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***  LSD_bound  ***

elNémo ID: 20020616593360594

Job options:

ID        	=	 20020616593360594
JOBID     	=	 LSD_bound
USERID    	=	 Connor
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 LSD_bound

HEADER    MEMBRANE PROTEIN                        09-NOV-16   5TVN              
TITLE     CRYSTAL STRUCTURE OF THE LSD-BOUND 5-HT2B RECEPTOR                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHIMERA PROTEIN OF HUMAN 5-HYDROXYTRYPTAMINE RECEPTOR 2B   
COMPND   3 AND E. COLI SOLUBLE CYTOCHROME B562;                                 
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: 5-HT2B,SEROTONIN RECEPTOR 2B,CYTOCHROME B-562,5-HT2B,       
COMPND   6 SEROTONIN RECEPTOR 2B;                                               
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI;                 
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606, 562;                                           
SOURCE   5 GENE: HTR2B, CYBC;                                                   
SOURCE   6 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM;       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 274590;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    LSD, GPCR, SEROTONIN RECEPTOR, MEMBRANE PROTEIN                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.WACKER,S.WANG,J.D.MCCORVY,R.M.BETZ,A.J.VENKATAKRISHNAN,A.LEVIT,     
AUTHOR   2 K.LANSU,Z.L.SCHOOLS,T.CHE,D.E.NICHOLS,B.K.SHOICHET,R.O.DROR,B.L.ROTH 
REVDAT   5   27-NOV-19 5TVN    1       REMARK                                   
REVDAT   4   27-SEP-17 5TVN    1       REMARK                                   
REVDAT   3   22-FEB-17 5TVN    1       REMARK                                   
REVDAT   2   08-FEB-17 5TVN    1       JRNL                                     
REVDAT   1   01-FEB-17 5TVN    0                                                
JRNL        AUTH   D.WACKER,S.WANG,J.D.MCCORVY,R.M.BETZ,A.J.VENKATAKRISHNAN,    
JRNL        AUTH 2 A.LEVIT,K.LANSU,Z.L.SCHOOLS,T.CHE,D.E.NICHOLS,B.K.SHOICHET,  
JRNL        AUTH 3 R.O.DROR,B.L.ROTH                                            
JRNL        TITL   CRYSTAL STRUCTURE OF AN LSD-BOUND HUMAN SEROTONIN RECEPTOR.  
JRNL        REF    CELL                          V. 168   377 2017              
JRNL        REFN                   ISSN 1097-4172                               
JRNL        PMID   28129538                                                     
JRNL        DOI    10.1016/J.CELL.2016.12.033                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.16                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 12393                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.150                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 638                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.1653 -  4.9527    0.86     2336   139  0.1939 0.2747        
REMARK   3     2  4.9527 -  3.9342    0.91     2373   121  0.1901 0.2058        
REMARK   3     3  3.9342 -  3.4378    0.92     2411   124  0.2159 0.2795        
REMARK   3     4  3.4378 -  3.1238    0.92     2356   130  0.2564 0.2903        
REMARK   3     5  3.1238 -  2.9002    0.89     2279   124  0.2573 0.3150        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.040           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 63.91                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 62.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           3092                                  
REMARK   3   ANGLE     :  0.848           4231                                  
REMARK   3   CHIRALITY :  0.029            524                                  
REMARK   3   PLANARITY :  0.004            512                                  
REMARK   3   DIHEDRAL  : 11.645           1081                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 41 THROUGH 248 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -21.9482 -15.7463  -0.4471              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4615 T22:   0.3347                                     
REMARK   3      T33:   0.2148 T12:   0.0375                                     
REMARK   3      T13:   0.0144 T23:   0.0279                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0198 L22:   2.1555                                     
REMARK   3      L33:   0.4267 L12:  -0.0323                                     
REMARK   3      L13:   0.1402 L23:   0.4707                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0452 S12:  -0.0682 S13:   0.0349                       
REMARK   3      S21:   0.1524 S22:  -0.0913 S23:  -0.2105                       
REMARK   3      S31:   0.0927 S32:   0.0467 S33:   0.0521                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1001 THROUGH 1106 )               
REMARK   3    ORIGIN FOR THE GROUP (A): -43.9290  -6.1836 -43.8908              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4981 T22:   0.6432                                     
REMARK   3      T33:   0.2460 T12:  -0.0942                                     
REMARK   3      T13:  -0.0518 T23:   0.0617                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2713 L22:   7.5586                                     
REMARK   3      L33:   4.5493 L12:   1.0007                                     
REMARK   3      L13:  -1.0553 L23:  -1.0327                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0443 S12:  -0.0448 S13:   0.0417                       
REMARK   3      S21:  -0.6231 S22:   0.0248 S23:   0.2392                       
REMARK   3      S31:  -0.1961 S32:   0.1457 S33:  -0.1013                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 313 THROUGH 400 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -27.5307 -22.9025  -5.2819              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7251 T22:   0.3091                                     
REMARK   3      T33:   0.3194 T12:  -0.0381                                     
REMARK   3      T13:  -0.0316 T23:   0.0896                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5155 L22:   1.1922                                     
REMARK   3      L33:   2.1289 L12:  -0.3206                                     
REMARK   3      L13:   1.0112 L23:   0.5433                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2444 S12:   0.0615 S13:   0.0387                       
REMARK   3      S21:   0.2207 S22:  -0.0962 S23:  -0.0053                       
REMARK   3      S31:   0.4766 S32:   0.1282 S33:  -0.1282                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5TVN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-NOV-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000224860.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5-8.0                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000, DENZO                    
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000, SCALEPACK                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12422                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.4                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.14900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.78300                            
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: 4IB4                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS/HCL PH 7.5-8.0, 90-130 MM    
REMARK 280  POTASSIUM PHOSPHATE MONOBASIC, 28-30% PEG400, LIPIDIC CUBIC         
REMARK 280  PHASE, TEMPERATURE 293K                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       85.49500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       85.49500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       29.59750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       59.58850            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       29.59750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       59.58850            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       85.49500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       29.59750            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       59.58850            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       85.49500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       29.59750            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       59.58850            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A   198                                                      
REMARK 465     VAL A   199                                                      
REMARK 465     ASP A   200                                                      
REMARK 465     ASP A  1050                                                      
REMARK 465     LYS A  1051                                                      
REMARK 465     SER A  1052                                                      
REMARK 465     PRO A  1053                                                      
REMARK 465     ASP A  1054                                                      
REMARK 465     SER A  1055                                                      
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 A  41    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  42    CG   CD   OE1  OE2                                  
REMARK 470     MET A  43    CG   SD   CE                                        
REMARK 470     LYS A  44    CG   CD   CE   NZ                                   
REMARK 470     GLN A  45    CG   CD   OE1  NE2                                  
REMARK 470     ILE A  46    CG1  CG2  CD1                                       
REMARK 470     VAL A  47    CG1  CG2                                            
REMARK 470     GLU A  48    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  49    CG   CD   OE1  OE2                                  
REMARK 470     GLN A  50    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  83    CG   CD   CE   NZ                                   
REMARK 470     LYS A  84    CG   CD   CE   NZ                                   
REMARK 470     GLU A 118    CG   CD   OE1  OE2                                  
REMARK 470     MET A 120    CG   SD   CE                                        
REMARK 470     LYS A 158    CG   CD   CE   NZ                                   
REMARK 470     LYS A 159    CG   CD   CE   NZ                                   
REMARK 470     ILE A 161    CG1  CG2  CD1                                       
REMARK 470     ASN A 164    CG   OD1  ND2                                       
REMARK 470     GLN A 165    CG   CD   OE1  NE2                                  
REMARK 470     TYR A 166    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN A 167    CG   OD1  ND2                                       
REMARK 470     ILE A 195    CG1  CG2  CD1                                       
REMARK 470     GLU A 196    CG   CD   OE1  OE2                                  
REMARK 470     THR A 197    OG1  CG2                                            
REMARK 470     ASN A 201    CG   OD1  ND2                                       
REMARK 470     ASN A 203    CG   OD1  ND2                                       
REMARK 470     LYS A 246    CG   CD   CE   NZ                                   
REMARK 470     GLU A1004    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1015    CG   CD   CE   NZ                                   
REMARK 470     GLU A1018    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1019    CG   CD   CE   NZ                                   
REMARK 470     ASP A1021    CG   OD1  OD2                                       
REMARK 470     LYS A1027    CG   CD   CE   NZ                                   
REMARK 470     LYS A1042    CG   CD   CE   NZ                                   
REMARK 470     GLU A1049    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1057    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1077    CG   CD   CE   NZ                                   
REMARK 470     LYS A1083    CG   CD   CE   NZ                                   
REMARK 470     LYS A1085    CG   CD   CE   NZ                                   
REMARK 470     GLU A1092    CG   CD   OE1  OE2                                  
REMARK 470     GLN A1093    CG   CD   OE1  NE2                                  
REMARK 470     THR A1096    OG1  CG2                                            
REMARK 470     GLN A1103    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 321    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 324    CG   CD   CE   NZ                                   
REMARK 470     ARG A 400    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    GLN A 162       55.35   -140.72                                   
REMARK 500    ASN A 164       -4.87     63.71                                   
REMARK 500    SER A 168     -154.97   -109.20                                   
REMARK 500    ASN A 203       45.60    -79.91                                   
REMARK 500    PHE A 226      -56.43   -129.21                                   
REMARK 500    LYS A1047       33.56    -78.76                                   
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     OLC A 2003                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7LD A 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 2002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 2004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 2005                
DBREF  5TVN A   41   248  UNP    P41595   5HT2B_HUMAN     41    248             
DBREF  5TVN A 1001  1106  UNP    P0ABE7   C562_ECOLX      23    128             
DBREF  5TVN A  313   400  UNP    P41595   5HT2B_HUMAN    313    400             
SEQADV 5TVN TRP A  144  UNP  P41595    MET   144 ENGINEERED MUTATION            
SEQADV 5TVN TRP A 1007  UNP  P0ABE7    MET    29 ENGINEERED MUTATION            
SEQADV 5TVN ILE A 1102  UNP  P0ABE7    HIS   124 ENGINEERED MUTATION            
SEQADV 5TVN LEU A 1106  UNP  P0ABE7    ARG   128 ENGINEERED MUTATION            
SEQRES   1 A  402  GLU GLU MET LYS GLN ILE VAL GLU GLU GLN GLY ASN LYS          
SEQRES   2 A  402  LEU HIS TRP ALA ALA LEU LEU ILE LEU MET VAL ILE ILE          
SEQRES   3 A  402  PRO THR ILE GLY GLY ASN THR LEU VAL ILE LEU ALA VAL          
SEQRES   4 A  402  SER LEU GLU LYS LYS LEU GLN TYR ALA THR ASN TYR PHE          
SEQRES   5 A  402  LEU MET SER LEU ALA VAL ALA ASP LEU LEU VAL GLY LEU          
SEQRES   6 A  402  PHE VAL MET PRO ILE ALA LEU LEU THR ILE MET PHE GLU          
SEQRES   7 A  402  ALA MET TRP PRO LEU PRO LEU VAL LEU CYS PRO ALA TRP          
SEQRES   8 A  402  LEU PHE LEU ASP VAL LEU PHE SER THR ALA SER ILE TRP          
SEQRES   9 A  402  HIS LEU CYS ALA ILE SER VAL ASP ARG TYR ILE ALA ILE          
SEQRES  10 A  402  LYS LYS PRO ILE GLN ALA ASN GLN TYR ASN SER ARG ALA          
SEQRES  11 A  402  THR ALA PHE ILE LYS ILE THR VAL VAL TRP LEU ILE SER          
SEQRES  12 A  402  ILE GLY ILE ALA ILE PRO VAL PRO ILE LYS GLY ILE GLU          
SEQRES  13 A  402  THR ASP VAL ASP ASN PRO ASN ASN ILE THR CYS VAL LEU          
SEQRES  14 A  402  THR LYS GLU ARG PHE GLY ASP PHE MET LEU PHE GLY SER          
SEQRES  15 A  402  LEU ALA ALA PHE PHE THR PRO LEU ALA ILE MET ILE VAL          
SEQRES  16 A  402  THR TYR PHE LEU THR ILE HIS ALA LEU GLN LYS LYS ALA          
SEQRES  17 A  402  ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN          
SEQRES  18 A  402  LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL          
SEQRES  19 A  402  LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP          
SEQRES  20 A  402  ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER          
SEQRES  21 A  402  PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE          
SEQRES  22 A  402  ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU          
SEQRES  23 A  402  ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA          
SEQRES  24 A  402  GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS          
SEQRES  25 A  402  TYR LEU VAL GLN THR ILE SER ASN GLU GLN ARG ALA SER          
SEQRES  26 A  402  LYS VAL LEU GLY ILE VAL PHE PHE LEU PHE LEU LEU MET          
SEQRES  27 A  402  TRP CYS PRO PHE PHE ILE THR ASN ILE THR LEU VAL LEU          
SEQRES  28 A  402  CYS ASP SER CYS ASN GLN THR THR LEU GLN MET LEU LEU          
SEQRES  29 A  402  GLU ILE PHE VAL TRP ILE GLY TYR VAL SER SER GLY VAL          
SEQRES  30 A  402  ASN PRO LEU VAL TYR THR LEU PHE ASN LYS THR PHE ARG          
SEQRES  31 A  402  ASP ALA PHE GLY ARG TYR ILE THR CYS ASN TYR ARG              
HET    7LD  A2001      24                                                       
HET    CLR  A2002      28                                                       
HET    OLC  A2003      19                                                       
HET    PEG  A2004       7                                                       
HET    PO4  A2005       5                                                       
HETNAM     7LD (8ALPHA)-N,N-DIETHYL-6-METHYL-9,10-DIDEHYDROERGOLINE-8-          
HETNAM   2 7LD  CARBOXAMIDE                                                     
HETNAM     CLR CHOLESTEROL                                                      
HETNAM     OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     PO4 PHOSPHATE ION                                                    
HETSYN     OLC 1-OLEOYL-R-GLYCEROL                                              
FORMUL   2  7LD    C20 H25 N3 O                                                 
FORMUL   3  CLR    C27 H46 O                                                    
FORMUL   4  OLC    C21 H40 O4                                                   
FORMUL   5  PEG    C4 H10 O3                                                    
FORMUL   6  PO4    O4 P 3-                                                      
FORMUL   7  HOH   *(H2 O)                                                       
HELIX    1 AA1 LYS A   53  VAL A   64  1                                  12    
HELIX    2 AA2 VAL A   64  GLU A   82  1                                  19    
HELIX    3 AA3 LYS A   83  GLN A   86  5                                   4    
HELIX    4 AA4 TYR A   87  VAL A  107  1                                  21    
HELIX    5 AA5 VAL A  107  LEU A  112  1                                   6    
HELIX    6 AA6 LEU A  112  PHE A  117  1                                   6    
HELIX    7 AA7 VAL A  126  LYS A  159  1                                  34    
HELIX    8 AA8 SER A  168  ILE A  188  1                                  21    
HELIX    9 AA9 ILE A  188  GLY A  194  1                                   7    
HELIX   10 AB1 THR A  210  PHE A  226  1                                  17    
HELIX   11 AB2 PHE A  226  LYS A 1019  1                                  42    
HELIX   12 AB3 ALA A 1023  LYS A 1042  1                                  20    
HELIX   13 AB4 ARG A 1062  GLY A 1082  1                                  21    
HELIX   14 AB5 LYS A 1083  TYR A 1101  1                                  19    
HELIX   15 AB6 TYR A 1101  CYS A  350  1                                  44    
HELIX   16 AB7 ASN A  354  VAL A  375  1                                  22    
HELIX   17 AB8 VAL A  375  LEU A  382  1                                   8    
HELIX   18 AB9 ASN A  384  ILE A  395  1                                  12    
SSBOND   1 CYS A  128    CYS A  207                          1555   1555  2.03  
SSBOND   2 CYS A  350    CYS A  353                          1555   1555  2.03  
SITE     1 AC1  9 TRP A 131  LEU A 132  ASP A 135  VAL A 136                    
SITE     2 AC1  9 SER A 139  PHE A 217  GLY A 221  PHE A 340                    
SITE     3 AC1  9 LEU A 362                                                     
SITE     1 AC2  5 ILE A  65  ILE A  66  GLY A  70  TYR A 394                    
SITE     2 AC2  5 TYR A 399                                                     
SITE     1 AC3  8 HIS A  55  LEU A  59  SER A 150  MET A 233                    
SITE     2 AC3  8 THR A 240  LEU A 326  GLY A 327  PHE A 330                    
SITE     1 AC4  2 TYR A  87  TYR A 380                                          
SITE     1 AC5  7 GLN A1041  PRO A1046  LYS A1047  ASP A1060                    
SITE     2 AC5  7 ARG A1062  HIS A1063  ASP A1066                               
CRYST1   59.195  119.177  170.990  90.00  90.00  90.00 C 2 2 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      0.016893  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008391  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005848        0.00000                         
ATOM      1  N   GLU A  41     -22.691 -31.146  40.279  1.00155.69           N  
ANISOU    1  N   GLU A  41    24882  21681  12593   -245   -773   3287       N  
ATOM      2  CA  GLU A  41     -23.130 -32.476  40.686  1.00158.86           C  
ANISOU    2  CA  GLU A  41    25385  22021  12953   -274   -673   3591       C  
ATOM      3  C   GLU A  41     -22.144 -33.543  40.222  1.00161.10           C  
ANISOU    3  C   GLU A  41    25648  22105  13458   -203   -896   3792       C  
ATOM      4  O   GLU A  41     -21.174 -33.243  39.524  1.00162.43           O  
ANISOU    4  O   GLU A  41    25713  22180  13822   -137  -1110   3685       O  
ATOM      5  CB  GLU A  41     -24.527 -32.771  40.137  1.00154.89           C  
ANISOU    5  CB  GLU A  41    24823  21449  12580   -373   -342   3603       C  
ATOM      6  N   GLU A  42     -22.398 -34.788  40.612  1.00153.75           N  
ANISOU    6  N   GLU A  42    24809  21104  12505   -217   -839   4083       N  
ATOM      7  CA  GLU A  42     -21.504 -35.891  40.279  1.00132.43           C  
ANISOU    7  CA  GLU A  42    22099  18209  10008   -145  -1042   4293       C  
ATOM      8  C   GLU A  42     -22.229 -37.008  39.534  1.00122.64           C  
ANISOU    8  C   GLU A  42    20800  16766   9031   -194   -860   4465       C  
ATOM      9  O   GLU A  42     -22.985 -37.777  40.129  1.00118.45           O  
ANISOU    9  O   GLU A  42    20368  16247   8389   -249   -688   4677       O  
ATOM     10  CB  GLU A  42     -20.852 -36.448  41.547  1.00123.15           C  
ANISOU   10  CB  GLU A  42    21102  17123   8565    -89  -1218   4514       C  
ATOM     11  N   MET A  43     -21.991 -37.088  38.228  1.00113.41           N  
ANISOU   11  N   MET A  43    19468  15411   8213   -176   -897   4372       N  
ATOM     12  CA  MET A  43     -22.564 -38.142  37.398  1.00114.83           C  
ANISOU   12  CA  MET A  43    19572  15378   8678   -214   -755   4512       C  
ATOM     13  C   MET A  43     -21.464 -38.870  36.631  1.00119.59           C  
ANISOU   13  C   MET A  43    20094  15765   9580   -121   -992   4588       C  
ATOM     14  O   MET A  43     -20.937 -38.352  35.647  1.00119.79           O  
ANISOU   14  O   MET A  43    19984  15718   9815    -84  -1095   4398       O  
ATOM     15  CB  MET A  43     -23.596 -37.564  36.427  1.00 95.98           C  
ANISOU   15  CB  MET A  43    17054  12968   6447   -298   -516   4309       C  
ATOM     16  N   LYS A  44     -21.119 -40.070  37.090  1.00117.78           N  
ANISOU   16  N   LYS A  44    19947  15431   9374    -82  -1074   4865       N  
ATOM     17  CA  LYS A  44     -20.031 -40.840  36.494  1.00112.80           C  
ANISOU   17  CA  LYS A  44    19249  14591   9020     15  -1309   4950       C  
ATOM     18  C   LYS A  44     -20.462 -41.523  35.202  1.00114.51           C  
ANISOU   18  C   LYS A  44    19322  14577   9611    -10  -1188   4955       C  
ATOM     19  O   LYS A  44     -19.626 -42.004  34.437  1.00116.42           O  
ANISOU   19  O   LYS A  44    19468  14636  10129     65  -1359   4958       O  
ATOM     20  CB  LYS A  44     -19.505 -41.881  37.483  1.00121.13           C  
ANISOU   20  CB  LYS A  44    20448  15609   9968     74  -1445   5246       C  
ATOM     21  N   GLN A  45     -21.768 -41.567  34.963  1.00114.80           N  
ANISOU   21  N   GLN A  45    19337  14621   9659   -117   -897   4949       N  
ATOM     22  CA  GLN A  45     -22.297 -42.138  33.730  1.00107.96           C  
ANISOU   22  CA  GLN A  45    18333  13551   9135   -152   -767   4932       C  
ATOM     23  C   GLN A  45     -22.258 -41.111  32.611  1.00107.62           C  
ANISOU   23  C   GLN A  45    18143  13519   9229   -157   -766   4632       C  
ATOM     24  O   GLN A  45     -22.560 -41.421  31.460  1.00 98.51           O  
ANISOU   24  O   GLN A  45    16863  12206   8360   -175   -692   4574       O  
ATOM     25  CB  GLN A  45     -23.727 -42.638  33.933  1.00 97.78           C  
ANISOU   25  CB  GLN A  45    17074  12255   7822   -270   -459   5052       C  
ATOM     26  N   ILE A  46     -21.886 -39.884  32.960  1.00121.83           N  
ANISOU   26  N   ILE A  46    19961  15505  10822   -140   -850   4442       N  
ATOM     27  CA  ILE A  46     -21.852 -38.788  32.001  1.00121.70           C  
ANISOU   27  CA  ILE A  46    19817  15518  10904   -143   -846   4158       C  
ATOM     28  C   ILE A  46     -20.603 -38.851  31.131  1.00119.12           C  
ANISOU   28  C   ILE A  46    19382  15053  10825    -44  -1093   4091       C  
ATOM     29  O   ILE A  46     -19.781 -37.936  31.142  1.00120.62           O  
ANISOU   29  O   ILE A  46    19546  15328  10957      9  -1261   3932       O  
ATOM     30  CB  ILE A  46     -21.904 -37.420  32.707  1.00122.68           C  
ANISOU   30  CB  ILE A  46    19995  15884  10734   -159   -843   3973       C  
ATOM     31  N   VAL A  47     -20.463 -39.937  30.379  1.00119.61           N  
ANISOU   31  N   VAL A  47    19375  14896  11174    -19  -1111   4207       N  
ATOM     32  CA  VAL A  47     -19.348 -40.083  29.456  1.00116.20           C  
ANISOU   32  CA  VAL A  47    18826  14315  11009     72  -1322   4140       C  
ATOM     33  C   VAL A  47     -19.685 -39.411  28.130  1.00110.48           C  
ANISOU   33  C   VAL A  47    17959  13555  10465     45  -1227   3914       C  
ATOM     34  O   VAL A  47     -19.612 -40.030  27.067  1.00115.99           O  
ANISOU   34  O   VAL A  47    18551  14070  11451     64  -1225   3914       O  
ATOM     35  CB  VAL A  47     -18.999 -41.563  29.216  1.00116.91           C  
ANISOU   35  CB  VAL A  47    18901  14176  11345    119  -1391   4352       C  
ATOM     36  N   GLU A  48     -20.066 -38.139  28.205  1.00111.62           N  
ANISOU   36  N   GLU A  48    18101  13874  10436      4  -1149   3720       N  
ATOM     37  CA  GLU A  48     -20.415 -37.368  27.021  1.00 91.80           C  
ANISOU   37  CA  GLU A  48    15467  11350   8061    -20  -1056   3502       C  
ATOM     38  C   GLU A  48     -19.160 -36.819  26.367  1.00 90.26           C  
ANISOU   38  C   GLU A  48    15174  11118   8001     69  -1282   3366       C  
ATOM     39  O   GLU A  48     -18.962 -35.608  26.298  1.00 69.45           O  
ANISOU   39  O   GLU A  48    12511   8605   5272     73  -1311   3178       O  
ATOM     40  CB  GLU A  48     -21.368 -36.225  27.378  1.00 75.97           C  
ANISOU   40  CB  GLU A  48    13495   9538   5832    -98   -873   3348       C  
ATOM     41  N   GLU A  49     -18.305 -37.726  25.908  1.00 94.92           N  
ANISOU   41  N   GLU A  49    15710  11534   8824    142  -1441   3462       N  
ATOM     42  CA  GLU A  49     -17.093 -37.356  25.194  1.00104.92           C  
ANISOU   42  CA  GLU A  49    16864  12735  10265    228  -1651   3345       C  
ATOM     43  C   GLU A  49     -17.351 -37.450  23.701  1.00115.61           C  
ANISOU   43  C   GLU A  49    18085  13957  11884    225  -1563   3243       C  
ATOM     44  O   GLU A  49     -17.618 -38.534  23.183  1.00132.59           O  
ANISOU   44  O   GLU A  49    20204  15943  14232    224  -1510   3349       O  
ATOM     45  CB  GLU A  49     -15.925 -38.258  25.595  1.00103.72           C  
ANISOU   45  CB  GLU A  49    16717  12469  10221    317  -1892   3494       C  
ATOM     46  N   GLN A  50     -17.280 -36.311  23.019  1.00108.52           N  
ANISOU   46  N   GLN A  50    17112  13128  10991    226  -1548   3036       N  
ATOM     47  CA  GLN A  50     -17.579 -36.246  21.594  1.00 92.12           C  
ANISOU   47  CA  GLN A  50    14920  10951   9129    222  -1456   2925       C  
ATOM     48  C   GLN A  50     -16.667 -37.158  20.786  1.00 91.07           C  
ANISOU   48  C   GLN A  50    14686  10616   9300    304  -1604   2975       C  
ATOM     49  O   GLN A  50     -15.443 -37.039  20.842  1.00 86.60           O  
ANISOU   49  O   GLN A  50    14067  10023   8813    384  -1820   2954       O  
ATOM     50  CB  GLN A  50     -17.459 -34.808  21.088  1.00 78.03           C  
ANISOU   50  CB  GLN A  50    13079   9280   7290    225  -1449   2705       C  
ATOM     51  N   GLY A  51     -17.277 -38.072  20.038  1.00 92.75           N  
ANISOU   51  N   GLY A  51    14862  10681   9697    282  -1488   3031       N  
ATOM     52  CA  GLY A  51     -16.533 -39.012  19.224  1.00 94.98           C  
ANISOU   52  CA  GLY A  51    15039  10758  10291    356  -1605   3067       C  
ATOM     53  C   GLY A  51     -15.888 -38.354  18.021  1.00 91.34           C  
ANISOU   53  C   GLY A  51    14445  10263   9996    413  -1672   2887       C  
ATOM     54  O   GLY A  51     -16.142 -37.184  17.729  1.00 93.74           O  
ANISOU   54  O   GLY A  51    14745  10694  10177    390  -1606   2740       O  
ATOM     55  N   ASN A  52     -15.053 -39.112  17.319  1.00 87.76           N  
ANISOU   55  N   ASN A  52    13878   9634   9834    491  -1798   2897       N  
ATOM     56  CA  ASN A  52     -14.342 -38.600  16.155  1.00 71.30           C  
ANISOU   56  CA  ASN A  52    11653   7500   7937    557  -1867   2736       C  
ATOM     57  C   ASN A  52     -15.279 -38.354  14.979  1.00 66.56           C  
ANISOU   57  C   ASN A  52    11017   6880   7392    517  -1673   2621       C  
ATOM     58  O   ASN A  52     -16.004 -39.251  14.552  1.00 72.45           O  
ANISOU   58  O   ASN A  52    11743   7519   8265    486  -1549   2659       O  
ATOM     59  CB  ASN A  52     -13.235 -39.569  15.740  1.00 64.88           C  
ANISOU   59  CB  ASN A  52    10710   6497   7445    652  -2038   2770       C  
ATOM     60  CG  ASN A  52     -12.147 -38.899  14.931  1.00 66.21           C  
ANISOU   60  CG  ASN A  52    10730   6647   7779    735  -2162   2615       C  
ATOM     61  OD1 ASN A  52     -12.349 -37.826  14.364  1.00 71.97           O  
ANISOU   61  OD1 ASN A  52    11417   7492   8435    718  -2066   2457       O  
ATOM     62  ND2 ASN A  52     -10.981 -39.531  14.872  1.00 74.54           N  
ANISOU   62  ND2 ASN A  52    11667   7576   9079    821  -2340   2631       N  
ATOM     63  N   LYS A  53     -15.258 -37.135  14.456  1.00 60.14           N  
ANISOU   63  N   LYS A  53    10125   6209   6517    517  -1603   2429       N  
ATOM     64  CA  LYS A  53     -16.125 -36.773  13.344  1.00 64.33           C  
ANISOU   64  CA  LYS A  53    10553   6785   7107    481  -1378   2260       C  
ATOM     65  C   LYS A  53     -15.311 -36.472  12.088  1.00 58.41           C  
ANISOU   65  C   LYS A  53     9591   6010   6591    555  -1392   2076       C  
ATOM     66  O   LYS A  53     -15.641 -35.567  11.323  1.00 52.79           O  
ANISOU   66  O   LYS A  53     8803   5402   5854    541  -1265   1912       O  
ATOM     67  CB  LYS A  53     -16.995 -35.574  13.724  1.00 80.52           C  
ANISOU   67  CB  LYS A  53    12694   9021   8878    407  -1248   2192       C  
ATOM     68  CG  LYS A  53     -17.887 -35.831  14.931  1.00 84.51           C  
ANISOU   68  CG  LYS A  53    13407   9564   9137    325  -1195   2357       C  
ATOM     69  CD  LYS A  53     -18.715 -34.605  15.282  1.00 82.13           C  
ANISOU   69  CD  LYS A  53    13180   9447   8580    256  -1062   2264       C  
ATOM     70  CE  LYS A  53     -19.607 -34.872  16.484  1.00 80.82           C  
ANISOU   70  CE  LYS A  53    13173   9343   8192    171   -971   2396       C  
ATOM     71  NZ  LYS A  53     -18.817 -35.323  17.665  1.00 86.18           N  
ANISOU   71  NZ  LYS A  53    13904  10035   8806    199  -1135   2532       N  
ATOM     72  N   LEU A  54     -14.251 -37.245  11.881  1.00 55.39           N  
ANISOU   72  N   LEU A  54     9116   5488   6442    634  -1543   2110       N  
ATOM     73  CA  LEU A  54     -13.372 -37.055  10.736  1.00 48.13           C  
ANISOU   73  CA  LEU A  54     7994   4536   5759    706  -1555   1943       C  
ATOM     74  C   LEU A  54     -14.029 -37.509   9.435  1.00 68.84           C  
ANISOU   74  C   LEU A  54    10503   7112   8541    699  -1369   1819       C  
ATOM     75  O   LEU A  54     -13.767 -36.941   8.373  1.00 82.63           O  
ANISOU   75  O   LEU A  54    12114   8908  10373    726  -1291   1646       O  
ATOM     76  CB  LEU A  54     -12.057 -37.806  10.946  1.00 49.87           C  
ANISOU   76  CB  LEU A  54     8140   4609   6199    794  -1771   2011       C  
ATOM     77  CG  LEU A  54     -10.923 -37.500   9.967  1.00 49.23           C  
ANISOU   77  CG  LEU A  54     7849   4502   6355    873  -1807   1844       C  
ATOM     78  CD1 LEU A  54     -10.426 -36.071  10.148  1.00 48.39           C  
ANISOU   78  CD1 LEU A  54     7727   4546   6114    873  -1842   1755       C  
ATOM     79  CD2 LEU A  54      -9.786 -38.500  10.134  1.00 51.18           C  
ANISOU   79  CD2 LEU A  54     8012   4568   6866    957  -2005   1915       C  
ATOM     80  N   HIS A  55     -14.885 -38.525   9.515  1.00 53.20           N  
ANISOU   80  N   HIS A  55     8580   5036   6598    660  -1299   1907       N  
ATOM     81  CA  HIS A  55     -15.534 -39.050   8.318  1.00 49.59           C  
ANISOU   81  CA  HIS A  55     8017   4524   6302    655  -1141   1785       C  
ATOM     82  C   HIS A  55     -16.509 -38.046   7.696  1.00 52.46           C  
ANISOU   82  C   HIS A  55     8378   5044   6511    601   -956   1644       C  
ATOM     83  O   HIS A  55     -16.729 -38.065   6.487  1.00 51.61           O  
ANISOU   83  O   HIS A  55     8153   4937   6520    618   -849   1487       O  
ATOM     84  CB  HIS A  55     -16.253 -40.372   8.621  1.00 58.09           C  
ANISOU   84  CB  HIS A  55     9152   5449   7471    621  -1115   1916       C  
ATOM     85  CG  HIS A  55     -17.103 -40.341   9.854  1.00 77.86           C  
ANISOU   85  CG  HIS A  55    11850   7994   9738    537  -1092   2094       C  
ATOM     86  ND1 HIS A  55     -16.592 -40.555  11.115  1.00 50.63           N  
ANISOU   86  ND1 HIS A  55     8533   4517   6187    540  -1252   2293       N  
ATOM     87  CD2 HIS A  55     -18.434 -40.145  10.014  1.00 74.62           C  
ANISOU   87  CD2 HIS A  55    11525   7652   9176    447   -924   2102       C  
ATOM     88  CE1 HIS A  55     -17.570 -40.479  12.003  1.00 53.86           C  
ANISOU   88  CE1 HIS A  55     9109   4983   6372    453  -1171   2418       C  
ATOM     89  NE2 HIS A  55     -18.696 -40.232  11.360  1.00 61.36           N  
ANISOU   89  NE2 HIS A  55    10027   5988   7299    394   -967   2302       N  
ATOM     90  N   TRP A  56     -17.081 -37.164   8.511  1.00 58.81           N  
ANISOU   90  N   TRP A  56     9311   5980   7054    539   -925   1693       N  
ATOM     91  CA  TRP A  56     -17.968 -36.128   7.983  1.00 54.89           C  
ANISOU   91  CA  TRP A  56     8808   5628   6421    492   -766   1562       C  
ATOM     92  C   TRP A  56     -17.156 -35.038   7.307  1.00 55.75           C  
ANISOU   92  C   TRP A  56     8811   5830   6539    540   -787   1420       C  
ATOM     93  O   TRP A  56     -17.582 -34.461   6.305  1.00 60.58           O  
ANISOU   93  O   TRP A  56     9349   6511   7156    536   -666   1277       O  
ATOM     94  CB  TRP A  56     -18.836 -35.516   9.083  1.00 50.37           C  
ANISOU   94  CB  TRP A  56     8396   5161   5582    410   -718   1647       C  
ATOM     95  CG  TRP A  56     -19.661 -36.512   9.821  1.00 62.97           C  
ANISOU   95  CG  TRP A  56    10104   6672   7148    351   -677   1800       C  
ATOM     96  CD1 TRP A  56     -19.546 -36.854  11.134  1.00 71.02           C  
ANISOU   96  CD1 TRP A  56    11275   7672   8036    324   -764   1988       C  
ATOM     97  CD2 TRP A  56     -20.727 -37.309   9.290  1.00 68.74           C  
ANISOU   97  CD2 TRP A  56    10808   7323   7988    309   -537   1783       C  
ATOM     98  NE1 TRP A  56     -20.476 -37.811  11.458  1.00 80.59           N  
ANISOU   98  NE1 TRP A  56    12558   8793   9269    264   -674   2102       N  
ATOM     99  CE2 TRP A  56     -21.213 -38.109  10.341  1.00 77.51           C  
ANISOU   99  CE2 TRP A  56    12051   8359   9039    253   -535   1972       C  
ATOM    100  CE3 TRP A  56     -21.317 -37.423   8.027  1.00 69.96           C  
ANISOU  100  CE3 TRP A  56    10838   7459   8283    314   -419   1623       C  
ATOM    101  CZ2 TRP A  56     -22.261 -39.010  10.173  1.00 84.64           C  
ANISOU  101  CZ2 TRP A  56    12955   9162  10043    198   -410   2007       C  
ATOM    102  CZ3 TRP A  56     -22.359 -38.320   7.861  1.00 76.72           C  
ANISOU  102  CZ3 TRP A  56    11694   8220   9234    264   -311   1645       C  
ATOM    103  CH2 TRP A  56     -22.819 -39.101   8.927  1.00 83.15           C  
ANISOU  103  CH2 TRP A  56    12630   8952  10011    205   -303   1834       C  
ATOM    104  N   ALA A  57     -15.983 -34.757   7.863  1.00 53.57           N  
ANISOU  104  N   ALA A  57     8530   5553   6271    586   -945   1465       N  
ATOM    105  CA  ALA A  57     -15.098 -33.749   7.298  1.00 51.96           C  
ANISOU  105  CA  ALA A  57     8218   5422   6103    631   -970   1343       C  
ATOM    106  C   ALA A  57     -14.555 -34.216   5.950  1.00 50.76           C  
ANISOU  106  C   ALA A  57     7898   5197   6191    691   -926   1222       C  
ATOM    107  O   ALA A  57     -14.418 -33.423   5.020  1.00 50.27           O  
ANISOU  107  O   ALA A  57     7746   5212   6143    704   -840   1089       O  
ATOM    108  CB  ALA A  57     -13.961 -33.436   8.258  1.00 45.81           C  
ANISOU  108  CB  ALA A  57     7463   4641   5302    666  -1164   1416       C  
ATOM    109  N   ALA A  58     -14.255 -35.507   5.849  1.00 44.51           N  
ANISOU  109  N   ALA A  58     7068   4256   5587    728   -980   1271       N  
ATOM    110  CA  ALA A  58     -13.776 -36.079   4.596  1.00 44.38           C  
ANISOU  110  CA  ALA A  58     6895   4164   5805    786   -931   1146       C  
ATOM    111  C   ALA A  58     -14.854 -36.016   3.515  1.00 50.71           C  
ANISOU  111  C   ALA A  58     7673   5019   6576    755   -746   1024       C  
ATOM    112  O   ALA A  58     -14.557 -35.775   2.346  1.00 56.97           O  
ANISOU  112  O   ALA A  58     8352   5843   7451    790   -666    878       O  
ATOM    113  CB  ALA A  58     -13.321 -37.513   4.806  1.00 43.56           C  
ANISOU  113  CB  ALA A  58     6758   3875   5917    829  -1034   1225       C  
ATOM    114  N   LEU A  59     -16.106 -36.224   3.909  1.00 50.65           N  
ANISOU  114  N   LEU A  59     7773   5024   6447    688   -678   1082       N  
ATOM    115  CA  LEU A  59     -17.209 -36.223   2.958  1.00 50.89           C  
ANISOU  115  CA  LEU A  59     7783   5095   6457    658   -522    969       C  
ATOM    116  C   LEU A  59     -17.528 -34.818   2.455  1.00 52.37           C  
ANISOU  116  C   LEU A  59     7967   5448   6483    638   -433    869       C  
ATOM    117  O   LEU A  59     -17.972 -34.650   1.321  1.00 53.21           O  
ANISOU  117  O   LEU A  59     8011   5598   6607    645   -328    738       O  
ATOM    118  CB  LEU A  59     -18.452 -36.862   3.584  1.00 62.75           C  
ANISOU  118  CB  LEU A  59     9389   6551   7903    589   -475   1063       C  
ATOM    119  CG  LEU A  59     -18.409 -38.392   3.670  1.00 66.72           C  
ANISOU  119  CG  LEU A  59     9870   6869   8612    605   -519   1128       C  
ATOM    120  CD1 LEU A  59     -19.677 -38.956   4.295  1.00 69.61           C  
ANISOU  120  CD1 LEU A  59    10337   7188   8924    527   -453   1227       C  
ATOM    121  CD2 LEU A  59     -18.184 -38.994   2.291  1.00 62.68           C  
ANISOU  121  CD2 LEU A  59     9213   6295   8308    662   -471    962       C  
ATOM    122  N   LEU A  60     -17.297 -33.810   3.293  1.00 55.15           N  
ANISOU  122  N   LEU A  60     8386   5889   6680    615   -482    929       N  
ATOM    123  CA  LEU A  60     -17.523 -32.423   2.889  1.00 45.97           C  
ANISOU  123  CA  LEU A  60     7214   4868   5383    597   -410    844       C  
ATOM    124  C   LEU A  60     -16.415 -31.950   1.954  1.00 51.59           C  
ANISOU  124  C   LEU A  60     7801   5602   6199    659   -414    745       C  
ATOM    125  O   LEU A  60     -16.640 -31.116   1.078  1.00 54.29           O  
ANISOU  125  O   LEU A  60     8102   6033   6492    657   -320    648       O  
ATOM    126  CB  LEU A  60     -17.610 -31.506   4.108  1.00 40.23           C  
ANISOU  126  CB  LEU A  60     6591   4221   4472    553   -464    926       C  
ATOM    127  CG  LEU A  60     -18.775 -31.770   5.061  1.00 47.39           C  
ANISOU  127  CG  LEU A  60     7631   5134   5240    482   -429   1017       C  
ATOM    128  CD1 LEU A  60     -18.639 -30.922   6.312  1.00 41.53           C  
ANISOU  128  CD1 LEU A  60     6992   4471   4318    449   -498   1089       C  
ATOM    129  CD2 LEU A  60     -20.107 -31.512   4.377  1.00 53.88           C  
ANISOU  129  CD2 LEU A  60     8451   6007   6012    438   -279    931       C  
ATOM    130  N   ILE A  61     -15.213 -32.481   2.153  1.00 45.61           N  
ANISOU  130  N   ILE A  61     6981   4758   5590    712   -521    776       N  
ATOM    131  CA  ILE A  61     -14.115 -32.220   1.236  1.00 43.25           C  
ANISOU  131  CA  ILE A  61     6546   4458   5427    771   -509    679       C  
ATOM    132  C   ILE A  61     -14.443 -32.797  -0.134  1.00 45.80           C  
ANISOU  132  C   ILE A  61     6795   4766   5842    795   -388    557       C  
ATOM    133  O   ILE A  61     -14.375 -32.100  -1.144  1.00 49.88           O  
ANISOU  133  O   ILE A  61     7255   5366   6332    805   -288    454       O  
ATOM    134  CB  ILE A  61     -12.791 -32.824   1.739  1.00 48.10           C  
ANISOU  134  CB  ILE A  61     7094   4962   6219    826   -654    729       C  
ATOM    135  CG1 ILE A  61     -12.306 -32.084   2.987  1.00 54.39           C  
ANISOU  135  CG1 ILE A  61     7952   5792   6920    812   -789    825       C  
ATOM    136  CG2 ILE A  61     -11.732 -32.769   0.648  1.00 44.91           C  
ANISOU  136  CG2 ILE A  61     6529   4541   5992    887   -611    609       C  
ATOM    137  CD1 ILE A  61     -10.953 -32.550   3.493  1.00 39.76           C  
ANISOU  137  CD1 ILE A  61     6027   3836   5245    871   -955    869       C  
ATOM    138  N   LEU A  62     -14.816 -34.073  -0.157  1.00 51.14           N  
ANISOU  138  N   LEU A  62     7474   5334   6622    803   -398    570       N  
ATOM    139  CA  LEU A  62     -15.070 -34.773  -1.409  1.00 49.11           C  
ANISOU  139  CA  LEU A  62     7141   5047   6471    833   -302    440       C  
ATOM    140  C   LEU A  62     -16.306 -34.242  -2.132  1.00 48.63           C  
ANISOU  140  C   LEU A  62     7126   5094   6258    792   -178    363       C  
ATOM    141  O   LEU A  62     -16.261 -33.978  -3.332  1.00 48.56           O  
ANISOU  141  O   LEU A  62     7056   5147   6249    819    -87    237       O  
ATOM    142  CB  LEU A  62     -15.214 -36.278  -1.153  1.00 44.41           C  
ANISOU  142  CB  LEU A  62     6539   4293   6044    847   -355    476       C  
ATOM    143  CG  LEU A  62     -15.496 -37.190  -2.352  1.00 52.12           C  
ANISOU  143  CG  LEU A  62     7432   5214   7156    879   -273    331       C  
ATOM    144  CD1 LEU A  62     -14.519 -36.929  -3.489  1.00 51.37           C  
ANISOU  144  CD1 LEU A  62     7214   5161   7144    941   -214    187       C  
ATOM    145  CD2 LEU A  62     -15.438 -38.651  -1.928  1.00 58.36           C  
ANISOU  145  CD2 LEU A  62     8202   5821   8150    897   -350    384       C  
ATOM    146  N   MET A  63     -17.401 -34.068  -1.401  1.00 50.97           N  
ANISOU  146  N   MET A  63     7529   5414   6422    730   -176    439       N  
ATOM    147  CA  MET A  63     -18.679 -33.740  -2.028  1.00 52.89           C  
ANISOU  147  CA  MET A  63     7805   5733   6556    693    -74    366       C  
ATOM    148  C   MET A  63     -18.999 -32.245  -2.094  1.00 51.12           C  
ANISOU  148  C   MET A  63     7619   5652   6150    664    -29    356       C  
ATOM    149  O   MET A  63     -19.854 -31.833  -2.875  1.00 53.52           O  
ANISOU  149  O   MET A  63     7929   6029   6379    651     50    275       O  
ATOM    150  CB  MET A  63     -19.810 -34.463  -1.300  1.00 53.12           C  
ANISOU  150  CB  MET A  63     7912   5696   6576    638    -76    436       C  
ATOM    151  CG  MET A  63     -19.783 -35.972  -1.464  1.00 45.61           C  
ANISOU  151  CG  MET A  63     6915   4593   5820    662    -99    426       C  
ATOM    152  SD  MET A  63     -20.872 -36.791  -0.287  1.00146.76           S  
ANISOU  152  SD  MET A  63    19824  17305  18633    588   -110    563       S  
ATOM    153  CE  MET A  63     -22.366 -35.823  -0.483  1.00 79.76           C  
ANISOU  153  CE  MET A  63    11393   8948   9963    522     -1    507       C  
ATOM    154  N   VAL A  64     -18.331 -31.429  -1.285  1.00 44.94           N  
ANISOU  154  N   VAL A  64     6861   4907   5307    656    -87    434       N  
ATOM    155  CA  VAL A  64     -18.670 -30.009  -1.251  1.00 42.65           C  
ANISOU  155  CA  VAL A  64     6605   4738   4864    625    -50    426       C  
ATOM    156  C   VAL A  64     -17.498 -29.072  -1.560  1.00 42.17           C  
ANISOU  156  C   VAL A  64     6479   4726   4819    658    -62    406       C  
ATOM    157  O   VAL A  64     -17.630 -28.170  -2.387  1.00 42.10           O  
ANISOU  157  O   VAL A  64     6445   4801   4751    661     12    345       O  
ATOM    158  CB  VAL A  64     -19.260 -29.607   0.117  1.00 45.05           C  
ANISOU  158  CB  VAL A  64     7013   5060   5044    565    -91    526       C  
ATOM    159  CG1 VAL A  64     -19.923 -28.249   0.020  1.00 42.11           C  
ANISOU  159  CG1 VAL A  64     6668   4800   4530    530    -34    492       C  
ATOM    160  CG2 VAL A  64     -20.270 -30.637   0.584  1.00 33.82           C  
ANISOU  160  CG2 VAL A  64     5652   3569   3628    527    -77    569       C  
ATOM    161  N   ILE A  65     -16.360 -29.269  -0.901  1.00 41.85           N  
ANISOU  161  N   ILE A  65     6406   4628   4865    683   -157    462       N  
ATOM    162  CA  ILE A  65     -15.250 -28.330  -1.059  1.00 45.18           C  
ANISOU  162  CA  ILE A  65     6758   5088   5321    707   -173    445       C  
ATOM    163  C   ILE A  65     -14.599 -28.429  -2.439  1.00 49.45           C  
ANISOU  163  C   ILE A  65     7189   5633   5966    756    -86    347       C  
ATOM    164  O   ILE A  65     -14.354 -27.411  -3.087  1.00 60.69           O  
ANISOU  164  O   ILE A  65     8576   7133   7352    756    -16    308       O  
ATOM    165  CB  ILE A  65     -14.174 -28.528   0.029  1.00 33.67           C  
ANISOU  165  CB  ILE A  65     5285   3562   3945    725   -315    522       C  
ATOM    166  CG1 ILE A  65     -14.814 -28.470   1.421  1.00 60.56           C  
ANISOU  166  CG1 ILE A  65     8818   6974   7219    677   -397    623       C  
ATOM    167  CG2 ILE A  65     -13.081 -27.484  -0.116  1.00 33.69           C  
ANISOU  167  CG2 ILE A  65     5203   3600   4000    744   -330    495       C  
ATOM    168  CD1 ILE A  65     -13.898 -27.966   2.527  1.00 34.50           C  
ANISOU  168  CD1 ILE A  65     5525   3667   3915    681   -536    685       C  
ATOM    169  N   ILE A  66     -14.326 -29.647  -2.892  1.00 40.21           N  
ANISOU  169  N   ILE A  66     5968   4382   4928    796    -83    306       N  
ATOM    170  CA  ILE A  66     -13.741 -29.843  -4.215  1.00 46.79           C  
ANISOU  170  CA  ILE A  66     6702   5225   5853    842     13    196       C  
ATOM    171  C   ILE A  66     -14.694 -29.442  -5.360  1.00 52.35           C  
ANISOU  171  C   ILE A  66     7438   6027   6426    830    138    117       C  
ATOM    172  O   ILE A  66     -14.271 -28.742  -6.284  1.00 57.46           O  
ANISOU  172  O   ILE A  66     8039   6746   7049    845    227     64       O  
ATOM    173  CB  ILE A  66     -13.274 -31.304  -4.411  1.00 53.17           C  
ANISOU  173  CB  ILE A  66     7443   5913   6847    890    -16    154       C  
ATOM    174  CG1 ILE A  66     -12.149 -31.632  -3.425  1.00 54.86           C  
ANISOU  174  CG1 ILE A  66     7607   6026   7213    915   -149    228       C  
ATOM    175  CG2 ILE A  66     -12.815 -31.534  -5.843  1.00 51.85           C  
ANISOU  175  CG2 ILE A  66     7181   5769   6751    936    103     18       C  
ATOM    176  CD1 ILE A  66     -11.648 -33.056  -3.509  1.00 44.46           C  
ANISOU  176  CD1 ILE A  66     6217   4571   6105    965   -197    199       C  
ATOM    177  N   PRO A  67     -15.976 -29.870  -5.314  1.00 45.11           N  
ANISOU  177  N   PRO A  67     6598   5113   5427    802    144    112       N  
ATOM    178  CA  PRO A  67     -16.863 -29.401  -6.389  1.00 48.62           C  
ANISOU  178  CA  PRO A  67     7072   5655   5748    795    240     36       C  
ATOM    179  C   PRO A  67     -17.007 -27.879  -6.445  1.00 50.86           C  
ANISOU  179  C   PRO A  67     7386   6042   5896    767    273     73       C  
ATOM    180  O   PRO A  67     -17.182 -27.323  -7.531  1.00 57.27           O  
ANISOU  180  O   PRO A  67     8193   6935   6632    778    356     17       O  
ATOM    181  CB  PRO A  67     -18.205 -30.057  -6.045  1.00 50.40           C  
ANISOU  181  CB  PRO A  67     7368   5849   5935    762    217     39       C  
ATOM    182  CG  PRO A  67     -17.832 -31.278  -5.284  1.00 48.57           C  
ANISOU  182  CG  PRO A  67     7117   5487   5849    772    143     80       C  
ATOM    183  CD  PRO A  67     -16.648 -30.868  -4.460  1.00 41.56           C  
ANISOU  183  CD  PRO A  67     6204   4576   5013    781     73    164       C  
ATOM    184  N   THR A  68     -16.928 -27.220  -5.293  1.00 40.55           N  
ANISOU  184  N   THR A  68     6114   4732   4561    731    205    165       N  
ATOM    185  CA  THR A  68     -17.016 -25.763  -5.236  1.00 38.86           C  
ANISOU  185  CA  THR A  68     5920   4599   4248    703    226    197       C  
ATOM    186  C   THR A  68     -15.809 -25.086  -5.883  1.00 42.05           C  
ANISOU  186  C   THR A  68     6240   5027   4708    731    276    183       C  
ATOM    187  O   THR A  68     -15.956 -24.175  -6.698  1.00 44.51           O  
ANISOU  187  O   THR A  68     6552   5414   4947    728    353    167       O  
ATOM    188  CB  THR A  68     -17.136 -25.267  -3.786  1.00 45.05           C  
ANISOU  188  CB  THR A  68     6755   5368   4996    661    138    281       C  
ATOM    189  OG1 THR A  68     -18.388 -25.693  -3.237  1.00 40.30           O  
ANISOU  189  OG1 THR A  68     6235   4758   4320    624    122    296       O  
ATOM    190  CG2 THR A  68     -17.055 -23.750  -3.733  1.00 29.45           C  
ANISOU  190  CG2 THR A  68     4778   3460   2953    638    155    300       C  
ATOM    191  N   ILE A  69     -14.615 -25.533  -5.511  1.00 45.87           N  
ANISOU  191  N   ILE A  69     6651   5444   5334    758    231    193       N  
ATOM    192  CA  ILE A  69     -13.386 -24.941  -6.024  1.00 44.89           C  
ANISOU  192  CA  ILE A  69     6430   5328   5298    780    282    178       C  
ATOM    193  C   ILE A  69     -13.171 -25.293  -7.490  1.00 44.78           C  
ANISOU  193  C   ILE A  69     6370   5350   5296    816    410     92       C  
ATOM    194  O   ILE A  69     -12.790 -24.443  -8.292  1.00 54.05           O  
ANISOU  194  O   ILE A  69     7511   6584   6440    816    508     83       O  
ATOM    195  CB  ILE A  69     -12.163 -25.398  -5.212  1.00 49.42           C  
ANISOU  195  CB  ILE A  69     6924   5809   6044    803    186    201       C  
ATOM    196  CG1 ILE A  69     -12.319 -24.992  -3.747  1.00 44.56           C  
ANISOU  196  CG1 ILE A  69     6366   5172   5392    769     51    284       C  
ATOM    197  CG2 ILE A  69     -10.884 -24.817  -5.795  1.00 47.22           C  
ANISOU  197  CG2 ILE A  69     6524   5530   5885    824    252    173       C  
ATOM    198  CD1 ILE A  69     -11.269 -25.590  -2.842  1.00 43.71           C  
ANISOU  198  CD1 ILE A  69     6202   4970   5437    795    -78    316       C  
ATOM    199  N   GLY A  70     -13.423 -26.550  -7.835  1.00 43.59           N  
ANISOU  199  N   GLY A  70     6218   5160   5185    846    414     28       N  
ATOM    200  CA  GLY A  70     -13.263 -27.005  -9.202  1.00 43.85           C  
ANISOU  200  CA  GLY A  70     6213   5229   5219    883    531    -75       C  
ATOM    201  C   GLY A  70     -14.258 -26.374 -10.155  1.00 42.24           C  
ANISOU  201  C   GLY A  70     6087   5137   4825    870    612    -98       C  
ATOM    202  O   GLY A  70     -13.898 -25.961 -11.255  1.00 47.07           O  
ANISOU  202  O   GLY A  70     6678   5820   5388    886    726   -140       O  
ATOM    203  N   GLY A  71     -15.513 -26.294  -9.725  1.00 45.97           N  
ANISOU  203  N   GLY A  71     6650   5623   5193    839    552    -70       N  
ATOM    204  CA  GLY A  71     -16.583 -25.800 -10.571  1.00 49.50           C  
ANISOU  204  CA  GLY A  71     7170   6164   5475    830    600    -97       C  
ATOM    205  C   GLY A  71     -16.459 -24.331 -10.919  1.00 54.84           C  
ANISOU  205  C   GLY A  71     7861   6918   6056    811    653    -34       C  
ATOM    206  O   GLY A  71     -16.800 -23.920 -12.027  1.00 60.23           O  
ANISOU  206  O   GLY A  71     8579   7685   6622    823    727    -62       O  
ATOM    207  N   ASN A  72     -15.968 -23.538  -9.972  1.00 56.05           N  
ANISOU  207  N   ASN A  72     7993   7042   6262    781    610     51       N  
ATOM    208  CA  ASN A  72     -15.842 -22.099 -10.175  1.00 50.58           C  
ANISOU  208  CA  ASN A  72     7305   6402   5510    758    651    116       C  
ATOM    209  C   ASN A  72     -14.551 -21.725 -10.885  1.00 52.80           C  
ANISOU  209  C   ASN A  72     7506   6696   5859    776    753    117       C  
ATOM    210  O   ASN A  72     -14.414 -20.618 -11.400  1.00 62.59           O  
ANISOU  210  O   ASN A  72     8749   7985   7047    761    820    167       O  
ATOM    211  CB  ASN A  72     -15.935 -21.364  -8.841  1.00 49.07           C  
ANISOU  211  CB  ASN A  72     7122   6173   5350    716    558    189       C  
ATOM    212  CG  ASN A  72     -17.309 -21.472  -8.219  1.00 47.78           C  
ANISOU  212  CG  ASN A  72     7042   6011   5100    689    487    193       C  
ATOM    213  OD1 ASN A  72     -18.264 -20.862  -8.697  1.00 49.46           O  
ANISOU  213  OD1 ASN A  72     7307   6278   5208    678    507    194       O  
ATOM    214  ND2 ASN A  72     -17.417 -22.246  -7.146  1.00 51.98           N  
ANISOU  214  ND2 ASN A  72     7586   6482   5682    678    405    199       N  
ATOM    215  N   THR A  73     -13.602 -22.650 -10.907  1.00 60.07           N  
ANISOU  215  N   THR A  73     8349   7566   6910    807    770     65       N  
ATOM    216  CA  THR A  73     -12.396 -22.457 -11.693  1.00 59.57           C  
ANISOU  216  CA  THR A  73     8198   7515   6923    826    890     44       C  
ATOM    217  C   THR A  73     -12.753 -22.569 -13.171  1.00 55.12           C  
ANISOU  217  C   THR A  73     7680   7047   6216    849   1017    -13       C  
ATOM    218  O   THR A  73     -12.307 -21.764 -13.989  1.00 64.17           O  
ANISOU  218  O   THR A  73     8816   8251   7313    843   1136     17       O  
ATOM    219  CB  THR A  73     -11.307 -23.484 -11.337  1.00 53.17           C  
ANISOU  219  CB  THR A  73     7279   6615   6309    858    871    -12       C  
ATOM    220  OG1 THR A  73     -10.986 -23.377  -9.946  1.00 44.98           O  
ANISOU  220  OG1 THR A  73     6212   5495   5386    840    734     46       O  
ATOM    221  CG2 THR A  73     -10.054 -23.232 -12.158  1.00 54.56           C  
ANISOU  221  CG2 THR A  73     7348   6801   6579    874   1013    -42       C  
ATOM    222  N   LEU A  74     -13.571 -23.566 -13.497  1.00 41.33           N  
ANISOU  222  N   LEU A  74     5988   5314   4401    874    989    -93       N  
ATOM    223  CA  LEU A  74     -14.010 -23.796 -14.870  1.00 53.12           C  
ANISOU  223  CA  LEU A  74     7536   6904   5744    901   1085   -168       C  
ATOM    224  C   LEU A  74     -14.727 -22.575 -15.448  1.00 63.04           C  
ANISOU  224  C   LEU A  74     8883   8253   6815    879   1114    -91       C  
ATOM    225  O   LEU A  74     -14.440 -22.150 -16.567  1.00 65.24           O  
ANISOU  225  O   LEU A  74     9183   8616   6989    891   1235    -91       O  
ATOM    226  CB  LEU A  74     -14.924 -25.022 -14.936  1.00 47.23           C  
ANISOU  226  CB  LEU A  74     6830   6141   4973    926   1015   -270       C  
ATOM    227  CG  LEU A  74     -14.275 -26.366 -14.600  1.00 42.64           C  
ANISOU  227  CG  LEU A  74     6164   5464   4574    957    994   -358       C  
ATOM    228  CD1 LEU A  74     -15.294 -27.494 -14.670  1.00 35.80           C  
ANISOU  228  CD1 LEU A  74     5339   4572   3690    974    925   -451       C  
ATOM    229  CD2 LEU A  74     -13.106 -26.639 -15.535  1.00 37.14           C  
ANISOU  229  CD2 LEU A  74     5386   4792   3933    993   1135   -439       C  
ATOM    230  N   VAL A  75     -15.652 -22.016 -14.672  1.00 53.49           N  
ANISOU  230  N   VAL A  75     7728   7027   5571    848   1006    -23       N  
ATOM    231  CA  VAL A  75     -16.406 -20.836 -15.084  1.00 47.85           C  
ANISOU  231  CA  VAL A  75     7091   6379   4711    828   1008     55       C  
ATOM    232  C   VAL A  75     -15.485 -19.634 -15.263  1.00 49.27           C  
ANISOU  232  C   VAL A  75     7232   6570   4921    806   1097    155       C  
ATOM    233  O   VAL A  75     -15.703 -18.794 -16.137  1.00 65.26           O  
ANISOU  233  O   VAL A  75     9312   8666   6820    803   1162    212       O  
ATOM    234  CB  VAL A  75     -17.502 -20.478 -14.056  1.00 43.63           C  
ANISOU  234  CB  VAL A  75     6598   5805   4173    796    877     97       C  
ATOM    235  CG1 VAL A  75     -18.327 -19.291 -14.541  1.00 33.33           C  
ANISOU  235  CG1 VAL A  75     5365   4561   2739    782    872    167       C  
ATOM    236  CG2 VAL A  75     -18.389 -21.678 -13.786  1.00 33.11           C  
ANISOU  236  CG2 VAL A  75     5292   4447   2840    809    798      7       C  
ATOM    237  N   ILE A  76     -14.456 -19.553 -14.427  1.00 36.67           N  
ANISOU  237  N   ILE A  76     5538   4896   3498    789   1094    179       N  
ATOM    238  CA  ILE A  76     -13.521 -18.437 -14.493  1.00 45.91           C  
ANISOU  238  CA  ILE A  76     6649   6055   4739    763   1174    266       C  
ATOM    239  C   ILE A  76     -12.587 -18.583 -15.688  1.00 52.03           C  
ANISOU  239  C   ILE A  76     7388   6882   5501    784   1346    241       C  
ATOM    240  O   ILE A  76     -12.382 -17.632 -16.439  1.00 58.90           O  
ANISOU  240  O   ILE A  76     8278   7800   6302    768   1451    319       O  
ATOM    241  CB  ILE A  76     -12.701 -18.311 -13.194  1.00 46.98           C  
ANISOU  241  CB  ILE A  76     6685   6089   5076    741   1100    286       C  
ATOM    242  CG1 ILE A  76     -13.555 -17.664 -12.103  1.00 41.76           C  
ANISOU  242  CG1 ILE A  76     6069   5397   4402    707    964    338       C  
ATOM    243  CG2 ILE A  76     -11.446 -17.487 -13.426  1.00 54.63           C  
ANISOU  243  CG2 ILE A  76     7555   7034   6166    723   1207    339       C  
ATOM    244  CD1 ILE A  76     -12.907 -17.664 -10.736  1.00 42.09           C  
ANISOU  244  CD1 ILE A  76     6036   5350   4608    690    864    344       C  
ATOM    245  N   LEU A  77     -12.031 -19.778 -15.862  1.00 53.77           N  
ANISOU  245  N   LEU A  77     7554   7087   5790    818   1380    133       N  
ATOM    246  CA  LEU A  77     -11.171 -20.071 -17.006  1.00 51.64           C  
ANISOU  246  CA  LEU A  77     7245   6870   5507    841   1556     80       C  
ATOM    247  C   LEU A  77     -11.891 -19.822 -18.327  1.00 64.70           C  
ANISOU  247  C   LEU A  77     9022   8652   6910    855   1641     84       C  
ATOM    248  O   LEU A  77     -11.312 -19.269 -19.266  1.00 39.86           O  
ANISOU  248  O   LEU A  77     5879   5569   3698    849   1801    124       O  
ATOM    249  CB  LEU A  77     -10.680 -21.520 -16.952  1.00 43.38           C  
ANISOU  249  CB  LEU A  77     6126   5781   4575    883   1555    -60       C  
ATOM    250  CG  LEU A  77      -9.598 -21.848 -15.925  1.00 48.31           C  
ANISOU  250  CG  LEU A  77     6607   6283   5464    881   1506    -71       C  
ATOM    251  CD1 LEU A  77      -9.273 -23.335 -15.944  1.00 49.74           C  
ANISOU  251  CD1 LEU A  77     6728   6416   5754    928   1493   -208       C  
ATOM    252  CD2 LEU A  77      -8.351 -21.023 -16.198  1.00 44.38           C  
ANISOU  252  CD2 LEU A  77     6005   5773   5084    859   1645    -22       C  
ATOM    253  N   ALA A  78     -13.156 -20.234 -18.386  1.00 52.51           N  
ANISOU  253  N   ALA A  78     7580   7144   5228    872   1532     45       N  
ATOM    254  CA  ALA A  78     -13.967 -20.093 -19.590  1.00 51.88           C  
ANISOU  254  CA  ALA A  78     7625   7185   4904    893   1572     35       C  
ATOM    255  C   ALA A  78     -14.053 -18.638 -20.037  1.00 60.56           C  
ANISOU  255  C   ALA A  78     8782   8331   5896    863   1627    189       C  
ATOM    256  O   ALA A  78     -13.645 -18.298 -21.147  1.00 61.25           O  
ANISOU  256  O   ALA A  78     8910   8505   5858    869   1774    218       O  
ATOM    257  CB  ALA A  78     -15.358 -20.658 -19.356  1.00 45.37           C  
ANISOU  257  CB  ALA A  78     6878   6364   3997    910   1416    -25       C  
ATOM    258  N   VAL A  79     -14.576 -17.781 -19.165  1.00 58.72           N  
ANISOU  258  N   VAL A  79     8555   8039   5717    829   1515    289       N  
ATOM    259  CA  VAL A  79     -14.687 -16.357 -19.462  1.00 53.89           C  
ANISOU  259  CA  VAL A  79     7986   7446   5043    799   1548    441       C  
ATOM    260  C   VAL A  79     -13.308 -15.735 -19.695  1.00 58.28           C  
ANISOU  260  C   VAL A  79     8457   7982   5706    771   1713    514       C  
ATOM    261  O   VAL A  79     -13.166 -14.788 -20.467  1.00 57.55           O  
ANISOU  261  O   VAL A  79     8411   7934   5522    754   1813    628       O  
ATOM    262  CB  VAL A  79     -15.408 -15.605 -18.325  1.00 48.73           C  
ANISOU  262  CB  VAL A  79     7329   6713   4475    767   1396    509       C  
ATOM    263  CG1 VAL A  79     -15.650 -14.154 -18.710  1.00 41.05           C  
ANISOU  263  CG1 VAL A  79     6404   5752   3443    741   1418    660       C  
ATOM    264  CG2 VAL A  79     -16.727 -16.285 -17.994  1.00 49.51           C  
ANISOU  264  CG2 VAL A  79     7491   6819   4502    788   1246    428       C  
ATOM    265  N   SER A  80     -12.291 -16.288 -19.040  1.00 63.60           N  
ANISOU  265  N   SER A  80     9003   8582   6582    766   1740    450       N  
ATOM    266  CA  SER A  80     -10.935 -15.757 -19.135  1.00 61.58           C  
