CNRS Nantes University UFIP UFIP
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***  TRANSFERASE 26-JUN-15 5C8U  ***

elNémo ID: 20072100285297268

Job options:

ID        	=	 20072100285297268
JOBID     	=	 TRANSFERASE 26-JUN-15 5C8U
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    TRANSFERASE                             26-JUN-15   5C8U              
TITLE     CRYSTAL STRUCTURE OF THE SARS CORONAVIRUS NSP14-NSP10 COMPLEX         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NON-STRUCTURAL PROTEIN 10;                                 
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: NSP10;                                                      
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: GUANINE-N7 METHYLTRANSFERASE;                              
COMPND   8 CHAIN: B, D;                                                         
COMPND   9 SYNONYM: NSP14;                                                      
COMPND  10 EC: 2.1.1.-, 3.1.13.-;                                               
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN SARS CORONAVIRUS;                         
SOURCE   3 ORGANISM_COMMON: SARS-COV;                                           
SOURCE   4 ORGANISM_TAXID: 227859;                                              
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HUMAN SARS CORONAVIRUS;                         
SOURCE  10 ORGANISM_COMMON: SARS-COV;                                           
SOURCE  11 ORGANISM_TAXID: 227859;                                              
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    NSP14, NSP10, EXORIBONUCLEASE, METHYL TRANSFERASE, TRANSFERASE        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.Y.MA,L.J.WU,R.G.ZHANG,Z.H.RAO                                       
REVDAT   2   12-AUG-15 5C8U    1       JRNL                                     
REVDAT   1   15-JUL-15 5C8U    0                                                
JRNL        AUTH   Y.Y.MA,L.J.WU,N.SHAW,Y.GAO,J.WANG,Y.N.SUN,Z.Y.LOU,L.M.YAN,   
JRNL        AUTH 2 R.G.ZHANG,Z.H.RAO                                            
JRNL        TITL   STRUCTURAL BASIS AND FUNCTIONAL ANALYSIS OF THE SARS         
JRNL        TITL 2 CORONAVIRUS NSP14-NSP10 COMPLEX                              
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 112  9436 2015              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   26159422                                                     
JRNL        DOI    10.1073/PNAS.1508686112                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.7.1_743                                     
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.35                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 45999                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2326                            
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 45.3540 -  8.7260    0.99     2700   149  0.2160 0.2323        
REMARK   3     2  8.7260 -  6.9340    1.00     2633   143  0.1916 0.2573        
REMARK   3     3  6.9340 -  6.0599    1.00     2610   126  0.2143 0.2660        
REMARK   3     4  6.0599 -  5.5068    1.00     2600   121  0.2295 0.2837        
REMARK   3     5  5.5068 -  5.1127    1.00     2568   140  0.2102 0.2611        
REMARK   3     6  5.1127 -  4.8116    1.00     2583   128  0.1857 0.2535        
REMARK   3     7  4.8116 -  4.5709    1.00     2556   144  0.1683 0.2374        
REMARK   3     8  4.5709 -  4.3721    1.00     2564   133  0.1859 0.2154        
REMARK   3     9  4.3721 -  4.2039    1.00     2565   145  0.1973 0.2476        
REMARK   3    10  4.2039 -  4.0589    1.00     2560   131  0.2093 0.2527        
REMARK   3    11  4.0589 -  3.9321    1.00     2534   148  0.2334 0.2639        
REMARK   3    12  3.9321 -  3.8197    1.00     2534   140  0.2417 0.2917        
REMARK   3    13  3.8197 -  3.7192    1.00     2547   144  0.2579 0.3775        
REMARK   3    14  3.7192 -  3.6285    1.00     2548   127  0.2753 0.3466        
REMARK   3    15  3.6285 -  3.5461    1.00     2527   141  0.2938 0.3382        
REMARK   3    16  3.5461 -  3.4706    1.00     2519   142  0.3148 0.4098        
REMARK   3    17  3.4706 -  3.4012    0.99     2525   124  0.3351 0.3993        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.31                                          
REMARK   3   B_SOL              : 99.97                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.830            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.760           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 109.9                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 151.5                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -27.37050                                            
REMARK   3    B22 (A**2) : 60.63650                                             
REMARK   3    B33 (A**2) : -33.26610                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  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      :  0.024          10542                                  
REMARK   3   ANGLE     :  1.343          14246                                  
REMARK   3   CHIRALITY :  0.090           1540                                  
REMARK   3   PLANARITY :  0.006           1828                                  
REMARK   3   DIHEDRAL  : 19.190           3716                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A): -17.9809 -62.7553 -10.1240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7938 T22:   0.7624                                     
REMARK   3      T33:   0.7957 T12:  -0.0392                                     
REMARK   3      T13:  -0.2417 T23:  -0.2138                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2213 L22:   0.0458                                     
REMARK   3      L33:   0.1651 L12:  -0.0841                                     
REMARK   3      L13:   0.2239 L23:  -0.5009                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2650 S12:   0.1452 S13:   0.0153                       
REMARK   3      S21:  -0.1102 S22:   0.1096 S23:   0.0089                       
REMARK   3      S31:  -0.2555 S32:  -0.0662 S33:  -0.0029                       
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 5C8U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000211109.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-SEP-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.984                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46052                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : 0.08600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.74900                            
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: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 77.97                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% (V/V) TACSIMATE PH 7.0, 0.1 M        
REMARK 280  HEPES PH 7.0, 2% (W/V) POLYETHYLENE GLYCOL 3350, VAPOR DIFFUSION,   
REMARK 280  HANGING DROP, TEMPERATURE 289K                                      
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       89.92200            
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       89.92200            
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       94.96400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       97.48950            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       94.96400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       97.48950            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       89.92200            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       94.96400            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       97.48950            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       89.92200            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       94.96400            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       97.48950            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -4                                                      
REMARK 465     PRO A    -3                                                      
REMARK 465     LEU A    -2                                                      
REMARK 465     GLN A   132                                                      
REMARK 465     LEU A   133                                                      
REMARK 465     ARG A   134                                                      
REMARK 465     GLU A   135                                                      
REMARK 465     PRO A   136                                                      
REMARK 465     LEU A   137                                                      
REMARK 465     MET A   138                                                      
REMARK 465     GLN A   139                                                      
REMARK 465     MET B     0                                                      
REMARK 465     SER B   454                                                      
REMARK 465     HIS B   455                                                      
REMARK 465     GLY B   456                                                      
REMARK 465     LYS B   457                                                      
REMARK 465     GLN B   458                                                      
REMARK 465     VAL B   459                                                      
REMARK 465     VAL B   460                                                      
REMARK 465     SER B   461                                                      
REMARK 465     ASP B   462                                                      
REMARK 465     ILE B   463                                                      
REMARK 465     ASP B   464                                                      
REMARK 465     LEU B   526                                                      
REMARK 465     GLN B   527                                                      
REMARK 465     GLY C    -4                                                      
REMARK 465     PRO C    -3                                                      
REMARK 465     LEU C    -2                                                      
REMARK 465     GLN C   132                                                      
REMARK 465     LEU C   133                                                      
REMARK 465     ARG C   134                                                      
REMARK 465     GLU C   135                                                      
REMARK 465     PRO C   136                                                      
REMARK 465     LEU C   137                                                      
REMARK 465     MET C   138                                                      
REMARK 465     GLN C   139                                                      
REMARK 465     MET D     0                                                      
REMARK 465     SER D   454                                                      
REMARK 465     HIS D   455                                                      
REMARK 465     GLY D   456                                                      
REMARK 465     LYS D   457                                                      
REMARK 465     GLN D   458                                                      
REMARK 465     VAL D   459                                                      
