -1664   -867       C  
ATOM   5689  CE2 PHE B 329     -19.266  20.912 -19.185  1.00131.25           C  
ANISOU 5689  CE2 PHE B 329    22501  13929  13437   1375  -1707   -814       C  
ATOM   5690  CZ  PHE B 329     -19.217  21.893 -20.151  1.00129.31           C  
ANISOU 5690  CZ  PHE B 329    22322  13590  13219   1306  -1728   -832       C  
ATOM   5691  N   ARG B 330     -23.848  22.482 -14.399  1.00124.75           N  
ANISOU 5691  N   ARG B 330    22761  13079  11558   2506  -1459   -985       N  
ATOM   5692  CA  ARG B 330     -24.991  22.505 -13.478  1.00124.30           C  
ANISOU 5692  CA  ARG B 330    22847  13089  11293   2774  -1325   -999       C  
ATOM   5693  C   ARG B 330     -25.485  23.933 -13.268  1.00127.03           C  
ANISOU 5693  C   ARG B 330    23535  13282  11450   2950  -1358  -1078       C  
ATOM   5694  O   ARG B 330     -24.684  24.848 -13.052  1.00127.11           O  
ANISOU 5694  O   ARG B 330    23799  13089  11407   2865  -1554  -1138       O  
ATOM   5695  CB  ARG B 330     -24.673  21.829 -12.137  1.00124.59           C  
ANISOU 5695  CB  ARG B 330    22963  13148  11226   2791  -1368   -993       C  
ATOM   5696  N   GLN B 331     -26.810  24.112 -13.392  1.00122.87           N  
ANISOU 5696  N   GLN B 331    23000  12854  10830   3191  -1168  -1073       N  
ATOM   5697  CA  GLN B 331     -27.539  25.373 -13.242  1.00124.09           C  
ANISOU 5697  CA  GLN B 331    23451  12897  10801   3417  -1151  -1140       C  
ATOM   5698  C   GLN B 331     -29.029  25.134 -13.003  1.00127.72           C  
ANISOU 5698  C   GLN B 331    23839  13537  11152   3704   -909  -1113       C  
ATOM   5699  O   GLN B 331     -29.636  24.310 -13.679  1.00127.04           O  
ANISOU 5699  O   GLN B 331    23424  13646  11197   3696   -754  -1037       O  
ATOM   5700  CB  GLN B 331     -27.316  26.317 -14.444  1.00125.30           C  
ANISOU 5700  CB  GLN B 331    23640  12920  11046   3333  -1232  -1163       C  
ATOM   5701  CG  GLN B 331     -27.391  25.673 -15.826  1.00140.81           C  
ANISOU 5701  CG  GLN B 331    25234  15019  13248   3190  -1148  -1089       C  
ATOM   5702  CD  GLN B 331     -26.549  26.442 -16.808  1.00159.82           C  
ANISOU 5702  CD  GLN B 331    27698  17261  15767   2992  -1302  -1110       C  
ATOM   5703  OE1 GLN B 331     -25.313  26.358 -16.811  1.00154.26           O  
ANISOU 5703  OE1 GLN B 331    26992  16464  15155   2749  -1463  -1113       O  
ATOM   5704  NE2 GLN B 331     -27.200  27.209 -17.669  1.00152.08           N  
ANISOU 5704  NE2 GLN B 331    26762  16244  14779   3088  -1256  -1118       N  
ATOM   5705  N   LEU B 332     -29.610  25.858 -12.046  1.00125.12           N  
ANISOU 5705  N   LEU B 332    23818  13142  10582   3953   -878  -1173       N  
ATOM   5706  CA  LEU B 332     -31.025  25.790 -11.675  1.00125.78           C  
ANISOU 5706  CA  LEU B 332    23873  13386  10531   4255   -648  -1154       C  
ATOM   5707  C   LEU B 332     -31.954  26.107 -12.860  1.00129.50           C  
ANISOU 5707  C   LEU B 332    24163  13946  11094   4359   -525  -1122       C  
ATOM   5708  O   LEU B 332     -31.668  27.033 -13.621  1.00129.51           O  
ANISOU 5708  O   LEU B 332    24283  13790  11134   4318   -636  -1164       O  
ATOM   5709  CB  LEU B 332     -31.274  26.826 -10.566  1.00128.38           C  
ANISOU 5709  CB  LEU B 332    24639  13561  10577   4497   -678  -1247       C  
ATOM   5710  CG  LEU B 332     -31.490  26.309  -9.175  1.00134.20           C  
ANISOU 5710  CG  LEU B 332    25491  14367  11132   4616   -604  -1248       C  
ATOM   5711  CD1 LEU B 332     -30.170  26.118  -8.455  1.00134.48           C  
ANISOU 5711  CD1 LEU B 332    25695  14252  11151   4396   -826  -1280       C  
ATOM   5712  CD2 LEU B 332     -32.342  27.269  -8.406  1.00140.23           C  
ANISOU 5712  CD2 LEU B 332    26587  15069  11625   4953   -516  -1318       C  
ATOM   5713  N   CYS B 333     -33.084  25.380 -12.984  1.00125.72           N  
ANISOU 5713  N   CYS B 333    23413  13716  10640   4497   -302  -1047       N  
ATOM   5714  CA  CYS B 333     -34.086  25.600 -14.040  1.00156.29           C  
ANISOU 5714  CA  CYS B 333    27089  17702  14592   4614   -177  -1006       C  
ATOM   5715  C   CYS B 333     -34.887  26.882 -13.740  1.00176.74           C  
ANISOU 5715  C   CYS B 333    29970  20202  16983   4935   -136  -1073       C  
ATOM   5716  O   CYS B 333     -35.110  27.716 -14.620  1.00139.02           O  
ANISOU 5716  O   CYS B 333    25242  15339  12242   4987   -177  -1094       O  
ATOM   5717  CB  CYS B 333     -35.012  24.391 -14.184  1.00155.68           C  
ANISOU 5717  CB  CYS B 333    26633  17920  14600   4644     33   -899       C  
ATOM   5718  SG  CYS B 333     -34.204  22.783 -13.954  1.00157.51           S  
ANISOU 5718  SG  CYS B 333    26609  18258  14979   4347     16   -828       S  
TER    5719      CYS B 333                                                      
HETATM 5720  C   DI7 C   1     -19.930  39.915 -33.275  1.00 82.04           C  
HETATM 5721  N   DI7 C   1     -18.958  38.886 -35.233  1.00 85.17           N  
HETATM 5722  O   DI7 C   1     -21.075  39.607 -33.496  1.00 80.16           O  
HETATM 5723  CA  DI7 C   1     -18.967  40.083 -34.443  1.00 81.71           C  
HETATM 5724  CB  DI7 C   1     -19.316  41.280 -35.362  1.00 76.79           C  
HETATM 5725  CD  DI7 C   1     -19.677  42.580 -34.686  1.00 73.60           C  
HETATM 5726  OH  DI7 C   1     -20.664  46.279 -32.909  1.00 75.30           O  
HETATM 5727  CZ  DI7 C   1     -20.342  45.049 -33.499  1.00 72.78           C  