ANISOU  266  CA  SER A  80     8636   8286   6476    738   1888    502       C  
ATOM    267  C   SER A  80     -10.336 -15.901 -20.532  1.00 68.79           C  
ANISOU  267  C   SER A  80     9574   9297   7267    751   2101    491       C  
ATOM    268  O   SER A  80      -9.999 -14.906 -21.173  1.00 74.37           O  
ANISOU  268  O   SER A  80    10301  10033   7924    722   2229    613       O  
ATOM    269  CB  SER A  80     -10.019 -16.444 -18.118  1.00 61.16           C  
ANISOU  269  CB  SER A  80     8436   8130   6674    739   1846    418       C  
ATOM    270  OG  SER A  80     -10.372 -16.100 -16.789  1.00 62.18           O  
ANISOU  270  OG  SER A  80     8538   8169   6918    717   1672    449       O  
ATOM    271  N   LEU A  81     -10.206 -17.137 -21.004  1.00 73.43           N  
ANISOU  271  N   LEU A  81    10160   9933   7806    795   2145    345       N  
ATOM    272  CA  LEU A  81      -9.444 -17.391 -22.223  1.00 69.74           C  
ANISOU  272  CA  LEU A  81     9692   9553   7253    808   2365    304       C  
ATOM    273  C   LEU A  81     -10.307 -17.641 -23.464  1.00 73.07           C  
ANISOU  273  C   LEU A  81    10281  10124   7359    842   2402    275       C  
ATOM    274  O   LEU A  81      -9.906 -17.289 -24.572  1.00 82.28           O  
ANISOU  274  O   LEU A  81    11500  11387   8377    838   2586    317       O  
ATOM    275  CB  LEU A  81      -8.483 -18.567 -22.003  1.00 65.34           C  
ANISOU  275  CB  LEU A  81     8996   8945   6884    834   2420    145       C  
ATOM    276  CG  LEU A  81      -9.014 -19.949 -21.617  1.00 67.60           C  
ANISOU  276  CG  LEU A  81     9283   9210   7191    883   2282    -16       C  
ATOM    277  CD1 LEU A  81      -9.196 -20.826 -22.849  1.00 75.00           C  
ANISOU  277  CD1 LEU A  81    10291  10266   7938    929   2389   -151       C  
ATOM    278  CD2 LEU A  81      -8.076 -20.611 -20.619  1.00 67.33           C  
ANISOU  278  CD2 LEU A  81     9079   9044   7462    888   2237    -89       C  
ATOM    279  N   GLU A  82     -11.480 -18.244 -23.291  1.00 76.14           N  
ANISOU  279  N   GLU A  82    10754  10534   7642    876   2229    203       N  
ATOM    280  CA  GLU A  82     -12.387 -18.439 -24.421  1.00 78.93           C  
ANISOU  280  CA  GLU A  82    11266  11024   7699    911   2229    169       C  
ATOM    281  C   GLU A  82     -12.913 -17.088 -24.893  1.00 89.83           C  
ANISOU  281  C   GLU A  82    12763  12457   8913    886   2231    358       C  
ATOM    282  O   GLU A  82     -13.812 -16.512 -24.283  1.00 90.46           O  
ANISOU  282  O   GLU A  82    12880  12489   9003    874   2065    437       O  
ATOM    283  CB  GLU A  82     -13.546 -19.367 -24.051  1.00 79.54           C  
ANISOU  283  CB  GLU A  82    11388  11092   7740    949   2032     47       C  
ATOM    284  CG  GLU A  82     -13.137 -20.806 -23.773  1.00 84.29           C  
ANISOU  284  CG  GLU A  82    11896  11650   8482    981   2030   -144       C  
ATOM    285  CD  GLU A  82     -12.477 -21.472 -24.966  1.00 93.80           C  
ANISOU  285  CD  GLU A  82    13106  12955   9577   1015   2213   -269       C  
ATOM    286  OE1 GLU A  82     -12.873 -21.174 -26.113  1.00102.08           O  
ANISOU  286  OE1 GLU A  82    14287  14140  10358   1032   2278   -256       O  
ATOM    287  OE2 GLU A  82     -11.562 -22.298 -24.758  1.00 91.36           O  
ANISOU  287  OE2 GLU A  82    12674  12590   9450   1028   2288   -385       O  
ATOM    288  N   LYS A  83     -12.342 -16.597 -25.989  1.00111.00           N  
ANISOU  288  N   LYS A  83    15499  15232  11445    878   2424    430       N  
ATOM    289  CA  LYS A  83     -12.599 -15.243 -26.476  1.00100.20           C  
ANISOU  289  CA  LYS A  83    14209  13889   9973    834   2429    628       C  
ATOM    290  C   LYS A  83     -14.051 -14.999 -26.882  1.00 94.33           C  
ANISOU  290  C   LYS A  83    13593  13198   9049    840   2218    651       C  
ATOM    291  O   LYS A  83     -14.505 -13.857 -26.917  1.00 97.17           O  
ANISOU  291  O   LYS A  83    14002  13535   9385    809   2153    814       O  
ATOM    292  CB  LYS A  83     -11.681 -14.932 -27.662  1.00109.13           C  
ANISOU  292  CB  LYS A  83    15338  15102  11026    790   2628    668       C  
ATOM    293  N   LYS A  84     -14.778 -16.068 -27.186  1.00109.77           N  
ANISOU  293  N   LYS A  84    15593  15214  10899    881   2112    484       N  
ATOM    294  CA  LYS A  84     -16.165 -15.937 -27.616  1.00 48.19           C  
ANISOU  294  CA  LYS A  84     7901   7463   2947    891   1914    486       C  
ATOM    295  C   LYS A  84     -17.122 -15.737 -26.442  1.00 75.00           C  
ANISOU  295  C   LYS A  84    11290  10759   6448    909   1732    510       C  
ATOM    296  O   LYS A  84     -18.305 -15.462 -26.644  1.00 69.17           O  
ANISOU  296  O   LYS A  84    10623  10037   5622    916   1564    529       O  
ATOM    297  CB  LYS A  84     -16.587 -17.162 -28.427  1.00 49.15           C  
ANISOU  297  CB  LYS A  84     8064   7684   2928    925   1874    288       C  
ATOM    298  N   LEU A  85     -16.614 -15.875 -25.220  1.00 68.73           N  
ANISOU  298  N   LEU A  85    10409   9863   5841    917   1767    508       N  
ATOM    299  CA  LEU A  85     -17.446 -15.732 -24.027  1.00 67.12           C  
ANISOU  299  CA  LEU A  85    10173   9558   5773    912   1587    514       C  
ATOM    300  C   LEU A  85     -17.263 -14.386 -23.329  1.00 62.24           C  
ANISOU  300  C   LEU A  85     9510   8847   5292    861   1575    688       C  
ATOM    301  O   LEU A  85     -17.852 -14.143 -22.277  1.00 53.33           O  
ANISOU  301  O   LEU A  85     8338   7628   4299    843   1435    694       O  
ATOM    302  CB  LEU A  85     -17.152 -16.860 -23.034  1.00 62.22           C  
ANISOU  302  CB  LEU A  85     9435   8855   5351    912   1547    365       C  
ATOM    303  CG  LEU A  85     -17.820 -18.214 -23.278  1.00 58.92           C  
ANISOU  303  CG  LEU A  85     9045   8477   4864    959   1469    180       C  
ATOM    304  CD1 LEU A  85     -17.309 -19.246 -22.287  1.00 61.44           C  
ANISOU  304  CD1 LEU A  85     9241   8698   5406    954   1452     67       C  
ATOM    305  CD2 LEU A  85     -19.333 -18.091 -23.183  1.00 40.02           C  
ANISOU  305  CD2 LEU A  85     6730   6088   2389    974   1284    173       C  
ATOM    306  N   GLN A  86     -16.453 -13.511 -23.913  1.00 66.46           N  
ANISOU  306  N   GLN A  86    10053   9402   5797    836   1727    824       N  
ATOM    307  CA  GLN A  86     -16.105 -12.255 -23.259  1.00 58.76           C  
ANISOU  307  CA  GLN A  86     9014   8324   4988    784   1733    979       C  
ATOM    308  C   GLN A  86     -17.046 -11.102 -23.612  1.00 55.84           C  
ANISOU  308  C   GLN A  86     8745   7958   4512    783   1643   1131       C  
ATOM    309  O   GLN A  86     -16.835 -10.386 -24.589  1.00 64.70           O  
ANISOU  309  O   GLN A  86     9931   9130   5521    768   1728   1256       O  
ATOM    310  CB  GLN A  86     -14.662 -11.879 -23.596  1.00 58.02           C  
ANISOU  310  CB  GLN A  86     8850   8221   4973    749   1950   1052       C  
ATOM    311  CG  GLN A  86     -13.641 -12.679 -22.807  1.00 60.38           C  
ANISOU  311  CG  GLN A  86     8997   8454   5491    737   2003    930       C  
ATOM    312  CD  GLN A  86     -12.355 -12.907 -23.570  1.00 71.54           C  
ANISOU  312  CD  GLN A  86    10363   9912   6907    729   2236    921       C  
ATOM    313  OE1 GLN A  86     -12.206 -12.461 -24.707  1.00 79.65           O  
ANISOU  313  OE1 GLN A  86    11480  11030   7755    727   2376   1012       O  
ATOM    314  NE2 GLN A  86     -11.413 -13.605 -22.945  1.00 75.04           N  
ANISOU  314  NE2 GLN A  86    10664  10291   7557    724   2281    813       N  
ATOM    315  N   TYR A  87     -18.084 -10.935 -22.801  1.00 56.45           N  
ANISOU  315  N   TYR A  87     8817   7972   4661    786   1456   1107       N  
ATOM    316  CA  TYR A  87     -18.979  -9.791 -22.911  1.00 57.11           C  
ANISOU  316  CA  TYR A  87     8962   8026   4710    783   1350   1240       C  
ATOM    317  C   TYR A  87     -19.557  -9.437 -21.539  1.00 67.44           C  
ANISOU  317  C   TYR A  87    10184   9212   6227    760   1203   1212       C  
ATOM    318  O   TYR A  87     -19.219 -10.063 -20.535  1.00 71.90           O  
ANISOU  318  O   TYR A  87    10654   9725   6941    743   1188   1103       O  
ATOM    319  CB  TYR A  87     -20.097 -10.061 -23.924  1.00 55.62           C  
ANISOU  319  CB  TYR A  87     8901   7938   4295    828   1243   1212       C  
ATOM    320  CG  TYR A  87     -20.775 -11.406 -23.786  1.00 70.09           C  
ANISOU  320  CG  TYR A  87    10743   9816   6070    869   1148   1015       C  
ATOM    321  CD1 TYR A  87     -21.883 -11.568 -22.964  1.00 79.80           C  
ANISOU  321  CD1 TYR A  87    11962  10991   7369    886    980    947       C  
ATOM    322  CD2 TYR A  87     -20.319 -12.511 -24.495  1.00 78.23           C  
ANISOU  322  CD2 TYR A  87    11783  10937   7003    883   1225    888       C  
ATOM    323  CE1 TYR A  87     -22.510 -12.795 -22.841  1.00 82.42           C  
ANISOU  323  CE1 TYR A  87    12294  11352   7670    917    899    771       C  
ATOM    324  CE2 TYR A  87     -20.940 -13.743 -24.379  1.00 76.06           C  
ANISOU  324  CE2 TYR A  87    11512  10692   6696    921   1139    708       C  
ATOM    325  CZ  TYR A  87     -22.035 -13.879 -23.551  1.00 82.62           C  
ANISOU  325  CZ  TYR A  87    12340  11464   7588    940    979    657       C  
ATOM    326  OH  TYR A  87     -22.657 -15.103 -23.431  1.00 88.49           O  
ANISOU  326  OH  TYR A  87    13082  12226   8314    974    899    482       O  
ATOM    327  N   ALA A  88     -20.427  -8.432 -21.509  1.00 68.65           N  
ANISOU  327  N   ALA A  88    10374   9322   6388    759   1094   1309       N  
ATOM    328  CA  ALA A  88     -20.870  -7.812 -20.262  1.00 61.43           C  
ANISOU  328  CA  ALA A  88     9374   8287   5679    729    983   1302       C  
ATOM    329  C   ALA A  88     -21.519  -8.786 -19.283  1.00 62.64           C  
ANISOU  329  C   ALA A  88     9485   8424   5892    737    873   1129       C  
ATOM    330  O   ALA A  88     -21.230  -8.751 -18.085  1.00 71.60           O  
ANISOU  330  O   ALA A  88    10524   9477   7204    703    853   1082       O  
ATOM    331  CB  ALA A  88     -21.828  -6.675 -20.566  1.00 72.47           C  
ANISOU  331  CB  ALA A  88    10826   9649   7060    739    879   1420       C  
ATOM    332  N   THR A  89     -22.395  -9.644 -19.796  1.00 65.29           N  
ANISOU  332  N   THR A  89     9893   8835   6078    781    801   1037       N  
ATOM    333  CA  THR A  89     -23.132 -10.591 -18.963  1.00 66.39           C  
ANISOU  333  CA  THR A  89     9999   8956   6271    787    700    882       C  
ATOM    334  C   THR A  89     -22.201 -11.478 -18.138  1.00 68.49           C  
ANISOU  334  C   THR A  89    10182   9195   6645    764    768    793       C  
ATOM    335  O   THR A  89     -22.420 -11.681 -16.943  1.00 74.15           O  
ANISOU  335  O   THR A  89    10835   9843   7494    739    707    730       O  
ATOM    336  CB  THR A  89     -24.056 -11.482 -19.823  1.00 73.23           C  
ANISOU  336  CB  THR A  89    10950   9910   6962    840    630    790       C  
ATOM    337  OG1 THR A  89     -25.208 -10.729 -20.222  1.00 73.68           O  
ANISOU  337  OG1 THR A  89    11063   9965   6968    862    508    843       O  
ATOM    338  CG2 THR A  89     -24.512 -12.706 -19.043  1.00 80.02           C  
ANISOU  338  CG2 THR A  89    11766  10752   7888    840    572    625       C  
ATOM    339  N   ASN A  90     -21.147 -11.976 -18.774  1.00 61.75           N  
ANISOU  339  N   ASN A  90     9331   8395   5736    772    897    792       N  
ATOM    340  CA  ASN A  90     -20.257 -12.945 -18.145  1.00 56.19           C  
ANISOU  340  CA  ASN A  90     8550   7667   5132    762    953    700       C  
ATOM    341  C   ASN A  90     -19.284 -12.339 -17.140  1.00 52.93           C  
ANISOU  341  C   ASN A  90     8033   7163   4913    715    991    752       C  
ATOM    342  O   ASN A  90     -18.886 -13.006 -16.186  1.00 62.81           O  
ANISOU  342  O   ASN A  90     9216   8367   6283    703    970    676       O  
ATOM    343  CB  ASN A  90     -19.478 -13.700 -19.218  1.00 60.51           C  
ANISOU  343  CB  ASN A  90     9124   8300   5565    791   1081    662       C  
ATOM    344  CG  ASN A  90     -20.387 -14.417 -20.190  1.00 58.20           C  
ANISOU  344  CG  ASN A  90     8931   8103   5078    840   1034    583       C  
ATOM    345  OD1 ASN A  90     -21.535 -14.726 -19.872  1.00 59.00           O  
ANISOU  345  OD1 ASN A  90     9056   8192   5170    853    901    518       O  
ATOM    346  ND2 ASN A  90     -19.882 -14.679 -21.386  1.00 37.85           N  
ANISOU  346  ND2 ASN A  90     6411   5622   2348    867   1147    580       N  
ATOM    347  N   TYR A  91     -18.897 -11.086 -17.358  1.00 52.25           N  
ANISOU  347  N   TYR A  91     7937   7050   4866    691   1041    882       N  
ATOM    348  CA  TYR A  91     -18.010 -10.390 -16.428  1.00 56.37           C  
ANISOU  348  CA  TYR A  91     8354   7478   5587    647   1065    926       C  
ATOM    349  C   TYR A  91     -18.660 -10.289 -15.057  1.00 52.07           C  
ANISOU  349  C   TYR A  91     7770   6861   5154    626    928    869       C  
ATOM    350  O   TYR A  91     -17.998 -10.420 -14.029  1.00 56.37           O  
ANISOU  350  O   TYR A  91     8233   7346   5841    602    914    830       O  
ATOM    351  CB  TYR A  91     -17.656  -8.996 -16.948  1.00 61.04           C  
ANISOU  351  CB  TYR A  91     8942   8041   6209    622   1133   1080       C  
ATOM    352  CG  TYR A  91     -16.807  -9.013 -18.195  1.00 71.92           C  
ANISOU  352  CG  TYR A  91    10349   9484   7493    630   1299   1151       C  
ATOM    353  CD1 TYR A  91     -15.768  -9.923 -18.338  1.00 72.67           C  
ANISOU  353  CD1 TYR A  91    10392   9608   7612    635   1409   1079       C  
ATOM    354  CD2 TYR A  91     -17.044  -8.121 -19.232  1.00 81.14           C  
ANISOU  354  CD2 TYR A  91    11596  10685   8548    632   1350   1292       C  
ATOM    355  CE1 TYR A  91     -14.986  -9.943 -19.479  1.00 76.54           C  
ANISOU  355  CE1 TYR A  91    10905  10163   8014    640   1581   1133       C  
ATOM    356  CE2 TYR A  91     -16.269  -8.133 -20.376  1.00 87.20           C  
ANISOU  356  CE2 TYR A  91    12401  11521   9209    635   1519   1363       C  
ATOM    357  CZ  TYR A  91     -15.242  -9.045 -20.495  1.00 86.75           C  
ANISOU  357  CZ  TYR A  91    12287  11498   9175    637   1642   1276       C  
ATOM    358  OH  TYR A  91     -14.470  -9.057 -21.635  1.00 99.03           O  
ANISOU  358  OH  TYR A  91    13877  13127  10624    638   1829   1336       O  
ATOM    359  N   PHE A  92     -19.967 -10.056 -15.055  1.00 50.95           N  
ANISOU  359  N   PHE A  92     7688   6727   4943    638    827    861       N  
ATOM    360  CA  PHE A  92     -20.738 -10.073 -13.825  1.00 54.21           C  
ANISOU  360  CA  PHE A  92     8076   7087   5436    620    712    791       C  
ATOM    361  C   PHE A  92     -20.821 -11.502 -13.305  1.00 58.07           C  
ANISOU  361  C   PHE A  92     8563   7594   5906    631    685    671       C  
ATOM    362  O   PHE A  92     -20.699 -11.749 -12.103  1.00 61.14           O  
ANISOU  362  O   PHE A  92     8905   7934   6391    606    639    620       O  
ATOM    363  CB  PHE A  92     -22.136  -9.499 -14.055  1.00 61.53           C  
ANISOU  363  CB  PHE A  92     9057   8015   6308    632    621    805       C  
ATOM    364  CG  PHE A  92     -22.904  -9.263 -12.791  1.00 66.90           C  
ANISOU  364  CG  PHE A  92     9700   8633   7087    606    525    741       C  
ATOM    365  CD1 PHE A  92     -22.639  -8.156 -12.006  1.00 66.49           C  
ANISOU  365  CD1 PHE A  92     9585   8504   7173    571    510    778       C  
ATOM    366  CD2 PHE A  92     -23.891 -10.145 -12.387  1.00 68.89           C  
ANISOU  366  CD2 PHE A  92     9976   8902   7298    615    458    637       C  
ATOM    367  CE1 PHE A  92     -23.341  -7.934 -10.839  1.00 64.38           C  
ANISOU  367  CE1 PHE A  92     9288   8189   6984    547    433    706       C  
ATOM    368  CE2 PHE A  92     -24.597  -9.925 -11.222  1.00 68.17           C  
ANISOU  368  CE2 PHE A  92     9853   8760   7289    587    391    578       C  
ATOM    369  CZ  PHE A  92     -24.320  -8.819 -10.448  1.00 62.78           C  
ANISOU  369  CZ  PHE A  92     9116   8012   6726    554    380    609       C  
ATOM    370  N   LEU A  93     -21.021 -12.439 -14.228  1.00 51.13           N  
ANISOU  370  N   LEU A  93     7739   6787   4902    668    713    627       N  
ATOM    371  CA  LEU A  93     -21.109 -13.852 -13.890  1.00 45.59           C  
ANISOU  371  CA  LEU A  93     7036   6096   4192    682    692    516       C  
ATOM    372  C   LEU A  93     -19.781 -14.365 -13.342  1.00 41.61           C  
ANISOU  372  C   LEU A  93     6458   5557   3795    671    748    500       C  
ATOM    373  O   LEU A  93     -19.753 -15.166 -12.406  1.00 41.06           O  
ANISOU  373  O   LEU A  93     6361   5448   3791    662    699    436       O  
ATOM    374  CB  LEU A  93     -21.531 -14.661 -15.115  1.00 50.06           C  
ANISOU  374  CB  LEU A  93     7669   6743   4609    727    713    464       C  
ATOM    375  CG  LEU A  93     -21.798 -16.153 -14.939  1.00 57.20           C  
ANISOU  375  CG  LEU A  93     8573   7652   5508    746    686    339       C  
ATOM    376  CD1 LEU A  93     -22.909 -16.377 -13.930  1.00 60.60           C  
ANISOU  376  CD1 LEU A  93     9002   8033   5992    725    579    291       C  
ATOM    377  CD2 LEU A  93     -22.164 -16.760 -16.280  1.00 63.34           C  
ANISOU  377  CD2 LEU A  93     9415   8515   6135    793    707    283       C  
ATOM    378  N   MET A  94     -18.683 -13.899 -13.931  1.00 38.44           N  
ANISOU  378  N   MET A  94     6023   5164   3417    670    851    562       N  
ATOM    379  CA  MET A  94     -17.351 -14.259 -13.459  1.00 40.84           C  
ANISOU  379  CA  MET A  94     6238   5426   3851    661    903    548       C  
ATOM    380  C   MET A  94     -17.137 -13.782 -12.028  1.00 44.64           C  
ANISOU  380  C   MET A  94     6660   5826   4477    624    821    558       C  
ATOM    381  O   MET A  94     -16.610 -14.519 -11.192  1.00 48.62           O  
ANISOU  381  O   MET A  94     7116   6289   5068    622    783    506       O  
ATOM    382  CB  MET A  94     -16.276 -13.667 -14.369  1.00 34.39           C  
ANISOU  382  CB  MET A  94     5388   4629   3049    659   1040    620       C  
ATOM    383  CG  MET A  94     -14.874 -13.814 -13.825  1.00 32.98           C  
ANISOU  383  CG  MET A  94     5095   4391   3045    645   1089    609       C  
ATOM    384  SD  MET A  94     -13.629 -13.197 -14.963  1.00 53.67           S  
ANISOU  384  SD  MET A  94     7664   7032   5694    639   1279    686       S  
ATOM    385  CE  MET A  94     -12.134 -13.815 -14.197  1.00125.30           C  
ANISOU  385  CE  MET A  94    16587  16027  14995    635   1302    621       C  
ATOM    386  N   SER A  95     -17.547 -12.543 -11.763  1.00 42.39           N  
ANISOU  386  N   SER A  95     6378   5516   4214    597    788    621       N  
ATOM    387  CA  SER A  95     -17.497 -11.965 -10.424  1.00 45.92           C  
ANISOU  387  CA  SER A  95     6777   5893   4777    562    704    616       C  
ATOM    388  C   SER A  95     -18.169 -12.877  -9.402  1.00 44.48           C  
ANISOU  388  C   SER A  95     6624   5704   4574    560    608    535       C  
ATOM    389  O   SER A  95     -17.682 -13.043  -8.284  1.00 45.17           O  
ANISOU  389  O   SER A  95     6670   5746   4747    543    553    509       O  
ATOM    390  CB  SER A  95     -18.165 -10.584 -10.417  1.00 50.07           C  
ANISOU  390  CB  SER A  95     7315   6396   5313    540    678    677       C  
ATOM    391  OG  SER A  95     -18.510 -10.175  -9.105  1.00 29.17           O  
ANISOU  391  OG  SER A  95     4645   3699   2740    511    584    638       O  
ATOM    392  N   LEU A  96     -19.290 -13.467  -9.799  1.00 38.20           N  
ANISOU  392  N   LEU A  96     5899   4950   3664    578    588    498       N  
ATOM    393  CA  LEU A  96     -19.997 -14.410  -8.948  1.00 30.42           C  
ANISOU  393  CA  LEU A  96     4945   3956   2659    573    517    429       C  
ATOM    394  C   LEU A  96     -19.163 -15.666  -8.736  1.00 29.26           C  
ANISOU  394  C   LEU A  96     4771   3794   2551    590    526    390       C  
ATOM    395  O   LEU A  96     -19.064 -16.172  -7.620  1.00 36.44           O  
ANISOU  395  O   LEU A  96     5673   4665   3506    574    464    367       O  
ATOM    396  CB  LEU A  96     -21.355 -14.766  -9.555  1.00 27.73           C  
ANISOU  396  CB  LEU A  96     4670   3655   2211    589    499    392       C  
ATOM    397  CG  LEU A  96     -22.113 -15.937  -8.928  1.00 27.25           C  
ANISOU  397  CG  LEU A  96     4638   3584   2134    586    450    319       C  
ATOM    398  CD1 LEU A  96     -22.406 -15.676  -7.463  1.00 26.72           C  
ANISOU  398  CD1 LEU A  96     4564   3473   2116    543    392    312       C  
ATOM    399  CD2 LEU A  96     -23.395 -16.191  -9.695  1.00 27.26           C  
ANISOU  399  CD2 LEU A  96     4687   3621   2051    604    434    276       C  
ATOM    400  N   ALA A  97     -18.560 -16.159  -9.815  1.00 31.04           N  
ANISOU  400  N   ALA A  97     4985   4051   2758    623    604    384       N  
ATOM    401  CA  ALA A  97     -17.716 -17.347  -9.752  1.00 31.80           C  
ANISOU  401  CA  ALA A  97     5043   4126   2913    645    619    340       C  
ATOM    402  C   ALA A  97     -16.520 -17.114  -8.832  1.00 43.43           C  
ANISOU  402  C   ALA A  97     6437   5538   4526    630    594    365       C  
ATOM    403  O   ALA A  97     -16.063 -18.028  -8.147  1.00 50.34           O  
ANISOU  403  O   ALA A  97     7287   6370   5471    638    545    335       O  
ATOM    404  CB  ALA A  97     -17.251 -17.740 -11.147  1.00 45.72           C  
ANISOU  404  CB  ALA A  97     6800   5939   4630    682    725    318       C  
ATOM    405  N   VAL A  98     -16.024 -15.881  -8.824  1.00 48.10           N  
ANISOU  405  N   VAL A  98     6987   6120   5168    609    618    421       N  
ATOM    406  CA  VAL A  98     -14.945 -15.485  -7.927  1.00 44.02           C  
ANISOU  406  CA  VAL A  98     6388   5542   4794    591    579    437       C  
ATOM    407  C   VAL A  98     -15.392 -15.553  -6.471  1.00 54.03           C  
ANISOU  407  C   VAL A  98     7684   6777   6069    568    452    420       C  
ATOM    408  O   VAL A  98     -14.698 -16.119  -5.625  1.00 57.62           O  
ANISOU  408  O   VAL A  98     8103   7188   6602    572    383    404       O  
ATOM    409  CB  VAL A  98     -14.455 -14.058  -8.232  1.00 46.35           C  
ANISOU  409  CB  VAL A  98     6631   5825   5153    568    631    497       C  
ATOM    410  CG1 VAL A  98     -13.519 -13.567  -7.136  1.00 47.12           C  
ANISOU  410  CG1 VAL A  98     6643   5853   5405    546    561    497       C  
ATOM    411  CG2 VAL A  98     -13.776 -14.007  -9.589  1.00 54.98           C  
ANISOU  411  CG2 VAL A  98     7691   6948   6250    586    773    525       C  
ATOM    412  N   ALA A  99     -16.555 -14.971  -6.190  1.00 55.37           N  
ANISOU  412  N   ALA A  99     7918   6969   6153    544    421    424       N  
ATOM    413  CA  ALA A  99     -17.101 -14.952  -4.838  1.00 45.12           C  
ANISOU  413  CA  ALA A  99     6656   5652   4835    516    321    404       C  
ATOM    414  C   ALA A  99     -17.303 -16.364  -4.306  1.00 46.84           C  
ANISOU  414  C   ALA A  99     6917   5861   5020    527    275    376       C  
ATOM    415  O   ALA A  99     -16.992 -16.650  -3.151  1.00 53.73           O  
ANISOU  415  O   ALA A  99     7794   6703   5918    515    192    374       O  
ATOM    416  CB  ALA A  99     -18.415 -14.180  -4.804  1.00 27.51           C  
ANISOU  416  CB  ALA A  99     4480   3447   2524    493    318    399       C  
ATOM    417  N   ASP A 100     -17.812 -17.248  -5.157  1.00 41.79           N  
ANISOU  417  N   ASP A 100     6308   5244   4325    552    324    356       N  
ATOM    418  CA  ASP A 100     -18.070 -18.625  -4.753  1.00 53.57           C  
ANISOU  418  CA  ASP A 100     7835   6715   5804    561    288    331       C  
ATOM    419  C   ASP A 100     -16.779 -19.431  -4.634  1.00 48.74           C  
ANISOU  419  C   ASP A 100     7163   6056   5301    590    268    333       C  
ATOM    420  O   ASP A 100     -16.680 -20.337  -3.807  1.00 37.25           O  
ANISOU  420  O   ASP A 100     5726   4558   3870    591    199    337       O  
ATOM    421  CB  ASP A 100     -19.033 -19.292  -5.734  1.00 54.13           C  
ANISOU  421  CB  ASP A 100     7947   6818   5803    579    340    293       C  
ATOM    422  CG  ASP A 100     -20.449 -18.772  -5.592  1.00 68.27           C  
ANISOU  422  CG  ASP A 100     9796   8637   7507    550    332    282       C  
ATOM    423  OD1 ASP A 100     -20.825 -18.383  -4.465  1.00 68.58           O  
ANISOU  423  OD1 ASP A 100     9859   8663   7536    514    283    294       O  
ATOM    424  OD2 ASP A 100     -21.186 -18.747  -6.599  1.00 74.01           O  
ANISOU  424  OD2 ASP A 100    10542   9401   8176    566    372    255       O  
ATOM    425  N   LEU A 101     -15.789 -19.095  -5.454  1.00 52.47           N  
ANISOU  425  N   LEU A 101     7561   6531   5846    613    331    333       N  
ATOM    426  CA  LEU A 101     -14.476 -19.724  -5.351  1.00 51.82           C  
ANISOU  426  CA  LEU A 101     7397   6395   5897    642    315    326       C  
ATOM    427  C   LEU A 101     -13.830 -19.367  -4.018  1.00 54.18           C  
ANISOU  427  C   LEU A 101     7670   6647   6271    624    201    354       C  
ATOM    428  O   LEU A 101     -13.216 -20.211  -3.365  1.00 62.41           O  
ANISOU  428  O   LEU A 101     8689   7634   7391    643    121    355       O  
ATOM    429  CB  LEU A 101     -13.571 -19.296  -6.508  1.00 50.13           C  
ANISOU  429  CB  LEU A 101     7101   6198   5750    662    427    318       C  
ATOM    430  CG  LEU A 101     -12.122 -19.789  -6.442  1.00 48.93           C  
ANISOU  430  CG  LEU A 101     6837   5984   5769    691    424    300       C  
ATOM    431  CD1 LEU A 101     -12.069 -21.309  -6.418  1.00 51.75           C  
ANISOU  431  CD1 LEU A 101     7195   6301   6165    727    393    256       C  
ATOM    432  CD2 LEU A 101     -11.302 -19.235  -7.599  1.00 41.30           C  
ANISOU  432  CD2 LEU A 101     5790   5040   4861    701    563    295       C  
ATOM    433  N   LEU A 102     -13.981 -18.108  -3.620  1.00 49.22           N  
ANISOU  433  N   LEU A 102     7044   6037   5621    591    184    374       N  
ATOM    434  CA  LEU A 102     -13.424 -17.623  -2.364  1.00 46.03           C  
ANISOU  434  CA  LEU A 102     6618   5598   5273    573     70    385       C  
ATOM    435  C   LEU A 102     -14.109 -18.268  -1.161  1.00 46.74           C  
ANISOU  435  C   LEU A 102     6804   5685   5271    558    -33    394       C  
ATOM    436  O   LEU A 102     -13.498 -18.425  -0.104  1.00 51.48           O  
ANISOU  436  O   LEU A 102     7399   6251   5911    558   -148    404       O  
ATOM    437  CB  LEU A 102     -13.535 -16.100  -2.290  1.00 48.59           C  
ANISOU  437  CB  LEU A 102     6922   5940   5600    540     85    391       C  
ATOM    438  CG  LEU A 102     -12.641 -15.341  -3.275  1.00 50.56           C  
ANISOU  438  CG  LEU A 102     7067   6176   5967    547    178    401       C  
ATOM    439  CD1 LEU A 102     -13.017 -13.867  -3.334  1.00 50.42           C  
ANISOU  439  CD1 LEU A 102     7044   6170   5944    512    204    417       C  
ATOM    440  CD2 LEU A 102     -11.171 -15.506  -2.912  1.00 48.97           C  
ANISOU  440  CD2 LEU A 102     6754   5911   5942    565    126    390       C  
ATOM    441  N   VAL A 103     -15.376 -18.642  -1.324  1.00 45.82           N  
ANISOU  441  N   VAL A 103     6775   5603   5031    543      8    391       N  
ATOM    442  CA  VAL A 103     -16.094 -19.375  -0.283  1.00 41.98           C  
ANISOU  442  CA  VAL A 103     6382   5112   4457    524    -60    407       C  
ATOM    443  C   VAL A 103     -15.402 -20.702   0.001  1.00 46.22           C  
ANISOU  443  C   VAL A 103     6909   5589   5064    556   -122    430       C  
ATOM    444  O   VAL A 103     -15.069 -21.012   1.142  1.00 54.23           O  
ANISOU  444  O   VAL A 103     7957   6575   6074    551   -232    464       O  
ATOM    445  CB  VAL A 103     -17.560 -19.657  -0.672  1.00 41.60           C  
ANISOU  445  CB  VAL A 103     6407   5100   4300    504     11    392       C  
ATOM    446  CG1 VAL A 103     -18.217 -20.558   0.360  1.00 40.32           C  
ANISOU  446  CG1 VAL A 103     6333   4921   4068    481    -40    416       C  
ATOM    447  CG2 VAL A 103     -18.337 -18.366  -0.815  1.00 40.62           C  
ANISOU  447  CG2 VAL A 103     6295   5024   4115    474     54    370       C  
ATOM    448  N   GLY A 104     -15.179 -21.479  -1.052  1.00 47.64           N  
ANISOU  448  N   GLY A 104     7043   5748   5310    592    -57    410       N  
ATOM    449  CA  GLY A 104     -14.575 -22.790  -0.918  1.00 45.61           C  
ANISOU  449  CA  GLY A 104     6764   5421   5146    627   -107    422       C  
ATOM    450  C   GLY A 104     -13.095 -22.754  -0.597  1.00 41.48           C  
ANISOU  450  C   GLY A 104     6147   4843   4770    658   -187    430       C  
ATOM    451  O   GLY A 104     -12.506 -23.781  -0.263  1.00 40.61           O  
ANISOU  451  O   GLY A 104     6015   4662   4753    689   -261    448       O  
ATOM    452  N   LEU A 105     -12.492 -21.573  -0.687  1.00 42.99           N  
ANISOU  452  N   LEU A 105     6276   5059   5001    650   -177    416       N  
ATOM    453  CA  LEU A 105     -11.046 -21.447  -0.532  1.00 49.62           C  
ANISOU  453  CA  LEU A 105     6999   5842   6011    679   -239    409       C  
ATOM    454  C   LEU A 105     -10.625 -20.930   0.846  1.00 51.58           C  
ANISOU  454  C   LEU A 105     7264   6074   6260    664   -396    435       C  
ATOM    455  O   LEU A 105      -9.572 -21.307   1.359  1.00 55.75           O  
ANISOU  455  O   LEU A 105     7727   6537   6917    695   -509    441       O  
ATOM    456  CB  LEU A 105     -10.485 -20.530  -1.622  1.00 47.47           C  
ANISOU  456  CB  LEU A 105     6626   5592   5820    682   -118    372       C  
ATOM    457  CG  LEU A 105      -9.191 -20.988  -2.299  1.00 56.67           C  
ANISOU  457  CG  LEU A 105     7652   6700   7182    726    -80    339       C  
ATOM    458  CD1 LEU A 105      -9.260 -22.469  -2.647  1.00 60.24           C  
ANISOU  458  CD1 LEU A 105     8111   7112   7664    765    -72    321       C  
ATOM    459  CD2 LEU A 105      -8.909 -20.161  -3.549  1.00 51.57           C  
ANISOU  459  CD2 LEU A 105     6934   6092   6569    719     85    314       C  
ATOM    460  N   PHE A 106     -11.443 -20.070   1.444  1.00 48.91           N  
ANISOU  460  N   PHE A 106     7009   5794   5780    619   -407    441       N  
ATOM    461  CA  PHE A 106     -11.079 -19.447   2.713  1.00 52.06           C  
ANISOU  461  CA  PHE A 106     7427   6193   6161    603   -549    446       C  
ATOM    462  C   PHE A 106     -12.134 -19.650   3.793  1.00 59.32           C  
ANISOU  462  C   PHE A 106     8499   7155   6886    569   -606    478       C  
ATOM    463  O   PHE A 106     -11.805 -19.752   4.978  1.00 65.26           O  
ANISOU  463  O   PHE A 106     9299   7899   7600    568   -749    500       O  
ATOM    464  CB  PHE A 106     -10.825 -17.953   2.515  1.00 49.74           C  
ANISOU  464  CB  PHE A 106     7063   5922   5912    579   -514    403       C  
ATOM    465  CG  PHE A 106      -9.681 -17.654   1.594  1.00 59.21           C  
ANISOU  465  CG  PHE A 106     8108   7075   7312    605   -457    379       C  
ATOM    466  CD1 PHE A 106      -8.372 -17.823   2.017  1.00 64.49           C  
ANISOU  466  CD1 PHE A 106     8674   7676   8152    636   -569    366       C  
ATOM    467  CD2 PHE A 106      -9.912 -17.207   0.304  1.00 56.49           C  
ANISOU  467  CD2 PHE A 106     7722   6755   6985    599   -289    371       C  
ATOM    468  CE1 PHE A 106      -7.314 -17.551   1.170  1.00 63.68           C  
ANISOU  468  CE1 PHE A 106     8418   7527   8250    655   -499    338       C  
ATOM    469  CE2 PHE A 106      -8.858 -16.932  -0.546  1.00 54.11           C  
ANISOU  469  CE2 PHE A 106     7284   6416   6860    617   -215    354       C  
ATOM    470  CZ  PHE A 106      -7.559 -17.104  -0.113  1.00 58.30           C  
ANISOU  470  CZ  PHE A 106     7701   6875   7575    643   -312    335       C  
ATOM    471  N   VAL A 107     -13.398 -19.705   3.387  1.00 45.82           N  
ANISOU  471  N   VAL A 107     6864   5492   5054    540   -493    478       N  
ATOM    472  CA  VAL A 107     -14.481 -19.899   4.340  1.00 46.05           C  
ANISOU  472  CA  VAL A 107     7029   5561   4907    501   -515    504       C  
ATOM    473  C   VAL A 107     -14.671 -21.378   4.669  1.00 57.29           C  
ANISOU  473  C   VAL A 107     8521   6941   6304    513   -551    569       C  
ATOM    474  O   VAL A 107     -14.587 -21.781   5.829  1.00 65.98           O  
ANISOU  474  O   VAL A 107     9703   8035   7331    505   -661    621       O  
ATOM    475  CB  VAL A 107     -15.809 -19.333   3.813  1.00 43.84           C  
ANISOU  475  CB  VAL A 107     6790   5339   4530    463   -383    471       C  
ATOM    476  CG1 VAL A 107     -16.929 -19.596   4.809  1.00 35.48           C  
ANISOU  476  CG1 VAL A 107     5860   4316   3304    419   -388    490       C  
ATOM    477  CG2 VAL A 107     -15.677 -17.847   3.516  1.00 39.74           C  
ANISOU  477  CG2 VAL A 107     6206   4850   4045    450   -352    417       C  
ATOM    478  N   MET A 108     -14.920 -22.181   3.639  1.00 57.22           N  
ANISOU  478  N   MET A 108     8481   6903   6357    534   -461    568       N  
ATOM    479  CA  MET A 108     -15.229 -23.600   3.816  1.00 59.11           C  
ANISOU  479  CA  MET A 108     8776   7089   6596    543   -477    623       C  
ATOM    480  C   MET A 108     -14.138 -24.445   4.498  1.00 60.23           C  
ANISOU  480  C   MET A 108     8904   7151   6831    582   -624    684       C  
ATOM    481  O   MET A 108     -14.459 -25.258   5.366  1.00 59.33           O  
ANISOU  481  O   MET A 108     8887   7008   6650    570   -689    761       O  
ATOM    482  CB  MET A 108     -15.586 -24.223   2.461  1.00 31.80           C  
ANISOU  482  CB  MET A 108     5263   3609   3209    564   -358    583       C  
ATOM    483  CG  MET A 108     -16.870 -23.669   1.867  1.00 43.86           C  
ANISOU  483  CG  MET A 108     6826   5204   4634    528   -235    538       C  
ATOM    484  SD  MET A 108     -17.369 -24.476   0.338  1.00 40.96           S  
ANISOU  484  SD  MET A 108     6414   4820   4328    556   -119    482       S  
ATOM    485  CE  MET A 108     -17.335 -26.171   0.862  1.00 74.49           C  
ANISOU  485  CE  MET A 108    10695   8968   8640    569   -179    538       C  
ATOM    486  N   PRO A 109     -12.855 -24.274   4.117  1.00 53.88           N  
ANISOU  486  N   PRO A 109     7978   6306   6189    628   -676    654       N  
ATOM    487  CA  PRO A 109     -11.866 -25.140   4.777  1.00 52.20           C  
ANISOU  487  CA  PRO A 109     7747   6006   6081    670   -830    711       C  
ATOM    488  C   PRO A 109     -11.712 -24.876   6.281  1.00 46.53           C  
ANISOU  488  C   PRO A 109     7126   5306   5247    653   -990    773       C  
ATOM    489  O   PRO A 109     -11.540 -25.823   7.045  1.00 47.88           O  
ANISOU  489  O   PRO A 109     7362   5420   5411    668  -1105    859       O  
ATOM    490  CB  PRO A 109     -10.564 -24.820   4.029  1.00 45.02           C  
ANISOU  490  CB  PRO A 109     6670   5056   5379    718   -836    647       C  
ATOM    491  CG  PRO A 109     -10.782 -23.481   3.424  1.00 53.69           C  
ANISOU  491  CG  PRO A 109     7728   6233   6438    689   -725    579       C  
ATOM    492  CD  PRO A 109     -12.236 -23.435   3.074  1.00 56.32           C  
ANISOU  492  CD  PRO A 109     8159   6631   6608    646   -597    578       C  
ATOM    493  N   ILE A 110     -11.785 -23.615   6.696  1.00 53.29           N  
ANISOU  493  N   ILE A 110     7997   6239   6012    622  -1000    729       N  
ATOM    494  CA  ILE A 110     -11.680 -23.262   8.112  1.00 49.68           C  
ANISOU  494  CA  ILE A 110     7638   5817   5421    604  -1148    765       C  
ATOM    495  C   ILE A 110     -12.964 -23.646   8.854  1.00 45.39           C  
ANISOU  495  C   ILE A 110     7268   5323   4654    552  -1106    829       C  
ATOM    496  O   ILE A 110     -12.969 -23.801  10.075  1.00 50.90           O  
ANISOU  496  O   ILE A 110     8082   6042   5216    539  -1224    891       O  
ATOM    497  CB  ILE A 110     -11.382 -21.753   8.289  1.00 55.54           C  
ANISOU  497  CB  ILE A 110     8331   6621   6152    586  -1165    677       C  
ATOM    498  CG1 ILE A 110     -10.136 -21.367   7.487  1.00 59.10           C  
ANISOU  498  CG1 ILE A 110     8599   7015   6843    630  -1181    617       C  
ATOM    499  CG2 ILE A 110     -11.190 -21.391   9.754  1.00 53.46           C  
ANISOU  499  CG2 ILE A 110     8166   6398   5749    574  -1332    693       C  
ATOM    500  CD1 ILE A 110      -9.572 -20.006   7.837  1.00 58.24           C  
ANISOU  500  CD1 ILE A 110     8425   6936   6768    620  -1242    540       C  
ATOM    501  N   ALA A 111     -14.048 -23.823   8.105  1.00 44.48           N  
ANISOU  501  N   ALA A 111     7170   5228   4504    522   -936    814       N  
ATOM    502  CA  ALA A 111     -15.307 -24.281   8.682  1.00 36.03           C  
ANISOU  502  CA  ALA A 111     6242   4191   3258    470   -870    870       C  
ATOM    503  C   ALA A 111     -15.227 -25.756   9.069  1.00 70.94           C  
ANISOU  503  C   ALA A 111    10725   8527   7702    486   -933    987       C  
ATOM    504  O   ALA A 111     -16.046 -26.250   9.843  1.00 53.05           O  
ANISOU  504  O   ALA A 111     8592   6275   5290    443   -914   1065       O  
ATOM    505  CB  ALA A 111     -16.452 -24.049   7.711  1.00 34.59           C  
ANISOU  505  CB  ALA A 111     6038   4041   3064    438   -684    809       C  
ATOM    506  N   LEU A 112     -14.242 -26.459   8.517  1.00 76.97           N  
ANISOU  506  N   LEU A 112    11388   9196   8660    546  -1001   1000       N  
ATOM    507  CA  LEU A 112     -14.017 -27.858   8.865  1.00 72.54           C  
ANISOU  507  CA  LEU A 112    10867   8532   8161    571  -1082   1112       C  
ATOM    508  C   LEU A 112     -13.419 -27.977  10.254  1.00 78.98           C  
ANISOU  508  C   LEU A 112    11782   9343   8884    579  -1275   1211       C  
ATOM    509  O   LEU A 112     -13.591 -28.990  10.930  1.00 82.50           O  
ANISOU  509  O   LEU A 112    12329   9731   9287    575  -1338   1338       O  
ATOM    510  CB  LEU A 112     -13.094 -28.535   7.854  1.00 65.85           C  
ANISOU  510  CB  LEU A 112     9868   7581   7570    639  -1100   1078       C  
ATOM    511  CG  LEU A 112     -13.607 -28.722   6.431  1.00 55.63           C  
ANISOU  511  CG  LEU A 112     8485   6278   6373    641   -924    989       C  
ATOM    512  CD1 LEU A 112     -12.549 -29.432   5.609  1.00 55.23           C  
ANISOU  512  CD1 LEU A 112     8292   6126   6568    711   -957    953       C  
ATOM    513  CD2 LEU A 112     -14.904 -29.510   6.436  1.00 47.48           C  
ANISOU  513  CD2 LEU A 112     7547   5232   5262    597   -824   1035       C  
ATOM    514  N   LEU A 113     -12.704 -26.938  10.671  1.00 76.06           N  
ANISOU  514  N   LEU A 113    11383   9030   8486    592  -1374   1154       N  
ATOM    515  CA  LEU A 113     -12.061 -26.932  11.977  1.00 73.66           C  
ANISOU  515  CA  LEU A 113    11169   8733   8084    606  -1579   1229       C  
ATOM    516  C   LEU A 113     -13.106 -26.731  13.065  1.00 77.55           C  
ANISOU  516  C   LEU A 113    11856   9322   8286    538  -1547   1287       C  
ATOM    517  O   LEU A 113     -12.888 -27.083  14.223  1.00 89.46           O  
ANISOU  517  O   LEU A 113    13494  10836   9659    538  -1693   1390       O  
ATOM    518  CB  LEU A 113     -10.986 -25.846  12.047  1.00 71.22           C  
ANISOU  518  CB  LEU A 113    10755   8452   7854    639  -1695   1129       C  
ATOM    519  CG  LEU A 113      -9.988 -25.827  10.884  1.00 62.75           C  
ANISOU  519  CG  LEU A 113     9473   7298   7071    695  -1684   1049       C  
ATOM    520  CD1 LEU A 113      -8.825 -24.895  11.189  1.00 61.70           C  
ANISOU  520  CD1 LEU A 113     9241   7172   7030    727  -1832    973       C  
ATOM    521  CD2 LEU A 113      -9.489 -27.227  10.553  1.00 53.74           C  
ANISOU  521  CD2 LEU A 113     8284   6025   6109    748  -1739   1127       C  
ATOM    522  N   THR A 114     -14.244 -26.164  12.677  1.00 78.90           N  
ANISOU  522  N   THR A 114    12048   9569   8362    480  -1354   1219       N  
ATOM    523  CA  THR A 114     -15.406 -26.074  13.550  1.00 90.08           C  
ANISOU  523  CA  THR A 114    13632  11069   9525    408  -1273   1263       C  
ATOM    524  C   THR A 114     -15.886 -27.487  13.872  1.00 92.26           C  
ANISOU  524  C   THR A 114    14012  11270   9773    393  -1256   1419       C  
ATOM    525  O   THR A 114     -16.452 -27.751  14.936  1.00 87.68           O  
ANISOU  525  O   THR A 114    13599  10733   8984    346  -1259   1516       O  
ATOM    526  CB  THR A 114     -16.540 -25.257  12.890  1.00 88.36           C  
ANISOU  526  CB  THR A 114    13382  10924   9268    356  -1062   1150       C  
ATOM    527  OG1 THR A 114     -16.107 -23.905  12.701  1.00 88.72           O  
ANISOU  527  OG1 THR A 114    13342  11032   9335    366  -1084   1019       O  
ATOM    528  CG2 THR A 114     -17.799 -25.263  13.751  1.00 96.07           C  
ANISOU  528  CG2 THR A 114    14517  11975  10009    279   -956   1189       C  
ATOM    529  N   ILE A 115     -15.618 -28.399  12.944  1.00 90.64           N  
ANISOU  529  N   ILE A 115    13704  10949   9787    432  -1238   1442       N  
ATOM    530  CA  ILE A 115     -16.078 -29.777  13.033  1.00 80.87           C  
ANISOU  530  CA  ILE A 115    12531   9613   8583    421  -1209   1576       C  
ATOM    531  C   ILE A 115     -15.046 -30.717  13.649  1.00 89.11           C  
ANISOU  531  C   ILE A 115    13606  10552   9699    476  -1418   1713       C  
ATOM    532  O   ILE A 115     -15.359 -31.460  14.581  1.00 89.27           O  
ANISOU  532  O   ILE A 115    13776  10546   9597    449  -1462   1869       O  
ATOM    533  CB  ILE A 115     -16.464 -30.304  11.642  1.00 69.85           C  
ANISOU  533  CB  ILE A 115    11005   8142   7395    432  -1067   1509       C  
ATOM    534  CG1 ILE A 115     -17.613 -29.471  11.078  1.00 72.66           C  
ANISOU  534  CG1 ILE A 115    11345   8593   7672    377   -871   1392       C  
ATOM    535  CG2 ILE A 115     -16.842 -31.770  11.702  1.00 71.81           C  
ANISOU  535  CG2 ILE A 115    11298   8266   7720    425  -1051   1637       C  
ATOM    536  CD1 ILE A 115     -18.130 -29.964   9.752  1.00 77.14           C  
ANISOU  536  CD1 ILE A 115    11802   9101   8407    384   -736   1322       C  
ATOM    537  N   MET A 116     -13.824 -30.690  13.121  1.00 94.18           N  
ANISOU  537  N   MET A 116    14104  11131  10549    552  -1542   1659       N  
ATOM    538  CA  MET A 116     -12.764 -31.577  13.592  1.00 89.10           C  
ANISOU  538  CA  MET A 116    13458  10370  10024    616  -1754   1773       C  
ATOM    539  C   MET A 116     -12.499 -31.380  15.080  1.00 91.32           C  
ANISOU  539  C   MET A 116    13909  10710  10077    608  -1932   1885       C  
ATOM    540  O   MET A 116     -12.619 -32.315  15.865  1.00100.60           O  
ANISOU  540  O   MET A 116    15217  11827  11181    602  -2013   2057       O  
ATOM    541  CB  MET A 116     -11.476 -31.355  12.799  1.00 83.61           C  
ANISOU  541  CB  MET A 116    12564   9614   9591    696  -1848   1666       C  
ATOM    542  CG  MET A 116     -11.550 -31.790  11.343  1.00 81.84           C  
ANISOU  542  CG  MET A 116    12178   9315   9604    718  -1699   1572       C  
ATOM    543  SD  MET A 116     -10.010 -31.441  10.469  1.00129.75           S  
ANISOU  543  SD  MET A 116    18012  15324  15963    805  -1785   1442       S  
ATOM    544  CE  MET A 116     -10.377 -32.073   8.831  1.00 43.77           C  
ANISOU  544  CE  MET A 116     6983   4368   5281    817  -1578   1343       C  
ATOM    545  N   PHE A 117     -12.144 -30.156  15.455  1.00 88.36           N  
ANISOU  545  N   PHE A 117    13532  10451   9591    606  -1992   1785       N  
ATOM    546  CA  PHE A 117     -11.954 -29.791  16.854  1.00 84.86           C  
ANISOU  546  CA  PHE A 117    13253  10091   8898    595  -2153   1855       C  
ATOM    547  C   PHE A 117     -13.133 -28.983  17.356  1.00 90.75           C  
ANISOU  547  C   PHE A 117    14133  10990   9357    508  -1993   1812       C  
ATOM    548  O   PHE A 117     -13.130 -27.762  17.263  1.00 96.45           O  
ANISOU  548  O   PHE A 117    14806  11812  10030    495  -1958   1662       O  
ATOM    549  CB  PHE A 117     -10.668 -28.995  17.027  1.00 81.45           C  
ANISOU  549  CB  PHE A 117    12721   9674   8552    657  -2357   1759       C  
ATOM    550  CG  PHE A 117      -9.545 -29.474  16.162  1.00 80.32           C  
ANISOU  550  CG  PHE A 117    12376   9389   8751    738  -2449   1727       C  
ATOM    551  CD1 PHE A 117      -8.676 -30.449  16.618  1.00 77.80           C  
ANISOU  551  CD1 PHE A 117    12064   8950   8545    803  -2669   1853       C  
ATOM    552  CD2 PHE A 117      -9.342 -28.935  14.900  1.00 79.80           C  
ANISOU  552  CD2 PHE A 117    12113   9311   8896    751  -2317   1572       C  
ATOM    553  CE1 PHE A 117      -7.636 -30.888  15.827  1.00 79.94           C  
ANISOU  553  CE1 PHE A 117    12137   9087   9150    878  -2747   1810       C  
ATOM    554  CE2 PHE A 117      -8.300 -29.372  14.106  1.00 74.84           C  
ANISOU  554  CE2 PHE A 117    11298   8559   8580    823  -2383   1533       C  
ATOM    555  CZ  PHE A 117      -7.448 -30.348  14.573  1.00 74.84           C  
ANISOU  555  CZ  PHE A 117    11294   8437   8706    887  -2595   1645       C  
ATOM    556  N   GLU A 118     -14.133 -29.668  17.898  1.00 98.54           N  
ANISOU  556  N   GLU A 118    15231  12002  10209    444  -1858   1916       N  
ATOM    557  CA  GLU A 118     -15.430 -29.051  18.170  1.00105.49           C  
ANISOU  557  CA  GLU A 118    16188  13011  10884    355  -1643   1858       C  
ATOM    558  C   GLU A 118     -15.363 -27.875  19.135  1.00110.78           C  
ANISOU  558  C   GLU A 118    16906  13841  11345    331  -1682   1759       C  
ATOM    559  O   GLU A 118     -15.996 -26.845  18.904  1.00109.25           O  
ANISOU  559  O   GLU A 118    16704  13736  11069    291  -1557   1626       O  
ATOM    560  CB  GLU A 118     -16.415 -30.094  18.717  1.00102.94           C  
ANISOU  560  CB  GLU A 118    15959  12677  10477    294  -1505   1998       C  
ATOM    561  N   ALA A 119     -14.596 -28.020  20.208  1.00116.99           N  
ANISOU  561  N   ALA A 119    17740  14660  12052    359  -1861   1817       N  
ATOM    562  CA  ALA A 119     -14.692 -27.075  21.313  1.00122.40           C  
ANISOU  562  CA  ALA A 119    18497  15504  12506    328  -1883   1739       C  
ATOM    563  C   ALA A 119     -14.156 -25.685  20.985  1.00121.50           C  
ANISOU  563  C   ALA A 119    18307  15440  12417    352  -1961   1553       C  
ATOM    564  O   ALA A 119     -14.892 -24.700  21.060  1.00118.90           O  
ANISOU  564  O   ALA A 119    17995  15216  11966    302  -1829   1429       O  
ATOM    565  CB  ALA A 119     -13.977 -27.629  22.537  1.00126.35           C  
ANISOU  565  CB  ALA A 119    19074  16025  12910    357  -2066   1852       C  
ATOM    566  N   MET A 120     -12.880 -25.603  20.622  1.00119.50           N  
ANISOU  566  N   MET A 120    17961  15103  12339    431  -2175   1531       N  
ATOM    567  CA  MET A 120     -12.203 -24.311  20.585  1.00113.98           C  
ANISOU  567  CA  MET A 120    17197  14451  11659    459  -2295   1367       C  
ATOM    568  C   MET A 120     -11.665 -23.899  19.218  1.00102.17           C  
ANISOU  568  C   MET A 120    15541  12858  10422    508  -2312   1281       C  
ATOM    569  O   MET A 120     -11.700 -24.662  18.253  1.00107.65           O  
ANISOU  569  O   MET A 120    16139  13447  11316    525  -2222   1334       O  
ATOM    570  CB  MET A 120     -11.053 -24.309  21.594  1.00120.35           C  
ANISOU  570  CB  MET A 120    18011  15272  12444    509  -2555   1380       C  
ATOM    571  N   TRP A 121     -11.161 -22.669  19.167  1.00 97.60           N  
ANISOU  571  N   TRP A 121    14859  12326   9899    519  -2366   1116       N  
ATOM    572  CA  TRP A 121     -10.604 -22.074  17.959  1.00 88.36           C  
ANISOU  572  CA  TRP A 121    13455  11090   9028    548  -2313    994       C  
ATOM    573  C   TRP A 121      -9.092 -22.288  17.901  1.00 91.77           C  
ANISOU  573  C   TRP A 121    13757  11422   9688    628  -2547    995       C  
ATOM    574  O   TRP A 121      -8.348 -21.696  18.681  1.00 94.34           O  
ANISOU  574  O   TRP A 121    14087  11780   9978    653  -2748    934       O  
ATOM    575  CB  TRP A 121     -10.945 -20.580  17.915  1.00 81.73           C  
ANISOU  575  CB  TRP A 121    12566  10342   8145    509  -2227    818       C  
ATOM    576  CG  TRP A 121     -10.339 -19.810  16.774  1.00 73.61           C  
ANISOU  576  CG  TRP A 121    11310   9253   7406    533  -2178    698       C  
ATOM    577  CD1 TRP A 121      -9.262 -18.975  16.834  1.00 70.57           C  
ANISOU  577  CD1 TRP A 121    10794   8845   7174    568  -2326    589       C  
ATOM    578  CD2 TRP A 121     -10.795 -19.775  15.414  1.00 67.76           C  
ANISOU  578  CD2 TRP A 121    10449   8468   6829    520  -1962    675       C  
ATOM    579  NE1 TRP A 121      -9.007 -18.437  15.597  1.00 68.14           N  
ANISOU  579  NE1 TRP A 121    10293   8478   7117    574  -2202    513       N  
ATOM    580  CE2 TRP A 121      -9.935 -18.910  14.708  1.00 67.27           C  
ANISOU  580  CE2 TRP A 121    10193   8360   7005    546  -1982    566       C  
ATOM    581  CE3 TRP A 121     -11.838 -20.399  14.724  1.00 66.31           C  
ANISOU  581  CE3 TRP A 121    10302   8278   6616    488  -1759    736       C  
ATOM    582  CZ2 TRP A 121     -10.088 -18.652  13.346  1.00 64.81           C  
ANISOU  582  CZ2 TRP A 121     9742   8007   6877    543  -1801    528       C  
ATOM    583  CZ3 TRP A 121     -11.990 -20.139  13.373  1.00 64.40           C  
ANISOU  583  CZ3 TRP A 121     9915   7995   6557    490  -1597    684       C  
ATOM    584  CH2 TRP A 121     -11.119 -19.274  12.699  1.00 61.23           C  
ANISOU  584  CH2 TRP A 121     9339   7558   6366    517  -1617    587       C  
ATOM    585  N   PRO A 122      -8.636 -23.142  16.972  1.00 89.66           N  
ANISOU  585  N   PRO A 122    13367  11031   9670    671  -2524   1053       N  
ATOM    586  CA  PRO A 122      -7.228 -23.542  16.858  1.00 87.67           C  
ANISOU  586  CA  PRO A 122    12978  10664   9667    750  -2733   1064       C  
ATOM    587  C   PRO A 122      -6.323 -22.426  16.336  1.00 86.91           C  
ANISOU  587  C   PRO A 122    12676  10551   9795    774  -2767    900       C  
ATOM    588  O   PRO A 122      -5.214 -22.243  16.837  1.00 94.61           O  
ANISOU  588  O   PRO A 122    13584  11487  10876    824  -2998    866       O  
ATOM    589  CB  PRO A 122      -7.271 -24.710  15.859  1.00 90.68           C  
ANISOU  589  CB  PRO A 122    13284  10928  10242    775  -2625   1148       C  
ATOM    590  CG  PRO A 122      -8.726 -25.095  15.747  1.00 90.72           C  
ANISOU  590  CG  PRO A 122    13431  10989  10049    708  -2407   1215       C  
ATOM    591  CD  PRO A 122      -9.479 -23.832  15.982  1.00 89.44           C  
ANISOU  591  CD  PRO A 122    13321  10961   9701    646  -2295   1105       C  
ATOM    592  N   LEU A 123      -6.803 -21.695  15.335  1.00 79.42           N  
ANISOU  592  N   LEU A 123    11627   9625   8923    737  -2543    803       N  
ATOM    593  CA  LEU A 123      -6.038 -20.625  14.699  1.00 75.24           C  
ANISOU  593  CA  LEU A 123    10897   9071   8620    749  -2532    661       C  
ATOM    594  C   LEU A 123      -5.799 -19.450  15.654  1.00 73.21           C  
ANISOU  594  C   LEU A 123    10668   8891   8259    733  -2670    553       C  
ATOM    595  O   LEU A 123      -6.360 -19.421  16.748  1.00 73.58           O  
ANISOU  595  O   LEU A 123    10901   9028   8027    708  -2744    581       O  
ATOM    596  CB  LEU A 123      -6.773 -20.153  13.440  1.00 73.27           C  
ANISOU  596  CB  LEU A 123    10570   8837   8434    707  -2252    607       C  
ATOM    597  CG  LEU A 123      -7.091 -21.249  12.420  1.00 70.08           C  
ANISOU  597  CG  LEU A 123    10137   8368   8122    720  -2102    687       C  
ATOM    598  CD1 LEU A 123      -7.800 -20.668  11.206  1.00 65.87           C  
ANISOU  598  CD1 LEU A 123     9535   7864   7631    682  -1847    625       C  
ATOM    599  CD2 LEU A 123      -5.826 -21.990  12.009  1.00 73.01           C  
ANISOU  599  CD2 LEU A 123    10358   8613   8769    791  -2214    707       C  
ATOM    600  N   PRO A 124      -4.943 -18.488  15.258  1.00 75.06           N  
ANISOU  600  N   PRO A 124    10713   9084   8721    748  -2705    427       N  
ATOM    601  CA  PRO A 124      -4.818 -17.242  16.026  1.00 71.79           C  
ANISOU  601  CA  PRO A 124    10305   8739   8234    726  -2805    299       C  
ATOM    602  C   PRO A 124      -6.155 -16.534  16.266  1.00 72.89           C  
ANISOU  602  C   PRO A 124    10581   8998   8116    655  -2640    257       C  
ATOM    603  O   PRO A 124      -7.149 -16.827  15.603  1.00 76.12           O  
ANISOU  603  O   PRO A 124    11038   9429   8456    620  -2421    311       O  
ATOM    604  CB  PRO A 124      -3.903 -16.390  15.147  1.00 68.75           C  
ANISOU  604  CB  PRO A 124     9670   8270   8183    739  -2773    186       C  
ATOM    605  CG  PRO A 124      -3.020 -17.382  14.489  1.00 66.90           C  
ANISOU  605  CG  PRO A 124     9311   7918   8192    796  -2808    256       C  
ATOM    606  CD  PRO A 124      -3.865 -18.614  14.257  1.00 75.65           C  
ANISOU  606  CD  PRO A 124    10559   9037   9146    792  -2697    399       C  
ATOM    607  N   LEU A 125      -6.164 -15.599  17.210  1.00 76.63           N  
ANISOU  607  N   LEU A 125    11107   9547   8464    637  -2752    148       N  
ATOM    608  CA  LEU A 125      -7.395 -14.942  17.635  1.00 73.40           C  
ANISOU  608  CA  LEU A 125    10834   9254   7800    573  -2621     94       C  
ATOM    609  C   LEU A 125      -7.952 -13.973  16.593  1.00 70.28           C  
ANISOU  609  C   LEU A 125    10318   8848   7538    532  -2390      9       C  
ATOM    610  O   LEU A 125      -9.167 -13.832  16.460  1.00 72.92           O  
ANISOU  610  O   LEU A 125    10744   9247   7713    483  -2206     15       O  
ATOM    611  CB  LEU A 125      -7.161 -14.202  18.955  1.00 66.75           C  
ANISOU  611  CB  LEU A 125    10074   8493   6796    571  -2818    -20       C  
ATOM    612  CG  LEU A 125      -6.518 -15.039  20.062  1.00 75.15           C  
ANISOU  612  CG  LEU A 125    11264   9573   7718    617  -3084     58       C  
ATOM    613  CD1 LEU A 125      -6.310 -14.213  21.323  1.00 88.58           C  
ANISOU  613  CD1 LEU A 125    13046  11366   9244    615  -3278    -77       C  
ATOM    614  CD2 LEU A 125      -7.355 -16.274  20.354  1.00 75.89           C  
ANISOU  614  CD2 LEU A 125    11561   9710   7562    603  -3012    237       C  
ATOM    615  N   VAL A 126      -7.067 -13.307  15.857  1.00 68.13           N  
ANISOU  615  N   VAL A 126     9836   8487   7562    551  -2399    -64       N  
ATOM    616  CA  VAL A 126      -7.491 -12.309  14.880  1.00 69.88           C  
ANISOU  616  CA  VAL A 126     9941   8690   7921    514  -2198   -134       C  
ATOM    617  C   VAL A 126      -8.027 -12.970  13.614  1.00 69.05           C  
ANISOU  617  C   VAL A 126     9811   8552   7874    509  -1981    -27       C  
ATOM    618  O   VAL A 126      -8.694 -12.331  12.798  1.00 75.53           O  
ANISOU  618  O   VAL A 126    10586   9375   8736    475  -1793    -53       O  
ATOM    619  CB  VAL A 126      -6.339 -11.354  14.510  1.00 73.41           C  
ANISOU  619  CB  VAL A 126    10170   9047   8676    531  -2271   -238       C  
ATOM    620  CG1 VAL A 126      -6.892 -10.040  13.977  1.00 68.12           C  
ANISOU  620  CG1 VAL A 126     9423   8378   8082    484  -2113   -333       C  
ATOM    621  CG2 VAL A 126      -5.467 -11.095  15.725  1.00 81.75           C  
ANISOU  621  CG2 VAL A 126    11229  10109   9722    559  -2547   -326       C  
ATOM    622  N   LEU A 127      -7.739 -14.256  13.454  1.00 64.82           N  
ANISOU  622  N   LEU A 127     9307   7981   7342    545  -2015     89       N  
ATOM    623  CA  LEU A 127      -8.261 -15.008  12.321  1.00 69.14           C  
ANISOU  623  CA  LEU A 127     9843   8500   7926    544  -1824    181       C  
ATOM    624  C   LEU A 127      -9.752 -15.293  12.493  1.00 70.08           C  
ANISOU  624  C   LEU A 127    10133   8704   7790    498  -1685    224       C  
ATOM    625  O   LEU A 127     -10.457 -15.551  11.519  1.00 73.78           O  
ANISOU  625  O   LEU A 127    10591   9167   8274    483  -1502    263       O  
ATOM    626  CB  LEU A 127      -7.488 -16.318  12.137  1.00 70.62           C  
ANISOU  626  CB  LEU A 127    10003   8612   8216    598  -1909    278       C  
ATOM    627  CG  LEU A 127      -6.119 -16.214  11.459  1.00 69.49           C  
ANISOU  627  CG  LEU A 127     9649   8364   8389    642  -1963    244       C  
ATOM    628  CD1 LEU A 127      -5.560 -17.597  11.162  1.00 61.45           C  
ANISOU  628  CD1 LEU A 127     8607   7270   7471    695  -2011    338       C  
ATOM    629  CD2 LEU A 127      -6.207 -15.388  10.182  1.00 63.08           C  
ANISOU  629  CD2 LEU A 127     8699   7530   7737    619  -1757    194       C  
ATOM    630  N   CYS A 128     -10.230 -15.234  13.732  1.00 68.40           N  
ANISOU  630  N   CYS A 128    10076   8572   7343    476  -1772    212       N  
ATOM    631  CA  CYS A 128     -11.635 -15.515  14.020  1.00 63.28           C  
ANISOU  631  CA  CYS A 128     9587   8003   6453    428  -1639    248       C  
ATOM    632  C   CYS A 128     -12.581 -14.439  13.461  1.00 53.09           C  
ANISOU  632  C   CYS A 128     8258   6749   5166    382  -1457    158       C  
ATOM    633  O   CYS A 128     -13.550 -14.780  12.782  1.00 49.07           O  
ANISOU  633  O   CYS A 128     7776   6248   4622    359  -1286    201       O  
ATOM    634  CB  CYS A 128     -11.850 -15.689  15.530  1.00 43.16           C  
ANISOU  634  CB  CYS A 128     7218   5539   3642    413  -1771    255       C  
ATOM    635  SG  CYS A 128     -13.525 -16.178  15.997  1.00 66.82           S  
ANISOU  635  SG  CYS A 128    10416   8630   6344    350  -1599    312       S  
ATOM    636  N   PRO A 129     -12.317 -13.143  13.735  1.00 50.00           N  
ANISOU  636  N   PRO A 129     7797   6371   4831    370  -1502     29       N  
ATOM    637  CA  PRO A 129     -13.214 -12.157  13.121  1.00 45.42           C  
ANISOU  637  CA  PRO A 129     7169   5806   4282    332  -1331    -45       C  
ATOM    638  C   PRO A 129     -13.011 -12.064  11.613  1.00 46.45           C  
ANISOU  638  C   PRO A 129     7154   5858   4635    347  -1209     -9       C  
ATOM    639  O   PRO A 129     -13.960 -11.784  10.882  1.00 45.65           O  
ANISOU  639  O   PRO A 129     7048   5767   4529    322  -1046     -9       O  
ATOM    640  CB  PRO A 129     -12.820 -10.841  13.804  1.00 41.68           C  
ANISOU  640  CB  PRO A 129     6643   5346   3847    321  -1431   -191       C  
ATOM    641  CG  PRO A 129     -12.061 -11.239  15.017  1.00 41.45           C  
ANISOU  641  CG  PRO A 129     6693   5348   3709    344  -1644   -197       C  
ATOM    642  CD  PRO A 129     -11.350 -12.490  14.633  1.00 43.98           C  
ANISOU  642  CD  PRO A 129     7001   5611   4099    388  -1702    -62       C  
ATOM    643  N   ALA A 130     -11.783 -12.299  11.164  1.00 42.28           N  
ANISOU  643  N   ALA A 130     6510   5256   4299    389  -1288     19       N  
ATOM    644  CA  ALA A 130     -11.476 -12.305   9.739  1.00 39.45           C  
ANISOU  644  CA  ALA A 130     6022   4830   4139    405  -1167     59       C  
ATOM    645  C   ALA A 130     -12.279 -13.382   9.019  1.00 39.08           C  
ANISOU  645  C   ALA A 130     6044   4795   4010    406  -1035    154       C  
ATOM    646  O   ALA A 130     -12.886 -13.124   7.980  1.00 35.60           O  
ANISOU  646  O   ALA A 130     5567   4350   3608    394   -880    162       O  
ATOM    647  CB  ALA A 130      -9.987 -12.518   9.517  1.00 39.49           C  
ANISOU  647  CB  ALA A 130     5894   4755   4357    449  -1276     68       C  
ATOM    648  N   TRP A 131     -12.285 -14.585   9.582  1.00 35.89           N  
ANISOU  648  N   TRP A 131     5740   4401   3495    422  -1104    225       N  
ATOM    649  CA  TRP A 131     -12.988 -15.704   8.971  1.00 35.07           C  
ANISOU  649  CA  TRP A 131     5696   4295   3334    424   -994    310       C  
ATOM    650  C   TRP A 131     -14.495 -15.471   8.926  1.00 40.22           C  
ANISOU  650  C   TRP A 131     6441   5011   3831    377   -855    295       C  
ATOM    651  O   TRP A 131     -15.128 -15.651   7.886  1.00 39.78           O  
ANISOU  651  O   TRP A 131     6360   4947   3807    374   -716    313       O  
ATOM    652  CB  TRP A 131     -12.682 -17.000   9.718  1.00 36.07           C  
ANISOU  652  CB  TRP A 131     5913   4407   3384    448  -1111    395       C  
ATOM    653  CG  TRP A 131     -13.546 -18.134   9.285  1.00 35.42           C  
ANISOU  653  CG  TRP A 131     5906   4320   3231    441  -1003    474       C  
ATOM    654  CD1 TRP A 131     -13.668 -18.633   8.021  1.00 36.52           C  
ANISOU  654  CD1 TRP A 131     5975   4419   3482    459   -883    495       C  
ATOM    655  CD2 TRP A 131     -14.404 -18.927  10.112  1.00 35.87           C  
ANISOU  655  CD2 TRP A 131     6121   4413   3094    413  -1003    540       C  
ATOM    656  NE1 TRP A 131     -14.555 -19.680   8.008  1.00 34.20           N  
ANISOU  656  NE1 TRP A 131     5777   4126   3091    445   -819    559       N  
ATOM    657  CE2 TRP A 131     -15.020 -19.882   9.283  1.00 38.50           C  
ANISOU  657  CE2 TRP A 131     6459   4713   3455    415   -885    595       C  
ATOM    658  CE3 TRP A 131     -14.711 -18.919  11.476  1.00 43.52           C  
ANISOU  658  CE3 TRP A 131     7229   5441   3865    385  -1087    557       C  
ATOM    659  CZ2 TRP A 131     -15.926 -20.822   9.767  1.00 42.23           C  
ANISOU  659  CZ2 TRP A 131     7060   5196   3790    386   -845    669       C  
ATOM    660  CZ3 TRP A 131     -15.611 -19.854  11.957  1.00 51.87           C  
ANISOU  660  CZ3 TRP A 131     8426   6517   4765    355  -1036    641       C  