REMARK 465     VAL D   460                                                      
REMARK 465     SER D   461                                                      
REMARK 465     ASP D   462                                                      
REMARK 465     ILE D   463                                                      
REMARK 465     ASP D   464                                                      
REMARK 465     LEU D   526                                                      
REMARK 465     GLN D   527                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CE1  HIS D   229    ZN     ZN D   601              1.09            
REMARK 500   CE1  HIS B   229    ZN     ZN B   601              1.27            
REMARK 500   CE1  HIS B   487    ZN     ZN B   603              1.47            
REMARK 500   O    ASP C    64     OG1  THR C   101              1.95            
REMARK 500   O    LEU D   519     OG1  THR D   522              2.01            
REMARK 500   OH   TYR A    27     OD2  ASP A   106              2.03            
REMARK 500   NH2  ARG B   163     OH   TYR B   235              2.04            
REMARK 500   OD1  ASN A    40     OG1  THR B    25              2.10            
REMARK 500   O    VAL A   108     OG1  THR A   111              2.16            
REMARK 500   OE1  GLN D   313     NE1  TRP D   385              2.16            
REMARK 500   N    GLY B    88     OG   SER B   112              2.16            
REMARK 500   O    VAL D   405     ND2  ASN D   410              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    GLU B   453     O    GLU B   453     3555     2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  40       -0.79     81.70                                   
REMARK 500    VAL A 119      -71.90    -80.34                                   
REMARK 500    GLN B  22       -8.39     85.20                                   
REMARK 500    LYS B  61       71.07     40.35                                   
REMARK 500    ARG B  98      -71.87   -113.20                                   
REMARK 500    LEU B 107      -64.04   -107.06                                   
REMARK 500    LYS B 155      -70.67    -46.80                                   
REMARK 500    LEU B 209      -12.49     83.00                                   
REMARK 500    ASN B 228      -70.80    -74.88                                   
REMARK 500    ASP B 301       -3.81     67.74                                   
REMARK 500    ALA B 337      -73.39    -53.24                                   
REMARK 500    ILE B 338       72.81     40.71                                   
REMARK 500    ASP B 390     -178.61    -69.05                                   
REMARK 500    ASN B 422      -59.99   -125.11                                   
REMARK 500    HIS B 424       70.91     44.12                                   
REMARK 500    CYS B 473      155.46    174.72                                   
REMARK 500    ASN B 518       -7.24    -59.68                                   
REMARK 500    LEU C  92      -61.65   -109.90                                   
REMARK 500    VAL C 119      -70.95    -90.85                                   
REMARK 500    CYS C 130     -169.86   -160.29                                   
REMARK 500    LEU D   7      -71.54    -51.80                                   
REMARK 500    GLN D  22       -6.13     83.88                                   
REMARK 500    THR D  97      -77.24   -123.38                                   
REMARK 500    LEU D 107      -62.35   -121.52                                   
REMARK 500    ASP D 144     -126.26     60.10                                   
REMARK 500    VAL D 263      -73.95    -85.19                                   
REMARK 500    ARG D 289      -11.72     64.01                                   
REMARK 500    VAL D 290     -142.92     48.95                                   
REMARK 500    GLU D 364     -111.86     52.28                                   
REMARK 500    GLU D 365       -5.60     92.07                                   
REMARK 500    ASP D 415      -66.79   -101.90                                   
REMARK 500    ASN D 422      -61.32   -123.08                                   
REMARK 500    HIS D 424      -13.03     71.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS A   87     GLY A   88                  -35.89                    
REMARK 500 ARG B   84     ALA B   85                  138.00                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  74   SG                                                     
REMARK 620 2 CYS A  77   SG  110.5                                              
REMARK 620 3 HIS A  83   NE2 119.8 107.1                                        
REMARK 620 4 CYS A  90   SG   97.4 113.3 108.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 117   SG                                                     
REMARK 620 2 CYS A 120   SG  108.0                                              
REMARK 620 3 CYS A 128   SG  108.8 107.3                                        
REMARK 620 4 CYS A 130   SG  108.1 112.2 112.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 604  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  90   OD1                                                    
REMARK 620 2 GLU B 191   OE1  87.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 207   SG                                                     
REMARK 620 2 CYS B 210   SG   98.4                                              
REMARK 620 3 CYS B 226   SG  110.3 123.8                                        
REMARK 620 4 HIS B 229   ND1 169.2  81.3  62.1                                  
REMARK 620 5 HIS B 229   NE2 126.8  92.9 105.5  63.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 602  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 257   NE2                                                    
REMARK 620 2 CYS B 261   SG  106.6                                              
REMARK 620 3 HIS B 264   ND1 113.1  92.2                                        
REMARK 620 4 CYS B 279   SG   98.2 120.2 126.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 603  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 452   SG                                                     
REMARK 620 2 CYS B 477   SG  112.5                                              
REMARK 620 3 CYS B 484   SG   98.8 110.4                                        
REMARK 620 4 HIS B 487   ND1 107.5 112.9 114.0                                  
REMARK 620 5 HIS B 487   NE2  59.0  97.8 149.8  61.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  74   SG                                                     
REMARK 620 2 CYS C  77   SG  106.9                                              
REMARK 620 3 HIS C  83   NE2 116.1  98.7                                        
REMARK 620 4 CYS C  90   SG  111.2 116.5 107.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 117   SG                                                     
REMARK 620 2 CYS C 120   SG  110.2                                              
REMARK 620 3 CYS C 128   SG  113.1 101.7                                        
REMARK 620 4 CYS C 130   SG  108.4 115.2 108.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 604  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  90   OD1                                                    
REMARK 620 2 ASP D  90   OD2  50.7                                              
REMARK 620 3 GLU D 191   OE1  93.3 100.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 207   SG                                                     
REMARK 620 2 CYS D 210   SG  101.6                                              
REMARK 620 3 CYS D 226   SG  109.2 108.6                                        
REMARK 620 4 HIS D 229   ND1  67.5 163.0  87.7                                  
REMARK 620 5 HIS D 229   NE2 108.3 114.6 113.7  60.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 602  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 257   NE2                                                    
REMARK 620 2 CYS D 261   SG   99.3                                              
REMARK 620 3 HIS D 264   ND1 121.5 107.0                                        
REMARK 620 4 HIS D 264   NE2  86.8 158.9  53.6                                  
REMARK 620 5 CYS D 279   SG  101.6 108.8 116.9  89.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 603  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 452   SG                                                     
REMARK 620 2 CYS D 477   SG  104.3                                              
REMARK 620 3 CYS D 484   SG  108.8  95.7                                        
REMARK 620 4 HIS D 487   ND1 111.8 123.4 111.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 604                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5C8S   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5C8T   RELATED DB: PDB                                   
DBREF  5C8U A    1   139  UNP    P0C6X7   R1AB_CVHSA    4231   4369             
DBREF  5C8U B    1   527  UNP    P0C6X7   R1AB_CVHSA    5903   6429             
DBREF  5C8U C    1   139  UNP    P0C6X7   R1AB_CVHSA    4231   4369             
DBREF  5C8U D    1   527  UNP    P0C6X7   R1AB_CVHSA    5903   6429             
SEQADV 5C8U GLY A   -4  UNP  P0C6X7              EXPRESSION TAG                 
SEQADV 5C8U PRO A   -3  UNP  P0C6X7              EXPRESSION TAG                 
SEQADV 5C8U LEU A   -2  UNP  P0C6X7              EXPRESSION TAG                 
SEQADV 5C8U GLY A   -1  UNP  P0C6X7              EXPRESSION TAG                 
SEQADV 5C8U SER A    0  UNP  P0C6X7              EXPRESSION TAG                 
SEQADV 5C8U MET B    0  UNP  P0C6X7              EXPRESSION TAG                 
SEQADV 5C8U GLY C   -4  UNP  P0C6X7              EXPRESSION TAG                 
SEQADV 5C8U PRO C   -3  UNP  P0C6X7              EXPRESSION TAG                 
SEQADV 5C8U LEU C   -2  UNP  P0C6X7              EXPRESSION TAG                 
SEQADV 5C8U GLY C   -1  UNP  P0C6X7              EXPRESSION TAG                 
SEQADV 5C8U SER C    0  UNP  P0C6X7              EXPRESSION TAG                 
SEQADV 5C8U MET D    0  UNP  P0C6X7              EXPRESSION TAG                 
SEQRES   1 A  144  GLY PRO LEU GLY SER ALA GLY ASN ALA THR GLU VAL PRO          
SEQRES   2 A  144  ALA ASN SER THR VAL LEU SER PHE CYS ALA PHE ALA VAL          
SEQRES   3 A  144  ASP PRO ALA LYS ALA TYR LYS ASP TYR LEU ALA SER GLY          
SEQRES   4 A  144  GLY GLN PRO ILE THR ASN CYS VAL LYS MET LEU CYS THR          
SEQRES   5 A  144  HIS THR GLY THR GLY GLN ALA ILE THR VAL THR PRO GLU          
SEQRES   6 A  144  ALA ASN MET ASP GLN GLU SER PHE GLY GLY ALA SER CYS          
SEQRES   7 A  144  CYS LEU TYR CYS ARG CYS HIS ILE ASP HIS PRO ASN PRO          
SEQRES   8 A  144  LYS GLY PHE CYS ASP LEU LYS GLY LYS TYR VAL GLN ILE          
SEQRES   9 A  144  PRO THR THR CYS ALA ASN ASP PRO VAL GLY PHE THR LEU          
SEQRES  10 A  144  ARG ASN THR VAL CYS THR VAL CYS GLY MET TRP LYS GLY          
SEQRES  11 A  144  TYR GLY CYS SER CYS ASP GLN LEU ARG GLU PRO LEU MET          
SEQRES  12 A  144  GLN                                                          
SEQRES   1 B  528  MET ALA GLU ASN VAL THR GLY LEU PHE LYS ASP CYS SER          
SEQRES   2 B  528  LYS ILE ILE THR GLY LEU HIS PRO THR GLN ALA PRO THR          
SEQRES   3 B  528  HIS LEU SER VAL ASP ILE LYS PHE LYS THR GLU GLY LEU          
SEQRES   4 B  528  CYS VAL ASP ILE PRO GLY ILE PRO LYS ASP MET THR TYR          