HETATM 5728  CD1 DI7 C   1     -21.048  42.975 -34.510  1.00 74.41           C  
HETATM 5729  CD2 DI7 C   1     -18.660  43.472 -34.288  1.00 72.84           C  
HETATM 5730  CE1 DI7 C   1     -21.362  44.194 -33.909  1.00 71.98           C  
HETATM 5731  CE2 DI7 C   1     -19.003  44.694 -33.699  1.00 72.26           C  
HETATM 5732  CE3 DI7 C   1     -22.239  42.150 -34.950  1.00 73.63           C  
HETATM 5733  CE4 DI7 C   1     -17.184  43.193 -34.471  1.00 73.50           C  
HETATM 5734  N   DAR C   2     -19.482  40.130 -32.030  1.00 84.98           N  
HETATM 5735  CA  DAR C   2     -20.324  40.037 -30.813  1.00 86.08           C  
HETATM 5736  CB  DAR C   2     -21.207  41.278 -30.638  1.00 88.60           C  
HETATM 5737  CG  DAR C   2     -20.387  42.593 -30.609  1.00 91.10           C  
HETATM 5738  CD  DAR C   2     -20.499  43.086 -29.159  1.00 96.49           C  
HETATM 5739  NE  DAR C   2     -19.223  43.573 -28.616  1.00 98.77           N  
HETATM 5740  CZ  DAR C   2     -19.124  43.878 -27.318  1.00 99.07           C  
HETATM 5741  NH1 DAR C   2     -20.168  43.701 -26.507  1.00 97.92           N  
HETATM 5742  NH2 DAR C   2     -17.972  44.350 -26.829  1.00 99.73           N  
HETATM 5743  C   DAR C   2     -19.484  39.720 -29.575  1.00 82.21           C  
HETATM 5744  O   DAR C   2     -19.847  40.000 -28.469  1.00 80.25           O  
ATOM   5745  N   PHE C   3     -18.314  39.136 -29.783  1.00 82.42           N  
ATOM   5746  CA  PHE C   3     -17.378  38.723 -28.754  1.00 82.25           C  
ATOM   5747  C   PHE C   3     -16.688  39.871 -28.027  1.00 83.05           C  
ATOM   5748  O   PHE C   3     -15.970  40.590 -28.685  1.00 84.51           O  
ATOM   5749  CB  PHE C   3     -16.351  37.781 -29.382  1.00 81.74           C  
ATOM   5750  CG  PHE C   3     -15.346  37.250 -28.398  1.00 80.14           C  
ATOM   5751  CD1 PHE C   3     -14.077  37.840 -28.319  1.00 78.32           C  
ATOM   5752  CD2 PHE C   3     -15.676  36.165 -27.572  1.00 77.23           C  
ATOM   5753  CE1 PHE C   3     -13.140  37.344 -27.407  1.00 76.50           C  
ATOM   5754  CE2 PHE C   3     -14.728  35.675 -26.665  1.00 74.37           C  
ATOM   5755  CZ  PHE C   3     -13.464  36.256 -26.594  1.00 74.34           C  
HETATM 5756  N   SAR C   4     -16.817  39.984 -26.678  1.00 81.49           N  
HETATM 5757  CA  SAR C   4     -17.711  39.060 -25.941  1.00 81.66           C  
HETATM 5758  C   SAR C   4     -18.956  39.705 -25.304  1.00 82.94           C  
HETATM 5759  O   SAR C   4     -19.149  40.893 -25.433  1.00 85.54           O  
HETATM 5760  CN  SAR C   4     -16.069  41.001 -25.929  1.00 78.46           C  
HETATM 5761  CBQ OXJ C   5     -19.702  37.559 -24.381  1.00 82.14           C  
HETATM 5762  CBR OXJ C   5     -20.947  39.665 -23.883  1.00 80.20           C  
HETATM 5763  CBS OXJ C   5     -22.298  39.700 -24.506  1.00 82.76           C  
HETATM 5764  CBT OXJ C   5     -23.367  39.219 -23.745  1.00 85.63           C  
HETATM 5765  CBU OXJ C   5     -24.684  39.289 -24.246  1.00 89.78           C  
HETATM 5766  CBV OXJ C   5     -24.905  39.906 -25.476  1.00 87.04           C  
HETATM 5767  CBW OXJ C   5     -23.840  40.422 -26.231  1.00 86.09           C  
HETATM 5768  CBX OXJ C   5     -22.523  40.344 -25.720  1.00 83.64           C  
HETATM 5769  CBY OXJ C   5     -24.101  41.062 -27.564  1.00 88.15           C  
HETATM 5770  CBZ OXJ C   5     -25.830  38.726 -23.453  1.00 97.29           C  
HETATM 5771  FCA OXJ C   5     -23.493  42.293 -27.601  1.00 89.78           F  
HETATM 5772  FCB OXJ C   5     -23.584  40.285 -28.570  1.00 87.41           F  
HETATM 5773  FCC OXJ C   5     -25.452  41.211 -27.775  1.00 88.56           F  
HETATM 5774  FCD OXJ C   5     -26.179  37.451 -23.835  1.00 98.63           F  
HETATM 5775  FCE OXJ C   5     -26.929  39.530 -23.620  1.00 99.70           F  
HETATM 5776  FCF OXJ C   5     -25.454  38.681 -22.130  1.00 98.61           F  
HETATM 5777  NBO OXJ C   5     -19.860  38.992 -24.603  1.00 81.57           N  
TER    5778      OXJ C   5                                                      
HETATM 5779  C   DI7 D   1     -20.413   3.397 -43.297  1.00 82.06           C  
HETATM 5780  N   DI7 D   1     -19.403   4.166 -41.228  1.00 79.08           N  
HETATM 5781  O   DI7 D   1     -21.489   3.891 -43.108  1.00 84.65           O  
HETATM 5782  CA  DI7 D   1     -19.501   3.056 -42.119  1.00 79.17           C  
HETATM 5783  CB  DI7 D   1     -20.005   1.844 -41.303  1.00 78.18           C  
HETATM 5784  CD  DI7 D   1     -20.325   0.592 -42.086  1.00 79.81           C  
HETATM 5785  OH  DI7 D   1     -21.290  -2.911 -44.202  1.00 84.56           O  
HETATM 5786  CZ  DI7 D   1     -20.962  -1.749 -43.504  1.00 79.38           C  
HETATM 5787  CD1 DI7 D   1     -21.680   0.239 -42.365  1.00 78.35           C  
HETATM 5788  CD2 DI7 D   1     -19.301  -0.297 -42.505  1.00 80.28           C  
HETATM 5789  CE1 DI7 D   1     -21.980  -0.921 -43.058  1.00 77.24           C  
HETATM 5790  CE2 DI7 D   1     -19.631  -1.447 -43.222  1.00 78.51           C  
HETATM 5791  CE3 DI7 D   1     -22.864   1.073 -41.970  1.00 76.45           C  
HETATM 5792  CE4 DI7 D   1     -17.835  -0.076 -42.221  1.00 80.76           C  
HETATM 5793  N   DAR D   2     -20.017   3.140 -44.541  1.00 82.94           N  
HETATM 5794  CA  DAR D   2     -20.874   3.390 -45.714  1.00 84.96           C  
HETATM 5795  CB  DAR D   2     -21.537   2.072 -46.089  1.00 90.43           C  
HETATM 5796  CG  DAR D   2     -20.491   0.925 -46.075  1.00 94.09           C  
HETATM 5797  CD  DAR D   2     -20.925  -0.129 -47.097  1.00 97.28           C  