ATOM    661  CH2 TRP A 131     -16.206 -20.793  11.105  1.00 36.50           C  
ANISOU  661  CH2 TRP A 131     6469   4523   2875    355   -915    698       C  
ATOM    662  N   LEU A 132     -15.061 -15.073  10.060  1.00 40.41           N  
ANISOU  662  N   LEU A 132     6568   5099   3688    342   -895    255       N  
ATOM    663  CA  LEU A 132     -16.484 -14.773  10.145  1.00 34.18           C  
ANISOU  663  CA  LEU A 132     5855   4368   2764    294   -765    224       C  
ATOM    664  C   LEU A 132     -16.880 -13.671   9.165  1.00 53.68           C  
ANISOU  664  C   LEU A 132     8221   6825   5349    285   -653    157       C  
ATOM    665  O   LEU A 132     -17.936 -13.744   8.538  1.00 65.45           O  
ANISOU  665  O   LEU A 132     9727   8328   6814    266   -522    162       O  
ATOM    666  CB  LEU A 132     -16.857 -14.374  11.575  1.00 35.33           C  
ANISOU  666  CB  LEU A 132     6114   4587   2722    260   -828    169       C  
ATOM    667  CG  LEU A 132     -16.895 -15.509  12.603  1.00 50.01           C  
ANISOU  667  CG  LEU A 132     8123   6477   4402    255   -902    256       C  
ATOM    668  CD1 LEU A 132     -16.970 -14.967  14.024  1.00 37.96           C  
ANISOU  668  CD1 LEU A 132     6703   5032   2690    228   -989    190       C  
ATOM    669  CD2 LEU A 132     -18.068 -16.433  12.322  1.00 37.51           C  
ANISOU  669  CD2 LEU A 132     6618   4900   2731    226   -757    328       C  
ATOM    670  N   PHE A 133     -16.026 -12.660   9.029  1.00 41.73           N  
ANISOU  670  N   PHE A 133     6599   5281   3975    298   -712     98       N  
ATOM    671  CA  PHE A 133     -16.276 -11.566   8.094  1.00 39.30           C  
ANISOU  671  CA  PHE A 133     6190   4948   3795    290   -617     52       C  
ATOM    672  C   PHE A 133     -16.316 -12.064   6.653  1.00 41.46           C  
ANISOU  672  C   PHE A 133     6407   5185   4162    313   -509    125       C  
ATOM    673  O   PHE A 133     -17.232 -11.729   5.902  1.00 54.35           O  
ANISOU  673  O   PHE A 133     8034   6825   5791    300   -395    121       O  
ATOM    674  CB  PHE A 133     -15.211 -10.475   8.243  1.00 51.77           C  
ANISOU  674  CB  PHE A 133     7655   6485   5530    299   -706    -13       C  
ATOM    675  CG  PHE A 133     -15.229  -9.446   7.141  1.00 52.65           C  
ANISOU  675  CG  PHE A 133     7649   6548   5808    296   -611    -27       C  
ATOM    676  CD1 PHE A 133     -16.266  -8.530   7.042  1.00 49.15           C  
ANISOU  676  CD1 PHE A 133     7212   6120   5345    266   -532    -82       C  
ATOM    677  CD2 PHE A 133     -14.201  -9.391   6.211  1.00 48.70           C  
ANISOU  677  CD2 PHE A 133     7030   5983   5491    322   -598     18       C  
ATOM    678  CE1 PHE A 133     -16.279  -7.583   6.030  1.00 49.22           C  
ANISOU  678  CE1 PHE A 133     7120   6076   5508    265   -455    -77       C  
ATOM    679  CE2 PHE A 133     -14.207  -8.449   5.197  1.00 40.62           C  
ANISOU  679  CE2 PHE A 133     5910   4914   4608    316   -504     23       C  
ATOM    680  CZ  PHE A 133     -15.247  -7.543   5.106  1.00 43.82           C  
ANISOU  680  CZ  PHE A 133     6331   5331   4986    289   -439    -17       C  
ATOM    681  N   LEU A 134     -15.325 -12.863   6.272  1.00 32.33           N  
ANISOU  681  N   LEU A 134     5208   3989   3089    350   -550    184       N  
ATOM    682  CA  LEU A 134     -15.264 -13.409   4.920  1.00 36.22           C  
ANISOU  682  CA  LEU A 134     5648   4452   3660    375   -449    240       C  
ATOM    683  C   LEU A 134     -16.454 -14.318   4.637  1.00 33.96           C  
ANISOU  683  C   LEU A 134     5458   4199   3248    366   -363    275       C  
ATOM    684  O   LEU A 134     -16.941 -14.387   3.509  1.00 43.35           O  
ANISOU  684  O   LEU A 134     6623   5386   4461    374   -257    290       O  
ATOM    685  CB  LEU A 134     -13.956 -14.172   4.704  1.00 36.60           C  
ANISOU  685  CB  LEU A 134     5629   4448   3828    417   -513    280       C  
ATOM    686  CG  LEU A 134     -12.690 -13.314   4.629  1.00 40.89           C  
ANISOU  686  CG  LEU A 134     6041   4942   4555    430   -570    247       C  
ATOM    687  CD1 LEU A 134     -11.459 -14.186   4.453  1.00 40.60           C  
ANISOU  687  CD1 LEU A 134     5932   4849   4646    473   -631    279       C  
ATOM    688  CD2 LEU A 134     -12.792 -12.295   3.505  1.00 36.80           C  
ANISOU  688  CD2 LEU A 134     5437   4409   4137    419   -444    239       C  
ATOM    689  N   ASP A 135     -16.925 -15.012   5.666  1.00 30.68           N  
ANISOU  689  N   ASP A 135     5150   3811   2695    349   -412    288       N  
ATOM    690  CA  ASP A 135     -18.083 -15.881   5.513  1.00 48.18           C  
ANISOU  690  CA  ASP A 135     7450   6049   4807    333   -330    318       C  
ATOM    691  C   ASP A 135     -19.315 -15.078   5.119  1.00 42.44           C  
ANISOU  691  C   ASP A 135     6728   5354   4043    303   -225    266       C  
ATOM    692  O   ASP A 135     -19.954 -15.367   4.108  1.00 40.62           O  
ANISOU  692  O   ASP A 135     6483   5119   3832    310   -136    277       O  
ATOM    693  CB  ASP A 135     -18.356 -16.660   6.801  1.00 55.10           C  
ANISOU  693  CB  ASP A 135     8446   6947   5541    312   -394    350       C  
ATOM    694  CG  ASP A 135     -19.651 -17.447   6.738  1.00 52.12           C  
ANISOU  694  CG  ASP A 135     8150   6586   5067    283   -295    374       C  
ATOM    695  OD1 ASP A 135     -20.716 -16.868   7.033  1.00 53.83           O  
ANISOU  695  OD1 ASP A 135     8405   6846   5204    243   -226    324       O  
ATOM    696  OD2 ASP A 135     -19.606 -18.641   6.383  1.00 56.10           O  
ANISOU  696  OD2 ASP A 135     8669   7051   5594    302   -286    437       O  
ATOM    697  N   VAL A 136     -19.643 -14.071   5.919  1.00 41.10           N  
ANISOU  697  N   VAL A 136     6575   5216   3827    271   -245    202       N  
ATOM    698  CA  VAL A 136     -20.833 -13.261   5.678  1.00 51.10           C  
ANISOU  698  CA  VAL A 136     7838   6505   5073    243   -157    144       C  
ATOM    699  C   VAL A 136     -20.714 -12.488   4.371  1.00 56.39           C  
ANISOU  699  C   VAL A 136     8408   7143   5875    266   -106    142       C  
ATOM    700  O   VAL A 136     -21.691 -12.314   3.646  1.00 64.20           O  
ANISOU  700  O   VAL A 136     9392   8136   6866    262    -26    133       O  
ATOM    701  CB  VAL A 136     -21.084 -12.279   6.836  1.00 49.56           C  
ANISOU  701  CB  VAL A 136     7668   6343   4819    208   -192     58       C  
ATOM    702  CG1 VAL A 136     -22.359 -11.494   6.603  1.00 29.51           C  
ANISOU  702  CG1 VAL A 136     5116   3817   2281    181    -99    -10       C  
ATOM    703  CG2 VAL A 136     -21.173 -13.036   8.147  1.00 51.01           C  
ANISOU  703  CG2 VAL A 136     7968   6570   4843    185   -239     69       C  
ATOM    704  N   LEU A 137     -19.502 -12.037   4.076  1.00 55.86           N  
ANISOU  704  N   LEU A 137     8263   7042   5921    290   -155    157       N  
ATOM    705  CA  LEU A 137     -19.227 -11.307   2.849  1.00 50.56           C  
ANISOU  705  CA  LEU A 137     7500   6337   5373    309   -102    175       C  
ATOM    706  C   LEU A 137     -19.504 -12.142   1.600  1.00 58.24           C  
ANISOU  706  C   LEU A 137     8478   7312   6339    336    -24    231       C  
ATOM    707  O   LEU A 137     -20.368 -11.800   0.792  1.00 65.91           O  
ANISOU  707  O   LEU A 137     9447   8291   7303    336     44    231       O  
ATOM    708  CB  LEU A 137     -17.778 -10.834   2.840  1.00 29.05           C  
ANISOU  708  CB  LEU A 137     4687   3571   2781    325   -161    183       C  
ATOM    709  CG  LEU A 137     -17.312 -10.178   1.544  1.00 37.38           C  
ANISOU  709  CG  LEU A 137     5649   4588   3967    342    -92    222       C  
ATOM    710  CD1 LEU A 137     -18.185  -8.978   1.204  1.00 37.88           C  
ANISOU  710  CD1 LEU A 137     5696   4644   4053    322    -43    199       C  
ATOM    711  CD2 LEU A 137     -15.855  -9.781   1.656  1.00 31.59           C  
ANISOU  711  CD2 LEU A 137     4817   3805   3382    352   -145    225       C  
ATOM    712  N   PHE A 138     -18.768 -13.238   1.452  1.00 47.81           N  
ANISOU  712  N   PHE A 138     7160   5981   5025    361    -43    272       N  
ATOM    713  CA  PHE A 138     -18.844 -14.048   0.244  1.00 37.19           C  
ANISOU  713  CA  PHE A 138     5808   4636   3687    392     27    310       C  
ATOM    714  C   PHE A 138     -20.190 -14.743   0.077  1.00 39.47           C  
ANISOU  714  C   PHE A 138     6170   4951   3874    382     73    299       C  
ATOM    715  O   PHE A 138     -20.661 -14.930  -1.043  1.00 47.38           O  
ANISOU  715  O   PHE A 138     7167   5964   4873    401    137    305       O  
ATOM    716  CB  PHE A 138     -17.719 -15.079   0.233  1.00 34.63           C  
ANISOU  716  CB  PHE A 138     5459   4283   3414    422     -9    340       C  
ATOM    717  CG  PHE A 138     -16.349 -14.473   0.217  1.00 44.72           C  
ANISOU  717  CG  PHE A 138     6643   5526   4823    436    -45    346       C  
ATOM    718  CD1 PHE A 138     -16.104 -13.313  -0.494  1.00 56.19           C  
ANISOU  718  CD1 PHE A 138     8026   6970   6355    432      9    348       C  
ATOM    719  CD2 PHE A 138     -15.306 -15.061   0.907  1.00 48.92           C  
ANISOU  719  CD2 PHE A 138     7151   6024   5414    452   -136    354       C  
ATOM    720  CE1 PHE A 138     -14.847 -12.746  -0.513  1.00 54.59           C  
ANISOU  720  CE1 PHE A 138     7724   6725   6294    438    -14    352       C  
ATOM    721  CE2 PHE A 138     -14.046 -14.500   0.891  1.00 46.14           C  
ANISOU  721  CE2 PHE A 138     6695   5631   5205    464   -172    348       C  
ATOM    722  CZ  PHE A 138     -13.817 -13.341   0.178  1.00 49.98           C  
ANISOU  722  CZ  PHE A 138     7105   6107   5777    454   -104    345       C  
ATOM    723  N   SER A 139     -20.810 -15.124   1.187  1.00 27.29           N  
ANISOU  723  N   SER A 139     4697   3421   2250    352     42    281       N  
ATOM    724  CA  SER A 139     -22.119 -15.762   1.128  1.00 26.97           C  
ANISOU  724  CA  SER A 139     4716   3397   2135    335     92    265       C  
ATOM    725  C   SER A 139     -23.193 -14.781   0.680  1.00 38.66           C  
ANISOU  725  C   SER A 139     6181   4895   3614    320    142    221       C  
ATOM    726  O   SER A 139     -24.113 -15.144  -0.049  1.00 41.07           O  
ANISOU  726  O   SER A 139     6494   5206   3905    326    190    209       O  
ATOM    727  CB  SER A 139     -22.495 -16.354   2.486  1.00 34.50           C  
ANISOU  727  CB  SER A 139     5749   4359   3001    298     61    266       C  
ATOM    728  OG  SER A 139     -21.421 -17.098   3.028  1.00 44.87           O  
ANISOU  728  OG  SER A 139     7077   5650   4321    314    -11    314       O  
ATOM    729  N   THR A 140     -23.077 -13.537   1.125  1.00 44.83           N  
ANISOU  729  N   THR A 140     6933   5678   4423    304    121    192       N  
ATOM    730  CA  THR A 140     -24.067 -12.523   0.796  1.00 26.51           C  
ANISOU  730  CA  THR A 140     4589   3360   2123    292    156    148       C  
ATOM    731  C   THR A 140     -23.918 -12.074  -0.653  1.00 36.01           C  
ANISOU  731  C   THR A 140     5741   4551   3390    328    184    185       C  
ATOM    732  O   THR A 140     -24.909 -11.865  -1.358  1.00 31.03           O  
ANISOU  732  O   THR A 140     5109   3924   2758    334    215    171       O  
ATOM    733  CB  THR A 140     -23.945 -11.311   1.732  1.00 29.65           C  
ANISOU  733  CB  THR A 140     4965   3753   2549    264    122     96       C  
ATOM    734  OG1 THR A 140     -24.037 -11.753   3.093  1.00 34.96           O  
ANISOU  734  OG1 THR A 140     5701   4451   3133    232     97     63       O  
ATOM    735  CG2 THR A 140     -25.037 -10.309   1.457  1.00 39.66           C  
ANISOU  735  CG2 THR A 140     6202   5011   3857    253    156     44       C  
ATOM    736  N   ALA A 141     -22.669 -11.939  -1.089  1.00 41.58           N  
ANISOU  736  N   ALA A 141     6405   5242   4152    351    173    233       N  
ATOM    737  CA  ALA A 141     -22.365 -11.516  -2.447  1.00 26.43           C  
ANISOU  737  CA  ALA A 141     4445   3317   2279    382    213    282       C  
ATOM    738  C   ALA A 141     -22.909 -12.510  -3.461  1.00 26.19           C  
ANISOU  738  C   ALA A 141     4451   3314   2186    410    252    293       C  
ATOM    739  O   ALA A 141     -23.346 -12.125  -4.544  1.00 31.73           O  
ANISOU  739  O   ALA A 141     5148   4026   2880    430    282    313       O  
ATOM    740  CB  ALA A 141     -20.867 -11.345  -2.624  1.00 26.83           C  
ANISOU  740  CB  ALA A 141     4440   3346   2408    395    209    325       C  
ATOM    741  N   SER A 142     -22.886 -13.791  -3.109  1.00 33.77           N  
ANISOU  741  N   SER A 142     5447   4281   3102    412    246    279       N  
ATOM    742  CA  SER A 142     -23.393 -14.821  -4.008  1.00 41.11           C  
ANISOU  742  CA  SER A 142     6404   5230   3986    438    277    271       C  
ATOM    743  C   SER A 142     -24.906 -14.697  -4.179  1.00 43.13           C  
ANISOU  743  C   SER A 142     6685   5496   4205    427    282    227       C  
ATOM    744  O   SER A 142     -25.425 -14.830  -5.285  1.00 63.93           O  
ANISOU  744  O   SER A 142     9324   8150   6816    455    299    221       O  
ATOM    745  CB  SER A 142     -23.035 -16.218  -3.496  1.00 43.89           C  
ANISOU  745  CB  SER A 142     6781   5569   4327    439    263    266       C  
ATOM    746  OG  SER A 142     -23.814 -16.567  -2.368  1.00 53.52           O  
ANISOU  746  OG  SER A 142     8044   6779   5511    401    242    241       O  
ATOM    747  N   ILE A 143     -25.605 -14.435  -3.080  1.00 35.03           N  
ANISOU  747  N   ILE A 143     5674   4460   3176    387    267    191       N  
ATOM    748  CA  ILE A 143     -27.059 -14.312  -3.109  1.00 39.57           C  
ANISOU  748  CA  ILE A 143     6257   5037   3743    372    277    137       C  
ATOM    749  C   ILE A 143     -27.496 -13.052  -3.853  1.00 46.98           C  
ANISOU  749  C   ILE A 143     7160   5973   4718    388    268    138       C  
ATOM    750  O   ILE A 143     -28.470 -13.066  -4.609  1.00 56.58           O  
ANISOU  750  O   ILE A 143     8374   7192   5933    405    264    113       O  
ATOM    751  CB  ILE A 143     -27.645 -14.293  -1.685  1.00 31.97           C  
ANISOU  751  CB  ILE A 143     5315   4065   2766    321    281     93       C  
ATOM    752  CG1 ILE A 143     -27.237 -15.559  -0.928  1.00 31.97           C  
ANISOU  752  CG1 ILE A 143     5363   4063   2723    304    284    112       C  
ATOM    753  CG2 ILE A 143     -29.160 -14.167  -1.726  1.00 33.25           C  
ANISOU  753  CG2 ILE A 143     5468   4221   2944    303    304     27       C  
ATOM    754  CD1 ILE A 143     -27.836 -15.662   0.454  1.00 26.15           C  
ANISOU  754  CD1 ILE A 143     4665   3327   1943    251    301     81       C  
ATOM    755  N   TRP A 144     -26.763 -11.965  -3.643  1.00 38.78           N  
ANISOU  755  N   TRP A 144     6090   4920   3724    384    256    170       N  
ATOM    756  CA  TRP A 144     -27.092 -10.696  -4.278  1.00 36.22           C  
ANISOU  756  CA  TRP A 144     5730   4577   3454    397    245    187       C  
ATOM    757  C   TRP A 144     -26.703 -10.662  -5.753  1.00 39.26           C  
ANISOU  757  C   TRP A 144     6119   4979   3818    442    256    257       C  
ATOM    758  O   TRP A 144     -27.309  -9.931  -6.536  1.00 51.92           O  
ANISOU  758  O   TRP A 144     7714   6575   5437    462    239    278       O  
ATOM    759  CB  TRP A 144     -26.424  -9.543  -3.532  1.00 34.33           C  
ANISOU  759  CB  TRP A 144     5449   4305   3289    374    230    192       C  
ATOM    760  CG  TRP A 144     -27.232  -9.054  -2.373  1.00 38.70           C  
ANISOU  760  CG  TRP A 144     5992   4842   3870    336    218    107       C  
ATOM    761  CD1 TRP A 144     -27.185  -9.510  -1.087  1.00 42.09           C  
ANISOU  761  CD1 TRP A 144     6448   5286   4256    300    220     54       C  
ATOM    762  CD2 TRP A 144     -28.229  -8.022  -2.391  1.00 38.97           C  
ANISOU  762  CD2 TRP A 144     5987   4842   3976    331    207     62       C  
ATOM    763  NE1 TRP A 144     -28.081  -8.820  -0.305  1.00 46.10           N  
ANISOU  763  NE1 TRP A 144     6939   5781   4796    270    225    -30       N  
ATOM    764  CE2 TRP A 144     -28.733  -7.901  -1.086  1.00 48.07           C  
ANISOU  764  CE2 TRP A 144     7139   5995   5130    290    216    -32       C  
ATOM    765  CE3 TRP A 144     -28.734  -7.186  -3.395  1.00 38.36           C  
ANISOU  765  CE3 TRP A 144     5877   4734   3966    360    188     95       C  
ATOM    766  CZ2 TRP A 144     -29.724  -6.977  -0.748  1.00 49.17           C  
ANISOU  766  CZ2 TRP A 144     7232   6099   5349    276    214   -110       C  
ATOM    767  CZ3 TRP A 144     -29.718  -6.270  -3.058  1.00 41.15           C  
ANISOU  767  CZ3 TRP A 144     6184   5043   4408    349    170     28       C  
ATOM    768  CH2 TRP A 144     -30.202  -6.173  -1.748  1.00 42.66           C  
ANISOU  768  CH2 TRP A 144     6363   5233   4615    307    188    -81       C  
ATOM    769  N   HIS A 145     -25.697 -11.443  -6.134  1.00 30.32           N  
ANISOU  769  N   HIS A 145     5001   3871   2649    459    283    294       N  
ATOM    770  CA  HIS A 145     -25.323 -11.547  -7.542  1.00 30.93           C  
ANISOU  770  CA  HIS A 145     5092   3979   2683    500    311    350       C  
ATOM    771  C   HIS A 145     -26.478 -12.127  -8.356  1.00 36.06           C  
ANISOU  771  C   HIS A 145     5780   4659   3264    527    293    311       C  
ATOM    772  O   HIS A 145     -26.773 -11.655  -9.453  1.00 41.85           O  
ANISOU  772  O   HIS A 145     6530   5412   3961    558    285    350       O  
ATOM    773  CB  HIS A 145     -24.070 -12.410  -7.721  1.00 28.45           C  
ANISOU  773  CB  HIS A 145     4776   3682   2353    513    353    371       C  
ATOM    774  CG  HIS A 145     -22.791 -11.633  -7.736  1.00 40.60           C  
ANISOU  774  CG  HIS A 145     6267   5198   3960    507    384    435       C  
ATOM    775  ND1 HIS A 145     -22.110 -11.293  -6.583  1.00 45.92           N  
ANISOU  775  ND1 HIS A 145     6899   5832   4715    477    359    427       N  
ATOM    776  CD2 HIS A 145     -22.059 -11.137  -8.761  1.00 49.34           C  
ANISOU  776  CD2 HIS A 145     7359   6316   5071    526    439    507       C  
ATOM    777  CE1 HIS A 145     -21.020 -10.620  -6.901  1.00 48.65           C  
ANISOU  777  CE1 HIS A 145     7194   6157   5132    477    393    484       C  
ATOM    778  NE2 HIS A 145     -20.965 -10.510  -8.217  1.00 50.98           N  
ANISOU  778  NE2 HIS A 145     7505   6482   5384    504    452    539       N  
ATOM    779  N   LEU A 146     -27.133 -13.145  -7.806  1.00 38.00           N  
ANISOU  779  N   LEU A 146     6040   4904   3495    515    281    238       N  
ATOM    780  CA  LEU A 146     -28.248 -13.795  -8.487  1.00 41.23           C  
ANISOU  780  CA  LEU A 146     6471   5331   3862    537    256    183       C  
ATOM    781  C   LEU A 146     -29.459 -12.882  -8.570  1.00 35.54           C  
ANISOU  781  C   LEU A 146     5734   4591   3180    536    209    161       C  
ATOM    782  O   LEU A 146     -30.213 -12.918  -9.543  1.00 29.83           O  
ANISOU  782  O   LEU A 146     5023   3886   2424    570    169    145       O  
ATOM    783  CB  LEU A 146     -28.630 -15.092  -7.778  1.00 44.21           C  
ANISOU  783  CB  LEU A 146     6856   5696   4245    515    263    114       C  
ATOM    784  CG  LEU A 146     -27.573 -16.193  -7.782  1.00 39.35           C  
ANISOU  784  CG  LEU A 146     6254   5089   3609    525    295    125       C  
ATOM    785  CD1 LEU A 146     -28.176 -17.475  -7.263  1.00 33.50           C  
ANISOU  785  CD1 LEU A 146     5523   4323   2884    507    294     64       C  
ATOM    786  CD2 LEU A 146     -27.025 -16.391  -9.181  1.00 26.63           C  
ANISOU  786  CD2 LEU A 146     4656   3521   1939    575    312    143       C  
ATOM    787  N   CYS A 147     -29.644 -12.072  -7.536  1.00 38.76           N  
ANISOU  787  N   CYS A 147     6107   4959   3659    498    206    152       N  
ATOM    788  CA  CYS A 147     -30.729 -11.107  -7.509  1.00 36.12           C  
ANISOU  788  CA  CYS A 147     5741   4592   3392    496    164    124       C  
ATOM    789  C   CYS A 147     -30.563 -10.128  -8.665  1.00 41.24           C  
ANISOU  789  C   CYS A 147     6393   5242   4035    537    131    205       C  
ATOM    790  O   CYS A 147     -31.507  -9.855  -9.408  1.00 47.13           O  
ANISOU  790  O   CYS A 147     7138   5984   4786    567     73    195       O  
ATOM    791  CB  CYS A 147     -30.756 -10.369  -6.168  1.00 27.08           C  
ANISOU  791  CB  CYS A 147     4558   3408   2325    449    179     91       C  
ATOM    792  SG  CYS A 147     -32.032  -9.096  -6.024  1.00 46.05           S  
ANISOU  792  SG  CYS A 147     6899   5754   4842    445    135     40       S  
ATOM    793  N   ALA A 148     -29.344  -9.624  -8.821  1.00 42.17           N  
ANISOU  793  N   ALA A 148     6514   5363   4146    538    165    291       N  
ATOM    794  CA  ALA A 148     -29.036  -8.668  -9.876  1.00 48.26           C  
ANISOU  794  CA  ALA A 148     7294   6132   4911    568    152    393       C  
ATOM    795  C   ALA A 148     -29.192  -9.290 -11.260  1.00 47.79           C  
ANISOU  795  C   ALA A 148     7295   6134   4728    617    140    421       C  
ATOM    796  O   ALA A 148     -29.749  -8.668 -12.164  1.00 64.16           O  
ANISOU  796  O   ALA A 148     9389   8208   6779    651     88    469       O  
ATOM    797  CB  ALA A 148     -27.630  -8.123  -9.697  1.00 51.01           C  
ANISOU  797  CB  ALA A 148     7623   6465   5292    551    208    472       C  
ATOM    798  N   ILE A 149     -28.693 -10.513 -11.417  1.00 38.23           N  
ANISOU  798  N   ILE A 149     6113   4973   3437    624    183    387       N  
ATOM    799  CA  ILE A 149     -28.821 -11.243 -12.676  1.00 36.88           C  
ANISOU  799  CA  ILE A 149     6001   4870   3142    670    176    385       C  
ATOM    800  C   ILE A 149     -30.286 -11.406 -13.076  1.00 38.58           C  
ANISOU  800  C   ILE A 149     6226   5086   3347    696     83    316       C  
ATOM    801  O   ILE A 149     -30.645 -11.204 -14.234  1.00 48.80           O  
ANISOU  801  O   ILE A 149     7567   6420   4557    741     34    348       O  
ATOM    802  CB  ILE A 149     -28.149 -12.627 -12.589  1.00 40.27           C  
ANISOU  802  CB  ILE A 149     6443   5335   3524    670    232    329       C  
ATOM    803  CG1 ILE A 149     -26.626 -12.471 -12.618  1.00 36.50           C  
ANISOU  803  CG1 ILE A 149     5957   4867   3045    662    318    403       C  
ATOM    804  CG2 ILE A 149     -28.613 -13.529 -13.725  1.00 43.42           C  
ANISOU  804  CG2 ILE A 149     6892   5796   3810    716    207    276       C  
ATOM    805  CD1 ILE A 149     -25.869 -13.781 -12.543  1.00 37.49           C  
ANISOU  805  CD1 ILE A 149     6082   5015   3147    666    370    351       C  
ATOM    806  N   SER A 150     -31.128 -11.754 -12.107  1.00 40.23           N  
ANISOU  806  N   SER A 150     6390   5252   3644    666     58    222       N  
ATOM    807  CA  SER A 150     -32.565 -11.868 -12.339  1.00 38.45           C  
ANISOU  807  CA  SER A 150     6148   5011   3450    684    -28    143       C  
ATOM    808  C   SER A 150     -33.147 -10.566 -12.880  1.00 51.29           C  
ANISOU  808  C   SER A 150     7766   6610   5111    711   -105    202       C  
ATOM    809  O   SER A 150     -33.921 -10.573 -13.837  1.00 62.13           O  
ANISOU  809  O   SER A 150     9163   8003   6441    756   -193    190       O  
ATOM    810  CB  SER A 150     -33.288 -12.259 -11.049  1.00 30.95           C  
ANISOU  810  CB  SER A 150     5141   4008   2611    635    -13     44       C  
ATOM    811  OG  SER A 150     -32.668 -13.370 -10.436  1.00 35.58           O  
ANISOU  811  OG  SER A 150     5738   4608   3174    606     56     14       O  
ATOM    812  N   VAL A 151     -32.772  -9.453 -12.259  1.00 45.55           N  
ANISOU  812  N   VAL A 151     7005   5832   4470    684    -82    264       N  
ATOM    813  CA  VAL A 151     -33.262  -8.141 -12.665  1.00 49.40           C  
ANISOU  813  CA  VAL A 151     7475   6273   5022    706   -154    329       C  
ATOM    814  C   VAL A 151     -32.801  -7.806 -14.083  1.00 53.29           C  
ANISOU  814  C   VAL A 151     8044   6814   5389    756   -179    453       C  
ATOM    815  O   VAL A 151     -33.563  -7.254 -14.878  1.00 59.61           O  
ANISOU  815  O   VAL A 151     8861   7603   6183    798   -279    489       O  
ATOM    816  CB  VAL A 151     -32.795  -7.043 -11.681  1.00 46.72           C  
ANISOU  816  CB  VAL A 151     7077   5862   4811    664   -115    364       C  
ATOM    817  CG1 VAL A 151     -33.152  -5.655 -12.194  1.00 30.80           C  
ANISOU  817  CG1 VAL A 151     5042   3785   2876    690   -186    450       C  
ATOM    818  CG2 VAL A 151     -33.400  -7.279 -10.306  1.00 41.99           C  
ANISOU  818  CG2 VAL A 151     6413   5224   4318    617    -94    237       C  
ATOM    819  N   ASP A 152     -31.560  -8.159 -14.401  1.00 50.56           N  
ANISOU  819  N   ASP A 152     7745   6523   4941    751    -89    518       N  
ATOM    820  CA  ASP A 152     -31.014  -7.914 -15.731  1.00 57.19           C  
ANISOU  820  CA  ASP A 152     8666   7422   5640    791    -81    636       C  
ATOM    821  C   ASP A 152     -31.780  -8.667 -16.810  1.00 54.30           C  
ANISOU  821  C   ASP A 152     8366   7128   5136    846   -161    587       C  
ATOM    822  O   ASP A 152     -32.062  -8.123 -17.878  1.00 64.92           O  
ANISOU  822  O   ASP A 152     9774   8501   6393    891   -228    672       O  
ATOM    823  CB  ASP A 152     -29.536  -8.304 -15.786  1.00 71.09           C  
ANISOU  823  CB  ASP A 152    10448   9227   7334    772     50    686       C  
ATOM    824  CG  ASP A 152     -28.625  -7.227 -15.227  1.00103.32           C  
ANISOU  824  CG  ASP A 152    14483  13244  11529    733    115    784       C  
ATOM    825  OD1 ASP A 152     -28.998  -6.036 -15.279  1.00119.11           O  
ANISOU  825  OD1 ASP A 152    16463  15180  13613    734     64    860       O  
ATOM    826  OD2 ASP A 152     -27.529  -7.575 -14.738  1.00112.81           O  
ANISOU  826  OD2 ASP A 152    15660  14452  12750    702    210    781       O  
ATOM    827  N   ARG A 153     -32.116  -9.918 -16.526  1.00 44.26           N  
ANISOU  827  N   ARG A 153     7082   5885   3848    843   -160    451       N  
ATOM    828  CA  ARG A 153     -32.830 -10.741 -17.488  1.00 45.07           C  
ANISOU  828  CA  ARG A 153     7237   6053   3836    893   -240    376       C  
ATOM    829  C   ARG A 153     -34.224 -10.179 -17.734  1.00 47.50           C  
ANISOU  829  C   ARG A 153     7522   6317   4209    924   -391    350       C  
ATOM    830  O   ARG A 153     -34.702 -10.155 -18.866  1.00 59.65           O  
ANISOU  830  O   ARG A 153     9125   7906   5632    981   -489    366       O  
ATOM    831  CB  ARG A 153     -32.894 -12.190 -17.005  1.00 36.47           C  
ANISOU  831  CB  ARG A 153     6121   4978   2760    876   -203    231       C  
ATOM    832  CG  ARG A 153     -31.520 -12.834 -16.856  1.00 51.29           C  
ANISOU  832  CG  ARG A 153     8015   6893   4579    855    -70    250       C  
ATOM    833  CD  ARG A 153     -30.979 -13.399 -18.171  1.00 68.73           C  
ANISOU  833  CD  ARG A 153    10310   9204   6602    902    -45    257       C  
ATOM    834  NE  ARG A 153     -30.790 -12.394 -19.219  1.00 78.50           N  
ANISOU  834  NE  ARG A 153    11620  10487   7719    936    -63    387       N  
ATOM    835  CZ  ARG A 153     -29.741 -11.583 -19.305  1.00 79.49           C  
ANISOU  835  CZ  ARG A 153    11762  10615   7827    919     32    525       C  
ATOM    836  NH1 ARG A 153     -28.775 -11.644 -18.399  1.00 82.58           N  
ANISOU  836  NH1 ARG A 153    12094  10965   8318    871    139    538       N  
ATOM    837  NH2 ARG A 153     -29.659 -10.707 -20.299  1.00 71.98           N  
ANISOU  837  NH2 ARG A 153    10885   9701   6763    948     16    654       N  
ATOM    838  N   TYR A 154     -34.865  -9.702 -16.674  1.00 51.11           N  
ANISOU  838  N   TYR A 154     7887   6681   4850    889   -412    306       N  
ATOM    839  CA  TYR A 154     -36.174  -9.076 -16.812  1.00 51.81           C  
ANISOU  839  CA  TYR A 154     7933   6712   5042    917   -551    276       C  
ATOM    840  C   TYR A 154     -36.077  -7.781 -17.617  1.00 50.50           C  
ANISOU  840  C   TYR A 154     7812   6532   4843    955   -619    433       C  
ATOM    841  O   TYR A 154     -36.914  -7.516 -18.478  1.00 54.29           O  
ANISOU  841  O   TYR A 154     8319   7016   5292   1011   -760    445       O  
ATOM    842  CB  TYR A 154     -36.791  -8.804 -15.440  1.00 42.64           C  
ANISOU  842  CB  TYR A 154     6657   5454   4091    866   -531    190       C  
ATOM    843  CG  TYR A 154     -38.024  -7.937 -15.500  1.00 34.93           C  
ANISOU  843  CG  TYR A 154     5615   4399   3258    892   -660    167       C  
ATOM    844  CD1 TYR A 154     -39.196  -8.402 -16.083  1.00 36.26           C  
ANISOU  844  CD1 TYR A 154     5765   4569   3444    935   -788     72       C  
ATOM    845  CD2 TYR A 154     -38.017  -6.651 -14.976  1.00 33.81           C  
ANISOU  845  CD2 TYR A 154     5420   4174   3253    876   -661    231       C  
ATOM    846  CE1 TYR A 154     -40.330  -7.607 -16.144  1.00 40.84           C  
ANISOU  846  CE1 TYR A 154     6271   5067   4177    963   -917     46       C  
ATOM    847  CE2 TYR A 154     -39.145  -5.850 -15.030  1.00 35.97           C  
ANISOU  847  CE2 TYR A 154     5622   4364   3681    904   -783    204       C  
ATOM    848  CZ  TYR A 154     -40.296  -6.333 -15.614  1.00 41.54           C  
ANISOU  848  CZ  TYR A 154     6308   5072   4405    948   -911    114       C  
ATOM    849  OH  TYR A 154     -41.414  -5.535 -15.668  1.00 51.54           O  
ANISOU  849  OH  TYR A 154     7491   6246   5846    979  -1041     82       O  
ATOM    850  N   ILE A 155     -35.053  -6.982 -17.330  1.00 50.09           N  
ANISOU  850  N   ILE A 155     7767   6458   4807    925   -525    556       N  
ATOM    851  CA  ILE A 155     -34.798  -5.747 -18.068  1.00 51.58           C  
ANISOU  851  CA  ILE A 155     8002   6624   4973    952   -565    729       C  
ATOM    852  C   ILE A 155     -34.524  -6.051 -19.543  1.00 56.60           C  
ANISOU  852  C   ILE A 155     8769   7368   5370   1007   -595    815       C  
ATOM    853  O   ILE A 155     -35.005  -5.349 -20.433  1.00 61.53           O  
ANISOU  853  O   ILE A 155     9446   7986   5944   1056   -710    914       O  
ATOM    854  CB  ILE A 155     -33.611  -4.965 -17.449  1.00 56.60           C  
ANISOU  854  CB  ILE A 155     8611   7213   5680    901   -437    834       C  
ATOM    855  CG1 ILE A 155     -34.036  -4.327 -16.123  1.00 59.70           C  
ANISOU  855  CG1 ILE A 155     8883   7492   6308    859   -441    763       C  
ATOM    856  CG2 ILE A 155     -33.100  -3.891 -18.400  1.00 54.85           C  
ANISOU  856  CG2 ILE A 155     8457   6983   5399    925   -445   1035       C  
ATOM    857  CD1 ILE A 155     -32.907  -3.646 -15.377  1.00 56.76           C  
ANISOU  857  CD1 ILE A 155     8472   7071   6023    807   -327    830       C  
ATOM    858  N   ALA A 156     -33.768  -7.117 -19.792  1.00 55.96           N  
ANISOU  858  N   ALA A 156     8739   7383   5140   1000   -496    771       N  
ATOM    859  CA  ALA A 156     -33.449  -7.544 -21.152  1.00 49.48           C  
ANISOU  859  CA  ALA A 156     8045   6681   4074   1049   -502    823       C  
ATOM    860  C   ALA A 156     -34.696  -7.975 -21.923  1.00 55.52           C  
ANISOU  860  C   ALA A 156     8846   7483   4764   1112   -678    736       C  
ATOM    861  O   ALA A 156     -34.742  -7.878 -23.150  1.00 65.34           O  
ANISOU  861  O   ALA A 156    10204   8808   5813   1166   -744    810       O  
ATOM    862  CB  ALA A 156     -32.437  -8.674 -21.121  1.00 37.71           C  
ANISOU  862  CB  ALA A 156     6577   5271   2478   1027   -356    758       C  
ATOM    863  N   ILE A 157     -35.702  -8.458 -21.202  1.00 51.17           N  
ANISOU  863  N   ILE A 157     8199   6874   4368   1105   -755    577       N  
ATOM    864  CA  ILE A 157     -36.960  -8.857 -21.819  1.00 51.38           C  
ANISOU  864  CA  ILE A 157     8233   6917   4374   1162   -934    474       C  
ATOM    865  C   ILE A 157     -37.837  -7.644 -22.097  1.00 64.93           C  
ANISOU  865  C   ILE A 157     9933   8557   6180   1199  -1094    562       C  
ATOM    866  O   ILE A 157     -38.315  -7.455 -23.218  1.00 71.18           O  
ANISOU  866  O   ILE A 157    10809   9396   6839   1266  -1238    609       O  
ATOM    867  CB  ILE A 157     -37.735  -9.847 -20.934  1.00 49.03           C  
ANISOU  867  CB  ILE A 157     7823   6573   4232   1134   -945    270       C  
ATOM    868  CG1 ILE A 157     -37.002 -11.186 -20.871  1.00 51.75           C  
ANISOU  868  CG1 ILE A 157     8192   6992   4478   1112   -823    177       C  
ATOM    869  CG2 ILE A 157     -39.151 -10.045 -21.464  1.00 53.65           C  
ANISOU  869  CG2 ILE A 157     8381   7143   4860   1189  -1144    162       C  
ATOM    870  CD1 ILE A 157     -37.705 -12.227 -20.027  1.00 56.84           C  
ANISOU  870  CD1 ILE A 157     8736   7587   5273   1081   -822     -8       C  
ATOM    871  N   LYS A 158     -38.039  -6.825 -21.070  1.00 69.25           N  
ANISOU  871  N   LYS A 158    10373   8984   6955   1159  -1073    579       N  
ATOM    872  CA  LYS A 158     -38.883  -5.642 -21.179  1.00 65.00           C  
ANISOU  872  CA  LYS A 158     9793   8347   6556   1191  -1219    649       C  
ATOM    873  C   LYS A 158     -38.329  -4.650 -22.196  1.00 54.61           C  
ANISOU  873  C   LYS A 158     8594   7054   5100   1228  -1252    874       C  
ATOM    874  O   LYS A 158     -39.035  -4.232 -23.111  1.00 55.87           O  
ANISOU  874  O   LYS A 158     8808   7216   5204   1295  -1427    935       O  
ATOM    875  CB  LYS A 158     -39.035  -4.966 -19.814  1.00 58.73           C  
ANISOU  875  CB  LYS A 158     8860   7424   6031   1134  -1158    614       C  
ATOM    876  N   LYS A 159     -37.062  -4.285 -22.036  1.00 51.82           N  
ANISOU  876  N   LYS A 159     8279   6716   4694   1185  -1085   1000       N  
ATOM    877  CA  LYS A 159     -36.434  -3.305 -22.914  1.00 58.24           C  
ANISOU  877  CA  LYS A 159     9197   7539   5392   1206  -1081   1230       C  
ATOM    878  C   LYS A 159     -35.224  -3.881 -23.641  1.00 61.13           C  
ANISOU  878  C   LYS A 159     9688   8041   5496   1198   -933   1304       C  
ATOM    879  O   LYS A 159     -34.086  -3.667 -23.224  1.00 59.42           O  
ANISOU  879  O   LYS A 159     9459   7816   5301   1143   -759   1374       O  
ATOM    880  CB  LYS A 159     -36.020  -2.067 -22.114  1.00 57.76           C  
ANISOU  880  CB  LYS A 159     9052   7344   5551   1159  -1017   1338       C  
ATOM    881  N   PRO A 160     -35.464  -4.612 -24.741  1.00 66.76           N  
ANISOU  881  N   PRO A 160    10519   8881   5967   1253  -1004   1276       N  
ATOM    882  CA  PRO A 160     -34.368  -5.179 -25.531  1.00 69.86           C  
ANISOU  882  CA  PRO A 160    11034   9412   6096   1252   -861   1331       C  
ATOM    883  C   PRO A 160     -33.597  -4.097 -26.275  1.00 78.80           C  
ANISOU  883  C   PRO A 160    12269  10552   7119   1252   -798   1587       C  
ATOM    884  O   PRO A 160     -32.467  -4.321 -26.706  1.00 79.79           O  
ANISOU  884  O   PRO A 160    12436  10760   7120   1207   -620   1643       O  
ATOM    885  CB  PRO A 160     -35.086  -6.110 -26.506  1.00 60.36           C  
ANISOU  885  CB  PRO A 160     9922   8328   4685   1320   -995   1218       C  
ATOM    886  CG  PRO A 160     -36.430  -5.500 -26.666  1.00 60.44           C  
ANISOU  886  CG  PRO A 160     9905   8260   4798   1372  -1234   1221       C  
ATOM    887  CD  PRO A 160     -36.779  -4.936 -25.318  1.00 67.25           C  
ANISOU  887  CD  PRO A 160    10598   8961   5993   1323  -1225   1180       C  
ATOM    888  N   ILE A 161     -34.213  -2.930 -26.421  1.00 84.91           N  
ANISOU  888  N   ILE A 161    13041  11228   7994   1276   -932   1724       N  
ATOM    889  CA  ILE A 161     -33.542  -1.784 -27.015  1.00 93.09           C  
ANISOU  889  CA  ILE A 161    14135  12237   8997   1254   -870   1974       C  
ATOM    890  C   ILE A 161     -32.565  -1.164 -26.025  1.00 98.70           C  
ANISOU  890  C   ILE A 161    14761  12841   9900   1189   -696   2047       C  
ATOM    891  O   ILE A 161     -32.763  -0.042 -25.562  1.00106.97           O  
ANISOU  891  O   ILE A 161    15733  13743  11166   1174   -742   2145       O  
ATOM    892  CB  ILE A 161     -34.544  -0.712 -27.470  1.00103.28           C  
ANISOU  892  CB  ILE A 161    15442  13438  10362   1303  -1085   2103       C  
ATOM    893  N   GLN A 162     -31.515  -1.905 -25.695  1.00105.20           N  
ANISOU  893  N   GLN A 162    15568  13731  10674   1141   -500   1977       N  
ATOM    894  CA  GLN A 162     -30.481  -1.401 -24.809  1.00113.74           C  
ANISOU  894  CA  GLN A 162    16549  14724  11943   1067   -330   2025       C  
ATOM    895  C   GLN A 162     -29.117  -1.865 -25.310  1.00127.31           C  
ANISOU  895  C   GLN A 162    18332  16549  13490   1034   -116   2081       C  
ATOM    896  O   GLN A 162     -28.343  -2.491 -24.580  1.00112.49           O  
ANISOU  896  O   GLN A 162    16380  14681  11680    991     20   1973       O  
ATOM    897  CB  GLN A 162     -30.729  -1.860 -23.371  1.00104.33           C  
ANISOU  897  CB  GLN A 162    15200  13459  10980   1029   -330   1819       C  
ATOM    898  CG  GLN A 162     -29.968  -1.044 -22.339  1.00107.34           C  
ANISOU  898  CG  GLN A 162    15464  13716  11605    962   -223   1865       C  
ATOM    899  CD  GLN A 162     -30.404  -1.339 -20.923  1.00114.34           C  
ANISOU  899  CD  GLN A 162    16210  14528  12706    930   -252   1673       C  
ATOM    900  OE1 GLN A 162     -29.868  -2.234 -20.269  1.00122.63           O  
ANISOU  900  OE1 GLN A 162    17219  15622  13755    897   -155   1546       O  
ATOM    901  NE2 GLN A 162     -31.380  -0.579 -20.436  1.00115.16           N  
ANISOU  901  NE2 GLN A 162    16240  14518  12998    941   -385   1652       N  
ATOM    902  N   ALA A 163     -28.832  -1.547 -26.569  1.00147.28           N  
ANISOU  902  N   ALA A 163    20936  19152  15871   1011    -95   2202       N  
ATOM    903  CA  ALA A 163     -27.616  -2.009 -27.219  1.00155.76           C  
ANISOU  903  CA  ALA A 163    22035  20333  16813    952     99   2212       C  
ATOM    904  C   ALA A 163     -26.471  -1.023 -27.015  1.00160.55           C  
ANISOU  904  C   ALA A 163    22600  20852  17549    888    263   2385       C  
ATOM    905  O   ALA A 163     -26.360  -0.018 -27.736  1.00168.06           O  
ANISOU  905  O   ALA A 163    23598  21771  18487    863    258   2575       O  
ATOM    906  CB  ALA A 163     -27.862  -2.223 -28.695  1.00163.22           C  
ANISOU  906  CB  ALA A 163    23090  21411  17515    957     49   2245       C  
ATOM    907  N   ASN A 164     -25.644  -1.319 -26.014  1.00153.82           N  
ANISOU  907  N   ASN A 164    21658  19956  16831    862    402   2318       N  
ATOM    908  CA  ASN A 164     -24.450  -0.548 -25.656  1.00144.11           C  
ANISOU  908  CA  ASN A 164    20362  18638  15754    802    574   2446       C  
ATOM    909  C   ASN A 164     -24.736   0.873 -25.191  1.00149.90           C  
ANISOU  909  C   ASN A 164    21054  19201  16701    798    509   2612       C  
ATOM    910  O   ASN A 164     -23.819   1.595 -24.796  1.00144.07           O  
ANISOU  910  O   ASN A 164    20244  18366  16132    749    638   2715       O  
ATOM    911  CB  ASN A 164     -23.462  -0.505 -26.820  1.00128.96           C  
ANISOU  911  CB  ASN A 164    18497  16809  13693    748    728   2539       C  
ATOM    912  N   GLN A 165     -25.998   1.280 -25.257  1.00156.17           N  
ANISOU  912  N   GLN A 165    21883  19950  17504    853    308   2633       N  
ATOM    913  CA  GLN A 165     -26.429   2.510 -24.614  1.00167.40           C  
ANISOU  913  CA  GLN A 165    23238  21192  19173    860    221   2741       C  
ATOM    914  C   GLN A 165     -26.273   2.316 -23.109  1.00147.81           C  
ANISOU  914  C   GLN A 165    20583  18625  16952    815    234   2547       C  
ATOM    915  O   GLN A 165     -25.832   3.209 -22.385  1.00147.25           O  
ANISOU  915  O   GLN A 165    20399  18414  17133    768    273   2591       O  
ATOM    916  CB  GLN A 165     -27.874   2.839 -24.981  1.00181.32           C  
ANISOU  916  CB  GLN A 165    25055  22929  20910    928    -15   2759       C  
ATOM    917  N   TYR A 166     -26.655   1.125 -22.662  1.00148.02           N  
ANISOU  917  N   TYR A 166    20594  18739  16910    832    197   2330       N  
ATOM    918  CA  TYR A 166     -26.389   0.626 -21.321  1.00127.70           C  
ANISOU  918  CA  TYR A 166    17886  16126  14507    791    233   2139       C  
ATOM    919  C   TYR A 166     -26.192  -0.874 -21.486  1.00123.17           C  
ANISOU  919  C   TYR A 166    17360  15702  13738    806    287   1992       C  
ATOM    920  O   TYR A 166     -26.186  -1.369 -22.616  1.00128.28           O  
ANISOU  920  O   TYR A 166    18131  16468  14140    844    308   2041       O  
ATOM    921  CB  TYR A 166     -27.530   0.945 -20.350  1.00108.10           C  
ANISOU  921  CB  TYR A 166    15311  13544  12220    800     72   2016       C  
ATOM    922  N   ASN A 167     -26.060  -1.593 -20.375  1.00123.65           N  
ANISOU  922  N   ASN A 167    17326  15754  13903    780    304   1811       N  
ATOM    923  CA  ASN A 167     -25.669  -2.999 -20.403  1.00116.40           C  
ANISOU  923  CA  ASN A 167    16431  14951  12845    785    374   1677       C  
ATOM    924  C   ASN A 167     -24.374  -3.160 -21.195  1.00113.37           C  
ANISOU  924  C   ASN A 167    16096  14637  12341    770    552   1777       C  
ATOM    925  O   ASN A 167     -24.259  -4.031 -22.058  1.00119.90           O  
ANISOU  925  O   ASN A 167    17015  15591  12953    802    597   1749       O  
ATOM    926  CB  ASN A 167     -26.780  -3.873 -20.994  1.00119.23           C  
ANISOU  926  CB  ASN A 167    16872  15402  13026    844    255   1580       C  
ATOM    927  N   SER A 168     -23.411  -2.292 -20.898  1.00100.47           N  
ANISOU  927  N   SER A 168    14394  12918  10860    721    657   1887       N  
ATOM    928  CA  SER A 168     -22.118  -2.296 -21.569  1.00 80.82           C  
ANISOU  928  CA  SER A 168    11928  10476   8305    696    846   1990       C  
ATOM    929  C   SER A 168     -21.038  -2.784 -20.616  1.00 65.66           C  
ANISOU  929  C   SER A 168     9886   8525   6538    651    950   1883       C  
ATOM    930  O   SER A 168     -21.321  -3.507 -19.664  1.00 62.08           O  
ANISOU  930  O   SER A 168     9373   8065   6151    652    880   1716       O  
ATOM    931  CB  SER A 168     -21.771  -0.897 -22.075  1.00 82.83           C  
ANISOU  931  CB  SER A 168    12194  10647   8630    672    898   2215       C  
ATOM    932  OG  SER A 168     -22.816  -0.374 -22.874  1.00 90.35           O  
ANISOU  932  OG  SER A 168    13256  11611   9461    717    774   2324       O  
ATOM    933  N   ARG A 169     -19.799  -2.378 -20.868  1.00 60.46           N  
ANISOU  933  N   ARG A 169     9188   7843   5942    611   1115   1985       N  
ATOM    934  CA  ARG A 169     -18.702  -2.718 -19.972  1.00 52.65           C  
ANISOU  934  CA  ARG A 169     8069   6809   5128    569   1202   1895       C  
ATOM    935  C   ARG A 169     -18.741  -1.839 -18.728  1.00 61.47           C  
ANISOU  935  C   ARG A 169     9063   7779   6515    531   1119   1876       C  
ATOM    936  O   ARG A 169     -18.430  -2.289 -17.624  1.00 67.39           O  
ANISOU  936  O   ARG A 169     9718   8495   7391    513   1089   1738       O  
ATOM    937  CB  ARG A 169     -17.357  -2.574 -20.683  1.00 59.11           C  
ANISOU  937  CB  ARG A 169     8871   7646   5944    539   1412   2000       C  
ATOM    938  CG  ARG A 169     -16.151  -2.674 -19.764  1.00 71.66           C  
ANISOU  938  CG  ARG A 169    10304   9159   7763    492   1493   1929       C  
ATOM    939  CD  ARG A 169     -14.889  -2.999 -20.543  1.00 86.01           C  
ANISOU  939  CD  ARG A 169    12107  11030   9542    474   1709   1976       C  
ATOM    940  NE  ARG A 169     -14.844  -4.391 -20.985  1.00100.49           N  
ANISOU  940  NE  ARG A 169    13998  12997  11186    514   1749   1850       N  
ATOM    941  CZ  ARG A 169     -15.075  -4.798 -22.230  1.00 95.53           C  
ANISOU  941  CZ  ARG A 169    13505  12497  10297    548   1823   1892       C  
ATOM    942  NH1 ARG A 169     -15.381  -3.921 -23.177  1.00 93.17           N  
ANISOU  942  NH1 ARG A 169    13309  12216   9874    547   1861   2074       N  
ATOM    943  NH2 ARG A 169     -15.002  -6.088 -22.527  1.00 92.91           N  
ANISOU  943  NH2 ARG A 169    13206  12272   9824    584   1853   1751       N  
ATOM    944  N   ALA A 170     -19.128  -0.582 -18.917  1.00 58.24           N  
ANISOU  944  N   ALA A 170     8659   7282   6190    521   1078   2014       N  
ATOM    945  CA  ALA A 170     -19.267   0.355 -17.811  1.00 42.94           C  
ANISOU  945  CA  ALA A 170     6607   5199   4509    488    992   1990       C  
ATOM    946  C   ALA A 170     -20.408  -0.059 -16.898  1.00 40.01           C  
ANISOU  946  C   ALA A 170     6228   4829   4145    513    826   1826       C  
ATOM    947  O   ALA A 170     -20.262  -0.057 -15.677  1.00 60.74           O  
ANISOU  947  O   ALA A 170     8755   7394   6931    487    781   1705       O  
ATOM    948  CB  ALA A 170     -19.489   1.767 -18.328  1.00 47.69           C  
ANISOU  948  CB  ALA A 170     7219   5700   5203    477    983   2179       C  
ATOM    949  N   THR A 171     -21.544  -0.417 -17.488  1.00 39.97           N  
ANISOU  949  N   THR A 171     6328   4894   3966    562    736   1820       N  
ATOM    950  CA  THR A 171     -22.686  -0.871 -16.703  1.00 50.77           C  
ANISOU  950  CA  THR A 171     7686   6265   5339    583    593   1664       C  
ATOM    951  C   THR A 171     -22.315  -2.115 -15.909  1.00 53.22           C  
ANISOU  951  C   THR A 171     7962   6634   5625    574    616   1496       C  
ATOM    952  O   THR A 171     -22.675  -2.236 -14.743  1.00 66.54           O  
ANISOU  952  O   THR A 171     9586   8279   7419    559    545   1370       O  
ATOM    953  CB  THR A 171     -23.915  -1.174 -17.581  1.00 53.60           C  
ANISOU  953  CB  THR A 171     8158   6695   5513    640    495   1678       C  
ATOM    954  OG1 THR A 171     -24.245  -0.018 -18.361  1.00 52.02           O  
ANISOU  954  OG1 THR A 171     7999   6438   5329    654    461   1852       O  
ATOM    955  CG2 THR A 171     -25.105  -1.545 -16.714  1.00 52.08           C  
ANISOU  955  CG2 THR A 171     7933   6486   5367    655    358   1516       C  
ATOM    956  N   ALA A 172     -21.573  -3.023 -16.538  1.00 44.79           N  
ANISOU  956  N   ALA A 172     6937   5661   4421    584    720   1496       N  
ATOM    957  CA  ALA A 172     -21.150  -4.256 -15.883  1.00 45.55           C  
ANISOU  957  CA  ALA A 172     7002   5805   4500    580    743   1351       C  
ATOM    958  C   ALA A 172     -20.368  -3.949 -14.612  1.00 46.03           C  
ANISOU  958  C   ALA A 172     6943   5778   4769    534    751   1297       C  
ATOM    959  O   ALA A 172     -20.653  -4.498 -13.551  1.00 45.92           O  
ANISOU  959  O   ALA A 172     6895   5755   4798    527    682   1168       O  
ATOM    960  CB  ALA A 172     -20.314  -5.109 -16.831  1.00 45.39           C  
ANISOU  960  CB  ALA A 172     7029   5882   4335    596    870   1370       C  
ATOM    961  N   PHE A 173     -19.404  -3.040 -14.720  1.00 51.15           N  
ANISOU  961  N   PHE A 173     7528   6358   5548    501    832   1399       N  
ATOM    962  CA  PHE A 173     -18.534  -2.707 -13.596  1.00 46.14           C  
ANISOU  962  CA  PHE A 173     6773   5638   5120    459    837   1347       C  
ATOM    963  C   PHE A 173     -19.254  -1.973 -12.464  1.00 48.86           C  
ANISOU  963  C   PHE A 173     7065   5896   5601    441    712   1279       C  
ATOM    964  O   PHE A 173     -18.829  -2.036 -11.309  1.00 44.58           O  
ANISOU  964  O   PHE A 173     6446   5313   5179    416    676   1180       O  
ATOM    965  CB  PHE A 173     -17.350  -1.870 -14.083  1.00 51.80           C  
ANISOU  965  CB  PHE A 173     7426   6294   5962    426    960   1474       C  
ATOM    966  CG  PHE A 173     -16.341  -2.655 -14.877  1.00 66.76           C  
ANISOU  966  CG  PHE A 173     9332   8262   7771    431   1105   1502       C  
ATOM    967  CD1 PHE A 173     -16.296  -4.037 -14.791  1.00 71.56           C  
ANISOU  967  CD1 PHE A 173     9970   8961   8258    459   1104   1386       C  
ATOM    968  CD2 PHE A 173     -15.441  -2.013 -15.710  1.00 77.46           C  
ANISOU  968  CD2 PHE A 173    10663   9591   9177    407   1250   1641       C  
ATOM    969  CE1 PHE A 173     -15.371  -4.763 -15.520  1.00 74.22           C  
ANISOU  969  CE1 PHE A 173    10308   9361   8532    466   1240   1395       C  
ATOM    970  CE2 PHE A 173     -14.514  -2.735 -16.442  1.00 80.36           C  
ANISOU  970  CE2 PHE A 173    11034  10029   9470    410   1399   1654       C  
ATOM    971  CZ  PHE A 173     -14.480  -4.112 -16.346  1.00 78.44           C  
ANISOU  971  CZ  PHE A 173    10816   9876   9111    442   1392   1523       C  
ATOM    972  N   ILE A 174     -20.341  -1.282 -12.786  1.00 47.54           N  
ANISOU  972  N   ILE A 174     6942   5704   5419    457    644   1326       N  
ATOM    973  CA  ILE A 174     -21.062  -0.523 -11.769  1.00 52.52           C  
ANISOU  973  CA  ILE A 174     7516   6249   6191    442    537   1254       C  
ATOM    974  C   ILE A 174     -21.846  -1.475 -10.853  1.00 52.20           C  
ANISOU  974  C   ILE A 174     7496   6263   6077    452    458   1089       C  
ATOM    975  O   ILE A 174     -21.764  -1.385  -9.632  1.00 67.73           O  
ANISOU  975  O   ILE A 174     9400   8190   8144    426    414    981       O  
ATOM    976  CB  ILE A 174     -21.999   0.524 -12.416  1.00 51.99           C  
ANISOU  976  CB  ILE A 174     7477   6124   6153    460    483   1354       C  
ATOM    977  CG1 ILE A 174     -21.176   1.573 -13.174  1.00 53.67           C  
ANISOU  977  CG1 ILE A 174     7662   6261   6467    440    565   1531       C  
ATOM    978  CG2 ILE A 174     -22.865   1.204 -11.372  1.00 37.56           C  
ANISOU  978  CG2 ILE A 174     5588   4213   4471    449    374   1252       C  
ATOM    979  CD1 ILE A 174     -22.014   2.611 -13.923  1.00 37.44           C  
ANISOU  979  CD1 ILE A 174     5644   4142   4440    460    511   1662       C  
ATOM    980  N   LYS A 175     -22.574  -2.416 -11.446  1.00 51.33           N  
ANISOU  980  N   LYS A 175     7473   6242   5787    488    444   1069       N  
ATOM    981  CA  LYS A 175     -23.351  -3.381 -10.663  1.00 58.93           C  
ANISOU  981  CA  LYS A 175     8456   7252   6684    494    383    926       C  
ATOM    982  C   LYS A 175     -22.474  -4.398  -9.935  1.00 49.91           C  
ANISOU  982  C   LYS A 175     7294   6146   5524    478    419    848       C  
ATOM    983  O   LYS A 175     -22.878  -4.932  -8.894  1.00 51.75           O  
ANISOU  983  O   LYS A 175     7520   6386   5756    465    370    735       O  
ATOM    984  CB  LYS A 175     -24.368  -4.106 -11.552  1.00 58.81           C  
ANISOU  984  CB  LYS A 175     8530   7312   6504    538    352    922       C  
ATOM    985  CG  LYS A 175     -24.717  -3.375 -12.832  1.00 75.45           C  
ANISOU  985  CG  LYS A 175    10687   9417   8565    568    346   1054       C  
ATOM    986  CD  LYS A 175     -25.901  -4.022 -13.569  1.00 84.99           C  
ANISOU  986  CD  LYS A 175    11975  10693   9626    614    279   1024       C  
ATOM    987  CE  LYS A 175     -26.977  -4.531 -12.597  1.00 89.63           C  
ANISOU  987  CE  LYS A 175    12535  11271  10249    609    200    871       C  
ATOM    988  NZ  LYS A 175     -28.308  -4.726 -13.263  1.00 92.39           N  
ANISOU  988  NZ  LYS A 175    12932  11646  10528    651    108    846       N  
ATOM    989  N   ILE A 176     -21.302  -4.691 -10.490  1.00 44.74           N  
ANISOU  989  N   ILE A 176     6631   5513   4854    478    505    910       N  
ATOM    990  CA  ILE A 176     -20.331  -5.505  -9.782  1.00 39.76           C  
ANISOU  990  CA  ILE A 176     5962   4896   4249    465    530    845       C  
ATOM    991  C   ILE A 176     -19.902  -4.794  -8.495  1.00 42.03           C  
ANISOU  991  C   ILE A 176     6165   5105   4700    426    481    794       C  
ATOM    992  O   ILE A 176     -19.924  -5.366  -7.400  1.00 41.42           O  
ANISOU  992  O   ILE A 176     6080   5035   4623    415    427    695       O  
ATOM    993  CB  ILE A 176     -19.109  -5.781 -10.664  1.00 38.91           C  
ANISOU  993  CB  ILE A 176     5841   4813   4132    471    641    920       C  
ATOM    994  CG1 ILE A 176     -19.452  -6.757 -11.796  1.00 44.41           C  
ANISOU  994  CG1 ILE A 176     6625   5603   4644    512    687    932       C  
ATOM    995  CG2 ILE A 176     -17.938  -6.302  -9.845  1.00 34.98           C  
ANISOU  995  CG2 ILE A 176     5269   4294   3729    454    653    863       C  
ATOM    996  CD1 ILE A 176     -18.343  -6.907 -12.820  1.00 49.74           C  
ANISOU  996  CD1 ILE A 176     7293   6310   5295    519    817   1008       C  
ATOM    997  N   THR A 177     -19.517  -3.534  -8.655  1.00 46.99           N  
ANISOU  997  N   THR A 177     6733   5657   5464    407    498    864       N  
ATOM    998  CA  THR A 177     -19.062  -2.710  -7.550  1.00 38.70           C  
ANISOU  998  CA  THR A 177     5594   4525   4587    372    451    812       C  
ATOM    999  C   THR A 177     -20.132  -2.579  -6.474  1.00 36.65           C  
ANISOU  999  C   THR A 177     5347   4257   4322    363    355    697       C  
ATOM   1000  O   THR A 177     -19.837  -2.697  -5.288  1.00 46.66           O  
ANISOU 1000  O   THR A 177     6581   5514   5633    343    303    598       O  
ATOM   1001  CB  THR A 177     -18.662  -1.305  -8.027  1.00 41.88           C  
ANISOU 1001  CB  THR A 177     5929   4832   5151    352    486    912       C  
ATOM   1002  OG1 THR A 177     -17.716  -1.406  -9.101  1.00 40.30           O  
ANISOU 1002  OG1 THR A 177     5723   4643   4946    356    599   1030       O  
ATOM   1003  CG2 THR A 177     -18.042  -0.523  -6.883  1.00 39.02           C  
ANISOU 1003  CG2 THR A 177     5462   4381   4985    316    435    839       C  
ATOM   1004  N   VAL A 178     -21.374  -2.352  -6.894  1.00 30.31           N  
ANISOU 1004  N   VAL A 178     4592   3462   3461    381    330    707       N  
ATOM   1005  CA  VAL A 178     -22.479  -2.146  -5.959  1.00 29.85           C  
ANISOU 1005  CA  VAL A 178     4537   3392   3413    371    257    595       C  
ATOM   1006  C   VAL A 178     -22.776  -3.388  -5.123  1.00 44.91           C  
ANISOU 1006  C   VAL A 178     6493   5373   5198    369    236    490       C  
ATOM   1007  O   VAL A 178     -22.950  -3.295  -3.905  1.00 51.51           O  
ANISOU 1007  O   VAL A 178     7311   6199   6063    344    193    385       O  
ATOM   1008  CB  VAL A 178     -23.771  -1.724  -6.695  1.00 30.02           C  
ANISOU 1008  CB  VAL A 178     4592   3403   3411    396    233    628       C  
ATOM   1009  CG1 VAL A 178     -24.982  -1.849  -5.776  1.00 29.50           C  
ANISOU 1009  CG1 VAL A 178     4532   3344   3334    389    176    496       C  
ATOM   1010  CG2 VAL A 178     -23.642  -0.308  -7.214  1.00 32.68           C  
ANISOU 1010  CG2 VAL A 178     4874   3642   3900    393    231    722       C  
ATOM   1011  N   VAL A 179     -22.837  -4.544  -5.779  1.00 43.50           N  
ANISOU 1011  N   VAL A 179     6379   5266   4883    393    268    518       N  
ATOM   1012  CA  VAL A 179     -23.128  -5.800  -5.094  1.00 48.36           C  
ANISOU 1012  CA  VAL A 179     7043   5941   5392    391    254    437       C  
ATOM   1013  C   VAL A 179     -22.102  -6.056  -3.997  1.00 45.69           C  
ANISOU 1013  C   VAL A 179     6675   5596   5091    367    234    392       C  
ATOM   1014  O   VAL A 179     -22.451  -6.465  -2.889  1.00 51.12           O  
ANISOU 1014  O   VAL A 179     7384   6300   5738    348    196    308       O  
ATOM   1015  CB  VAL A 179     -23.154  -6.994  -6.077  1.00 50.95           C  
ANISOU 1015  CB  VAL A 179     7431   6334   5594    424    294    476       C  
ATOM   1016  CG1 VAL A 179     -23.117  -8.313  -5.322  1.00 27.11           C  
ANISOU 1016  CG1 VAL A 179     4447   3355   2500    418    283    409       C  
ATOM   1017  CG2 VAL A 179     -24.392  -6.931  -6.953  1.00 27.69           C  
ANISOU 1017  CG2 VAL A 179     4527   3407   2589    449    283    488       C  
ATOM   1018  N   TRP A 180     -20.838  -5.787  -4.301  1.00 39.31           N  
ANISOU 1018  N   TRP A 180     5815   4761   4362    368    260    450       N  
ATOM   1019  CA  TRP A 180     -19.781  -5.958  -3.320  1.00 42.66           C  
ANISOU 1019  CA  TRP A 180     6197   5168   4843    351    223    408       C  
ATOM   1020  C   TRP A 180     -19.888  -4.940  -2.189  1.00 45.19           C  
ANISOU 1020  C   TRP A 180     6473   5441   5256    320    159    330       C  
ATOM   1021  O   TRP A 180     -19.631  -5.272  -1.038  1.00 46.25           O  
ANISOU 1021  O   TRP A 180     6615   5589   5368    305    100    254       O  
ATOM   1022  CB  TRP A 180     -18.411  -5.883  -3.995  1.00 29.10           C  
ANISOU 1022  CB  TRP A 180     4417   3425   3215    359    273    481       C  
ATOM   1023  CG  TRP A 180     -18.068  -7.174  -4.664  1.00 47.27           C  
ANISOU 1023  CG  TRP A 180     6757   5781   5423    388    321    512       C  
ATOM   1024  CD1 TRP A 180     -18.185  -7.468  -5.988  1.00 32.23           C  
ANISOU 1024  CD1 TRP A 180     4883   3910   3454    413    403    581       C  
ATOM   1025  CD2 TRP A 180     -17.590  -8.367  -4.029  1.00 51.24           C  
ANISOU 1025  CD2 TRP A 180     7276   6309   5883    396    286    468       C  
ATOM   1026  NE1 TRP A 180     -17.796  -8.764  -6.222  1.00 36.70           N  
ANISOU 1026  NE1 TRP A 180     5474   4519   3951    437    426    568       N  
ATOM   1027  CE2 TRP A 180     -17.426  -9.338  -5.033  1.00 41.29           C  
ANISOU 1027  CE2 TRP A 180     6044   5089   4555    427    354    505       C  
ATOM   1028  CE3 TRP A 180     -17.277  -8.704  -2.707  1.00 46.03           C  
ANISOU 1028  CE3 TRP A 180     6613   5641   5234    383    198    402       C  
ATOM   1029  CZ2 TRP A 180     -16.961 -10.623  -4.764  1.00 45.18           C  
ANISOU 1029  CZ2 TRP A 180     6549   5601   5016    445    338    477       C  
ATOM   1030  CZ3 TRP A 180     -16.817  -9.981  -2.439  1.00 43.21           C  
ANISOU 1030  CZ3 TRP A 180     6279   5305   4833    401    176    392       C  
ATOM   1031  CH2 TRP A 180     -16.662 -10.925  -3.463  1.00 43.58           C  
ANISOU 1031  CH2 TRP A 180     6341   5378   4837    432    246    428       C  
ATOM   1032  N   LEU A 181     -20.283  -3.712  -2.506  1.00 29.19           N  
ANISOU 1032  N   LEU A 181     4403   3358   3330    312    165    345       N  
ATOM   1033  CA  LEU A 181     -20.459  -2.699  -1.471  1.00 41.90           C  
ANISOU 1033  CA  LEU A 181     5963   4916   5040    284    106    253       C  
ATOM   1034  C   LEU A 181     -21.620  -3.073  -0.551  1.00 45.10           C  
ANISOU 1034  C   LEU A 181     6431   5369   5335    273     75    146       C  
ATOM   1035  O   LEU A 181     -21.550  -2.878   0.664  1.00 29.43           O  
ANISOU 1035  O   LEU A 181     4440   3387   3355    250     23     42       O  
ATOM   1036  CB  LEU A 181     -20.684  -1.320  -2.095  1.00 30.21           C  
ANISOU 1036  CB  LEU A 181     4417   3349   3711    280    122    299       C  
ATOM   1037  CG  LEU A 181     -19.457  -0.719  -2.785  1.00 30.96           C  
ANISOU 1037  CG  LEU A 181     4435   3379   3951    277    160    398       C  
ATOM   1038  CD1 LEU A 181     -19.836   0.489  -3.618  1.00 45.69           C  
ANISOU 1038  CD1 LEU A 181     6259   5161   5940    277    187    481       C  
ATOM   1039  CD2 LEU A 181     -18.388  -0.346  -1.774  1.00 31.53           C  
ANISOU 1039  CD2 LEU A 181     4425   3405   4150    252    106    320       C  
ATOM   1040  N   ILE A 182     -22.681  -3.618  -1.139  1.00 37.55           N  
ANISOU 1040  N   ILE A 182     5535   4453   4279    289    109    168       N  
ATOM   1041  CA  ILE A 182     -23.823  -4.102  -0.371  1.00 41.58           C  
ANISOU 1041  CA  ILE A 182     6101   5007   4689    276    101     75       C  
ATOM   1042  C   ILE A 182     -23.410  -5.230   0.570  1.00 45.31           C  
ANISOU 1042  C   ILE A 182     6632   5541   5043    264     83     37       C  
ATOM   1043  O   ILE A 182     -23.713  -5.200   1.763  1.00 50.80           O  
ANISOU 1043  O   ILE A 182     7349   6256   5695    237     57    -58       O  
ATOM   1044  CB  ILE A 182     -24.955  -4.596  -1.294  1.00 38.65           C  
ANISOU 1044  CB  ILE A 182     5773   4662   4251    299    136    110       C  
ATOM   1045  CG1 ILE A 182     -25.606  -3.415  -2.016  1.00 28.22           C  
ANISOU 1045  CG1 ILE A 182     4402   3278   3044    311    131    134       C  
ATOM   1046  CG2 ILE A 182     -25.998  -5.370  -0.505  1.00 27.65           C  
ANISOU 1046  CG2 ILE A 182     4434   3317   2755    281    144     21       C  
ATOM   1047  CD1 ILE A 182     -26.727  -3.814  -2.945  1.00 28.74           C  
ANISOU 1047  CD1 ILE A 182     4504   3364   3053    339    143    162       C  
ATOM   1048  N   SER A 183     -22.703  -6.216   0.029  1.00 40.05           N  
ANISOU 1048  N   SER A 183     5992   4902   4323    284     98    112       N  
ATOM   1049  CA  SER A 183     -22.288  -7.374   0.810  1.00 38.12           C  
ANISOU 1049  CA  SER A 183     5803   4703   3977    279     73     97       C  
ATOM   1050  C   SER A 183     -21.173  -7.037   1.801  1.00 38.25           C  
ANISOU 1050  C   SER A 183     5788   4703   4042    265      3     61       C  
ATOM   1051  O   SER A 183     -20.999  -7.731   2.802  1.00 41.05           O  
ANISOU 1051  O   SER A 183     6196   5093   4307    254    -42     28       O  
ATOM   1052  CB  SER A 183     -21.843  -8.507  -0.119  1.00 32.96           C  
ANISOU 1052  CB  SER A 183     5174   4071   3280    310    106    179       C  
ATOM   1053  OG  SER A 183     -20.751  -8.111  -0.926  1.00 40.98           O  
ANISOU 1053  OG  SER A 183     6124   5053   4392    329    121    244       O  
ATOM   1054  N   ILE A 184     -20.416  -5.980   1.524  1.00 44.42           N  
ANISOU 1054  N   ILE A 184     6482   5427   4968    267    -12     71       N  