SEQRES   5 B  528  ARG ARG LEU ILE SER MET MET GLY PHE LYS MET ASN TYR          
SEQRES   6 B  528  GLN VAL ASN GLY TYR PRO ASN MET PHE ILE THR ARG GLU          
SEQRES   7 B  528  GLU ALA ILE ARG HIS VAL ARG ALA TRP ILE GLY PHE ASP          
SEQRES   8 B  528  VAL GLU GLY CYS HIS ALA THR ARG ASP ALA VAL GLY THR          
SEQRES   9 B  528  ASN LEU PRO LEU GLN LEU GLY PHE SER THR GLY VAL ASN          
SEQRES  10 B  528  LEU VAL ALA VAL PRO THR GLY TYR VAL ASP THR GLU ASN          
SEQRES  11 B  528  ASN THR GLU PHE THR ARG VAL ASN ALA LYS PRO PRO PRO          
SEQRES  12 B  528  GLY ASP GLN PHE LYS HIS LEU ILE PRO LEU MET TYR LYS          
SEQRES  13 B  528  GLY LEU PRO TRP ASN VAL VAL ARG ILE LYS ILE VAL GLN          
SEQRES  14 B  528  MET LEU SER ASP THR LEU LYS GLY LEU SER ASP ARG VAL          
SEQRES  15 B  528  VAL PHE VAL LEU TRP ALA HIS GLY PHE GLU LEU THR SER          
SEQRES  16 B  528  MET LYS TYR PHE VAL LYS ILE GLY PRO GLU ARG THR CYS          
SEQRES  17 B  528  CYS LEU CYS ASP LYS ARG ALA THR CYS PHE SER THR SER          
SEQRES  18 B  528  SER ASP THR TYR ALA CYS TRP ASN HIS SER VAL GLY PHE          
SEQRES  19 B  528  ASP TYR VAL TYR ASN PRO PHE MET ILE ASP VAL GLN GLN          
SEQRES  20 B  528  TRP GLY PHE THR GLY ASN LEU GLN SER ASN HIS ASP GLN          
SEQRES  21 B  528  HIS CYS GLN VAL HIS GLY ASN ALA HIS VAL ALA SER CYS          
SEQRES  22 B  528  ASP ALA ILE MET THR ARG CYS LEU ALA VAL HIS GLU CYS          
SEQRES  23 B  528  PHE VAL LYS ARG VAL ASP TRP SER VAL GLU TYR PRO ILE          
SEQRES  24 B  528  ILE GLY ASP GLU LEU ARG VAL ASN SER ALA CYS ARG LYS          
SEQRES  25 B  528  VAL GLN HIS MET VAL VAL LYS SER ALA LEU LEU ALA ASP          
SEQRES  26 B  528  LYS PHE PRO VAL LEU HIS ASP ILE GLY ASN PRO LYS ALA          
SEQRES  27 B  528  ILE LYS CYS VAL PRO GLN ALA GLU VAL GLU TRP LYS PHE          
SEQRES  28 B  528  TYR ASP ALA GLN PRO CYS SER ASP LYS ALA TYR LYS ILE          
SEQRES  29 B  528  GLU GLU LEU PHE TYR SER TYR ALA THR HIS HIS ASP LYS          
SEQRES  30 B  528  PHE THR ASP GLY VAL CYS LEU PHE TRP ASN CYS ASN VAL          
SEQRES  31 B  528  ASP ARG TYR PRO ALA ASN ALA ILE VAL CYS ARG PHE ASP          
SEQRES  32 B  528  THR ARG VAL LEU SER ASN LEU ASN LEU PRO GLY CYS ASP          
SEQRES  33 B  528  GLY GLY SER LEU TYR VAL ASN LYS HIS ALA PHE HIS THR          
SEQRES  34 B  528  PRO ALA PHE ASP LYS SER ALA PHE THR ASN LEU LYS GLN          
SEQRES  35 B  528  LEU PRO PHE PHE TYR TYR SER ASP SER PRO CYS GLU SER          
SEQRES  36 B  528  HIS GLY LYS GLN VAL VAL SER ASP ILE ASP TYR VAL PRO          
SEQRES  37 B  528  LEU LYS SER ALA THR CYS ILE THR ARG CYS ASN LEU GLY          
SEQRES  38 B  528  GLY ALA VAL CYS ARG HIS HIS ALA ASN GLU TYR ARG GLN          
SEQRES  39 B  528  TYR LEU ASP ALA TYR ASN MET MET ILE SER ALA GLY PHE          
SEQRES  40 B  528  SER LEU TRP ILE TYR LYS GLN PHE ASP THR TYR ASN LEU          
SEQRES  41 B  528  TRP ASN THR PHE THR ARG LEU GLN                              
SEQRES   1 C  144  GLY PRO LEU GLY SER ALA GLY ASN ALA THR GLU VAL PRO          
SEQRES   2 C  144  ALA ASN SER THR VAL LEU SER PHE CYS ALA PHE ALA VAL          
SEQRES   3 C  144  ASP PRO ALA LYS ALA TYR LYS ASP TYR LEU ALA SER GLY          
SEQRES   4 C  144  GLY GLN PRO ILE THR ASN CYS VAL LYS MET LEU CYS THR          
SEQRES   5 C  144  HIS THR GLY THR GLY GLN ALA ILE THR VAL THR PRO GLU          
SEQRES   6 C  144  ALA ASN MET ASP GLN GLU SER PHE GLY GLY ALA SER CYS          
SEQRES   7 C  144  CYS LEU TYR CYS ARG CYS HIS ILE ASP HIS PRO ASN PRO          
SEQRES   8 C  144  LYS GLY PHE CYS ASP LEU LYS GLY LYS TYR VAL GLN ILE          
SEQRES   9 C  144  PRO THR THR CYS ALA ASN ASP PRO VAL GLY PHE THR LEU          
SEQRES  10 C  144  ARG ASN THR VAL CYS THR VAL CYS GLY MET TRP LYS GLY          
SEQRES  11 C  144  TYR GLY CYS SER CYS ASP GLN LEU ARG GLU PRO LEU MET          
SEQRES  12 C  144  GLN                                                          
SEQRES   1 D  528  MET ALA GLU ASN VAL THR GLY LEU PHE LYS ASP CYS SER          
SEQRES   2 D  528  LYS ILE ILE THR GLY LEU HIS PRO THR GLN ALA PRO THR          
SEQRES   3 D  528  HIS LEU SER VAL ASP ILE LYS PHE LYS THR GLU GLY LEU          
SEQRES   4 D  528  CYS VAL ASP ILE PRO GLY ILE PRO LYS ASP MET THR TYR          
SEQRES   5 D  528  ARG ARG LEU ILE SER MET MET GLY PHE LYS MET ASN TYR          
SEQRES   6 D  528  GLN VAL ASN GLY TYR PRO ASN MET PHE ILE THR ARG GLU          
SEQRES   7 D  528  GLU ALA ILE ARG HIS VAL ARG ALA TRP ILE GLY PHE ASP          
SEQRES   8 D  528  VAL GLU GLY CYS HIS ALA THR ARG ASP ALA VAL GLY THR          
SEQRES   9 D  528  ASN LEU PRO LEU GLN LEU GLY PHE SER THR GLY VAL ASN          
SEQRES  10 D  528  LEU VAL ALA VAL PRO THR GLY TYR VAL ASP THR GLU ASN          
SEQRES  11 D  528  ASN THR GLU PHE THR ARG VAL ASN ALA LYS PRO PRO PRO          
SEQRES  12 D  528  GLY ASP GLN PHE LYS HIS LEU ILE PRO LEU MET TYR LYS          
SEQRES  13 D  528  GLY LEU PRO TRP ASN VAL VAL ARG ILE LYS ILE VAL GLN          
SEQRES  14 D  528  MET LEU SER ASP THR LEU LYS GLY LEU SER ASP ARG VAL          
SEQRES  15 D  528  VAL PHE VAL LEU TRP ALA HIS GLY PHE GLU LEU THR SER          
SEQRES  16 D  528  MET LYS TYR PHE VAL LYS ILE GLY PRO GLU ARG THR CYS          
SEQRES  17 D  528  CYS LEU CYS ASP LYS ARG ALA THR CYS PHE SER THR SER          
SEQRES  18 D  528  SER ASP THR TYR ALA CYS TRP ASN HIS SER VAL GLY PHE          
SEQRES  19 D  528  ASP TYR VAL TYR ASN PRO PHE MET ILE ASP VAL GLN GLN          
SEQRES  20 D  528  TRP GLY PHE THR GLY ASN LEU GLN SER ASN HIS ASP GLN          
SEQRES  21 D  528  HIS CYS GLN VAL HIS GLY ASN ALA HIS VAL ALA SER CYS          
SEQRES  22 D  528  ASP ALA ILE MET THR ARG CYS LEU ALA VAL HIS GLU CYS          
SEQRES  23 D  528  PHE VAL LYS ARG VAL ASP TRP SER VAL GLU TYR PRO ILE          
SEQRES  24 D  528  ILE GLY ASP GLU LEU ARG VAL ASN SER ALA CYS ARG LYS          
SEQRES  25 D  528  VAL GLN HIS MET VAL VAL LYS SER ALA LEU LEU ALA ASP          
SEQRES  26 D  528  LYS PHE PRO VAL LEU HIS ASP ILE GLY ASN PRO LYS ALA          
SEQRES  27 D  528  ILE LYS CYS VAL PRO GLN ALA GLU VAL GLU TRP LYS PHE          
SEQRES  28 D  528  TYR ASP ALA GLN PRO CYS SER ASP LYS ALA TYR LYS ILE          
SEQRES  29 D  528  GLU GLU LEU PHE TYR SER TYR ALA THR HIS HIS ASP LYS          
SEQRES  30 D  528  PHE THR ASP GLY VAL CYS LEU PHE TRP ASN CYS ASN VAL          
SEQRES  31 D  528  ASP ARG TYR PRO ALA ASN ALA ILE VAL CYS ARG PHE ASP          
SEQRES  32 D  528  THR ARG VAL LEU SER ASN LEU ASN LEU PRO GLY CYS ASP          
SEQRES  33 D  528  GLY GLY SER LEU TYR VAL ASN LYS HIS ALA PHE HIS THR          
SEQRES  34 D  528  PRO ALA PHE ASP LYS SER ALA PHE THR ASN LEU LYS GLN          
SEQRES  35 D  528  LEU PRO PHE PHE TYR TYR SER ASP SER PRO CYS GLU SER          
SEQRES  36 D  528  HIS GLY LYS GLN VAL VAL SER ASP ILE ASP TYR VAL PRO          
SEQRES  37 D  528  LEU LYS SER ALA THR CYS ILE THR ARG CYS ASN LEU GLY          
SEQRES  38 D  528  GLY ALA VAL CYS ARG HIS HIS ALA ASN GLU TYR ARG GLN          
SEQRES  39 D  528  TYR LEU ASP ALA TYR ASN MET MET ILE SER ALA GLY PHE          
SEQRES  40 D  528  SER LEU TRP ILE TYR LYS GLN PHE ASP THR TYR ASN LEU          
SEQRES  41 D  528  TRP ASN THR PHE THR ARG LEU GLN                              
HET     ZN  A 201       1                                                       
HET     ZN  A 202       1                                                       
HET     ZN  B 601       1                                                       
HET     ZN  B 602       1                                                       
HET     ZN  B 603       1                                                       
HET     MG  B 604       1                                                       
HET     ZN  C 201       1                                                       
HET     ZN  C 202       1                                                       
HET     ZN  D 601       1                                                       
HET     ZN  D 602       1                                                       
HET     ZN  D 603       1                                                       
HET     MG  D 604       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   5   ZN    10(ZN 2+)                                                    
FORMUL  10   MG    2(MG 2+)                                                     
HELIX    1   1 VAL C    7  ALA C   20  1                                  14
HELIX    2   2 ASP C   22  GLY C   34  1                                  13
HELIX    3   3 ALA C   71  CYS C   79  1                                   9
HELIX    4   4 ASP C  106  ASN C  114  1                                   9
HELIX    5   5 ASP D   30  LYS D   32  1                                   3
HELIX    6   6 THR D   75  HIS D   82  1                                   8
HELIX    7   7 GLY D  143  TYR D  154  1                                  12
HELIX    8   8 PRO D  158  GLY D  176  1                                  19
HELIX    9   9 ALA D  187  VAL D  199  1                                  13
HELIX   10  10 GLN D  245  TRP D  247  1                                   3
HELIX   11  11 ASN D  252  CYS D  261  1                                  10
HELIX   12  12 VAL D  269  PHE D  286  1                                  18
HELIX   13  13 ASP D  301  ASP D  324  1                                  24
HELIX   14  14 SER D  369  HIS D  374  1                                   6
HELIX   15  15 CYS D  484  ALA D  504  1                                  21
HELIX   16  16 THR D  516  ARG D  525  1                                  10
SHEET    1   1 1 LYS C  43  MET C  44  0
SHEET    2   2 1 GLU C  66  GLY C  69  0
SHEET    3   3 1 TYR C  96  ILE C  99  0
SHEET    4   4 1 LYS D  34  THR D  35  0
SHEET    5   5 1 LEU D  38  CYS D  39  0
SHEET    6   6 1 ARG D  53  ILE D  55  0
SHEET    7   7 1 TRP D  86  ALA D  96  0
SHEET    8   8 1 ASN D 104  PHE D 111  0
SHEET    9   9 1 ASN D 116  VAL D 118  0
SHEET   10  10 1 THR D 122  ASP D 126  0
SHEET   11  11 1 THR D 131  ARG D 135  0
SHEET   12  12 1 ALA D 138  LYS D 139  0
SHEET   13  13 1 VAL D 182  LEU D 185  0
SHEET   14  14 1 CYS D 216  SER D 218  0
SHEET   15  15 1 THR D 223  ALA D 225  0
SHEET   16  16 1 TYR D 235  VAL D 236  0
SHEET   17  17 1 PHE D 240  ASP D 243  0
SHEET   18  18 1 VAL D 328  ILE D 332  0
SHEET   19  19 1 GLU D 347  TYR D 351  0
SHEET   20  20 1 VAL D 381  TRP D 385  0
SHEET   21  21 1 ALA D 396  PHE D 401  0
SHEET   22  22 1 ASN D 410  PRO D 412  0
SHEET   23  23 1 SER D 418  TYR D 420  0
SHEET   24  24 1 HIS D 427  THR D 428  0
SHEET   25  25 1 LYS D 440  GLN D 441  0
SHEET   26  26 1 TYR D 446  TYR D 447  0
SHEET   27  27 1 CYS D 473  ILE D 474  0
SHEET   28  28 1 PHE D 506  ILE D 510  0
LINK         SG  CYS A  74                ZN    ZN A 201     1555   1555  2.23  
LINK         SG  CYS A  77                ZN    ZN A 201     1555   1555  2.31  
LINK         NE2 HIS A  83                ZN    ZN A 201     1555   1555  2.17  
LINK         SG  CYS A  90                ZN    ZN A 201     1555   1555  2.22  
LINK         SG  CYS A 117                ZN    ZN A 202     1555   1555  2.35  
LINK         SG  CYS A 120                ZN    ZN A 202     1555   1555  2.31  
LINK         SG  CYS A 128                ZN    ZN A 202     1555   1555  2.28  
LINK         SG  CYS A 130                ZN    ZN A 202     1555   1555  2.31  
LINK         OD1 ASP B  90                MG    MG B 604     1555   1555  2.00  
LINK         OE1 GLU B 191                MG    MG B 604     1555   1555  2.08  
LINK         SG  CYS B 207                ZN    ZN B 601     1555   1555  2.47  