HETATM 5798  NE  DAR D   2     -19.814  -0.463 -48.001  1.00 97.51           N  
HETATM 5799  CZ  DAR D   2     -19.951  -0.395 -49.324  1.00 97.18           C  
HETATM 5800  NH1 DAR D   2     -21.082   0.032 -49.888  1.00 94.71           N  
HETATM 5801  NH2 DAR D   2     -18.921  -0.743 -50.093  1.00 99.55           N  
HETATM 5802  C   DAR D   2     -20.072   3.934 -46.894  1.00 81.04           C  
HETATM 5803  O   DAR D   2     -20.504   3.900 -48.017  1.00 78.16           O  
ATOM   5804  N   PHE D   3     -18.864   4.419 -46.643  1.00 81.42           N  
ATOM   5805  CA  PHE D   3     -17.993   4.953 -47.670  1.00 81.33           C  
ATOM   5806  C   PHE D   3     -17.266   3.811 -48.373  1.00 84.22           C  
ATOM   5807  O   PHE D   3     -16.604   3.088 -47.666  1.00 86.80           O  
ATOM   5808  CB  PHE D   3     -17.011   5.922 -47.028  1.00 79.89           C  
ATOM   5809  CG  PHE D   3     -15.960   6.390 -47.994  1.00 81.35           C  
ATOM   5810  CD1 PHE D   3     -14.669   5.839 -47.921  1.00 83.60           C  
ATOM   5811  CD2 PHE D   3     -16.268   7.377 -48.945  1.00 78.73           C  
ATOM   5812  CE1 PHE D   3     -13.686   6.267 -48.823  1.00 83.14           C  
ATOM   5813  CE2 PHE D   3     -15.278   7.812 -49.827  1.00 78.36           C  
ATOM   5814  CZ  PHE D   3     -13.998   7.257 -49.760  1.00 80.83           C  
HETATM 5815  N   SAR D   4     -17.316   3.661 -49.724  1.00 83.19           N  
HETATM 5816  CA  SAR D   4     -18.106   4.596 -50.550  1.00 83.93           C  
HETATM 5817  C   SAR D   4     -19.316   3.978 -51.245  1.00 86.61           C  
HETATM 5818  O   SAR D   4     -19.434   2.791 -51.200  1.00 91.12           O  
HETATM 5819  CN  SAR D   4     -16.533   2.610 -50.384  1.00 81.45           C  
HETATM 5820  CBQ OXJ D   5     -20.204   6.131 -52.038  1.00 86.90           C  
HETATM 5821  CBR OXJ D   5     -21.285   3.957 -52.657  1.00 89.19           C  
HETATM 5822  CBS OXJ D   5     -22.655   3.958 -52.079  1.00 94.81           C  
HETATM 5823  CBT OXJ D   5     -23.687   4.513 -52.842  1.00 98.03           C  
HETATM 5824  CBU OXJ D   5     -25.010   4.472 -52.361  1.00103.88           C  
HETATM 5825  CBV OXJ D   5     -25.272   3.872 -51.125  1.00101.67           C  
HETATM 5826  CBW OXJ D   5     -24.244   3.310 -50.361  1.00100.19           C  
HETATM 5827  CBX OXJ D   5     -22.919   3.333 -50.860  1.00 97.69           C  
HETATM 5828  CBY OXJ D   5     -24.553   2.647 -49.057  1.00102.05           C  
HETATM 5829  CBZ OXJ D   5     -26.112   5.076 -53.172  1.00113.17           C  
HETATM 5830  FCA OXJ D   5     -24.029   1.386 -49.074  1.00105.16           F  
HETATM 5831  FCB OXJ D   5     -23.999   3.338 -48.012  1.00101.22           F  
HETATM 5832  FCC OXJ D   5     -25.906   2.542 -48.882  1.00102.02           F  
HETATM 5833  FCD OXJ D   5     -26.052   6.438 -53.087  1.00115.40           F  
HETATM 5834  FCE OXJ D   5     -27.346   4.655 -52.727  1.00116.46           F  
HETATM 5835  FCF OXJ D   5     -25.952   4.691 -54.486  1.00115.44           F  
HETATM 5836  NBO OXJ D   5     -20.252   4.678 -51.907  1.00 87.10           N  
TER    5837      OXJ D   5                                                      
HETATM 5838  C1  CLR A1201     -33.810  36.984 -25.553  1.00138.11           C  
HETATM 5839  C2  CLR A1201     -34.084  37.143 -24.051  1.00138.32           C  
HETATM 5840  C3  CLR A1201     -33.409  38.383 -23.502  1.00137.52           C  
HETATM 5841  C4  CLR A1201     -33.869  39.615 -24.267  1.00137.19           C  
HETATM 5842  C5  CLR A1201     -33.665  39.470 -25.763  1.00136.32           C  
HETATM 5843  C6  CLR A1201     -33.022  40.412 -26.449  1.00134.85           C  
HETATM 5844  C7  CLR A1201     -32.768  40.383 -27.926  1.00134.24           C  
HETATM 5845  C8  CLR A1201     -33.652  39.361 -28.637  1.00134.55           C  
HETATM 5846  C9  CLR A1201     -33.639  38.030 -27.849  1.00135.41           C  
HETATM 5847  C10 CLR A1201     -34.228  38.200 -26.410  1.00137.46           C  
HETATM 5848  C11 CLR A1201     -34.296  36.865 -28.630  1.00133.96           C  
HETATM 5849  C12 CLR A1201     -34.000  36.795 -30.137  1.00133.32           C  
HETATM 5850  C13 CLR A1201     -34.130  38.148 -30.868  1.00133.28           C  
HETATM 5851  C14 CLR A1201     -33.210  39.122 -30.092  1.00133.83           C  
HETATM 5852  C15 CLR A1201     -33.043  40.316 -31.045  1.00133.37           C  
HETATM 5853  C16 CLR A1201     -33.109  39.712 -32.456  1.00132.54           C  
HETATM 5854  C17 CLR A1201     -33.488  38.223 -32.279  1.00131.93           C  
HETATM 5855  C18 CLR A1201     -35.609  38.607 -30.895  1.00133.97           C  
HETATM 5856  C19 CLR A1201     -35.771  38.313 -26.434  1.00139.67           C  
HETATM 5857  C20 CLR A1201     -34.256  37.648 -33.490  1.00130.34           C  
HETATM 5858  C21 CLR A1201     -33.828  36.222 -33.832  1.00130.90           C  
HETATM 5859  C22 CLR A1201     -34.167  38.561 -34.734  1.00127.93           C  
HETATM 5860  C23 CLR A1201     -35.263  38.407 -35.787  1.00125.65           C  
HETATM 5861  C24 CLR A1201     -34.725  37.874 -37.111  1.00124.68           C  
HETATM 5862  C25 CLR A1201     -35.292  38.451 -38.401  1.00123.54           C  
HETATM 5863  C26 CLR A1201     -34.265  39.264 -39.171  1.00121.97           C  
HETATM 5864  C27 CLR A1201     -35.876  37.363 -39.284  1.00122.96           C  
HETATM 5865  O1  CLR A1201     -33.699  38.517 -22.105  1.00136.83           O  
HETATM 5866  C1  OLA A1202     -13.365  24.278 -18.144  1.00121.52           C  
HETATM 5867  O1  OLA A1202     -13.488  25.309 -17.441  1.00121.92           O  