ATOM   1055  CA  ILE A 184     -19.386  -5.531   2.454  1.00 45.52           C  
ANISOU 1055  CA  ILE A 184     6575   5542   5181    254    -91     19       C  
ATOM   1056  C   ILE A 184     -20.048  -4.862   3.651  1.00 49.38           C  
ANISOU 1056  C   ILE A 184     7081   6041   5641    224   -136   -102       C  
ATOM   1057  O   ILE A 184     -19.671  -5.102   4.801  1.00 48.42           O  
ANISOU 1057  O   ILE A 184     6993   5950   5456    212   -209   -167       O  
ATOM   1058  CB  ILE A 184     -18.384  -4.560   1.787  1.00 30.01           C  
ANISOU 1058  CB  ILE A 184     4496   3499   3407    259    -86     62       C  
ATOM   1059  CG1 ILE A 184     -17.310  -5.345   1.034  1.00 31.60           C  
ANISOU 1059  CG1 ILE A 184     4673   3698   3636    284    -59    151       C  
ATOM   1060  CG2 ILE A 184     -17.721  -3.663   2.818  1.00 30.92           C  
ANISOU 1060  CG2 ILE A 184     4544   3571   3631    238   -174    -32       C  
ATOM   1061  CD1 ILE A 184     -16.303  -4.478   0.319  1.00 30.63           C  
ANISOU 1061  CD1 ILE A 184     4435   3499   3703    283    -29    203       C  
ATOM   1062  N   GLY A 185     -21.051  -4.034   3.374  1.00 29.83           N  
ANISOU 1062  N   GLY A 185     4585   3541   3208    215    -93   -135       N  
ATOM   1063  CA  GLY A 185     -21.773  -3.338   4.422  1.00 35.28           C  
ANISOU 1063  CA  GLY A 185     5281   4237   3886    187   -116   -265       C  
ATOM   1064  C   GLY A 185     -22.489  -4.287   5.358  1.00 40.73           C  
ANISOU 1064  C   GLY A 185     6080   5013   4382    170   -108   -318       C  
ATOM   1065  O   GLY A 185     -22.462  -4.117   6.576  1.00 51.06           O  
ANISOU 1065  O   GLY A 185     7420   6355   5626    147   -153   -420       O  
ATOM   1066  N   ILE A 186     -23.128  -5.296   4.782  1.00 48.13           N  
ANISOU 1066  N   ILE A 186     7078   5986   5225    179    -48   -249       N  
ATOM   1067  CA  ILE A 186     -23.862  -6.280   5.562  1.00 39.16           C  
ANISOU 1067  CA  ILE A 186     6042   4919   3918    159    -22   -278       C  
ATOM   1068  C   ILE A 186     -22.920  -7.088   6.452  1.00 44.44           C  
ANISOU 1068  C   ILE A 186     6774   5629   4481    156    -91   -262       C  
ATOM   1069  O   ILE A 186     -23.257  -7.405   7.591  1.00 52.06           O  
ANISOU 1069  O   ILE A 186     7818   6649   5313    128   -101   -320       O  
ATOM   1070  CB  ILE A 186     -24.667  -7.219   4.645  1.00 28.68           C  
ANISOU 1070  CB  ILE A 186     4750   3605   2543    172     50   -205       C  
ATOM   1071  CG1 ILE A 186     -25.727  -6.416   3.888  1.00 35.48           C  
ANISOU 1071  CG1 ILE A 186     5556   4428   3497    176     99   -232       C  
ATOM   1072  CG2 ILE A 186     -25.331  -8.318   5.447  1.00 28.79           C  
ANISOU 1072  CG2 ILE A 186     4862   3678   2399    145     83   -221       C  
ATOM   1073  CD1 ILE A 186     -26.530  -7.225   2.892  1.00 27.78           C  
ANISOU 1073  CD1 ILE A 186     4603   3461   2492    194    152   -173       C  
ATOM   1074  N   ALA A 187     -21.727  -7.391   5.948  1.00 45.82           N  
ANISOU 1074  N   ALA A 187     6913   5776   4719    185   -140   -183       N  
ATOM   1075  CA  ALA A 187     -20.783  -8.228   6.685  1.00 46.99           C  
ANISOU 1075  CA  ALA A 187     7113   5951   4791    191   -222   -155       C  
ATOM   1076  C   ALA A 187     -19.975  -7.456   7.731  1.00 44.77           C  
ANISOU 1076  C   ALA A 187     6807   5667   4536    182   -329   -240       C  
ATOM   1077  O   ALA A 187     -19.416  -8.050   8.651  1.00 41.38           O  
ANISOU 1077  O   ALA A 187     6440   5273   4008    182   -415   -242       O  
ATOM   1078  CB  ALA A 187     -19.840  -8.927   5.716  1.00 36.02           C  
ANISOU 1078  CB  ALA A 187     5683   4528   3476    228   -229    -50       C  
ATOM   1079  N   ILE A 188     -19.923  -6.135   7.598  1.00 48.94           N  
ANISOU 1079  N   ILE A 188     7244   6150   5201    175   -333   -311       N  
ATOM   1080  CA  ILE A 188     -19.027  -5.324   8.423  1.00 42.99           C  
ANISOU 1080  CA  ILE A 188     6440   5377   4517    171   -444   -400       C  
ATOM   1081  C   ILE A 188     -19.377  -5.183   9.926  1.00 47.84           C  
ANISOU 1081  C   ILE A 188     7139   6060   4977    144   -502   -523       C  
ATOM   1082  O   ILE A 188     -18.504  -4.813  10.707  1.00 47.37           O  
ANISOU 1082  O   ILE A 188     7060   6000   4937    146   -621   -592       O  
ATOM   1083  CB  ILE A 188     -18.875  -3.899   7.816  1.00 54.55           C  
ANISOU 1083  CB  ILE A 188     7772   6755   6201    169   -428   -442       C  
ATOM   1084  CG1 ILE A 188     -17.458  -3.363   8.049  1.00 55.01           C  
ANISOU 1084  CG1 ILE A 188     7733   6756   6411    179   -536   -469       C  
ATOM   1085  CG2 ILE A 188     -19.923  -2.940   8.358  1.00 33.21           C  
ANISOU 1085  CG2 ILE A 188     5068   4057   3494    141   -397   -569       C  
ATOM   1086  CD1 ILE A 188     -16.361  -4.295   7.565  1.00 46.10           C  
ANISOU 1086  CD1 ILE A 188     6589   5616   5312    208   -568   -359       C  
ATOM   1087  N   PRO A 189     -20.631  -5.465  10.347  1.00 52.48           N  
ANISOU 1087  N   PRO A 189     7818   6709   5411    117   -420   -559       N  
ATOM   1088  CA  PRO A 189     -20.806  -5.444  11.806  1.00 48.89           C  
ANISOU 1088  CA  PRO A 189     7458   6334   4784     91   -471   -666       C  
ATOM   1089  C   PRO A 189     -19.975  -6.485  12.562  1.00 56.64           C  
ANISOU 1089  C   PRO A 189     8538   7367   5616    103   -579   -605       C  
ATOM   1090  O   PRO A 189     -19.573  -6.224  13.695  1.00 71.79           O  
ANISOU 1090  O   PRO A 189    10506   9333   7439     95   -681   -694       O  
ATOM   1091  CB  PRO A 189     -22.299  -5.733  11.977  1.00 57.51           C  
ANISOU 1091  CB  PRO A 189     8626   7478   5748     58   -337   -691       C  
ATOM   1092  CG  PRO A 189     -22.914  -5.184  10.756  1.00 56.64           C  
ANISOU 1092  CG  PRO A 189     8414   7296   5811     67   -247   -671       C  
ATOM   1093  CD  PRO A 189     -21.936  -5.474   9.657  1.00 59.24           C  
ANISOU 1093  CD  PRO A 189     8676   7562   6269    105   -285   -543       C  
ATOM   1094  N   VAL A 190     -19.719  -7.635  11.947  1.00 53.81           N  
ANISOU 1094  N   VAL A 190     8207   6996   5241    124   -566   -461       N  
ATOM   1095  CA  VAL A 190     -18.990  -8.716  12.609  1.00 51.30           C  
ANISOU 1095  CA  VAL A 190     7982   6713   4796    139   -670   -386       C  
ATOM   1096  C   VAL A 190     -17.575  -8.313  13.064  1.00 57.95           C  
ANISOU 1096  C   VAL A 190     8766   7528   5722    166   -845   -425       C  
ATOM   1097  O   VAL A 190     -17.240  -8.490  14.236  1.00 63.49           O  
ANISOU 1097  O   VAL A 190     9558   8288   6276    164   -960   -464       O  
ATOM   1098  CB  VAL A 190     -18.896  -9.974  11.702  1.00 45.23           C  
ANISOU 1098  CB  VAL A 190     7224   5912   4050    163   -624   -232       C  
ATOM   1099  CG1 VAL A 190     -17.913 -10.983  12.279  1.00 38.82           C  
ANISOU 1099  CG1 VAL A 190     6473   5106   3169    189   -757   -152       C  
ATOM   1100  CG2 VAL A 190     -20.268 -10.599  11.507  1.00 49.47           C  
ANISOU 1100  CG2 VAL A 190     7838   6482   4475    133   -478   -196       C  
ATOM   1101  N   PRO A 191     -16.737  -7.769  12.156  1.00 52.24           N  
ANISOU 1101  N   PRO A 191     7895   6719   5236    193   -868   -414       N  
ATOM   1102  CA  PRO A 191     -15.391  -7.444  12.645  1.00 59.48           C  
ANISOU 1102  CA  PRO A 191     8747   7603   6248    217  -1039   -458       C  
ATOM   1103  C   PRO A 191     -15.344  -6.180  13.505  1.00 55.19           C  
ANISOU 1103  C   PRO A 191     8174   7074   5723    198  -1113   -628       C  
ATOM   1104  O   PRO A 191     -14.476  -6.061  14.372  1.00 39.91           O  
ANISOU 1104  O   PRO A 191     6242   5151   3773    211  -1279   -691       O  
ATOM   1105  CB  PRO A 191     -14.592  -7.248  11.354  1.00 36.57           C  
ANISOU 1105  CB  PRO A 191     5689   4601   3604    243  -1008   -395       C  
ATOM   1106  CG  PRO A 191     -15.595  -6.764  10.382  1.00 38.33           C  
ANISOU 1106  CG  PRO A 191     5878   4805   3879    224   -839   -381       C  
ATOM   1107  CD  PRO A 191     -16.864  -7.500  10.710  1.00 44.15           C  
ANISOU 1107  CD  PRO A 191     6759   5622   4393    203   -753   -356       C  
ATOM   1108  N   ILE A 192     -16.260  -5.249  13.258  1.00 38.06           N  
ANISOU 1108  N   ILE A 192     5968   4897   3596    169  -1000   -707       N  
ATOM   1109  CA  ILE A 192     -16.320  -4.011  14.026  1.00 39.19           C  
ANISOU 1109  CA  ILE A 192     6073   5044   3773    150  -1055   -885       C  
ATOM   1110  C   ILE A 192     -16.678  -4.316  15.477  1.00 50.19           C  
ANISOU 1110  C   ILE A 192     7623   6555   4891    132  -1122   -970       C  
ATOM   1111  O   ILE A 192     -16.167  -3.686  16.404  1.00 46.51           O  
ANISOU 1111  O   ILE A 192     7153   6111   4409    132  -1253  -1107       O  
ATOM   1112  CB  ILE A 192     -17.341  -3.027  13.423  1.00 43.24           C  
ANISOU 1112  CB  ILE A 192     6517   5517   4396    125   -912   -944       C  
ATOM   1113  CG1 ILE A 192     -16.845  -2.522  12.067  1.00 42.86           C  
ANISOU 1113  CG1 ILE A 192     6312   5349   4622    141   -867   -866       C  
ATOM   1114  CG2 ILE A 192     -17.588  -1.849  14.356  1.00 48.20           C  
ANISOU 1114  CG2 ILE A 192     7122   6158   5032    103   -958  -1146       C  
ATOM   1115  CD1 ILE A 192     -17.783  -1.542  11.398  1.00 41.94           C  
ANISOU 1115  CD1 ILE A 192     6124   5178   4632    124   -746   -902       C  
ATOM   1116  N   LYS A 193     -17.544  -5.306  15.667  1.00 51.38           N  
ANISOU 1116  N   LYS A 193     7916   6782   4823    117  -1030   -889       N  
ATOM   1117  CA  LYS A 193     -17.956  -5.704  17.005  1.00 52.35           C  
ANISOU 1117  CA  LYS A 193     8208   7024   4658     94  -1066   -943       C  
ATOM   1118  C   LYS A 193     -16.969  -6.708  17.591  1.00 42.56           C  
ANISOU 1118  C   LYS A 193     7057   5815   3298    124  -1229   -848       C  
ATOM   1119  O   LYS A 193     -16.437  -6.506  18.683  1.00 52.31           O  
ANISOU 1119  O   LYS A 193     8355   7107   4414    129  -1380   -936       O  
ATOM   1120  CB  LYS A 193     -19.373  -6.288  16.982  1.00 49.90           C  
ANISOU 1120  CB  LYS A 193     8005   6774   4182     57   -881   -896       C  
ATOM   1121  CG  LYS A 193     -19.986  -6.456  18.364  1.00 65.49           C  
ANISOU 1121  CG  LYS A 193    10146   8874   5862     21   -871   -976       C  
ATOM   1122  CD  LYS A 193     -21.503  -6.338  18.329  1.00 67.64           C  
ANISOU 1122  CD  LYS A 193    10453   9184   6062    -25   -664  -1023       C  
ATOM   1123  CE  LYS A 193     -22.095  -6.382  19.736  1.00 69.24           C  
ANISOU 1123  CE  LYS A 193    10816   9518   5974    -66   -634  -1123       C  
ATOM   1124  NZ  LYS A 193     -21.503  -5.351  20.643  1.00 53.67           N  
ANISOU 1124  NZ  LYS A 193     8833   7586   3975    -60   -767  -1311       N  
ATOM   1125  N   GLY A 194     -16.726  -7.786  16.856  1.00 41.53           N  
ANISOU 1125  N   GLY A 194     6931   5644   3205    146  -1207   -674       N  
ATOM   1126  CA  GLY A 194     -15.796  -8.812  17.291  1.00 49.74           C  
ANISOU 1126  CA  GLY A 194     8039   6691   4167    180  -1361   -568       C  
ATOM   1127  C   GLY A 194     -16.410  -9.805  18.259  1.00 55.89           C  
ANISOU 1127  C   GLY A 194     9027   7571   4637    158  -1351   -497       C  
ATOM   1128  O   GLY A 194     -17.563  -9.663  18.669  1.00 56.55           O  
ANISOU 1128  O   GLY A 194     9202   7729   4556    112  -1216   -545       O  
ATOM   1129  N   ILE A 195     -15.635 -10.823  18.615  1.00 55.97           N  
ANISOU 1129  N   ILE A 195     9108   7579   4579    191  -1491   -378       N  
ATOM   1130  CA  ILE A 195     -16.068 -11.809  19.594  1.00 60.13           C  
ANISOU 1130  CA  ILE A 195     9842   8193   4812    173  -1505   -286       C  
ATOM   1131  C   ILE A 195     -15.388 -11.523  20.926  1.00 47.82           C  
ANISOU 1131  C   ILE A 195     8379   6710   3079    186  -1714   -364       C  
ATOM   1132  O   ILE A 195     -14.173 -11.340  20.978  1.00 52.14           O  
ANISOU 1132  O   ILE A 195     8844   7208   3760    234  -1913   -387       O  
ATOM   1133  CB  ILE A 195     -15.750 -13.243  19.139  1.00 45.03           C  
ANISOU 1133  CB  ILE A 195     7962   6221   2927    201  -1524    -84       C  
ATOM   1134  N   GLU A 196     -16.179 -11.477  21.995  1.00 53.60           N  
ANISOU 1134  N   GLU A 196     9285   7565   3517    143  -1667   -410       N  
ATOM   1135  CA  GLU A 196     -15.685 -11.095  23.316  1.00 56.18           C  
ANISOU 1135  CA  GLU A 196     9722   7987   3635    150  -1852   -510       C  
ATOM   1136  C   GLU A 196     -14.519 -11.960  23.781  1.00 59.00           C  
ANISOU 1136  C   GLU A 196    10143   8327   3948    205  -2101   -385       C  
ATOM   1137  O   GLU A 196     -14.489 -13.167  23.539  1.00 59.01           O  
ANISOU 1137  O   GLU A 196    10194   8288   3939    216  -2085   -189       O  
ATOM   1138  CB  GLU A 196     -16.816 -11.159  24.346  1.00 57.33           C  
ANISOU 1138  CB  GLU A 196    10018   8276   3488     86  -1699   -537       C  
ATOM   1139  N   THR A 197     -13.557 -11.328  24.445  1.00 70.90           N  
ANISOU 1139  N   THR A 197    11620   9854   5466    240  -2327   -506       N  
ATOM   1140  CA  THR A 197     -12.390 -12.031  24.964  1.00 83.24           C  
ANISOU 1140  CA  THR A 197    13189  11395   7041    292  -2563   -406       C  
ATOM   1141  C   THR A 197     -12.483 -12.204  26.477  1.00 90.82           C  
ANISOU 1141  C   THR A 197    14270  12501   7736    266  -2601   -406       C  
ATOM   1142  O   THR A 197     -12.910 -11.296  27.190  1.00103.48           O  
ANISOU 1142  O   THR A 197    15896  14211   9212    229  -2556   -574       O  
ATOM   1143  CB  THR A 197     -11.082 -11.290  24.619  1.00 76.98           C  
ANISOU 1143  CB  THR A 197    12234  10507   6506    354  -2806   -530       C  
ATOM   1144  N   ASN A 201      -7.634 -12.956  32.331  1.00112.18           N  
ANISOU 1144  N   ASN A 201    17189  15507   9927    448  -3853   -418       N  
ATOM   1145  CA  ASN A 201      -8.453 -13.889  31.560  1.00119.19           C  
ANISOU 1145  CA  ASN A 201    18121  16345  10820    426  -3635   -226       C  
ATOM   1146  C   ASN A 201      -7.610 -14.733  30.614  1.00131.92           C  
ANISOU 1146  C   ASN A 201    19637  17773  12715    492  -3753    -79       C  
ATOM   1147  O   ASN A 201      -6.487 -14.351  30.276  1.00137.04           O  
ANISOU 1147  O   ASN A 201    20143  18314  13612    551  -3965   -164       O  
ATOM   1148  CB  ASN A 201      -9.524 -13.137  30.760  1.00112.25           C  
ANISOU 1148  CB  ASN A 201    17198  15466   9985    369  -3378   -338       C  
ATOM   1149  N   PRO A 202      -8.151 -15.885  30.176  1.00134.89           N  
ANISOU 1149  N   PRO A 202    20076  18106  13070    482  -3610    134       N  
ATOM   1150  CA  PRO A 202      -7.438 -16.684  29.177  1.00129.92           C  
ANISOU 1150  CA  PRO A 202    19345  17298  12723    540  -3695    262       C  
ATOM   1151  C   PRO A 202      -7.642 -16.177  27.752  1.00120.12           C  
ANISOU 1151  C   PRO A 202    17965  15945  11728    537  -3580    186       C  
ATOM   1152  O   PRO A 202      -8.722 -15.693  27.398  1.00115.21           O  
ANISOU 1152  O   PRO A 202    17372  15376  11026    478  -3351    127       O  
ATOM   1153  CB  PRO A 202      -8.053 -18.073  29.346  1.00130.37           C  
ANISOU 1153  CB  PRO A 202    19530  17361  12643    522  -3571    505       C  
ATOM   1154  CG  PRO A 202      -9.460 -17.788  29.737  1.00129.85           C  
ANISOU 1154  CG  PRO A 202    19581  17440  12316    438  -3306    479       C  
ATOM   1155  CD  PRO A 202      -9.393 -16.553  30.616  1.00132.95           C  
ANISOU 1155  CD  PRO A 202    19987  17968  12559    419  -3372    266       C  
ATOM   1156  N   ASN A 203      -6.591 -16.301  26.945  1.00116.43           N  
ANISOU 1156  N   ASN A 203    17344  15326  11569    603  -3742    189       N  
ATOM   1157  CA  ASN A 203      -6.637 -15.964  25.529  1.00112.56           C  
ANISOU 1157  CA  ASN A 203    16714  14721  11331    612  -3658    145       C  
ATOM   1158  C   ASN A 203      -7.278 -17.082  24.716  1.00107.07           C  
ANISOU 1158  C   ASN A 203    16061  13964  10657    601  -3480    336       C  
ATOM   1159  O   ASN A 203      -6.765 -17.478  23.670  1.00105.75           O  
ANISOU 1159  O   ASN A 203    15773  13661  10745    646  -3516    389       O  
ATOM   1160  CB  ASN A 203      -5.230 -15.676  25.004  1.00113.60           C  
ANISOU 1160  CB  ASN A 203    16643  14717  11803    687  -3898     70       C  
ATOM   1161  N   ASN A 204      -8.398 -17.595  25.216  1.00105.93           N  
ANISOU 1161  N   ASN A 204    16078  13918  10255    541  -3285    434       N  
ATOM   1162  CA  ASN A 204      -9.140 -18.652  24.545  1.00100.76           C  
ANISOU 1162  CA  ASN A 204    15467  13210   9606    519  -3097    606       C  
ATOM   1163  C   ASN A 204     -10.509 -18.157  24.094  1.00 97.43           C  
ANISOU 1163  C   ASN A 204    15088  12852   9080    447  -2814    550       C  
ATOM   1164  O   ASN A 204     -11.255 -17.562  24.874  1.00 95.50           O  
ANISOU 1164  O   ASN A 204    14928  12740   8619    391  -2711    466       O  
ATOM   1165  CB  ASN A 204      -9.289 -19.867  25.464  1.00 97.10           C  
ANISOU 1165  CB  ASN A 204    15137  12782   8974    513  -3106    793       C  
ATOM   1166  CG  ASN A 204     -10.407 -20.796  25.030  1.00 99.60           C  
ANISOU 1166  CG  ASN A 204    15525  13083   9235    465  -2860    942       C  
ATOM   1167  OD1 ASN A 204     -10.260 -21.566  24.079  1.00106.09           O  
ANISOU 1167  OD1 ASN A 204    16283  13776  10249    492  -2837   1041       O  
ATOM   1168  ND2 ASN A 204     -11.534 -20.731  25.730  1.00 97.29           N  
ANISOU 1168  ND2 ASN A 204    15354  12920   8691    395  -2675    949       N  
ATOM   1169  N   ILE A 205     -10.834 -18.410  22.831  1.00 92.96           N  
ANISOU 1169  N   ILE A 205    14457  12191   8673    449  -2689    591       N  
ATOM   1170  CA  ILE A 205     -12.051 -17.879  22.230  1.00 95.38           C  
ANISOU 1170  CA  ILE A 205    14777  12536   8925    388  -2436    526       C  
ATOM   1171  C   ILE A 205     -12.876 -18.993  21.578  1.00 88.10           C  
ANISOU 1171  C   ILE A 205    13893  11563   8019    362  -2240    686       C  
ATOM   1172  O   ILE A 205     -12.334 -20.021  21.172  1.00100.61           O  
ANISOU 1172  O   ILE A 205    15450  13043   9735    406  -2315    822       O  
ATOM   1173  CB  ILE A 205     -11.710 -16.785  21.183  1.00 83.57           C  
ANISOU 1173  CB  ILE A 205    13064  10982   7708    401  -2391    366       C  
ATOM   1174  CG1 ILE A 205     -12.956 -16.012  20.747  1.00 89.79           C  
ANISOU 1174  CG1 ILE A 205    13837  11824   8456    336  -2129    267       C  
ATOM   1175  CG2 ILE A 205     -10.998 -17.387  19.978  1.00 80.50           C  
ANISOU 1175  CG2 ILE A 205    12499  10448   7638    450  -2390    441       C  
ATOM   1176  CD1 ILE A 205     -12.683 -15.006  19.648  1.00 89.31           C  
ANISOU 1176  CD1 ILE A 205    13551  11695   8688    344  -2056    139       C  
ATOM   1177  N   THR A 206     -14.190 -18.796  21.508  1.00 69.91           N  
ANISOU 1177  N   THR A 206    11641   9326   5596    292  -1993    659       N  
ATOM   1178  CA  THR A 206     -15.061 -19.701  20.766  1.00 64.64           C  
ANISOU 1178  CA  THR A 206    10985   8603   4971    264  -1796    777       C  
ATOM   1179  C   THR A 206     -15.687 -18.955  19.593  1.00 64.55           C  
ANISOU 1179  C   THR A 206    10846   8568   5112    243  -1610    663       C  
ATOM   1180  O   THR A 206     -16.549 -18.093  19.780  1.00 66.38           O  
ANISOU 1180  O   THR A 206    11099   8881   5241    193  -1476    547       O  
ATOM   1181  CB  THR A 206     -16.170 -20.292  21.650  1.00 69.90           C  
ANISOU 1181  CB  THR A 206    11764   9358   5438    195  -1626    854       C  
ATOM   1182  OG1 THR A 206     -17.109 -19.267  21.995  1.00 76.22           O  
ANISOU 1182  OG1 THR A 206    12582  10269   6109    136  -1473    708       O  
ATOM   1183  CG2 THR A 206     -15.578 -20.890  22.918  1.00 81.59           C  
ANISOU 1183  CG2 THR A 206    13331  10884   6784    211  -1780    951       C  
ATOM   1184  N   CYS A 207     -15.248 -19.293  18.385  1.00 56.86           N  
ANISOU 1184  N   CYS A 207     9712   7482   4409    282  -1587    691       N  
ATOM   1185  CA  CYS A 207     -15.645 -18.566  17.185  1.00 50.36           C  
ANISOU 1185  CA  CYS A 207     8730   6631   3775    272  -1425    586       C  
ATOM   1186  C   CYS A 207     -17.081 -18.876  16.777  1.00 49.19           C  
ANISOU 1186  C   CYS A 207     8628   6501   3560    215  -1189    610       C  
ATOM   1187  O   CYS A 207     -17.331 -19.808  16.013  1.00 52.63           O  
ANISOU 1187  O   CYS A 207     9035   6865   4096    222  -1110    703       O  
ATOM   1188  CB  CYS A 207     -14.692 -18.891  16.035  1.00 42.66           C  
ANISOU 1188  CB  CYS A 207     7582   5539   3088    331  -1472    611       C  
ATOM   1189  SG  CYS A 207     -14.468 -17.557  14.839  1.00 72.40           S  
ANISOU 1189  SG  CYS A 207    11137   9278   7093    339  -1386    459       S  
ATOM   1190  N   VAL A 208     -18.018 -18.083  17.285  1.00 48.42           N  
ANISOU 1190  N   VAL A 208     8593   6497   3310    160  -1081    515       N  
ATOM   1191  CA  VAL A 208     -19.429 -18.264  16.971  1.00 51.09           C  
ANISOU 1191  CA  VAL A 208     8963   6854   3595    103   -859    516       C  
ATOM   1192  C   VAL A 208     -20.207 -16.965  17.187  1.00 57.44           C  
ANISOU 1192  C   VAL A 208     9749   7737   4340     61   -754    351       C  
ATOM   1193  O   VAL A 208     -19.832 -16.131  18.011  1.00 72.61           O  
ANISOU 1193  O   VAL A 208    11702   9725   6163     60   -848    254       O  
ATOM   1194  CB  VAL A 208     -20.053 -19.397  17.823  1.00 46.67           C  
ANISOU 1194  CB  VAL A 208     8585   6322   2827     63   -814    655       C  
ATOM   1195  CG1 VAL A 208     -20.230 -18.954  19.269  1.00 52.38           C  
ANISOU 1195  CG1 VAL A 208     9429   7165   3306     26   -844    611       C  
ATOM   1196  CG2 VAL A 208     -21.380 -19.855  17.233  1.00 41.87           C  
ANISOU 1196  CG2 VAL A 208     7971   5692   2245     14   -590    678       C  
ATOM   1197  N   LEU A 209     -21.277 -16.787  16.421  1.00 57.80           N  
ANISOU 1197  N   LEU A 209     9733   7768   4461     30   -568    310       N  
ATOM   1198  CA  LEU A 209     -22.175 -15.657  16.609  1.00 50.78           C  
ANISOU 1198  CA  LEU A 209     8823   6940   3530    -12   -452    159       C  
ATOM   1199  C   LEU A 209     -23.316 -16.046  17.543  1.00 48.94           C  
ANISOU 1199  C   LEU A 209     8738   6784   3072    -80   -318    173       C  
ATOM   1200  O   LEU A 209     -24.251 -16.734  17.135  1.00 54.36           O  
ANISOU 1200  O   LEU A 209     9434   7443   3778   -111   -171    232       O  
ATOM   1201  CB  LEU A 209     -22.730 -15.178  15.266  1.00 46.00           C  
ANISOU 1201  CB  LEU A 209     8064   6274   3138     -6   -334    103       C  
ATOM   1202  CG  LEU A 209     -21.712 -14.694  14.234  1.00 57.97           C  
ANISOU 1202  CG  LEU A 209     9429   7718   4880     53   -427     87       C  
ATOM   1203  CD1 LEU A 209     -22.409 -14.310  12.937  1.00 58.50           C  
ANISOU 1203  CD1 LEU A 209     9374   7736   5115     55   -299     51       C  
ATOM   1204  CD2 LEU A 209     -20.916 -13.520  14.782  1.00 61.64           C  
ANISOU 1204  CD2 LEU A 209     9854   8210   5357     67   -549    -27       C  
ATOM   1205  N   THR A 210     -23.238 -15.608  18.795  1.00 45.34           N  
ANISOU 1205  N   THR A 210     8397   6425   2405   -103   -367    112       N  
ATOM   1206  CA  THR A 210     -24.263 -15.945  19.776  1.00 52.05           C  
ANISOU 1206  CA  THR A 210     9317   7359   3100   -165   -223    122       C  
ATOM   1207  C   THR A 210     -25.473 -15.021  19.678  1.00 49.68           C  
ANISOU 1207  C   THR A 210     8963   7095   2816   -211    -41    -38       C  
ATOM   1208  O   THR A 210     -25.373 -13.895  19.192  1.00 50.11           O  
ANISOU 1208  O   THR A 210     8956   7133   2949   -198    -60   -182       O  
ATOM   1209  CB  THR A 210     -23.716 -15.888  21.213  1.00 46.47           C  
ANISOU 1209  CB  THR A 210     8697   6756   2202   -165   -336    119       C  
ATOM   1210  OG1 THR A 210     -23.535 -14.521  21.607  1.00 53.71           O  
ANISOU 1210  OG1 THR A 210     9591   7737   3080   -162   -384    -74       O  
ATOM   1211  CG2 THR A 210     -22.392 -16.631  21.314  1.00 47.00           C  
ANISOU 1211  CG2 THR A 210     8803   6780   2274   -110   -551    255       C  
ATOM   1212  N   LYS A 211     -26.614 -15.514  20.149  1.00 53.27           N  
ANISOU 1212  N   LYS A 211     9443   7590   3207   -266    134    -12       N  
ATOM   1213  CA  LYS A 211     -27.854 -14.747  20.182  1.00 50.32           C  
ANISOU 1213  CA  LYS A 211     9018   7250   2852   -312    316   -162       C  
ATOM   1214  C   LYS A 211     -27.714 -13.514  21.066  1.00 60.24           C  
ANISOU 1214  C   LYS A 211    10279   8601   4007   -314    280   -340       C  
ATOM   1215  O   LYS A 211     -28.313 -12.471  20.805  1.00 63.06           O  
ANISOU 1215  O   LYS A 211    10564   8958   4438   -328    363   -509       O  
ATOM   1216  CB  LYS A 211     -29.002 -15.628  20.685  1.00 52.91           C  
ANISOU 1216  CB  LYS A 211     9384   7604   3117   -369    497    -87       C  
ATOM   1217  CG  LYS A 211     -30.325 -14.907  20.888  1.00 50.01           C  
ANISOU 1217  CG  LYS A 211     8963   7274   2763   -418    692   -242       C  
ATOM   1218  CD  LYS A 211     -31.346 -15.818  21.553  1.00 51.04           C  
ANISOU 1218  CD  LYS A 211     9146   7435   2814   -476    861   -159       C  
ATOM   1219  CE  LYS A 211     -32.695 -15.133  21.690  1.00 71.65           C  
ANISOU 1219  CE  LYS A 211    11690  10069   5466   -524   1062   -318       C  
ATOM   1220  NZ  LYS A 211     -33.729 -16.051  22.247  1.00 82.38           N  
ANISOU 1220  NZ  LYS A 211    13093  11442   6768   -587   1242   -236       N  
ATOM   1221  N   GLU A 212     -26.911 -13.642  22.116  1.00 69.93           N  
ANISOU 1221  N   GLU A 212    11590   9908   5072   -298    149   -308       N  
ATOM   1222  CA  GLU A 212     -26.742 -12.572  23.086  1.00 77.52           C  
ANISOU 1222  CA  GLU A 212    12568  10973   5915   -298    103   -480       C  
ATOM   1223  C   GLU A 212     -26.055 -11.362  22.465  1.00 74.78           C  
ANISOU 1223  C   GLU A 212    12146  10574   5692   -265    -17   -633       C  
ATOM   1224  O   GLU A 212     -26.560 -10.243  22.544  1.00 82.88           O  
ANISOU 1224  O   GLU A 212    13116  11621   6754   -281     51   -825       O  
ATOM   1225  CB  GLU A 212     -25.945 -13.065  24.299  1.00 88.68           C  
ANISOU 1225  CB  GLU A 212    14092  12481   7124   -282    -34   -400       C  
ATOM   1226  CG  GLU A 212     -26.663 -14.109  25.150  1.00 99.34           C  
ANISOU 1226  CG  GLU A 212    15532  13898   8315   -320     91   -268       C  
ATOM   1227  CD  GLU A 212     -26.721 -15.475  24.491  1.00101.53           C  
ANISOU 1227  CD  GLU A 212    15824  14076   8675   -324    118    -49       C  
ATOM   1228  OE1 GLU A 212     -25.782 -15.815  23.741  1.00104.15           O  
ANISOU 1228  OE1 GLU A 212    16134  14316   9120   -281    -30     36       O  
ATOM   1229  OE2 GLU A 212     -27.706 -16.208  24.721  1.00105.70           O  
ANISOU 1229  OE2 GLU A 212    16384  14612   9165   -370    289     32       O  
ATOM   1230  N   ARG A 213     -24.910 -11.597  21.832  1.00 60.61           N  
ANISOU 1230  N   ARG A 213    10348   8702   3978   -217   -193   -548       N  
ATOM   1231  CA  ARG A 213     -24.078 -10.509  21.332  1.00 45.99           C  
ANISOU 1231  CA  ARG A 213     8427   6795   2251   -178   -335   -676       C  
ATOM   1232  C   ARG A 213     -24.487 -10.025  19.941  1.00 68.15           C  
ANISOU 1232  C   ARG A 213    11042   9491   5362   -163   -245   -703       C  
ATOM   1233  O   ARG A 213     -24.379  -8.837  19.638  1.00 72.26           O  
ANISOU 1233  O   ARG A 213    11434   9978   6043   -148   -268   -849       O  
ATOM   1234  CB  ARG A 213     -22.612 -10.943  21.320  1.00 46.17           C  
ANISOU 1234  CB  ARG A 213     8459   6783   2302   -119   -569   -571       C  
ATOM   1235  CG  ARG A 213     -21.646  -9.888  20.810  1.00 55.87           C  
ANISOU 1235  CG  ARG A 213     9522   7944   3764    -70   -713   -680       C  
ATOM   1236  CD  ARG A 213     -20.205 -10.341  20.971  1.00 58.46           C  
ANISOU 1236  CD  ARG A 213     9861   8243   4107    -15   -946   -591       C  
ATOM   1237  NE  ARG A 213     -19.580  -9.783  22.165  1.00 72.73           N  
ANISOU 1237  NE  ARG A 213    11744  10134   5756     -8  -1111   -710       N  
ATOM   1238  CZ  ARG A 213     -18.684  -8.802  22.143  1.00 71.26           C  
ANISOU 1238  CZ  ARG A 213    11438   9911   5725     26  -1262   -842       C  
ATOM   1239  NH1 ARG A 213     -18.309  -8.276  20.986  1.00 46.79           N  
ANISOU 1239  NH1 ARG A 213     8143   6694   2942     52  -1255   -854       N  
ATOM   1240  NH2 ARG A 213     -18.162  -8.349  23.277  1.00 72.25           N  
ANISOU 1240  NH2 ARG A 213    11641  10118   5692     33  -1420   -960       N  
ATOM   1241  N   PHE A 214     -24.961 -10.938  19.099  1.00 54.78           N  
ANISOU 1241  N   PHE A 214     9330   7738   3746   -167   -148   -562       N  
ATOM   1242  CA  PHE A 214     -25.264 -10.600  17.713  1.00 40.44           C  
ANISOU 1242  CA  PHE A 214     7346   5820   2198   -145    -86   -565       C  
ATOM   1243  C   PHE A 214     -26.723 -10.843  17.332  1.00 54.22           C  
ANISOU 1243  C   PHE A 214     9077   7557   3967   -189    122   -573       C  
ATOM   1244  O   PHE A 214     -27.031 -11.045  16.157  1.00 48.59           O  
ANISOU 1244  O   PHE A 214     8264   6764   3435   -171    171   -520       O  
ATOM   1245  CB  PHE A 214     -24.349 -11.388  16.770  1.00 43.36           C  
ANISOU 1245  CB  PHE A 214     7668   6107   2700    -94   -185   -406       C  
ATOM   1246  CG  PHE A 214     -22.939 -10.865  16.711  1.00 40.83           C  
ANISOU 1246  CG  PHE A 214     7282   5755   2475    -43   -375   -425       C  
ATOM   1247  CD1 PHE A 214     -21.974 -11.331  17.588  1.00 40.69           C  
ANISOU 1247  CD1 PHE A 214     7364   5778   2319    -26   -532   -374       C  
ATOM   1248  CD2 PHE A 214     -22.581  -9.906  15.778  1.00 40.02           C  
ANISOU 1248  CD2 PHE A 214     7016   5578   2610    -13   -398   -489       C  
ATOM   1249  CE1 PHE A 214     -20.677 -10.853  17.535  1.00 40.91           C  
ANISOU 1249  CE1 PHE A 214     7315   5768   2460     21   -712   -402       C  
ATOM   1250  CE2 PHE A 214     -21.286  -9.424  15.720  1.00 42.03           C  
ANISOU 1250  CE2 PHE A 214     7198   5795   2976     28   -560   -508       C  
ATOM   1251  CZ  PHE A 214     -20.332  -9.899  16.603  1.00 42.58           C  
ANISOU 1251  CZ  PHE A 214     7355   5903   2922     46   -719   -472       C  
ATOM   1252  N   GLY A 215     -27.613 -10.810  18.319  1.00 41.27           N  
ANISOU 1252  N   GLY A 215     7532   6001   2147   -246    242   -648       N  
ATOM   1253  CA  GLY A 215     -29.036 -11.001  18.085  1.00 49.96           C  
ANISOU 1253  CA  GLY A 215     8611   7095   3278   -293    446   -675       C  
ATOM   1254  C   GLY A 215     -29.623 -10.077  17.034  1.00 58.25           C  
ANISOU 1254  C   GLY A 215     9481   8065   4584   -275    500   -779       C  
ATOM   1255  O   GLY A 215     -30.386 -10.514  16.172  1.00 64.14           O  
ANISOU 1255  O   GLY A 215    10164   8752   5453   -279    594   -729       O  
ATOM   1256  N   ASP A 216     -29.268  -8.797  17.106  1.00 66.05           N  
ANISOU 1256  N   ASP A 216    10387   9048   5661   -254    430   -923       N  
ATOM   1257  CA  ASP A 216     -29.696  -7.820  16.110  1.00 58.69           C  
ANISOU 1257  CA  ASP A 216     9286   8031   4985   -231    455  -1010       C  
ATOM   1258  C   ASP A 216     -29.151  -8.169  14.734  1.00 50.99           C  
ANISOU 1258  C   ASP A 216     8227   6961   4185   -179    380   -871       C  
ATOM   1259  O   ASP A 216     -29.873  -8.128  13.737  1.00 45.60           O  
ANISOU 1259  O   ASP A 216     7453   6214   3659   -170    448   -858       O  
ATOM   1260  CB  ASP A 216     -29.239  -6.413  16.498  1.00 66.21           C  
ANISOU 1260  CB  ASP A 216    10168   8982   6006   -216    374  -1177       C  
ATOM   1261  CG  ASP A 216     -30.306  -5.633  17.233  1.00 75.33           C  
ANISOU 1261  CG  ASP A 216    11308  10179   7135   -259    503  -1372       C  
ATOM   1262  OD1 ASP A 216     -31.500  -5.964  17.072  1.00 81.96           O  
ANISOU 1262  OD1 ASP A 216    12135  11014   7990   -292    660  -1382       O  
ATOM   1263  OD2 ASP A 216     -29.951  -4.683  17.964  1.00 76.43           O  
ANISOU 1263  OD2 ASP A 216    11437  10350   7251   -259    447  -1525       O  
ATOM   1264  N   PHE A 217     -27.869  -8.513  14.690  1.00 60.18           N  
ANISOU 1264  N   PHE A 217     9423   8121   5323   -144    238   -775       N  
ATOM   1265  CA  PHE A 217     -27.208  -8.822  13.432  1.00 35.19           C  
ANISOU 1265  CA  PHE A 217     6181   4875   2315    -95    170   -654       C  
ATOM   1266  C   PHE A 217     -27.722 -10.121  12.832  1.00 55.34           C  
ANISOU 1266  C   PHE A 217     8771   7410   4846    -99    244   -521       C  
ATOM   1267  O   PHE A 217     -27.839 -10.245  11.616  1.00 46.29           O  
ANISOU 1267  O   PHE A 217     7542   6198   3848    -70    257   -466       O  
ATOM   1268  CB  PHE A 217     -25.695  -8.902  13.625  1.00 40.98           C  
ANISOU 1268  CB  PHE A 217     6930   5606   3034    -58      5   -597       C  
ATOM   1269  CG  PHE A 217     -24.952  -9.283  12.380  1.00 41.74           C  
ANISOU 1269  CG  PHE A 217     6950   5625   3283    -10    -50   -476       C  
ATOM   1270  CD1 PHE A 217     -24.727  -8.349  11.385  1.00 34.08           C  
ANISOU 1270  CD1 PHE A 217     5846   4585   2519     19    -64   -503       C  
ATOM   1271  CD2 PHE A 217     -24.478 -10.573  12.204  1.00 49.46           C  
ANISOU 1271  CD2 PHE A 217     7991   6600   4201      5    -81   -335       C  
ATOM   1272  CE1 PHE A 217     -24.046  -8.692  10.235  1.00 37.46           C  
ANISOU 1272  CE1 PHE A 217     6211   4953   3070     60    -97   -395       C  
ATOM   1273  CE2 PHE A 217     -23.796 -10.922  11.056  1.00 51.19           C  
ANISOU 1273  CE2 PHE A 217     8136   6753   4560     49   -119   -241       C  
ATOM   1274  CZ  PHE A 217     -23.579  -9.978  10.068  1.00 49.21           C  
ANISOU 1274  CZ  PHE A 217     7758   6445   4494     75   -121   -273       C  
ATOM   1275  N   MET A 218     -28.021 -11.095  13.683  1.00 65.34           N  
ANISOU 1275  N   MET A 218    10166   8734   5927   -136    292   -469       N  
ATOM   1276  CA  MET A 218     -28.525 -12.375  13.207  1.00 64.14           C  
ANISOU 1276  CA  MET A 218    10049   8555   5765   -146    365   -348       C  
ATOM   1277  C   MET A 218     -29.922 -12.228  12.606  1.00 75.00           C  
ANISOU 1277  C   MET A 218    11352   9901   7246   -170    509   -409       C  
ATOM   1278  O   MET A 218     -30.310 -12.988  11.720  1.00 82.04           O  
ANISOU 1278  O   MET A 218    12210  10741   8220   -160    547   -335       O  
ATOM   1279  CB  MET A 218     -28.539 -13.399  14.340  1.00 66.94           C  
ANISOU 1279  CB  MET A 218    10563   8971   5902   -186    387   -270       C  
ATOM   1280  CG  MET A 218     -27.160 -13.876  14.768  1.00 75.17           C  
ANISOU 1280  CG  MET A 218    11679  10024   6858   -153    225   -172       C  
ATOM   1281  SD  MET A 218     -27.204 -14.861  16.276  1.00 69.12           S  
ANISOU 1281  SD  MET A 218    11118   9339   5805   -202    237    -84       S  
ATOM   1282  CE  MET A 218     -28.443 -16.074  15.837  1.00110.36           C  
ANISOU 1282  CE  MET A 218    16360  14517  11056   -246    416     11       C  
ATOM   1283  N   LEU A 219     -30.669 -11.237  13.086  1.00 79.86           N  
ANISOU 1283  N   LEU A 219    11933  10543   7868   -199    581   -556       N  
ATOM   1284  CA  LEU A 219     -32.028 -10.998  12.611  1.00 69.31           C  
ANISOU 1284  CA  LEU A 219    10513   9174   6647   -221    711   -634       C  
ATOM   1285  C   LEU A 219     -32.065 -10.096  11.381  1.00 66.23           C  
ANISOU 1285  C   LEU A 219     9978   8708   6478   -172    661   -674       C  
ATOM   1286  O   LEU A 219     -32.599 -10.475  10.340  1.00 64.25           O  
ANISOU 1286  O   LEU A 219     9666   8402   6344   -153    686   -630       O  
ATOM   1287  CB  LEU A 219     -32.877 -10.379  13.723  1.00 67.19           C  
ANISOU 1287  CB  LEU A 219    10268   8965   6295   -277    826   -783       C  
ATOM   1288  CG  LEU A 219     -34.258  -9.865  13.308  1.00 64.56           C  
ANISOU 1288  CG  LEU A 219     9822   8590   6118   -295    950   -900       C  
ATOM   1289  CD1 LEU A 219     -35.195 -11.016  12.981  1.00 70.18           C  
ANISOU 1289  CD1 LEU A 219    10543   9276   6845   -327   1064   -829       C  
ATOM   1290  CD2 LEU A 219     -34.849  -8.981  14.392  1.00 57.73           C  
ANISOU 1290  CD2 LEU A 219     8958   7780   5195   -339   1043  -1076       C  
ATOM   1291  N   PHE A 220     -31.499  -8.901  11.509  1.00 67.54           N  
ANISOU 1291  N   PHE A 220    10092   8870   6701   -150    585   -756       N  
ATOM   1292  CA  PHE A 220     -31.549  -7.911  10.439  1.00 59.82           C  
ANISOU 1292  CA  PHE A 220     8981   7815   5933   -108    542   -790       C  
ATOM   1293  C   PHE A 220     -30.475  -8.152   9.385  1.00 65.30           C  
ANISOU 1293  C   PHE A 220     9651   8466   6696    -54    434   -659       C  
ATOM   1294  O   PHE A 220     -30.557  -7.628   8.274  1.00 72.46           O  
ANISOU 1294  O   PHE A 220    10464   9309   7758    -17    409   -642       O  
ATOM   1295  CB  PHE A 220     -31.411  -6.500  11.015  1.00 60.14           C  
ANISOU 1295  CB  PHE A 220     8966   7854   6032   -110    513   -935       C  
ATOM   1296  CG  PHE A 220     -32.572  -6.086  11.873  1.00 76.67           C  
ANISOU 1296  CG  PHE A 220    11053   9978   8098   -158    633  -1091       C  
ATOM   1297  CD1 PHE A 220     -33.805  -5.813  11.304  1.00 83.40           C  
ANISOU 1297  CD1 PHE A 220    11812  10778   9098   -161    718  -1152       C  
ATOM   1298  CD2 PHE A 220     -32.434  -5.978  13.247  1.00 85.44           C  
ANISOU 1298  CD2 PHE A 220    12252  11174   9038   -198    660  -1183       C  
ATOM   1299  CE1 PHE A 220     -34.877  -5.435  12.088  1.00 86.16           C  
ANISOU 1299  CE1 PHE A 220    12142  11152   9443   -205    840  -1306       C  
ATOM   1300  CE2 PHE A 220     -33.503  -5.600  14.037  1.00 88.71           C  
ANISOU 1300  CE2 PHE A 220    12660  11624   9422   -244    790  -1337       C  
ATOM   1301  CZ  PHE A 220     -34.726  -5.328  13.457  1.00 86.46           C  
ANISOU 1301  CZ  PHE A 220    12268  11279   9305   -249    886  -1401       C  
ATOM   1302  N   GLY A 221     -29.470  -8.946   9.736  1.00 60.42           N  
ANISOU 1302  N   GLY A 221     9116   7881   5960    -48    371   -566       N  
ATOM   1303  CA  GLY A 221     -28.416  -9.280   8.799  1.00 30.82           C  
ANISOU 1303  CA  GLY A 221     5342   4093   2275      0    284   -449       C  
ATOM   1304  C   GLY A 221     -28.858 -10.370   7.847  1.00 59.54           C  
ANISOU 1304  C   GLY A 221     8985   7708   5931     14    328   -355       C  
ATOM   1305  O   GLY A 221     -28.305 -10.511   6.760  1.00 65.69           O  
ANISOU 1305  O   GLY A 221     9719   8448   6794     57    285   -280       O  
ATOM   1306  N   SER A 222     -29.856 -11.144   8.259  1.00 58.17           N  
ANISOU 1306  N   SER A 222     8864   7557   5681    -25    420   -364       N  
ATOM   1307  CA  SER A 222     -30.416 -12.185   7.406  1.00 57.35           C  
ANISOU 1307  CA  SER A 222     8757   7424   5610    -16    465   -296       C  
ATOM   1308  C   SER A 222     -31.459 -11.592   6.467  1.00 53.48           C  
ANISOU 1308  C   SER A 222     8169   6892   5259     -3    507   -358       C  
ATOM   1309  O   SER A 222     -31.594 -12.021   5.320  1.00 58.24           O  
ANISOU 1309  O   SER A 222     8736   7460   5933     31    493   -307       O  
ATOM   1310  CB  SER A 222     -31.032 -13.306   8.245  1.00 55.34           C  
ANISOU 1310  CB  SER A 222     8593   7197   5235    -67    547   -272       C  
ATOM   1311  OG  SER A 222     -30.032 -14.065   8.901  1.00 58.20           O  
ANISOU 1311  OG  SER A 222     9050   7585   5477    -68    489   -181       O  
ATOM   1312  N   LEU A 223     -32.195 -10.601   6.961  1.00 46.86           N  
ANISOU 1312  N   LEU A 223     7289   6056   4460    -28    551   -473       N  
ATOM   1313  CA  LEU A 223     -33.188  -9.912   6.150  1.00 50.18           C  
ANISOU 1313  CA  LEU A 223     7609   6428   5031    -12    574   -539       C  
ATOM   1314  C   LEU A 223     -32.526  -9.211   4.967  1.00 54.02           C  
ANISOU 1314  C   LEU A 223     8030   6871   5626     47    480   -488       C  
ATOM   1315  O   LEU A 223     -33.015  -9.284   3.841  1.00 58.44           O  
ANISOU 1315  O   LEU A 223     8540   7392   6271     80    468   -462       O  
ATOM   1316  CB  LEU A 223     -33.965  -8.899   6.992  1.00 53.50           C  
ANISOU 1316  CB  LEU A 223     7987   6853   5488    -46    633   -683       C  
ATOM   1317  CG  LEU A 223     -34.781  -9.454   8.160  1.00 59.00           C  
ANISOU 1317  CG  LEU A 223     8741   7596   6079   -112    755   -749       C  
ATOM   1318  CD1 LEU A 223     -35.434  -8.319   8.930  1.00 56.48           C  
ANISOU 1318  CD1 LEU A 223     8369   7282   5807   -140    813   -910       C  
ATOM   1319  CD2 LEU A 223     -35.825 -10.451   7.679  1.00 68.40           C  
ANISOU 1319  CD2 LEU A 223     9918   8763   7310   -128    832   -728       C  
ATOM   1320  N   ALA A 224     -31.408  -8.543   5.230  1.00 46.00           N  
ANISOU 1320  N   ALA A 224     7015   5858   4603     60    414   -472       N  
ATOM   1321  CA  ALA A 224     -30.705  -7.789   4.199  1.00 42.35           C  
ANISOU 1321  CA  ALA A 224     6492   5351   4249    108    341   -417       C  
ATOM   1322  C   ALA A 224     -29.971  -8.702   3.227  1.00 47.62           C  
ANISOU 1322  C   ALA A 224     7186   6021   4886    144    310   -293       C  
ATOM   1323  O   ALA A 224     -29.834  -8.383   2.046  1.00 55.24           O  
ANISOU 1323  O   ALA A 224     8108   6954   5928    184    281   -238       O  
ATOM   1324  CB  ALA A 224     -29.723  -6.810   4.834  1.00 36.67           C  
ANISOU 1324  CB  ALA A 224     5753   4626   3554    105    286   -449       C  
ATOM   1325  N   ALA A 225     -29.496  -9.837   3.727  1.00 41.48           N  
ANISOU 1325  N   ALA A 225     6485   5282   3995    130    316   -247       N  
ATOM   1326  CA  ALA A 225     -28.635 -10.700   2.932  1.00 38.15           C  
ANISOU 1326  CA  ALA A 225     6083   4858   3553    165    284   -143       C  
ATOM   1327  C   ALA A 225     -29.403 -11.765   2.158  1.00 43.87           C  
ANISOU 1327  C   ALA A 225     6822   5580   4266    176    323   -118       C  
ATOM   1328  O   ALA A 225     -28.930 -12.238   1.126  1.00 52.20           O  
ANISOU 1328  O   ALA A 225     7870   6627   5336    215    302    -53       O  
ATOM   1329  CB  ALA A 225     -27.598 -11.355   3.821  1.00 40.30           C  
ANISOU 1329  CB  ALA A 225     6418   5158   3736    154    249   -104       C  
ATOM   1330  N   PHE A 226     -30.578 -12.149   2.647  1.00 39.20           N  
ANISOU 1330  N   PHE A 226     6246   4993   3654    140    383   -176       N  
ATOM   1331  CA  PHE A 226     -31.312 -13.235   2.009  1.00 41.71           C  
ANISOU 1331  CA  PHE A 226     6571   5301   3977    145    416   -162       C  
ATOM   1332  C   PHE A 226     -32.769 -12.909   1.690  1.00 39.30           C  
ANISOU 1332  C   PHE A 226     6210   4972   3750    136    456   -243       C  
ATOM   1333  O   PHE A 226     -33.192 -13.019   0.542  1.00 44.98           O  
ANISOU 1333  O   PHE A 226     6891   5670   4527    172    431   -239       O  
ATOM   1334  CB  PHE A 226     -31.255 -14.491   2.879  1.00 39.96           C  
ANISOU 1334  CB  PHE A 226     6425   5092   3666    109    454   -131       C  
ATOM   1335  CG  PHE A 226     -31.986 -15.666   2.290  1.00 42.59           C  
ANISOU 1335  CG  PHE A 226     6758   5401   4024    109    489   -123       C  
ATOM   1336  CD1 PHE A 226     -31.460 -16.352   1.209  1.00 26.75           C  
ANISOU 1336  CD1 PHE A 226     4744   3379   2039    156    447    -72       C  
ATOM   1337  CD2 PHE A 226     -33.197 -16.085   2.820  1.00 47.71           C  
ANISOU 1337  CD2 PHE A 226     7407   6037   4683     61    570   -176       C  
ATOM   1338  CE1 PHE A 226     -32.131 -17.431   0.664  1.00 36.49           C  
ANISOU 1338  CE1 PHE A 226     5972   4586   3307    158    472    -81       C  
ATOM   1339  CE2 PHE A 226     -33.871 -17.163   2.280  1.00 27.76           C  
ANISOU 1339  CE2 PHE A 226     4868   3476   2203     59    598   -176       C  
ATOM   1340  CZ  PHE A 226     -33.337 -17.837   1.202  1.00 36.48           C  
ANISOU 1340  CZ  PHE A 226     5966   4565   3331    109    542   -132       C  
ATOM   1341  N   PHE A 227     -33.540 -12.520   2.696  1.00 36.80           N  
ANISOU 1341  N   PHE A 227     5888   4661   3435     88    516   -324       N  
ATOM   1342  CA  PHE A 227     -34.977 -12.355   2.502  1.00 41.93           C  
ANISOU 1342  CA  PHE A 227     6474   5281   4177     74    564   -412       C  
ATOM   1343  C   PHE A 227     -35.318 -11.150   1.631  1.00 46.40           C  
ANISOU 1343  C   PHE A 227     6955   5811   4862    116    506   -448       C  
ATOM   1344  O   PHE A 227     -36.362 -11.130   0.977  1.00 52.41           O  
ANISOU 1344  O   PHE A 227     7656   6538   5719    130    504   -495       O  
ATOM   1345  CB  PHE A 227     -35.685 -12.260   3.855  1.00 36.79           C  
ANISOU 1345  CB  PHE A 227     5836   4646   3496      8    663   -496       C  
ATOM   1346  CG  PHE A 227     -35.620 -13.532   4.648  1.00 37.92           C  
ANISOU 1346  CG  PHE A 227     6065   4814   3527    -39    730   -450       C  
ATOM   1347  CD1 PHE A 227     -36.486 -14.577   4.371  1.00 43.48           C  
ANISOU 1347  CD1 PHE A 227     6758   5489   4273    -58    787   -451       C  
ATOM   1348  CD2 PHE A 227     -34.680 -13.695   5.651  1.00 46.15           C  
ANISOU 1348  CD2 PHE A 227     7198   5902   4433    -61    727   -401       C  
ATOM   1349  CE1 PHE A 227     -36.424 -15.757   5.086  1.00 48.86           C  
ANISOU 1349  CE1 PHE A 227     7518   6179   4866   -103    851   -394       C  
ATOM   1350  CE2 PHE A 227     -34.613 -14.874   6.373  1.00 53.57           C  
ANISOU 1350  CE2 PHE A 227     8226   6858   5270   -102    780   -340       C  
ATOM   1351  CZ  PHE A 227     -35.487 -15.906   6.090  1.00 48.91           C  
ANISOU 1351  CZ  PHE A 227     7625   6232   4728   -124    848   -331       C  
ATOM   1352  N   THR A 228     -34.436 -10.155   1.605  1.00 43.95           N  
ANISOU 1352  N   THR A 228     6638   5502   4560    138    453   -421       N  
ATOM   1353  CA  THR A 228     -34.640  -9.008   0.728  1.00 38.03           C  
ANISOU 1353  CA  THR A 228     5814   4708   3927    180    392   -428       C  
ATOM   1354  C   THR A 228     -34.328  -9.365  -0.730  1.00 44.27           C  
ANISOU 1354  C   THR A 228     6611   5494   4716    236    329   -335       C  
ATOM   1355  O   THR A 228     -35.145  -9.089  -1.610  1.00 43.39           O  
ANISOU 1355  O   THR A 228     6452   5352   4684    268    291   -351       O  
ATOM   1356  CB  THR A 228     -33.798  -7.795   1.162  1.00 39.39           C  
ANISOU 1356  CB  THR A 228     5969   4870   4129    181    360   -428       C  
ATOM   1357  OG1 THR A 228     -34.120  -7.451   2.516  1.00 50.26           O  
ANISOU 1357  OG1 THR A 228     7344   6260   5494    131    417   -533       O  
ATOM   1358  CG2 THR A 228     -34.076  -6.606   0.257  1.00 35.77           C  
ANISOU 1358  CG2 THR A 228     5433   4350   3808    222    300   -422       C  
ATOM   1359  N   PRO A 229     -33.163  -9.989  -1.004  1.00 52.32           N  
ANISOU 1359  N   PRO A 229     7688   6546   5646    251    314   -244       N  
ATOM   1360  CA  PRO A 229     -33.023 -10.407  -2.404  1.00 38.97           C  
ANISOU 1360  CA  PRO A 229     6005   4860   3943    303    271   -177       C  
ATOM   1361  C   PRO A 229     -33.988 -11.537  -2.770  1.00 31.67           C  
ANISOU 1361  C   PRO A 229     5086   3938   3009    304    286   -218       C  
ATOM   1362  O   PRO A 229     -34.268 -11.723  -3.949  1.00 31.81           O  
ANISOU 1362  O   PRO A 229     5097   3956   3035    348    239   -200       O  
ATOM   1363  CB  PRO A 229     -31.563 -10.871  -2.492  1.00 28.66           C  
ANISOU 1363  CB  PRO A 229     4748   3584   2557    314    268    -91       C  
ATOM   1364  CG  PRO A 229     -31.178 -11.199  -1.105  1.00 26.22           C  
ANISOU 1364  CG  PRO A 229     4471   3289   2203    266    304   -115       C  
ATOM   1365  CD  PRO A 229     -31.929 -10.240  -0.236  1.00 50.17           C  
ANISOU 1365  CD  PRO A 229     7466   6303   5293    232    322   -201       C  
ATOM   1366  N   LEU A 230     -34.498 -12.266  -1.779  1.00 43.78           N  
ANISOU 1366  N   LEU A 230     6632   5473   4528    254    349   -273       N  
ATOM   1367  CA  LEU A 230     -35.520 -13.280  -2.037  1.00 47.39           C  
ANISOU 1367  CA  LEU A 230     7078   5917   5013    246    371   -323       C  
ATOM   1368  C   LEU A 230     -36.835 -12.620  -2.446  1.00 47.78           C  
ANISOU 1368  C   LEU A 230     7047   5927   5181    257    347   -405       C  
ATOM   1369  O   LEU A 230     -37.481 -13.055  -3.394  1.00 50.23           O  
ANISOU 1369  O   LEU A 230     7331   6222   5530    289    302   -427       O  
ATOM   1370  CB  LEU A 230     -35.739 -14.175  -0.810  1.00 47.99           C  
ANISOU 1370  CB  LEU A 230     7188   5995   5051    183    459   -347       C  
ATOM   1371  CG  LEU A 230     -36.915 -15.164  -0.842  1.00 60.91           C  
ANISOU 1371  CG  LEU A 230     8797   7601   6746    157    505   -409       C  
ATOM   1372  CD1 LEU A 230     -36.796 -16.133  -2.009  1.00 27.40           C  
ANISOU 1372  CD1 LEU A 230     4559   3350   2501    201    452   -383       C  
ATOM   1373  CD2 LEU A 230     -37.035 -15.930   0.472  1.00 28.01           C  
ANISOU 1373  CD2 LEU A 230     4676   3436   2532     87    606   -409       C  
ATOM   1374  N   ALA A 231     -37.225 -11.568  -1.731  1.00 40.67           N  
ANISOU 1374  N   ALA A 231     6103   5007   4345    233    369   -460       N  
ATOM   1375  CA  ALA A 231     -38.460 -10.849  -2.041  1.00 44.55           C  
ANISOU 1375  CA  ALA A 231     6503   5448   4976    246    342   -546       C  
ATOM   1376  C   ALA A 231     -38.396 -10.217  -3.426  1.00 50.08           C  
ANISOU 1376  C   ALA A 231     7182   6132   5712    317    226   -493       C  
ATOM   1377  O   ALA A 231     -39.365 -10.266  -4.187  1.00 49.49           O  
ANISOU 1377  O   ALA A 231     7056   6027   5720    348    168   -537       O  
ATOM   1378  CB  ALA A 231     -38.740  -9.782  -0.990  1.00 29.27           C  
ANISOU 1378  CB  ALA A 231     4521   3492   3107    210    391   -620       C  
ATOM   1379  N   ILE A 232     -37.251  -9.621  -3.741  1.00 43.92           N  
ANISOU 1379  N   ILE A 232     6444   5372   4872    343    191   -398       N  
ATOM   1380  CA  ILE A 232     -37.039  -9.003  -5.043  1.00 43.25           C  
ANISOU 1380  CA  ILE A 232     6359   5279   4796    406     95   -321       C  
ATOM   1381  C   ILE A 232     -37.174 -10.031  -6.163  1.00 48.59           C  
ANISOU 1381  C   ILE A 232     7073   5987   5401    445     51   -297       C  
ATOM   1382  O   ILE A 232     -37.858  -9.791  -7.159  1.00 51.46           O  
ANISOU 1382  O   ILE A 232     7413   6335   5804    493    -36   -301       O  
ATOM   1383  CB  ILE A 232     -35.656  -8.329  -5.121  1.00 37.50           C  
ANISOU 1383  CB  ILE A 232     5670   4566   4012    415     92   -216       C  
ATOM   1384  CG1 ILE A 232     -35.580  -7.174  -4.121  1.00 27.99           C  
ANISOU 1384  CG1 ILE A 232     4417   3319   2899    384    115   -255       C  
ATOM   1385  CG2 ILE A 232     -35.384  -7.822  -6.526  1.00 38.05           C  
ANISOU 1385  CG2 ILE A 232     5756   4634   4066    476     12   -117       C  
ATOM   1386  CD1 ILE A 232     -34.190  -6.624  -3.929  1.00 27.75           C  
ANISOU 1386  CD1 ILE A 232     4413   3298   2833    379    123   -173       C  
ATOM   1387  N   MET A 233     -36.540 -11.185  -5.982  1.00 46.40           N  
ANISOU 1387  N   MET A 233     6853   5753   5023    428    102   -278       N  
ATOM   1388  CA  MET A 233     -36.577 -12.241  -6.987  1.00 39.33           C  
ANISOU 1388  CA  MET A 233     5992   4888   4062    464     68   -271       C  
ATOM   1389  C   MET A 233     -37.965 -12.859  -7.135  1.00 43.02           C  
ANISOU 1389  C   MET A 233     6407   5326   4614    461     44   -378       C  
ATOM   1390  O   MET A 233     -38.296 -13.406  -8.186  1.00 46.90           O  
ANISOU 1390  O   MET A 233     6907   5831   5082    505    -24   -394       O  
ATOM   1391  CB  MET A 233     -35.544 -13.318  -6.655  1.00 36.36           C  
ANISOU 1391  CB  MET A 233     5677   4550   3588    444    130   -233       C  
ATOM   1392  CG  MET A 233     -34.116 -12.836  -6.859  1.00 38.50           C  
ANISOU 1392  CG  MET A 233     5992   4853   3784    461    138   -129       C  
ATOM   1393  SD  MET A 233     -32.861 -13.875  -6.101  1.00 61.15           S  
ANISOU 1393  SD  MET A 233     8910   7745   6580    431    206    -91       S  
ATOM   1394  CE  MET A 233     -32.823 -15.237  -7.258  1.00 33.82           C  
ANISOU 1394  CE  MET A 233     5479   4312   3060    474    189   -104       C  
ATOM   1395  N   ILE A 234     -38.774 -12.767  -6.085  1.00 44.17           N  
ANISOU 1395  N   ILE A 234     6495   5429   4859    410    101   -459       N  
ATOM   1396  CA  ILE A 234     -40.163 -13.211  -6.152  1.00 47.45           C  
ANISOU 1396  CA  ILE A 234     6836   5801   5392    402     87   -570       C  
ATOM   1397  C   ILE A 234     -40.967 -12.224  -6.987  1.00 51.26           C  
ANISOU 1397  C   ILE A 234     7257   6249   5972    454    -27   -597       C  
ATOM   1398  O   ILE A 234     -41.765 -12.613  -7.838  1.00 60.74           O  
ANISOU 1398  O   ILE A 234     8424   7435   7222    491   -111   -650       O  
ATOM   1399  CB  ILE A 234     -40.792 -13.344  -4.749  1.00 48.43           C  
ANISOU 1399  CB  ILE A 234     6913   5890   5597    325    204   -648       C  
ATOM   1400  CG1 ILE A 234     -40.182 -14.530  -3.999  1.00 46.45           C  
ANISOU 1400  CG1 ILE A 234     6728   5664   5255    276    302   -617       C  
ATOM   1401  CG2 ILE A 234     -42.302 -13.511  -4.846  1.00 39.78           C  
ANISOU 1401  CG2 ILE A 234     5714   4735   4664    317    192   -771       C  
ATOM   1402  CD1 ILE A 234     -40.710 -14.698  -2.591  1.00 30.41           C  
ANISOU 1402  CD1 ILE A 234     4675   3612   3266    197    429   -674       C  
ATOM   1403  N   VAL A 235     -40.732 -10.940  -6.738  1.00 50.34           N  
ANISOU 1403  N   VAL A 235     7124   6115   5889    460    -39   -560       N  
ATOM   1404  CA  VAL A 235     -41.382  -9.863  -7.475  1.00 40.19           C  
ANISOU 1404  CA  VAL A 235     5782   4785   4705    512   -154   -564       C  
ATOM   1405  C   VAL A 235     -40.997  -9.866  -8.956  1.00 39.96           C  
ANISOU 1405  C   VAL A 235     5817   4794   4574    585   -273   -472       C  
ATOM   1406  O   VAL A 235     -41.866  -9.797  -9.825  1.00 40.88           O  
ANISOU 1406  O   VAL A 235     5898   4888   4747    634   -389   -507       O  
ATOM   1407  CB  VAL A 235     -41.037  -8.493  -6.858  1.00 36.18           C  
ANISOU 1407  CB  VAL A 235     5247   4242   4259    499   -134   -534       C  
ATOM   1408  CG1 VAL A 235     -41.497  -7.361  -7.762  1.00 32.25           C  
ANISOU 1408  CG1 VAL A 235     4707   3692   3856    562   -267   -500       C  
ATOM   1409  CG2 VAL A 235     -41.663  -8.368  -5.477  1.00 30.63           C  
ANISOU 1409  CG2 VAL A 235     4471   3501   3666    434    -28   -652       C  
ATOM   1410  N   THR A 236     -39.700  -9.956  -9.242  1.00 38.35           N  
ANISOU 1410  N   THR A 236     5706   4649   4218    593   -244   -360       N  
ATOM   1411  CA  THR A 236     -39.232  -9.985 -10.628  1.00 43.35           C  
ANISOU 1411  CA  THR A 236     6412   5332   4727    658   -330   -269       C  
ATOM   1412  C   THR A 236     -39.771 -11.200 -11.381  1.00 42.97           C  
ANISOU 1412  C   THR A 236     6380   5318   4629    685   -381   -339       C  
ATOM   1413  O   THR A 236     -39.987 -11.143 -12.592  1.00 47.18           O  
ANISOU 1413  O   THR A 236     6948   5879   5100    748   -492   -314       O  
ATOM   1414  CB  THR A 236     -37.694  -9.994 -10.716  1.00 49.40           C  
ANISOU 1414  CB  THR A 236     7263   6155   5350    653   -261   -151       C  
ATOM   1415  OG1 THR A 236     -37.182 -11.136 -10.021  1.00 73.48           O  
ANISOU 1415  OG1 THR A 236    10336   9235   8348    610   -163   -188       O  
ATOM   1416  CG2 THR A 236     -37.110  -8.728 -10.110  1.00 44.76           C  
ANISOU 1416  CG2 THR A 236     6656   5529   4821    631   -228    -82       C  
ATOM   1417  N   TYR A 237     -39.987 -12.294 -10.657  1.00 45.95           N  
ANISOU 1417  N   TYR A 237     6734   5690   5035    638   -302   -427       N  
ATOM   1418  CA  TYR A 237     -40.514 -13.522 -11.248  1.00 49.83           C  
ANISOU 1418  CA  TYR A 237     7225   6197   5511    656   -342   -511       C  
ATOM   1419  C   TYR A 237     -41.877 -13.301 -11.891  1.00 45.52           C  
ANISOU 1419  C   TYR A 237     6607   5609   5080    697   -473   -599       C  
ATOM   1420  O   TYR A 237     -42.111 -13.695 -13.034  1.00 44.88           O  
ANISOU 1420  O   TYR A 237     6555   5562   4934    754   -583   -619       O  
ATOM   1421  CB  TYR A 237     -40.619 -14.624 -10.191  1.00 52.98           C  
ANISOU 1421  CB  TYR A 237     7596   6573   5962    589   -226   -582       C  
ATOM   1422  CG  TYR A 237     -41.373 -15.848 -10.661  1.00 30.80           C  
ANISOU 1422  CG  TYR A 237     4757   3750   3197    597   -264   -690       C  
ATOM   1423  CD1 TYR A 237     -40.733 -16.844 -11.378  1.00 30.80           C  
ANISOU 1423  CD1 TYR A 237     4821   3799   3082    625   -275   -683       C  
ATOM   1424  CD2 TYR A 237     -42.727 -16.005 -10.387  1.00 31.93           C  
ANISOU 1424  CD2 TYR A 237     4795   3824   3513    578   -287   -809       C  
ATOM   1425  CE1 TYR A 237     -41.417 -17.963 -11.813  1.00 37.55           C  
ANISOU 1425  CE1 TYR A 237     5641   4634   3994    633   -316   -794       C  
ATOM   1426  CE2 TYR A 237     -43.419 -17.117 -10.818  1.00 32.09           C  
ANISOU 1426  CE2 TYR A 237     4775   3821   3597    584   -326   -914       C  
ATOM   1427  CZ  TYR A 237     -42.760 -18.093 -11.530  1.00 33.98           C  
ANISOU 1427  CZ  TYR A 237     5083   4108   3719    612   -345   -908       C  
ATOM   1428  OH  TYR A 237     -43.444 -19.207 -11.959  1.00 33.50           O  
ANISOU 1428  OH  TYR A 237     4975   4016   3737    618   -388  -1025       O  
ATOM   1429  N   PHE A 238     -42.780 -12.679 -11.142  1.00 43.98           N  
ANISOU 1429  N   PHE A 238     6313   5340   5058    667   -465   -662       N  
ATOM   1430  CA  PHE A 238     -44.128 -12.434 -11.629  1.00 41.00           C  
ANISOU 1430  CA  PHE A 238     5843   4905   4830    703   -591   -757       C  
ATOM   1431  C   PHE A 238     -44.132 -11.325 -12.671  1.00 45.58           C  
ANISOU 1431  C   PHE A 238     6453   5492   5373    779   -742   -673       C  
ATOM   1432  O   PHE A 238     -44.935 -11.345 -13.605  1.00 44.83           O  
ANISOU 1432  O   PHE A 238     6334   5386   5314    838   -896   -719       O  
ATOM   1433  CB  PHE A 238     -45.064 -12.096 -10.467  1.00 33.32           C  
ANISOU 1433  CB  PHE A 238     4745   3846   4067    646   -518   -858       C  
ATOM   1434  CG  PHE A 238     -45.397 -13.278  -9.601  1.00 39.99           C  
ANISOU 1434  CG  PHE A 238     5551   4674   4970    575   -390   -952       C  
ATOM   1435  CD1 PHE A 238     -46.195 -14.299 -10.086  1.00 39.22           C  
ANISOU 1435  CD1 PHE A 238     5403   4554   4944    584   -442  -1056       C  
ATOM   1436  CD2 PHE A 238     -44.915 -13.370  -8.305  1.00 40.04           C  
ANISOU 1436  CD2 PHE A 238     5571   4681   4960    499   -221   -935       C  
ATOM   1437  CE1 PHE A 238     -46.506 -15.393  -9.298  1.00 37.19           C  
ANISOU 1437  CE1 PHE A 238     5107   4268   4757    515   -317  -1131       C  
ATOM   1438  CE2 PHE A 238     -45.224 -14.460  -7.511  1.00 35.39           C  
ANISOU 1438  CE2 PHE A 238     4956   4073   4417    432   -100  -1001       C  
ATOM   1439  CZ  PHE A 238     -46.020 -15.473  -8.009  1.00 34.93           C  
ANISOU 1439  CZ  PHE A 238     4844   3983   4445    438   -143  -1094       C  
ATOM   1440  N   LEU A 239     -43.225 -10.366 -12.515  1.00 42.14           N  
ANISOU 1440  N   LEU A 239     6071   5070   4870    778   -704   -546       N  
ATOM   1441  CA  LEU A 239     -43.067  -9.307 -13.503  1.00 36.90           C  
ANISOU 1441  CA  LEU A 239     5452   4411   4157    845   -831   -432       C  
ATOM   1442  C   LEU A 239     -42.626  -9.887 -14.847  1.00 43.67           C  
ANISOU 1442  C   LEU A 239     6424   5361   4810    905   -913   -374       C  
ATOM   1443  O   LEU A 239     -43.041  -9.407 -15.900  1.00 51.91           O  
ANISOU 1443  O   LEU A 239     7493   6409   5822    973  -1068   -332       O  
ATOM   1444  CB  LEU A 239     -42.062  -8.259 -13.020  1.00 33.74           C  
ANISOU 1444  CB  LEU A 239     5085   4003   3732    822   -752   -306       C  
ATOM   1445  CG  LEU A 239     -42.512  -7.290 -11.925  1.00 34.58           C  
ANISOU 1445  CG  LEU A 239     5085   4015   4040    783   -709   -352       C  
ATOM   1446  CD1 LEU A 239     -41.398  -6.310 -11.603  1.00 40.60           C  
ANISOU 1446  CD1 LEU A 239     5887   4773   4765    766   -646   -226       C  
ATOM   1447  CD2 LEU A 239     -43.778  -6.546 -12.329  1.00 34.94           C  
ANISOU 1447  CD2 LEU A 239     5036   3975   4266    830   -857   -404       C  
ATOM   1448  N   THR A 240     -41.792 -10.924 -14.803  1.00 36.14           N  
ANISOU 1448  N   THR A 240     5537   4478   3717    880   -813   -374       N  
ATOM   1449  CA  THR A 240     -41.309 -11.576 -16.019  1.00 34.64           C  