LINK         SG  CYS B 210                ZN    ZN B 601     1555   1555  2.23  
LINK         SG  CYS B 226                ZN    ZN B 601     1555   1555  2.33  
LINK         ND1 HIS B 229                ZN    ZN B 601     1555   1555  1.96  
LINK         NE2 HIS B 229                ZN    ZN B 601     1555   1555  2.08  
LINK         NE2 HIS B 257                ZN    ZN B 602     1555   1555  2.32  
LINK         SG  CYS B 261                ZN    ZN B 602     1555   1555  2.07  
LINK         ND1 HIS B 264                ZN    ZN B 602     1555   1555  2.68  
LINK         SG  CYS B 279                ZN    ZN B 602     1555   1555  2.17  
LINK         SG  CYS B 452                ZN    ZN B 603     1555   1555  2.47  
LINK         SG  CYS B 477                ZN    ZN B 603     1555   1555  2.56  
LINK         SG  CYS B 484                ZN    ZN B 603     1555   1555  2.48  
LINK         ND1 HIS B 487                ZN    ZN B 603     1555   1555  2.07  
LINK         NE2 HIS B 487                ZN    ZN B 603     1555   1555  2.12  
LINK         SG  CYS C  74                ZN    ZN C 201     1555   1555  2.22  
LINK         SG  CYS C  77                ZN    ZN C 201     1555   1555  2.27  
LINK         NE2 HIS C  83                ZN    ZN C 201     1555   1555  2.33  
LINK         SG  CYS C  90                ZN    ZN C 201     1555   1555  2.28  
LINK         SG  CYS C 117                ZN    ZN C 202     1555   1555  2.30  
LINK         SG  CYS C 120                ZN    ZN C 202     1555   1555  2.42  
LINK         SG  CYS C 128                ZN    ZN C 202     1555   1555  2.38  
LINK         SG  CYS C 130                ZN    ZN C 202     1555   1555  2.43  
LINK         OD1 ASP D  90                MG    MG D 604     1555   1555  2.17  
LINK         OD2 ASP D  90                MG    MG D 604     1555   1555  2.80  
LINK         OE1 GLU D 191                MG    MG D 604     1555   1555  2.33  
LINK         SG  CYS D 207                ZN    ZN D 601     1555   1555  2.54  
LINK         SG  CYS D 210                ZN    ZN D 601     1555   1555  2.26  
LINK         SG  CYS D 226                ZN    ZN D 601     1555   1555  2.50  
LINK         ND1 HIS D 229                ZN    ZN D 601     1555   1555  1.78  
LINK         NE2 HIS D 229                ZN    ZN D 601     1555   1555  2.36  
LINK         NE2 HIS D 257                ZN    ZN D 602     1555   1555  2.39  
LINK         SG  CYS D 261                ZN    ZN D 602     1555   1555  2.44  
LINK         ND1 HIS D 264                ZN    ZN D 602     1555   1555  2.65  
LINK         NE2 HIS D 264                ZN    ZN D 602     1555   1555  1.72  
LINK         SG  CYS D 279                ZN    ZN D 602     1555   1555  2.39  
LINK         SG  CYS D 452                ZN    ZN D 603     1555   1555  2.32  
LINK         SG  CYS D 477                ZN    ZN D 603     1555   1555  2.25  
LINK         SG  CYS D 484                ZN    ZN D 603     1555   1555  2.45  
LINK         ND1 HIS D 487                ZN    ZN D 603     1555   1555  1.95  
CISPEP   1 SER A    0    ALA A    1          0       -18.32                     
CISPEP   2 TYR A  126    GLY A  127          0        14.66                     
CISPEP   3 ALA B    1    GLU B    2          0         3.44                     
CISPEP   4 GLY B  156    LEU B  157          0        -8.94                     
CISPEP   5 ILE B  299    GLY B  300          0        -1.16                     
CISPEP   6 CYS B  414    ASP B  415          0       -24.40                     
CISPEP   7 GLY B  481    ALA B  482          0       -12.18                     
CISPEP   8 THR C   47    HIS C   48          0         1.04                     
CISPEP   9 ALA C   54    ILE C   55          0         6.62                     
CISPEP  10 CYS C  120    GLY C  121          0       -12.25                     
CISPEP  11 GLU D    2    ASN D    3          0       -10.75                     
CISPEP  12 GLY D   17    LEU D   18          0         1.43                     
CISPEP  13 LYS D  359    ALA D  360          0        -0.86                     
CISPEP  14 CYS D  414    ASP D  415          0        -7.57                     
SITE     1 AC1  4 CYS A  74  CYS A  77  HIS A  83  CYS A  90                    
SITE     1 AC2  4 CYS A 117  CYS A 120  CYS A 128  CYS A 130                    
SITE     1 AC3  4 CYS B 207  CYS B 210  CYS B 226  HIS B 229                    
SITE     1 AC4  4 HIS B 257  CYS B 261  HIS B 264  CYS B 279                    
SITE     1 AC5  4 CYS B 452  CYS B 477  CYS B 484  HIS B 487                    
SITE     1 AC6  3 ASP B  90  ALA B 187  GLU B 191                               
SITE     1 AC7  4 CYS C  74  CYS C  77  HIS C  83  CYS C  90                    
SITE     1 AC8  4 CYS C 117  CYS C 120  CYS C 128  CYS C 130                    
SITE     1 AC9  4 CYS D 207  CYS D 210  CYS D 226  HIS D 229                    
SITE     1 AD1  4 HIS D 257  CYS D 261  HIS D 264  CYS D 279                    
SITE     1 AD2  4 CYS D 452  CYS D 477  CYS D 484  HIS D 487                    
SITE     1 AD3  3 ASP D  90  ALA D 187  GLU D 191                               
CRYST1  189.928  194.979  179.844  90.00  90.00  90.00 C 2 2 21     16          
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      0.005265  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005129  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005560        0.00000                         
ATOM      1  N   GLY C  -1     -12.787-100.295 -41.245  1.00136.32           N
ANISOU    1  N   GLY C  -1    17876  17648  16273  -1701   -552  -3803       N
ATOM      2  CA  GLY C  -1     -12.267-101.275 -42.186  1.00172.17           C
ANISOU    2  CA  GLY C  -1    22502  22184  20732  -1691   -499  -3869       C
ATOM      3  C   GLY C  -1     -13.053-101.369 -43.488  1.00197.60           C
ANISOU    3  C   GLY C  -1    25825  25399  23857  -1727   -575  -3907       C
ATOM      4  O   GLY C  -1     -14.212-100.939 -43.568  1.00206.49           O
ANISOU    4  O   GLY C  -1    26951  26511  24997  -1764   -680  -3891       O
ATOM      5  N   SER C   0     -12.411-101.937 -44.507  1.00196.23           N
ANISOU    5  N   SER C   0    25739  25236  23581  -1716   -522  -3955       N
ATOM      6  CA  SER C   0     -13.023-102.137 -45.817  1.00206.86           C
ANISOU    6  CA  SER C   0    27193  26578  24826  -1747   -584  -3999       C
ATOM      7  C   SER C   0     -14.090-103.230 -45.789  1.00216.42           C
ANISOU    7  C   SER C   0    28432  27721  26079  -1762   -656  -4059       C
ATOM      8  O   SER C   0     -15.189-103.058 -46.321  1.00214.50           O
ANISOU    8  O   SER C   0    28229  27461  25812  -1806   -759  -4063       O
ATOM      9  CB  SER C   0     -11.947-102.495 -46.841  1.00187.76           C
ANISOU    9  CB  SER C   0    24858  24192  22289  -1720   -497  -4034       C
ATOM     10  OG  SER C   0     -10.718-102.778 -46.193  1.00172.84           O
ANISOU   10  OG  SER C   0    22922  22319  20431  -1671   -380  -4022       O
ATOM     11  N   ALA C   1     -13.756-104.350 -45.155  1.00203.44           N
ANISOU   11  N   ALA C   1    26762  26039  24498  -1727   -604  -4102       N
ATOM     12  CA  ALA C   1     -14.663-105.489 -45.057  1.00162.89           C
ANISOU   12  CA  ALA C   1    21646  20835  19408  -1737   -668  -4158       C
ATOM     13  C   ALA C   1     -15.904-105.142 -44.236  1.00154.76           C
ANISOU   13  C   ALA C   1    20540  19780  18482  -1767   -773  -4115       C
ATOM     14  O   ALA C   1     -15.885-104.197 -43.448  1.00157.04           O
ANISOU   14  O   ALA C   1    20743  20097  18829  -1765   -772  -4048       O
ATOM     15  CB  ALA C   1     -13.943-106.677 -44.446  1.00111.27           C
ANISOU   15  CB  ALA C   1    15082  14268  12927  -1691   -583  -4204       C
ATOM     16  N   GLY C   2     -16.984-105.895 -44.437  1.00128.83           N
ANISOU   16  N   GLY C   2    17289  16442  15216  -1792   -865  -4149       N
ATOM     17  CA  GLY C   2     -18.179-105.744 -43.622  1.00131.32           C
ANISOU   17  CA  GLY C   2    17530  16731  15634  -1813   -963  -4106       C
ATOM     18  C   GLY C   2     -19.250-104.827 -44.187  1.00124.52           C
ANISOU   18  C   GLY C   2    16698  15881  14733  -1865  -1070  -4062       C
ATOM     19  O   GLY C   2     -18.993-104.001 -45.060  1.00133.76           O
ANISOU   19  O   GLY C   2    17925  17092  15806  -1886  -1063  -4049       O
ATOM     20  N   ASN C   3     -20.465-104.974 -43.678  1.00118.63           N
ANISOU   20  N   ASN C   3    15909  15100  14064  -1887  -1170  -4034       N
ATOM     21  CA  ASN C   3     -21.589-104.186 -44.162  1.00121.80           C
ANISOU   21  CA  ASN C   3    16335  15507  14436  -1938  -1278  -3986       C
ATOM     22  C   ASN C   3     -22.130-103.314 -43.044  1.00109.52           C
ANISOU   22  C   ASN C   3    14667  13969  12977  -1931  -1313  -3905       C
ATOM     23  O   ASN C   3     -22.569-103.814 -42.016  1.00124.71           O
ANISOU   23  O   ASN C   3    16510  15864  15008  -1910  -1336  -3890       O
ATOM     24  CB  ASN C   3     -22.701-105.094 -44.706  1.00104.03           C
ANISOU   24  CB  ASN C   3    14148  13200  12178  -1975  -1381  -4015       C
ATOM     25  CG  ASN C   3     -22.171-106.403 -45.269  1.00137.52           C
ANISOU   25  CG  ASN C   3    18470  17404  16378  -1960  -1343  -4104       C
ATOM     26  OD1 ASN C   3     -22.690-107.479 -44.954  1.00163.61           O
ANISOU   26  OD1 ASN C   3    21768  20654  19742  -1957  -1389  -4131       O
ATOM     27  ND2 ASN C   3     -21.138-106.318 -46.115  1.00121.26           N
ANISOU   27  ND2 ASN C   3    16486  15374  14213  -1948  -1260  -4148       N
ATOM     28  N   ALA C   4     -22.097-102.007 -43.248  1.00 89.74           N
ANISOU   28  N   ALA C   4    12156  11509  10432  -1948  -1318  -3853       N
ATOM     29  CA  ALA C   4     -22.533-101.076 -42.220  1.00122.15           C
ANISOU   29  CA  ALA C   4    16161  15632  14619  -1937  -1347  -3776       C
ATOM     30  C   ALA C   4     -23.992-101.270 -41.811  1.00105.84           C
ANISOU   30  C   ALA C   4    14060  13532  12621  -1957  -1461  -3736       C
ATOM     31  O   ALA C   4     -24.817-101.690 -42.602  1.00 85.78           O
ANISOU   31  O   ALA C   4    11588  10965  10039  -1999  -1538  -3749       O
ATOM     32  CB  ALA C   4     -22.284 -99.645 -42.658  1.00151.39           C
ANISOU   32  CB  ALA C   4    19877  19387  18257  -1956  -1342  -3729       C
ATOM     33  N   THR C   5     -24.258-101.023 -40.535  1.00119.54           N
ANISOU   33  N   THR C   5    15688  15269  14463  -1923  -1468  -3686       N
ATOM     34  CA  THR C   5     -25.584-101.110 -39.962  1.00120.13           C
ANISOU   34  CA  THR C   5    15711  15321  14613  -1930  -1569  -3634       C
ATOM     35  C   THR C   5     -26.305 -99.766 -39.833  1.00143.65           C
ANISOU   35  C   THR C   5    18662  18329  17590  -1946  -1629  -3552       C
ATOM     36  O   THR C   5     -27.504 -99.718 -39.554  1.00145.34           O
ANISOU   36  O   THR C   5    18847  18528  17848  -1958  -1721  -3499       O
ATOM     37  CB  THR C   5     -25.453-101.719 -38.574  1.00140.32           C
ANISOU   37  CB  THR C   5    18158  17863  17293  -1875  -1540  -3627       C
ATOM     38  OG1 THR C   5     -24.332-102.609 -38.576  1.00144.33           O
ANISOU   38  OG1 THR C   5    18679  18361  17798  -1851  -1445  -3700       O
ATOM     39  CG2 THR C   5     -26.706-102.477 -38.184  1.00160.34           C
ANISOU   39  CG2 THR C   5    20658  20362  19902  -1881  -1639  -3601       C