HETATM 5868  O2  OLA A1202     -12.208  23.823 -18.315  1.00121.46           O  
HETATM 5869  C2  OLA A1202     -14.595  23.632 -18.762  1.00120.69           C  
HETATM 5870  C3  OLA A1202     -14.339  22.238 -19.346  1.00118.94           C  
HETATM 5871  C4  OLA A1202     -14.201  22.245 -20.867  1.00117.58           C  
HETATM 5872  C5  OLA A1202     -12.733  22.214 -21.303  1.00116.65           C  
HETATM 5873  C6  OLA A1202     -12.598  21.782 -22.760  1.00114.60           C  
HETATM 5874  C7  OLA A1202     -11.655  22.660 -23.575  1.00111.57           C  
HETATM 5875  C8  OLA A1202     -12.228  22.905 -24.972  1.00109.40           C  
HETATM 5876  C9  OLA A1202     -11.349  23.902 -25.694  1.00107.26           C  
HETATM 5877  C10 OLA A1202     -11.417  24.258 -26.987  1.00105.77           C  
HETATM 5878  C11 OLA A1202     -12.389  23.785 -28.053  1.00103.38           C  
HETATM 5879  C12 OLA A1202     -11.865  24.238 -29.419  1.00101.41           C  
HETATM 5880  C13 OLA A1202     -12.979  24.577 -30.406  1.00100.78           C  
HETATM 5881  C14 OLA A1202     -13.118  23.548 -31.525  1.00100.45           C  
HETATM 5882  C15 OLA A1202     -13.433  24.195 -32.880  1.00 99.45           C  
HETATM 5883  C16 OLA A1202     -13.003  23.293 -34.044  1.00 97.53           C  
HETATM 5884  C17 OLA A1202     -12.393  24.052 -35.224  1.00 95.36           C  
HETATM 5885  C18 OLA A1202     -12.855  23.497 -36.574  1.00 92.48           C  
HETATM 5886  C1  OLA A1203      -2.149  41.473 -58.201  1.00139.06           C  
HETATM 5887  O1  OLA A1203      -2.123  41.590 -59.451  1.00139.68           O  
HETATM 5888  O2  OLA A1203      -1.173  41.881 -57.526  1.00139.26           O  
HETATM 5889  C2  OLA A1203      -3.340  40.840 -57.517  1.00136.95           C  
HETATM 5890  C3  OLA A1203      -4.450  41.869 -57.335  1.00134.51           C  
HETATM 5891  C4  OLA A1203      -4.503  42.383 -55.898  1.00131.25           C  
HETATM 5892  C5  OLA A1203      -5.890  42.903 -55.530  1.00127.54           C  
HETATM 5893  C6  OLA A1203      -6.674  41.864 -54.731  1.00124.35           C  
HETATM 5894  C7  OLA A1203      -7.216  42.443 -53.429  1.00121.76           C  
HETATM 5895  C8  OLA A1203      -6.249  42.204 -52.272  1.00118.58           C  
HETATM 5896  C9  OLA A1203      -6.874  42.723 -51.002  1.00115.01           C  
HETATM 5897  C10 OLA A1203      -6.201  43.139 -49.929  1.00112.88           C  
HETATM 5898  C11 OLA A1203      -4.704  43.181 -49.736  1.00112.22           C  
HETATM 5899  C12 OLA A1203      -4.441  43.643 -48.306  1.00113.67           C  
HETATM 5900  C13 OLA A1203      -4.366  42.474 -47.322  1.00116.07           C  
HETATM 5901  C14 OLA A1203      -4.089  42.941 -45.893  1.00116.80           C  
HETATM 5902  C15 OLA A1203      -3.989  41.765 -44.923  1.00117.53           C  
HETATM 5903  C16 OLA A1203      -4.271  42.215 -43.491  1.00119.28           C  
HETATM 5904  C17 OLA A1203      -4.438  41.031 -42.536  1.00119.87           C  
HETATM 5905  C18 OLA A1203      -4.223  41.432 -41.079  1.00119.38           C  
HETATM 5906  C6  OLA B1201     -26.406  10.890 -12.097  1.00122.91           C  
HETATM 5907  C7  OLA B1201     -27.018  10.316 -13.373  1.00122.98           C  
HETATM 5908  C8  OLA B1201     -26.329  10.846 -14.632  1.00123.03           C  
HETATM 5909  C9  OLA B1201     -27.154  11.971 -15.236  1.00122.80           C  
HETATM 5910  C10 OLA B1201     -27.090  12.423 -16.502  1.00121.79           C  
HETATM 5911  C11 OLA B1201     -26.177  11.909 -17.604  1.00119.69           C  
HETATM 5912  C12 OLA B1201     -26.925  10.961 -18.538  1.00117.41           C  
HETATM 5913  C13 OLA B1201     -27.702  11.717 -19.607  1.00115.87           C  
HETATM 5914  C14 OLA B1201     -27.883  10.871 -20.861  1.00115.51           C  
HETATM 5915  C15 OLA B1201     -28.431  11.705 -22.019  1.00114.53           C  
HETATM 5916  C16 OLA B1201     -27.462  11.759 -23.201  1.00112.49           C  
HETATM 5917  C17 OLA B1201     -28.160  12.211 -24.478  1.00110.90           C  
HETATM 5918  C18 OLA B1201     -27.935  13.694 -24.760  1.00110.49           C  
HETATM 5919  C10 OLA B1202     -28.493  15.257 -32.734  1.00110.26           C  
HETATM 5920  C11 OLA B1202     -28.858  13.905 -33.297  1.00111.49           C  
HETATM 5921  C12 OLA B1202     -28.901  12.893 -32.154  1.00112.73           C  
HETATM 5922  C13 OLA B1202     -29.743  11.672 -32.525  1.00112.26           C  
HETATM 5923  C14 OLA B1202     -29.740  10.630 -31.410  1.00110.85           C  
HETATM 5924  C15 OLA B1202     -31.105  10.553 -30.738  1.00109.93           C  
HETATM 5925  C16 OLA B1202     -31.269   9.277 -29.921  1.00109.03           C  
HETATM 5926  C17 OLA B1202     -31.199   9.575 -28.427  1.00108.62           C  
HETATM 5927  C18 OLA B1202     -32.165   8.690 -27.651  1.00108.48           C  
HETATM 5928  C10 OLA B1203      -5.389   0.036 -19.984  1.00106.63           C  
HETATM 5929  C11 OLA B1203      -5.590   0.749 -21.303  1.00107.32           C  
HETATM 5930  C12 OLA B1203      -6.959   0.425 -21.903  1.00106.61           C  
HETATM 5931  C13 OLA B1203      -6.850  -0.485 -23.124  1.00105.76           C  
HETATM 5932  C14 OLA B1203      -7.209   0.264 -24.404  1.00105.52           C  
HETATM 5933  C15 OLA B1203      -7.026  -0.611 -25.636  1.00105.06           C  
HETATM 5934  C16 OLA B1203      -5.890  -0.083 -26.502  1.00105.20           C  
HETATM 5935  C17 OLA B1203      -5.244  -1.218 -27.293  1.00105.42           C  
HETATM 5936  C18 OLA B1203      -4.835  -0.763 -28.692  1.00104.40           C  
HETATM 5937  C10 OLA B1204     -34.712  -7.391 -58.606  1.00101.59           C  