ANISOU 1449  CA  THR A 240     5453   4383   3328    932   -866   -342       C  
ATOM   1450  C   THR A 240     -42.438 -12.306 -16.746  1.00 42.93           C  
ANISOU 1450  C   THR A 240     6469   5432   4411    976  -1007   -474       C  
ATOM   1451  O   THR A 240     -42.516 -12.268 -17.973  1.00 49.61           O  
ANISOU 1451  O   THR A 240     7387   6336   5126   1045  -1135   -446       O  
ATOM   1452  CB  THR A 240     -40.175 -12.580 -15.719  1.00 33.63           C  
ANISOU 1452  CB  THR A 240     5383   4316   3078    895   -721   -334       C  
ATOM   1453  OG1 THR A 240     -39.079 -11.899 -15.099  1.00 40.01           O  
ANISOU 1453  OG1 THR A 240     6219   5125   3858    858   -606   -215       O  
ATOM   1454  CG2 THR A 240     -39.687 -13.233 -17.003  1.00 34.37           C  
ANISOU 1454  CG2 THR A 240     5580   4509   2971    950   -768   -319       C  
ATOM   1455  N   ILE A 241     -43.307 -12.968 -15.987  1.00 35.49           N  
ANISOU 1455  N   ILE A 241     5418   4424   3643    935   -981   -618       N  
ATOM   1456  CA  ILE A 241     -44.470 -13.639 -16.563  1.00 36.61           C  
ANISOU 1456  CA  ILE A 241     5498   4544   3867    971  -1115   -762       C  
ATOM   1457  C   ILE A 241     -45.343 -12.635 -17.308  1.00 46.07           C  
ANISOU 1457  C   ILE A 241     6668   5709   5127   1039  -1309   -748       C  
ATOM   1458  O   ILE A 241     -45.788 -12.890 -18.429  1.00 46.44           O  
ANISOU 1458  O   ILE A 241     6749   5794   5101   1107  -1473   -787       O  
ATOM   1459  CB  ILE A 241     -45.320 -14.347 -15.486  1.00 50.13           C  
ANISOU 1459  CB  ILE A 241     7078   6170   5800    903  -1036   -909       C  
ATOM   1460  CG1 ILE A 241     -44.495 -15.408 -14.754  1.00 35.05           C  
ANISOU 1460  CG1 ILE A 241     5201   4284   3832    839   -860   -913       C  
ATOM   1461  CG2 ILE A 241     -46.563 -14.971 -16.104  1.00 45.79           C  
ANISOU 1461  CG2 ILE A 241     6445   5583   5369    940  -1184  -1065       C  
ATOM   1462  CD1 ILE A 241     -44.123 -16.580 -15.613  1.00 35.39           C  
ANISOU 1462  CD1 ILE A 241     5310   4392   3744    871   -892   -958       C  
ATOM   1463  N   HIS A 242     -45.574 -11.487 -16.680  1.00 41.66           N  
ANISOU 1463  N   HIS A 242     6048   5077   4702   1022  -1296   -695       N  
ATOM   1464  CA  HIS A 242     -46.371 -10.430 -17.287  1.00 48.83           C  
ANISOU 1464  CA  HIS A 242     6920   5934   5700   1086  -1479   -668       C  
ATOM   1465  C   HIS A 242     -45.697  -9.882 -18.539  1.00 49.39           C  
ANISOU 1465  C   HIS A 242     7139   6088   5540   1158  -1586   -508       C  
ATOM   1466  O   HIS A 242     -46.360  -9.613 -19.541  1.00 41.68           O  
ANISOU 1466  O   HIS A 242     6179   5114   4543   1234  -1786   -507       O  
ATOM   1467  CB  HIS A 242     -46.615  -9.299 -16.286  1.00 57.27           C  
ANISOU 1467  CB  HIS A 242     7891   6902   6966   1049  -1420   -643       C  
ATOM   1468  CG  HIS A 242     -47.491  -8.201 -16.816  1.00 73.28           C  
ANISOU 1468  CG  HIS A 242     9859   8853   9131   1114  -1611   -623       C  
ATOM   1469  ND1 HIS A 242     -48.790  -8.424 -17.220  1.00 80.81           N  
ANISOU 1469  ND1 HIS A 242    10712   9750  10243   1157  -1776   -755       N  
ATOM   1470  CD2 HIS A 242     -47.250  -6.888 -17.008  1.00 79.85           C  
ANISOU 1470  CD2 HIS A 242    10714   9645   9981   1145  -1668   -484       C  
ATOM   1471  CE1 HIS A 242     -49.313  -7.283 -17.638  1.00 86.56           C  
ANISOU 1471  CE1 HIS A 242    11404  10408  11078   1215  -1935   -697       C  
ATOM   1472  NE2 HIS A 242     -48.406  -6.336 -17.522  1.00 88.77           N  
ANISOU 1472  NE2 HIS A 242    11759  10694  11277   1209  -1872   -529       N  
ATOM   1473  N   ALA A 243     -44.379  -9.723 -18.473  1.00 39.18           N  
ANISOU 1473  N   ALA A 243     5953   4860   4073   1133  -1452   -372       N  
ATOM   1474  CA  ALA A 243     -43.608  -9.214 -19.599  1.00 40.03           C  
ANISOU 1474  CA  ALA A 243     6207   5051   3951   1189  -1510   -206       C  
ATOM   1475  C   ALA A 243     -43.711 -10.137 -20.813  1.00 56.46           C  
ANISOU 1475  C   ALA A 243     8381   7236   5835   1249  -1618   -258       C  
ATOM   1476  O   ALA A 243     -43.925  -9.678 -21.936  1.00 42.77           O  
ANISOU 1476  O   ALA A 243     6729   5543   3978   1322  -1778   -183       O  
ATOM   1477  CB  ALA A 243     -42.154  -9.028 -19.201  1.00 38.81           C  
ANISOU 1477  CB  ALA A 243     6129   4942   3676   1141  -1321    -77       C  
ATOM   1478  N   LEU A 244     -43.565 -11.438 -20.579  1.00 45.78           N  
ANISOU 1478  N   LEU A 244     7017   5924   4454   1218  -1533   -387       N  
ATOM   1479  CA  LEU A 244     -43.585 -12.419 -21.658  1.00 41.45           C  
ANISOU 1479  CA  LEU A 244     6550   5474   3726   1269  -1616   -463       C  
ATOM   1480  C   LEU A 244     -44.974 -12.553 -22.276  1.00 61.33           C  
ANISOU 1480  C   LEU A 244     9007   7959   6339   1330  -1846   -590       C  
ATOM   1481  O   LEU A 244     -45.109 -12.711 -23.488  1.00 52.84           O  
ANISOU 1481  O   LEU A 244     8026   6966   5084   1403  -1996   -593       O  
ATOM   1482  CB  LEU A 244     -43.101 -13.778 -21.149  1.00 40.30           C  
ANISOU 1482  CB  LEU A 244     6386   5354   3571   1217  -1466   -577       C  
ATOM   1483  CG  LEU A 244     -41.654 -13.827 -20.645  1.00 43.69           C  
ANISOU 1483  CG  LEU A 244     6880   5827   3895   1165  -1256   -467       C  
ATOM   1484  CD1 LEU A 244     -41.386 -15.119 -19.887  1.00 40.92           C  
ANISOU 1484  CD1 LEU A 244     6478   5462   3608   1108  -1123   -585       C  
ATOM   1485  CD2 LEU A 244     -40.665 -13.661 -21.790  1.00 39.75           C  
ANISOU 1485  CD2 LEU A 244     6536   5451   3117   1213  -1251   -349       C  
ATOM   1486  N   GLN A 245     -46.005 -12.491 -21.439  1.00 66.36           N  
ANISOU 1486  N   GLN A 245     9483   8474   7256   1299  -1872   -701       N  
ATOM   1487  CA  GLN A 245     -47.381 -12.560 -21.917  1.00 50.00           C  
ANISOU 1487  CA  GLN A 245     7322   6348   5327   1353  -2091   -833       C  
ATOM   1488  C   GLN A 245     -47.737 -11.300 -22.697  1.00 49.63           C  
ANISOU 1488  C   GLN A 245     7321   6291   5246   1430  -2284   -707       C  
ATOM   1489  O   GLN A 245     -48.445 -11.359 -23.701  1.00 49.43           O  
ANISOU 1489  O   GLN A 245     7318   6289   5174   1509  -2509   -756       O  
ATOM   1490  CB  GLN A 245     -48.351 -12.750 -20.748  1.00 61.35           C  
ANISOU 1490  CB  GLN A 245     8564   7652   7095   1293  -2039   -978       C  
ATOM   1491  CG  GLN A 245     -48.300 -14.128 -20.107  1.00 74.39           C  
ANISOU 1491  CG  GLN A 245    10159   9297   8807   1227  -1894  -1121       C  
ATOM   1492  CD  GLN A 245     -49.245 -14.257 -18.927  1.00 78.44           C  
ANISOU 1492  CD  GLN A 245    10486   9680   9637   1159  -1820  -1247       C  
ATOM   1493  OE1 GLN A 245     -49.760 -13.262 -18.416  1.00 77.02           O  
ANISOU 1493  OE1 GLN A 245    10221   9418   9624   1152  -1836  -1221       O  
ATOM   1494  NE2 GLN A 245     -49.476 -15.489 -18.486  1.00 83.19           N  
ANISOU 1494  NE2 GLN A 245    11022  10257  10328   1109  -1732  -1384       N  
ATOM   1495  N   LYS A 246     -47.239 -10.159 -22.231  1.00 57.47           N  
ANISOU 1495  N   LYS A 246     8326   7242   6266   1408  -2206   -544       N  
ATOM   1496  CA  LYS A 246     -47.493  -8.887 -22.900  1.00 46.75           C  
ANISOU 1496  CA  LYS A 246     7012   5857   4894   1475  -2375   -398       C  
ATOM   1497  C   LYS A 246     -46.713  -8.790 -24.206  1.00 55.80           C  
ANISOU 1497  C   LYS A 246     8363   7139   5697   1536  -2441   -247       C  
ATOM   1498  O   LYS A 246     -47.122  -8.096 -25.131  1.00 60.46           O  
ANISOU 1498  O   LYS A 246     9018   7736   6220   1614  -2644   -155       O  
ATOM   1499  CB  LYS A 246     -47.134  -7.712 -21.989  1.00 45.78           C  
ANISOU 1499  CB  LYS A 246     6836   5640   4917   1428  -2259   -274       C  
ATOM   1500  N   LYS A 247     -45.588  -9.492 -24.274  1.00 55.27           N  
ANISOU 1500  N   LYS A 247     8400   7182   5417   1501  -2266   -220       N  
ATOM   1501  CA  LYS A 247     -44.742  -9.466 -25.460  1.00 48.12           C  
ANISOU 1501  CA  LYS A 247     7691   6418   4175   1549  -2282    -86       C  
ATOM   1502  C   LYS A 247     -45.307 -10.361 -26.550  1.00 49.81           C  
ANISOU 1502  C   LYS A 247     7967   6726   4233   1620  -2459   -217       C  
ATOM   1503  O   LYS A 247     -45.341  -9.986 -27.725  1.00 51.81           O  
ANISOU 1503  O   LYS A 247     8357   7061   4269   1696  -2615   -123       O  
ATOM   1504  CB  LYS A 247     -43.320  -9.902 -25.114  1.00 46.58           C  
ANISOU 1504  CB  LYS A 247     7567   6299   3833   1486  -2024    -26       C  
ATOM   1505  CG  LYS A 247     -42.334  -9.734 -26.253  1.00 57.45           C  
ANISOU 1505  CG  LYS A 247     9139   7815   4876   1524  -1997    130       C  
ATOM   1506  CD  LYS A 247     -40.924 -10.053 -25.798  1.00 52.61           C  
ANISOU 1506  CD  LYS A 247     8565   7252   4172   1457  -1734    189       C  
ATOM   1507  CE  LYS A 247     -39.977  -8.905 -26.089  1.00 49.23           C  
ANISOU 1507  CE  LYS A 247     8236   6841   3629   1451  -1651    437       C  
ATOM   1508  NZ  LYS A 247     -38.600  -9.199 -25.613  1.00 47.32           N  
ANISOU 1508  NZ  LYS A 247     8013   6637   3328   1386  -1400    483       N  
ATOM   1509  N   ALA A 248     -45.741 -11.552 -26.149  1.00 55.34           N  
ANISOU 1509  N   ALA A 248     8569   7413   5044   1594  -2435   -436       N  
ATOM   1510  CA  ALA A 248     -46.350 -12.504 -27.067  1.00 50.68           C  
ANISOU 1510  CA  ALA A 248     8008   6895   4353   1655  -2604   -603       C  
ATOM   1511  C   ALA A 248     -47.656 -11.946 -27.613  1.00 63.67           C  
ANISOU 1511  C   ALA A 248     9603   8480   6109   1732  -2897   -640       C  
ATOM   1512  O   ALA A 248     -48.022 -12.202 -28.759  1.00 54.72           O  
ANISOU 1512  O   ALA A 248     8561   7433   4798   1813  -3098   -685       O  
ATOM   1513  CB  ALA A 248     -46.587 -13.833 -26.373  1.00 49.48           C  
ANISOU 1513  CB  ALA A 248     7734   6707   4359   1601  -2507   -825       C  
ATOM   1514  N   ALA A1001     -48.354 -11.183 -26.778  1.00 71.13           N  
ANISOU 1514  N   ALA A1001     9498  12100   5428  -1143   1265   1409       N  
ATOM   1515  CA  ALA A1001     -49.611 -10.560 -27.170  1.00 62.29           C  
ANISOU 1515  CA  ALA A1001     8217  10809   4642  -1097   1559   1219       C  
ATOM   1516  C   ALA A1001     -49.380  -9.501 -28.238  1.00 52.25           C  
ANISOU 1516  C   ALA A1001     6817   9451   3584  -1044   1364    985       C  
ATOM   1517  O   ALA A1001     -50.096  -9.450 -29.238  1.00 50.71           O  
ANISOU 1517  O   ALA A1001     6361   9087   3819   -966   1365    944       O  
ATOM   1518  CB  ALA A1001     -50.302  -9.950 -25.963  1.00 58.70           C  
ANISOU 1518  CB  ALA A1001     7996  10398   3911  -1147   1974   1103       C  
ATOM   1519  N   ASP A1002     -48.374  -8.660 -28.016  1.00 52.15           N  
ANISOU 1519  N   ASP A1002     6999   9553   3263  -1107   1179    848       N  
ATOM   1520  CA  ASP A1002     -48.054  -7.579 -28.941  1.00 61.87           C  
ANISOU 1520  CA  ASP A1002     8163  10691   4654  -1085   1018    642       C  
ATOM   1521  C   ASP A1002     -47.610  -8.114 -30.296  1.00 57.06           C  
ANISOU 1521  C   ASP A1002     7321  10015   4344  -1023    733    745       C  
ATOM   1522  O   ASP A1002     -47.996  -7.582 -31.336  1.00 54.85           O  
ANISOU 1522  O   ASP A1002     6906   9579   4356   -958    690    647       O  
ATOM   1523  CB  ASP A1002     -46.972  -6.675 -28.353  1.00 61.17           C  
ANISOU 1523  CB  ASP A1002     8336  10739   4168  -1221    867    490       C  
ATOM   1524  CG  ASP A1002     -47.486  -5.818 -27.214  1.00 64.27           C  
ANISOU 1524  CG  ASP A1002     9025  11127   4266  -1291   1176    280       C  
ATOM   1525  OD1 ASP A1002     -48.528  -6.172 -26.626  1.00 72.92           O  
ANISOU 1525  OD1 ASP A1002    10143  12180   5383  -1235   1532    318       O  
ATOM   1526  OD2 ASP A1002     -46.847  -4.789 -26.907  1.00 71.70           O  
ANISOU 1526  OD2 ASP A1002    10191  12092   4961  -1415   1091     66       O  
ATOM   1527  N   LEU A1003     -46.800  -9.169 -30.275  1.00 55.16           N  
ANISOU 1527  N   LEU A1003     7059   9881   4018  -1033    549    952       N  
ATOM   1528  CA  LEU A1003     -46.337  -9.802 -31.502  1.00 47.99           C  
ANISOU 1528  CA  LEU A1003     5976   8893   3363   -968    343   1040       C  
ATOM   1529  C   LEU A1003     -47.501 -10.341 -32.327  1.00 44.25           C  
ANISOU 1529  C   LEU A1003     5334   8218   3262   -903    436   1061       C  
ATOM   1530  O   LEU A1003     -47.524 -10.189 -33.548  1.00 42.12           O  
ANISOU 1530  O   LEU A1003     4968   7828   3206   -867    304    997       O  
ATOM   1531  CB  LEU A1003     -45.355 -10.930 -31.191  1.00 49.70           C  
ANISOU 1531  CB  LEU A1003     6196   9223   3464   -954    194   1277       C  
ATOM   1532  CG  LEU A1003     -43.941 -10.515 -30.786  1.00 50.88           C  
ANISOU 1532  CG  LEU A1003     6402   9580   3352  -1014    -33   1294       C  
ATOM   1533  CD1 LEU A1003     -43.045 -11.738 -30.641  1.00 60.89           C  
ANISOU 1533  CD1 LEU A1003     7591  10899   4645   -932   -185   1564       C  
ATOM   1534  CD2 LEU A1003     -43.361  -9.529 -31.785  1.00 43.50           C  
ANISOU 1534  CD2 LEU A1003     5394   8606   2529  -1042   -153   1110       C  
ATOM   1535  N   GLU A1004     -48.463 -10.968 -31.658  1.00 51.35           N  
ANISOU 1535  N   GLU A1004     6204   9084   4224   -911    657   1157       N  
ATOM   1536  CA  GLU A1004     -49.640 -11.500 -32.336  1.00 56.06           C  
ANISOU 1536  CA  GLU A1004     6596   9499   5206   -894    730   1183       C  
ATOM   1537  C   GLU A1004     -50.427 -10.379 -33.010  1.00 53.04           C  
ANISOU 1537  C   GLU A1004     6084   9017   5051   -851    736   1001       C  
ATOM   1538  O   GLU A1004     -50.958 -10.552 -34.105  1.00 50.68           O  
ANISOU 1538  O   GLU A1004     5623   8584   5051   -835    593    990       O  
ATOM   1539  CB  GLU A1004     -50.533 -12.259 -31.353  1.00 47.54           C  
ANISOU 1539  CB  GLU A1004     5490   8409   4163   -940   1022   1327       C  
ATOM   1540  N   ASP A1005     -50.487  -9.226 -32.351  1.00 56.33           N  
ANISOU 1540  N   ASP A1005     6600   9485   5316   -832    887    861       N  
ATOM   1541  CA  ASP A1005     -51.164  -8.061 -32.905  1.00 58.47           C  
ANISOU 1541  CA  ASP A1005     6771   9630   5815   -753    911    706       C  
ATOM   1542  C   ASP A1005     -50.416  -7.528 -34.121  1.00 58.73           C  
ANISOU 1542  C   ASP A1005     6843   9611   5860   -738    597    645       C  
ATOM   1543  O   ASP A1005     -51.028  -7.155 -35.122  1.00 67.28           O  
ANISOU 1543  O   ASP A1005     7787  10556   7219   -675    476    625       O  
ATOM   1544  CB  ASP A1005     -51.303  -6.964 -31.847  1.00 77.39           C  
ANISOU 1544  CB  ASP A1005     9332  12049   8024   -736   1192    547       C  
ATOM   1545  CG  ASP A1005     -52.568  -7.107 -31.023  1.00 95.85           C  
ANISOU 1545  CG  ASP A1005    11547  14345  10526   -695   1591    564       C  
ATOM   1546  OD1 ASP A1005     -53.442  -7.910 -31.411  1.00108.31           O  
ANISOU 1546  OD1 ASP A1005    12840  15860  12451   -681   1614    699       O  
ATOM   1547  OD2 ASP A1005     -52.688  -6.416 -29.989  1.00100.24           O  
ANISOU 1547  OD2 ASP A1005    12297  14924  10868   -692   1900    432       O  
ATOM   1548  N   ASN A1006     -49.091  -7.491 -34.024  1.00 60.11           N  
ANISOU 1548  N   ASN A1006     7200   9903   5737   -801    465    635       N  
ATOM   1549  CA  ASN A1006     -48.253  -7.070 -35.140  1.00 59.34           C  
ANISOU 1549  CA  ASN A1006     7149   9767   5632   -808    225    597       C  
ATOM   1550  C   ASN A1006     -48.461  -7.977 -36.343  1.00 44.92           C  
ANISOU 1550  C   ASN A1006     5214   7851   4003   -785     56    691       C  
ATOM   1551  O   ASN A1006     -48.567  -7.515 -37.477  1.00 45.34           O  
ANISOU 1551  O   ASN A1006     5269   7794   4164   -762    -94    654       O  
ATOM   1552  CB  ASN A1006     -46.776  -7.062 -34.737  1.00 66.32           C  
ANISOU 1552  CB  ASN A1006     8169  10814   6215   -894    135    603       C  
ATOM   1553  CG  ASN A1006     -46.467  -6.034 -33.665  1.00 74.03           C  
ANISOU 1553  CG  ASN A1006     9309  11870   6949   -972    235    466       C  
ATOM   1554  OD1 ASN A1006     -45.843  -6.344 -32.650  1.00 83.86           O  
ANISOU 1554  OD1 ASN A1006    10648  13291   7925  -1052    234    507       O  
ATOM   1555  ND2 ASN A1006     -46.907  -4.800 -33.884  1.00 76.12           N  
ANISOU 1555  ND2 ASN A1006     9635  11987   7299   -953    308    307       N  
ATOM   1556  N   TRP A1007     -48.528  -9.275 -36.073  1.00 48.85           N  
ANISOU 1556  N   TRP A1007     5658   8378   4525   -804     83    815       N  
ATOM   1557  CA  TRP A1007     -48.743 -10.283 -37.102  1.00 52.79           C  
ANISOU 1557  CA  TRP A1007     6102   8763   5193   -812    -53    876       C  
ATOM   1558  C   TRP A1007     -50.027 -10.038 -37.890  1.00 55.66           C  
ANISOU 1558  C   TRP A1007     6322   8985   5840   -808   -142    840       C  
ATOM   1559  O   TRP A1007     -49.997  -9.907 -39.115  1.00 53.27           O  
ANISOU 1559  O   TRP A1007     6069   8594   5579   -816   -350    804       O  
ATOM   1560  CB  TRP A1007     -48.772 -11.675 -36.469  1.00 51.79           C  
ANISOU 1560  CB  TRP A1007     5951   8642   5085   -839     43   1020       C  
ATOM   1561  CG  TRP A1007     -49.214 -12.760 -37.399  1.00 59.30           C  
ANISOU 1561  CG  TRP A1007     6865   9424   6244   -880    -59   1053       C  
ATOM   1562  CD1 TRP A1007     -50.434 -13.371 -37.422  1.00 61.48           C  
ANISOU 1562  CD1 TRP A1007     6991   9584   6782   -952    -29   1092       C  
ATOM   1563  CD2 TRP A1007     -48.439 -13.373 -38.437  1.00 62.47           C  
ANISOU 1563  CD2 TRP A1007     7392   9733   6610   -875   -190   1033       C  
ATOM   1564  NE1 TRP A1007     -50.467 -14.324 -38.411  1.00 65.89           N  
ANISOU 1564  NE1 TRP A1007     7603   9979   7451  -1018   -175   1082       N  
ATOM   1565  CE2 TRP A1007     -49.255 -14.344 -39.049  1.00 65.08           C  
ANISOU 1565  CE2 TRP A1007     7695   9880   7152   -959   -253   1036       C  
ATOM   1566  CE3 TRP A1007     -47.136 -13.191 -38.910  1.00 61.33           C  
ANISOU 1566  CE3 TRP A1007     7377   9635   6291   -818   -232   1004       C  
ATOM   1567  CZ2 TRP A1007     -48.810 -15.133 -40.107  1.00 69.92           C  
ANISOU 1567  CZ2 TRP A1007     8469  10338   7759   -983   -349    983       C  
ATOM   1568  CZ3 TRP A1007     -46.696 -13.976 -39.959  1.00 64.43           C  
ANISOU 1568  CZ3 TRP A1007     7891   9884   6706   -815   -283    972       C  
ATOM   1569  CH2 TRP A1007     -47.531 -14.934 -40.546  1.00 69.36           C  
ANISOU 1569  CH2 TRP A1007     8550  10309   7497   -894   -337    948       C  
ATOM   1570  N   GLU A1008     -51.154  -9.969 -37.187  1.00 56.87           N  
ANISOU 1570  N   GLU A1008     6296   9124   6188   -799     16    864       N  
ATOM   1571  CA  GLU A1008     -52.438  -9.805 -37.856  1.00 63.42           C  
ANISOU 1571  CA  GLU A1008     6899   9835   7363   -792    -90    866       C  
ATOM   1572  C   GLU A1008     -52.591  -8.408 -38.454  1.00 53.29           C  
ANISOU 1572  C   GLU A1008     5622   8500   6127   -693   -205    791       C  
ATOM   1573  O   GLU A1008     -53.446  -8.189 -39.304  1.00 55.94           O  
ANISOU 1573  O   GLU A1008     5799   8738   6718   -671   -409    819       O  
ATOM   1574  CB  GLU A1008     -53.592 -10.103 -36.893  1.00 72.59           C  
ANISOU 1574  CB  GLU A1008     7808  10996   8778   -800    171    929       C  
ATOM   1575  CG  GLU A1008     -53.721  -9.145 -35.725  1.00 82.61           C  
ANISOU 1575  CG  GLU A1008     9093  12329   9965   -708    495    869       C  
ATOM   1576  CD  GLU A1008     -54.942  -9.441 -34.874  1.00 96.35           C  
ANISOU 1576  CD  GLU A1008    10572  14053  11984   -711    815    933       C  
ATOM   1577  OE1 GLU A1008     -55.785 -10.255 -35.308  1.00100.55           O  
ANISOU 1577  OE1 GLU A1008    10841  14515  12848   -790    734   1029       O  
ATOM   1578  OE2 GLU A1008     -55.060  -8.862 -33.774  1.00103.82           O  
ANISOU 1578  OE2 GLU A1008    11584  15049  12815   -654   1163    878       O  
ATOM   1579  N   THR A1009     -51.759  -7.468 -38.019  1.00 50.62           N  
ANISOU 1579  N   THR A1009     5470   8213   5551   -646   -101    710       N  
ATOM   1580  CA  THR A1009     -51.747  -6.139 -38.622  1.00 42.27           C  
ANISOU 1580  CA  THR A1009     4479   7060   4523   -563   -198    651       C  
ATOM   1581  C   THR A1009     -51.164  -6.217 -40.031  1.00 61.97           C  
ANISOU 1581  C   THR A1009     7126   9508   6912   -607   -501    677       C  
ATOM   1582  O   THR A1009     -51.679  -5.600 -40.965  1.00 56.11           O  
ANISOU 1582  O   THR A1009     6368   8652   6301   -553   -702    711       O  
ATOM   1583  CB  THR A1009     -50.941  -5.135 -37.777  1.00 50.54           C  
ANISOU 1583  CB  THR A1009     5723   8146   5335   -552     -4    535       C  
ATOM   1584  OG1 THR A1009     -51.707  -4.762 -36.627  1.00 53.75           O  
ANISOU 1584  OG1 THR A1009     6036   8540   5846   -487    297    480       O  
ATOM   1585  CG2 THR A1009     -50.624  -3.881 -38.581  1.00 42.02           C  
ANISOU 1585  CG2 THR A1009     4784   6934   4247   -507   -129    490       C  
ATOM   1586  N   LEU A1010     -50.090  -6.987 -40.175  1.00 59.40           N  
ANISOU 1586  N   LEU A1010     6958   9267   6346   -695   -519    675       N  
ATOM   1587  CA  LEU A1010     -49.476  -7.223 -41.478  1.00 51.60           C  
ANISOU 1587  CA  LEU A1010     6148   8233   5225   -744   -723    683       C  
ATOM   1588  C   LEU A1010     -50.452  -7.886 -42.442  1.00 50.43           C  
ANISOU 1588  C   LEU A1010     5932   7989   5239   -780   -963    728       C  
ATOM   1589  O   LEU A1010     -50.653  -7.415 -43.559  1.00 64.45           O  
ANISOU 1589  O   LEU A1010     7819   9681   6986   -783  -1193    745       O  
ATOM   1590  CB  LEU A1010     -48.228  -8.096 -41.330  1.00 56.42           C  
ANISOU 1590  CB  LEU A1010     6876   8936   5626   -798   -633    679       C  
ATOM   1591  CG  LEU A1010     -46.864  -7.409 -41.269  1.00 63.92           C  
ANISOU 1591  CG  LEU A1010     7965   9961   6362   -815   -553    644       C  
ATOM   1592  CD1 LEU A1010     -46.914  -6.185 -40.385  1.00 75.57           C  
ANISOU 1592  CD1 LEU A1010     9417  11467   7830   -802   -455    591       C  
ATOM   1593  CD2 LEU A1010     -45.810  -8.383 -40.768  1.00 65.16           C  
ANISOU 1593  CD2 LEU A1010     8110  10233   6415   -830   -451    683       C  
ATOM   1594  N   ASN A1011     -51.058  -8.980 -41.999  1.00 43.70           N  
ANISOU 1594  N   ASN A1011     4917   7144   4546   -831   -926    756       N  
ATOM   1595  CA  ASN A1011     -51.925  -9.775 -42.857  1.00 46.21           C  
ANISOU 1595  CA  ASN A1011     5170   7367   5020   -927  -1174    777       C  
ATOM   1596  C   ASN A1011     -53.214  -9.056 -43.243  1.00 52.10           C  
ANISOU 1596  C   ASN A1011     5685   8060   6052   -889  -1393    835       C  
ATOM   1597  O   ASN A1011     -53.662  -9.157 -44.383  1.00 62.13           O  
ANISOU 1597  O   ASN A1011     7009   9262   7336   -960  -1732    854       O  
ATOM   1598  CB  ASN A1011     -52.253 -11.105 -42.180  1.00 51.60           C  
ANISOU 1598  CB  ASN A1011     5721   8040   5843  -1016  -1046    803       C  
ATOM   1599  CG  ASN A1011     -51.011 -11.907 -41.849  1.00 58.97           C  
ANISOU 1599  CG  ASN A1011     6862   9000   6543  -1020   -864    789       C  
ATOM   1600  OD1 ASN A1011     -50.429 -12.559 -42.716  1.00 65.69           O  
ANISOU 1600  OD1 ASN A1011     7934   9770   7255  -1073   -951    738       O  
ATOM   1601  ND2 ASN A1011     -50.596 -11.860 -40.588  1.00 63.25           N  
ANISOU 1601  ND2 ASN A1011     7345   9651   7036   -957   -607    839       N  
ATOM   1602  N   ASP A1012     -53.807  -8.334 -42.297  1.00 49.98           N  
ANISOU 1602  N   ASP A1012     5167   7816   6009   -771  -1201    867       N  
ATOM   1603  CA  ASP A1012     -55.036  -7.595 -42.568  1.00 62.82           C  
ANISOU 1603  CA  ASP A1012     6505   9377   7989   -680  -1365    946       C  
ATOM   1604  C   ASP A1012     -54.811  -6.534 -43.637  1.00 68.11           C  
ANISOU 1604  C   ASP A1012     7371   9973   8535   -601  -1635    981       C  
ATOM   1605  O   ASP A1012     -55.597  -6.412 -44.577  1.00 78.01           O  
ANISOU 1605  O   ASP A1012     8525  11169   9947   -609  -2005   1077       O  
ATOM   1606  CB  ASP A1012     -55.573  -6.946 -41.291  1.00 62.32           C  
ANISOU 1606  CB  ASP A1012     6187   9324   8168   -534  -1002    947       C  
ATOM   1607  CG  ASP A1012     -56.171  -7.956 -40.333  1.00 69.54           C  
ANISOU 1607  CG  ASP A1012     6847  10292   9281   -617   -756    968       C  
ATOM   1608  OD1 ASP A1012     -56.540  -9.059 -40.786  1.00 78.59           O  
ANISOU 1608  OD1 ASP A1012     7901  11428  10531   -779   -941   1009       O  
ATOM   1609  OD2 ASP A1012     -56.260  -7.654 -39.125  1.00 74.68           O  
ANISOU 1609  OD2 ASP A1012     7431  10982   9964   -538   -362    938       O  
ATOM   1610  N   ASN A1013     -53.730  -5.776 -43.491  1.00 61.10           N  
ANISOU 1610  N   ASN A1013     6768   9086   7361   -545  -1468    921       N  
ATOM   1611  CA  ASN A1013     -53.409  -4.713 -44.432  1.00 61.39           C  
ANISOU 1611  CA  ASN A1013     7037   9029   7260   -482  -1658    972       C  
ATOM   1612  C   ASN A1013     -53.049  -5.247 -45.814  1.00 64.82           C  
ANISOU 1612  C   ASN A1013     7754   9456   7418   -619  -1980    998       C  
ATOM   1613  O   ASN A1013     -53.226  -4.553 -46.818  1.00 63.90           O  
ANISOU 1613  O   ASN A1013     7790   9254   7234   -586  -2254   1100       O  
ATOM   1614  CB  ASN A1013     -52.271  -3.851 -43.889  1.00 62.01           C  
ANISOU 1614  CB  ASN A1013     7347   9103   7113   -446  -1372    888       C  
ATOM   1615  CG  ASN A1013     -52.738  -2.883 -42.822  1.00 78.16           C  
ANISOU 1615  CG  ASN A1013     9223  11078   9397   -293  -1114    855       C  
ATOM   1616  OD1 ASN A1013     -53.259  -1.811 -43.129  1.00 93.39           O  
ANISOU 1616  OD1 ASN A1013    11123  12846  11513   -149  -1186    926       O  
ATOM   1617  ND2 ASN A1013     -52.557  -3.257 -41.561  1.00 83.19           N  
ANISOU 1617  ND2 ASN A1013     9775  11816  10016   -318   -801    751       N  
ATOM   1618  N   LEU A1014     -52.547  -6.478 -45.866  1.00 58.42           N  
ANISOU 1618  N   LEU A1014     7048   8714   6433   -765  -1932    912       N  
ATOM   1619  CA  LEU A1014     -52.299  -7.134 -47.144  1.00 60.67           C  
ANISOU 1619  CA  LEU A1014     7630   8970   6452   -908  -2193    894       C  
ATOM   1620  C   LEU A1014     -53.605  -7.303 -47.918  1.00 62.58           C  
ANISOU 1620  C   LEU A1014     7728   9164   6886   -967  -2639    984       C  
ATOM   1621  O   LEU A1014     -53.667  -7.022 -49.116  1.00 63.86           O  
ANISOU 1621  O   LEU A1014     8155   9279   6832  -1020  -2967   1041       O  
ATOM   1622  CB  LEU A1014     -51.622  -8.490 -46.940  1.00 55.47           C  
ANISOU 1622  CB  LEU A1014     7078   8344   5652  -1027  -2014    774       C  
ATOM   1623  CG  LEU A1014     -50.118  -8.469 -46.659  1.00 52.25           C  
ANISOU 1623  CG  LEU A1014     6888   7986   4979   -999  -1684    706       C  
ATOM   1624  CD1 LEU A1014     -49.581  -9.884 -46.518  1.00 54.98           C  
ANISOU 1624  CD1 LEU A1014     7304   8326   5259  -1075  -1535    623       C  
ATOM   1625  CD2 LEU A1014     -49.381  -7.725 -47.759  1.00 54.16           C  
ANISOU 1625  CD2 LEU A1014     7484   8188   4908  -1010  -1741    716       C  
ATOM   1626  N   LYS A1015     -54.648  -7.754 -47.228  1.00 51.67           N  
ANISOU 1626  N   LYS A1015     5923   7802   5907   -972  -2658   1012       N  
ATOM   1627  CA  LYS A1015     -55.961  -7.895 -47.844  1.00 55.60           C  
ANISOU 1627  CA  LYS A1015     6167   8273   6686  -1038  -3102   1117       C  
ATOM   1628  C   LYS A1015     -56.542  -6.527 -48.179  1.00 77.24           C  
ANISOU 1628  C   LYS A1015     8779  10969   9600   -844  -3319   1295       C  
ATOM   1629  O   LYS A1015     -57.291  -6.383 -49.145  1.00 76.47           O  
ANISOU 1629  O   LYS A1015     8647  10848   9562   -888  -3810   1423       O  
ATOM   1630  CB  LYS A1015     -56.916  -8.664 -46.927  1.00 59.47           C  
ANISOU 1630  CB  LYS A1015     6174   8791   7632  -1093  -2996   1120       C  
ATOM   1631  N   VAL A1016     -56.194  -5.526 -47.378  1.00 56.16           N  
ANISOU 1631  N   VAL A1016     6056   8271   7012   -633  -2970   1308       N  
ATOM   1632  CA  VAL A1016     -56.651  -4.165 -47.627  1.00 71.63           C  
ANISOU 1632  CA  VAL A1016     7933  10126   9157   -415  -3103   1475       C  
ATOM   1633  C   VAL A1016     -56.053  -3.656 -48.935  1.00 76.36           C  
ANISOU 1633  C   VAL A1016     9015  10666   9332   -456  -3405   1559       C  
ATOM   1634  O   VAL A1016     -56.748  -3.051 -49.751  1.00 81.66           O  
ANISOU 1634  O   VAL A1016     9655  11268  10105   -379  -3819   1761       O  
ATOM   1635  CB  VAL A1016     -56.280  -3.218 -46.467  1.00 56.65           C  
ANISOU 1635  CB  VAL A1016     5972   8168   7384   -213  -2614   1418       C  
ATOM   1636  CG1 VAL A1016     -56.567  -1.769 -46.840  1.00 59.15           C  
ANISOU 1636  CG1 VAL A1016     6314   8309   7850     14  -2724   1581       C  
ATOM   1637  CG2 VAL A1016     -57.037  -3.606 -45.209  1.00 56.99           C  
ANISOU 1637  CG2 VAL A1016     5556   8259   7840   -155  -2308   1365       C  
ATOM   1638  N   ILE A1017     -54.765  -3.924 -49.132  1.00 68.40           N  
ANISOU 1638  N   ILE A1017     8445   9688   7857   -576  -3191   1423       N  
ATOM   1639  CA  ILE A1017     -54.074  -3.559 -50.364  1.00 61.99           C  
ANISOU 1639  CA  ILE A1017     8141   8827   6586   -650  -3379   1484       C  
ATOM   1640  C   ILE A1017     -54.629  -4.331 -51.557  1.00 67.52           C  
ANISOU 1640  C   ILE A1017     9000   9559   7095   -832  -3881   1527       C  
ATOM   1641  O   ILE A1017     -54.934  -3.749 -52.600  1.00 64.12           O  
ANISOU 1641  O   ILE A1017     8773   9052   6537   -799  -4162   1661       O  
ATOM   1642  CB  ILE A1017     -52.563  -3.826 -50.261  1.00 68.79           C  
ANISOU 1642  CB  ILE A1017     9364   9726   7046   -749  -2979   1316       C  
ATOM   1643  CG1 ILE A1017     -51.932  -2.925 -49.200  1.00 75.21           C  
ANISOU 1643  CG1 ILE A1017    10084  10506   7985   -617  -2561   1278       C  
ATOM   1644  CG2 ILE A1017     -51.886  -3.600 -51.603  1.00 55.16           C  
ANISOU 1644  CG2 ILE A1017     8173   7952   4832   -853  -3122   1372       C  
ATOM   1645  CD1 ILE A1017     -50.581  -3.400 -48.728  1.00 47.94           C  
ANISOU 1645  CD1 ILE A1017     6786   7142   4288   -716  -2173   1109       C  
ATOM   1646  N   GLU A1018     -54.760  -5.644 -51.388  1.00 69.08           N  
ANISOU 1646  N   GLU A1018     9111   9832   7302  -1008  -3877   1366       N  
ATOM   1647  CA  GLU A1018     -55.227  -6.523 -52.456  1.00 69.04           C  
ANISOU 1647  CA  GLU A1018     9276   9802   7152  -1183  -4152   1280       C  
ATOM   1648  C   GLU A1018     -56.643  -6.187 -52.919  1.00 70.78           C  
ANISOU 1648  C   GLU A1018     9184  10003   7708  -1137  -4595   1445       C  
ATOM   1649  O   GLU A1018     -56.980  -6.380 -54.087  1.00 74.30           O  
ANISOU 1649  O   GLU A1018     9869  10416   7947  -1238  -4871   1441       O  
ATOM   1650  CB  GLU A1018     -55.168  -7.983 -52.001  1.00 61.58           C  
ANISOU 1650  CB  GLU A1018     8258   8897   6243  -1380  -4047   1087       C  
ATOM   1651  N   LYS A1019     -57.467  -5.688 -52.003  1.00 68.04           N  
ANISOU 1651  N   LYS A1019     8285   9680   7889   -980  -4649   1596       N  
ATOM   1652  CA  LYS A1019     -58.861  -5.385 -52.315  1.00 86.95           C  
ANISOU 1652  CA  LYS A1019    10273  12059  10705   -905  -5024   1766       C  
ATOM   1653  C   LYS A1019     -59.111  -3.883 -52.419  1.00 91.22           C  
ANISOU 1653  C   LYS A1019    10732  12512  11414   -614  -5122   2022       C  
ATOM   1654  O   LYS A1019     -60.230  -3.416 -52.207  1.00 91.97           O  
ANISOU 1654  O   LYS A1019    10334  12584  12027   -449  -5308   2199       O  
ATOM   1655  CB  LYS A1019     -59.787  -5.993 -51.257  1.00 73.39           C  
ANISOU 1655  CB  LYS A1019     7907  10403   9576   -924  -4974   1761       C  
ATOM   1656  N   ALA A1020     -58.067  -3.132 -52.754  1.00 96.26           N  
ANISOU 1656  N   ALA A1020    11850  13081  11644   -549  -4972   2049       N  
ATOM   1657  CA  ALA A1020     -58.165  -1.677 -52.821  1.00105.58           C  
ANISOU 1657  CA  ALA A1020    13028  14125  12965   -278  -5031   2302       C  
ATOM   1658  C   ALA A1020     -58.339  -1.171 -54.250  1.00119.61           C  
ANISOU 1658  C   ALA A1020    15168  15836  14443   -283  -5347   2444       C  
ATOM   1659  O   ALA A1020     -57.506  -1.430 -55.117  1.00129.74           O  
ANISOU 1659  O   ALA A1020    16995  17130  15169   -454  -5284   2339       O  
ATOM   1660  CB  ALA A1020     -56.936  -1.041 -52.189  1.00 96.45           C  
ANISOU 1660  CB  ALA A1020    12149  12901  11595   -212  -4656   2281       C  
ATOM   1661  N   ASP A1021     -59.426  -0.443 -54.486  1.00130.51           N  
ANISOU 1661  N   ASP A1021    16225  17146  16215    -81  -5662   2694       N  
ATOM   1662  CA  ASP A1021     -59.669   0.175 -55.785  1.00132.03           C  
ANISOU 1662  CA  ASP A1021    16728  17279  16157    -54  -5998   2889       C  
ATOM   1663  C   ASP A1021     -58.993   1.541 -55.863  1.00118.11           C  
ANISOU 1663  C   ASP A1021    15282  15319  14275    158  -5843   3090       C  
ATOM   1664  O   ASP A1021     -58.637   2.011 -56.943  1.00108.19           O  
ANISOU 1664  O   ASP A1021    14496  14008  12603    118  -5960   3204       O  
ATOM   1665  CB  ASP A1021     -61.171   0.310 -56.048  1.00 95.76           C  
ANISOU 1665  CB  ASP A1021    11631  12707  12048     65  -6435   3089       C  
ATOM   1666  N   ASN A1022     -58.810   2.166 -54.704  1.00111.27           N  
ANISOU 1666  N   ASN A1022    14171  14327  13780    371  -5564   3136       N  
ATOM   1667  CA  ASN A1022     -58.224   3.501 -54.619  1.00121.17           C  
ANISOU 1667  CA  ASN A1022    15698  15326  15017    580  -5398   3334       C  
ATOM   1668  C   ASN A1022     -56.713   3.465 -54.374  1.00116.93           C  
ANISOU 1668  C   ASN A1022    15661  14770  13996    401  -4995   3164       C  
ATOM   1669  O   ASN A1022     -56.170   2.452 -53.935  1.00122.93           O  
ANISOU 1669  O   ASN A1022    16430  15714  14566    188  -4795   2894       O  
ATOM   1670  CB  ASN A1022     -58.921   4.297 -53.511  1.00128.75           C  
ANISOU 1670  CB  ASN A1022    16120  16086  16712    942  -5304   3491       C  
ATOM   1671  CG  ASN A1022     -58.476   5.744 -53.458  1.00137.10           C  
ANISOU 1671  CG  ASN A1022    17460  16786  17845   1189  -5153   3720       C  
ATOM   1672  OD1 ASN A1022     -57.940   6.277 -54.429  1.00146.13           O  
ANISOU 1672  OD1 ASN A1022    19134  17842  18546   1117  -5219   3841       O  
ATOM   1673  ND2 ASN A1022     -58.689   6.386 -52.315  1.00139.38           N  
ANISOU 1673  ND2 ASN A1022    17417  16877  18663   1446  -4709   3633       N  
ATOM   1674  N   ALA A1023     -56.039   4.576 -54.663  1.00111.05           N  
ANISOU 1674  N   ALA A1023    15327  13794  13072    482  -4861   3332       N  
ATOM   1675  CA  ALA A1023     -54.600   4.683 -54.450  1.00100.65           C  
ANISOU 1675  CA  ALA A1023    14467  12439  11336    301  -4440   3186       C  
ATOM   1676  C   ALA A1023     -54.252   5.052 -53.011  1.00 94.69           C  
ANISOU 1676  C   ALA A1023    13423  11597  10958    403  -3856   2934       C  
ATOM   1677  O   ALA A1023     -53.336   4.480 -52.425  1.00 87.74           O  
ANISOU 1677  O   ALA A1023    12599  10860   9880    214  -3460   2634       O  
ATOM   1678  CB  ALA A1023     -54.001   5.705 -55.405  1.00104.33           C  
ANISOU 1678  CB  ALA A1023    15468  12699  11474    295  -4390   3391       C  
ATOM   1679  N   ALA A1024     -54.983   6.011 -52.447  1.00100.76           N  
ANISOU 1679  N   ALA A1024    13899  12121  12262    706  -3807   3058       N  
ATOM   1680  CA  ALA A1024     -54.678   6.529 -51.115  1.00 97.98           C  
ANISOU 1680  CA  ALA A1024    13371  11635  12222    801  -3248   2815       C  
ATOM   1681  C   ALA A1024     -54.729   5.452 -50.035  1.00 97.25           C  
ANISOU 1681  C   ALA A1024    12902  11812  12236    706  -2994   2484       C  
ATOM   1682  O   ALA A1024     -53.974   5.503 -49.065  1.00 94.53           O  
ANISOU 1682  O   ALA A1024    12595  11480  11844    619  -2529   2213       O  
ATOM   1683  CB  ALA A1024     -55.630   7.664 -50.764  1.00104.00           C  
ANISOU 1683  CB  ALA A1024    13875  12062  13577   1178  -3247   3005       C  
ATOM   1684  N   GLN A1025     -55.617   4.477 -50.205  1.00103.44           N  
ANISOU 1684  N   GLN A1025    13337  12808  13157    701  -3318   2522       N  
ATOM   1685  CA  GLN A1025     -55.793   3.429 -49.205  1.00105.74           C  
ANISOU 1685  CA  GLN A1025    13263  13326  13586    616  -3088   2258       C  
ATOM   1686  C   GLN A1025     -54.753   2.324 -49.359  1.00102.43           C  
ANISOU 1686  C   GLN A1025    13115  13152  12651    295  -3000   2051       C  
ATOM   1687  O   GLN A1025     -54.658   1.429 -48.520  1.00109.94           O  
ANISOU 1687  O   GLN A1025    13855  14278  13640    200  -2770   1836       O  
ATOM   1688  CB  GLN A1025     -57.206   2.846 -49.284  1.00106.80           C  
ANISOU 1688  CB  GLN A1025    12869  13557  14153    722  -3445   2390       C  
ATOM   1689  CG  GLN A1025     -57.568   2.249 -50.629  1.00104.52           C  
ANISOU 1689  CG  GLN A1025    12696  13390  13629    579  -4075   2587       C  
ATOM   1690  CD  GLN A1025     -59.068   2.129 -50.819  1.00103.73           C  
ANISOU 1690  CD  GLN A1025    12037  13308  14067    734  -4518   2811       C  
ATOM   1691  OE1 GLN A1025     -59.843   2.863 -50.205  1.00101.13           O  
ANISOU 1691  OE1 GLN A1025    11289  12820  14315   1038  -4384   2916       O  
ATOM   1692  NE2 GLN A1025     -59.485   1.207 -51.679  1.00102.50           N  
ANISOU 1692  NE2 GLN A1025    11868  13335  13744    521  -5045   2880       N  
ATOM   1693  N   VAL A1026     -53.974   2.390 -50.432  1.00 98.90           N  
ANISOU 1693  N   VAL A1026    13146  12699  11731    142  -3155   2131       N  
ATOM   1694  CA  VAL A1026     -52.852   1.478 -50.611  1.00 87.77           C  
ANISOU 1694  CA  VAL A1026    12021  11473   9854   -125  -2988   1938       C  
ATOM   1695  C   VAL A1026     -51.633   2.022 -49.875  1.00 75.10           C  
ANISOU 1695  C   VAL A1026    10580   9818   8137   -179  -2492   1773       C  
ATOM   1696  O   VAL A1026     -50.910   1.276 -49.210  1.00 66.11           O  
ANISOU 1696  O   VAL A1026     9391   8845   6884   -310  -2215   1554       O  
ATOM   1697  CB  VAL A1026     -52.522   1.270 -52.105  1.00 61.95           C  
ANISOU 1697  CB  VAL A1026     9217   8221   6100   -279  -3310   2077       C  
ATOM   1698  CG1 VAL A1026     -51.251   0.450 -52.272  1.00 58.92           C  
ANISOU 1698  CG1 VAL A1026     9136   7980   5271   -516  -3026   1868       C  
ATOM   1699  CG2 VAL A1026     -53.689   0.601 -52.810  1.00 65.15           C  
ANISOU 1699  CG2 VAL A1026     9475   8711   6569   -292  -3860   2203       C  
ATOM   1700  N   LYS A1027     -51.429   3.332 -49.983  1.00 71.72           N  
ANISOU 1700  N   LYS A1027    10338   9146   7768    -82  -2407   1894       N  
ATOM   1701  CA  LYS A1027     -50.281   3.999 -49.376  1.00 68.90           C  
ANISOU 1701  CA  LYS A1027    10157   8704   7318   -175  -1986   1751       C  
ATOM   1702  C   LYS A1027     -50.243   3.846 -47.856  1.00 78.21           C  
ANISOU 1702  C   LYS A1027    11026   9956   8735   -150  -1657   1496       C  
ATOM   1703  O   LYS A1027     -49.217   3.463 -47.296  1.00 78.35           O  
ANISOU 1703  O   LYS A1027    11088  10119   8563   -327  -1397   1306       O  
ATOM   1704  CB  LYS A1027     -50.275   5.484 -49.743  1.00 63.90           C  
ANISOU 1704  CB  LYS A1027     9770   7731   6780    -67  -1975   1941       C  
ATOM   1705  N   ASP A1028     -51.354   4.143 -47.188  1.00 85.91           N  
ANISOU 1705  N   ASP A1028    11687  10833  10122     72  -1661   1505       N  
ATOM   1706  CA  ASP A1028     -51.381   4.079 -45.729  1.00 91.54           C  
ANISOU 1706  CA  ASP A1028    12171  11594  11015     97  -1313   1265       C  
ATOM   1707  C   ASP A1028     -51.483   2.642 -45.215  1.00 95.32           C  
ANISOU 1707  C   ASP A1028    12400  12385  11433      1  -1299   1141       C  
ATOM   1708  O   ASP A1028     -51.085   2.354 -44.088  1.00107.56           O  
ANISOU 1708  O   ASP A1028    13874  14048  12946    -69  -1010    942       O  
ATOM   1709  CB  ASP A1028     -52.524   4.934 -45.166  1.00 98.42           C  
ANISOU 1709  CB  ASP A1028    12812  12221  12362    385  -1227   1305       C  
ATOM   1710  CG  ASP A1028     -53.888   4.523 -45.688  1.00103.85           C  
ANISOU 1710  CG  ASP A1028    13150  12932  13376    579  -1562   1515       C  
ATOM   1711  OD1 ASP A1028     -54.005   3.453 -46.321  1.00105.16           O  
ANISOU 1711  OD1 ASP A1028    13249  13326  13383    455  -1854   1580       O  
ATOM   1712  OD2 ASP A1028     -54.854   5.282 -45.458  1.00110.93           O  
ANISOU 1712  OD2 ASP A1028    13828  13603  14717    854  -1531   1613       O  
ATOM   1713  N   ALA A1029     -52.011   1.745 -46.042  1.00 88.04           N  
ANISOU 1713  N   ALA A1029    11384  11585  10484    -18  -1624   1265       N  
ATOM   1714  CA  ALA A1029     -52.038   0.327 -45.697  1.00 68.87           C  
ANISOU 1714  CA  ALA A1029     8776   9406   7986   -138  -1618   1161       C  
ATOM   1715  C   ALA A1029     -50.620  -0.227 -45.691  1.00 64.62           C  
ANISOU 1715  C   ALA A1029     8490   9014   7051   -347  -1458   1035       C  
ATOM   1716  O   ALA A1029     -50.306  -1.154 -44.947  1.00 63.67           O  
ANISOU 1716  O   ALA A1029     8250   9064   6878   -427  -1300    912       O  
ATOM   1717  CB  ALA A1029     -52.908  -0.449 -46.664  1.00 62.33           C  
ANISOU 1717  CB  ALA A1029     7834   8633   7215   -151  -2028   1303       C  
ATOM   1718  N   LEU A1030     -49.768   0.351 -46.530  1.00 65.07           N  
ANISOU 1718  N   LEU A1030     8882   8991   6851   -425  -1486   1092       N  
ATOM   1719  CA  LEU A1030     -48.362  -0.021 -46.577  1.00 54.53           C  
ANISOU 1719  CA  LEU A1030     7744   7775   5201   -607  -1297    994       C  
ATOM   1720  C   LEU A1030     -47.601   0.553 -45.385  1.00 57.69           C  
ANISOU 1720  C   LEU A1030     8100   8188   5632   -654   -988    848       C  
ATOM   1721  O   LEU A1030     -46.740  -0.112 -44.813  1.00 55.44           O  
ANISOU 1721  O   LEU A1030     7763   8082   5219   -767   -834    739       O  
ATOM   1722  CB  LEU A1030     -47.727   0.451 -47.887  1.00 53.42           C  
ANISOU 1722  CB  LEU A1030     7972   7538   4788   -691  -1381   1115       C  
ATOM   1723  CG  LEU A1030     -47.909  -0.460 -49.102  1.00 61.86           C  
ANISOU 1723  CG  LEU A1030     9214   8669   5621   -750  -1623   1188       C  
ATOM   1724  CD1 LEU A1030     -47.236   0.137 -50.327  1.00 64.88           C  
ANISOU 1724  CD1 LEU A1030    10022   8946   5683   -840  -1636   1313       C  
ATOM   1725  CD2 LEU A1030     -47.342  -1.838 -48.808  1.00 66.33           C  
ANISOU 1725  CD2 LEU A1030     9696   9429   6076   -847  -1487   1036       C  
ATOM   1726  N   THR A1031     -47.922   1.789 -45.012  1.00 60.28           N  
ANISOU 1726  N   THR A1031     8459   8311   6132   -569   -913    849       N  
ATOM   1727  CA  THR A1031     -47.241   2.445 -43.901  1.00 61.11           C  
ANISOU 1727  CA  THR A1031     8586   8396   6238   -652   -646    680       C  
ATOM   1728  C   THR A1031     -47.667   1.833 -42.574  1.00 68.50           C  
ANISOU 1728  C   THR A1031     9277   9483   7266   -610   -512    536       C  
ATOM   1729  O   THR A1031     -46.915   1.859 -41.600  1.00 81.02           O  
ANISOU 1729  O   THR A1031    10878  11174   8730   -737   -339    385       O  
ATOM   1730  CB  THR A1031     -47.510   3.962 -43.871  1.00 57.56           C  
ANISOU 1730  CB  THR A1031     8294   7621   5957   -574   -572    695       C  
ATOM   1731  OG1 THR A1031     -48.908   4.202 -43.679  1.00 64.77           O  
ANISOU 1731  OG1 THR A1031     9029   8392   7189   -320   -626    751       O  
ATOM   1732  CG2 THR A1031     -47.061   4.609 -45.170  1.00 65.00           C  
ANISOU 1732  CG2 THR A1031     9521   8393   6783   -629   -685    876       C  
ATOM   1733  N   LYS A1032     -48.877   1.285 -42.537  1.00 60.77           N  
ANISOU 1733  N   LYS A1032     8075   8519   6494   -451   -602    597       N  
ATOM   1734  CA  LYS A1032     -49.334   0.557 -41.363  1.00 55.40           C  
ANISOU 1734  CA  LYS A1032     7171   7990   5889   -424   -448    497       C  
ATOM   1735  C   LYS A1032     -48.526  -0.725 -41.212  1.00 56.66           C  
ANISOU 1735  C   LYS A1032     7306   8410   5813   -573   -464    479       C  
ATOM   1736  O   LYS A1032     -48.169  -1.119 -40.101  1.00 64.45           O  
ANISOU 1736  O   LYS A1032     8246   9543   6701   -637   -299    381       O  
ATOM   1737  CB  LYS A1032     -50.827   0.244 -41.456  1.00 55.67           C  
ANISOU 1737  CB  LYS A1032     6923   7971   6256   -241   -531    593       C  
ATOM   1738  CG  LYS A1032     -51.728   1.414 -41.103  1.00 57.14           C  
ANISOU 1738  CG  LYS A1032     7036   7911   6763    -36   -397    585       C  
ATOM   1739  CD  LYS A1032     -53.188   1.018 -41.201  1.00 59.35           C  
ANISOU 1739  CD  LYS A1032     6941   8170   7438    143   -484    706       C  
ATOM   1740  CE  LYS A1032     -54.108   2.182 -40.891  1.00 62.63           C  
ANISOU 1740  CE  LYS A1032     7235   8316   8245    398   -320    720       C  
ATOM   1741  NZ  LYS A1032     -55.532   1.770 -41.013  1.00 67.28           N  
ANISOU 1741  NZ  LYS A1032     7370   8904   9289    573   -416    866       N  
ATOM   1742  N   MET A1033     -48.233  -1.369 -42.337  1.00 45.41           N  
ANISOU 1742  N   MET A1033     5940   7025   4287   -621   -658    579       N  
ATOM   1743  CA  MET A1033     -47.393  -2.558 -42.334  1.00 41.31           C  
ANISOU 1743  CA  MET A1033     5419   6697   3580   -731   -647    569       C  
ATOM   1744  C   MET A1033     -45.970  -2.220 -41.909  1.00 42.75           C  
ANISOU 1744  C   MET A1033     5707   6969   3565   -861   -508    498       C  
ATOM   1745  O   MET A1033     -45.345  -2.967 -41.158  1.00 50.71           O  
ANISOU 1745  O   MET A1033     6629   8154   4485   -918   -430    468       O  
ATOM   1746  CB  MET A1033     -47.382  -3.214 -43.713  1.00 51.82           C  
ANISOU 1746  CB  MET A1033     6856   8005   4827   -755   -843    658       C  
ATOM   1747  CG  MET A1033     -48.700  -3.855 -44.103  1.00 65.08           C  
ANISOU 1747  CG  MET A1033     8395   9643   6689   -688  -1044    722       C  
ATOM   1748  SD  MET A1033     -48.587  -4.746 -45.663  1.00 65.54           S  
ANISOU 1748  SD  MET A1033     8669   9680   6555   -775  -1284    771       S  
ATOM   1749  CE  MET A1033     -47.184  -5.807 -45.326  1.00 38.96           C  
ANISOU 1749  CE  MET A1033     5365   6447   2990   -859  -1041    686       C  
ATOM   1750  N   ARG A1034     -45.466  -1.086 -42.386  1.00 45.03           N  
ANISOU 1750  N   ARG A1034     6170   7131   3809   -916   -494    494       N  
ATOM   1751  CA  ARG A1034     -44.094  -0.686 -42.104  1.00 51.58           C  
ANISOU 1751  CA  ARG A1034     7067   8035   4497  -1082   -386    436       C  
ATOM   1752  C   ARG A1034     -43.897  -0.400 -40.619  1.00 52.67           C  
ANISOU 1752  C   ARG A1034     7134   8264   4615  -1147   -280    302       C  
ATOM   1753  O   ARG A1034     -42.831  -0.661 -40.064  1.00 54.52           O  
ANISOU 1753  O   ARG A1034     7313   8674   4729  -1283   -253    267       O  
ATOM   1754  CB  ARG A1034     -43.709   0.543 -42.933  1.00 45.15           C  
ANISOU 1754  CB  ARG A1034     6470   7019   3668  -1153   -373    470       C  
ATOM   1755  CG  ARG A1034     -42.210   0.764 -43.028  1.00 45.41           C  
ANISOU 1755  CG  ARG A1034     6535   7135   3583  -1359   -270    452       C  
ATOM   1756  CD  ARG A1034     -41.866   2.116 -43.630  1.00 47.35           C  
ANISOU 1756  CD  ARG A1034     7005   7146   3840  -1466   -213    480       C  
ATOM   1757  NE  ARG A1034     -40.427   2.262 -43.822  1.00 48.06           N  
ANISOU 1757  NE  ARG A1034     7077   7323   3861  -1688    -95    484       N  
ATOM   1758  CZ  ARG A1034     -39.660   3.073 -43.102  1.00 61.13           C  
ANISOU 1758  CZ  ARG A1034     8711   8963   5551  -1897    -28    381       C  
ATOM   1759  NH1 ARG A1034     -40.197   3.808 -42.138  1.00 74.55           N  
ANISOU 1759  NH1 ARG A1034    10471  10547   7309  -1905    -43    239       N  
ATOM   1760  NH2 ARG A1034     -38.359   3.145 -43.341  1.00 64.63           N  
ANISOU 1760  NH2 ARG A1034     9070   9501   5985  -2110     69    408       N  
ATOM   1761  N   ALA A1035     -44.931   0.133 -39.978  1.00 49.69           N  
ANISOU 1761  N   ALA A1035     6760   7766   4353  -1047   -220    230       N  
ATOM   1762  CA  ALA A1035     -44.853   0.466 -38.562  1.00 44.71           C  
ANISOU 1762  CA  ALA A1035     6146   7197   3645  -1115    -87     74       C  
ATOM   1763  C   ALA A1035     -44.844  -0.802 -37.715  1.00 46.79           C  
ANISOU 1763  C   ALA A1035     6258   7716   3803  -1110    -79    100       C  
ATOM   1764  O   ALA A1035     -44.088  -0.913 -36.749  1.00 44.19           O  
ANISOU 1764  O   ALA A1035     5950   7557   3282  -1245    -63     34       O  
ATOM   1765  CB  ALA A1035     -46.008   1.367 -38.164  1.00 44.17           C  
ANISOU 1765  CB  ALA A1035     6139   6895   3750   -977     50    -16       C  
ATOM   1766  N   ALA A1036     -45.685  -1.759 -38.093  1.00 45.42           N  
ANISOU 1766  N   ALA A1036     5942   7560   3756   -969   -116    212       N  
ATOM   1767  CA  ALA A1036     -45.802  -3.014 -37.365  1.00 41.76           C  
ANISOU 1767  CA  ALA A1036     5351   7285   3232   -955    -89    270       C  
ATOM   1768  C   ALA A1036     -44.556  -3.877 -37.529  1.00 44.44           C  
ANISOU 1768  C   ALA A1036     5651   7804   3431  -1040   -188    356       C  
ATOM   1769  O   ALA A1036     -44.112  -4.523 -36.578  1.00 48.52           O  
ANISOU 1769  O   ALA A1036     6124   8498   3812  -1083   -173    390       O  
ATOM   1770  CB  ALA A1036     -47.033  -3.772 -37.824  1.00 38.96           C  
ANISOU 1770  CB  ALA A1036     4847   6860   3097   -820   -108    364       C  
ATOM   1771  N   ALA A1037     -44.002  -3.891 -38.739  1.00 44.51           N  
ANISOU 1771  N   ALA A1037     5681   7756   3474  -1051   -274    408       N  
ATOM   1772  CA  ALA A1037     -42.784  -4.646 -39.013  1.00 42.00           C  
ANISOU 1772  CA  ALA A1037     5300   7576   3083  -1100   -310    487       C  
ATOM   1773  C   ALA A1037     -41.640  -4.159 -38.130  1.00 52.81           C  
ANISOU 1773  C   ALA A1037     6639   9105   4322  -1246   -320    447       C  
ATOM   1774  O   ALA A1037     -40.919  -4.959 -37.534  1.00 51.84           O  
ANISOU 1774  O   ALA A1037     6390   9166   4140  -1259   -362    532       O  
ATOM   1775  CB  ALA A1037     -42.406  -4.536 -40.480  1.00 43.65           C  
ANISOU 1775  CB  ALA A1037     5588   7674   3325  -1099   -330    520       C  
ATOM   1776  N   LEU A1038     -41.482  -2.841 -38.050  1.00 59.47           N  
ANISOU 1776  N   LEU A1038     7599   9862   5134  -1365   -304    328       N  
ATOM   1777  CA  LEU A1038     -40.454  -2.240 -37.210  1.00 40.64           C  
ANISOU 1777  CA  LEU A1038     5207   7610   2624  -1564   -352    256       C  
ATOM   1778  C   LEU A1038     -40.764  -2.482 -35.741  1.00 59.03           C  
ANISOU 1778  C   LEU A1038     7565  10083   4781  -1589   -369    206       C  
ATOM   1779  O   LEU A1038     -39.862  -2.630 -34.914  1.00 43.23           O  
ANISOU 1779  O   LEU A1038     5503   8292   2629  -1726   -489    222       O  
ATOM   1780  CB  LEU A1038     -40.343  -0.740 -37.476  1.00 41.89           C  
ANISOU 1780  CB  LEU A1038     5537   7576   2802  -1706   -310    118       C  
ATOM   1781  CG  LEU A1038     -39.793  -0.299 -38.829  1.00 41.75           C  
ANISOU 1781  CG  LEU A1038     5541   7426   2896  -1749   -279    182       C  
ATOM   1782  CD1 LEU A1038     -39.896   1.212 -38.960  1.00 55.97           C  
ANISOU 1782  CD1 LEU A1038     7557   8979   4730  -1875   -220     61       C  
ATOM   1783  CD2 LEU A1038     -38.355  -0.765 -39.003  1.00 42.39           C  
ANISOU 1783  CD2 LEU A1038     5413   7708   2987  -1873   -315    273       C  
ATOM   1784  N   ASP A1039     -42.053  -2.513 -35.427  1.00 53.99           N  
ANISOU 1784  N   ASP A1039     7015   9334   4163  -1461   -250    158       N  
ATOM   1785  CA  ASP A1039     -42.511  -2.739 -34.065  1.00 48.63           C  
ANISOU 1785  CA  ASP A1039     6415   8766   3298  -1474   -187    110       C  
ATOM   1786  C   ASP A1039     -42.146  -4.148 -33.609  1.00 55.31           C  
ANISOU 1786  C   ASP A1039     7121   9835   4060  -1428   -274    307       C  
ATOM   1787  O   ASP A1039     -41.620  -4.340 -32.513  1.00 61.55           O  
ANISOU 1787  O   ASP A1039     7960  10822   4603  -1534   -356    328       O  
ATOM   1788  CB  ASP A1039     -44.021  -2.519 -33.976  1.00 57.76           C  
ANISOU 1788  CB  ASP A1039     7634   9736   4578  -1321     21     42       C  
ATOM   1789  CG  ASP A1039     -44.485  -2.222 -32.571  1.00 75.82           C  
ANISOU 1789  CG  ASP A1039    10096  12067   6644  -1371    189    -90       C  
ATOM   1790  OD1 ASP A1039     -43.627  -1.931 -31.713  1.00 93.35           O  
ANISOU 1790  OD1 ASP A1039    12460  14438   8572  -1561    104   -171       O  
ATOM   1791  OD2 ASP A1039     -45.709  -2.274 -32.326  1.00 84.62           O  
ANISOU 1791  OD2 ASP A1039    11206  13070   7876  -1232    411   -115       O  
ATOM   1792  N   ALA A1040     -42.418  -5.128 -34.465  1.00 51.26           N  
ANISOU 1792  N   ALA A1040     6463   9272   3743  -1276   -271    455       N  
ATOM   1793  CA  ALA A1040     -42.133  -6.527 -34.158  1.00 48.29           C  
ANISOU 1793  CA  ALA A1040     5968   9031   3350  -1201   -323    656       C  
ATOM   1794  C   ALA A1040     -40.632  -6.808 -34.125  1.00 47.68           C  
ANISOU 1794  C   ALA A1040     5759   9132   3225  -1265   -497    766       C  
ATOM   1795  O   ALA A1040     -40.169  -7.659 -33.366  1.00 45.28           O  
ANISOU 1795  O   ALA A1040     5387   8992   2825  -1241   -587    934       O  
ATOM   1796  CB  ALA A1040     -42.814  -7.438 -35.165  1.00 38.97           C  
ANISOU 1796  CB  ALA A1040     4704   7695   2406  -1051   -266    743       C  
ATOM   1797  N   GLN A1041     -39.876  -6.097 -34.953  1.00 44.39           N  
ANISOU 1797  N   GLN A1041     5288   8678   2899  -1340   -538    699       N  
ATOM   1798  CA  GLN A1041     -38.429  -6.270 -34.993  1.00 42.56           C  
ANISOU 1798  CA  GLN A1041     4858   8615   2699  -1407   -675    804       C  
ATOM   1799  C   GLN A1041     -37.775  -5.716 -33.734  1.00 56.13           C  
ANISOU 1799  C   GLN A1041     6590  10550   4188  -1608   -863    772       C  
ATOM   1800  O   GLN A1041     -36.767  -6.241 -33.264  1.00 62.90           O  
ANISOU 1800  O   GLN A1041     7250  11619   5032  -1633  -1048    936       O  
ATOM   1801  CB  GLN A1041     -37.841  -5.588 -36.228  1.00 46.75           C  
ANISOU 1801  CB  GLN A1041     5337   9034   3392  -1463   -613    739       C  
ATOM   1802  CG  GLN A1041     -36.358  -5.838 -36.438  1.00 43.77           C  
ANISOU 1802  CG  GLN A1041     4681   8813   3138  -1511   -686    864       C  
ATOM   1803  CD  GLN A1041     -35.764  -4.924 -37.492  1.00 49.54           C  
ANISOU 1803  CD  GLN A1041     5392   9440   3990  -1634   -582    784       C  
ATOM   1804  OE1 GLN A1041     -36.186  -3.777 -37.638  1.00 50.64           O  
ANISOU 1804  OE1 GLN A1041     5732   9445   4062  -1771   -550    626       O  
ATOM   1805  NE2 GLN A1041     -34.781  -5.426 -38.234  1.00 45.17           N  
ANISOU 1805  NE2 GLN A1041     4606   8925   3630  -1576   -493    904       N  
ATOM   1806  N   LYS A1042     -38.360  -4.654 -33.186  1.00 57.92           N  
ANISOU 1806  N   LYS A1042     7057  10705   4244  -1747   -822    560       N  
ATOM   1807  CA  LYS A1042     -37.780  -3.965 -32.038  1.00 48.97           C  
ANISOU 1807  CA  LYS A1042     6014   9660   2930  -1955   -969    454       C  
ATOM   1808  C   LYS A1042     -38.072  -4.682 -30.719  1.00 62.51           C  
ANISOU 1808  C   LYS A1042     7832  11439   4480  -1884  -1006    535       C  
ATOM   1809  O   LYS A1042     -37.701  -4.203 -29.646  1.00 53.90           O  
ANISOU 1809  O   LYS A1042     6883  10415   3182  -2045  -1132    448       O  
ATOM   1810  CB  LYS A1042     -38.292  -2.524 -31.973  1.00 49.53           C  
ANISOU 1810  CB  LYS A1042     6360   9570   2888  -2125   -864    167       C  
ATOM   1811  N   ALA A1043     -38.735  -5.832 -30.805  1.00 56.37           N  
ANISOU 1811  N   ALA A1043     7012  10634   3772  -1664   -900    702       N  
ATOM   1812  CA  ALA A1043     -39.023  -6.644 -29.629  1.00 62.32           C  
ANISOU 1812  CA  ALA A1043     7872  11444   4363  -1596   -915    825       C  
ATOM   1813  C   ALA A1043     -37.891  -7.630 -29.372  1.00 75.93           C  
ANISOU 1813  C   ALA A1043     9370  13343   6137  -1545  -1156   1100       C  
ATOM   1814  O   ALA A1043     -38.064  -8.628 -28.674  1.00 77.86           O  
ANISOU 1814  O   ALA A1043     9656  13622   6307  -1434  -1175   1292       O  
ATOM   1815  CB  ALA A1043     -40.339  -7.382 -29.803  1.00 60.50           C  
ANISOU 1815  CB  ALA A1043     7710  11091   4186  -1423   -668    884       C  
ATOM   1816  N   THR A1044     -36.730  -7.336 -29.947  1.00 81.70           N  
ANISOU 1816  N   THR A1044     9851  14189   7002  -1626  -1331   1137       N  
ATOM   1817  CA  THR A1044     -35.578  -8.224 -29.889  1.00 77.81           C  
ANISOU 1817  CA  THR A1044     9055  13878   6630  -1551  -1556   1422       C  
ATOM   1818  C   THR A1044     -34.339  -7.426 -30.274  1.00 75.99           C  
ANISOU 1818  C   THR A1044     8573  13792   6507  -1739  -1746   1382       C  
ATOM   1819  O   THR A1044     -34.391  -6.609 -31.193  1.00 88.06           O  
ANISOU 1819  O   THR A1044    10082  15261   8116  -1841  -1635   1214       O  
ATOM   1820  CB  THR A1044     -35.760  -9.441 -30.831  1.00 75.40           C  
ANISOU 1820  CB  THR A1044     8567  13530   6553  -1289  -1427   1643       C  
ATOM   1821  OG1 THR A1044     -36.882 -10.219 -30.396  1.00 82.82           O  
ANISOU 1821  OG1 THR A1044     9726  14333   7410  -1156  -1266   1697       O  
ATOM   1822  CG2 THR A1044     -34.526 -10.329 -30.854  1.00 84.89           C  
ANISOU 1822  CG2 THR A1044     9411  14908   7936  -1164  -1634   1962       C  
ATOM   1823  N   PRO A1045     -33.227  -7.635 -29.553  1.00 60.92           N  
ANISOU 1823  N   PRO A1045     6471  12071   4607  -1802  -2043   1545       N  
ATOM   1824  CA  PRO A1045     -31.982  -6.952 -29.907  1.00 77.57           C  
ANISOU 1824  CA  PRO A1045     8264  14324   6886  -1994  -2233   1537       C  
ATOM   1825  C   PRO A1045     -31.507  -7.310 -31.305  1.00 75.85           C  
ANISOU 1825  C   PRO A1045     7658  14152   7012  -1869  -2112   1666       C  
ATOM   1826  O   PRO A1045     -31.883  -8.360 -31.829  1.00 69.94           O  
ANISOU 1826  O   PRO A1045     6836  13365   6374  -1591  -1968   1840       O  
ATOM   1827  CB  PRO A1045     -30.989  -7.460 -28.854  1.00 68.19           C  
ANISOU 1827  CB  PRO A1045     6905  13314   5690  -1998  -2581   1761       C  
ATOM   1828  CG  PRO A1045     -31.592  -8.716 -28.328  1.00 67.93           C  
ANISOU 1828  CG  PRO A1045     7003  13239   5568  -1728  -2538   1975       C  
ATOM   1829  CD  PRO A1045     -33.064  -8.473 -28.354  1.00 64.22           C  
ANISOU 1829  CD  PRO A1045     6951  12566   4882  -1713  -2232   1751       C  
ATOM   1830  N   PRO A1046     -30.680  -6.444 -31.906  1.00 82.11           N  
ANISOU 1830  N   PRO A1046     8204  15016   7977  -2084  -2154   1581       N  
ATOM   1831  CA  PRO A1046     -30.046  -6.768 -33.185  1.00 77.26           C  
ANISOU 1831  CA  PRO A1046     7194  14400   7761  -1957  -1969   1698       C  
ATOM   1832  C   PRO A1046     -29.213  -8.051 -33.112  1.00 72.21           C  
ANISOU 1832  C   PRO A1046     6122  13897   7419  -1675  -2062   2055       C  
ATOM   1833  O   PRO A1046     -28.934  -8.555 -32.024  1.00 77.99           O  
ANISOU 1833  O   PRO A1046     6838  14737   8058  -1627  -2340   2223       O  
ATOM   1834  CB  PRO A1046     -29.145  -5.558 -33.446  1.00 82.53           C  
ANISOU 1834  CB  PRO A1046     7659  15136   8564  -2305  -2044   1566       C  
ATOM   1835  CG  PRO A1046     -29.736  -4.456 -32.647  1.00 86.59           C  
ANISOU 1835  CG  PRO A1046     8610  15589   8702  -2598  -2169   1288       C  
ATOM   1836  CD  PRO A1046     -30.284  -5.111 -31.418  1.00 91.57           C  
ANISOU 1836  CD  PRO A1046     9519  16213   9061  -2447  -2299   1349       C  
ATOM   1837  N   LYS A1047     -28.800  -8.560 -34.267  1.00 67.92           N  
ANISOU 1837  N   LYS A1047     5334  13207   7267  -1452  -1735   2129       N  
ATOM   1838  CA  LYS A1047     -27.997  -9.772 -34.309  1.00 74.91           C  
ANISOU 1838  CA  LYS A1047     5798  14156   8509  -1138  -1744   2455       C  
ATOM   1839  C   LYS A1047     -26.537  -9.483 -33.971  1.00 87.93           C  
ANISOU 1839  C   LYS A1047     6852  16097  10460  -1276  -2032   2642       C  
ATOM   1840  O   LYS A1047     -25.620 -10.108 -34.502  1.00 88.76           O  
ANISOU 1840  O   LYS A1047     6483  16208  11032  -1051  -1886   2851       O  
ATOM   1841  CB  LYS A1047     -28.104 -10.440 -35.675  1.00 74.47           C  
ANISOU 1841  CB  LYS A1047     5744  13805   8745   -845  -1236   2431       C  
ATOM   1842  CG  LYS A1047     -27.696 -11.899 -35.641  1.00 89.80           C  
ANISOU 1842  CG  LYS A1047     7431  15697  10992   -444  -1175   2736       C  
ATOM   1843  CD  LYS A1047     -28.818 -12.736 -35.057  1.00 97.30           C  
ANISOU 1843  CD  LYS A1047     8782  16520  11666   -285  -1233   2787       C  