ATOM     40  N   GLU C   6     -25.597 -98.661 -40.033  1.00146.37           N
ANISOU   40  N   GLU C   6    19015  18715  17884  -1945  -1580  -3536       N
ATOM     41  CA  GLU C   6     -26.137 -97.413 -39.499  1.00129.27           C
ANISOU   41  CA  GLU C   6    16795  16576  15747  -1940  -1622  -3457       C
ATOM     42  C   GLU C   6     -25.910 -96.112 -40.266  1.00145.96           C
ANISOU   42  C   GLU C   6    18954  18729  17774  -1973  -1623  -3429       C
ATOM     43  O   GLU C   6     -24.883 -95.904 -40.922  1.00132.49           O
ANISOU   43  O   GLU C   6    17297  17048  15995  -1980  -1556  -3465       O
ATOM     44  CB  GLU C   6     -25.704 -97.253 -38.043  1.00106.87           C
ANISOU   44  CB  GLU C   6    13849  13746  13011  -1877  -1574  -3431       C
ATOM     45  CG  GLU C   6     -26.560 -98.039 -37.072  1.00121.60           C
ANISOU   45  CG  GLU C   6    15639  15581  14981  -1848  -1623  -3410       C
ATOM     46  CD  GLU C   6     -27.899 -97.378 -36.827  1.00136.79           C
ANISOU   46  CD  GLU C   6    17534  17509  16933  -1858  -1725  -3330       C
ATOM     47  OE1 GLU C   6     -28.685 -97.900 -36.004  1.00139.73           O
ANISOU   47  OE1 GLU C   6    17838  17863  17392  -1832  -1773  -3298       O
ATOM     48  OE2 GLU C   6     -28.158 -96.329 -37.456  1.00127.02           O
ANISOU   48  OE2 GLU C   6    16339  16293  15630  -1891  -1757  -3296       O
ATOM     49  N   VAL C   7     -26.911 -95.244 -40.152  1.00153.99           N
ANISOU   49  N   VAL C   7    19951  19756  18803  -1990  -1702  -3360       N
ATOM     50  CA  VAL C   7     -26.887 -93.906 -40.717  1.00160.41           C
ANISOU   50  CA  VAL C   7    20790  20606  19552  -2019  -1718  -3319       C
ATOM     51  C   VAL C   7     -26.391 -92.925 -39.660  1.00139.68           C
ANISOU   51  C   VAL C   7    18087  18005  16980  -1971  -1683  -3274       C
ATOM     52  O   VAL C   7     -26.842 -92.955 -38.512  1.00105.52           O
ANISOU   52  O   VAL C   7    13682  13666  12744  -1928  -1702  -3239       O
ATOM     53  CB  VAL C   7     -28.296 -93.495 -41.189  1.00151.62           C
ANISOU   53  CB  VAL C   7    19699  19488  18422  -2067  -1827  -3264       C
ATOM     54  CG1 VAL C   7     -29.361 -94.169 -40.325  1.00127.95           C
ANISOU   54  CG1 VAL C   7    16643  16455  15516  -2044  -1888  -3231       C
ATOM     55  CG2 VAL C   7     -28.458 -91.981 -41.170  1.00158.55           C
ANISOU   55  CG2 VAL C   7    20559  20402  19282  -2076  -1851  -3198       C
ATOM     56  N   PRO C   8     -25.444 -92.061 -40.049  1.00119.87           N
ANISOU   56  N   PRO C   8    15600  15532  14414  -1976  -1633  -3275       N
ATOM     57  CA  PRO C   8     -24.786 -91.045 -39.219  1.00119.35           C
ANISOU   57  CA  PRO C   8    15477  15490  14382  -1937  -1596  -3235       C
ATOM     58  C   PRO C   8     -25.728 -90.187 -38.383  1.00135.56           C
ANISOU   58  C   PRO C   8    17470  17541  16494  -1918  -1665  -3162       C
ATOM     59  O   PRO C   8     -25.329 -89.754 -37.305  1.00143.16           O
ANISOU   59  O   PRO C   8    18368  18508  17519  -1867  -1636  -3137       O
ATOM     60  CB  PRO C   8     -24.086 -90.171 -40.254  1.00133.34           C
ANISOU   60  CB  PRO C   8    17306  17301  16056  -1974  -1576  -3234       C
ATOM     61  CG  PRO C   8     -23.718 -91.137 -41.329  1.00147.12           C
ANISOU   61  CG  PRO C   8    19127  19043  17730  -2005  -1544  -3302       C
ATOM     62  CD  PRO C   8     -24.837 -92.152 -41.386  1.00139.87           C
ANISOU   62  CD  PRO C   8    18221  18084  16840  -2020  -1604  -3320       C
ATOM     63  N   ALA C   9     -26.935 -89.927 -38.873  1.00159.88           N
ANISOU   63  N   ALA C   9    20574  20617  19555  -1956  -1752  -3126       N
ATOM     64  CA  ALA C   9     -27.923 -89.166 -38.112  1.00173.48           C
ANISOU   64  CA  ALA C   9    22243  22339  21333  -1934  -1819  -3052       C
ATOM     65  C   ALA C   9     -28.251 -89.879 -36.797  1.00163.90           C
ANISOU   65  C   ALA C   9    20950  21100  20225  -1873  -1817  -3043       C
ATOM     66  O   ALA C   9     -28.618 -89.255 -35.790  1.00133.62           O
ANISOU   66  O   ALA C   9    17051  17268  16450  -1827  -1839  -2990       O
ATOM     67  CB  ALA C   9     -29.180 -88.966 -38.945  1.00155.49           C
ANISOU   67  CB  ALA C   9    20007  20058  19014  -1991  -1910  -3015       C
ATOM     68  N   ASN C  10     -28.112 -91.197 -36.824  1.00147.77           N
ANISOU   68  N   ASN C  10    18910  19033  18201  -1871  -1791  -3097       N
ATOM     69  CA  ASN C  10     -28.352 -92.025 -35.656  1.00150.72           C
ANISOU   69  CA  ASN C  10    19207  19385  18676  -1816  -1785  -3095       C
ATOM     70  C   ASN C  10     -27.175 -92.097 -34.667  1.00165.54           C
ANISOU   70  C   ASN C  10    21025  21267  20604  -1759  -1695  -3120       C
ATOM     71  O   ASN C  10     -27.383 -92.160 -33.454  1.00174.02           O
ANISOU   71  O   ASN C  10    22018  22337  21766  -1703  -1695  -3091       O
ATOM     72  CB  ASN C  10     -28.774 -93.432 -36.103  1.00133.52           C
ANISOU   72  CB  ASN C  10    17055  17175  16501  -1840  -1805  -3138       C
ATOM     73  CG  ASN C  10     -30.212 -93.750 -35.736  1.00162.53           C
ANISOU   73  CG  ASN C  10    20693  20832  20229  -1837  -1899  -3082       C
ATOM     74  OD1 ASN C  10     -30.921 -92.915 -35.159  1.00140.98           O
ANISOU   74  OD1 ASN C  10    17919  18116  17531  -1814  -1947  -3010       O
ATOM     75  ND2 ASN C  10     -30.653 -94.960 -36.070  1.00179.10           N
ANISOU   75  ND2 ASN C  10    22812  22900  22337  -1859  -1929  -3111       N
ATOM     76  N   SER C  11     -25.950 -92.064 -35.191  1.00150.75           N
ANISOU   76  N   SER C  11    19195  19407  18677  -1773  -1618  -3168       N
ATOM     77  CA  SER C  11     -24.759 -92.476 -34.437  1.00146.60           C
ANISOU   77  CA  SER C  11    18625  18881  18195  -1730  -1523  -3202       C
ATOM     78  C   SER C  11     -24.570 -91.811 -33.070  1.00168.61           C
ANISOU   78  C   SER C  11    21327  21675  21060  -1670  -1508  -3157       C
ATOM     79  O   SER C  11     -24.381 -92.500 -32.061  1.00162.72           O
ANISOU   79  O   SER C  11    20513  20917  20397  -1625  -1473  -3168       O
ATOM     80  CB  SER C  11     -23.485 -92.346 -35.292  1.00133.53           C
ANISOU   80  CB  SER C  11    17033  17245  16458  -1756  -1447  -3245       C
ATOM     81  OG  SER C  11     -23.031 -91.010 -35.347  1.00154.04           O
ANISOU   81  OG  SER C  11    19637  19871  19020  -1758  -1444  -3204       O
ATOM     82  N   THR C  12     -24.611 -90.482 -33.040  1.00175.15           N
ANISOU   82  N   THR C  12    22161  22523  21863  -1670  -1535  -3107       N
ATOM     83  CA  THR C  12     -24.442 -89.741 -31.790  1.00174.24           C
ANISOU   83  CA  THR C  12    21977  22414  21815  -1614  -1528  -3063       C
ATOM     84  C   THR C  12     -25.345 -90.263 -30.668  1.00147.91           C
ANISOU   84  C   THR C  12    18560  19062  18575  -1563  -1564  -3038       C
ATOM     85  O   THR C  12     -24.885 -90.533 -29.565  1.00123.34           O
ANISOU   85  O   THR C  12    15380  15947  15537  -1511  -1519  -3040       O
ATOM     86  CB  THR C  12     -24.672 -88.228 -32.001  1.00165.82           C
ANISOU   86  CB  THR C  12    20933  21365  20704  -1624  -1577  -3007       C
ATOM     87  OG1 THR C  12     -23.489 -87.639 -32.557  1.00168.20           O
ANISOU   87  OG1 THR C  12    21279  21686  20945  -1647  -1524  -3021       O
ATOM     88  CG2 THR C  12     -25.005 -87.536 -30.685  1.00122.68           C
ANISOU   88  CG2 THR C  12    15400  15900  15315  -1561  -1602  -2954       C
ATOM     89  N   VAL C  13     -26.628 -90.419 -30.961  1.00143.86           N
ANISOU   89  N   VAL C  13    18055  18543  18063  -1578  -1646  -3010       N
ATOM     90  CA  VAL C  13     -27.577 -90.899 -29.972  1.00148.70           C
ANISOU   90  CA  VAL C  13    18591  19145  18763  -1531  -1690  -2976       C
ATOM     91  C   VAL C  13     -27.168 -92.252 -29.399  1.00138.96           C
ANISOU   91  C   VAL C  13    17306  17897  17597  -1506  -1637  -3023       C
ATOM     92  O   VAL C  13     -27.242 -92.468 -28.189  1.00107.04           O
ANISOU   92  O   VAL C  13    13176  13854  13640  -1446  -1627  -3003       O
ATOM     93  CB  VAL C  13     -28.983 -91.059 -30.573  1.00164.59           C
ANISOU   93  CB  VAL C  13    20628  21151  20757  -1562  -1786  -2940       C
ATOM     94  CG1 VAL C  13     -30.028 -91.115 -29.455  1.00121.71           C
ANISOU   94  CG1 VAL C  13    15113  15720  15411  -1503  -1841  -2876       C
ATOM     95  CG2 VAL C  13     -29.274 -89.942 -31.564  1.00185.24           C
ANISOU   95  CG2 VAL C  13    23318  23781  23285  -1612  -1829  -2911       C
ATOM     96  N   LEU C  14     -26.757 -93.167 -30.272  1.00143.03           N
ANISOU   96  N   LEU C  14    17873  18399  18073  -1551  -1606  -3084       N
ATOM     97  CA  LEU C  14     -26.495 -94.540 -29.856  1.00137.84           C
ANISOU   97  CA  LEU C  14    17172  17724  17476  -1534  -1566  -3130       C
ATOM     98  C   LEU C  14     -25.260 -94.639 -28.978  1.00134.54           C
ANISOU   98  C   LEU C  14    16701  17313  17106  -1493  -1468  -3155       C
ATOM     99  O   LEU C  14     -25.308 -95.223 -27.890  1.00122.88           O
ANISOU   99  O   LEU C  14    15136  15831  15721  -1445  -1452  -3150       O
ATOM    100  CB  LEU C  14     -26.340 -95.457 -31.068  1.00132.46           C
ANISOU  100  CB  LEU C  14    16571  17025  16733  -1591  -1558  -3191       C
ATOM    101  CG  LEU C  14     -27.566 -95.660 -31.950  1.00120.02           C
ANISOU  101  CG  LEU C  14    15048  15436  15117  -1637  -1655  -3173       C
ATOM    102  CD1 LEU C  14     -27.252 -95.168 -33.337  1.00128.13           C
ANISOU  102  CD1 LEU C  14    16183  16471  16029  -1698  -1652  -3198       C
ATOM    103  CD2 LEU C  14     -27.944 -97.127 -31.977  1.00126.19           C
ANISOU  103  CD2 LEU C  14    15818  16188  15941  -1642  -1673  -3208       C
ATOM    104  N   SER C  15     -24.152 -94.079 -29.459  1.00118.36           N
ANISOU  104  N   SER C  15    14702  15275  14994  -1512  -1404  -3179       N
ATOM    105  CA  SER C  15     -22.897 -94.152 -28.723  1.00111.62           C
ANISOU  105  CA  SER C  15    13805  14427  14177  -1481  -1308  -3198       C
ATOM    106  C   SER C  15     -23.136 -93.676 -27.303  1.00117.13           C
ANISOU  106  C   SER C  15    14410  15131  14963  -1419  -1319  -3149       C
ATOM    107  O   SER C  15     -22.684 -94.298 -26.342  1.00129.06           O
ANISOU  107  O   SER C  15    15846  16638  16552  -1381  -1266  -3161       O
ATOM    108  CB  SER C  15     -21.802 -93.331 -29.411  1.00116.34           C
ANISOU  108  CB  SER C  15    14470  15042  14692  -1509  -1255  -3207       C
ATOM    109  OG  SER C  15     -22.281 -92.072 -29.844  1.00133.39           O
ANISOU  109  OG  SER C  15    16669  17215  16796  -1526  -1318  -3160       O
ATOM    110  N   PHE C  16     -23.872 -92.577 -27.185  1.00104.90           N
ANISOU  110  N   PHE C  16    12865  13591  13400  -1409  -1388  -3091       N
ATOM    111  CA  PHE C  16     -24.237 -92.026 -25.891  1.00101.71           C
ANISOU  111  CA  PHE C  16    12382  13194  13070  -1345  -1411  -3040       C
ATOM    112  C   PHE C  16     -24.933 -93.074 -25.034  1.00101.99           C
ANISOU  112  C   PHE C  16    12330  13223  13200  -1305  -1429  -3036       C
ATOM    113  O   PHE C  16     -24.738 -93.134 -23.827  1.00144.87           O