HETATM 5938  C11 OLA B1204     -33.783  -7.333 -57.412  1.00102.87           C  
HETATM 5939  C12 OLA B1204     -32.354  -7.073 -57.889  1.00104.05           C  
HETATM 5940  C13 OLA B1204     -31.307  -7.508 -56.859  1.00103.55           C  
HETATM 5941  C14 OLA B1204     -29.898  -7.470 -57.454  1.00101.81           C  
HETATM 5942  C15 OLA B1204     -28.965  -8.477 -56.791  1.00 99.09           C  
HETATM 5943  C16 OLA B1204     -27.663  -7.823 -56.346  1.00 97.63           C  
HETATM 5944  C17 OLA B1204     -26.502  -8.294 -57.219  1.00 98.02           C  
HETATM 5945  C18 OLA B1204     -25.155  -8.066 -56.536  1.00 97.58           C  
HETATM 5946  C1  OLA B1205      -1.807  -5.092 -49.960  1.00129.27           C  
HETATM 5947  O1  OLA B1205      -1.788  -5.126 -51.213  1.00129.37           O  
HETATM 5948  O2  OLA B1205      -2.834  -4.663 -49.394  1.00130.37           O  
HETATM 5949  C2  OLA B1205      -0.622  -5.574 -49.147  1.00126.94           C  
HETATM 5950  C3  OLA B1205      -0.233  -4.558 -48.075  1.00124.83           C  
HETATM 5951  C4  OLA B1205      -0.861  -4.911 -46.731  1.00123.45           C  
HETATM 5952  C5  OLA B1205       0.204  -5.053 -45.650  1.00122.74           C  
HETATM 5953  C6  OLA B1205      -0.264  -5.999 -44.551  1.00122.49           C  
HETATM 5954  C7  OLA B1205       0.339  -5.632 -43.199  1.00122.51           C  
HETATM 5955  C10 OLC B1206     -35.812   5.204 -38.206  1.00127.92           C  
HETATM 5956  C9  OLC B1206     -35.839   5.562 -39.498  1.00127.23           C  
HETATM 5957  C11 OLC B1206     -34.878   4.166 -37.616  1.00128.09           C  
HETATM 5958  C8  OLC B1206     -34.936   4.989 -40.573  1.00126.39           C  
HETATM 5959  C24 OLC B1206     -35.188   5.314 -52.965  1.00124.61           C  
HETATM 5960  C12 OLC B1206     -35.662   3.207 -36.727  1.00127.71           C  
HETATM 5961  C7  OLC B1206     -35.644   5.004 -41.926  1.00125.45           C  
HETATM 5962  C6  OLC B1206     -34.837   5.747 -42.987  1.00124.43           C  
HETATM 5963  C5  OLC B1206     -33.968   4.787 -43.794  1.00123.35           C  
HETATM 5964  C4  OLC B1206     -33.493   5.450 -45.075  1.00122.20           C  
HETATM 5965  C3  OLC B1206     -33.589   4.461 -46.223  1.00121.71           C  
HETATM 5966  C2  OLC B1206     -34.773   4.813 -47.109  1.00121.90           C  
HETATM 5967  C21 OLC B1206     -34.892   4.584 -50.597  1.00123.75           C  
HETATM 5968  C1  OLC B1206     -34.275   5.430 -48.397  1.00121.96           C  
HETATM 5969  C22 OLC B1206     -34.253   5.334 -51.760  1.00124.35           C  
HETATM 5970  O19 OLC B1206     -34.104   6.641 -48.492  1.00119.92           O  
HETATM 5971  O25 OLC B1206     -34.443   5.618 -54.150  1.00124.24           O  
HETATM 5972  O23 OLC B1206     -33.998   6.688 -51.370  1.00124.25           O  
HETATM 5973  O20 OLC B1206     -34.010   4.615 -49.472  1.00122.87           O  
HETATM 5974  O   HOH A1301     -18.887  46.806 -30.523  1.00 82.84           O  
HETATM 5975  O   HOH A1302     -15.910  43.651 -28.955  1.00 74.32           O  
HETATM 5976  O   HOH C 101     -23.274  47.045 -33.212  1.00 76.07           O  
CONECT 1418 2007                                                                
CONECT 2007 1418                                                                
CONECT 4104 4689                                                                
CONECT 4689 4104                                                                
CONECT 5720 5722 5723 5734                                                      
CONECT 5721 5723                                                                
CONECT 5722 5720                                                                
CONECT 5723 5720 5721 5724                                                      
CONECT 5724 5723 5725                                                           
CONECT 5725 5724 5728 5729                                                      
CONECT 5726 5727                                                                
CONECT 5727 5726 5730 5731                                                      
CONECT 5728 5725 5730 5732                                                      
CONECT 5729 5725 5731 5733                                                      
CONECT 5730 5727 5728                                                           
CONECT 5731 5727 5729                                                           
CONECT 5732 5728                                                                
CONECT 5733 5729                                                                
CONECT 5734 5720 5735                                                           
CONECT 5735 5734 5736 5743                                                      
CONECT 5736 5735 5737                                                           
CONECT 5737 5736 5738                                                           
CONECT 5738 5737 5739                                                           
CONECT 5739 5738 5740                                                           
CONECT 5740 5739 5741 5742                                                      
CONECT 5741 5740                                                                
CONECT 5742 5740                                                                
CONECT 5743 5735 5744 5745                                                      
CONECT 5744 5743                                                                
CONECT 5745 5743                                                                
CONECT 5747 5756                                                                