ATOM   1844  CE  LYS A1047     -28.479 -14.228 -34.972  1.00107.53           C  
ANISOU 1844  CE  LYS A1047     9886  17704  13267    119  -1168   3105       C  
ATOM   1845  NZ  LYS A1047     -27.787 -14.764 -36.178  1.00113.25           N  
ANISOU 1845  NZ  LYS A1047    10354  18222  14453    376   -741   3118       N  
ATOM   1846  N   LEU A1048     -26.328  -8.515 -33.086  1.00 96.40           N  
ANISOU 1846  N   LEU A1048     8075  17261  11291  -1620  -2352   2498       N  
ATOM   1847  CA  LEU A1048     -25.019  -8.282 -32.496  1.00103.43           C  
ANISOU 1847  CA  LEU A1048     8603  18279  12419  -1742  -2648   2609       C  
ATOM   1848  C   LEU A1048     -24.686  -9.508 -31.663  1.00120.78           C  
ANISOU 1848  C   LEU A1048    10675  20527  14688  -1439  -2882   2929       C  
ATOM   1849  O   LEU A1048     -23.526  -9.906 -31.544  1.00126.67           O  
ANISOU 1849  O   LEU A1048    10950  21354  15826  -1327  -3024   3150       O  
ATOM   1850  CB  LEU A1048     -25.013  -6.999 -31.651  1.00 92.80           C  
ANISOU 1850  CB  LEU A1048     7546  16975  10740  -2177  -2935   2350       C  
ATOM   1851  CG  LEU A1048     -26.108  -6.790 -30.595  1.00 91.34           C  
ANISOU 1851  CG  LEU A1048     7979  16739   9988  -2272  -3078   2184       C  
ATOM   1852  CD1 LEU A1048     -25.763  -7.440 -29.261  1.00 83.91           C  
ANISOU 1852  CD1 LEU A1048     7072  15907   8902  -2192  -3454   2377       C  
ATOM   1853  CD2 LEU A1048     -26.389  -5.305 -30.403  1.00 79.16           C  
ANISOU 1853  CD2 LEU A1048     6766  15128   8181  -2681  -3104   1826       C  
ATOM   1854  N   GLU A1049     -25.738 -10.098 -31.098  1.00125.37           N  
ANISOU 1854  N   GLU A1049    11688  21040  14906  -1306  -2900   2952       N  
ATOM   1855  CA  GLU A1049     -25.669 -11.378 -30.404  1.00121.86           C  
ANISOU 1855  CA  GLU A1049    11216  20586  14498   -993  -3045   3269       C  
ATOM   1856  C   GLU A1049     -24.624 -11.382 -29.296  1.00130.72           C  
ANISOU 1856  C   GLU A1049    12140  21867  15659  -1078  -3502   3429       C  
ATOM   1857  O   GLU A1049     -23.938 -12.382 -29.082  1.00141.56           O  
ANISOU 1857  O   GLU A1049    13196  23257  17333   -792  -3619   3756       O  
ATOM   1858  CB  GLU A1049     -25.383 -12.503 -31.402  1.00120.16           C  
ANISOU 1858  CB  GLU A1049    10627  20262  14767   -573  -2737   3518       C  
ATOM   1859  N   PRO A1056     -24.321 -17.791 -33.282  1.00135.70           N  
ANISOU 1859  N   PRO A1056    11664  21437  18461   1298  -1741   4632       N  
ATOM   1860  CA  PRO A1056     -24.728 -17.057 -34.486  1.00136.66           C  
ANISOU 1860  CA  PRO A1056    11809  21545  18572   1173  -1345   4321       C  
ATOM   1861  C   PRO A1056     -24.084 -17.634 -35.744  1.00142.64           C  
ANISOU 1861  C   PRO A1056    12280  22026  19892   1506   -763   4305       C  
ATOM   1862  O   PRO A1056     -23.332 -16.933 -36.423  1.00138.60           O  
ANISOU 1862  O   PRO A1056    11423  21612  19627   1389   -565   4187       O  
ATOM   1863  CB  PRO A1056     -24.223 -15.634 -34.220  1.00132.36           C  
ANISOU 1863  CB  PRO A1056    11149  21285  17856    709  -1615   4116       C  
ATOM   1864  CG  PRO A1056     -24.066 -15.552 -32.738  1.00132.11           C  
ANISOU 1864  CG  PRO A1056    11247  21419  17528    539  -2182   4243       C  
ATOM   1865  CD  PRO A1056     -23.639 -16.919 -32.312  1.00136.14           C  
ANISOU 1865  CD  PRO A1056    11603  21786  18338    949  -2235   4612       C  
ATOM   1866  N   GLU A1057     -24.378 -18.896 -36.045  1.00147.46           N  
ANISOU 1866  N   GLU A1057    13067  22267  20695   1902   -457   4408       N  
ATOM   1867  CA  GLU A1057     -23.756 -19.578 -37.174  1.00154.93           C  
ANISOU 1867  CA  GLU A1057    13800  22898  22170   2259    138   4387       C  
ATOM   1868  C   GLU A1057     -24.760 -19.910 -38.273  1.00157.16           C  
ANISOU 1868  C   GLU A1057    14731  22749  22235   2278    673   3999       C  
ATOM   1869  O   GLU A1057     -24.371 -20.201 -39.403  1.00173.76           O  
ANISOU 1869  O   GLU A1057    16804  24591  24626   2463   1234   3846       O  
ATOM   1870  CB  GLU A1057     -23.060 -20.859 -36.705  1.00161.62           C  
ANISOU 1870  CB  GLU A1057    14324  23582  23504   2728    100   4804       C  
ATOM   1871  N   MET A1058     -26.047 -19.873 -37.944  1.00157.95           N  
ANISOU 1871  N   MET A1058    15415  22774  21826   2078    503   3840       N  
ATOM   1872  CA  MET A1058     -27.079 -20.152 -38.939  1.00145.30           C  
ANISOU 1872  CA  MET A1058    14418  20793  19997   2043    913   3479       C  
ATOM   1873  C   MET A1058     -28.266 -19.186 -38.857  1.00141.13           C  
ANISOU 1873  C   MET A1058    14349  20382  18892   1621    710   3186       C  
ATOM   1874  O   MET A1058     -28.219 -18.198 -38.124  1.00137.55           O  
ANISOU 1874  O   MET A1058    13764  20286  18214   1348    326   3215       O  
ATOM   1875  CB  MET A1058     -27.551 -21.604 -38.823  1.00134.34           C  
ANISOU 1875  CB  MET A1058    13290  19001  18750   2363   1056   3611       C  
ATOM   1876  CG  MET A1058     -26.691 -22.569 -39.637  1.00131.98           C  
ANISOU 1876  CG  MET A1058    12790  18357  18997   2789   1568   3672       C  
ATOM   1877  SD  MET A1058     -27.149 -24.310 -39.498  1.00185.12           S  
ANISOU 1877  SD  MET A1058    19837  24537  25964   3178   1765   3835       S  
ATOM   1878  CE  MET A1058     -26.893 -24.603 -37.750  1.00106.02           C  
ANISOU 1878  CE  MET A1058     9470  14807  16007   3286   1121   4413       C  
ATOM   1879  N   LYS A1059     -29.324 -19.507 -39.604  1.00145.10           N  
ANISOU 1879  N   LYS A1059    15386  20564  19180   1576    965   2907       N  
ATOM   1880  CA  LYS A1059     -30.339 -18.542 -40.050  1.00124.35           C  
ANISOU 1880  CA  LYS A1059    13161  17973  16113   1225    931   2571       C  
ATOM   1881  C   LYS A1059     -30.789 -17.483 -39.044  1.00101.02           C  
ANISOU 1881  C   LYS A1059    10199  15364  12821    916    483   2585       C  
ATOM   1882  O   LYS A1059     -30.988 -17.753 -37.858  1.00102.99           O  
ANISOU 1882  O   LYS A1059    10397  15747  12988    925    161   2806       O  
ATOM   1883  CB  LYS A1059     -31.576 -19.287 -40.558  1.00117.47           C  
ANISOU 1883  CB  LYS A1059    12821  16737  15074   1229   1091   2378       C  
ATOM   1884  CG  LYS A1059     -32.360 -18.491 -41.594  1.00108.34           C  
ANISOU 1884  CG  LYS A1059    12048  15516  13602    967   1210   2013       C  
ATOM   1885  CD  LYS A1059     -33.330 -19.359 -42.375  1.00107.05           C  
ANISOU 1885  CD  LYS A1059    12358  14960  13355    991   1411   1811       C  
ATOM   1886  CE  LYS A1059     -33.998 -18.557 -43.482  1.00102.09           C  
ANISOU 1886  CE  LYS A1059    12089  14288  12413    744   1487   1485       C  
ATOM   1887  NZ  LYS A1059     -35.319 -19.126 -43.875  1.00 97.68           N  
ANISOU 1887  NZ  LYS A1059    11974  13461  11681    637   1449   1305       N  
ATOM   1888  N   ASP A1060     -30.959 -16.273 -39.568  1.00100.07           N  
ANISOU 1888  N   ASP A1060    10178  15356  12487    643    500   2341       N  
ATOM   1889  CA  ASP A1060     -31.275 -15.086 -38.787  1.00 56.54           C  
ANISOU 1889  CA  ASP A1060     4674  10128   6679    338    154   2292       C  
ATOM   1890  C   ASP A1060     -32.600 -14.496 -39.264  1.00 52.40           C  
ANISOU 1890  C   ASP A1060     4614   9475   5822    136    194   2005       C  
ATOM   1891  O   ASP A1060     -32.634 -13.680 -40.184  1.00 53.55           O  
ANISOU 1891  O   ASP A1060     4879   9577   5890     -4    347   1801       O  
ATOM   1892  CB  ASP A1060     -30.129 -14.076 -38.912  1.00 62.99           C  
ANISOU 1892  CB  ASP A1060     5119  11189   7626    191    120   2300       C  
ATOM   1893  CG  ASP A1060     -30.487 -12.697 -38.397  1.00 62.62           C  
ANISOU 1893  CG  ASP A1060     5176  11350   7267   -166   -152   2156       C  
ATOM   1894  OD1 ASP A1060     -31.322 -12.581 -37.474  1.00 59.98           O  
ANISOU 1894  OD1 ASP A1060     5056  11084   6650   -263   -410   2149       O  
ATOM   1895  OD2 ASP A1060     -29.914 -11.723 -38.925  1.00 63.78           O  
ANISOU 1895  OD2 ASP A1060     5200  11570   7462   -350    -68   2049       O  
ATOM   1896  N   PHE A1061     -33.689 -14.919 -38.628  1.00 55.84           N  
ANISOU 1896  N   PHE A1061     5294   9844   6080    127     59   2017       N  
ATOM   1897  CA  PHE A1061     -35.035 -14.562 -39.070  1.00 47.75           C  
ANISOU 1897  CA  PHE A1061     4650   8671   4822    -18     94   1784       C  
ATOM   1898  C   PHE A1061     -35.376 -13.094 -38.840  1.00 45.58           C  
ANISOU 1898  C   PHE A1061     4439   8569   4311   -280    -61   1632       C  
ATOM   1899  O   PHE A1061     -36.293 -12.561 -39.461  1.00 43.39           O  
ANISOU 1899  O   PHE A1061     4419   8170   3898   -388    -12   1438       O  
ATOM   1900  CB  PHE A1061     -36.071 -15.439 -38.364  1.00 50.76           C  
ANISOU 1900  CB  PHE A1061     5206   8942   5141     34     19   1868       C  
ATOM   1901  CG  PHE A1061     -35.854 -16.909 -38.560  1.00 62.46           C  
ANISOU 1901  CG  PHE A1061     6684  10184   6864    281    179   2014       C  
ATOM   1902  CD1 PHE A1061     -36.040 -17.490 -39.802  1.00 64.76           C  
ANISOU 1902  CD1 PHE A1061     7170  10171   7263    357    445   1851       C  
ATOM   1903  CD2 PHE A1061     -35.474 -17.715 -37.498  1.00 75.82           C  
ANISOU 1903  CD2 PHE A1061     8220  11931   8656    433     62   2315       C  
ATOM   1904  CE1 PHE A1061     -35.842 -18.844 -39.986  1.00 72.64           C  
ANISOU 1904  CE1 PHE A1061     8208  10893   8497    583    625   1955       C  
ATOM   1905  CE2 PHE A1061     -35.276 -19.072 -37.675  1.00 82.09           C  
ANISOU 1905  CE2 PHE A1061     9030  12451   9710    681    228   2465       C  
ATOM   1906  CZ  PHE A1061     -35.461 -19.637 -38.921  1.00 81.10           C  
ANISOU 1906  CZ  PHE A1061     9100  11991   9723    757    528   2269       C  
ATOM   1907  N   ARG A1062     -34.641 -12.443 -37.945  1.00 52.85           N  
ANISOU 1907  N   ARG A1062     5131   9757   5193   -385   -266   1725       N  
ATOM   1908  CA  ARG A1062     -34.882 -11.037 -37.646  1.00 50.51           C  
ANISOU 1908  CA  ARG A1062     4917   9588   4686   -643   -399   1566       C  
ATOM   1909  C   ARG A1062     -34.548 -10.167 -38.855  1.00 50.50           C  
ANISOU 1909  C   ARG A1062     4949   9500   4738   -744   -223   1405       C  
ATOM   1910  O   ARG A1062     -35.116  -9.089 -39.032  1.00 45.92           O  
ANISOU 1910  O   ARG A1062     4564   8881   4003   -917   -245   1237       O  
ATOM   1911  CB  ARG A1062     -34.063 -10.598 -36.430  1.00 52.35           C  
ANISOU 1911  CB  ARG A1062     4922  10117   4853   -769   -680   1687       C  
ATOM   1912  CG  ARG A1062     -34.447  -9.238 -35.870  1.00 53.77           C  
ANISOU 1912  CG  ARG A1062     5265  10393   4773  -1047   -822   1500       C  
ATOM   1913  CD  ARG A1062     -33.446  -8.783 -34.822  1.00 57.02           C  
ANISOU 1913  CD  ARG A1062     5454  11095   5116  -1221  -1124   1591       C  
ATOM   1914  NE  ARG A1062     -33.921  -7.625 -34.071  1.00 54.80           N  
ANISOU 1914  NE  ARG A1062     5413  10875   4531  -1487  -1257   1393       N  
ATOM   1915  CZ  ARG A1062     -33.602  -6.367 -34.356  1.00 55.48           C  
ANISOU 1915  CZ  ARG A1062     5525  10947   4609  -1730  -1261   1204       C  
ATOM   1916  NH1 ARG A1062     -32.805  -6.098 -35.380  1.00 62.38           N  
ANISOU 1916  NH1 ARG A1062     6182  11770   5749  -1756  -1134   1209       N  
ATOM   1917  NH2 ARG A1062     -34.081  -5.377 -33.617  1.00 51.58           N  
ANISOU 1917  NH2 ARG A1062     5293  10461   3843  -1952  -1354   1007       N  
ATOM   1918  N   HIS A1063     -33.631 -10.652 -39.688  1.00 46.96           N  
ANISOU 1918  N   HIS A1063     4327   8999   4518   -622    -17   1470       N  
ATOM   1919  CA  HIS A1063     -33.220  -9.932 -40.889  1.00 57.69           C  
ANISOU 1919  CA  HIS A1063     5737  10270   5913   -713    211   1349       C  
ATOM   1920  C   HIS A1063     -34.370  -9.804 -41.886  1.00 55.46           C  
ANISOU 1920  C   HIS A1063     5879   9745   5448   -722    333   1174       C  
ATOM   1921  O   HIS A1063     -34.360  -8.927 -42.748  1.00 64.64           O  
ANISOU 1921  O   HIS A1063     7200  10832   6527   -850    447   1068       O  
ATOM   1922  CB  HIS A1063     -32.026 -10.629 -41.548  1.00 62.36           C  
ANISOU 1922  CB  HIS A1063     6056  10841   6797   -546    480   1460       C  
ATOM   1923  CG  HIS A1063     -31.530  -9.936 -42.781  1.00 63.73           C  
ANISOU 1923  CG  HIS A1063     6295  10929   6991   -646    781   1356       C  
ATOM   1924  ND1 HIS A1063     -31.279  -8.586 -42.826  1.00 63.39           N  
ANISOU 1924  ND1 HIS A1063     6237  10972   6875   -917    725   1292       N  
ATOM   1925  CD2 HIS A1063     -31.247 -10.417 -44.019  1.00 57.01           C  
ANISOU 1925  CD2 HIS A1063     5569   9891   6201   -522   1169   1306       C  
ATOM   1926  CE1 HIS A1063     -30.857  -8.256 -44.038  1.00 64.98           C  
ANISOU 1926  CE1 HIS A1063     6538  11054   7098   -958   1065   1237       C  
ATOM   1927  NE2 HIS A1063     -30.830  -9.349 -44.776  1.00 63.81           N  
ANISOU 1927  NE2 HIS A1063     6486  10751   7008   -720   1343   1237       N  
ATOM   1928  N   GLY A1064     -35.361 -10.679 -41.755  1.00 45.34           N  
ANISOU 1928  N   GLY A1064     4778   8339   4111   -602    289   1164       N  
ATOM   1929  CA  GLY A1064     -36.539 -10.639 -42.602  1.00 43.62           C  
ANISOU 1929  CA  GLY A1064     4920   7914   3741   -626    320   1017       C  
ATOM   1930  C   GLY A1064     -37.281  -9.317 -42.548  1.00 43.54           C  
ANISOU 1930  C   GLY A1064     5060   7918   3566   -805    175    914       C  
ATOM   1931  O   GLY A1064     -37.863  -8.883 -43.544  1.00 51.79           O  
ANISOU 1931  O   GLY A1064     6363   8814   4500   -853    210    817       O  
ATOM   1932  N   PHE A1065     -37.262  -8.671 -41.387  1.00 39.86           N  
ANISOU 1932  N   PHE A1065     4458   7615   3072   -898      8    937       N  
ATOM   1933  CA  PHE A1065     -37.903  -7.369 -41.242  1.00 48.97           C  
ANISOU 1933  CA  PHE A1065     5754   8745   4106  -1048    -89    828       C  
ATOM   1934  C   PHE A1065     -37.162  -6.296 -42.030  1.00 41.62           C  
ANISOU 1934  C   PHE A1065     4864   7782   3169  -1187      9    786       C  
ATOM   1935  O   PHE A1065     -37.782  -5.379 -42.563  1.00 43.00           O  
ANISOU 1935  O   PHE A1065     5259   7819   3262  -1259     -1    709       O  
ATOM   1936  CB  PHE A1065     -37.993  -6.968 -39.771  1.00 44.47           C  
ANISOU 1936  CB  PHE A1065     5085   8338   3475  -1129   -248    830       C  
ATOM   1937  CG  PHE A1065     -38.976  -7.781 -38.990  1.00 44.19           C  
ANISOU 1937  CG  PHE A1065     5081   8305   3405  -1026   -306    868       C  
ATOM   1938  CD1 PHE A1065     -40.336  -7.605 -39.167  1.00 37.82           C  
ANISOU 1938  CD1 PHE A1065     4440   7351   2578  -1000   -303    787       C  
ATOM   1939  CD2 PHE A1065     -38.539  -8.732 -38.084  1.00 47.63           C  
ANISOU 1939  CD2 PHE A1065     5361   8883   3853   -955   -362   1013       C  
ATOM   1940  CE1 PHE A1065     -41.244  -8.359 -38.449  1.00 38.87           C  
ANISOU 1940  CE1 PHE A1065     4571   7482   2717   -930   -313    832       C  
ATOM   1941  CE2 PHE A1065     -39.439  -9.487 -37.368  1.00 40.30           C  
ANISOU 1941  CE2 PHE A1065     4487   7938   2889   -880   -379   1072       C  
ATOM   1942  CZ  PHE A1065     -40.793  -9.302 -37.548  1.00 37.82           C  
ANISOU 1942  CZ  PHE A1065     4325   7478   2565   -879   -333    973       C  
ATOM   1943  N   ASP A1066     -35.839  -6.409 -42.098  1.00 41.75           N  
ANISOU 1943  N   ASP A1066     4648   7913   3300  -1220    110    859       N  
ATOM   1944  CA  ASP A1066     -35.041  -5.484 -42.897  1.00 43.23           C  
ANISOU 1944  CA  ASP A1066     4847   8064   3516  -1371    263    843       C  
ATOM   1945  C   ASP A1066     -35.434  -5.584 -44.362  1.00 48.02           C  
ANISOU 1945  C   ASP A1066     5761   8461   4022  -1311    456    810       C  
ATOM   1946  O   ASP A1066     -35.589  -4.575 -45.049  1.00 44.38           O  
ANISOU 1946  O   ASP A1066     5520   7879   3462  -1436    506    776       O  
ATOM   1947  CB  ASP A1066     -33.547  -5.770 -42.742  1.00 45.84           C  
ANISOU 1947  CB  ASP A1066     4796   8565   4057  -1396    369    951       C  
ATOM   1948  CG  ASP A1066     -33.086  -5.700 -41.307  1.00 56.94           C  
ANISOU 1948  CG  ASP A1066     5903  10205   5525  -1479    107   1006       C  
ATOM   1949  OD1 ASP A1066     -33.583  -4.825 -40.566  1.00 62.68           O  
ANISOU 1949  OD1 ASP A1066     6753  10951   6112  -1641    -85    910       O  
ATOM   1950  OD2 ASP A1066     -32.223  -6.516 -40.924  1.00 62.41           O  
ANISOU 1950  OD2 ASP A1066     6256  11055   6403  -1377     93   1149       O  
ATOM   1951  N   ILE A1067     -35.595  -6.819 -44.824  1.00 56.19           N  
ANISOU 1951  N   ILE A1067     6844   9439   5066  -1129    556    825       N  
ATOM   1952  CA  ILE A1067     -35.990  -7.088 -46.196  1.00 52.89           C  
ANISOU 1952  CA  ILE A1067     6772   8829   4494  -1084    713    772       C  
ATOM   1953  C   ILE A1067     -37.420  -6.627 -46.449  1.00 53.49           C  
ANISOU 1953  C   ILE A1067     7155   8775   4393  -1115    485    710       C  
ATOM   1954  O   ILE A1067     -37.694  -5.954 -47.445  1.00 56.18           O  
ANISOU 1954  O   ILE A1067     7792   8989   4565  -1190    513    696       O  
ATOM   1955  CB  ILE A1067     -35.868  -8.586 -46.526  1.00 49.23           C  
ANISOU 1955  CB  ILE A1067     6316   8301   4088   -895    864    767       C  
ATOM   1956  CG1 ILE A1067     -34.436  -9.067 -46.279  1.00 48.30           C  
ANISOU 1956  CG1 ILE A1067     5836   8297   4218   -811   1103    861       C  
ATOM   1957  CG2 ILE A1067     -36.281  -8.850 -47.963  1.00 45.17           C  
ANISOU 1957  CG2 ILE A1067     6233   7583   3346   -890   1011    674       C  
ATOM   1958  CD1 ILE A1067     -34.235 -10.545 -46.530  1.00 49.86           C  
ANISOU 1958  CD1 ILE A1067     6028   8387   4531   -586   1293    865       C  
ATOM   1959  N   LEU A1068     -38.324  -6.979 -45.536  1.00 48.21           N  
ANISOU 1959  N   LEU A1068     6401   8139   3776  -1055    264    698       N  
ATOM   1960  CA  LEU A1068     -39.738  -6.650 -45.691  1.00 52.60           C  
ANISOU 1960  CA  LEU A1068     7153   8583   4251  -1057     51    658       C  
ATOM   1961  C   LEU A1068     -39.955  -5.144 -45.823  1.00 55.98           C  
ANISOU 1961  C   LEU A1068     7692   8952   4626  -1165    -17    659       C  
ATOM   1962  O   LEU A1068     -40.642  -4.690 -46.737  1.00 61.74           O  
ANISOU 1962  O   LEU A1068     8680   9536   5242  -1176   -102    668       O  
ATOM   1963  CB  LEU A1068     -40.553  -7.192 -44.514  1.00 52.45           C  
ANISOU 1963  CB  LEU A1068     6958   8627   4343   -989   -101    659       C  
ATOM   1964  CG  LEU A1068     -42.074  -7.093 -44.661  1.00 48.03           C  
ANISOU 1964  CG  LEU A1068     6509   7953   3785   -967   -295    631       C  
ATOM   1965  CD1 LEU A1068     -42.578  -8.092 -45.697  1.00 48.35           C  
ANISOU 1965  CD1 LEU A1068     6735   7868   3768   -939   -339    606       C  
ATOM   1966  CD2 LEU A1068     -42.776  -7.300 -43.327  1.00 43.90           C  
ANISOU 1966  CD2 LEU A1068     5786   7509   3386   -929   -365    639       C  
ATOM   1967  N   VAL A1069     -39.360  -4.376 -44.916  1.00 50.55           N  
ANISOU 1967  N   VAL A1069     6827   8362   4019  -1253      3    655       N  
ATOM   1968  CA  VAL A1069     -39.497  -2.922 -44.940  1.00 53.38           C  
ANISOU 1968  CA  VAL A1069     7304   8617   4360  -1367    -30    641       C  
ATOM   1969  C   VAL A1069     -38.925  -2.336 -46.236  1.00 56.66           C  
ANISOU 1969  C   VAL A1069     7949   8911   4669  -1457    115    698       C  
ATOM   1970  O   VAL A1069     -39.500  -1.413 -46.816  1.00 56.89           O  
ANISOU 1970  O   VAL A1069     8221   8763   4631  -1483     51    733       O  
ATOM   1971  CB  VAL A1069     -38.807  -2.275 -43.718  1.00 50.68           C  
ANISOU 1971  CB  VAL A1069     6759   8395   4101  -1497    -29    593       C  
ATOM   1972  CG1 VAL A1069     -38.763  -0.760 -43.855  1.00 48.48           C  
ANISOU 1972  CG1 VAL A1069     6643   7955   3823  -1645    -12    562       C  
ATOM   1973  CG2 VAL A1069     -39.526  -2.674 -42.436  1.00 49.15           C  
ANISOU 1973  CG2 VAL A1069     6439   8298   3938  -1421   -158    539       C  
ATOM   1974  N   GLY A1070     -37.805  -2.887 -46.695  1.00 55.00           N  
ANISOU 1974  N   GLY A1070     7663   8784   4451  -1489    333    727       N  
ATOM   1975  CA  GLY A1070     -37.203  -2.457 -47.946  1.00 56.00           C  
ANISOU 1975  CA  GLY A1070     8024   8805   4451  -1579    551    786       C  
ATOM   1976  C   GLY A1070     -38.135  -2.677 -49.124  1.00 53.88           C  
ANISOU 1976  C   GLY A1070     8151   8377   3942  -1503    473    809       C  
ATOM   1977  O   GLY A1070     -38.202  -1.859 -50.043  1.00 46.90           O  
ANISOU 1977  O   GLY A1070     7579   7347   2892  -1584    512    885       O  
ATOM   1978  N   GLN A1071     -38.858  -3.792 -49.092  1.00 55.32           N  
ANISOU 1978  N   GLN A1071     8336   8583   4100  -1366    340    755       N  
ATOM   1979  CA  GLN A1071     -39.859  -4.089 -50.105  1.00 44.72           C  
ANISOU 1979  CA  GLN A1071     7345   7111   2537  -1324    172    759       C  
ATOM   1980  C   GLN A1071     -41.053  -3.153 -49.975  1.00 44.38           C  
ANISOU 1980  C   GLN A1071     7376   6966   2521  -1310   -144    820       C  
ATOM   1981  O   GLN A1071     -41.632  -2.728 -50.972  1.00 71.85           O  
ANISOU 1981  O   GLN A1071    11181  10316   5804  -1327   -289    899       O  
ATOM   1982  CB  GLN A1071     -40.322  -5.540 -49.995  1.00 46.64           C  
ANISOU 1982  CB  GLN A1071     7534   7385   2801  -1219    101    671       C  
ATOM   1983  CG  GLN A1071     -39.231  -6.569 -50.216  1.00 53.85           C  
ANISOU 1983  CG  GLN A1071     8403   8340   3716  -1180    431    615       C  
ATOM   1984  CD  GLN A1071     -39.669  -7.968 -49.835  1.00 54.21           C  
ANISOU 1984  CD  GLN A1071     8354   8382   3862  -1071    367    537       C  
ATOM   1985  OE1 GLN A1071     -40.558  -8.149 -49.001  1.00 53.84           O  
ANISOU 1985  OE1 GLN A1071     8132   8365   3958  -1035    118    540       O  
ATOM   1986  NE2 GLN A1071     -39.047  -8.968 -50.445  1.00 56.31           N  
ANISOU 1986  NE2 GLN A1071     8749   8582   4065  -1018    631    466       N  
ATOM   1987  N   ILE A1072     -41.424  -2.841 -48.737  1.00 54.30           N  
ANISOU 1987  N   ILE A1072     8337   8277   4018  -1268   -245    790       N  
ATOM   1988  CA  ILE A1072     -42.535  -1.933 -48.484  1.00 48.49           C  
ANISOU 1988  CA  ILE A1072     7619   7425   3383  -1216   -478    838       C  
ATOM   1989  C   ILE A1072     -42.219  -0.562 -49.060  1.00 50.06           C  
ANISOU 1989  C   ILE A1072     8051   7459   3509  -1299   -424    939       C  
ATOM   1990  O   ILE A1072     -43.020   0.001 -49.803  1.00 54.87           O  
ANISOU 1990  O   ILE A1072     8889   7910   4050  -1251   -617   1055       O  
ATOM   1991  CB  ILE A1072     -42.850  -1.808 -46.980  1.00 45.22           C  
ANISOU 1991  CB  ILE A1072     6883   7087   3211  -1168   -496    759       C  
ATOM   1992  CG1 ILE A1072     -43.433  -3.121 -46.453  1.00 42.97           C  
ANISOU 1992  CG1 ILE A1072     6402   6919   3004  -1079   -574    705       C  
ATOM   1993  CG2 ILE A1072     -43.826  -0.665 -46.732  1.00 41.87           C  
ANISOU 1993  CG2 ILE A1072     6487   6496   2925  -1101   -632    796       C  
ATOM   1994  CD1 ILE A1072     -43.859  -3.069 -44.996  1.00 46.61           C  
ANISOU 1994  CD1 ILE A1072     6601   7459   3650  -1032   -569    645       C  
ATOM   1995  N   ASP A1073     -41.040  -0.046 -48.729  1.00 58.52           N  
ANISOU 1995  N   ASP A1073     9059   8564   4613  -1433   -177    915       N  
ATOM   1996  CA  ASP A1073     -40.588   1.247 -49.233  1.00 69.15           C  
ANISOU 1996  CA  ASP A1073    10627   9732   5916  -1557    -71   1012       C  
ATOM   1997  C   ASP A1073     -40.617   1.312 -50.759  1.00 75.43           C  
ANISOU 1997  C   ASP A1073    11827  10410   6423  -1579    -58   1161       C  
ATOM   1998  O   ASP A1073     -41.078   2.297 -51.333  1.00 73.75           O  
ANISOU 1998  O   ASP A1073    11885   9986   6150  -1579   -162   1307       O  
ATOM   1999  CB  ASP A1073     -39.178   1.552 -48.723  1.00 69.21           C  
ANISOU 1999  CB  ASP A1073    10455   9828   6012  -1747    202    957       C  
ATOM   2000  CG  ASP A1073     -39.163   1.938 -47.259  1.00 75.61           C  
ANISOU 2000  CG  ASP A1073    10989  10696   7041  -1785    146    828       C  
ATOM   2001  OD1 ASP A1073     -40.217   2.382 -46.756  1.00 82.01           O  
ANISOU 2001  OD1 ASP A1073    11828  11391   7939  -1674    -23    796       O  
ATOM   2002  OD2 ASP A1073     -38.102   1.802 -46.614  1.00 74.74           O  
ANISOU 2002  OD2 ASP A1073    10636  10748   7015  -1925    271    761       O  
ATOM   2003  N   ASP A1074     -40.130   0.259 -51.409  1.00 68.95           N  
ANISOU 2003  N   ASP A1074    11080   9709   5410  -1592     76   1128       N  
ATOM   2004  CA  ASP A1074     -40.146   0.191 -52.865  1.00 70.75           C  
ANISOU 2004  CA  ASP A1074    11755   9842   5283  -1628    110   1236       C  
ATOM   2005  C   ASP A1074     -41.576   0.157 -53.394  1.00 65.26           C  
ANISOU 2005  C   ASP A1074    11229   9043   4525  -1486   -309   1297       C  
ATOM   2006  O   ASP A1074     -41.904   0.828 -54.373  1.00 66.21           O  
ANISOU 2006  O   ASP A1074    11650   9002   4504  -1475   -415   1437       O  
ATOM   2007  CB  ASP A1074     -39.372  -1.032 -53.357  1.00 81.25           C  
ANISOU 2007  CB  ASP A1074    13056  11280   6534  -1603    374   1109       C  
ATOM   2008  CG  ASP A1074     -37.900  -0.740 -53.570  1.00 88.67           C  
ANISOU 2008  CG  ASP A1074    13959  12248   7484  -1740    830   1131       C  
ATOM   2009  OD1 ASP A1074     -37.582   0.318 -54.153  1.00102.10           O  
ANISOU 2009  OD1 ASP A1074    15866  13808   9121  -1844    942   1257       O  
ATOM   2010  OD2 ASP A1074     -37.061  -1.568 -53.156  1.00 86.18           O  
ANISOU 2010  OD2 ASP A1074    13390  12089   7266  -1746   1084   1041       O  
ATOM   2011  N   ALA A1075     -42.426  -0.628 -52.741  1.00 66.88           N  
ANISOU 2011  N   ALA A1075    11212   9347   4851  -1388   -553   1211       N  
ATOM   2012  CA  ALA A1075     -43.835  -0.695 -53.107  1.00 63.45           C  
ANISOU 2012  CA  ALA A1075    10833   8842   4432  -1274   -977   1277       C  
ATOM   2013  C   ALA A1075     -44.533   0.616 -52.763  1.00 68.70           C  
ANISOU 2013  C   ALA A1075    11478   9353   5272  -1207  -1175   1445       C  
ATOM   2014  O   ALA A1075     -45.526   0.986 -53.390  1.00 69.38           O  
ANISOU 2014  O   ALA A1075    11720   9328   5315  -1129  -1523   1609       O  
ATOM   2015  CB  ALA A1075     -44.514  -1.863 -52.409  1.00 49.78           C  
ANISOU 2015  CB  ALA A1075     8819   7247   2849  -1213  -1140   1145       C  
ATOM   2016  N   LEU A1076     -44.001   1.316 -51.767  1.00 64.95           N  
ANISOU 2016  N   LEU A1076    10780   8851   5046  -1218   -948   1388       N  
ATOM   2017  CA  LEU A1076     -44.554   2.596 -51.343  1.00 63.04           C  
ANISOU 2017  CA  LEU A1076    10501   8404   5048  -1131  -1036   1488       C  
ATOM   2018  C   LEU A1076     -44.171   3.697 -52.328  1.00 62.32           C  
ANISOU 2018  C   LEU A1076    10820   8087   4770  -1209   -986   1700       C  
ATOM   2019  O   LEU A1076     -44.860   4.709 -52.440  1.00 59.57           O  
ANISOU 2019  O   LEU A1076    10568   7505   4562  -1098  -1151   1866       O  
ATOM   2020  CB  LEU A1076     -44.072   2.943 -49.933  1.00 59.39           C  
ANISOU 2020  CB  LEU A1076     9731   7973   4860  -1160   -803   1314       C  
ATOM   2021  CG  LEU A1076     -44.894   3.931 -49.106  1.00 55.65           C  
ANISOU 2021  CG  LEU A1076     9128   7308   4707  -1023   -870   1313       C  
ATOM   2022  CD1 LEU A1076     -46.379   3.648 -49.237  1.00 64.06           C  
ANISOU 2022  CD1 LEU A1076    10065   8344   5931   -798  -1192   1402       C  
ATOM   2023  CD2 LEU A1076     -44.464   3.846 -47.654  1.00 68.73           C  
ANISOU 2023  CD2 LEU A1076    10502   9079   6531  -1078   -666   1082       C  
ATOM   2024  N   LYS A1077     -43.068   3.495 -53.042  1.00 66.76           N  
ANISOU 2024  N   LYS A1077    11625   8703   5036  -1389   -727   1711       N  
ATOM   2025  CA  LYS A1077     -42.663   4.428 -54.087  1.00 71.35           C  
ANISOU 2025  CA  LYS A1077    12650   9079   5380  -1492   -637   1937       C  
ATOM   2026  C   LYS A1077     -43.621   4.350 -55.269  1.00 74.61           C  
ANISOU 2026  C   LYS A1077    13341   9422   5585  -1368   -992   2110       C  
ATOM   2027  O   LYS A1077     -43.931   5.363 -55.896  1.00 76.94           O  
ANISOU 2027  O   LYS A1077    13902   9488   5842  -1329  -1106   2346       O  
ATOM   2028  CB  LYS A1077     -41.234   4.146 -54.551  1.00 65.73           C  
ANISOU 2028  CB  LYS A1077    12042   8461   4470  -1697   -201   1874       C  
ATOM   2029  N   LEU A1078     -44.080   3.138 -55.569  1.00 75.87           N  
ANISOU 2029  N   LEU A1078    13376   9770   5680  -1297  -1156   1964       N  
ATOM   2030  CA  LEU A1078     -45.055   2.921 -56.631  1.00 79.15           C  
ANISOU 2030  CA  LEU A1078    13945  10161   5968  -1197  -1521   2057       C  
ATOM   2031  C   LEU A1078     -46.378   3.570 -56.283  1.00 81.83           C  
ANISOU 2031  C   LEU A1078    14171  10377   6542  -1025  -1968   2257       C  
ATOM   2032  O   LEU A1078     -47.039   4.160 -57.137  1.00 83.56           O  
ANISOU 2032  O   LEU A1078    14576  10471   6704   -941  -2246   2474       O  
ATOM   2033  CB  LEU A1078     -45.272   1.430 -56.874  1.00 83.59           C  
ANISOU 2033  CB  LEU A1078    14392  10919   6450  -1202  -1589   1830       C  
ATOM   2034  CG  LEU A1078     -44.022   0.573 -57.037  1.00 78.39           C  
ANISOU 2034  CG  LEU A1078    13774  10372   5640  -1316  -1148   1619       C  
ATOM   2035  CD1 LEU A1078     -44.422  -0.879 -57.251  1.00 66.94           C  
ANISOU 2035  CD1 LEU A1078    12258   9042   4136  -1304  -1263   1420       C  
ATOM   2036  CD2 LEU A1078     -43.171   1.091 -58.191  1.00 80.65           C  
ANISOU 2036  CD2 LEU A1078    14436  10566   5641  -1410   -881   1706       C  
ATOM   2037  N   ALA A1079     -46.763   3.442 -55.018  1.00 81.04           N  
ANISOU 2037  N   ALA A1079    13750  10320   6723   -962  -2036   2198       N  
ATOM   2038  CA  ALA A1079     -48.023   3.990 -54.538  1.00 82.74           C  
ANISOU 2038  CA  ALA A1079    13724  10411   7303   -746  -2391   2348       C  
ATOM   2039  C   ALA A1079     -48.033   5.510 -54.627  1.00 83.77           C  
ANISOU 2039  C   ALA A1079    14026  10221   7582   -649  -2349   2583       C  
ATOM   2040  O   ALA A1079     -49.073   6.117 -54.868  1.00 77.83           O  
ANISOU 2040  O   ALA A1079    13237   9300   7036   -445  -2699   2821       O  
ATOM   2041  CB  ALA A1079     -48.285   3.540 -53.111  1.00 81.58           C  
ANISOU 2041  CB  ALA A1079    13043  10379   7577   -661  -2246   2097       C  
ATOM   2042  N   ASN A1080     -46.870   6.121 -54.428  1.00 94.05           N  
ANISOU 2042  N   ASN A1080    15497  11423   8816   -799  -1923   2525       N  
ATOM   2043  CA  ASN A1080     -46.754   7.568 -54.517  1.00 92.57           C  
ANISOU 2043  CA  ASN A1080    15524  10883   8766   -753  -1828   2732       C  
ATOM   2044  C   ASN A1080     -46.857   8.047 -55.950  1.00 89.18           C  
ANISOU 2044  C   ASN A1080    15621  10299   7965   -774  -2052   3098       C  
ATOM   2045  O   ASN A1080     -47.531   9.035 -56.242  1.00 89.11           O  
ANISOU 2045  O   ASN A1080    15740   9997   8120   -595  -2275   3389       O  
ATOM   2046  CB  ASN A1080     -45.441   8.036 -53.900  1.00 91.51           C  
ANISOU 2046  CB  ASN A1080    15408  10693   8670   -970  -1323   2554       C  
ATOM   2047  CG  ASN A1080     -45.597   8.413 -52.449  1.00 90.92           C  
ANISOU 2047  CG  ASN A1080    14948  10548   9048   -888  -1167   2323       C  
ATOM   2048  OD1 ASN A1080     -46.659   8.875 -52.035  1.00 92.05           O  
ANISOU 2048  OD1 ASN A1080    14928  10520   9525   -638  -1350   2380       O  
ATOM   2049  ND2 ASN A1080     -44.549   8.209 -51.663  1.00 86.37           N  
ANISOU 2049  ND2 ASN A1080    14222  10108   8486  -1096   -828   2062       N  
ATOM   2050  N   GLU A1081     -46.191   7.332 -56.846  1.00 91.80           N  
ANISOU 2050  N   GLU A1081    16101  10852   7926   -939  -1903   2981       N  
ATOM   2051  CA  GLU A1081     -46.236   7.672 -58.255  1.00 90.80           C  
ANISOU 2051  CA  GLU A1081    16297  10671   7531   -939  -1990   3164       C  
ATOM   2052  C   GLU A1081     -47.639   7.498 -58.803  1.00 97.56           C  
ANISOU 2052  C   GLU A1081    17063  11563   8444   -730  -2541   3316       C  
ATOM   2053  O   GLU A1081     -48.048   8.202 -59.725  1.00103.96           O  
ANISOU 2053  O   GLU A1081    18108  12235   9158   -649  -2743   3586       O  
ATOM   2054  CB  GLU A1081     -45.255   6.820 -59.042  1.00 89.38           C  
ANISOU 2054  CB  GLU A1081    16266  10712   6984  -1138  -1684   2962       C  
ATOM   2055  CG  GLU A1081     -43.817   7.192 -58.809  1.00 94.02           C  
ANISOU 2055  CG  GLU A1081    16949  11244   7529  -1346  -1136   2888       C  
ATOM   2056  CD  GLU A1081     -42.897   6.435 -59.724  1.00107.64           C  
ANISOU 2056  CD  GLU A1081    18824  13143   8930  -1491   -831   2740       C  
ATOM   2057  OE1 GLU A1081     -43.284   5.331 -60.155  1.00115.23           O  
ANISOU 2057  OE1 GLU A1081    19748  14296   9738  -1449   -995   2588       O  
ATOM   2058  OE2 GLU A1081     -41.802   6.949 -60.032  1.00110.89           O  
ANISOU 2058  OE2 GLU A1081    19398  13475   9259  -1650   -418   2780       O  
ATOM   2059  N   GLY A1082     -48.377   6.559 -58.225  1.00 94.63           N  
ANISOU 2059  N   GLY A1082    16327  11384   8245   -654  -2783   3152       N  
ATOM   2060  CA  GLY A1082     -49.752   6.337 -58.621  1.00 95.06           C  
ANISOU 2060  CA  GLY A1082    16193  11489   8435   -479  -3311   3278       C  
ATOM   2061  C   GLY A1082     -49.991   5.017 -59.326  1.00 93.80           C  
ANISOU 2061  C   GLY A1082    16013  11607   8020   -599  -3462   3068       C  
ATOM   2062  O   GLY A1082     -51.129   4.695 -59.661  1.00 94.62           O  
ANISOU 2062  O   GLY A1082    15937  11781   8231   -508  -3907   3137       O  
ATOM   2063  N   LYS A1083     -48.927   4.251 -59.555  1.00 80.39           N  
ANISOU 2063  N   LYS A1083    14490  10040   6017   -802  -3087   2814       N  
ATOM   2064  CA  LYS A1083     -49.053   2.969 -60.241  1.00 81.16           C  
ANISOU 2064  CA  LYS A1083    14638  10331   5867   -923  -3175   2599       C  
ATOM   2065  C   LYS A1083     -49.630   1.925 -59.296  1.00 85.20           C  
ANISOU 2065  C   LYS A1083    14717  10991   6665   -899  -3298   2386       C  
ATOM   2066  O   LYS A1083     -48.903   1.091 -58.756  1.00 81.99           O  
ANISOU 2066  O   LYS A1083    14226  10688   6240   -991  -2976   2133       O  
ATOM   2067  CB  LYS A1083     -47.701   2.504 -60.786  1.00 80.68           C  
ANISOU 2067  CB  LYS A1083    14893  10317   5443  -1107  -2694   2414       C  
ATOM   2068  N   VAL A1084     -50.944   1.976 -59.110  1.00 79.11           N  
ANISOU 2068  N   VAL A1084    13650  10225   6181   -769  -3760   2509       N  
ATOM   2069  CA  VAL A1084     -51.624   1.142 -58.125  1.00 81.19           C  
ANISOU 2069  CA  VAL A1084    13450  10606   6791   -734  -3890   2359       C  
ATOM   2070  C   VAL A1084     -51.570  -0.346 -58.467  1.00 79.89           C  
ANISOU 2070  C   VAL A1084    13315  10596   6443   -913  -3873   2078       C  
ATOM   2071  O   VAL A1084     -51.192  -1.164 -57.626  1.00 76.07           O  
ANISOU 2071  O   VAL A1084    12642  10198   6064   -963  -3638   1861       O  
ATOM   2072  CB  VAL A1084     -53.095   1.574 -57.968  1.00 79.20           C  
ANISOU 2072  CB  VAL A1084    12834  10315   6942   -549  -4388   2582       C  
ATOM   2073  CG1 VAL A1084     -53.914   0.492 -57.271  1.00 81.84           C  
ANISOU 2073  CG1 VAL A1084    12706  10796   7593   -571  -4557   2418       C  
ATOM   2074  CG2 VAL A1084     -53.174   2.886 -57.218  1.00 80.90           C  
ANISOU 2074  CG2 VAL A1084    12921  10336   7481   -326  -4347   2822       C  
ATOM   2075  N   LYS A1085     -51.949  -0.694 -59.695  1.00 86.00           N  
ANISOU 2075  N   LYS A1085    14351  11388   6937  -1012  -4129   2092       N  
ATOM   2076  CA  LYS A1085     -51.940  -2.088 -60.133  1.00 91.05           C  
ANISOU 2076  CA  LYS A1085    15095  12118   7380  -1196  -4138   1833       C  
ATOM   2077  C   LYS A1085     -50.553  -2.684 -59.954  1.00 90.51           C  
ANISOU 2077  C   LYS A1085    15233  12061   7095  -1287  -3589   1597       C  
ATOM   2078  O   LYS A1085     -50.405  -3.834 -59.542  1.00 74.94           O  
ANISOU 2078  O   LYS A1085    13158  10147   5170  -1367  -3464   1365       O  
ATOM   2079  CB  LYS A1085     -52.380  -2.206 -61.597  1.00 87.20           C  
ANISOU 2079  CB  LYS A1085    14981  11624   6529  -1313  -4467   1896       C  
ATOM   2080  N   GLU A1086     -49.542  -1.877 -60.255  1.00 89.88           N  
ANISOU 2080  N   GLU A1086    15428  11913   6808  -1271  -3259   1678       N  
ATOM   2081  CA  GLU A1086     -48.155  -2.305 -60.173  1.00 84.60           C  
ANISOU 2081  CA  GLU A1086    14928  11253   5962  -1344  -2718   1493       C  
ATOM   2082  C   GLU A1086     -47.721  -2.473 -58.718  1.00 77.46           C  
ANISOU 2082  C   GLU A1086    13641  10406   5385  -1278  -2459   1396       C  
ATOM   2083  O   GLU A1086     -46.895  -3.329 -58.404  1.00 67.73           O  
ANISOU 2083  O   GLU A1086    12395   9226   4115  -1330  -2118   1193       O  
ATOM   2084  CB  GLU A1086     -47.252  -1.298 -60.894  1.00 80.13           C  
ANISOU 2084  CB  GLU A1086    14718  10597   5130  -1361  -2448   1638       C  
ATOM   2085  CG  GLU A1086     -45.766  -1.643 -60.893  1.00 75.28           C  
ANISOU 2085  CG  GLU A1086    14244   9993   4367  -1435  -1865   1477       C  
ATOM   2086  CD  GLU A1086     -44.996  -0.881 -61.958  1.00 88.10           C  
ANISOU 2086  CD  GLU A1086    16289  11528   5658  -1502  -1628   1605       C  
ATOM   2087  OE1 GLU A1086     -45.583   0.033 -62.577  1.00 91.26           O  
ANISOU 2087  OE1 GLU A1086    16873  11851   5952  -1480  -1913   1843       O  
ATOM   2088  OE2 GLU A1086     -43.801  -1.184 -62.168  1.00 90.91           O  
ANISOU 2088  OE2 GLU A1086    16779  11888   5874  -1571  -1148   1487       O  
ATOM   2089  N   ALA A1087     -48.294  -1.658 -57.835  1.00 79.34           N  
ANISOU 2089  N   ALA A1087    13580  10628   5938  -1158  -2628   1551       N  
ATOM   2090  CA  ALA A1087     -47.951  -1.685 -56.415  1.00 75.40           C  
ANISOU 2090  CA  ALA A1087    12745  10186   5719  -1108  -2417   1481       C  
ATOM   2091  C   ALA A1087     -48.555  -2.895 -55.705  1.00 68.73           C  
ANISOU 2091  C   ALA A1087    11586   9452   5077  -1119  -2542   1315       C  
ATOM   2092  O   ALA A1087     -47.914  -3.508 -54.851  1.00 59.86           O  
ANISOU 2092  O   ALA A1087    10309   8409   4027  -1141  -2261   1168       O  
ATOM   2093  CB  ALA A1087     -48.404  -0.399 -55.742  1.00 71.66           C  
ANISOU 2093  CB  ALA A1087    12116   9622   5489   -985  -2560   1705       C  
ATOM   2094  N   GLN A1088     -49.793  -3.225 -56.064  1.00 77.74           N  
ANISOU 2094  N   GLN A1088    12623  10595   6320  -1115  -2971   1357       N  
ATOM   2095  CA  GLN A1088     -50.493  -4.377 -55.505  1.00 61.98           C  
ANISOU 2095  CA  GLN A1088    10337   8679   4534  -1162  -3124   1221       C  
ATOM   2096  C   GLN A1088     -49.728  -5.676 -55.744  1.00 65.89           C  
ANISOU 2096  C   GLN A1088    11031   9196   4807  -1295  -2859    975       C  
ATOM   2097  O   GLN A1088     -49.709  -6.561 -54.889  1.00 65.63           O  
ANISOU 2097  O   GLN A1088    10781   9220   4933  -1325  -2765    850       O  
ATOM   2098  CB  GLN A1088     -51.897  -4.488 -56.103  1.00 66.42           C  
ANISOU 2098  CB  GLN A1088    10786   9229   5221  -1178  -3638   1316       C  
ATOM   2099  CG  GLN A1088     -52.824  -3.337 -55.751  1.00 67.43           C  
ANISOU 2099  CG  GLN A1088    10618   9323   5678  -1006  -3932   1575       C  
ATOM   2100  CD  GLN A1088     -54.136  -3.396 -56.511  1.00 90.24           C  
ANISOU 2100  CD  GLN A1088    13393  12208   8685  -1017  -4442   1695       C  
ATOM   2101  OE1 GLN A1088     -54.162  -3.273 -57.737  1.00103.83           O  
ANISOU 2101  OE1 GLN A1088    15466  13895  10090  -1087  -4611   1745       O  
ATOM   2102  NE2 GLN A1088     -55.232  -3.587 -55.787  1.00 72.91           N  
ANISOU 2102  NE2 GLN A1088    10688  10057   6956   -957  -4685   1749       N  
ATOM   2103  N   ALA A1089     -49.105  -5.785 -56.914  1.00 73.72           N  
ANISOU 2103  N   ALA A1089    12450  10129   5431  -1371  -2734    922       N  
ATOM   2104  CA  ALA A1089     -48.333  -6.971 -57.264  1.00 71.15           C  
ANISOU 2104  CA  ALA A1089    12370   9784   4880  -1478  -2456    695       C  
ATOM   2105  C   ALA A1089     -47.097  -7.082 -56.385  1.00 68.49           C  
ANISOU 2105  C   ALA A1089    11931   9493   4600  -1419  -1974    624       C  
ATOM   2106  O   ALA A1089     -46.679  -8.179 -56.014  1.00 72.15           O  
ANISOU 2106  O   ALA A1089    12383   9964   5065  -1458  -1779    458       O  
ATOM   2107  CB  ALA A1089     -47.940  -6.936 -58.730  1.00 73.88           C  
ANISOU 2107  CB  ALA A1089    13210  10050   4811  -1565  -2404    670       C  
ATOM   2108  N   ALA A1090     -46.518  -5.933 -56.056  1.00 68.97           N  
ANISOU 2108  N   ALA A1090    11924   9574   4707  -1337  -1797    761       N  
ATOM   2109  CA  ALA A1090     -45.351  -5.878 -55.188  1.00 67.08           C  
ANISOU 2109  CA  ALA A1090    11542   9400   4547  -1300  -1377    722       C  
ATOM   2110  C   ALA A1090     -45.719  -6.309 -53.777  1.00 69.13           C  
ANISOU 2110  C   ALA A1090    11403   9761   5103  -1262  -1435    694       C  
ATOM   2111  O   ALA A1090     -44.937  -6.970 -53.092  1.00 65.82           O  
ANISOU 2111  O   ALA A1090    10870   9414   4723  -1264  -1152    603       O  
ATOM   2112  CB  ALA A1090     -44.764  -4.477 -55.179  1.00 68.45           C  
ANISOU 2112  CB  ALA A1090    11747   9550   4708  -1272  -1227    881       C  
ATOM   2113  N   ALA A1091     -46.919  -5.928 -53.353  1.00 71.14           N  
ANISOU 2113  N   ALA A1091    11437  10025   5568  -1227  -1801    792       N  
ATOM   2114  CA  ALA A1091     -47.413  -6.252 -52.021  1.00 63.36           C  
ANISOU 2114  CA  ALA A1091    10065   9142   4867  -1202  -1870    789       C  
ATOM   2115  C   ALA A1091     -47.667  -7.747 -51.877  1.00 61.47           C  
ANISOU 2115  C   ALA A1091     9780   8920   4655  -1280  -1900    645       C  
ATOM   2116  O   ALA A1091     -47.566  -8.302 -50.785  1.00 68.25           O  
ANISOU 2116  O   ALA A1091    10317   9835   5782  -1224  -1720    591       O  
ATOM   2117  CB  ALA A1091     -48.678  -5.467 -51.723  1.00 58.77           C  
ANISOU 2117  CB  ALA A1091     9245   8544   4540  -1131  -2230    941       C  
ATOM   2118  N   GLU A1092     -48.001  -8.396 -52.986  1.00 57.80           N  
ANISOU 2118  N   GLU A1092     9593   8356   4014  -1367  -2057    560       N  
ATOM   2119  CA  GLU A1092     -48.199  -9.838 -52.990  1.00 69.54           C  
ANISOU 2119  CA  GLU A1092    11141   9805   5478  -1486  -2089    402       C  
ATOM   2120  C   GLU A1092     -46.865 -10.550 -52.797  1.00 76.20           C  
ANISOU 2120  C   GLU A1092    12131  10638   6186  -1464  -1623    279       C  
ATOM   2121  O   GLU A1092     -46.819 -11.693 -52.343  1.00 71.13           O  
ANISOU 2121  O   GLU A1092    11387   9940   5697  -1470  -1496    168       O  
ATOM   2122  CB  GLU A1092     -48.863 -10.291 -54.296  1.00 73.34           C  
ANISOU 2122  CB  GLU A1092    11920  10162   5782  -1608  -2369    322       C  
ATOM   2123  N   GLN A1093     -45.783  -9.862 -53.145  1.00 85.11           N  
ANISOU 2123  N   GLN A1093    13423  11786   7128  -1404  -1324    311       N  
ATOM   2124  CA  GLN A1093     -44.442 -10.416 -53.014  1.00 82.19           C  
ANISOU 2124  CA  GLN A1093    13116  11412   6700  -1349   -847    223       C  
ATOM   2125  C   GLN A1093     -43.947 -10.304 -51.575  1.00 77.99           C  
ANISOU 2125  C   GLN A1093    12087  11002   6544  -1212   -647    294       C  
ATOM   2126  O   GLN A1093     -43.012 -11.000 -51.174  1.00 76.43           O  
ANISOU 2126  O   GLN A1093    11785  10808   6447  -1131   -319    247       O  
ATOM   2127  CB  GLN A1093     -43.476  -9.709 -53.966  1.00 84.92           C  
ANISOU 2127  CB  GLN A1093    13752  11729   6786  -1343   -579    242       C  
ATOM   2128  N   LEU A1094     -44.581  -9.424 -50.805  1.00 70.99           N  
ANISOU 2128  N   LEU A1094    10909  10205   5859  -1182   -850    410       N  
ATOM   2129  CA  LEU A1094     -44.279  -9.278 -49.385  1.00 58.74           C  
ANISOU 2129  CA  LEU A1094     8939   8774   4604  -1085   -716    463       C  
ATOM   2130  C   LEU A1094     -44.561 -10.577 -48.641  1.00 65.57           C  
ANISOU 2130  C   LEU A1094     9614   9626   5674  -1049   -688    417       C  
ATOM   2131  O   LEU A1094     -43.933 -10.875 -47.626  1.00 75.85           O  
ANISOU 2131  O   LEU A1094    10669  11014   7138   -966   -498    453       O  
ATOM   2132  CB  LEU A1094     -45.101  -8.144 -48.771  1.00 51.27           C  
ANISOU 2132  CB  LEU A1094     7788   7879   3814  -1064   -925    559       C  
ATOM   2133  CG  LEU A1094     -44.808  -6.715 -49.223  1.00 56.66           C  
ANISOU 2133  CG  LEU A1094     8610   8543   4373  -1079   -930    639       C  
ATOM   2134  CD1 LEU A1094     -45.895  -5.774 -48.738  1.00 59.38           C  
ANISOU 2134  CD1 LEU A1094     8783   8864   4914  -1027  -1161    721       C  
ATOM   2135  CD2 LEU A1094     -43.464  -6.270 -48.696  1.00 51.63           C  
ANISOU 2135  CD2 LEU A1094     7877   7992   3748  -1077   -614    641       C  
ATOM   2136  N   LYS A1095     -45.516 -11.343 -49.156  1.00 57.53           N  
ANISOU 2136  N   LYS A1095     8724   8490   4644  -1131   -903    351       N  
ATOM   2137  CA  LYS A1095     -45.936 -12.584 -48.522  1.00 52.27           C  
ANISOU 2137  CA  LYS A1095     7908   7761   4191  -1134   -890    317       C  
ATOM   2138  C   LYS A1095     -44.819 -13.619 -48.504  1.00 55.32           C  
ANISOU 2138  C   LYS A1095     8387   8068   4563  -1057   -557    257       C  
ATOM   2139  O   LYS A1095     -44.713 -14.408 -47.566  1.00 55.09           O  
ANISOU 2139  O   LYS A1095     8149   8030   4753   -987   -442    306       O  
ATOM   2140  CB  LYS A1095     -47.167 -13.148 -49.231  1.00 46.21           C  
ANISOU 2140  CB  LYS A1095     7280   6862   3415  -1291  -1215    243       C  
ATOM   2141  CG  LYS A1095     -48.415 -12.313 -49.024  1.00 51.98           C  
ANISOU 2141  CG  LYS A1095     7778   7668   4305  -1329  -1552    342       C  
ATOM   2142  CD  LYS A1095     -49.611 -12.919 -49.726  1.00 61.65           C  
ANISOU 2142  CD  LYS A1095     9078   8783   5565  -1511  -1923    286       C  
ATOM   2143  CE  LYS A1095     -50.866 -12.108 -49.462  1.00 57.94           C  
ANISOU 2143  CE  LYS A1095     8276   8391   5347  -1513  -2244    418       C  
ATOM   2144  NZ  LYS A1095     -52.025 -12.631 -50.231  1.00 58.95           N  
ANISOU 2144  NZ  LYS A1095     8433   8437   5529  -1716  -2679    384       N  
ATOM   2145  N   THR A1096     -43.984 -13.613 -49.537  1.00 60.06           N  
ANISOU 2145  N   THR A1096     9306   8600   4915  -1058   -380    170       N  
ATOM   2146  CA  THR A1096     -42.863 -14.541 -49.604  1.00 59.16           C  
ANISOU 2146  CA  THR A1096     9262   8388   4829   -945     -9    116       C  
ATOM   2147  C   THR A1096     -41.904 -14.288 -48.441  1.00 53.81           C  
ANISOU 2147  C   THR A1096     8188   7883   4374   -785    190    270       C  
ATOM   2148  O   THR A1096     -41.423 -15.228 -47.808  1.00 51.63           O  
ANISOU 2148  O   THR A1096     7759   7557   4301   -660    360    316       O  
ATOM   2149  CB  THR A1096     -42.110 -14.430 -50.944  1.00 49.14           C  
ANISOU 2149  CB  THR A1096     8405   7024   3241   -970    216     -6       C  
ATOM   2150  N   THR A1097     -41.642 -13.014 -48.158  1.00 50.44           N  
ANISOU 2150  N   THR A1097     7609   7645   3910   -800    141    357       N  
ATOM   2151  CA  THR A1097     -40.831 -12.633 -47.004  1.00 47.15           C  
ANISOU 2151  CA  THR A1097     6824   7418   3672   -708    241    491       C  
ATOM   2152  C   THR A1097     -41.514 -13.046 -45.705  1.00 51.63           C  
ANISOU 2152  C   THR A1097     7139   8048   4433   -678     88    578       C  
ATOM   2153  O   THR A1097     -40.866 -13.546 -44.787  1.00 52.61           O  
ANISOU 2153  O   THR A1097     7034   8247   4707   -573    188    686       O  
ATOM   2154  CB  THR A1097     -40.557 -11.115 -46.972  1.00 42.85           C  
ANISOU 2154  CB  THR A1097     6218   7022   3039   -784    191    535       C  
ATOM   2155  OG1 THR A1097     -39.917 -10.715 -48.190  1.00 45.16           O  
ANISOU 2155  OG1 THR A1097     6769   7251   3138   -828    369    483       O  
ATOM   2156  CG2 THR A1097     -39.666 -10.755 -45.793  1.00 40.06           C  
ANISOU 2156  CG2 THR A1097     5510   6866   2847   -738    259    645       C  
ATOM   2157  N   ARG A1098     -42.827 -12.837 -45.637  1.00 56.59           N  
ANISOU 2157  N   ARG A1098     7801   8643   5058   -770   -152    551       N  
ATOM   2158  CA  ARG A1098     -43.614 -13.219 -44.466  1.00 55.04           C  
ANISOU 2158  CA  ARG A1098     7389   8489   5036   -763   -247    630       C  
ATOM   2159  C   ARG A1098     -43.568 -14.723 -44.212  1.00 52.55           C  
ANISOU 2159  C   ARG A1098     7078   8029   4858   -707   -142    660       C  
ATOM   2160  O   ARG A1098     -43.442 -15.165 -43.069  1.00 47.28           O  
ANISOU 2160  O   ARG A1098     6220   7429   4315   -639    -89    793       O  
ATOM   2161  CB  ARG A1098     -45.070 -12.773 -44.626  1.00 38.78           C  
ANISOU 2161  CB  ARG A1098     5335   6393   3008   -868   -488    595       C  
ATOM   2162  CG  ARG A1098     -45.962 -13.137 -43.443  1.00 38.48           C  
ANISOU 2162  CG  ARG A1098     5063   6389   3167   -873   -520    676       C  
ATOM   2163  CD  ARG A1098     -47.431 -13.129 -43.834  1.00 42.92           C  
ANISOU 2163  CD  ARG A1098     5596   6860   3850   -980   -737    639       C  
ATOM   2164  NE  ARG A1098     -47.702 -14.077 -44.911  1.00 54.86           N  
ANISOU 2164  NE  ARG A1098     7323   8181   5339  -1078   -840    546       N  
ATOM   2165  CZ  ARG A1098     -48.885 -14.227 -45.499  1.00 65.58           C  
ANISOU 2165  CZ  ARG A1098     8685   9446   6788  -1214  -1096    502       C  
ATOM   2166  NH1 ARG A1098     -49.916 -13.489 -45.116  1.00 73.72           N  
ANISOU 2166  NH1 ARG A1098     9463  10556   7991  -1228  -1246    567       N  
ATOM   2167  NH2 ARG A1098     -49.033 -15.115 -46.474  1.00 67.05           N  
ANISOU 2167  NH2 ARG A1098     9122   9451   6902  -1339  -1202    386       N  
ATOM   2168  N   ASN A1099     -43.679 -15.506 -45.281  1.00 52.81           N  
ANISOU 2168  N   ASN A1099     7373   7844   4847   -744   -111    538       N  
ATOM   2169  CA  ASN A1099     -43.687 -16.959 -45.167  1.00 60.52           C  
ANISOU 2169  CA  ASN A1099     8416   8606   5973   -703      6    539       C  
ATOM   2170  C   ASN A1099     -42.323 -17.524 -44.792  1.00 60.70           C  
ANISOU 2170  C   ASN A1099     8351   8621   6090   -497    281    640       C  
ATOM   2171  O   ASN A1099     -42.230 -18.559 -44.134  1.00 67.20           O  
ANISOU 2171  O   ASN A1099     9105   9328   7101   -405    372    750       O  
ATOM   2172  CB  ASN A1099     -44.155 -17.597 -46.478  1.00 68.36           C  
ANISOU 2172  CB  ASN A1099     9775   9338   6860   -828    -36    335       C  
ATOM   2173  CG  ASN A1099     -45.567 -17.195 -46.857  1.00 68.89           C  
ANISOU 2173  CG  ASN A1099     9881   9405   6887  -1038   -376    267       C  
ATOM   2174  OD1 ASN A1099     -46.351 -16.761 -46.014  1.00 59.95           O  
ANISOU 2174  OD1 ASN A1099     8472   8406   5900  -1073   -523    377       O  
ATOM   2175  ND2 ASN A1099     -45.895 -17.335 -48.135  1.00 78.51           N  
ANISOU 2175  ND2 ASN A1099    11447  10477   7905  -1179   -502     88       N  
ATOM   2176  N   ALA A1100     -41.265 -16.838 -45.211  1.00 57.92           N  
ANISOU 2176  N   ALA A1100     7983   8387   5638   -424    413    628       N  
ATOM   2177  CA  ALA A1100     -39.913 -17.359 -45.054  1.00 68.76           C  
ANISOU 2177  CA  ALA A1100     9230   9746   7149   -218    685    721       C  
ATOM   2178  C   ALA A1100     -39.290 -16.990 -43.711  1.00 68.94           C  
ANISOU 2178  C   ALA A1100     8867  10032   7294   -125    622    953       C  
ATOM   2179  O   ALA A1100     -38.790 -17.855 -42.993  1.00 74.45           O  
ANISOU 2179  O   ALA A1100     9407  10693   8187     38    697   1124       O  
ATOM   2180  CB  ALA A1100     -39.032 -16.867 -46.191  1.00 81.04           C  
ANISOU 2180  CB  ALA A1100    10928  11293   8572   -200    903    603       C  
ATOM   2181  N   TYR A1101     -39.321 -15.705 -43.376  1.00 61.30           N  
ANISOU 2181  N   TYR A1101     7777   9315   6200   -236    471    963       N  
ATOM   2182  CA  TYR A1101     -38.615 -15.211 -42.201  1.00 62.39           C  
ANISOU 2182  CA  TYR A1101     7597   9717   6390   -197    391   1139       C  
ATOM   2183  C   TYR A1101     -39.534 -14.933 -41.015  1.00 65.69           C  
ANISOU 2183  C   TYR A1101     7953  10260   6745   -286    177   1211       C  
ATOM   2184  O   TYR A1101     -39.305 -15.428 -39.910  1.00 63.22           O  
ANISOU 2184  O   TYR A1101     7489  10039   6493   -212    127   1396       O  
ATOM   2185  CB  TYR A1101     -37.850 -13.930 -42.543  1.00 42.31           C  
ANISOU 2185  CB  TYR A1101     4966   7351   3759   -282    406   1091       C  
ATOM   2186  CG  TYR A1101     -36.744 -14.093 -43.561  1.00 44.35           C  
ANISOU 2186  CG  TYR A1101     5221   7534   4094   -194    683   1056       C  
ATOM   2187  CD1 TYR A1101     -37.006 -14.009 -44.922  1.00 44.72           C  
ANISOU 2187  CD1 TYR A1101     5594   7400   3999   -248    835    878       C  
ATOM   2188  CD2 TYR A1101     -35.433 -14.308 -43.159  1.00 76.19           C  
ANISOU 2188  CD2 TYR A1101     8922  11688   8340    -63    795   1213       C  
ATOM   2189  CE1 TYR A1101     -35.994 -14.147 -45.855  1.00 51.69           C  
ANISOU 2189  CE1 TYR A1101     6510   8207   4922   -172   1161    836       C  
ATOM   2190  CE2 TYR A1101     -34.413 -14.448 -44.086  1.00 68.52           C  
ANISOU 2190  CE2 TYR A1101     7903  10644   7486     31   1116   1185       C  
ATOM   2191  CZ  TYR A1101     -34.699 -14.366 -45.431  1.00 57.16           C  
ANISOU 2191  CZ  TYR A1101     6831   9010   5876    -25   1331    987       C  
ATOM   2192  OH  TYR A1101     -33.688 -14.505 -46.354  1.00 60.37           O  
ANISOU 2192  OH  TYR A1101     7228   9337   6372     66   1720    951       O  
ATOM   2193  N   ILE A1102     -40.569 -14.134 -41.254  1.00 58.05           N  
ANISOU 2193  N   ILE A1102     7111   9291   5653   -434     66   1078       N  
ATOM   2194  CA  ILE A1102     -41.371 -13.562 -40.176  1.00 51.65           C  
ANISOU 2194  CA  ILE A1102     6232   8615   4777   -519    -70   1112       C  
ATOM   2195  C   ILE A1102     -42.136 -14.598 -39.355  1.00 59.82           C  
ANISOU 2195  C   ILE A1102     7254   9579   5895   -491    -68   1228       C  
ATOM   2196  O   ILE A1102     -42.183 -14.510 -38.128  1.00 60.35           O  
ANISOU 2196  O   ILE A1102     7229   9798   5902   -497   -104   1350       O  
ATOM   2197  CB  ILE A1102     -42.378 -12.541 -40.727  1.00 37.26           C  
ANISOU 2197  CB  ILE A1102     4522   6755   2879   -640   -160    958       C  
ATOM   2198  CG1 ILE A1102     -41.675 -11.567 -41.673  1.00 41.84           C  
ANISOU 2198  CG1 ILE A1102     5176   7353   3367   -679   -140    867       C  
ATOM   2199  CG2 ILE A1102     -43.058 -11.796 -39.590  1.00 36.72           C  
ANISOU 2199  CG2 ILE A1102     4372   6819   2763   -700   -224    973       C  
ATOM   2200  CD1 ILE A1102     -40.524 -10.828 -41.030  1.00 52.71           C  
ANISOU 2200  CD1 ILE A1102     6396   8930   4703   -699   -122    919       C  
ATOM   2201  N   GLN A1103     -42.737 -15.570 -40.033  1.00 59.92           N  
ANISOU 2201  N   GLN A1103     7391   9351   6026   -486    -20   1187       N  
ATOM   2202  CA  GLN A1103     -43.530 -16.588 -39.355  1.00 55.56           C  
ANISOU 2202  CA  GLN A1103     6837   8682   5591   -495      6   1299       C  
ATOM   2203  C   GLN A1103     -42.673 -17.398 -38.388  1.00 54.25           C  
ANISOU 2203  C   GLN A1103     6586   8559   5468   -353     75   1538       C  
ATOM   2204  O   GLN A1103     -43.104 -17.720 -37.282  1.00 62.14           O  
ANISOU 2204  O   GLN A1103     7546   9612   6451   -370     76   1700       O  
ATOM   2205  CB  GLN A1103     -44.199 -17.514 -40.373  1.00 62.36           C  
ANISOU 2205  CB  GLN A1103     7868   9243   6585   -551     29   1187       C  
ATOM   2206  N   LYS A1104     -41.452 -17.715 -38.805  1.00 51.43           N  
ANISOU 2206  N   LYS A1104     6193   8178   5169   -206    141   1581       N  
ATOM   2207  CA  LYS A1104     -40.548 -18.491 -37.967  1.00 59.33           C  
ANISOU 2207  CA  LYS A1104     7072   9213   6259    -32    169   1847       C  
ATOM   2208  C   LYS A1104     -39.955 -17.636 -36.853  1.00 61.29           C  
ANISOU 2208  C   LYS A1104     7142   9812   6334    -51     11   1982       C  
ATOM   2209  O   LYS A1104     -39.640 -18.139 -35.778  1.00 65.38           O  
ANISOU 2209  O   LYS A1104     7592  10419   6831     26    -56   2238       O  
ATOM   2210  CB  LYS A1104     -39.431 -19.110 -38.808  1.00 73.39           C  
ANISOU 2210  CB  LYS A1104     8822  10838   8225    161    321   1852       C  
ATOM   2211  CG  LYS A1104     -39.928 -20.069 -39.877  1.00 85.79           C  
ANISOU 2211  CG  LYS A1104    10641  12024   9931    172    494   1696       C  
ATOM   2212  CD  LYS A1104     -38.773 -20.678 -40.650  1.00102.42           C  
ANISOU 2212  CD  LYS A1104    12741  13956  12219    392    722   1688       C  
ATOM   2213  CE  LYS A1104     -39.265 -21.621 -41.736  1.00111.57           C  
ANISOU 2213  CE  LYS A1104    14229  14702  13460    376    911   1481       C  
ATOM   2214  NZ  LYS A1104     -38.130 -22.217 -42.495  1.00121.47           N  
ANISOU 2214  NZ  LYS A1104    15508  15754  14891    614   1214   1448       N  
ATOM   2215  N   TYR A1105     -39.810 -16.343 -37.117  1.00 61.84           N  
ANISOU 2215  N   TYR A1105     7171  10064   6262   -169    -63   1812       N  
ATOM   2216  CA  TYR A1105     -39.255 -15.408 -36.143  1.00 54.94           C  
ANISOU 2216  CA  TYR A1105     6170   9501   5202   -243   -226   1876       C  
ATOM   2217  C   TYR A1105     -40.150 -15.259 -34.916  1.00 50.29           C  
ANISOU 2217  C   TYR A1105     5680   9017   4411   -347   -288   1938       C  
ATOM   2218  O   TYR A1105     -39.667 -15.236 -33.782  1.00 46.90           O  
ANISOU 2218  O   TYR A1105     5204   8793   3821   -353   -418   2114       O  
ATOM   2219  CB  TYR A1105     -39.034 -14.042 -36.795  1.00 52.12           C  
ANISOU 2219  CB  TYR A1105     5801   9239   4764   -374   -252   1653       C  
ATOM   2220  CG  TYR A1105     -38.715 -12.930 -35.824  1.00 42.71           C  
ANISOU 2220  CG  TYR A1105     4552   8317   3359   -520   -416   1641       C  
ATOM   2221  CD1 TYR A1105     -37.404 -12.666 -35.445  1.00 44.95           C  
ANISOU 2221  CD1 TYR A1105     4623   8810   3648   -527   -551   1751       C  
ATOM   2222  CD2 TYR A1105     -39.723 -12.134 -35.294  1.00 49.32           C  
ANISOU 2222  CD2 TYR A1105     5543   9187   4011   -658   -431   1509       C  
ATOM   2223  CE1 TYR A1105     -37.110 -11.647 -34.561  1.00 49.93           C  
ANISOU 2223  CE1 TYR A1105     5238   9674   4060   -709   -733   1709       C  
ATOM   2224  CE2 TYR A1105     -39.438 -11.116 -34.407  1.00 46.76           C  
ANISOU 2224  CE2 TYR A1105     5232   9070   3467   -806   -554   1456       C  
ATOM   2225  CZ  TYR A1105     -38.131 -10.877 -34.046  1.00 48.94           C  
ANISOU 2225  CZ  TYR A1105     5339   9549   3708   -851   -723   1545       C  
ATOM   2226  OH  TYR A1105     -37.846  -9.861 -33.168  1.00 47.15           O  
ANISOU 2226  OH  TYR A1105     5161   9514   3240  -1046   -876   1462       O  
ATOM   2227  N   LEU A1106     -41.453 -15.142 -35.153  1.00 49.61           N  
ANISOU 2227  N   LEU A1106     5728   8795   4327   -435   -193   1796       N  
ATOM   2228  CA  LEU A1106     -42.417 -14.934 -34.079  1.00 50.26           C  
ANISOU 2228  CA  LEU A1106     5896   8952   4247   -533   -162   1825       C  
ATOM   2229  C   LEU A1106     -42.429 -16.085 -33.079  1.00 54.97           C  
ANISOU 2229  C   LEU A1106     6533   9538   4813   -468   -131   2112       C  
ATOM   2230  O   LEU A1106     -42.454 -15.861 -31.870  1.00 62.59           O  
ANISOU 2230  O   LEU A1106     7569  10691   5523   -525   -165   2224       O  
ATOM   2231  CB  LEU A1106     -43.819 -14.737 -34.654  1.00 51.11           C  
ANISOU 2231  CB  LEU A1106     6058   8889   4474   -613    -51   1651       C  
ATOM   2232  CG  LEU A1106     -44.024 -13.489 -35.511  1.00 52.84           C  
ANISOU 2232  CG  LEU A1106     6272   9109   4694   -676    -96   1405       C  
ATOM   2233  CD1 LEU A1106     -45.489 -13.346 -35.865  1.00 60.73           C  
ANISOU 2233  CD1 LEU A1106     7274   9965   5837   -736    -30   1298       C  
ATOM   2234  CD2 LEU A1106     -43.519 -12.249 -34.788  1.00 51.71           C  
ANISOU 2234  CD2 LEU A1106     6142   9185   4321   -744   -154   1336       C  
ATOM   2235  N   VAL A 313     -42.414 -17.314 -33.583  1.00 66.94           N  
ANISOU 2235  N   VAL A 313     8772  11447   5214   1469   -942   1942       N  
ATOM   2236  CA  VAL A 313     -42.401 -18.481 -32.710  1.00 57.28           C  
ANISOU 2236  CA  VAL A 313     7663   9992   4110   1376   -946   1595       C  
ATOM   2237  C   VAL A 313     -41.013 -18.674 -32.112  1.00 67.54           C  
ANISOU 2237  C   VAL A 313     9048  11184   5428   1319   -834   1630       C  