ANISOU  113  O   PHE C  16    17677  18658  18709  -1249  -1402  -3020       O
ATOM    114  CB  PHE C  16     -25.131 -90.797 -26.080  1.00110.33           C
ANISOU  114  CB  PHE C  16    13502  14294  14124  -1344  -1495  -2979       C
ATOM    115  CG  PHE C  16     -25.756 -90.280 -24.805  1.00124.83           C
ANISOU  115  CG  PHE C  16    15262  16137  16032  -1273  -1533  -2922       C
ATOM    116  CD1 PHE C  16     -27.094 -90.512 -24.537  1.00139.11           C
ANISOU  116  CD1 PHE C  16    17034  17947  17877  -1249  -1611  -2880       C
ATOM    117  CD2 PHE C  16     -25.016 -89.548 -23.890  1.00113.99           C
ANISOU  117  CD2 PHE C  16    13855  14768  14686  -1230  -1494  -2906       C
ATOM    118  CE1 PHE C  16     -27.680 -90.037 -23.377  1.00143.84           C
ANISOU  118  CE1 PHE C  16    17561  18554  18536  -1178  -1645  -2824       C
ATOM    119  CE2 PHE C  16     -25.595 -89.076 -22.732  1.00133.61           C
ANISOU  119  CE2 PHE C  16    16274  17259  17233  -1160  -1529  -2856       C
ATOM    120  CZ  PHE C  16     -26.930 -89.322 -22.474  1.00139.89           C
ANISOU  120  CZ  PHE C  16    17032  18059  18062  -1132  -1603  -2815       C
ATOM    121  N   CYS C  17     -25.742 -93.910 -25.658  1.00116.56           N
ANISOU  121  N   CYS C  17    14193  15056  15038  -1334  -1477  -3049       N
ATOM    122  CA  CYS C  17     -26.489 -94.904 -24.909  1.00135.98           C
ANISOU  122  CA  CYS C  17    16569  17511  17587  -1299  -1507  -3037       C
ATOM    123  C   CYS C  17     -25.653 -96.129 -24.566  1.00130.48           C
ANISOU  123  C   CYS C  17    15829  16804  16944  -1295  -1428  -3096       C
ATOM    124  O   CYS C  17     -25.841 -96.735 -23.506  1.00113.15           O
ANISOU  124  O   CYS C  17    13536  14613  14844  -1247  -1423  -3084       O
ATOM    125  CB  CYS C  17     -27.765 -95.296 -25.653  1.00154.57           C
ANISOU  125  CB  CYS C  17    18956  19855  19918  -1332  -1601  -3016       C
ATOM    126  SG  CYS C  17     -29.132 -94.151 -25.379  1.00141.71           S
ANISOU  126  SG  CYS C  17    17316  18243  18286  -1303  -1705  -2920       S
ATOM    127  N   ALA C  18     -24.748 -96.507 -25.468  1.00131.84           N
ANISOU  127  N   ALA C  18    16072  16966  17056  -1342  -1368  -3157       N
ATOM    128  CA  ALA C  18     -23.948 -97.712 -25.261  1.00134.45           C
ANISOU  128  CA  ALA C  18    16371  17285  17431  -1342  -1291  -3215       C
ATOM    129  C   ALA C  18     -23.014 -97.511 -24.080  1.00136.88           C
ANISOU  129  C   ALA C  18    16599  17605  17803  -1295  -1211  -3209       C
ATOM    130  O   ALA C  18     -22.675 -98.456 -23.357  1.00130.86           O
ANISOU  130  O   ALA C  18    15762  16839  17120  -1271  -1164  -3232       O
ATOM    131  CB  ALA C  18     -23.169 -98.068 -26.506  1.00101.62           C
ANISOU  131  CB  ALA C  18    12312  13115  13185  -1397  -1242  -3277       C
ATOM    132  N   PHE C  19     -22.602 -96.264 -23.891  1.00123.68           N
ANISOU  132  N   PHE C  19    14946  15949  16099  -1284  -1199  -3177       N
ATOM    133  CA  PHE C  19     -21.778 -95.911 -22.751  1.00125.73           C
ANISOU  133  CA  PHE C  19    15137  16218  16416  -1241  -1133  -3162       C
ATOM    134  C   PHE C  19     -22.590 -95.756 -21.466  1.00122.85           C
ANISOU  134  C   PHE C  19    14671  15863  16142  -1177  -1181  -3111       C
ATOM    135  O   PHE C  19     -22.139 -96.147 -20.392  1.00136.82           O
ANISOU  135  O   PHE C  19    16354  17639  17993  -1137  -1130  -3111       O
ATOM    136  CB  PHE C  19     -20.935 -94.673 -23.063  1.00116.60           C
ANISOU  136  CB  PHE C  19    14042  15070  15189  -1255  -1103  -3147       C
ATOM    137  CG  PHE C  19     -19.727 -94.984 -23.891  1.00126.55           C
ANISOU  137  CG  PHE C  19    15366  16328  16389  -1300  -1019  -3194       C
ATOM    138  CD1 PHE C  19     -18.523 -95.328 -23.292  1.00131.87           C
ANISOU  138  CD1 PHE C  19    16000  17005  17102  -1287   -920  -3211       C
ATOM    139  CD2 PHE C  19     -19.802 -94.984 -25.266  1.00120.25           C
ANISOU  139  CD2 PHE C  19    14665  15528  15496  -1352  -1038  -3220       C
ATOM    140  CE1 PHE C  19     -17.408 -95.638 -24.057  1.00 71.14           C
ANISOU  140  CE1 PHE C  19     8364   9313   9352  -1324   -841  -3249       C
ATOM    141  CE2 PHE C  19     -18.687 -95.296 -26.029  1.00135.24           C
ANISOU  141  CE2 PHE C  19    16621  17428  17336  -1386   -960  -3261       C
ATOM    142  CZ  PHE C  19     -17.490 -95.621 -25.416  1.00 98.54           C
ANISOU  142  CZ  PHE C  19    11932  12783  12727  -1370   -860  -3274       C
ATOM    143  N   ALA C  20     -23.810 -95.246 -21.594  1.00126.40           N
ANISOU  143  N   ALA C  20    15131  16318  16578  -1166  -1278  -3065       N
ATOM    144  CA  ALA C  20     -24.638 -94.903 -20.442  1.00129.46           C
ANISOU  144  CA  ALA C  20    15433  16719  17036  -1099  -1329  -3006       C
ATOM    145  C   ALA C  20     -24.812 -96.056 -19.464  1.00130.10           C
ANISOU  145  C   ALA C  20    15402  16806  17226  -1059  -1312  -3012       C
ATOM    146  O   ALA C  20     -24.828 -97.225 -19.848  1.00137.98           O
ANISOU  146  O   ALA C  20    16391  17791  18242  -1087  -1301  -3051       O
ATOM    147  CB  ALA C  20     -25.994 -94.398 -20.902  1.00140.45           C
ANISOU  147  CB  ALA C  20    16858  18115  18393  -1101  -1436  -2957       C
ATOM    148  N   VAL C  21     -24.917 -95.707 -18.187  1.00111.58           N
ANISOU  148  N   VAL C  21    12967  14476  14950   -992  -1311  -2971       N
ATOM    149  CA  VAL C  21     -25.075 -96.691 -17.131  1.00 95.78           C
ANISOU  149  CA  VAL C  21    10847  12487  13058   -947  -1296  -2968       C
ATOM    150  C   VAL C  21     -26.527 -97.136 -17.095  1.00112.87           C
ANISOU  150  C   VAL C  21    12970  14660  15255   -926  -1395  -2924       C
ATOM    151  O   VAL C  21     -26.823 -98.314 -16.862  1.00 98.67           O
ANISOU  151  O   VAL C  21    11104  12863  13523   -922  -1401  -2935       O
ATOM    152  CB  VAL C  21     -24.697 -96.083 -15.769  1.00 94.85           C
ANISOU  152  CB  VAL C  21    10650  12388  12999   -880  -1263  -2937       C
ATOM    153  CG1 VAL C  21     -24.505 -97.169 -14.738  1.00 93.10           C
ANISOU  153  CG1 VAL C  21    10305  12179  12888   -845  -1220  -2947       C
ATOM    154  CG2 VAL C  21     -23.438 -95.266 -15.894  1.00132.67           C
ANISOU  154  CG2 VAL C  21    15501  17169  17740   -902  -1190  -2958       C
ATOM    155  N   ASP C  22     -27.417 -96.171 -17.333  1.00107.66           N
ANISOU  155  N   ASP C  22    12353  14008  14548   -913  -1473  -2870       N
ATOM    156  CA  ASP C  22     -28.856 -96.392 -17.434  1.00121.91           C
ANISOU  156  CA  ASP C  22    14134  15821  16365   -897  -1574  -2814       C
ATOM    157  C   ASP C  22     -29.249 -95.989 -18.853  1.00135.69           C
ANISOU  157  C   ASP C  22    16002  17548  18008   -965  -1622  -2819       C
ATOM    158  O   ASP C  22     -29.695 -94.858 -19.074  1.00128.07           O
ANISOU  158  O   ASP C  22    15085  16587  16987   -958  -1666  -2776       O
ATOM    159  CB  ASP C  22     -29.602 -95.509 -16.421  1.00129.16           C
ANISOU  159  CB  ASP C  22    14993  16766  17314   -816  -1623  -2737       C
ATOM    160  CG  ASP C  22     -31.026 -96.004 -16.119  1.00155.82           C
ANISOU  160  CG  ASP C  22    18303  20162  20741   -778  -1716  -2668       C
ATOM    161  OD1 ASP C  22     -31.910 -95.907 -17.002  1.00151.51           O
ANISOU  161  OD1 ASP C  22    17816  19608  20142   -814  -1790  -2639       O
ATOM    162  OD2 ASP C  22     -31.265 -96.468 -14.980  1.00148.02           O
ANISOU  162  OD2 ASP C  22    17199  19199  19844   -712  -1717  -2638       O
ATOM    163  N   PRO C  23     -29.080 -96.907 -19.826  1.00136.42           N
ANISOU  163  N   PRO C  23    16143  17618  18073  -1030  -1614  -2871       N
ATOM    164  CA  PRO C  23     -29.213 -96.537 -21.243  1.00139.29           C
ANISOU  164  CA  PRO C  23    16630  17963  18332  -1101  -1643  -2888       C
ATOM    165  C   PRO C  23     -30.634 -96.077 -21.509  1.00149.17           C
ANISOU  165  C   PRO C  23    17895  19221  19561  -1096  -1752  -2814       C
ATOM    166  O   PRO C  23     -30.907 -95.243 -22.382  1.00123.65           O
ANISOU  166  O   PRO C  23    14751  15985  16245  -1134  -1786  -2800       O
ATOM    167  CB  PRO C  23     -28.966 -97.860 -21.986  1.00123.04           C
ANISOU  167  CB  PRO C  23    14597  15880  16272  -1155  -1625  -2951       C
ATOM    168  CG  PRO C  23     -28.608 -98.890 -20.923  1.00115.48           C
ANISOU  168  CG  PRO C  23    13527  14928  15422  -1113  -1580  -2968       C
ATOM    169  CD  PRO C  23     -29.156 -98.366 -19.638  1.00116.82           C
ANISOU  169  CD  PRO C  23    13597  15127  15662  -1035  -1608  -2898       C
ATOM    170  N   ALA C  24     -31.536 -96.654 -20.727  1.00161.37           N
ANISOU  170  N   ALA C  24    19347  20780  21187  -1048  -1805  -2763       N
ATOM    171  CA  ALA C  24     -32.930 -96.269 -20.688  1.00140.15           C
ANISOU  171  CA  ALA C  24    16646  18107  18499  -1025  -1906  -2675       C
ATOM    172  C   ALA C  24     -33.058 -94.775 -20.374  1.00152.72           C
ANISOU  172  C   ALA C  24    18258  19715  20052   -987  -1916  -2628       C
ATOM    173  O   ALA C  24     -33.453 -93.975 -21.231  1.00129.85           O
ANISOU  173  O   ALA C  24    15447  16814  17077  -1025  -1956  -2607       O
ATOM    174  CB  ALA C  24     -33.626 -97.089 -19.624  1.00 96.33           C
ANISOU  174  CB  ALA C  24    10971  12576  13054   -963  -1942  -2626       C
ATOM    175  N   LYS C  25     -32.698 -94.412 -19.146  1.00152.53           N
ANISOU  175  N   LYS C  25    18157  19712  20086   -912  -1878  -2612       N
ATOM    176  CA  LYS C  25     -32.751 -93.025 -18.686  1.00147.21           C
ANISOU  176  CA  LYS C  25    17496  19052  19385   -865  -1885  -2570       C
ATOM    177  C   LYS C  25     -32.037 -92.111 -19.675  1.00148.45           C
ANISOU  177  C   LYS C  25    17770  19191  19444   -926  -1857  -2610       C
ATOM    178  O   LYS C  25     -32.476 -90.984 -19.923  1.00147.17           O
ANISOU  178  O   LYS C  25    17657  19033  19228   -921  -1899  -2567       O
ATOM    179  CB  LYS C  25     -32.108 -92.904 -17.298  1.00142.46           C
ANISOU  179  CB  LYS C  25    16807  18468  18856   -787  -1828  -2573       C
ATOM    180  CG  LYS C  25     -32.478 -91.648 -16.516  1.00132.13           C
ANISOU  180  CG  LYS C  25    15484  17177  17542   -712  -1855  -2511       C
ATOM    181  CD  LYS C  25     -31.700 -90.421 -16.969  1.00131.16           C
ANISOU  181  CD  LYS C  25    15456  17038  17341   -740  -1825  -2536       C
ATOM    182  CE  LYS C  25     -31.983 -89.208 -16.089  1.00149.22           C
ANISOU  182  CE  LYS C  25    17728  19339  19629   -660  -1850  -2481       C
ATOM    183  NZ  LYS C  25     -31.488 -89.365 -14.685  1.00150.64           N
ANISOU  183  NZ  LYS C  25    17814  19533  19888   -581  -1803  -2482       N
ATOM    184  N   ALA C  26     -30.943 -92.612 -20.243  1.00138.42           N
ANISOU  184  N   ALA C  26    16541  17902  18152   -982  -1786  -2688       N
ATOM    185  CA  ALA C  26     -30.071 -91.811 -21.095  1.00127.72           C
ANISOU  185  CA  ALA C  26    15284  16534  16709  -1036  -1747  -2728       C
ATOM    186  C   ALA C  26     -30.777 -91.361 -22.361  1.00132.38           C
ANISOU  186  C   ALA C  26    15967  17118  17214  -1097  -1812  -2709       C
ATOM    187  O   ALA C  26     -30.613 -90.222 -22.805  1.00138.94           O