CONECT 5756 5747 5757 5760                                                      
CONECT 5757 5756 5758                                                           
CONECT 5758 5757 5759 5777                                                      
CONECT 5759 5758                                                                
CONECT 5760 5756                                                                
CONECT 5761 5777                                                                
CONECT 5762 5763 5777                                                           
CONECT 5763 5762 5764 5768                                                      
CONECT 5764 5763 5765                                                           
CONECT 5765 5764 5766 5770                                                      
CONECT 5766 5765 5767                                                           
CONECT 5767 5766 5768 5769                                                      
CONECT 5768 5763 5767                                                           
CONECT 5769 5767 5771 5772 5773                                                 
CONECT 5770 5765 5774 5775 5776                                                 
CONECT 5771 5769                                                                
CONECT 5772 5769                                                                
CONECT 5773 5769                                                                
CONECT 5774 5770                                                                
CONECT 5775 5770                                                                
CONECT 5776 5770                                                                
CONECT 5777 5758 5761 5762                                                      
CONECT 5779 5781 5782 5793                                                      
CONECT 5780 5782                                                                
CONECT 5781 5779                                                                
CONECT 5782 5779 5780 5783                                                      
CONECT 5783 5782 5784                                                           
CONECT 5784 5783 5787 5788                                                      
CONECT 5785 5786                                                                
CONECT 5786 5785 5789 5790                                                      
CONECT 5787 5784 5789 5791                                                      
CONECT 5788 5784 5790 5792                                                      
CONECT 5789 5786 5787                                                           
CONECT 5790 5786 5788                                                           
CONECT 5791 5787                                                                
CONECT 5792 5788                                                                
CONECT 5793 5779 5794                                                           
CONECT 5794 5793 5795 5802                                                      
CONECT 5795 5794 5796                                                           
CONECT 5796 5795 5797                                                           
CONECT 5797 5796 5798                                                           
CONECT 5798 5797 5799                                                           
CONECT 5799 5798 5800 5801                                                      
CONECT 5800 5799                                                                
CONECT 5801 5799                                                                
CONECT 5802 5794 5803 5804                                                      
CONECT 5803 5802                                                                
CONECT 5804 5802                                                                
CONECT 5806 5815                                                                
CONECT 5815 5806 5816 5819                                                      
CONECT 5816 5815 5817                                                           
CONECT 5817 5816 5818 5836                                                      
CONECT 5818 5817                                                                
CONECT 5819 5815                                                                
CONECT 5820 5836                                                                
CONECT 5821 5822 5836                                                           
CONECT 5822 5821 5823 5827                                                      
CONECT 5823 5822 5824                                                           
CONECT 5824 5823 5825 5829                                                      
CONECT 5825 5824 5826                                                           
CONECT 5826 5825 5827 5828                                                      
CONECT 5827 5822 5826                                                           
CONECT 5828 5826 5830 5831 5832                                                 
CONECT 5829 5824 5833 5834 5835                                                 
CONECT 5830 5828                                                                
CONECT 5831 5828                                                                
CONECT 5832 5828                                                                
CONECT 5833 5829                                                                
CONECT 5834 5829                                                                