ATOM   2238  O   VAL A 313     -40.865 -19.270 -31.048  1.00 79.72           O  
ANISOU 2238  O   VAL A 313    10708  12433   7150   1203   -806   1453       O  
ATOM   2239  CB  VAL A 313     -42.833 -19.766 -33.453  1.00 67.83           C  
ANISOU 2239  CB  VAL A 313     8974  11549   5247   1478  -1074   1249       C  
ATOM   2240  CG1 VAL A 313     -44.193 -19.569 -34.109  1.00 60.05           C  
ANISOU 2240  CG1 VAL A 313     7884  10704   4227   1542  -1195   1207       C  
ATOM   2241  CG2 VAL A 313     -41.796 -20.169 -34.491  1.00 71.59           C  
ANISOU 2241  CG2 VAL A 313     9400  12411   5390   1637  -1075   1243       C  
ATOM   2242  N   GLN A 314     -39.998 -18.154 -32.794  1.00 62.58           N  
ANISOU 2242  N   GLN A 314     8356  10811   4612   1399   -770   1870       N  
ATOM   2243  CA  GLN A 314     -38.628 -18.239 -32.309  1.00 60.88           C  
ANISOU 2243  CA  GLN A 314     8193  10536   4404   1355   -662   1923       C  
ATOM   2244  C   GLN A 314     -38.444 -17.367 -31.074  1.00 54.32           C  
ANISOU 2244  C   GLN A 314     7431   9318   3891   1188   -569   2099       C  
ATOM   2245  O   GLN A 314     -37.932 -17.822 -30.055  1.00 54.59           O  
ANISOU 2245  O   GLN A 314     7569   9103   4068   1093   -524   1966       O  
ATOM   2246  CB  GLN A 314     -37.643 -17.821 -33.403  1.00 64.61           C  
ANISOU 2246  CB  GLN A 314     8546  11416   4586   1471   -610   2157       C  
ATOM   2247  CG  GLN A 314     -36.180 -18.035 -33.056  1.00 65.50           C  
ANISOU 2247  CG  GLN A 314     8681  11534   4673   1445   -505   2168       C  
ATOM   2248  CD  GLN A 314     -35.249 -17.385 -34.060  1.00 72.95           C  
ANISOU 2248  CD  GLN A 314     9471  12719   5526   1458   -410   2360       C  
ATOM   2249  OE1 GLN A 314     -35.447 -16.235 -34.454  1.00 78.86           O  
ANISOU 2249  OE1 GLN A 314    10143  13460   6360   1405   -373   2645       O  
ATOM   2250  NE2 GLN A 314     -34.232 -18.123 -34.490  1.00 71.91           N  
ANISOU 2250  NE2 GLN A 314     9290  12811   5222   1535   -376   2202       N  
ATOM   2251  N   THR A 315     -38.874 -16.113 -31.175  1.00 61.65           N  
ANISOU 2251  N   THR A 315     8296  10198   4929   1161   -554   2392       N  
ATOM   2252  CA  THR A 315     -38.697 -15.141 -30.100  1.00 59.87           C  
ANISOU 2252  CA  THR A 315     8115   9624   5009   1020   -478   2567       C  
ATOM   2253  C   THR A 315     -39.394 -15.561 -28.816  1.00 57.25           C  
ANISOU 2253  C   THR A 315     7892   8931   4931    902   -489   2318       C  
ATOM   2254  O   THR A 315     -38.781 -15.597 -27.748  1.00 56.04           O  
ANISOU 2254  O   THR A 315     7822   8533   4937    794   -419   2276       O  
ATOM   2255  CB  THR A 315     -39.229 -13.758 -30.505  1.00 54.94           C  
ANISOU 2255  CB  THR A 315     7403   8991   4479   1033   -496   2896       C  
ATOM   2256  OG1 THR A 315     -38.519 -13.289 -31.656  1.00 57.17           O  
ANISOU 2256  OG1 THR A 315     7585   9605   4532   1117   -473   3176       O  
ATOM   2257  CG2 THR A 315     -39.053 -12.770 -29.361  1.00 53.71           C  
ANISOU 2257  CG2 THR A 315     7290   8453   4663    896   -434   3034       C  
ATOM   2258  N   ILE A 316     -40.678 -15.879 -28.931  1.00 54.84           N  
ANISOU 2258  N   ILE A 316     7572   8615   4650    922   -578   2155       N  
ATOM   2259  CA  ILE A 316     -41.491 -16.225 -27.774  1.00 49.98           C  
ANISOU 2259  CA  ILE A 316     7031   7696   4262    801   -585   1938       C  
ATOM   2260  C   ILE A 316     -41.002 -17.505 -27.102  1.00 48.62           C  
ANISOU 2260  C   ILE A 316     6980   7421   4071    735   -569   1673       C  
ATOM   2261  O   ILE A 316     -40.823 -17.540 -25.888  1.00 51.36           O  
ANISOU 2261  O   ILE A 316     7417   7495   4603    608   -510   1617       O  
ATOM   2262  CB  ILE A 316     -42.968 -16.377 -28.167  1.00 50.85           C  
ANISOU 2262  CB  ILE A 316     7075   7869   4378    838   -688   1810       C  
ATOM   2263  CG1 ILE A 316     -43.485 -15.058 -28.747  1.00 52.32           C  
ANISOU 2263  CG1 ILE A 316     7147   8121   4609    913   -718   2082       C  
ATOM   2264  CG2 ILE A 316     -43.800 -16.791 -26.968  1.00 49.41           C  
ANISOU 2264  CG2 ILE A 316     6953   7408   4413    697   -681   1586       C  
ATOM   2265  CD1 ILE A 316     -44.856 -15.150 -29.370  1.00 60.87           C  
ANISOU 2265  CD1 ILE A 316     8137   9338   5654    989   -835   1981       C  
ATOM   2266  N   SER A 317     -40.770 -18.546 -27.894  1.00 51.57           N  
ANISOU 2266  N   SER A 317     7356   8017   4220    830   -631   1510       N  
ATOM   2267  CA  SER A 317     -40.308 -19.824 -27.362  1.00 50.68           C  
ANISOU 2267  CA  SER A 317     7360   7800   4094    788   -644   1255       C  
ATOM   2268  C   SER A 317     -38.954 -19.702 -26.665  1.00 57.82           C  
ANISOU 2268  C   SER A 317     8338   8590   5041    745   -549   1344       C  
ATOM   2269  O   SER A 317     -38.770 -20.218 -25.560  1.00 61.23           O  
ANISOU 2269  O   SER A 317     8887   8766   5611    636   -527   1222       O  
ATOM   2270  CB  SER A 317     -40.224 -20.870 -28.475  1.00 55.25           C  
ANISOU 2270  CB  SER A 317     7910   8659   4424    931   -744   1061       C  
ATOM   2271  OG  SER A 317     -39.621 -22.062 -28.003  1.00 68.52           O  
ANISOU 2271  OG  SER A 317     9706  10224   6104    911   -769    831       O  
ATOM   2272  N   ASN A 318     -38.012 -19.020 -27.311  1.00 48.27           N  
ANISOU 2272  N   ASN A 318     7052   7581   3708    826   -494   1565       N  
ATOM   2273  CA  ASN A 318     -36.670 -18.864 -26.758  1.00 47.49           C  
ANISOU 2273  CA  ASN A 318     6993   7415   3638    792   -406   1652       C  
ATOM   2274  C   ASN A 318     -36.652 -18.077 -25.452  1.00 51.27           C  
ANISOU 2274  C   ASN A 318     7528   7561   4390    638   -333   1756       C  
ATOM   2275  O   ASN A 318     -36.026 -18.498 -24.481  1.00 55.11           O  
ANISOU 2275  O   ASN A 318     8112   7862   4963    567   -300   1662       O  
ATOM   2276  CB  ASN A 318     -35.750 -18.184 -27.771  1.00 63.59           C  
ANISOU 2276  CB  ASN A 318     8908   9763   5492    891   -355   1897       C  
ATOM   2277  CG  ASN A 318     -35.176 -19.156 -28.778  1.00 61.51           C  
ANISOU 2277  CG  ASN A 318     8603   9835   4935   1047   -400   1746       C  
ATOM   2278  OD1 ASN A 318     -35.670 -20.272 -28.933  1.00 67.30           O  
ANISOU 2278  OD1 ASN A 318     9387  10582   5601   1101   -495   1460       O  
ATOM   2279  ND2 ASN A 318     -34.117 -18.741 -29.462  1.00 65.86           N  
ANISOU 2279  ND2 ASN A 318     9049  10661   5312   1117   -333   1929       N  
ATOM   2280  N   GLU A 319     -37.335 -16.937 -25.433  1.00 46.11           N  
ANISOU 2280  N   GLU A 319     6810   6839   3872    600   -317   1940       N  
ATOM   2281  CA  GLU A 319     -37.386 -16.101 -24.239  1.00 44.90           C  
ANISOU 2281  CA  GLU A 319     6691   6384   3985    471   -258   2018       C  
ATOM   2282  C   GLU A 319     -38.113 -16.802 -23.097  1.00 58.98           C  
ANISOU 2282  C   GLU A 319     8582   7928   5900    367   -273   1773       C  
ATOM   2283  O   GLU A 319     -37.747 -16.647 -21.933  1.00 59.90           O  
ANISOU 2283  O   GLU A 319     8767   7823   6167    265   -220   1748       O  
ATOM   2284  CB  GLU A 319     -38.058 -14.763 -24.545  1.00 45.83           C  
ANISOU 2284  CB  GLU A 319     6709   6476   4229    477   -264   2243       C  
ATOM   2285  CG  GLU A 319     -37.091 -13.669 -24.949  1.00 54.63           C  
ANISOU 2285  CG  GLU A 319     7747   7650   5362    488   -211   2553       C  
ATOM   2286  CD  GLU A 319     -37.773 -12.328 -25.126  1.00 73.82           C  
ANISOU 2286  CD  GLU A 319    10096   9986   7967    487   -235   2778       C  
ATOM   2287  OE1 GLU A 319     -38.602 -12.198 -26.050  1.00 77.33           O  
ANISOU 2287  OE1 GLU A 319    10472  10595   8315    578   -303   2840       O  
ATOM   2288  OE2 GLU A 319     -37.485 -11.407 -24.334  1.00 81.99           O  
ANISOU 2288  OE2 GLU A 319    11132  10777   9243    402   -198   2882       O  
ATOM   2289  N   GLN A 320     -39.141 -17.571 -23.442  1.00 51.56           N  
ANISOU 2289  N   GLN A 320     7647   7047   4896    387   -347   1598       N  
ATOM   2290  CA  GLN A 320     -39.899 -18.338 -22.461  1.00 49.77           C  
ANISOU 2290  CA  GLN A 320     7509   6624   4775    273   -363   1378       C  
ATOM   2291  C   GLN A 320     -39.043 -19.452 -21.862  1.00 56.96           C  
ANISOU 2291  C   GLN A 320     8555   7449   5640    235   -360   1234       C  
ATOM   2292  O   GLN A 320     -39.045 -19.670 -20.650  1.00 64.51           O  
ANISOU 2292  O   GLN A 320     9602   8187   6720    114   -324   1164       O  
ATOM   2293  CB  GLN A 320     -41.156 -18.930 -23.102  1.00 52.61           C  
ANISOU 2293  CB  GLN A 320     7824   7089   5077    301   -453   1230       C  
ATOM   2294  CG  GLN A 320     -42.044 -19.708 -22.147  1.00 59.71           C  
ANISOU 2294  CG  GLN A 320     8794   7804   6090    160   -466   1022       C  
ATOM   2295  CD  GLN A 320     -42.941 -18.808 -21.324  1.00 70.40           C  
ANISOU 2295  CD  GLN A 320    10094   9017   7638     66   -416   1063       C  
ATOM   2296  OE1 GLN A 320     -43.395 -17.766 -21.796  1.00 68.85           O  
ANISOU 2296  OE1 GLN A 320     9783   8890   7487    133   -422   1192       O  
ATOM   2297  NE2 GLN A 320     -43.195 -19.203 -20.080  1.00 79.51           N  
ANISOU 2297  NE2 GLN A 320    11325   9980   8904    -83   -371    953       N  
ATOM   2298  N   ARG A 321     -38.313 -20.152 -22.726  1.00 58.33           N  
ANISOU 2298  N   ARG A 321     8732   7806   5626    350   -404   1187       N  
ATOM   2299  CA  ARG A 321     -37.455 -21.254 -22.304  1.00 48.29           C  
ANISOU 2299  CA  ARG A 321     7579   6464   4304    350   -426   1041       C  
ATOM   2300  C   ARG A 321     -36.349 -20.783 -21.368  1.00 47.10           C  
ANISOU 2300  C   ARG A 321     7478   6180   4237    298   -342   1148       C  
ATOM   2301  O   ARG A 321     -36.156 -21.347 -20.292  1.00 52.21           O  
ANISOU 2301  O   ARG A 321     8246   6624   4968    208   -340   1051       O  
ATOM   2302  CB  ARG A 321     -36.845 -21.950 -23.523  1.00 48.73           C  
ANISOU 2302  CB  ARG A 321     7597   6783   4135    517   -492    963       C  
ATOM   2303  N   ALA A 322     -35.628 -19.745 -21.783  1.00 47.79           N  
ANISOU 2303  N   ALA A 322     7467   6387   4303    348   -279   1355       N  
ATOM   2304  CA  ALA A 322     -34.538 -19.190 -20.989  1.00 40.81           C  
ANISOU 2304  CA  ALA A 322     6602   5397   3506    299   -205   1461       C  
ATOM   2305  C   ALA A 322     -35.043 -18.666 -19.650  1.00 45.50           C  
ANISOU 2305  C   ALA A 322     7252   5720   4317    152   -163   1462       C  
ATOM   2306  O   ALA A 322     -34.310 -18.639 -18.661  1.00 38.80           O  
ANISOU 2306  O   ALA A 322     6468   4731   3544     91   -127   1451       O  
ATOM   2307  CB  ALA A 322     -33.836 -18.085 -21.759  1.00 44.93           C  
ANISOU 2307  CB  ALA A 322     6988   6095   3989    356   -149   1705       C  
ATOM   2308  N   SER A 323     -36.306 -18.257 -19.627  1.00 50.35           N  
ANISOU 2308  N   SER A 323     7829   6281   5019    106   -172   1460       N  
ATOM   2309  CA  SER A 323     -36.933 -17.752 -18.415  1.00 50.77           C  
ANISOU 2309  CA  SER A 323     7911   6117   5262    -19   -132   1433       C  
ATOM   2310  C   SER A 323     -37.226 -18.886 -17.431  1.00 56.99           C  
ANISOU 2310  C   SER A 323     8834   6767   6053   -114   -150   1241       C  
ATOM   2311  O   SER A 323     -36.996 -18.753 -16.228  1.00 59.54           O  
ANISOU 2311  O   SER A 323     9219   6932   6470   -207   -106   1216       O  
ATOM   2312  CB  SER A 323     -38.220 -17.001 -18.761  1.00 46.18           C  
ANISOU 2312  CB  SER A 323     7229   5550   4768    -21   -144   1475       C  
ATOM   2313  OG  SER A 323     -38.853 -16.503 -17.599  1.00 56.20           O  
ANISOU 2313  OG  SER A 323     8505   6635   6212   -128   -105   1423       O  
ATOM   2314  N   LYS A 324     -37.723 -20.003 -17.953  1.00 58.35           N  
ANISOU 2314  N   LYS A 324     9049   7001   6121    -92   -220   1110       N  
ATOM   2315  CA  LYS A 324     -38.099 -21.141 -17.121  1.00 54.74           C  
ANISOU 2315  CA  LYS A 324     8720   6402   5676   -195   -251    950       C  
ATOM   2316  C   LYS A 324     -36.900 -21.788 -16.436  1.00 53.08           C  
ANISOU 2316  C   LYS A 324     8637   6098   5433   -199   -256    922       C  
ATOM   2317  O   LYS A 324     -36.948 -22.078 -15.241  1.00 56.19           O  
ANISOU 2317  O   LYS A 324     9127   6331   5890   -314   -235    883       O  
ATOM   2318  CB  LYS A 324     -38.843 -22.188 -17.954  1.00 39.30           C  
ANISOU 2318  CB  LYS A 324     6773   4523   3637   -166   -346    812       C  
ATOM   2319  N   VAL A 325     -35.828 -22.020 -17.186  1.00 49.09           N  
ANISOU 2319  N   VAL A 325     8124   5712   4816    -66   -287    941       N  
ATOM   2320  CA  VAL A 325     -34.668 -22.702 -16.623  1.00 48.09           C  
ANISOU 2320  CA  VAL A 325     8106   5511   4653    -43   -311    896       C  
ATOM   2321  C   VAL A 325     -33.946 -21.811 -15.620  1.00 49.18           C  
ANISOU 2321  C   VAL A 325     8242   5564   4881   -100   -229   1002       C  
ATOM   2322  O   VAL A 325     -33.457 -22.292 -14.597  1.00 47.40           O  
ANISOU 2322  O   VAL A 325     8129   5203   4677   -152   -239    957       O  
ATOM   2323  CB  VAL A 325     -33.680 -23.168 -17.717  1.00 47.15           C  
ANISOU 2323  CB  VAL A 325     7954   5578   4385    130   -364    865       C  
ATOM   2324  CG1 VAL A 325     -34.305 -24.275 -18.552  1.00 39.79           C  
ANISOU 2324  CG1 VAL A 325     7049   4702   3368    191   -471    702       C  
ATOM   2325  CG2 VAL A 325     -33.252 -22.010 -18.596  1.00 55.61           C  
ANISOU 2325  CG2 VAL A 325     8862   6858   5409    210   -298   1030       C  
ATOM   2326  N   LEU A 326     -33.900 -20.512 -15.899  1.00 46.83           N  
ANISOU 2326  N   LEU A 326     7815   5336   4642    -91   -160   1143       N  
ATOM   2327  CA  LEU A 326     -33.251 -19.572 -14.996  1.00 47.08           C  
ANISOU 2327  CA  LEU A 326     7825   5278   4784   -146    -94   1228       C  
ATOM   2328  C   LEU A 326     -34.004 -19.500 -13.671  1.00 43.80           C  
ANISOU 2328  C   LEU A 326     7479   4687   4476   -284    -67   1163       C  
ATOM   2329  O   LEU A 326     -33.405 -19.309 -12.617  1.00 43.92           O  
ANISOU 2329  O   LEU A 326     7541   4606   4540   -335    -42   1155       O  
ATOM   2330  CB  LEU A 326     -33.155 -18.186 -15.639  1.00 48.02           C  
ANISOU 2330  CB  LEU A 326     7789   5482   4974   -116    -42   1400       C  
ATOM   2331  CG  LEU A 326     -32.425 -17.108 -14.834  1.00 55.98           C  
ANISOU 2331  CG  LEU A 326     8754   6391   6124   -170     13   1487       C  
ATOM   2332  CD1 LEU A 326     -31.498 -16.302 -15.728  1.00 66.06           C  
ANISOU 2332  CD1 LEU A 326     9903   7800   7395   -105     39   1664       C  
ATOM   2333  CD2 LEU A 326     -33.420 -16.193 -14.140  1.00 57.79           C  
ANISOU 2333  CD2 LEU A 326     8949   6484   6527   -258     44   1488       C  
ATOM   2334  N   GLY A 327     -35.321 -19.662 -13.733  1.00 42.70           N  
ANISOU 2334  N   GLY A 327     7333   4530   4361   -341    -72   1109       N  
ATOM   2335  CA  GLY A 327     -36.146 -19.641 -12.542  1.00 35.69           C  
ANISOU 2335  CA  GLY A 327     6488   3521   3551   -475    -37   1041       C  
ATOM   2336  C   GLY A 327     -35.915 -20.855 -11.667  1.00 54.61           C  
ANISOU 2336  C   GLY A 327     9045   5823   5881   -545    -69    956       C  
ATOM   2337  O   GLY A 327     -35.808 -20.737 -10.449  1.00 59.45           O  
ANISOU 2337  O   GLY A 327     9712   6352   6526   -632    -32    939       O  
ATOM   2338  N   ILE A 328     -35.828 -22.024 -12.294  1.00 47.96           N  
ANISOU 2338  N   ILE A 328     8280   4996   4946   -502   -149    901       N  
ATOM   2339  CA  ILE A 328     -35.668 -23.281 -11.569  1.00 44.40           C  
ANISOU 2339  CA  ILE A 328     7995   4427   4450   -565   -206    833       C  
ATOM   2340  C   ILE A 328     -34.323 -23.364 -10.854  1.00 41.24           C  
ANISOU 2340  C   ILE A 328     7674   3974   4021   -524   -216    859       C  
ATOM   2341  O   ILE A 328     -34.256 -23.786  -9.700  1.00 53.60           O  
ANISOU 2341  O   ILE A 328     9350   5432   5582   -616   -217    850       O  
ATOM   2342  CB  ILE A 328     -35.812 -24.491 -12.512  1.00 48.36           C  
ANISOU 2342  CB  ILE A 328     8553   4937   4885   -504   -313    748       C  
ATOM   2343  CG1 ILE A 328     -37.188 -24.488 -13.176  1.00 49.44           C  
ANISOU 2343  CG1 ILE A 328     8607   5129   5049   -553   -316    704       C  
ATOM   2344  CG2 ILE A 328     -35.615 -25.794 -11.752  1.00 47.97           C  
ANISOU 2344  CG2 ILE A 328     8684   4723   4818   -571   -392    694       C  
ATOM   2345  CD1 ILE A 328     -37.324 -25.493 -14.299  1.00 53.00           C  
ANISOU 2345  CD1 ILE A 328     9077   5622   5438   -469   -430    601       C  
ATOM   2346  N   VAL A 329     -33.253 -22.962 -11.532  1.00 37.85           N  
ANISOU 2346  N   VAL A 329     7180   3639   3562   -388   -223    897       N  
ATOM   2347  CA  VAL A 329     -31.928 -23.019 -10.924  1.00 44.89           C  
ANISOU 2347  CA  VAL A 329     8124   4503   4430   -338   -239    911       C  
ATOM   2348  C   VAL A 329     -31.781 -21.973  -9.821  1.00 52.06           C  
ANISOU 2348  C   VAL A 329     8993   5369   5418   -421   -159    959       C  
ATOM   2349  O   VAL A 329     -31.110 -22.212  -8.818  1.00 58.73           O  
ANISOU 2349  O   VAL A 329     9922   6147   6245   -442   -176    945       O  
ATOM   2350  CB  VAL A 329     -30.805 -22.835 -11.968  1.00 42.59           C  
ANISOU 2350  CB  VAL A 329     7744   4356   4083   -178   -258    936       C  
ATOM   2351  CG1 VAL A 329     -30.747 -24.036 -12.898  1.00 45.92           C  
ANISOU 2351  CG1 VAL A 329     8219   4823   4407    -70   -358    842       C  
ATOM   2352  CG2 VAL A 329     -31.000 -21.555 -12.756  1.00 54.20           C  
ANISOU 2352  CG2 VAL A 329     9040   5953   5600   -159   -180   1040       C  
ATOM   2353  N   PHE A 330     -32.421 -20.822  -9.997  1.00 46.32           N  
ANISOU 2353  N   PHE A 330     8139   4680   4782   -459    -85   1006       N  
ATOM   2354  CA  PHE A 330     -32.383 -19.777  -8.982  1.00 46.45           C  
ANISOU 2354  CA  PHE A 330     8105   4649   4895   -529    -20   1019       C  
ATOM   2355  C   PHE A 330     -33.298 -20.140  -7.822  1.00 51.45           C  
ANISOU 2355  C   PHE A 330     8820   5209   5519   -659      2    952       C  
ATOM   2356  O   PHE A 330     -33.118 -19.667  -6.703  1.00 58.25           O  
ANISOU 2356  O   PHE A 330     9686   6038   6409   -716     36    925       O  
ATOM   2357  CB  PHE A 330     -32.783 -18.423  -9.569  1.00 39.23           C  
ANISOU 2357  CB  PHE A 330     7027   3775   4104   -515     34   1086       C  
ATOM   2358  CG  PHE A 330     -31.692 -17.758 -10.359  1.00 51.25           C  
ANISOU 2358  CG  PHE A 330     8451   5366   5655   -422     34   1188       C  
ATOM   2359  CD1 PHE A 330     -30.468 -18.382 -10.538  1.00 66.17           C  
ANISOU 2359  CD1 PHE A 330    10383   7306   7451   -349     -6   1191       C  
ATOM   2360  CD2 PHE A 330     -31.885 -16.504 -10.912  1.00 55.76           C  
ANISOU 2360  CD2 PHE A 330     8880   5955   6352   -411     70   1287       C  
ATOM   2361  CE1 PHE A 330     -29.462 -17.773 -11.263  1.00 64.79           C  
ANISOU 2361  CE1 PHE A 330    10097   7226   7293   -277      6   1289       C  
ATOM   2362  CE2 PHE A 330     -30.881 -15.888 -11.635  1.00 66.98           C  
ANISOU 2362  CE2 PHE A 330    10204   7447   7800   -349     76   1410       C  
ATOM   2363  CZ  PHE A 330     -29.667 -16.523 -11.810  1.00 65.90           C  
ANISOU 2363  CZ  PHE A 330    10096   7388   7554   -289     52   1411       C  
ATOM   2364  N   PHE A 331     -34.281 -20.986  -8.102  1.00 52.98           N  
ANISOU 2364  N   PHE A 331     9067   5394   5669   -711    -18    921       N  
ATOM   2365  CA  PHE A 331     -35.199 -21.459  -7.077  1.00 47.28           C  
ANISOU 2365  CA  PHE A 331     8416   4626   4922   -855      8    876       C  
ATOM   2366  C   PHE A 331     -34.499 -22.452  -6.154  1.00 48.10           C  
ANISOU 2366  C   PHE A 331     8688   4656   4933   -889    -43    878       C  
ATOM   2367  O   PHE A 331     -34.645 -22.389  -4.935  1.00 55.46           O  
ANISOU 2367  O   PHE A 331     9661   5577   5834   -985     -5    869       O  
ATOM   2368  CB  PHE A 331     -36.430 -22.098  -7.718  1.00 42.86           C  
ANISOU 2368  CB  PHE A 331     7850   4076   4357   -912     -6    848       C  
ATOM   2369  CG  PHE A 331     -37.483 -22.502  -6.736  1.00 50.51           C  
ANISOU 2369  CG  PHE A 331     8857   5026   5308  -1081     38    816       C  
ATOM   2370  CD1 PHE A 331     -38.331 -21.557  -6.184  1.00 49.37           C  
ANISOU 2370  CD1 PHE A 331     8591   4946   5221  -1149    130    780       C  
ATOM   2371  CD2 PHE A 331     -37.632 -23.830  -6.368  1.00 59.52           C  
ANISOU 2371  CD2 PHE A 331    10148   6088   6380  -1174    -17    823       C  
ATOM   2372  CE1 PHE A 331     -39.305 -21.928  -5.278  1.00 55.74           C  
ANISOU 2372  CE1 PHE A 331     9411   5778   5992  -1308    183    748       C  
ATOM   2373  CE2 PHE A 331     -38.604 -24.207  -5.463  1.00 56.21           C  
ANISOU 2373  CE2 PHE A 331     9752   5670   5935  -1352     33    821       C  
ATOM   2374  CZ  PHE A 331     -39.441 -23.255  -4.917  1.00 57.37           C  
ANISOU 2374  CZ  PHE A 331     9763   5921   6115  -1420    141    782       C  
ATOM   2375  N   LEU A 332     -33.730 -23.360  -6.746  1.00 53.89           N  
ANISOU 2375  N   LEU A 332     9511   5350   5613   -799   -136    886       N  
ATOM   2376  CA  LEU A 332     -32.982 -24.357  -5.986  1.00 57.84           C  
ANISOU 2376  CA  LEU A 332    10177   5762   6036   -802   -213    895       C  
ATOM   2377  C   LEU A 332     -31.929 -23.713  -5.093  1.00 50.55           C  
ANISOU 2377  C   LEU A 332     9246   4861   5099   -765   -195    907       C  
ATOM   2378  O   LEU A 332     -31.697 -24.167  -3.973  1.00 59.99           O  
ANISOU 2378  O   LEU A 332    10554   6010   6229   -824   -218    922       O  
ATOM   2379  CB  LEU A 332     -32.322 -25.365  -6.930  1.00 54.21           C  
ANISOU 2379  CB  LEU A 332     9791   5262   5544   -675   -330    871       C  
ATOM   2380  CG  LEU A 332     -33.280 -26.316  -7.645  1.00 52.41           C  
ANISOU 2380  CG  LEU A 332     9610   4978   5324   -717   -386    833       C  
ATOM   2381  CD1 LEU A 332     -32.533 -27.183  -8.643  1.00 56.52           C  
ANISOU 2381  CD1 LEU A 332    10178   5480   5817   -557   -509    772       C  
ATOM   2382  CD2 LEU A 332     -34.022 -27.173  -6.634  1.00 53.94           C  
ANISOU 2382  CD2 LEU A 332     9943   5047   5506   -891   -405    863       C  
ATOM   2383  N   PHE A 333     -31.290 -22.663  -5.599  1.00 35.38           N  
ANISOU 2383  N   PHE A 333     7188   3015   3240   -673   -160    908       N  
ATOM   2384  CA  PHE A 333     -30.310 -21.918  -4.819  1.00 41.28           C  
ANISOU 2384  CA  PHE A 333     7896   3784   4003   -645   -145    904       C  
ATOM   2385  C   PHE A 333     -30.935 -21.384  -3.538  1.00 39.52           C  
ANISOU 2385  C   PHE A 333     7669   3564   3783   -767    -79    874       C  
ATOM   2386  O   PHE A 333     -30.430 -21.619  -2.440  1.00 35.85           O  
ANISOU 2386  O   PHE A 333     7285   3092   3247   -790   -103    860       O  
ATOM   2387  CB  PHE A 333     -29.732 -20.760  -5.633  1.00 46.12           C  
ANISOU 2387  CB  PHE A 333     8341   4468   4716   -562   -108    926       C  
ATOM   2388  CG  PHE A 333     -28.824 -19.854  -4.843  1.00 60.21           C  
ANISOU 2388  CG  PHE A 333    10059   6264   6555   -554    -92    909       C  
ATOM   2389  CD1 PHE A 333     -27.472 -20.132  -4.737  1.00 62.70           C  
ANISOU 2389  CD1 PHE A 333    10394   6600   6830   -467   -153    906       C  
ATOM   2390  CD2 PHE A 333     -29.320 -18.721  -4.213  1.00 66.91           C  
ANISOU 2390  CD2 PHE A 333    10813   7105   7504   -627    -25    875       C  
ATOM   2391  CE1 PHE A 333     -26.633 -19.303  -4.017  1.00 63.42           C  
ANISOU 2391  CE1 PHE A 333    10412   6706   6979   -466   -148    876       C  
ATOM   2392  CE2 PHE A 333     -28.483 -17.889  -3.489  1.00 62.33           C  
ANISOU 2392  CE2 PHE A 333    10167   6527   6990   -620    -25    835       C  
ATOM   2393  CZ  PHE A 333     -27.138 -18.181  -3.393  1.00 54.07           C  
ANISOU 2393  CZ  PHE A 333     9140   5503   5902   -546    -86    839       C  
ATOM   2394  N   LEU A 334     -32.038 -20.658  -3.698  1.00 43.66           N  
ANISOU 2394  N   LEU A 334     8089   4116   4383   -833      1    854       N  
ATOM   2395  CA  LEU A 334     -32.742 -20.049  -2.579  1.00 39.27           C  
ANISOU 2395  CA  LEU A 334     7492   3594   3833   -935     72    796       C  
ATOM   2396  C   LEU A 334     -33.314 -21.107  -1.648  1.00 46.47           C  
ANISOU 2396  C   LEU A 334     8544   4506   4608  -1053     70    806       C  
ATOM   2397  O   LEU A 334     -33.308 -20.943  -0.426  1.00 52.28           O  
ANISOU 2397  O   LEU A 334     9301   5292   5272  -1115     99    772       O  
ATOM   2398  CB  LEU A 334     -33.864 -19.144  -3.090  1.00 35.58           C  
ANISOU 2398  CB  LEU A 334     6877   3157   3483   -961    143    765       C  
ATOM   2399  CG  LEU A 334     -33.468 -17.989  -4.010  1.00 37.08           C  
ANISOU 2399  CG  LEU A 334     6923   3339   3828   -863    147    786       C  
ATOM   2400  CD1 LEU A 334     -34.695 -17.440  -4.715  1.00 38.21           C  
ANISOU 2400  CD1 LEU A 334     6953   3501   4066   -876    189    781       C  
ATOM   2401  CD2 LEU A 334     -32.758 -16.891  -3.234  1.00 35.29           C  
ANISOU 2401  CD2 LEU A 334     6618   3101   3690   -844    159    731       C  
ATOM   2402  N   LEU A 335     -33.807 -22.193  -2.234  1.00 43.88           N  
ANISOU 2402  N   LEU A 335     8306   4125   4240  -1087     30    856       N  
ATOM   2403  CA  LEU A 335     -34.455 -23.248  -1.464  1.00 50.59           C  
ANISOU 2403  CA  LEU A 335     9286   4954   4982  -1225     25    897       C  
ATOM   2404  C   LEU A 335     -33.480 -23.959  -0.526  1.00 47.42           C  
ANISOU 2404  C   LEU A 335     9042   4510   4464  -1216    -49    949       C  
ATOM   2405  O   LEU A 335     -33.857 -24.385   0.563  1.00 45.48           O  
ANISOU 2405  O   LEU A 335     8876   4296   4110  -1337    -27    989       O  
ATOM   2406  CB  LEU A 335     -35.110 -24.266  -2.398  1.00 43.48           C  
ANISOU 2406  CB  LEU A 335     8445   3975   4099  -1260    -25    931       C  
ATOM   2407  CG  LEU A 335     -36.084 -25.219  -1.708  1.00 50.52           C  
ANISOU 2407  CG  LEU A 335     9433   4843   4921  -1445    -13    983       C  
ATOM   2408  CD1 LEU A 335     -37.291 -24.452  -1.188  1.00 40.79           C  
ANISOU 2408  CD1 LEU A 335     8060   3747   3694  -1569    119    936       C  
ATOM   2409  CD2 LEU A 335     -36.505 -26.330  -2.653  1.00 55.88           C  
ANISOU 2409  CD2 LEU A 335    10186   5405   5640  -1467    -98   1004       C  
ATOM   2410  N   MET A 336     -32.228 -24.085  -0.949  1.00 47.66           N  
ANISOU 2410  N   MET A 336     9109   4490   4508  -1070   -136    952       N  
ATOM   2411  CA  MET A 336     -31.223 -24.754  -0.134  1.00 54.17           C  
ANISOU 2411  CA  MET A 336    10076   5274   5232  -1032   -226    994       C  
ATOM   2412  C   MET A 336     -30.631 -23.812   0.914  1.00 60.59           C  
ANISOU 2412  C   MET A 336    10825   6192   6006  -1017   -187    944       C  
ATOM   2413  O   MET A 336     -30.049 -24.260   1.904  1.00 68.02           O  
ANISOU 2413  O   MET A 336    11873   7140   6831  -1019   -243    978       O  
ATOM   2414  CB  MET A 336     -30.120 -25.337  -1.021  1.00 58.25           C  
ANISOU 2414  CB  MET A 336    10644   5710   5777   -869   -344    995       C  
ATOM   2415  CG  MET A 336     -30.609 -26.446  -1.943  1.00 61.76           C  
ANISOU 2415  CG  MET A 336    11177   6043   6248   -870   -415   1018       C  
ATOM   2416  SD  MET A 336     -29.328 -27.095  -3.032  1.00 55.66           S  
ANISOU 2416  SD  MET A 336    10437   5213   5500   -650   -553    975       S  
ATOM   2417  CE  MET A 336     -28.159 -27.728  -1.837  1.00 91.97           C  
ANISOU 2417  CE  MET A 336    15189   9752  10005   -593   -668   1015       C  
ATOM   2418  N   TRP A 337     -30.789 -22.509   0.696  1.00 53.37           N  
ANISOU 2418  N   TRP A 337     9733   5351   5194   -998   -103    862       N  
ATOM   2419  CA  TRP A 337     -30.366 -21.515   1.675  1.00 38.08           C  
ANISOU 2419  CA  TRP A 337     7713   3506   3250   -992    -68    780       C  
ATOM   2420  C   TRP A 337     -31.475 -21.234   2.683  1.00 42.87           C  
ANISOU 2420  C   TRP A 337     8291   4216   3781  -1126     25    738       C  
ATOM   2421  O   TRP A 337     -31.243 -20.605   3.718  1.00 39.54           O  
ANISOU 2421  O   TRP A 337     7823   3894   3308  -1133     47    656       O  
ATOM   2422  CB  TRP A 337     -29.948 -20.218   0.985  1.00 47.64           C  
ANISOU 2422  CB  TRP A 337     8744   4723   4635   -908    -39    709       C  
ATOM   2423  CG  TRP A 337     -28.484 -20.134   0.690  1.00 42.87           C  
ANISOU 2423  CG  TRP A 337     8129   4096   4063   -784   -118    713       C  
ATOM   2424  CD1 TRP A 337     -27.901 -20.051  -0.539  1.00 39.71           C  
ANISOU 2424  CD1 TRP A 337     7670   3663   3756   -690   -144    751       C  
ATOM   2425  CD2 TRP A 337     -27.415 -20.122   1.644  1.00 46.52           C  
ANISOU 2425  CD2 TRP A 337     8624   4597   4456   -740   -181    672       C  
ATOM   2426  NE1 TRP A 337     -26.535 -19.988  -0.412  1.00 40.83           N  
ANISOU 2426  NE1 TRP A 337     7796   3821   3896   -597   -211    736       N  
ATOM   2427  CE2 TRP A 337     -26.211 -20.030   0.918  1.00 51.29           C  
ANISOU 2427  CE2 TRP A 337     9178   5181   5129   -623   -242    683       C  
ATOM   2428  CE3 TRP A 337     -27.360 -20.182   3.040  1.00 38.50           C  
ANISOU 2428  CE3 TRP A 337     7665   3652   3311   -786   -193    625       C  
ATOM   2429  CZ2 TRP A 337     -24.965 -19.996   1.542  1.00 49.10           C  
ANISOU 2429  CZ2 TRP A 337     8900   4941   4815   -551   -318    640       C  
ATOM   2430  CZ3 TRP A 337     -26.123 -20.150   3.656  1.00 39.01           C  
ANISOU 2430  CZ3 TRP A 337     7740   3752   3330   -707   -276    585       C  
ATOM   2431  CH2 TRP A 337     -24.943 -20.059   2.907  1.00 50.54           C  
ANISOU 2431  CH2 TRP A 337     9146   5179   4880   -592   -340    589       C  
ATOM   2432  N   CYS A 338     -32.680 -21.701   2.372  1.00 41.17           N  
ANISOU 2432  N   CYS A 338     8090   3995   3557  -1231     78    781       N  
ATOM   2433  CA  CYS A 338     -33.832 -21.528   3.258  1.00 51.77           C  
ANISOU 2433  CA  CYS A 338     9388   5465   4818  -1369    177    745       C  
ATOM   2434  C   CYS A 338     -33.682 -22.158   4.649  1.00 53.51           C  
ANISOU 2434  C   CYS A 338     9728   5778   4825  -1452    169    796       C  
ATOM   2435  O   CYS A 338     -33.984 -21.500   5.643  1.00 54.04           O  
ANISOU 2435  O   CYS A 338     9712   6007   4813  -1493    239    704       O  
ATOM   2436  CB  CYS A 338     -35.102 -22.074   2.595  1.00 40.29           C  
ANISOU 2436  CB  CYS A 338     7929   3986   3394  -1475    223    794       C  
ATOM   2437  SG  CYS A 338     -35.875 -20.940   1.427  1.00 55.51           S  
ANISOU 2437  SG  CYS A 338     9648   5913   5529  -1420    286    695       S  
ATOM   2438  N   PRO A 339     -33.231 -23.426   4.737  1.00 57.68           N  
ANISOU 2438  N   PRO A 339    10448   6212   5257  -1471     76    942       N  
ATOM   2439  CA  PRO A 339     -33.179 -24.013   6.083  1.00 50.90           C  
ANISOU 2439  CA  PRO A 339     9704   5453   4183  -1561     67   1023       C  
ATOM   2440  C   PRO A 339     -32.230 -23.287   7.039  1.00 47.74           C  
ANISOU 2440  C   PRO A 339     9266   5175   3699  -1470     45    928       C  
ATOM   2441  O   PRO A 339     -32.487 -23.275   8.240  1.00 56.80           O  
ANISOU 2441  O   PRO A 339    10424   6496   4662  -1549     88    930       O  
ATOM   2442  CB  PRO A 339     -32.696 -25.447   5.823  1.00 56.73           C  
ANISOU 2442  CB  PRO A 339    10657   6012   4886  -1561    -63   1195       C  
ATOM   2443  CG  PRO A 339     -32.029 -25.397   4.494  1.00 65.18           C  
ANISOU 2443  CG  PRO A 339    11708   6925   6134  -1408   -139   1149       C  
ATOM   2444  CD  PRO A 339     -32.805 -24.393   3.709  1.00 63.96           C  
ANISOU 2444  CD  PRO A 339    11362   6817   6122  -1413    -31   1035       C  
ATOM   2445  N   PHE A 340     -31.167 -22.681   6.520  1.00 50.03           N  
ANISOU 2445  N   PHE A 340     9499   5394   4115  -1312    -19    841       N  
ATOM   2446  CA  PHE A 340     -30.222 -21.968   7.374  1.00 53.22           C  
ANISOU 2446  CA  PHE A 340     9853   5904   4466  -1225    -54    732       C  
ATOM   2447  C   PHE A 340     -30.771 -20.646   7.898  1.00 57.66           C  
ANISOU 2447  C   PHE A 340    10224   6621   5064  -1246     50    544       C  
ATOM   2448  O   PHE A 340     -30.736 -20.385   9.101  1.00 66.35           O  
ANISOU 2448  O   PHE A 340    11307   7898   6005  -1269     66    470       O  
ATOM   2449  CB  PHE A 340     -28.912 -21.695   6.638  1.00 49.64           C  
ANISOU 2449  CB  PHE A 340     9373   5335   4154  -1065   -152    694       C  
ATOM   2450  CG  PHE A 340     -28.058 -20.665   7.315  1.00 42.58           C  
ANISOU 2450  CG  PHE A 340     8365   4539   3275   -985   -174    540       C  
ATOM   2451  CD1 PHE A 340     -27.412 -20.960   8.504  1.00 43.96           C  
ANISOU 2451  CD1 PHE A 340     8616   4825   3261   -965   -243    535       C  
ATOM   2452  CD2 PHE A 340     -27.914 -19.398   6.778  1.00 65.96           C  
ANISOU 2452  CD2 PHE A 340    11140   7476   6445   -935   -136    403       C  
ATOM   2453  CE1 PHE A 340     -26.632 -20.015   9.141  1.00 44.37           C  
ANISOU 2453  CE1 PHE A 340     8554   4974   3332   -892   -275    369       C  
ATOM   2454  CE2 PHE A 340     -27.133 -18.450   7.412  1.00 71.53           C  
ANISOU 2454  CE2 PHE A 340    11735   8251   7191   -874   -169    249       C  
ATOM   2455  CZ  PHE A 340     -26.495 -18.763   8.598  1.00 43.48           C  
ANISOU 2455  CZ  PHE A 340     8253   4820   3448   -851   -239    219       C  
ATOM   2456  N   PHE A 341     -31.257 -19.802   6.993  1.00 53.56           N  
ANISOU 2456  N   PHE A 341     9558   6038   4753  -1226    109    459       N  
ATOM   2457  CA  PHE A 341     -31.681 -18.461   7.376  1.00 49.80           C  
ANISOU 2457  CA  PHE A 341     8892   5665   4365  -1216    182    260       C  
ATOM   2458  C   PHE A 341     -32.984 -18.470   8.172  1.00 52.54           C  
ANISOU 2458  C   PHE A 341     9194   6197   4571  -1338    294    211       C  
ATOM   2459  O   PHE A 341     -33.197 -17.599   9.014  1.00 50.51           O  
ANISOU 2459  O   PHE A 341     8813   6095   4283  -1327    337     29       O  
ATOM   2460  CB  PHE A 341     -31.816 -17.569   6.141  1.00 46.44           C  
ANISOU 2460  CB  PHE A 341     8331   5101   4215  -1154    197    209       C  
ATOM   2461  CG  PHE A 341     -30.500 -17.055   5.625  1.00 48.99           C  
ANISOU 2461  CG  PHE A 341     8617   5309   4687  -1036    111    192       C  
ATOM   2462  CD1 PHE A 341     -29.767 -16.135   6.358  1.00 41.31           C  
ANISOU 2462  CD1 PHE A 341     7551   4384   3760   -980     75     37       C  
ATOM   2463  CD2 PHE A 341     -29.997 -17.489   4.409  1.00 58.14           C  
ANISOU 2463  CD2 PHE A 341     9821   6331   5939   -983     65    321       C  
ATOM   2464  CE1 PHE A 341     -28.553 -15.659   5.887  1.00 45.00           C  
ANISOU 2464  CE1 PHE A 341     7968   4754   4377   -892     -1     28       C  
ATOM   2465  CE2 PHE A 341     -28.785 -17.016   3.933  1.00 55.99           C  
ANISOU 2465  CE2 PHE A 341     9494   5986   5792   -886     -2    313       C  
ATOM   2466  CZ  PHE A 341     -28.063 -16.100   4.672  1.00 47.75           C  
ANISOU 2466  CZ  PHE A 341     8355   4981   4807   -849    -34    175       C  
ATOM   2467  N   ILE A 342     -33.848 -19.450   7.916  1.00 44.41           N  
ANISOU 2467  N   ILE A 342     8253   5162   3459  -1454    338    361       N  
ATOM   2468  CA  ILE A 342     -35.063 -19.604   8.711  1.00 50.27           C  
ANISOU 2468  CA  ILE A 342     8952   6109   4041  -1593    451    343       C  
ATOM   2469  C   ILE A 342     -34.700 -20.015  10.138  1.00 58.77           C  
ANISOU 2469  C   ILE A 342    10112   7382   4838  -1638    442    370       C  
ATOM   2470  O   ILE A 342     -35.264 -19.500  11.107  1.00 58.30           O  
ANISOU 2470  O   ILE A 342     9942   7565   4643  -1680    527    239       O  
ATOM   2471  CB  ILE A 342     -36.029 -20.640   8.093  1.00 54.11           C  
ANISOU 2471  CB  ILE A 342     9514   6533   4514  -1729    490    515       C  
ATOM   2472  CG1 ILE A 342     -36.587 -20.124   6.766  1.00 56.44           C  
ANISOU 2472  CG1 ILE A 342     9694   6695   5056  -1685    511    461       C  
ATOM   2473  CG2 ILE A 342     -37.182 -20.946   9.039  1.00 59.11           C  
ANISOU 2473  CG2 ILE A 342    10108   7405   4947  -1899    609    530       C  
ATOM   2474  CD1 ILE A 342     -37.498 -21.111   6.063  1.00 44.55           C  
ANISOU 2474  CD1 ILE A 342     8248   5120   3560  -1808    532    602       C  
ATOM   2475  N   THR A 343     -33.746 -20.934  10.260  1.00 61.65           N  
ANISOU 2475  N   THR A 343    10663   7652   5108  -1616    333    534       N  
ATOM   2476  CA  THR A 343     -33.260 -21.374  11.565  1.00 49.76           C  
ANISOU 2476  CA  THR A 343     9256   6319   3331  -1640    298    588       C  
ATOM   2477  C   THR A 343     -32.575 -20.227  12.306  1.00 72.52           C  
ANISOU 2477  C   THR A 343    12011   9347   6199  -1518    278    351       C  
ATOM   2478  O   THR A 343     -32.789 -20.033  13.501  1.00 71.49           O  
ANISOU 2478  O   THR A 343    11839   9479   5843  -1554    322    275       O  
ATOM   2479  CB  THR A 343     -32.272 -22.550  11.433  1.00 49.72           C  
ANISOU 2479  CB  THR A 343     9476   6145   3270  -1606    155    802       C  
ATOM   2480  OG1 THR A 343     -32.905 -23.633  10.741  1.00 49.61           O  
ANISOU 2480  OG1 THR A 343     9582   5973   3292  -1718    156   1002       O  
ATOM   2481  CG2 THR A 343     -31.817 -23.026  12.802  1.00 51.90           C  
ANISOU 2481  CG2 THR A 343     9860   6609   3252  -1629    109    882       C  
ATOM   2482  N   ASN A 344     -31.754 -19.472  11.581  1.00 67.89           N  
ANISOU 2482  N   ASN A 344    11352   8593   5849  -1379    209    233       N  
ATOM   2483  CA  ASN A 344     -31.025 -18.342  12.146  1.00 48.85           C  
ANISOU 2483  CA  ASN A 344     8810   6267   3485  -1266    169     -2       C  
ATOM   2484  C   ASN A 344     -31.968 -17.271  12.693  1.00 56.27           C  
ANISOU 2484  C   ASN A 344     9552   7394   4433  -1287    276   -241       C  
ATOM   2485  O   ASN A 344     -31.673 -16.625  13.700  1.00 51.31           O  
ANISOU 2485  O   ASN A 344     8839   6952   3705  -1237    261   -435       O  
ATOM   2486  CB  ASN A 344     -30.094 -17.738  11.089  1.00 49.45           C  
ANISOU 2486  CB  ASN A 344     8830   6106   3853  -1144     88    -52       C  
ATOM   2487  CG  ASN A 344     -28.944 -16.956  11.697  1.00 60.71           C  
ANISOU 2487  CG  ASN A 344    10181   7579   5309  -1034     -4   -229       C  
ATOM   2488  OD1 ASN A 344     -27.964 -17.535  12.167  1.00 66.07           O  
ANISOU 2488  OD1 ASN A 344    10967   8286   5852   -986   -104   -164       O  
ATOM   2489  ND2 ASN A 344     -29.054 -15.633  11.683  1.00 65.58           N  
ANISOU 2489  ND2 ASN A 344    10606   8191   6119   -989     18   -460       N  
ATOM   2490  N   ILE A 345     -33.102 -17.090  12.023  1.00 52.84           N  
ANISOU 2490  N   ILE A 345     9038   6918   4120  -1350    376   -242       N  
ATOM   2491  CA  ILE A 345     -34.105 -16.121  12.451  1.00 52.71           C  
ANISOU 2491  CA  ILE A 345     8824   7074   4128  -1360    477   -474       C  
ATOM   2492  C   ILE A 345     -34.825 -16.603  13.707  1.00 59.30           C  
ANISOU 2492  C   ILE A 345     9665   8244   4622  -1468    568   -474       C  
ATOM   2493  O   ILE A 345     -34.980 -15.855  14.674  1.00 66.65           O  
ANISOU 2493  O   ILE A 345    10463   9412   5449  -1428    599   -710       O  
ATOM   2494  CB  ILE A 345     -35.142 -15.850  11.338  1.00 53.29           C  
ANISOU 2494  CB  ILE A 345     8807   7017   4424  -1390    548   -464       C  
ATOM   2495  CG1 ILE A 345     -34.531 -14.982  10.236  1.00 58.31           C  
ANISOU 2495  CG1 ILE A 345     9374   7380   5400  -1269    472   -522       C  
ATOM   2496  CG2 ILE A 345     -36.371 -15.159  11.900  1.00 56.77           C  
ANISOU 2496  CG2 ILE A 345     9060   7683   4827  -1420    663   -673       C  
ATOM   2497  CD1 ILE A 345     -33.983 -13.660  10.729  1.00 60.63           C  
ANISOU 2497  CD1 ILE A 345     9518   7685   5832  -1154    420   -791       C  
ATOM   2498  N   THR A 346     -35.255 -17.860  13.692  1.00 58.97           N  
ANISOU 2498  N   THR A 346     9774   8227   4405  -1608    606   -208       N  
ATOM   2499  CA  THR A 346     -35.974 -18.430  14.823  1.00 69.86           C  
ANISOU 2499  CA  THR A 346    11167   9928   5448  -1743    702   -147       C  
ATOM   2500  C   THR A 346     -35.082 -18.535  16.057  1.00 69.64           C  
ANISOU 2500  C   THR A 346    11205  10101   5153  -1696    636   -169       C  
ATOM   2501  O   THR A 346     -35.573 -18.600  17.182  1.00 74.88           O  
ANISOU 2501  O   THR A 346    11820  11106   5524  -1766    716   -209       O  
ATOM   2502  CB  THR A 346     -36.544 -19.822  14.487  1.00 70.91           C  
ANISOU 2502  CB  THR A 346    11464   9995   5484  -1920    737    179       C  
ATOM   2503  OG1 THR A 346     -35.491 -20.674  14.024  1.00 77.28           O  
ANISOU 2503  OG1 THR A 346    12486  10544   6333  -1883    597    392       O  
ATOM   2504  CG2 THR A 346     -37.611 -19.713  13.407  1.00 74.03           C  
ANISOU 2504  CG2 THR A 346    11764  10264   6100  -1980    815    174       C  
ATOM   2505  N   LEU A 347     -33.771 -18.542  15.845  1.00 56.13           N  
ANISOU 2505  N   LEU A 347     9593   8202   3533  -1576    489   -149       N  
ATOM   2506  CA  LEU A 347     -32.828 -18.579  16.954  1.00 57.70           C  
ANISOU 2506  CA  LEU A 347     9844   8578   3500  -1508    403   -191       C  
ATOM   2507  C   LEU A 347     -32.880 -17.268  17.731  1.00 58.97           C  
ANISOU 2507  C   LEU A 347     9787   8972   3645  -1412    428   -559       C  
ATOM   2508  O   LEU A 347     -32.589 -17.229  18.926  1.00 61.16           O  
ANISOU 2508  O   LEU A 347    10055   9540   3643  -1389    410   -643       O  
ATOM   2509  CB  LEU A 347     -31.410 -18.852  16.445  1.00 56.18           C  
ANISOU 2509  CB  LEU A 347     9781   8122   3441  -1391    235   -106       C  
ATOM   2510  CG  LEU A 347     -30.296 -19.026  17.479  1.00 63.08           C  
ANISOU 2510  CG  LEU A 347    10730   9146   4091  -1308    114   -120       C  
ATOM   2511  CD1 LEU A 347     -30.710 -20.001  18.568  1.00 60.25           C  
ANISOU 2511  CD1 LEU A 347    10498   9060   3336  -1425    150     83       C  
ATOM   2512  CD2 LEU A 347     -29.024 -19.505  16.801  1.00 61.54           C  
ANISOU 2512  CD2 LEU A 347    10668   8672   4042  -1208    -43      6       C  
ATOM   2513  N   VAL A 348     -33.274 -16.198  17.049  1.00 64.87           N  
ANISOU 2513  N   VAL A 348    10359   9594   4696  -1351    462   -782       N  
ATOM   2514  CA  VAL A 348     -33.348 -14.880  17.667  1.00 71.11           C  
ANISOU 2514  CA  VAL A 348    10933  10547   5540  -1245    467  -1161       C  
ATOM   2515  C   VAL A 348     -34.758 -14.583  18.182  1.00 71.45           C  
ANISOU 2515  C   VAL A 348    10818  10883   5447  -1315    624  -1304       C  
ATOM   2516  O   VAL A 348     -34.934 -13.828  19.138  1.00 80.59           O  
ANISOU 2516  O   VAL A 348    11819  12320   6482  -1250    644  -1598       O  
ATOM   2517  CB  VAL A 348     -32.920 -13.776  16.674  1.00 65.51           C  
ANISOU 2517  CB  VAL A 348    10109   9515   5266  -1128    393  -1335       C  
ATOM   2518  CG1 VAL A 348     -32.801 -12.433  17.375  1.00 62.97           C  
ANISOU 2518  CG1 VAL A 348     9581   9317   5029  -1008    357  -1736       C  
ATOM   2519  CG2 VAL A 348     -31.604 -14.147  16.014  1.00 60.97           C  
ANISOU 2519  CG2 VAL A 348     9675   8663   4829  -1077    260  -1166       C  
ATOM   2520  N   LEU A 349     -35.759 -15.197  17.559  1.00 67.46           N  
ANISOU 2520  N   LEU A 349    10343  10333   4958  -1444    731  -1110       N  
ATOM   2521  CA  LEU A 349     -37.150 -14.868  17.861  1.00 74.48           C  
ANISOU 2521  CA  LEU A 349    11054  11478   5769  -1508    884  -1252       C  
ATOM   2522  C   LEU A 349     -37.854 -15.904  18.742  1.00 77.93           C  
ANISOU 2522  C   LEU A 349    11550  12267   5795  -1685   1006  -1055       C  
ATOM   2523  O   LEU A 349     -38.949 -15.650  19.243  1.00 80.27           O  
ANISOU 2523  O   LEU A 349    11677  12871   5952  -1742   1143  -1190       O  
ATOM   2524  CB  LEU A 349     -37.932 -14.681  16.560  1.00 73.30           C  
ANISOU 2524  CB  LEU A 349    10846  11069   5938  -1531    928  -1212       C  
ATOM   2525  CG  LEU A 349     -37.369 -13.630  15.600  1.00 65.96           C  
ANISOU 2525  CG  LEU A 349     9846   9793   5423  -1374    821  -1370       C  
ATOM   2526  CD1 LEU A 349     -38.344 -13.355  14.467  1.00 56.59           C  
ANISOU 2526  CD1 LEU A 349     8568   8433   4502  -1390    877  -1359       C  
ATOM   2527  CD2 LEU A 349     -37.023 -12.345  16.342  1.00 59.29           C  
ANISOU 2527  CD2 LEU A 349     8826   9058   4644  -1222    767  -1753       C  
ATOM   2528  N   CYS A 350     -37.234 -17.064  18.930  1.00 73.96           N  
ANISOU 2528  N   CYS A 350    11278  11722   5101  -1772    952   -731       N  
ATOM   2529  CA  CYS A 350     -37.800 -18.091  19.802  1.00 76.88           C  
ANISOU 2529  CA  CYS A 350    11725  12407   5080  -1954   1051   -496       C  
ATOM   2530  C   CYS A 350     -36.973 -18.233  21.077  1.00 84.81           C  
ANISOU 2530  C   CYS A 350    12795  13686   5743  -1906    987   -504       C  
ATOM   2531  O   CYS A 350     -35.759 -18.420  21.023  1.00 67.78           O  
ANISOU 2531  O   CYS A 350    10785  11340   3628  -1809    832   -436       O  
ATOM   2532  CB  CYS A 350     -37.890 -19.434  19.070  1.00 65.47           C  
ANISOU 2532  CB  CYS A 350    10503  10705   3670  -2113   1036    -84       C  
ATOM   2533  SG  CYS A 350     -38.381 -20.843  20.095  1.00 87.95           S  
ANISOU 2533  SG  CYS A 350    13495  13854   6068  -2359   1119    291       S  
ATOM   2534  N   ASP A 351     -37.635 -18.139  22.224  1.00 99.06           N  
ANISOU 2534  N   ASP A 351    14477  15962   7198  -1968   1107   -596       N  
ATOM   2535  CA  ASP A 351     -36.952 -18.250  23.508  1.00109.36           C  
ANISOU 2535  CA  ASP A 351    15808  17554   8190  -1895   1044   -607       C  
ATOM   2536  C   ASP A 351     -37.315 -19.548  24.220  1.00103.29           C  
ANISOU 2536  C   ASP A 351    15133  16897   7215  -2014   1082   -203       C  
ATOM   2537  O   ASP A 351     -36.907 -19.778  25.358  1.00105.08           O  
ANISOU 2537  O   ASP A 351    15372  17354   7200  -1949   1041   -156       O  
ATOM   2538  CB  ASP A 351     -37.283 -17.049  24.399  1.00116.07           C  
ANISOU 2538  CB  ASP A 351    16385  18774   8943  -1762   1098  -1046       C  
ATOM   2539  CG  ASP A 351     -36.709 -15.750  23.864  1.00111.53           C  
ANISOU 2539  CG  ASP A 351    15700  18012   8666  -1582   1003  -1453       C  
ATOM   2540  OD1 ASP A 351     -37.276 -15.202  22.894  1.00113.95           O  
ANISOU 2540  OD1 ASP A 351    15902  18069   9324  -1563   1040  -1567       O  
ATOM   2541  OD2 ASP A 351     -35.692 -15.278  24.412  1.00107.51           O  
ANISOU 2541  OD2 ASP A 351    15190  17545   8115  -1435    871  -1638       O  
ATOM   2542  N   SER A 352     -38.083 -20.394  23.541  1.00 95.80           N  
ANISOU 2542  N   SER A 352    14249  15774   6375  -2188   1154     82       N  
ATOM   2543  CA  SER A 352     -38.469 -21.689  24.087  1.00 91.83           C  
ANISOU 2543  CA  SER A 352    13838  15316   5738  -2321   1182    473       C  
ATOM   2544  C   SER A 352     -37.564 -22.786  23.538  1.00 87.99           C  
ANISOU 2544  C   SER A 352    13623  14430   5377  -2327   1022    811       C  
ATOM   2545  O   SER A 352     -37.367 -23.824  24.172  1.00 94.39           O  
ANISOU 2545  O   SER A 352    14551  15248   6064  -2364    976   1111       O  
ATOM   2546  CB  SER A 352     -39.931 -21.998  23.760  1.00 95.07           C  
ANISOU 2546  CB  SER A 352    14124  15791   6207  -2513   1349    562       C  
ATOM   2547  OG  SER A 352     -40.784 -20.945  24.176  1.00104.73           O  
ANISOU 2547  OG  SER A 352    15074  17373   7345  -2487   1491    220       O  
ATOM   2548  N   CYS A 353     -37.013 -22.542  22.354  1.00 77.04           N  
ANISOU 2548  N   CYS A 353    12332  12692   4246  -2282    935    751       N  
ATOM   2549  CA  CYS A 353     -36.192 -23.527  21.664  1.00 74.95           C  
ANISOU 2549  CA  CYS A 353    12302  12022   4152  -2269    779   1027       C  
ATOM   2550  C   CYS A 353     -34.825 -23.676  22.319  1.00 78.35           C  
ANISOU 2550  C   CYS A 353    12855  12457   4459  -2106    613   1057       C  
ATOM   2551  O   CYS A 353     -34.221 -22.691  22.743  1.00 83.43           O  
ANISOU 2551  O   CYS A 353    13427  13274   5000  -1974    579    776       O  
ATOM   2552  CB  CYS A 353     -36.029 -23.141  20.193  1.00 75.99           C  
ANISOU 2552  CB  CYS A 353    12488  11802   4585  -2256    743    931       C  
ATOM   2553  SG  CYS A 353     -37.552 -22.565  19.400  1.00 93.52           S  
ANISOU 2553  SG  CYS A 353    14529  14068   6937  -2402    937    785       S  
ATOM   2554  N   ASN A 354     -34.343 -24.912  22.398  1.00 73.59           N  
ANISOU 2554  N   ASN A 354    12424  11660   3878  -2110    502   1382       N  
ATOM   2555  CA  ASN A 354     -33.019 -25.182  22.943  1.00 74.24           C  
ANISOU 2555  CA  ASN A 354    12628  11720   3859  -1949    330   1437       C  
ATOM   2556  C   ASN A 354     -31.918 -24.668  22.026  1.00 74.65           C  
ANISOU 2556  C   ASN A 354    12756  11498   4111  -1813    190   1277       C  
ATOM   2557  O   ASN A 354     -31.658 -25.248  20.972  1.00 69.05           O  
ANISOU 2557  O   ASN A 354    12164  10417   3654  -1818    113   1409       O  
ATOM   2558  CB  ASN A 354     -32.833 -26.680  23.186  1.00 76.13           C  
ANISOU 2558  CB  ASN A 354    13027  11796   4102  -1987    244   1821       C  
ATOM   2559  CG  ASN A 354     -31.459 -27.013  23.733  1.00 87.72           C  
ANISOU 2559  CG  ASN A 354    14617  13242   5471  -1809     58   1885       C  
ATOM   2560  OD1 ASN A 354     -30.694 -27.752  23.113  1.00 75.84           O  
ANISOU 2560  OD1 ASN A 354    13256  11407   4153  -1747    -92   2030       O  
ATOM   2561  ND2 ASN A 354     -31.138 -26.467  24.902  1.00 87.69           N  
ANISOU 2561  ND2 ASN A 354    14546  13599   5173  -1715     61   1759       N  
ATOM   2562  N   GLN A 355     -31.273 -23.581  22.441  1.00 75.55           N  
ANISOU 2562  N   GLN A 355    12793  11800   4114  -1688    153    979       N  
ATOM   2563  CA  GLN A 355     -30.223 -22.941  21.654  1.00 71.23           C  
ANISOU 2563  CA  GLN A 355    12299  11026   3738  -1566     27    792       C  
ATOM   2564  C   GLN A 355     -29.084 -23.899  21.310  1.00 70.99           C  
ANISOU 2564  C   GLN A 355    12453  10703   3816  -1464   -164   1014       C  
ATOM   2565  O   GLN A 355     -28.511 -23.825  20.224  1.00 67.28           O  
ANISOU 2565  O   GLN A 355    12061   9920   3584  -1409   -246    985       O  
ATOM   2566  CB  GLN A 355     -29.665 -21.730  22.404  1.00 68.72           C  
ANISOU 2566  CB  GLN A 355    11856  10992   3261  -1450     -4    434       C  
ATOM   2567  CG  GLN A 355     -30.669 -20.614  22.638  1.00 79.20           C  
ANISOU 2567  CG  GLN A 355    12948  12575   4570  -1493    164    123       C  
ATOM   2568  CD  GLN A 355     -30.057 -19.429  23.366  1.00 90.32           C  
ANISOU 2568  CD  GLN A 355    14175  14204   5937  -1327    107   -270       C  
ATOM   2569  OE1 GLN A 355     -28.865 -19.150  23.227  1.00100.81           O  
ANISOU 2569  OE1 GLN A 355    15523  15379   7400  -1178    -51   -371       O  
ATOM   2570  NE2 GLN A 355     -30.870 -18.729  24.151  1.00 84.35           N  
ANISOU 2570  NE2 GLN A 355    13232  13818   4999  -1350    232   -508       N  
ATOM   2571  N   THR A 356     -28.762 -24.793  22.241  1.00 70.07           N  
ANISOU 2571  N   THR A 356    12398  10699   3525  -1428   -233   1230       N  
ATOM   2572  CA  THR A 356     -27.685 -25.760  22.045  1.00 70.06           C  
ANISOU 2572  CA  THR A 356    12554  10451   3614  -1318   -420   1431       C  
ATOM   2573  C   THR A 356     -27.906 -26.606  20.795  1.00 79.72           C  
ANISOU 2573  C   THR A 356    13879  11266   5145  -1379   -441   1614       C  
ATOM   2574  O   THR A 356     -27.032 -26.695  19.934  1.00 68.78           O  
ANISOU 2574  O   THR A 356    12569   9604   3959  -1270   -568   1582       O  
ATOM   2575  CB  THR A 356     -27.540 -26.702  23.255  1.00 73.67           C  
ANISOU 2575  CB  THR A 356    13064  11093   3833  -1297   -469   1673       C  
ATOM   2576  OG1 THR A 356     -27.215 -25.940  24.424  1.00 96.09           O  
ANISOU 2576  OG1 THR A 356    15810  14324   6377  -1206   -471   1486       O  
ATOM   2577  CG2 THR A 356     -26.440 -27.723  23.004  1.00 73.78           C  
ANISOU 2577  CG2 THR A 356    13231  10837   3964  -1178   -669   1867       C  
ATOM   2578  N   THR A 357     -29.081 -27.221  20.702  1.00 81.84           N  
ANISOU 2578  N   THR A 357    14136  11509   5448  -1546   -320   1787       N  
ATOM   2579  CA  THR A 357     -29.409 -28.078  19.568  1.00 84.61           C  
ANISOU 2579  CA  THR A 357    14568  11494   6086  -1612   -341   1941       C  
ATOM   2580  C   THR A 357     -29.817 -27.258  18.349  1.00 88.11           C  
ANISOU 2580  C   THR A 357    14950  11789   6738  -1644   -264   1749       C  
ATOM   2581  O   THR A 357     -29.696 -27.715  17.213  1.00 88.21           O  
ANISOU 2581  O   THR A 357    15027  11482   7008  -1626   -322   1793       O  
ATOM   2582  CB  THR A 357     -30.536 -29.068  19.918  1.00 94.19           C  
ANISOU 2582  CB  THR A 357    15786  12731   7270  -1791   -250   2191       C  
ATOM   2583  OG1 THR A 357     -31.649 -28.356  20.472  1.00 99.19           O  
ANISOU 2583  OG1 THR A 357    16273  13685   7732  -1922    -57   2099       O  
ATOM   2584  CG2 THR A 357     -30.045 -30.095  20.927  1.00100.99           C  
ANISOU 2584  CG2 THR A 357    16747  13647   7976  -1752   -352   2436       C  
ATOM   2585  N   LEU A 358     -30.296 -26.043  18.589  1.00100.06           N  
ANISOU 2585  N   LEU A 358    16336  13546   8137  -1681   -137   1522       N  
ATOM   2586  CA  LEU A 358     -30.650 -25.138  17.503  1.00 61.19           C  
ANISOU 2586  CA  LEU A 358    11355   8504   3389  -1702    -63   1329       C  
ATOM   2587  C   LEU A 358     -29.385 -24.588  16.850  1.00 59.03           C  
ANISOU 2587  C   LEU A 358    11143   8051   3234  -1531   -197   1184       C  
ATOM   2588  O   LEU A 358     -29.428 -24.040  15.749  1.00 66.55           O  
ANISOU 2588  O   LEU A 358    12009   8814   4461  -1485   -172   1055       O  
ATOM   2589  CB  LEU A 358     -31.531 -24.001  18.021  1.00 61.72           C  
ANISOU 2589  CB  LEU A 358    11259   8895   3295  -1786    108   1105       C  
ATOM   2590  CG  LEU A 358     -32.424 -23.287  17.008  1.00 59.69           C  
ANISOU 2590  CG  LEU A 358    10866   8541   3272  -1838    233    950       C  
ATOM   2591  CD1 LEU A 358     -33.230 -24.294  16.206  1.00 59.30           C  
ANISOU 2591  CD1 LEU A 358    10911   8280   3339  -1987    269   1192       C  
ATOM   2592  CD2 LEU A 358     -33.344 -22.316  17.722  1.00 60.96           C  
ANISOU 2592  CD2 LEU A 358    10806   9047   3311  -1886    393    719       C  
ATOM   2593  N   GLN A 359     -28.260 -24.735  17.541  1.00 72.64           N  
ANISOU 2593  N   GLN A 359    12919   9838   4841  -1398   -337   1185       N  
ATOM   2594  CA  GLN A 359     -26.965 -24.356  16.993  1.00 65.45           C  
ANISOU 2594  CA  GLN A 359    12020   8764   4086  -1214   -480   1056       C  
ATOM   2595  C   GLN A 359     -26.400 -25.501  16.162  1.00 61.32           C  
ANISOU 2595  C   GLN A 359    11654   7919   3725  -1156   -611   1263       C  
ATOM   2596  O   GLN A 359     -25.691 -25.279  15.180  1.00 63.95           O  
ANISOU 2596  O   GLN A 359    11981   8047   4269  -1041   -682   1180       O  
ATOM   2597  CB  GLN A 359     -25.992 -23.974  18.113  1.00 68.07           C  
ANISOU 2597  CB  GLN A 359    12324   9325   4213  -1092   -582    937       C  
ATOM   2598  CG  GLN A 359     -24.621 -23.521  17.628  1.00 67.18           C  
ANISOU 2598  CG  GLN A 359    12153   9072   4301   -896   -724    775       C  
ATOM   2599  CD  GLN A 359     -24.672 -22.209  16.868  1.00 64.11           C  
ANISOU 2599  CD  GLN A 359    11534   8617   4205   -857   -642    494       C  
ATOM   2600  OE1 GLN A 359     -25.555 -21.380  17.093  1.00 57.62           O  
ANISOU 2600  OE1 GLN A 359    10567   7937   3388   -933   -504    338       O  
ATOM   2601  NE2 GLN A 359     -23.723 -22.015  15.957  1.00 64.58           N  
ANISOU 2601  NE2 GLN A 359    11556   8466   4516   -736   -730    433       N  
ATOM   2602  N   MET A 360     -26.727 -26.726  16.563  1.00 62.80           N  
ANISOU 2602  N   MET A 360    11900   8071   3890  -1211   -631   1500       N  
ATOM   2603  CA  MET A 360     -26.300 -27.921  15.844  1.00 67.27           C  
ANISOU 2603  CA  MET A 360    12570   8334   4657  -1150   -753   1663       C  
ATOM   2604  C   MET A 360     -26.887 -27.943  14.439  1.00 57.10           C  
ANISOU 2604  C   MET A 360    11266   6804   3625  -1201   -695   1636       C  
ATOM   2605  O   MET A 360     -26.215 -28.319  13.480  1.00 55.82           O  
ANISOU 2605  O   MET A 360    11152   6405   3652  -1086   -800   1625       O  
ATOM   2606  CB  MET A 360     -26.713 -29.185  16.606  1.00 75.20           C  
ANISOU 2606  CB  MET A 360    13640   9352   5582  -1231   -775   1915       C  
ATOM   2607  CG  MET A 360     -26.618 -30.464  15.786  1.00 78.23           C  
ANISOU 2607  CG  MET A 360    14124   9405   6195  -1214   -878   2063       C  
ATOM   2608  SD  MET A 360     -27.051 -31.946  16.715  1.00145.99           S  
ANISOU 2608  SD  MET A 360    22800  17978  14691  -1314   -920   2370       S  
ATOM   2609  CE  MET A 360     -27.002 -33.182  15.419  1.00116.52           C  
ANISOU 2609  CE  MET A 360    19169  13825  11280  -1290  -1039   2441       C  
ATOM   2610  N   LEU A 361     -28.146 -27.534  14.328  1.00 56.78           N  
ANISOU 2610  N   LEU A 361    11146   6849   3578  -1364   -528   1614       N  
ATOM   2611  CA  LEU A 361     -28.820 -27.460  13.039  1.00 62.39           C  
ANISOU 2611  CA  LEU A 361    11822   7371   4511  -1417   -462   1578       C  
ATOM   2612  C   LEU A 361     -28.194 -26.374  12.165  1.00 61.32           C  
ANISOU 2612  C   LEU A 361    11654   7171   4474  -1304   -471   1391       C  
ATOM   2613  O   LEU A 361     -28.079 -26.537  10.951  1.00 58.64           O  
ANISOU 2613  O   LEU A 361    11318   6618   4345  -1250   -501   1379       O  
ATOM   2614  CB  LEU A 361     -30.317 -27.200  13.230  1.00 55.29           C  
ANISOU 2614  CB  LEU A 361    10831   6617   3559  -1616   -281   1588       C  
ATOM   2615  CG  LEU A 361     -31.086 -28.236  14.059  1.00 58.02           C  
ANISOU 2615  CG  LEU A 361    11193   7044   3807  -1756   -251   1789       C  
ATOM   2616  CD1 LEU A 361     -32.567 -27.892  14.120  1.00 58.42           C  
ANISOU 2616  CD1 LEU A 361    11128   7250   3819  -1948    -66   1772       C  
ATOM   2617  CD2 LEU A 361     -30.883 -29.640  13.508  1.00 58.59           C  
ANISOU 2617  CD2 LEU A 361    11372   6832   4059  -1737   -380   1954       C  
ATOM   2618  N   LEU A 362     -27.786 -25.270  12.786  1.00 52.22           N  
ANISOU 2618  N   LEU A 362    10401   6216   3223  -1248   -442   1215       N  
ATOM   2619  CA  LEU A 362     -27.098 -24.204  12.064  1.00 56.54           C  
ANISOU 2619  CA  LEU A 362    10780   6712   3992  -1107   -449    993       C  
ATOM   2620  C   LEU A 362     -25.801 -24.719  11.450  1.00 50.84           C  
ANISOU 2620  C   LEU A 362    10139   5805   3370   -943   -613   1030       C  
ATOM   2621  O   LEU A 362     -25.511 -24.457  10.284  1.00 47.82           O  
ANISOU 2621  O   LEU A 362     9685   5274   3211   -869   -617    968       O  
ATOM   2622  CB  LEU A 362     -26.806 -23.014  12.986  1.00 60.85           C  
ANISOU 2622  CB  LEU A 362    11163   7493   4463  -1062   -414    772       C  
ATOM   2623  CG  LEU A 362     -27.873 -21.920  13.104  1.00 50.63           C  
ANISOU 2623  CG  LEU A 362     9679   6340   3217  -1147   -250    597       C  
ATOM   2624  CD1 LEU A 362     -27.285 -20.648  13.695  1.00 50.90           C  
ANISOU 2624  CD1 LEU A 362     9538   6522   3281  -1051   -261    329       C  
ATOM   2625  CD2 LEU A 362     -28.512 -21.634  11.760  1.00 48.62           C  
ANISOU 2625  CD2 LEU A 362     9347   5900   3228  -1173   -174    583       C  
ATOM   2626  N   GLU A 363     -25.033 -25.464  12.242  1.00 56.40           N  
ANISOU 2626  N   GLU A 363    10989   6540   3899   -882   -749   1135       N  
ATOM   2627  CA  GLU A 363     -23.744 -25.990  11.798  1.00 58.68           C  
ANISOU 2627  CA  GLU A 363    11349   6684   4263   -707   -921   1155       C  
ATOM   2628  C   GLU A 363     -23.901 -27.020  10.683  1.00 60.57           C  
ANISOU 2628  C   GLU A 363    11713   6662   4640   -697   -975   1290       C  
ATOM   2629  O   GLU A 363     -22.939 -27.348   9.990  1.00 65.56           O  
ANISOU 2629  O   GLU A 363    12361   7164   5385   -540  -1094   1264       O  
ATOM   2630  CB  GLU A 363     -22.984 -26.607  12.973  1.00 58.72           C  
ANISOU 2630  CB  GLU A 363    11490   6786   4034   -641  -1067   1248       C  
ATOM   2631  CG  GLU A 363     -22.562 -25.604  14.033  1.00 75.06           C  
ANISOU 2631  CG  GLU A 363    13426   9124   5971   -606  -1052   1074       C  
ATOM   2632  CD  GLU A 363     -21.690 -26.222  15.110  1.00 87.77           C  