ANISOU  187  O   ALA C  26    16862  17950  17979  -1115  -1821  -2697       O
ATOM    188  CB  ALA C  26     -28.814 -92.582 -21.432  1.00113.95           C
ANISOU  188  CB  ALA C  26    13557  14775  14962  -1079  -1658  -2810       C
ATOM    189  N   TYR C  27     -31.555 -92.262 -22.947  1.00142.07           N
ANISOU  189  N   TYR C  27    17199  18337  18443  -1132  -1860  -2706       N
ATOM    190  CA  TYR C  27     -32.315 -91.929 -24.140  1.00165.62           C
ANISOU  190  CA  TYR C  27    20265  21314  21348  -1193  -1926  -2683       C
ATOM    191  C   TYR C  27     -33.345 -90.862 -23.783  1.00151.90           C
ANISOU  191  C   TYR C  27    18516  19593  19605  -1152  -1998  -2595       C
ATOM    192  O   TYR C  27     -33.354 -89.775 -24.365  1.00120.94           O
ANISOU  192  O   TYR C  27    14663  15675  15615  -1178  -2014  -2579       O
ATOM    193  CB  TYR C  27     -32.991 -93.184 -24.694  1.00178.15           C
ANISOU  193  CB  TYR C  27    21853  22887  22950  -1233  -1969  -2690       C
ATOM    194  CG  TYR C  27     -33.524 -93.049 -26.104  1.00168.21           C
ANISOU  194  CG  TYR C  27    20693  21616  21605  -1313  -2022  -2688       C
ATOM    195  CD1 TYR C  27     -32.766 -92.454 -27.103  1.00167.97           C
ANISOU  195  CD1 TYR C  27    20756  21579  21485  -1371  -1985  -2735       C
ATOM    196  CD2 TYR C  27     -34.776 -93.546 -26.440  1.00156.02           C
ANISOU  196  CD2 TYR C  27    19146  20066  20067  -1332  -2110  -2635       C
ATOM    197  CE1 TYR C  27     -33.250 -92.337 -28.397  1.00193.48           C
ANISOU  197  CE1 TYR C  27    24076  24802  24637  -1445  -2033  -2733       C
ATOM    198  CE2 TYR C  27     -35.268 -93.436 -27.725  1.00171.12           C
ANISOU  198  CE2 TYR C  27    21150  21966  21901  -1409  -2159  -2631       C
ATOM    199  CZ  TYR C  27     -34.504 -92.831 -28.704  1.00191.72           C
ANISOU  199  CZ  TYR C  27    23852  24571  24423  -1465  -2119  -2683       C
ATOM    200  OH  TYR C  27     -34.999 -92.722 -29.989  1.00192.49           O
ANISOU  200  OH  TYR C  27    24038  24659  24441  -1542  -2167  -2679       O
ATOM    201  N   LYS C  28     -34.179 -91.166 -22.791  1.00138.32           N
ANISOU  201  N   LYS C  28    16706  17889  17960  -1083  -2038  -2535       N
ATOM    202  CA  LYS C  28     -35.250 -90.271 -22.377  1.00139.50           C
ANISOU  202  CA  LYS C  28    16837  18058  18110  -1034  -2107  -2443       C
ATOM    203  C   LYS C  28     -34.744 -88.839 -22.195  1.00153.09           C
ANISOU  203  C   LYS C  28    18596  19783  19788  -1011  -2085  -2438       C
ATOM    204  O   LYS C  28     -35.392 -87.875 -22.617  1.00151.95           O
ANISOU  204  O   LYS C  28    18499  19644  19592  -1020  -2137  -2387       O
ATOM    205  CB  LYS C  28     -35.900 -90.786 -21.087  1.00138.35           C
ANISOU  205  CB  LYS C  28    16574  17933  18059   -945  -2131  -2388       C
ATOM    206  CG  LYS C  28     -37.037 -89.908 -20.570  1.00159.28           C
ANISOU  206  CG  LYS C  28    19199  20607  20713   -881  -2201  -2286       C
ATOM    207  CD  LYS C  28     -37.626 -90.439 -19.270  1.00154.17           C
ANISOU  207  CD  LYS C  28    18431  19986  20159   -787  -2221  -2229       C
ATOM    208  CE  LYS C  28     -38.331 -89.331 -18.487  1.00136.42           C
ANISOU  208  CE  LYS C  28    16157  17765  17913   -700  -2260  -2145       C
ATOM    209  NZ  LYS C  28     -38.195 -89.514 -17.011  1.00144.22           N
ANISOU  209  NZ  LYS C  28    17036  18778  18984   -596  -2234  -2127       N
ATOM    210  N   ASP C  29     -33.576 -88.711 -21.575  1.00169.54           N
ANISOU  210  N   ASP C  29    20660  21864  21894   -984  -2009  -2489       N
ATOM    211  CA  ASP C  29     -32.944 -87.411 -21.380  1.00167.70           C
ANISOU  211  CA  ASP C  29    20464  21630  21623   -966  -1986  -2490       C
ATOM    212  C   ASP C  29     -32.378 -86.840 -22.681  1.00156.93           C
ANISOU  212  C   ASP C  29    19206  20253  20167  -1052  -1974  -2528       C
ATOM    213  O   ASP C  29     -32.047 -85.653 -22.747  1.00146.74           O
ANISOU  213  O   ASP C  29    17958  18962  18833  -1049  -1976  -2516       O
ATOM    214  CB  ASP C  29     -31.832 -87.497 -20.326  1.00148.02           C
ANISOU  214  CB  ASP C  29    17919  19137  19185   -916  -1909  -2529       C
ATOM    215  CG  ASP C  29     -32.365 -87.469 -18.904  1.00162.63           C
ANISOU  215  CG  ASP C  29    19673  21006  21113   -813  -1927  -2477       C
ATOM    216  OD1 ASP C  29     -33.331 -88.206 -18.603  1.00150.32           O
ANISOU  216  OD1 ASP C  29    18052  19461  19601   -785  -1970  -2436       O
ATOM    217  OD2 ASP C  29     -31.813 -86.700 -18.086  1.00179.62           O
ANISOU  217  OD2 ASP C  29    21811  23159  23278   -760  -1900  -2473       O
ATOM    218  N   TYR C  30     -32.250 -87.681 -23.705  1.00136.89           N
ANISOU  218  N   TYR C  30    16709  17704  17597  -1127  -1965  -2572       N
ATOM    219  CA  TYR C  30     -31.769 -87.216 -25.002  1.00157.97           C
ANISOU  219  CA  TYR C  30    19477  20368  20178  -1209  -1956  -2606       C
ATOM    220  C   TYR C  30     -32.906 -86.564 -25.781  1.00200.43           C
ANISOU  220  C   TYR C  30    24904  25751  25501  -1243  -2039  -2548       C
ATOM    221  O   TYR C  30     -32.716 -85.566 -26.474  1.00223.51           O
ANISOU  221  O   TYR C  30    27892  28676  28356  -1281  -2050  -2543       O
ATOM    222  CB  TYR C  30     -31.148 -88.362 -25.801  1.00143.57           C
ANISOU  222  CB  TYR C  30    17683  18531  18337  -1273  -1910  -2680       C
ATOM    223  CG  TYR C  30     -30.466 -87.942 -27.096  1.00147.54           C
ANISOU  223  CG  TYR C  30    18283  19031  18746  -1351  -1888  -2721       C
ATOM    224  CD1 TYR C  30     -29.377 -87.073 -27.096  1.00132.46           C
ANISOU  224  CD1 TYR C  30    16401  17125  16803  -1353  -1838  -2741       C
ATOM    225  CD2 TYR C  30     -30.893 -88.439 -28.315  1.00146.79           C
ANISOU  225  CD2 TYR C  30    18249  18929  18595  -1423  -1918  -2738       C
ATOM    226  CE1 TYR C  30     -28.754 -86.703 -28.279  1.00144.49           C
ANISOU  226  CE1 TYR C  30    18006  18651  18241  -1422  -1819  -2773       C
ATOM    227  CE2 TYR C  30     -30.276 -88.072 -29.499  1.00141.28           C
ANISOU  227  CE2 TYR C  30    17636  18233  17811  -1491  -1898  -2775       C
ATOM    228  CZ  TYR C  30     -29.206 -87.212 -29.480  1.00154.78           C
ANISOU  228  CZ  TYR C  30    19367  19952  19490  -1489  -1848  -2791       C
ATOM    229  OH  TYR C  30     -28.597 -86.856 -30.667  1.00167.86           O
ANISOU  229  OH  TYR C  30    21102  21616  21061  -1555  -1829  -2822       O
ATOM    230  N   LEU C  31     -34.098 -87.132 -25.656  1.00211.18           N
ANISOU  230  N   LEU C  31    26229  27115  26894  -1229  -2100  -2498       N
ATOM    231  CA  LEU C  31     -35.265 -86.555 -26.295  1.00198.41           C
ANISOU  231  CA  LEU C  31    24649  25504  25233  -1257  -2181  -2431       C
ATOM    232  C   LEU C  31     -35.422 -85.119 -25.827  1.00176.55           C
ANISOU  232  C   LEU C  31    21885  22748  22450  -1210  -2201  -2379       C
ATOM    233  O   LEU C  31     -35.479 -84.198 -26.644  1.00175.04           O
ANISOU  233  O   LEU C  31    21760  22558  22190  -1257  -2224  -2367       O
ATOM    234  CB  LEU C  31     -36.510 -87.382 -25.976  1.00181.47           C
ANISOU  234  CB  LEU C  31    22449  23363  23140  -1233  -2243  -2372       C
ATOM    235  CG  LEU C  31     -36.381 -88.809 -26.511  1.00179.36           C
ANISOU  235  CG  LEU C  31    22186  23079  22885  -1284  -2231  -2423       C
ATOM    236  CD1 LEU C  31     -37.674 -89.586 -26.329  1.00185.96           C
ANISOU  236  CD1 LEU C  31    22974  23917  23765  -1271  -2306  -2355       C
ATOM    237  CD2 LEU C  31     -35.948 -88.782 -27.984  1.00169.66           C
ANISOU  237  CD2 LEU C  31    21060  21837  21568  -1384  -2221  -2478       C
ATOM    238  N   ALA C  32     -35.460 -84.934 -24.510  1.00150.73           N
ANISOU  238  N   ALA C  32    18541  19485  19243  -1117  -2193  -2351       N
ATOM    239  CA  ALA C  32     -35.610 -83.606 -23.921  1.00149.20           C
ANISOU  239  CA  ALA C  32    18348  19299  19041  -1059  -2213  -2302       C
ATOM    240  C   ALA C  32     -34.561 -82.585 -24.416  1.00164.03           C
ANISOU  240  C   ALA C  32    20295  21169  20859  -1097  -2179  -2343       C
ATOM    241  O   ALA C  32     -34.838 -81.388 -24.483  1.00188.60           O
ANISOU  241  O   ALA C  32    23439  24284  23935  -1086  -2215  -2301       O
ATOM    242  CB  ALA C  32     -35.623 -83.696 -22.390  1.00105.33           C
ANISOU  242  CB  ALA C  32    12703  13752  13564   -951  -2198  -2279       C
ATOM    243  N   SER C  33     -33.368 -83.051 -24.772  1.00136.72           N
ANISOU  243  N   SER C  33    16858  17701  17390  -1141  -2112  -2420       N
ATOM    244  CA  SER C  33     -32.332 -82.147 -25.264  1.00159.63           C
ANISOU  244  CA  SER C  33    19820  20597  20234  -1178  -2081  -2453       C
ATOM    245  C   SER C  33     -32.605 -81.726 -26.708  1.00179.06           C
ANISOU  245  C   SER C  33    22360  23061  22612  -1267  -2116  -2450       C
ATOM    246  O   SER C  33     -31.987 -80.784 -27.218  1.00157.51           O
ANISOU  246  O   SER C  33    19683  20334  19830  -1300  -2110  -2459       O
ATOM    247  CB  SER C  33     -30.953 -82.801 -25.184  1.00185.07           C
ANISOU  247  CB  SER C  33    23038  23811  23471  -1194  -1995  -2529       C
ATOM    248  OG  SER C  33     -30.547 -83.249 -26.467  1.00218.44           O
ANISOU  248  OG  SER C  33    27324  28036  27638  -1282  -1975  -2576       O
ATOM    249  N   GLY C  34     -33.509 -82.444 -27.373  1.00194.51           N
ANISOU  249  N   GLY C  34    24325  25020  24558  -1309  -2154  -2436       N
ATOM    250  CA  GLY C  34     -33.897 -82.103 -28.731  1.00198.53           C
ANISOU  250  CA  GLY C  34    24906  25534  24991  -1394  -2192  -2428       C
ATOM    251  C   GLY C  34     -33.217 -82.900 -29.832  1.00201.66           C
ANISOU  251  C   GLY C  34    25352  25926  25342  -1475  -2152  -2499       C
ATOM    252  O   GLY C  34     -33.258 -82.519 -31.006  1.00199.44           O
ANISOU  252  O   GLY C  34    25136  25653  24990  -1549  -2171  -2503       O
ATOM    253  N   GLY C  35     -32.577 -84.002 -29.459  1.00204.56           N
ANISOU  253  N   GLY C  35    25688  26284  25750  -1461  -2095  -2554       N
ATOM    254  CA  GLY C  35     -31.997 -84.896 -30.444  1.00211.86           C
ANISOU  254  CA  GLY C  35    26658  27202  26635  -1528  -2057  -2622       C
ATOM    255  C   GLY C  35     -33.055 -85.818 -31.022  1.00215.32           C
ANISOU  255  C   GLY C  35    27107  27633  27072  -1567  -2109  -2609       C
ATOM    256  O   GLY C  35     -33.970 -86.254 -30.306  1.00208.44           O
ANISOU  256  O   GLY C  35    26180  26759  26261  -1523  -2149  -2564       O
ATOM    257  N   GLN C  36     -32.930 -86.117 -32.315  1.00200.92           N
ANISOU  257  N   GLN C  36    25355  25808  25178  -1647  -2110  -2646       N
ATOM    258  CA  GLN C  36     -33.902 -86.956 -33.016  1.00191.83           C
ANISOU  258  CA  GLN C  36    24228  24645  24014  -1695  -2164  -2635       C
ATOM    259  C   GLN C  36     -33.897 -88.400 -32.518  1.00186.27           C
ANISOU  259  C   GLN C  36    23480  23921  23372  -1671  -2145  -2669       C
ATOM    260  O   GLN C  36     -32.833 -88.954 -32.244  1.00208.26           O
ANISOU  260  O   GLN C  36    26254  26701  26176  -1654  -2072  -2735       O