CONECT 5835 5829                                                                
CONECT 5836 5817 5820 5821                                                      
CONECT 5838 5839 5847                                                           
CONECT 5839 5838 5840                                                           
CONECT 5840 5839 5841 5865                                                      
CONECT 5841 5840 5842                                                           
CONECT 5842 5841 5843 5847                                                      
CONECT 5843 5842 5844                                                           
CONECT 5844 5843 5845                                                           
CONECT 5845 5844 5846 5851                                                      
CONECT 5846 5845 5847 5848                                                      
CONECT 5847 5838 5842 5846 5856                                                 
CONECT 5848 5846 5849                                                           
CONECT 5849 5848 5850                                                           
CONECT 5850 5849 5851 5854 5855                                                 
CONECT 5851 5845 5850 5852                                                      
CONECT 5852 5851 5853                                                           
CONECT 5853 5852 5854                                                           
CONECT 5854 5850 5853 5857                                                      
CONECT 5855 5850                                                                
CONECT 5856 5847                                                                
CONECT 5857 5854 5858 5859                                                      
CONECT 5858 5857                                                                
CONECT 5859 5857 5860                                                           
CONECT 5860 5859 5861                                                           
CONECT 5861 5860 5862                                                           
CONECT 5862 5861 5863 5864                                                      
CONECT 5863 5862                                                                
CONECT 5864 5862                                                                
CONECT 5865 5840                                                                
CONECT 5866 5867 5868 5869                                                      
CONECT 5867 5866                                                                
CONECT 5868 5866                                                                
CONECT 5869 5866 5870                                                           
CONECT 5870 5869 5871                                                           
CONECT 5871 5870 5872                                                           
CONECT 5872 5871 5873                                                           
CONECT 5873 5872 5874                                                           
CONECT 5874 5873 5875                                                           
CONECT 5875 5874 5876                                                           
CONECT 5876 5875 5877                                                           
CONECT 5877 5876 5878                                                           
CONECT 5878 5877 5879                                                           
CONECT 5879 5878 5880                                                           
CONECT 5880 5879 5881                                                           
CONECT 5881 5880 5882                                                           
CONECT 5882 5881 5883                                                           
CONECT 5883 5882 5884                                                           
CONECT 5884 5883 5885                                                           
CONECT 5885 5884                                                                
CONECT 5886 5887 5888 5889                                                      
CONECT 5887 5886                                                                
CONECT 5888 5886                                                                
CONECT 5889 5886 5890                                                           
CONECT 5890 5889 5891                                                           
CONECT 5891 5890 5892                                                           
CONECT 5892 5891 5893                                                           
CONECT 5893 5892 5894                                                           
CONECT 5894 5893 5895                                                           
CONECT 5895 5894 5896                                                           
CONECT 5896 5895 5897                                                           
CONECT 5897 5896 5898                                                           
CONECT 5898 5897 5899                                                           
CONECT 5899 5898 5900                                                           
CONECT 5900 5899 5901                                                           
CONECT 5901 5900 5902                                                           
CONECT 5902 5901 5903                                                           
CONECT 5903 5902 5904                                                           
CONECT 5904 5903 5905                                                           
CONECT 5905 5904                                                                