ANISOU 2632  CD  GLU A 363    15163  10837   7347   -513  -1219   1162       C  
ATOM   2633  OE1 GLU A 363     -20.649 -26.820  14.764  1.00 96.83           O  
ANISOU 2633  OE1 GLU A 363    16370  11849   8573   -357  -1378   1196       O  
ATOM   2634  OE2 GLU A 363     -22.046 -26.108  16.301  1.00 85.24           O  
ANISOU 2634  OE2 GLU A 363    14837  10754   6796   -581  -1182   1180       O  
ATOM   2635  N   ILE A 364     -25.117 -27.526  10.516  1.00 58.99           N  
ANISOU 2635  N   ILE A 364    11508   6412   4494   -848   -875   1382       N  
ATOM   2636  CA  ILE A 364     -25.415 -28.472   9.450  1.00 60.20           C  
ANISOU 2636  CA  ILE A 364    11686   6342   4846   -842   -907   1441       C  
ATOM   2637  C   ILE A 364     -25.991 -27.767   8.225  1.00 62.06           C  
ANISOU 2637  C   ILE A 364    11833   6518   5229   -873   -802   1351       C  
ATOM   2638  O   ILE A 364     -25.527 -27.977   7.105  1.00 61.58           O  
ANISOU 2638  O   ILE A 364    11765   6316   5318   -762   -861   1309       O  
ATOM   2639  CB  ILE A 364     -26.405 -29.552   9.920  1.00 55.50           C  
ANISOU 2639  CB  ILE A 364    11137   5713   4237   -991   -883   1597       C  
ATOM   2640  CG1 ILE A 364     -25.776 -30.410  11.018  1.00 57.27           C  
ANISOU 2640  CG1 ILE A 364    11459   5963   4337   -946  -1005   1723       C  
ATOM   2641  CG2 ILE A 364     -26.834 -30.425   8.752  1.00 55.21           C  
ANISOU 2641  CG2 ILE A 364    11119   5454   4404   -999   -915   1620       C  
ATOM   2642  CD1 ILE A 364     -26.698 -31.482  11.554  1.00 56.68           C  
ANISOU 2642  CD1 ILE A 364    11437   5859   4241  -1101   -987   1907       C  
ATOM   2643  N   PHE A 365     -26.997 -26.926   8.451  1.00 65.56           N  
ANISOU 2643  N   PHE A 365    12206   7086   5617  -1017   -646   1318       N  
ATOM   2644  CA  PHE A 365     -27.692 -26.231   7.369  1.00 51.54           C  
ANISOU 2644  CA  PHE A 365    10307   5273   4004  -1052   -534   1231       C  
ATOM   2645  C   PHE A 365     -26.771 -25.304   6.581  1.00 44.10           C  
ANISOU 2645  C   PHE A 365     9208   4325   3223   -893   -546   1073       C  
ATOM   2646  O   PHE A 365     -27.046 -24.980   5.425  1.00 42.72           O  
ANISOU 2646  O   PHE A 365     8940   4079   3212   -872   -499   1026       O  
ATOM   2647  CB  PHE A 365     -28.872 -25.427   7.921  1.00 45.92           C  
ANISOU 2647  CB  PHE A 365     9473   4734   3239  -1205   -366   1173       C  
ATOM   2648  CG  PHE A 365     -29.996 -26.274   8.446  1.00 55.05           C  
ANISOU 2648  CG  PHE A 365    10727   5914   4274  -1391   -317   1327       C  
ATOM   2649  CD1 PHE A 365     -30.149 -27.586   8.027  1.00 48.17           C  
ANISOU 2649  CD1 PHE A 365     9906   4880   3515  -1395   -399   1431       C  
ATOM   2650  CD2 PHE A 365     -30.903 -25.755   9.357  1.00 53.51           C  
ANISOU 2650  CD2 PHE A 365    10461   5936   3934  -1531   -184   1303       C  
ATOM   2651  CE1 PHE A 365     -31.186 -28.364   8.511  1.00 58.20           C  
ANISOU 2651  CE1 PHE A 365    11182   6183   4750  -1557   -353   1543       C  
ATOM   2652  CE2 PHE A 365     -31.941 -26.527   9.843  1.00 50.14           C  
ANISOU 2652  CE2 PHE A 365    10042   5565   3444  -1694   -127   1426       C  
ATOM   2653  CZ  PHE A 365     -32.082 -27.832   9.419  1.00 58.73           C  
ANISOU 2653  CZ  PHE A 365    11186   6471   4657  -1709   -213   1552       C  
ATOM   2654  N   VAL A 366     -25.681 -24.879   7.211  1.00 53.65           N  
ANISOU 2654  N   VAL A 366    10382   5621   4383   -787   -612    998       N  
ATOM   2655  CA  VAL A 366     -24.718 -23.993   6.570  1.00 50.93           C  
ANISOU 2655  CA  VAL A 366     9877   5283   4191   -655   -627    862       C  
ATOM   2656  C   VAL A 366     -24.033 -24.689   5.388  1.00 54.09           C  
ANISOU 2656  C   VAL A 366    10319   5537   4694   -530   -720    901       C  
ATOM   2657  O   VAL A 366     -23.587 -24.035   4.445  1.00 58.03           O  
ANISOU 2657  O   VAL A 366    10674   6032   5344   -455   -694    823       O  
ATOM   2658  CB  VAL A 366     -23.654 -23.498   7.585  1.00 51.77           C  
ANISOU 2658  CB  VAL A 366     9938   5518   4215   -574   -696    769       C  
ATOM   2659  CG1 VAL A 366     -22.786 -24.655   8.072  1.00 59.31           C  
ANISOU 2659  CG1 VAL A 366    11070   6434   5030   -480   -861    870       C  
ATOM   2660  CG2 VAL A 366     -22.802 -22.391   6.987  1.00 43.10           C  
ANISOU 2660  CG2 VAL A 366     8639   4438   3298   -482   -688    622       C  
ATOM   2661  N   TRP A 367     -23.971 -26.017   5.433  1.00 52.07           N  
ANISOU 2661  N   TRP A 367    10257   5168   4358   -508   -830   1023       N  
ATOM   2662  CA  TRP A 367     -23.312 -26.785   4.381  1.00 53.34           C  
ANISOU 2662  CA  TRP A 367    10465   5198   4605   -368   -938   1033       C  
ATOM   2663  C   TRP A 367     -24.253 -27.067   3.218  1.00 61.48           C  
ANISOU 2663  C   TRP A 367    11491   6126   5742   -424   -878   1056       C  
ATOM   2664  O   TRP A 367     -23.810 -27.349   2.104  1.00 68.21           O  
ANISOU 2664  O   TRP A 367    12311   6919   6687   -306   -926   1015       O  
ATOM   2665  CB  TRP A 367     -22.754 -28.093   4.944  1.00 49.66           C  
ANISOU 2665  CB  TRP A 367    10210   4628   4032   -295  -1114   1134       C  
ATOM   2666  CG  TRP A 367     -21.552 -27.874   5.797  1.00 45.93           C  
ANISOU 2666  CG  TRP A 367     9721   4258   3474   -179  -1209   1088       C  
ATOM   2667  CD1 TRP A 367     -21.508 -27.841   7.158  1.00 47.25           C  
ANISOU 2667  CD1 TRP A 367     9955   4524   3473   -230  -1234   1137       C  
ATOM   2668  CD2 TRP A 367     -20.217 -27.630   5.346  1.00 63.19           C  
ANISOU 2668  CD2 TRP A 367    11796   6485   5727     10  -1290    974       C  
ATOM   2669  NE1 TRP A 367     -20.225 -27.601   7.585  1.00 47.79           N  
ANISOU 2669  NE1 TRP A 367     9969   4681   3507    -79  -1338   1054       N  
ATOM   2670  CE2 TRP A 367     -19.411 -27.465   6.488  1.00 46.83           C  
ANISOU 2670  CE2 TRP A 367     9733   4523   3537     65  -1372    952       C  
ATOM   2671  CE3 TRP A 367     -19.622 -27.536   4.082  1.00 44.76           C  
ANISOU 2671  CE3 TRP A 367     9345   4132   3532    136  -1300    887       C  
ATOM   2672  CZ2 TRP A 367     -18.043 -27.215   6.410  1.00 47.06           C  
ANISOU 2672  CZ2 TRP A 367     9654   4628   3599    237  -1466    841       C  
ATOM   2673  CZ3 TRP A 367     -18.264 -27.288   4.007  1.00 45.05           C  
ANISOU 2673  CZ3 TRP A 367     9270   4256   3590    301  -1381    787       C  
ATOM   2674  CH2 TRP A 367     -17.490 -27.129   5.162  1.00 46.16           C  
ANISOU 2674  CH2 TRP A 367     9417   4491   3630    347  -1465    761       C  
ATOM   2675  N   ILE A 368     -25.552 -26.996   3.481  1.00 59.59           N  
ANISOU 2675  N   ILE A 368    11272   5890   5479   -600   -773   1110       N  
ATOM   2676  CA  ILE A 368     -26.540 -27.085   2.417  1.00 52.36           C  
ANISOU 2676  CA  ILE A 368    10319   4907   4666   -665   -704   1113       C  
ATOM   2677  C   ILE A 368     -26.515 -25.781   1.630  1.00 52.76           C  
ANISOU 2677  C   ILE A 368    10151   5058   4839   -627   -595   1004       C  
ATOM   2678  O   ILE A 368     -26.725 -25.762   0.419  1.00 53.48           O  
ANISOU 2678  O   ILE A 368    10178   5115   5029   -585   -578    981       O  
ATOM   2679  CB  ILE A 368     -27.951 -27.357   2.971  1.00 56.74           C  
ANISOU 2679  CB  ILE A 368    10897   5477   5186   -864   -617   1176       C  
ATOM   2680  CG1 ILE A 368     -27.934 -28.603   3.860  1.00 44.36           C  
ANISOU 2680  CG1 ILE A 368     9445   3858   3552   -902   -710   1264       C  
ATOM   2681  CG2 ILE A 368     -28.959 -27.513   1.837  1.00 41.76           C  
ANISOU 2681  CG2 ILE A 368     8939   3521   3407   -918   -562   1157       C  
ATOM   2682  CD1 ILE A 368     -29.286 -28.987   4.406  1.00 45.42           C  
ANISOU 2682  CD1 ILE A 368     9578   4024   3655  -1102   -626   1339       C  
ATOM   2683  N   GLY A 369     -26.233 -24.690   2.334  1.00 51.01           N  
ANISOU 2683  N   GLY A 369     9814   4958   4610   -640   -531    940       N  
ATOM   2684  CA  GLY A 369     -26.115 -23.387   1.712  1.00 41.72           C  
ANISOU 2684  CA  GLY A 369     8432   3850   3569   -610   -444    852       C  
ATOM   2685  C   GLY A 369     -24.798 -23.228   0.978  1.00 46.13           C  
ANISOU 2685  C   GLY A 369     8913   4417   4197   -453   -511    815       C  
ATOM   2686  O   GLY A 369     -24.760 -22.689  -0.130  1.00 53.93           O  
ANISOU 2686  O   GLY A 369     9774   5418   5299   -412   -464    801       O  
ATOM   2687  N   TYR A 370     -23.717 -23.690   1.602  1.00 51.88           N  
ANISOU 2687  N   TYR A 370     9710   5156   4847   -363   -620    805       N  
ATOM   2688  CA  TYR A 370     -22.388 -23.629   1.001  1.00 45.59           C  
ANISOU 2688  CA  TYR A 370     8830   4393   4100   -208   -690    761       C  
ATOM   2689  C   TYR A 370     -22.365 -24.306  -0.364  1.00 47.37           C  
ANISOU 2689  C   TYR A 370     9064   4568   4365   -121   -719    783       C  
ATOM   2690  O   TYR A 370     -21.955 -23.701  -1.358  1.00 51.80           O  
ANISOU 2690  O   TYR A 370     9468   5198   5015    -62   -674    757       O  
ATOM   2691  CB  TYR A 370     -21.351 -24.277   1.919  1.00 47.18           C  
ANISOU 2691  CB  TYR A 370     9131   4604   4192   -115   -826    749       C  
ATOM   2692  CG  TYR A 370     -20.867 -23.395   3.053  1.00 44.32           C  
ANISOU 2692  CG  TYR A 370     8690   4347   3804   -143   -818    680       C  
ATOM   2693  CD1 TYR A 370     -21.061 -22.020   3.026  1.00 46.95           C  
ANISOU 2693  CD1 TYR A 370     8841   4746   4254   -215   -707    608       C  
ATOM   2694  CD2 TYR A 370     -20.200 -23.939   4.144  1.00 50.87           C  
ANISOU 2694  CD2 TYR A 370     9625   5203   4498    -88   -935    679       C  
ATOM   2695  CE1 TYR A 370     -20.612 -21.212   4.058  1.00 49.10           C  
ANISOU 2695  CE1 TYR A 370     9032   5106   4517   -234   -714    513       C  
ATOM   2696  CE2 TYR A 370     -19.749 -23.139   5.181  1.00 55.36           C  
ANISOU 2696  CE2 TYR A 370    10113   5887   5032   -104   -938    593       C  
ATOM   2697  CZ  TYR A 370     -19.956 -21.777   5.131  1.00 52.84           C  
ANISOU 2697  CZ  TYR A 370     9608   5631   4840   -178   -827    497       C  
ATOM   2698  OH  TYR A 370     -19.510 -20.978   6.160  1.00 55.66           O  
ANISOU 2698  OH  TYR A 370     9877   6095   5176   -190   -844    382       O  
ATOM   2699  N   VAL A 371     -22.820 -25.556  -0.411  1.00 44.45           N  
ANISOU 2699  N   VAL A 371     8875   4085   3930   -117   -796    832       N  
ATOM   2700  CA  VAL A 371     -22.864 -26.303  -1.664  1.00 46.35           C  
ANISOU 2700  CA  VAL A 371     9134   4273   4203    -26   -843    823       C  
ATOM   2701  C   VAL A 371     -23.874 -25.676  -2.628  1.00 47.19           C  
ANISOU 2701  C   VAL A 371     9130   4413   4388   -107   -717    831       C  
ATOM   2702  O   VAL A 371     -23.749 -25.813  -3.842  1.00 48.82           O  
ANISOU 2702  O   VAL A 371     9267   4655   4627    -17   -722    802       O  
ATOM   2703  CB  VAL A 371     -23.211 -27.797  -1.429  1.00 60.17           C  
ANISOU 2703  CB  VAL A 371    11111   5856   5896    -20   -972    868       C  
ATOM   2704  CG1 VAL A 371     -24.655 -27.961  -0.990  1.00 63.80           C  
ANISOU 2704  CG1 VAL A 371    11663   6236   6341   -218   -903    948       C  
ATOM   2705  CG2 VAL A 371     -22.919 -28.630  -2.674  1.00 52.85           C  
ANISOU 2705  CG2 VAL A 371    10195   4881   5005    127  -1062    806       C  
ATOM   2706  N   SER A 372     -24.866 -24.972  -2.091  1.00 47.24           N  
ANISOU 2706  N   SER A 372     9109   4425   4413   -263   -610    861       N  
ATOM   2707  CA  SER A 372     -25.829 -24.280  -2.939  1.00 42.01           C  
ANISOU 2707  CA  SER A 372     8332   3797   3832   -331   -499    868       C  
ATOM   2708  C   SER A 372     -25.148 -23.121  -3.654  1.00 39.82           C  
ANISOU 2708  C   SER A 372     7854   3633   3645   -263   -439    850       C  
ATOM   2709  O   SER A 372     -25.332 -22.929  -4.854  1.00 45.94           O  
ANISOU 2709  O   SER A 372     8538   4455   4463   -221   -406    864       O  
ATOM   2710  CB  SER A 372     -27.019 -23.776  -2.122  1.00 43.58           C  
ANISOU 2710  CB  SER A 372     8534   3988   4035   -500   -404    887       C  
ATOM   2711  OG  SER A 372     -27.920 -23.041  -2.934  1.00 36.39           O  
ANISOU 2711  OG  SER A 372     7500   3112   3216   -547   -309    886       O  
ATOM   2712  N   SER A 373     -24.354 -22.357  -2.911  1.00 44.95           N  
ANISOU 2712  N   SER A 373     8431   4330   4320   -259   -429    824       N  
ATOM   2713  CA  SER A 373     -23.609 -21.243  -3.488  1.00 43.84           C  
ANISOU 2713  CA  SER A 373     8094   4279   4283   -217   -381    822       C  
ATOM   2714  C   SER A 373     -22.445 -21.742  -4.336  1.00 48.00           C  
ANISOU 2714  C   SER A 373     8577   4883   4777    -66   -446    815       C  
ATOM   2715  O   SER A 373     -22.167 -21.206  -5.404  1.00 65.15           O  
ANISOU 2715  O   SER A 373    10603   7148   7003    -26   -397    849       O  
ATOM   2716  CB  SER A 373     -23.091 -20.312  -2.389  1.00 36.78           C  
ANISOU 2716  CB  SER A 373     7130   3403   3441   -264   -367    774       C  
ATOM   2717  OG  SER A 373     -24.146 -19.579  -1.791  1.00 38.57           O  
ANISOU 2717  OG  SER A 373     7339   3594   3722   -387   -291    757       O  
ATOM   2718  N   GLY A 374     -21.775 -22.780  -3.849  1.00 42.94           N  
ANISOU 2718  N   GLY A 374     8061   4216   4040     21   -559    772       N  
ATOM   2719  CA  GLY A 374     -20.580 -23.301  -4.487  1.00 44.97           C  
ANISOU 2719  CA  GLY A 374     8270   4557   4260    185   -636    732       C  
ATOM   2720  C   GLY A 374     -20.755 -23.809  -5.906  1.00 50.84           C  
ANISOU 2720  C   GLY A 374     8981   5356   4979    275   -636    732       C  
ATOM   2721  O   GLY A 374     -19.968 -23.470  -6.789  1.00 56.33           O  
ANISOU 2721  O   GLY A 374     9516   6206   5682    364   -612    725       O  
ATOM   2722  N   VAL A 375     -21.779 -24.626  -6.131  1.00 51.31           N  
ANISOU 2722  N   VAL A 375     9181   5310   5005    248   -664    735       N  
ATOM   2723  CA  VAL A 375     -21.982 -25.233  -7.442  1.00 55.38           C  
ANISOU 2723  CA  VAL A 375     9678   5878   5487    345   -686    702       C  
ATOM   2724  C   VAL A 375     -22.953 -24.425  -8.302  1.00 64.53           C  
ANISOU 2724  C   VAL A 375    10727   7101   6691    259   -566    766       C  
ATOM   2725  O   VAL A 375     -23.284 -24.830  -9.416  1.00 79.31           O  
ANISOU 2725  O   VAL A 375    12572   9036   8524    326   -576    741       O  
ATOM   2726  CB  VAL A 375     -22.507 -26.681  -7.319  1.00 54.30           C  
ANISOU 2726  CB  VAL A 375     9751   5576   5306    376   -812    651       C  
ATOM   2727  CG1 VAL A 375     -21.660 -27.473  -6.332  1.00 56.58           C  
ANISOU 2727  CG1 VAL A 375    10172   5767   5558    452   -945    615       C  
ATOM   2728  CG2 VAL A 375     -23.970 -26.689  -6.899  1.00 48.14           C  
ANISOU 2728  CG2 VAL A 375     9072   4663   4556    195   -762    711       C  
ATOM   2729  N   ASN A 376     -23.394 -23.280  -7.789  1.00 59.55           N  
ANISOU 2729  N   ASN A 376    10027   6457   6142    123   -465    838       N  
ATOM   2730  CA  ASN A 376     -24.416 -22.481  -8.465  1.00 52.38           C  
ANISOU 2730  CA  ASN A 376     9028   5580   5295     39   -365    905       C  
ATOM   2731  C   ASN A 376     -24.017 -21.935  -9.842  1.00 58.16           C  
ANISOU 2731  C   ASN A 376     9582   6494   6022    119   -315    958       C  
ATOM   2732  O   ASN A 376     -24.797 -22.047 -10.787  1.00 66.61           O  
ANISOU 2732  O   ASN A 376    10631   7613   7066    129   -296    977       O  
ATOM   2733  CB  ASN A 376     -24.856 -21.318  -7.571  1.00 49.02           C  
ANISOU 2733  CB  ASN A 376     8554   5095   4977   -102   -283    950       C  
ATOM   2734  CG  ASN A 376     -25.835 -20.392  -8.267  1.00 50.65           C  
ANISOU 2734  CG  ASN A 376     8652   5326   5268   -169   -193   1021       C  
ATOM   2735  OD1 ASN A 376     -25.503 -19.253  -8.601  1.00 51.99           O  
ANISOU 2735  OD1 ASN A 376     8669   5552   5532   -182   -133   1091       O  
ATOM   2736  ND2 ASN A 376     -27.052 -20.879  -8.492  1.00 37.28           N  
ANISOU 2736  ND2 ASN A 376     7033   3583   3549   -214   -191   1008       N  
ATOM   2737  N   PRO A 377     -22.819 -21.329  -9.967  1.00 58.19           N  
ANISOU 2737  N   PRO A 377     9448   6616   6044    168   -293    988       N  
ATOM   2738  CA  PRO A 377     -22.473 -20.845 -11.310  1.00 54.59           C  
ANISOU 2738  CA  PRO A 377     8818   6362   5562    231   -237   1065       C  
ATOM   2739  C   PRO A 377     -22.266 -21.979 -12.313  1.00 62.59           C  
ANISOU 2739  C   PRO A 377     9852   7504   6425    390   -302    980       C  
ATOM   2740  O   PRO A 377     -22.559 -21.804 -13.493  1.00 70.60           O  
ANISOU 2740  O   PRO A 377    10770   8674   7382    431   -262   1030       O  
ATOM   2741  CB  PRO A 377     -21.167 -20.074 -11.081  1.00 47.34           C  
ANISOU 2741  CB  PRO A 377     7750   5538   4700    234   -206   1108       C  
ATOM   2742  CG  PRO A 377     -21.176 -19.731  -9.636  1.00 51.17           C  
ANISOU 2742  CG  PRO A 377     8311   5846   5285    135   -223   1072       C  
ATOM   2743  CD  PRO A 377     -21.820 -20.905  -8.972  1.00 54.78           C  
ANISOU 2743  CD  PRO A 377     8986   6163   5666    150   -305    971       C  
ATOM   2744  N   LEU A 378     -21.772 -23.122 -11.848  1.00 66.78           N  
ANISOU 2744  N   LEU A 378    10507   7972   6893    485   -413    848       N  
ATOM   2745  CA  LEU A 378     -21.577 -24.277 -12.717  1.00 60.39           C  
ANISOU 2745  CA  LEU A 378     9730   7255   5963    652   -501    727       C  
ATOM   2746  C   LEU A 378     -22.909 -24.739 -13.292  1.00 51.74           C  
ANISOU 2746  C   LEU A 378     8717   6095   4846    622   -516    705       C  
ATOM   2747  O   LEU A 378     -23.073 -24.820 -14.508  1.00 53.82           O  
ANISOU 2747  O   LEU A 378     8888   6536   5026    706   -504    688       O  
ATOM   2748  CB  LEU A 378     -20.903 -25.424 -11.958  1.00 59.03           C  
ANISOU 2748  CB  LEU A 378     9701   6962   5764    754   -641    592       C  
ATOM   2749  CG  LEU A 378     -20.538 -26.660 -12.785  1.00 48.79           C  
ANISOU 2749  CG  LEU A 378     8433   5739   4365    956   -759    430       C  
ATOM   2750  CD1 LEU A 378     -19.399 -26.347 -13.745  1.00 45.94           C  
ANISOU 2750  CD1 LEU A 378     7850   5693   3912   1103   -718    401       C  
ATOM   2751  CD2 LEU A 378     -20.176 -27.831 -11.882  1.00 42.05           C  
ANISOU 2751  CD2 LEU A 378     7771   4678   3527   1031   -921    318       C  
ATOM   2752  N   VAL A 379     -23.857 -25.029 -12.405  1.00 47.86           N  
ANISOU 2752  N   VAL A 379     8390   5370   4424    499   -543    705       N  
ATOM   2753  CA  VAL A 379     -25.196 -25.456 -12.798  1.00 52.84           C  
ANISOU 2753  CA  VAL A 379     9098   5921   5058    441   -559    682       C  
ATOM   2754  C   VAL A 379     -25.845 -24.460 -13.759  1.00 38.22           C  
ANISOU 2754  C   VAL A 379     7091   4224   3207    402   -452    781       C  
ATOM   2755  O   VAL A 379     -26.531 -24.851 -14.701  1.00 47.07           O  
ANISOU 2755  O   VAL A 379     8198   5414   4272    446   -478    734       O  
ATOM   2756  CB  VAL A 379     -26.101 -25.648 -11.558  1.00 37.85           C  
ANISOU 2756  CB  VAL A 379     7360   3780   3240    275   -567    704       C  
ATOM   2757  CG1 VAL A 379     -27.544 -25.892 -11.968  1.00 42.84           C  
ANISOU 2757  CG1 VAL A 379     8031   4355   3893    187   -561    695       C  
ATOM   2758  CG2 VAL A 379     -25.588 -26.798 -10.709  1.00 38.48           C  
ANISOU 2758  CG2 VAL A 379     7617   3699   3306    316   -694    627       C  
ATOM   2759  N   TYR A 380     -25.602 -23.175 -13.528  1.00 42.78           N  
ANISOU 2759  N   TYR A 380     7548   4851   3854    326   -346    915       N  
ATOM   2760  CA  TYR A 380     -26.165 -22.120 -14.365  1.00 37.61           C  
ANISOU 2760  CA  TYR A 380     6749   4319   3222    286   -254   1041       C  
ATOM   2761  C   TYR A 380     -25.544 -22.103 -15.762  1.00 47.00           C  
ANISOU 2761  C   TYR A 380     7791   5784   4282    426   -243   1065       C  
ATOM   2762  O   TYR A 380     -26.257 -22.091 -16.765  1.00 39.15           O  
ANISOU 2762  O   TYR A 380     6746   4907   3222    458   -236   1085       O  
ATOM   2763  CB  TYR A 380     -25.978 -20.759 -13.689  1.00 42.44           C  
ANISOU 2763  CB  TYR A 380     7276   4877   3973    170   -164   1173       C  
ATOM   2764  CG  TYR A 380     -26.592 -19.594 -14.437  1.00 52.57           C  
ANISOU 2764  CG  TYR A 380     8421   6236   5317    121    -84   1325       C  
ATOM   2765  CD1 TYR A 380     -27.961 -19.528 -14.660  1.00 51.48           C  
ANISOU 2765  CD1 TYR A 380     8314   6040   5207     69    -80   1329       C  
ATOM   2766  CD2 TYR A 380     -25.801 -18.552 -14.908  1.00 55.87           C  
ANISOU 2766  CD2 TYR A 380     8674   6779   5774    123    -20   1475       C  
ATOM   2767  CE1 TYR A 380     -28.525 -18.461 -15.339  1.00 49.44           C  
ANISOU 2767  CE1 TYR A 380     7933   5842   5010     41    -24   1474       C  
ATOM   2768  CE2 TYR A 380     -26.355 -17.482 -15.586  1.00 53.83           C  
ANISOU 2768  CE2 TYR A 380     8300   6568   5585     78     39   1640       C  
ATOM   2769  CZ  TYR A 380     -27.718 -17.440 -15.798  1.00 57.47           C  
ANISOU 2769  CZ  TYR A 380     8801   6964   6069     47     31   1637       C  
ATOM   2770  OH  TYR A 380     -28.274 -16.375 -16.473  1.00 64.83           O  
ANISOU 2770  OH  TYR A 380     9622   7937   7075     19     73   1806       O  
ATOM   2771  N   THR A 381     -24.216 -22.112 -15.815  1.00 42.95           N  
ANISOU 2771  N   THR A 381     7201   5398   3721    511   -242   1058       N  
ATOM   2772  CA  THR A 381     -23.479 -22.008 -17.070  1.00 40.64           C  
ANISOU 2772  CA  THR A 381     6739   5414   3289    637   -212   1092       C  
ATOM   2773  C   THR A 381     -23.573 -23.257 -17.943  1.00 48.88           C  
ANISOU 2773  C   THR A 381     7820   6583   4169    805   -306    912       C  
ATOM   2774  O   THR A 381     -23.285 -23.204 -19.139  1.00 52.10           O  
ANISOU 2774  O   THR A 381     8085   7281   4429    914   -280    926       O  
ATOM   2775  CB  THR A 381     -21.993 -21.714 -16.808  1.00 41.22           C  
ANISOU 2775  CB  THR A 381     6703   5601   3360    677   -185   1114       C  
ATOM   2776  OG1 THR A 381     -21.481 -22.660 -15.862  1.00 40.99           O  
ANISOU 2776  OG1 THR A 381     6811   5419   3345    731   -285    949       O  
ATOM   2777  CG2 THR A 381     -21.814 -20.316 -16.255  1.00 51.62           C  
ANISOU 2777  CG2 THR A 381     7929   6848   4837    519    -89   1302       C  
ATOM   2778  N   LEU A 382     -23.976 -24.375 -17.347  1.00 52.81           N  
ANISOU 2778  N   LEU A 382     8505   6868   4693    824   -419    744       N  
ATOM   2779  CA  LEU A 382     -24.025 -25.650 -18.061  1.00 56.05           C  
ANISOU 2779  CA  LEU A 382     8966   7343   4987    987   -538    538       C  
ATOM   2780  C   LEU A 382     -25.143 -25.712 -19.098  1.00 59.83           C  
ANISOU 2780  C   LEU A 382     9414   7922   5396    996   -541    524       C  
ATOM   2781  O   LEU A 382     -25.140 -26.585 -19.964  1.00 78.45           O  
ANISOU 2781  O   LEU A 382    11762  10412   7635   1149   -628    352       O  
ATOM   2782  CB  LEU A 382     -24.178 -26.809 -17.072  1.00 55.84           C  
ANISOU 2782  CB  LEU A 382     9160   7014   5041    983   -672    389       C  
ATOM   2783  CG  LEU A 382     -22.896 -27.337 -16.427  1.00 50.56           C  
ANISOU 2783  CG  LEU A 382     8528   6308   4374   1087   -743    304       C  
ATOM   2784  CD1 LEU A 382     -23.214 -28.414 -15.399  1.00 49.89           C  
ANISOU 2784  CD1 LEU A 382     8680   5894   4381   1056   -879    207       C  
ATOM   2785  CD2 LEU A 382     -21.948 -27.865 -17.488  1.00 49.65           C  
ANISOU 2785  CD2 LEU A 382     8287   6470   4110   1319   -793    155       C  
ATOM   2786  N   PHE A 383     -26.098 -24.793 -19.009  1.00 52.46           N  
ANISOU 2786  N   PHE A 383     8459   6931   4541    845   -457    685       N  
ATOM   2787  CA  PHE A 383     -27.179 -24.727 -19.989  1.00 51.38           C  
ANISOU 2787  CA  PHE A 383     8275   6906   4340    853   -459    688       C  
ATOM   2788  C   PHE A 383     -26.759 -23.897 -21.194  1.00 51.35           C  
ANISOU 2788  C   PHE A 383     8063   7256   4192    932   -374    825       C  
ATOM   2789  O   PHE A 383     -27.503 -23.763 -22.163  1.00 59.29           O  
ANISOU 2789  O   PHE A 383     9000   8423   5104    966   -375    845       O  
ATOM   2790  CB  PHE A 383     -28.446 -24.156 -19.358  1.00 41.17           C  
ANISOU 2790  CB  PHE A 383     7047   5400   3197    669   -420    786       C  
ATOM   2791  CG  PHE A 383     -29.058 -25.057 -18.329  1.00 45.10           C  
ANISOU 2791  CG  PHE A 383     7737   5595   3804    580   -501    660       C  
ATOM   2792  CD1 PHE A 383     -28.647 -25.002 -17.010  1.00 44.49           C  
ANISOU 2792  CD1 PHE A 383     7759   5308   3835    487   -487    691       C  
ATOM   2793  CD2 PHE A 383     -30.033 -25.974 -18.686  1.00 49.14           C  
ANISOU 2793  CD2 PHE A 383     8324   6042   4304    584   -596    516       C  
ATOM   2794  CE1 PHE A 383     -29.203 -25.839 -16.061  1.00 49.54           C  
ANISOU 2794  CE1 PHE A 383     8575   5691   4556    395   -557    606       C  
ATOM   2795  CE2 PHE A 383     -30.593 -26.813 -17.744  1.00 45.43           C  
ANISOU 2795  CE2 PHE A 383     8028   5294   3941    480   -667    428       C  
ATOM   2796  CZ  PHE A 383     -30.179 -26.746 -16.430  1.00 49.09           C  
ANISOU 2796  CZ  PHE A 383     8593   5562   4496    383   -644    486       C  
ATOM   2797  N   ASN A 384     -25.555 -23.341 -21.119  1.00 53.23           N  
ANISOU 2797  N   ASN A 384     8194   7624   4407    954   -302    927       N  
ATOM   2798  CA  ASN A 384     -24.954 -22.641 -22.244  1.00 53.06           C  
ANISOU 2798  CA  ASN A 384     7963   7966   4231   1026   -217   1071       C  
ATOM   2799  C   ASN A 384     -23.950 -23.549 -22.942  1.00 50.37           C  
ANISOU 2799  C   ASN A 384     7549   7896   3691   1231   -268    887       C  
ATOM   2800  O   ASN A 384     -23.044 -24.084 -22.305  1.00 49.74           O  
ANISOU 2800  O   ASN A 384     7512   7742   3645   1283   -309    767       O  
ATOM   2801  CB  ASN A 384     -24.279 -21.353 -21.776  1.00 52.26           C  
ANISOU 2801  CB  ASN A 384     7760   7852   4244    901    -99   1318       C  
ATOM   2802  CG  ASN A 384     -23.717 -20.544 -22.921  1.00 54.87           C  
ANISOU 2802  CG  ASN A 384     7871   8547   4429    938     -2   1520       C  
ATOM   2803  OD1 ASN A 384     -22.618 -20.813 -23.404  1.00 50.55           O  
ANISOU 2803  OD1 ASN A 384     7202   8270   3734   1048     19   1480       O  
ATOM   2804  ND2 ASN A 384     -24.468 -19.542 -23.362  1.00 66.26           N  
ANISOU 2804  ND2 ASN A 384     9253  10011   5912    847     56   1747       N  
ATOM   2805  N   LYS A 385     -24.115 -23.721 -24.251  1.00 56.28           N  
ANISOU 2805  N   LYS A 385     8181   8974   4228   1359   -272    853       N  
ATOM   2806  CA  LYS A 385     -23.315 -24.685 -25.002  1.00 50.27           C  
ANISOU 2806  CA  LYS A 385     7345   8495   3262   1581   -336    624       C  
ATOM   2807  C   LYS A 385     -21.837 -24.317 -25.058  1.00 51.26           C  
ANISOU 2807  C   LYS A 385     7304   8862   3309   1634   -251    694       C  
ATOM   2808  O   LYS A 385     -20.970 -25.188 -24.971  1.00 52.11           O  
ANISOU 2808  O   LYS A 385     7408   9033   3358   1787   -322    471       O  
ATOM   2809  CB  LYS A 385     -23.855 -24.834 -26.425  1.00 52.03           C  
ANISOU 2809  CB  LYS A 385     7456   9062   3250   1704   -351    579       C  
ATOM   2810  CG  LYS A 385     -23.095 -25.863 -27.246  1.00 60.01           C  
ANISOU 2810  CG  LYS A 385     8378  10388   4035   1955   -427    298       C  
ATOM   2811  CD  LYS A 385     -23.544 -25.889 -28.691  1.00 65.40           C  
ANISOU 2811  CD  LYS A 385     8921  11478   4451   2082   -429    265       C  
ATOM   2812  CE  LYS A 385     -22.692 -26.857 -29.499  1.00 73.44           C  
ANISOU 2812  CE  LYS A 385     9824  12848   5231   2347   -498    -36       C  
ATOM   2813  NZ  LYS A 385     -22.727 -28.235 -28.934  1.00 85.52           N  
ANISOU 2813  NZ  LYS A 385    11533  14072   6887   2456   -685   -402       N  
ATOM   2814  N   THR A 386     -21.555 -23.027 -25.207  1.00 52.06           N  
ANISOU 2814  N   THR A 386     7262   9094   3423   1506   -107   1003       N  
ATOM   2815  CA  THR A 386     -20.180 -22.552 -25.301  1.00 57.91           C  
ANISOU 2815  CA  THR A 386     7817  10086   4102   1522    -11   1105       C  
ATOM   2816  C   THR A 386     -19.426 -22.832 -24.005  1.00 58.01           C  
ANISOU 2816  C   THR A 386     7924   9819   4299   1488    -52   1004       C  
ATOM   2817  O   THR A 386     -18.274 -23.265 -24.029  1.00 66.83           O  
ANISOU 2817  O   THR A 386     8943  11117   5333   1610    -62    879       O  
ATOM   2818  CB  THR A 386     -20.126 -21.046 -25.617  1.00 65.24           C  
ANISOU 2818  CB  THR A 386     8590  11135   5061   1351    141   1489       C  
ATOM   2819  OG1 THR A 386     -20.976 -20.761 -26.735  1.00 69.29           O  
ANISOU 2819  OG1 THR A 386     9044  11867   5416   1376    163   1605       O  
ATOM   2820  CG2 THR A 386     -18.706 -20.615 -25.946  1.00 60.93           C  
ANISOU 2820  CG2 THR A 386     7814  10924   4413   1369    246   1597       C  
ATOM   2821  N   PHE A 387     -20.086 -22.589 -22.877  1.00 49.19           N  
ANISOU 2821  N   PHE A 387     6987   8283   3419   1330    -80   1053       N  
ATOM   2822  CA  PHE A 387     -19.530 -22.925 -21.571  1.00 56.00           C  
ANISOU 2822  CA  PHE A 387     7968   8863   4446   1299   -138    949       C  
ATOM   2823  C   PHE A 387     -19.348 -24.427 -21.427  1.00 48.47           C  
ANISOU 2823  C   PHE A 387     7141   7843   3432   1486   -292    630       C  
ATOM   2824  O   PHE A 387     -18.291 -24.898 -21.010  1.00 67.48           O  
ANISOU 2824  O   PHE A 387     9528  10275   5837   1584   -339    504       O  
ATOM   2825  CB  PHE A 387     -20.431 -22.418 -20.442  1.00 59.85           C  
ANISOU 2825  CB  PHE A 387     8626   8948   5168   1101   -139   1050       C  
ATOM   2826  CG  PHE A 387     -20.126 -21.018 -19.996  1.00 55.32           C  
ANISOU 2826  CG  PHE A 387     7949   8327   4741    922    -23   1304       C  
ATOM   2827  CD1 PHE A 387     -19.041 -20.761 -19.176  1.00 50.26           C  
ANISOU 2827  CD1 PHE A 387     7263   7639   4194    887    -10   1306       C  
ATOM   2828  CD2 PHE A 387     -20.938 -19.963 -20.374  1.00 53.70           C  
ANISOU 2828  CD2 PHE A 387     7695   8109   4600    794     56   1529       C  
ATOM   2829  CE1 PHE A 387     -18.761 -19.479 -18.754  1.00 45.25           C  
ANISOU 2829  CE1 PHE A 387     6532   6942   3720    717     81   1518       C  
ATOM   2830  CE2 PHE A 387     -20.666 -18.677 -19.954  1.00 56.67           C  
ANISOU 2830  CE2 PHE A 387     7982   8406   5144    632    142   1751       C  
ATOM   2831  CZ  PHE A 387     -19.575 -18.434 -19.141  1.00 54.45           C  
ANISOU 2831  CZ  PHE A 387     7653   8072   4963    588    155   1741       C  
ATOM   2832  N   ARG A 388     -20.397 -25.168 -21.771  1.00 66.65           N  
ANISOU 2832  N   ARG A 388     9572  10048   5702   1534   -382    499       N  
ATOM   2833  CA  ARG A 388     -20.414 -26.616 -21.601  1.00 68.54           C  
ANISOU 2833  CA  ARG A 388     9962  10150   5931   1690   -553    200       C  
ATOM   2834  C   ARG A 388     -19.330 -27.302 -22.429  1.00 71.91           C  
ANISOU 2834  C   ARG A 388    10243  10914   6168   1939   -599     -3       C  
ATOM   2835  O   ARG A 388     -18.698 -28.253 -21.970  1.00 81.37           O  
ANISOU 2835  O   ARG A 388    11519  12002   7397   2075   -725   -216       O  
ATOM   2836  CB  ARG A 388     -21.790 -27.176 -21.967  1.00 53.99           C  
ANISOU 2836  CB  ARG A 388     8249   8170   4093   1676   -633    110       C  
ATOM   2837  CG  ARG A 388     -21.989 -28.624 -21.564  1.00 58.87           C  
ANISOU 2837  CG  ARG A 388     9063   8529   4774   1778   -823   -164       C  
ATOM   2838  CD  ARG A 388     -23.426 -29.076 -21.771  1.00 66.19           C  
ANISOU 2838  CD  ARG A 388    10119   9279   5751   1710   -894   -227       C  
ATOM   2839  NE  ARG A 388     -23.843 -28.981 -23.167  1.00 71.98           N  
ANISOU 2839  NE  ARG A 388    10707  10341   6301   1808   -875   -274       N  
ATOM   2840  CZ  ARG A 388     -24.712 -28.088 -23.630  1.00 72.65           C  
ANISOU 2840  CZ  ARG A 388    10722  10526   6357   1691   -775    -88       C  
ATOM   2841  NH1 ARG A 388     -25.264 -27.206 -22.808  1.00 69.91           N  
ANISOU 2841  NH1 ARG A 388    10431   9964   6166   1475   -684    140       N  
ATOM   2842  NH2 ARG A 388     -25.030 -28.079 -24.917  1.00 79.83           N  
ANISOU 2842  NH2 ARG A 388    11499  11758   7075   1802   -773   -141       N  
ATOM   2843  N   ASP A 389     -19.114 -26.815 -23.646  1.00 59.52           N  
ANISOU 2843  N   ASP A 389     8455   9766   4395   2006   -501     64       N  
ATOM   2844  CA  ASP A 389     -18.061 -27.355 -24.497  1.00 64.01           C  
ANISOU 2844  CA  ASP A 389     8842  10727   4751   2245   -521   -125       C  
ATOM   2845  C   ASP A 389     -16.687 -26.935 -23.989  1.00 65.14           C  
ANISOU 2845  C   ASP A 389     8851  10980   4919   2245   -452    -59       C  
ATOM   2846  O   ASP A 389     -15.712 -27.673 -24.131  1.00 67.83           O  
ANISOU 2846  O   ASP A 389     9113  11487   5172   2450   -522   -286       O  
ATOM   2847  CB  ASP A 389     -18.247 -26.904 -25.948  1.00 56.69           C  
ANISOU 2847  CB  ASP A 389     7706  10264   3569   2304   -423    -48       C  
ATOM   2848  CG  ASP A 389     -19.468 -27.522 -26.600  1.00 63.55           C  
ANISOU 2848  CG  ASP A 389     8677  11093   4375   2364   -522   -192       C  
ATOM   2849  OD1 ASP A 389     -19.925 -28.585 -26.130  1.00 56.53           O  
ANISOU 2849  OD1 ASP A 389     7987   9886   3604   2425   -689   -436       O  
ATOM   2850  OD2 ASP A 389     -19.966 -26.947 -27.590  1.00 72.88           O  
ANISOU 2850  OD2 ASP A 389     9736  12564   5392   2348   -440    -56       O  
ATOM   2851  N   ALA A 390     -16.617 -25.746 -23.398  1.00 60.01           N  
ANISOU 2851  N   ALA A 390     8166  10236   4397   2020   -323    237       N  
ATOM   2852  CA  ALA A 390     -15.367 -25.242 -22.846  1.00 54.28           C  
ANISOU 2852  CA  ALA A 390     7307   9592   3725   1986   -256    315       C  
ATOM   2853  C   ALA A 390     -14.940 -26.093 -21.663  1.00 61.47           C  
ANISOU 2853  C   ALA A 390     8390  10181   4783   2053   -404    113       C  
ATOM   2854  O   ALA A 390     -13.766 -26.436 -21.521  1.00 63.00           O  
ANISOU 2854  O   ALA A 390     8476  10524   4938   2188   -436    -17       O  
ATOM   2855  CB  ALA A 390     -15.509 -23.790 -22.432  1.00 53.09           C  
ANISOU 2855  CB  ALA A 390     7101   9354   3717   1720   -110    659       C  
ATOM   2856  N   PHE A 391     -15.910 -26.427 -20.818  1.00 60.25           N  
ANISOU 2856  N   PHE A 391     8499   9599   4793   1959   -494     97       N  
ATOM   2857  CA  PHE A 391     -15.668 -27.262 -19.649  1.00 59.23           C  
ANISOU 2857  CA  PHE A 391     8567   9135   4802   2005   -644    -58       C  
ATOM   2858  C   PHE A 391     -15.100 -28.612 -20.060  1.00 62.76           C  
ANISOU 2858  C   PHE A 391     9025   9673   5148   2288   -805   -377       C  
ATOM   2859  O   PHE A 391     -14.106 -29.071 -19.500  1.00 69.17           O  
ANISOU 2859  O   PHE A 391     9828  10461   5991   2407   -889   -503       O  
ATOM   2860  CB  PHE A 391     -16.957 -27.459 -18.849  1.00 51.84           C  
ANISOU 2860  CB  PHE A 391     7900   7772   4024   1852   -706    -13       C  
ATOM   2861  CG  PHE A 391     -17.505 -26.193 -18.262  1.00 48.59           C  
ANISOU 2861  CG  PHE A 391     7493   7230   3739   1593   -572    259       C  
ATOM   2862  CD1 PHE A 391     -16.674 -25.116 -18.003  1.00 48.93           C  
ANISOU 2862  CD1 PHE A 391     7370   7402   3822   1500   -454    423       C  
ATOM   2863  CD2 PHE A 391     -18.852 -26.079 -17.963  1.00 53.84           C  
ANISOU 2863  CD2 PHE A 391     8320   7640   4495   1443   -572    335       C  
ATOM   2864  CE1 PHE A 391     -17.178 -23.949 -17.460  1.00 50.72           C  
ANISOU 2864  CE1 PHE A 391     7600   7485   4188   1273   -351    649       C  
ATOM   2865  CE2 PHE A 391     -19.361 -24.912 -17.418  1.00 47.53           C  
ANISOU 2865  CE2 PHE A 391     7516   6722   3820   1226   -460    556       C  
ATOM   2866  CZ  PHE A 391     -18.523 -23.847 -17.167  1.00 46.08           C  
ANISOU 2866  CZ  PHE A 391     7175   6648   3686   1146   -355    708       C  
ATOM   2867  N   GLY A 392     -15.737 -29.234 -21.048  1.00 61.45           N  
ANISOU 2867  N   GLY A 392     8869   9613   4866   2406   -858   -521       N  
ATOM   2868  CA  GLY A 392     -15.322 -30.534 -21.544  1.00 56.06           C  
ANISOU 2868  CA  GLY A 392     8195   9008   4097   2688  -1028   -856       C  
ATOM   2869  C   GLY A 392     -13.879 -30.572 -22.009  1.00 65.31           C  
ANISOU 2869  C   GLY A 392     9116  10576   5122   2890  -1002   -980       C  
ATOM   2870  O   GLY A 392     -13.216 -31.605 -21.914  1.00 67.18           O  
ANISOU 2870  O   GLY A 392     9378  10790   5358   3123  -1164  -1256       O  
ATOM   2871  N   ARG A 393     -13.387 -29.444 -22.510  1.00 72.76           N  
ANISOU 2871  N   ARG A 393     9810  11885   5951   2799   -803   -772       N  
ATOM   2872  CA  ARG A 393     -12.007 -29.359 -22.975  1.00 77.25           C  
ANISOU 2872  CA  ARG A 393    10101  12882   6371   2959   -748   -858       C  
ATOM   2873  C   ARG A 393     -11.059 -29.121 -21.807  1.00 60.00           C  
ANISOU 2873  C   ARG A 393     7915  10543   4340   2907   -761   -808       C  
ATOM   2874  O   ARG A 393      -9.903 -29.542 -21.837  1.00 61.82           O  
ANISOU 2874  O   ARG A 393     7998  10983   4509   3100   -811   -991       O  
ATOM   2875  CB  ARG A 393     -11.852 -28.245 -24.015  1.00 69.36           C  
ANISOU 2875  CB  ARG A 393     8821  12352   5182   2864   -526   -628       C  
ATOM   2876  CG  ARG A 393     -12.702 -28.436 -25.256  1.00 62.47           C  
ANISOU 2876  CG  ARG A 393     7915  11706   4113   2935   -510   -675       C  
ATOM   2877  CD  ARG A 393     -12.350 -27.424 -26.336  1.00 69.75           C  
ANISOU 2877  CD  ARG A 393     8535  13158   4809   2876   -300   -449       C  
ATOM   2878  NE  ARG A 393     -12.601 -26.046 -25.923  1.00 73.03           N  
ANISOU 2878  NE  ARG A 393     8933  13460   5355   2568   -139    -42       N  
ATOM   2879  CZ  ARG A 393     -13.755 -25.411 -26.105  1.00 71.76           C  
ANISOU 2879  CZ  ARG A 393     8870  13158   5237   2392    -85    184       C  
ATOM   2880  NH1 ARG A 393     -14.772 -26.032 -26.687  1.00 79.33           N  
ANISOU 2880  NH1 ARG A 393     9946  14083   6111   2483   -172     47       N  
ATOM   2881  NH2 ARG A 393     -13.895 -24.156 -25.702  1.00 62.10           N  
ANISOU 2881  NH2 ARG A 393     7621  11820   4155   2131     45    534       N  
ATOM   2882  N   TYR A 394     -11.561 -28.443 -20.779  1.00 57.60           N  
ANISOU 2882  N   TYR A 394     7766   9888   4231   2656   -722   -577       N  
ATOM   2883  CA  TYR A 394     -10.762 -28.124 -19.600  1.00 70.88           C  
ANISOU 2883  CA  TYR A 394     9456  11412   6062   2582   -736   -517       C  
ATOM   2884  C   TYR A 394     -10.527 -29.351 -18.730  1.00 70.96           C  
ANISOU 2884  C   TYR A 394     9678  11111   6170   2753   -964   -759       C  
ATOM   2885  O   TYR A 394      -9.423 -29.566 -18.232  1.00 73.72           O  
ANISOU 2885  O   TYR A 394     9948  11520   6542   2868  -1027   -862       O  
ATOM   2886  CB  TYR A 394     -11.437 -27.032 -18.768  1.00 73.45           C  
ANISOU 2886  CB  TYR A 394     9885  11463   6560   2272   -635   -222       C  
ATOM   2887  CG  TYR A 394     -11.500 -25.676 -19.434  1.00 69.02           C  
ANISOU 2887  CG  TYR A 394     9109  11160   5954   2085   -422     55       C  
ATOM   2888  CD1 TYR A 394     -10.744 -25.395 -20.565  1.00 68.06           C  
ANISOU 2888  CD1 TYR A 394     8694  11522   5643   2172   -313     67       C  
ATOM   2889  CD2 TYR A 394     -12.307 -24.672 -18.919  1.00 71.07           C  
ANISOU 2889  CD2 TYR A 394     9455  11182   6365   1822   -334    308       C  
ATOM   2890  CE1 TYR A 394     -10.799 -24.154 -21.169  1.00 69.08           C  
ANISOU 2890  CE1 TYR A 394     8635  11875   5739   1987   -125    356       C  
ATOM   2891  CE2 TYR A 394     -12.368 -23.430 -19.514  1.00 80.53           C  
ANISOU 2891  CE2 TYR A 394    10469  12578   7551   1654   -160    573       C  
ATOM   2892  CZ  TYR A 394     -11.613 -23.176 -20.637  1.00 78.16           C  
ANISOU 2892  CZ  TYR A 394     9891  12740   7066   1729    -57    613       C  
ATOM   2893  OH  TYR A 394     -11.678 -21.936 -21.224  1.00 80.77           O  
ANISOU 2893  OH  TYR A 394    10045  13253   7391   1547    110    913       O  
ATOM   2894  N   ILE A 395     -11.573 -30.151 -18.548  1.00 76.47           N  
ANISOU 2894  N   ILE A 395    10644  11477   6935   2765  -1093   -839       N  
ATOM   2895  CA  ILE A 395     -11.479 -31.362 -17.740  1.00 75.48           C  
ANISOU 2895  CA  ILE A 395    10750  11013   6918   2910  -1324  -1035       C  
ATOM   2896  C   ILE A 395     -10.589 -32.408 -18.405  1.00 68.19           C  
ANISOU 2896  C   ILE A 395     9718  10303   5890   3250  -1467  -1362       C  
ATOM   2897  O   ILE A 395     -10.156 -33.359 -17.760  1.00 72.90           O  
ANISOU 2897  O   ILE A 395    10450  10674   6575   3413  -1667  -1535       O  
ATOM   2898  CB  ILE A 395     -12.868 -31.976 -17.478  1.00 78.37           C  
ANISOU 2898  CB  ILE A 395    11412  10980   7384   2819  -1423  -1029       C  
ATOM   2899  CG1 ILE A 395     -13.575 -32.271 -18.801  1.00 78.48           C  
ANISOU 2899  CG1 ILE A 395    11370  11175   7273   2897  -1408  -1138       C  
ATOM   2900  CG2 ILE A 395     -13.709 -31.047 -16.616  1.00 78.86           C  
ANISOU 2900  CG2 ILE A 395    11595  10803   7565   2505  -1307   -739       C  
ATOM   2901  CD1 ILE A 395     -14.922 -32.932 -18.637  1.00 77.89           C  
ANISOU 2901  CD1 ILE A 395    11560  10732   7302   2814  -1515  -1159       C  
ATOM   2902  N   THR A 396     -10.324 -32.228 -19.695  1.00 61.06           N  
ANISOU 2902  N   THR A 396     8566   9842   4793   3362  -1368  -1445       N  
ATOM   2903  CA  THR A 396      -9.410 -33.100 -20.420  1.00 63.99           C  
ANISOU 2903  CA  THR A 396     8777  10499   5035   3698  -1479  -1774       C  
ATOM   2904  C   THR A 396      -8.052 -32.430 -20.580  1.00 72.79           C  
ANISOU 2904  C   THR A 396     9567  12047   6042   3750  -1352  -1750       C  
ATOM   2905  O   THR A 396      -7.198 -32.911 -21.323  1.00 67.90           O  
ANISOU 2905  O   THR A 396     8733  11791   5273   4013  -1387  -2000       O  
ATOM   2906  CB  THR A 396      -9.960 -33.478 -21.806  1.00 80.72           C  
ANISOU 2906  CB  THR A 396    10812  12882   6975   3829  -1470  -1937       C  
ATOM   2907  OG1 THR A 396     -10.254 -32.287 -22.548  1.00 81.10           O  
ANISOU 2907  OG1 THR A 396    10668  13268   6878   3640  -1223  -1683       O  
ATOM   2908  CG2 THR A 396     -11.223 -34.312 -21.669  1.00 82.05           C  
ANISOU 2908  CG2 THR A 396    11288  12619   7267   3807  -1631  -2019       C  
ATOM   2909  N   CYS A 397      -7.871 -31.314 -19.879  1.00 81.68           N  
ANISOU 2909  N   CYS A 397    10647  13135   7250   3494  -1205  -1459       N  
ATOM   2910  CA  CYS A 397      -6.606 -30.582 -19.857  1.00 89.68           C  
ANISOU 2910  CA  CYS A 397    11361  14505   8208   3487  -1084  -1399       C  
ATOM   2911  C   CYS A 397      -6.189 -30.101 -21.247  1.00 90.75           C  
ANISOU 2911  C   CYS A 397    11156  15226   8101   3539   -905  -1393       C  
ATOM   2912  O   CYS A 397      -5.053 -30.317 -21.670  1.00 97.21           O  
ANISOU 2912  O   CYS A 397    11712  16430   8793   3736   -900  -1569       O  
ATOM   2913  CB  CYS A 397      -5.500 -31.451 -19.245  1.00 98.98           C  
ANISOU 2913  CB  CYS A 397    12525  15647   9437   3743  -1273  -1663       C  
ATOM   2914  SG  CYS A 397      -6.015 -32.412 -17.793  1.00 69.89           S  
ANISOU 2914  SG  CYS A 397     9268  11296   5992   3766  -1540  -1725       S  
ATOM   2915  N   ASN A 398      -7.108 -29.443 -21.948  1.00 87.00           N  
ANISOU 2915  N   ASN A 398    10674  14832   7549   3365   -758  -1184       N  
ATOM   2916  CA  ASN A 398      -6.836 -28.942 -23.293  1.00 86.60           C  
ANISOU 2916  CA  ASN A 398    10315  15343   7245   3392   -582  -1131       C  
ATOM   2917  C   ASN A 398      -7.001 -27.426 -23.414  1.00 86.65           C  
ANISOU 2917  C   ASN A 398    10188  15471   7265   3066   -345   -716       C  
ATOM   2918  O   ASN A 398      -8.102 -26.896 -23.264  1.00 77.24           O  
ANISOU 2918  O   ASN A 398     9171  14010   6167   2855   -300   -494       O  
ATOM   2919  CB  ASN A 398      -7.741 -29.642 -24.310  1.00 81.80           C  
ANISOU 2919  CB  ASN A 398     9784  14814   6480   3537   -640  -1293       C  
ATOM   2920  CG  ASN A 398      -7.430 -31.122 -24.447  1.00 86.20           C  
ANISOU 2920  CG  ASN A 398    10407  15342   7002   3892   -872  -1734       C  
ATOM   2921  OD1 ASN A 398      -8.269 -31.974 -24.153  1.00 85.79           O  
ANISOU 2921  OD1 ASN A 398    10639  14889   7067   3952  -1052  -1880       O  
ATOM   2922  ND2 ASN A 398      -6.220 -31.434 -24.897  1.00 88.21           N  
ANISOU 2922  ND2 ASN A 398    10389  16020   7106   4127   -873  -1953       N  
ATOM   2923  N   TYR A 399      -5.896 -26.737 -23.690  1.00 92.69           N  
ANISOU 2923  N   TYR A 399    10633  16641   7947   3026   -200   -615       N  
ATOM   2924  CA  TYR A 399      -5.909 -25.286 -23.861  1.00 87.09           C  
ANISOU 2924  CA  TYR A 399     9764  16064   7264   2718     18   -216       C  
ATOM   2925  C   TYR A 399      -5.127 -24.861 -25.100  1.00 89.82           C  
ANISOU 2925  C   TYR A 399     9724  17066   7338   2757    196   -143       C  
ATOM   2926  O   TYR A 399      -3.920 -25.089 -25.191  1.00 89.65           O  
ANISOU 2926  O   TYR A 399     9455  17378   7231   2893    208   -297       O  
ATOM   2927  CB  TYR A 399      -5.330 -24.589 -22.627  1.00 77.47           C  
ANISOU 2927  CB  TYR A 399     8550  14586   6300   2524     29    -76       C  
ATOM   2928  CG  TYR A 399      -5.758 -25.198 -21.313  1.00 64.52           C  
ANISOU 2928  CG  TYR A 399     7244  12385   4884   2545   -164   -210       C  
ATOM   2929  CD1 TYR A 399      -7.011 -24.934 -20.778  1.00 71.00           C  
ANISOU 2929  CD1 TYR A 399     8353  12765   5859   2368   -189    -60       C  
ATOM   2930  CD2 TYR A 399      -4.905 -26.029 -20.601  1.00 78.80           C  
ANISOU 2930  CD2 TYR A 399     9072  14124   6743   2743   -322   -480       C  
ATOM   2931  CE1 TYR A 399      -7.405 -25.486 -19.573  1.00 68.23           C  
ANISOU 2931  CE1 TYR A 399     8297  11937   5691   2375   -353   -164       C  
ATOM   2932  CE2 TYR A 399      -5.290 -26.586 -19.395  1.00 77.73           C  
ANISOU 2932  CE2 TYR A 399     9245  13493   6796   2757   -500   -572       C  
ATOM   2933  CZ  TYR A 399      -6.542 -26.311 -18.886  1.00 72.83           C  
ANISOU 2933  CZ  TYR A 399     8903  12459   6310   2565   -508   -407       C  
ATOM   2934  OH  TYR A 399      -6.932 -26.862 -17.687  1.00 77.94           O  
ANISOU 2934  OH  TYR A 399     9846  12646   7122   2566   -672   -480       O  
ATOM   2935  N   ARG A 400      -5.821 -24.238 -26.048  1.00 91.63           N  
ANISOU 2935  N   ARG A 400     9895  17495   7426   2637    333     98       N  
ATOM   2936  CA  ARG A 400      -5.191 -23.730 -27.263  1.00 97.90           C  
ANISOU 2936  CA  ARG A 400    10326  18930   7940   2637    520    234       C  
ATOM   2937  C   ARG A 400      -6.106 -22.743 -27.979  1.00100.99           C  
ANISOU 2937  C   ARG A 400    10718  19384   8268   2411    666    620       C  
ATOM   2938  O   ARG A 400      -7.326 -22.785 -27.821  1.00 99.19           O  
ANISOU 2938  O   ARG A 400    10764  18787   8135   2355    595    670       O  
ATOM   2939  CB  ARG A 400      -4.820 -24.878 -28.205  1.00103.21           C  
ANISOU 2939  CB  ARG A 400    10865  20046   8304   2997    456   -146       C  
TER    2940      ARG A 400                                                      
HETATM 2941  N1  7LD A2001     -25.976 -12.817   6.961  1.00 46.14           N  
HETATM 2942  N3  7LD A2001     -21.864 -20.023  10.866  1.00 51.57           N  
HETATM 2943  C4  7LD A2001     -26.221 -12.989   9.395  1.00 56.04           C  
HETATM 2944  C5  7LD A2001     -25.866 -13.776  10.490  1.00 58.27           C  
HETATM 2945  C6  7LD A2001     -24.689 -15.220   9.007  1.00 59.44           C  
HETATM 2946  C7  7LD A2001     -24.779 -14.611   6.745  1.00 57.47           C  
HETATM 2947  C8  7LD A2001     -25.338 -13.597   6.082  1.00 47.24           C  
HETATM 2948  C10 7LD A2001     -23.329 -17.078   9.739  1.00 57.49           C  
HETATM 2949  C13 7LD A2001     -23.007 -18.837   8.162  1.00 61.05           C  
HETATM 2950  C15 7LD A2001     -23.988 -15.691   6.352  1.00 52.28           C  
HETATM 2951  C17 7LD A2001     -20.534 -20.017  10.238  1.00 53.29           C  
HETATM 2952  C20 7LD A2001     -22.772 -22.256  11.381  1.00 45.43           C  
HETATM 2953  N2  7LD A2001     -22.935 -17.809   7.116  1.00 54.54           N  
HETATM 2954  C12 7LD A2001     -23.226 -18.427   5.814  1.00 56.86           C  
HETATM 2955  C11 7LD A2001     -23.992 -16.826   7.392  1.00 50.73           C  
HETATM 2956  C3  7LD A2001     -25.080 -14.430   8.019  1.00 61.74           C  
HETATM 2957  C1  7LD A2001     -25.812 -13.339   8.177  1.00 55.91           C  
HETATM 2958  C2  7LD A2001     -25.086 -14.914  10.302  1.00 54.25           C  
HETATM 2959  C9  7LD A2001     -23.939 -16.350   8.714  1.00 57.43           C  
HETATM 2960  C14 7LD A2001     -22.597 -18.247   9.509  1.00 58.55           C  
HETATM 2961  C16 7LD A2001     -22.857 -19.171  10.533  1.00 58.60           C  
HETATM 2962  O1  7LD A2001     -23.959 -19.190  11.081  1.00 56.11           O  
HETATM 2963  C19 7LD A2001     -22.040 -21.027  11.928  1.00 50.59           C  
HETATM 2964  C18 7LD A2001     -19.495 -19.669  11.303  1.00 66.51           C  
HETATM 2965  C1  CLR A2002      -8.199 -27.367 -12.870  1.00 82.59           C  
HETATM 2966  C2  CLR A2002      -8.375 -27.192 -14.370  1.00 83.20           C  
HETATM 2967  C3  CLR A2002      -8.471 -28.553 -15.033  1.00 81.74           C  
HETATM 2968  C4  CLR A2002      -9.783 -29.184 -14.594  1.00 83.58           C  
HETATM 2969  C5  CLR A2002      -9.879 -29.238 -13.085  1.00 81.09           C  
HETATM 2970  C6  CLR A2002     -10.498 -30.300 -12.546  1.00 86.93           C  
HETATM 2971  C7  CLR A2002     -10.195 -30.816 -11.159  1.00 87.63           C  
HETATM 2972  C8  CLR A2002      -9.786 -29.679 -10.237  1.00 79.14           C  
HETATM 2973  C9  CLR A2002      -8.782 -28.754 -10.920  1.00 77.08           C  
HETATM 2974  C10 CLR A2002      -9.339 -28.134 -12.201  1.00 77.57           C  
HETATM 2975  C11 CLR A2002      -8.239 -27.681  -9.965  1.00 74.56           C  
HETATM 2976  C12 CLR A2002      -7.721 -28.244  -8.639  1.00 75.52           C  
HETATM 2977  C13 CLR A2002      -8.793 -29.117  -8.001  1.00 73.27           C  
HETATM 2978  C14 CLR A2002      -9.138 -30.223  -8.973  1.00 74.57           C  
HETATM 2979  C15 CLR A2002      -9.905 -31.243  -8.144  1.00 73.68           C  
HETATM 2980  C16 CLR A2002      -9.279 -31.125  -6.751  1.00 73.84           C  
HETATM 2981  C17 CLR A2002      -8.349 -29.908  -6.777  1.00 72.52           C  
HETATM 2982  C18 CLR A2002     -10.025 -28.286  -7.647  1.00 77.33           C  
HETATM 2983  C19 CLR A2002     -10.487 -27.184 -11.882  1.00 72.44           C  
HETATM 2984  C20 CLR A2002      -8.349 -29.092  -5.485  1.00 75.72           C  
HETATM 2985  C21 CLR A2002      -6.918 -28.845  -5.018  1.00 81.26           C  
HETATM 2986  C22 CLR A2002      -9.190 -29.747  -4.391  1.00 76.24           C  
HETATM 2987  C23 CLR A2002      -8.869 -29.191  -3.008  1.00 78.61           C  
HETATM 2988  C24 CLR A2002      -8.412 -30.297  -2.061  1.00 78.41           C  
HETATM 2989  C25 CLR A2002      -9.024 -30.179  -0.665  1.00 72.60           C  
HETATM 2990  C26 CLR A2002      -7.979 -30.477   0.402  1.00 77.25           C  
HETATM 2991  C27 CLR A2002      -9.670 -28.820  -0.414  1.00 67.19           C  
HETATM 2992  O1  CLR A2002      -8.467 -28.390 -16.454  1.00 83.37           O  
HETATM 2993  C10 OLC A2003     -44.263 -17.786  -3.568  1.00 53.72           C  
HETATM 2994  C9  OLC A2003     -43.517 -18.411  -4.475  1.00 49.41           C  
HETATM 2995  C11 OLC A2003     -45.359 -16.854  -4.029  1.00 64.85           C  
HETATM 2996  C8  OLC A2003     -43.798 -18.184  -5.941  1.00 43.06           C  
HETATM 2997  C24 OLC A2003     -35.881 -13.544 -13.604  1.00 79.02           C  
HETATM 2998  C12 OLC A2003     -46.722 -17.472  -3.746  1.00 73.40           C  
HETATM 2999  C7  OLC A2003     -42.669 -17.394  -6.592  1.00 37.56           C  
HETATM 3000  C6  OLC A2003     -41.503 -18.289  -6.997  1.00 35.70           C  
HETATM 3001  C5  OLC A2003     -40.210 -17.482  -6.989  1.00 40.41           C  
HETATM 3002  C4  OLC A2003     -39.054 -18.204  -7.672  1.00 45.49           C  
HETATM 3003  C3  OLC A2003     -37.915 -17.215  -7.901  1.00 47.75           C  
HETATM 3004  C2  OLC A2003     -36.978 -17.660  -9.017  1.00 53.32           C  
HETATM 3005  C21 OLC A2003     -36.262 -14.698 -11.427  1.00 76.45           C  
HETATM 3006  C1  OLC A2003     -36.331 -16.444  -9.640  1.00 73.67           C  
HETATM 3007  C22 OLC A2003     -36.777 -14.524 -12.852  1.00 72.03           C  
HETATM 3008  O19 OLC A2003     -35.313 -15.972  -9.164  1.00 93.24           O  
HETATM 3009  O25 OLC A2003     -36.194 -13.572 -15.003  1.00 78.79           O  
HETATM 3010  O23 OLC A2003     -36.771 -15.792 -13.517  1.00 65.50           O  
HETATM 3011  O20 OLC A2003     -36.904 -15.822 -10.826  1.00 79.66           O  
HETATM 3012  C1  PEG A2004     -27.922 -20.460 -19.023  1.00 35.38           C  
HETATM 3013  O1  PEG A2004     -29.055 -19.997 -19.781  1.00 47.31           O  
HETATM 3014  C2  PEG A2004     -26.890 -19.400 -18.532  1.00 43.22           C  
HETATM 3015  O2  PEG A2004     -26.212 -18.755 -19.421  1.00 50.25           O  
HETATM 3016  C3  PEG A2004     -25.079 -17.948 -18.999  1.00 51.99           C  
HETATM 3017  C4  PEG A2004     -24.204 -17.326 -20.099  1.00 59.57           C  
HETATM 3018  O4  PEG A2004     -24.829 -16.589 -21.051  1.00 67.61           O  
HETATM 3019  P   PO4 A2005     -30.773  -7.836 -37.826  1.00 62.46           P  
HETATM 3020  O1  PO4 A2005     -29.693  -7.119 -38.601  1.00 66.41           O  
HETATM 3021  O2  PO4 A2005     -32.124  -7.261 -38.183  1.00 56.54           O  
HETATM 3022  O3  PO4 A2005     -30.745  -9.302 -38.169  1.00 47.47           O  
HETATM 3023  O4  PO4 A2005     -30.530  -7.670 -36.345  1.00 72.79           O  
HETATM 3024  O   HOH A2101     -33.529 -14.017 -35.570  1.00 53.17           O  
CONECT  635 1189                                                                
CONECT 1189  635                                                                
CONECT 2533 2553                                                                
CONECT 2553 2533                                                                
CONECT 2941 2947 2957                                                           
CONECT 2942 2951 2961 2963                                                      
CONECT 2943 2944 2957                                                           
CONECT 2944 2943 2958                                                           
CONECT 2945 2956 2958 2959                                                      
CONECT 2946 2947 2950 2956                                                      
CONECT 2947 2941 2946                                                           
CONECT 2948 2959 2960                                                           
CONECT 2949 2953 2960                                                           
CONECT 2950 2946 2955                                                           
CONECT 2951 2942 2964                                                           
CONECT 2952 2963                                                                
CONECT 2953 2949 2954 2955                                                      
CONECT 2954 2953                                                                
CONECT 2955 2950 2953 2959                                                      
CONECT 2956 2945 2946 2957                                                      
CONECT 2957 2941 2943 2956                                                      
CONECT 2958 2944 2945                                                           
CONECT 2959 2945 2948 2955                                                      
CONECT 2960 2948 2949 2961                                                      
CONECT 2961 2942 2960 2962                                                      
CONECT 2962 2961                                                                
CONECT 2963 2942 2952                                                           
CONECT 2964 2951                                                                
CONECT 2965 2966 2974                                                           
CONECT 2966 2965 2967                                                           
CONECT 2967 2966 2968 2992                                                      
CONECT 2968 2967 2969                                                           
CONECT 2969 2968 2970 2974                                                      
CONECT 2970 2969 2971                                                           
CONECT 2971 2970 2972                                                           
CONECT 2972 2971 2973 2978                                                      
CONECT 2973 2972 2974 2975                                                      
CONECT 2974 2965 2969 2973 2983                                                 
CONECT 2975 2973 2976                                                           
CONECT 2976 2975 2977                                                           
CONECT 2977 2976 2978 2981 2982                                                 
CONECT 2978 2972 2977 2979                                                      
CONECT 2979 2978 2980                                                           
CONECT 2980 2979 2981                                                           
CONECT 2981 2977 2980 2984                                                      
CONECT 2982 2977                                                                
CONECT 2983 2974                                                                
CONECT 2984 2981 2985 2986                                                      
CONECT 2985 2984                                                                
CONECT 2986 2984 2987                                                           
CONECT 2987 2986 2988                                                           
CONECT 2988 2987 2989                                                           
CONECT 2989 2988 2990 2991                                                      
CONECT 2990 2989                                                                
CONECT 2991 2989                                                                
CONECT 2992 2967                                                                
CONECT 2993 2994 2995                                                           
CONECT 2994 2993 2996                                                           
CONECT 2995 2993 2998                                                           
CONECT 2996 2994 2999                                                           
CONECT 2997 3007 3009                                                           
CONECT 2998 2995                                                                
CONECT 2999 2996 3000                                                           
CONECT 3000 2999 3001                                                           
CONECT 3001 3000 3002                                                           
CONECT 3002 3001 3003                                                           
CONECT 3003 3002 3004                                                           
CONECT 3004 3003 3006                                                           
CONECT 3005 3007 3011                                                           
CONECT 3006 3004 3008 3011                                                      
CONECT 3007 2997 3005 3010                                                      
CONECT 3008 3006                                                                
CONECT 3009 2997                                                                
CONECT 3010 3007                                                                
CONECT 3011 3005 3006                                                           
CONECT 3012 3013 3014                                                           
CONECT 3013 3012                                                                
CONECT 3014 3012 3015                                                           
CONECT 3015 3014 3016                                                           
CONECT 3016 3015 3017                                                           
CONECT 3017 3016 3018                                                           
CONECT 3018 3017                                                                
CONECT 3019 3020 3021 3022 3023                                                 
CONECT 3020 3019                                                                
CONECT 3021 3019                                                                
CONECT 3022 3019                                                                
CONECT 3023 3019                                                                
MASTER      372    0    5   18    0    0   10    6 3023    1   87   31          
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.