CONECT 5906 5907                                                                
CONECT 5907 5906 5908                                                           
CONECT 5908 5907 5909                                                           
CONECT 5909 5908 5910                                                           
CONECT 5910 5909 5911                                                           
CONECT 5911 5910 5912                                                           
CONECT 5912 5911 5913                                                           
CONECT 5913 5912 5914                                                           
CONECT 5914 5913 5915                                                           
CONECT 5915 5914 5916                                                           
CONECT 5916 5915 5917                                                           
CONECT 5917 5916 5918                                                           
CONECT 5918 5917                                                                
CONECT 5919 5920                                                                
CONECT 5920 5919 5921                                                           
CONECT 5921 5920 5922                                                           
CONECT 5922 5921 5923                                                           
CONECT 5923 5922 5924                                                           
CONECT 5924 5923 5925                                                           
CONECT 5925 5924 5926                                                           
CONECT 5926 5925 5927                                                           
CONECT 5927 5926                                                                
CONECT 5928 5929                                                                
CONECT 5929 5928 5930                                                           
CONECT 5930 5929 5931                                                           
CONECT 5931 5930 5932                                                           
CONECT 5932 5931 5933                                                           
CONECT 5933 5932 5934                                                           
CONECT 5934 5933 5935                                                           
CONECT 5935 5934 5936                                                           
CONECT 5936 5935                                                                
CONECT 5937 5938                                                                
CONECT 5938 5937 5939                                                           
CONECT 5939 5938 5940                                                           
CONECT 5940 5939 5941                                                           
CONECT 5941 5940 5942                                                           
CONECT 5942 5941 5943                                                           
CONECT 5943 5942 5944                                                           
CONECT 5944 5943 5945                                                           
CONECT 5945 5944                                                                
CONECT 5946 5947 5948 5949                                                      
CONECT 5947 5946                                                                
CONECT 5948 5946                                                                
CONECT 5949 5946 5950                                                           
CONECT 5950 5949 5951                                                           
CONECT 5951 5950 5952                                                           
CONECT 5952 5951 5953                                                           
CONECT 5953 5952 5954                                                           
CONECT 5954 5953                                                                
CONECT 5955 5956 5957                                                           
CONECT 5956 5955 5958                                                           
CONECT 5957 5955 5960                                                           
CONECT 5958 5956 5961                                                           
CONECT 5959 5969 5971                                                           
CONECT 5960 5957                                                                
CONECT 5961 5958 5962                                                           
CONECT 5962 5961 5963                                                           
CONECT 5963 5962 5964                                                           
CONECT 5964 5963 5965                                                           
CONECT 5965 5964 5966                                                           
CONECT 5966 5965 5968                                                           
CONECT 5967 5969 5973                                                           
CONECT 5968 5966 5970 5973                                                      
CONECT 5969 5959 5967 5972                                                      
CONECT 5970 5968                                                                
CONECT 5971 5959                                                                
CONECT 5972 5969                                                                
CONECT 5973 5967 5968                                                           
MASTER      549    0   17   36    6    0    9    6 5972    4  238   72          
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: October 18th, 2018.