ATOM    261  CB  GLN C  36     -33.617 -86.944 -34.519  1.00199.24           C
ANISOU  261  CB  GLN C  36    25258  25586  24859  -1786  -2162  -2676       C
ATOM    262  CG  GLN C  36     -34.516 -86.021 -35.343  1.00209.88           C
ANISOU  262  CG  GLN C  36    26650  26947  26149  -1838  -2233  -2615       C
ATOM    263  CD  GLN C  36     -34.250 -84.547 -35.092  1.00208.09           C
ANISOU  263  CD  GLN C  36    26418  26741  25906  -1817  -2231  -2579       C
ATOM    264  OE1 GLN C  36     -33.414 -84.182 -34.260  1.00214.58           O
ANISOU  264  OE1 GLN C  36    27204  27567  26761  -1761  -2182  -2595       O
ATOM    265  NE2 GLN C  36     -34.964 -83.688 -35.817  1.00188.66           N
ANISOU  265  NE2 GLN C  36    23993  24294  23395  -1864  -2288  -2528       N
ATOM    266  N   PRO C  37     -35.093 -89.010 -32.397  1.00173.33           N
ANISOU  266  N   PRO C  37    21816  22272  21768  -1669  -2214  -2620       N
ATOM    267  CA  PRO C  37     -35.223 -90.438 -32.076  1.00170.94           C
ANISOU  267  CA  PRO C  37    21478  21950  21523  -1657  -2212  -2647       C
ATOM    268  C   PRO C  37     -34.550 -91.307 -33.136  1.00169.98           C
ANISOU  268  C   PRO C  37    21427  21809  21347  -1723  -2177  -2732       C
ATOM    269  O   PRO C  37     -34.232 -90.818 -34.224  1.00160.37           O
ANISOU  269  O   PRO C  37    20290  20598  20045  -1783  -2170  -2757       O
ATOM    270  CB  PRO C  37     -36.737 -90.671 -32.108  1.00154.56           C
ANISOU  270  CB  PRO C  37    19386  19871  19468  -1665  -2310  -2562       C
ATOM    271  CG  PRO C  37     -37.328 -89.353 -31.820  1.00159.88           C
ANISOU  271  CG  PRO C  37    20048  20568  20132  -1639  -2346  -2484       C
ATOM    272  CD  PRO C  37     -36.401 -88.336 -32.439  1.00174.28           C
ANISOU  272  CD  PRO C  37    21932  22403  21884  -1671  -2299  -2525       C
ATOM    273  N   ILE C  38     -34.306 -92.572 -32.810  1.00163.04           N
ANISOU  273  N   ILE C  38    20519  20911  20518  -1708  -2153  -2776       N
ATOM    274  CA  ILE C  38     -33.588 -93.461 -33.717  1.00166.54           C
ANISOU  274  CA  ILE C  38    21028  21335  20915  -1759  -2113  -2862       C
ATOM    275  C   ILE C  38     -34.339 -93.660 -35.031  1.00176.74           C
ANISOU  275  C   ILE C  38    22407  22613  22134  -1839  -2180  -2856       C
ATOM    276  O   ILE C  38     -35.474 -94.134 -35.037  1.00198.62           O
ANISOU  276  O   ILE C  38    25166  25369  24931  -1851  -2261  -2804       O
ATOM    277  CB  ILE C  38     -33.347 -94.819 -33.047  1.00173.18           C
ANISOU  277  CB  ILE C  38    21815  22154  21832  -1724  -2087  -2902       C
ATOM    278  CG1 ILE C  38     -32.291 -94.676 -31.945  1.00148.11           C
ANISOU  278  CG1 ILE C  38    18569  18992  18714  -1658  -1999  -2929       C
ATOM    279  CG2 ILE C  38     -32.915 -95.844 -34.074  1.00188.95           C
ANISOU  279  CG2 ILE C  38    23888  24125  23779  -1780  -2068  -2981       C
ATOM    280  CD1 ILE C  38     -32.470 -95.653 -30.815  1.00117.54           C
ANISOU  280  CD1 ILE C  38    14601  15112  14948  -1601  -1996  -2923       C
ATOM    281  N   THR C  39     -33.682 -93.326 -36.140  1.00165.81           N
ANISOU  281  N   THR C  39    21109  21233  20657  -1894  -2148  -2906       N
ATOM    282  CA  THR C  39     -34.341 -93.249 -37.445  1.00187.50           C
ANISOU  282  CA  THR C  39    23943  23974  23324  -1973  -2209  -2896       C
ATOM    283  C   THR C  39     -34.506 -94.569 -38.190  1.00194.03           C
ANISOU  283  C   THR C  39    24826  24766  24129  -2018  -2231  -2947       C
ATOM    284  O   THR C  39     -35.550 -94.828 -38.803  1.00213.00           O
ANISOU  284  O   THR C  39    27266  27152  26511  -2067  -2314  -2909       O
ATOM    285  CB  THR C  39     -33.603 -92.276 -38.396  1.00189.77           C
ANISOU  285  CB  THR C  39    24301  24288  23516  -2016  -2170  -2925       C
ATOM    286  OG1 THR C  39     -34.255 -92.270 -39.673  1.00203.96           O
ANISOU  286  OG1 THR C  39    26180  26080  25236  -2095  -2229  -2917       O
ATOM    287  CG2 THR C  39     -32.151 -92.703 -38.585  1.00176.31           C
ANISOU  287  CG2 THR C  39    22621  22585  21785  -2006  -2071  -3017       C
ATOM    288  N   ASN C  40     -33.467 -95.391 -38.145  1.00157.13           N
ANISOU  288  N   ASN C  40    20162  20080  19461  -2001  -2157  -3031       N
ATOM    289  CA  ASN C  40     -33.268 -96.406 -39.165  1.00141.41           C
ANISOU  289  CA  ASN C  40    18254  18060  17414  -2050  -2157  -3101       C
ATOM    290  C   ASN C  40     -34.019 -97.720 -38.945  1.00152.53           C
ANISOU  290  C   ASN C  40    19647  19427  18880  -2051  -2218  -3098       C
ATOM    291  O   ASN C  40     -33.938 -98.626 -39.778  1.00137.37           O
ANISOU  291  O   ASN C  40    17802  17477  16917  -2092  -2228  -3155       O
ATOM    292  CB  ASN C  40     -31.771 -96.652 -39.335  1.00110.39           C
ANISOU  292  CB  ASN C  40    14351  14138  13453  -2033  -2048  -3191       C
ATOM    293  CG  ASN C  40     -31.448 -97.432 -40.575  1.00139.41           C
ANISOU  293  CG  ASN C  40    18130  17792  17045  -2085  -2040  -3265       C
ATOM    294  OD1 ASN C  40     -32.273 -97.549 -41.477  1.00158.00           O
ANISOU  294  OD1 ASN C  40    20551  20132  19349  -2143  -2115  -3250       O
ATOM    295  ND2 ASN C  40     -30.235 -97.969 -40.635  1.00151.14           N
ANISOU  295  ND2 ASN C  40    19634  19277  18515  -2062  -1949  -3344       N
ATOM    296  N   CYS C  41     -34.772 -97.820 -37.853  1.00153.67           N
ANISOU  296  N   CYS C  41    19698  19570  19119  -2007  -2262  -3030       N
ATOM    297  CA  CYS C  41     -35.478 -99.064 -37.556  1.00152.95           C
ANISOU  297  CA  CYS C  41    19581  19443  19092  -2003  -2324  -3019       C
ATOM    298  C   CYS C  41     -36.354 -99.471 -38.733  1.00159.63           C
ANISOU  298  C   CYS C  41    20518  20259  19875  -2081  -2413  -3007       C
ATOM    299  O   CYS C  41     -36.787 -98.625 -39.510  1.00163.91           O
ANISOU  299  O   CYS C  41    21115  20815  20347  -2130  -2447  -2972       O
ATOM    300  CB  CYS C  41     -36.296 -98.958 -36.269  1.00141.54           C
ANISOU  300  CB  CYS C  41    18019  18009  17751  -1945  -2369  -2929       C
ATOM    301  SG  CYS C  41     -37.007 -97.341 -35.973  1.00175.15           S
ANISOU  301  SG  CYS C  41    22244  22308  21998  -1933  -2404  -2825       S
ATOM    302  N   VAL C  42     -36.564-100.776 -38.888  1.00175.47           N
ANISOU  302  N   VAL C  42    22543  22223  21905  -2095  -2449  -3039       N
ATOM    303  CA  VAL C  42     -37.266-101.323 -40.049  1.00161.30           C
ANISOU  303  CA  VAL C  42    20846  20392  20048  -2171  -2531  -3041       C
ATOM    304  C   VAL C  42     -38.792-101.254 -39.954  1.00166.46           C
ANISOU  304  C   VAL C  42    21475  21036  20734  -2197  -2654  -2927       C
ATOM    305  O   VAL C  42     -39.410-101.807 -39.033  1.00142.40           O
ANISOU  305  O   VAL C  42    18343  17980  17782  -2159  -2702  -2871       O
ATOM    306  CB  VAL C  42     -36.862-102.785 -40.313  1.00147.22           C
ANISOU  306  CB  VAL C  42    19104  18561  18273  -2177  -2526  -3124       C
ATOM    307  CG1 VAL C  42     -35.349-102.905 -40.382  1.00145.55           C
ANISOU  307  CG1 VAL C  42    18915  18358  18030  -2148  -2401  -3232       C
ATOM    308  CG2 VAL C  42     -37.438-103.710 -39.234  1.00135.64           C
ANISOU  308  CG2 VAL C  42    17540  17073  16925  -2134  -2577  -3082       C
ATOM    309  N   LYS C  43     -39.391-100.590 -40.936  1.00177.55           N
ANISOU  309  N   LYS C  43    22954  22446  22060  -2263  -2705  -2889       N
ATOM    310  CA  LYS C  43     -40.841-100.500 -41.026  1.00183.06           C
ANISOU  310  CA  LYS C  43    23644  23136  22776  -2300  -2822  -2777       C
ATOM    311  C   LYS C  43     -41.390-101.625 -41.911  1.00179.65           C
ANISOU  311  C   LYS C  43    23296  22648  22314  -2366  -2905  -2793       C
ATOM    312  O   LYS C  43     -40.760-102.049 -42.894  1.00123.35           O
ANISOU  312  O   LYS C  43    16266  15494  15106  -2407  -2877  -2886       O
ATOM    313  CB  LYS C  43     -41.275 -99.137 -41.571  1.00194.88           C
ANISOU  313  CB  LYS C  43    25170  24668  24208  -2339  -2837  -2716       C
ATOM    314  CG  LYS C  43     -42.709 -98.761 -41.208  1.00196.33           C
ANISOU  314  CG  LYS C  43    25302  24858  24434  -2346  -2937  -2577       C
ATOM    315  CD  LYS C  43     -43.269 -97.655 -42.104  1.00197.17           C
ANISOU  315  CD  LYS C  43    25467  24987  24462  -2412  -2969  -2522       C
ATOM    316  CE  LYS C  43     -42.520 -96.344 -41.944  1.00171.02           C
ANISOU  316  CE  LYS C  43    22137  21724  21120  -2383  -2885  -2540       C
ATOM    317  NZ  LYS C  43     -41.787 -95.959 -43.185  1.00142.46           N
ANISOU  317  NZ  LYS C  43    18620  18112  17395  -2444  -2840  -2620       N
ATOM    318  N   MET C  44     -42.567-102.117 -41.548  1.00201.41           N
ANISOU  318  N   MET C  44    26011  25384  25131  -2373  -3010  -2698       N
ATOM    319  CA  MET C  44     -43.176-103.237 -42.252  1.00206.38           C
ANISOU  319  CA  MET C  44    26712  25956  25745  -2432  -3102  -2700       C
ATOM    320  C   MET C  44     -44.455-102.845 -43.015  1.00215.31           C
ANISOU  320  C   MET C  44    27894  27080  26833  -2510  -3212  -2597       C
ATOM    321  O   MET C  44     -45.397-102.296 -42.434  1.00230.32           O
ANISOU  321  O   MET C  44    29723  29006  28782  -2496  -3266  -2475       O
ATOM    322  CB  MET C  44     -43.452-104.364 -41.255  1.00177.46           C
ANISOU  322  CB  MET C  44    22964  22269  22195  -2382  -3144  -2677       C
ATOM    323  CG  MET C  44     -42.201-105.079 -40.769  1.00119.52           C
ANISOU  323  CG  MET C  44    15601  14921  14889  -2326  -3048  -2793       C
ATOM    324  SD  MET C  44     -41.630-106.243 -42.009  1.00182.90           S
ANISOU  324  SD  MET C  44    23771  22885  22838  -2385  -3051  -2918       S
ATOM    325  CE  MET C  44     -43.251-106.780 -42.640  1.00314.69           C
ANISOU  325  CE  MET C  44    40513  39528  39525  -2464  -3225  -2812       C
ATOM    326  N   LEU C  45     -44.476-103.134 -44.316  1.00200.00           N
ANISOU  326  N   LEU C  45    26082  25108  24802  -2590  -3242  -2644       N
ATOM    327  CA  LEU C  45     -45.602-102.786 -45.180  1.00179.70           C
ANISOU  327  CA  LEU C  45    23573  22527  22179  -2675  -3341  -2556       C
ATOM    328  C   LEU C  45     -46.776-103.736 -44.977  1.00182.53           C
ANISOU  328  C   LEU C  45    23915  22841  22598  -2698  -3471  -2464       C
ATOM    329  O   LEU C  45     -46.665-104.937 -45.232  1.00147.19           O
ANISOU  329  O   LEU C  45    19486  18310  18128  -2714  -3509  -2519       O
ATOM    330  CB  LEU C  45     -45.169-102.811 -46.644  1.00138.03           C
ANISOU  330  CB  LEU C  45    18437  17229  16779  -2752  -3328  -2643       C
ATOM    331  CG  LEU C  45     -46.281-103.082 -47.653  1.00153.76           C
ANISOU  331  CG  LEU C  45    20517  19183  18721  -2850  -3448  -2579       C
ATOM    332  CD1 LEU C  45     -47.406-102.067 -47.503  1.00188.87           C
ANISOU  332  CD1 LEU C  45    24916  23665  23183  -2876  -3507  -2433       C
ATOM    333  CD2 LEU C  45     -45.724-103.068 -49.066  1.00142.40           C
ANISOU  333  CD2 LEU C  45    19217  17731  17160  -2917  -3422  -2676       C
ATOM    334  N   CYS C  46     -47.917-103.176 -44.588  1.00201.67           N
ANISOU  334  N   CYS C  46    26278  25287  25060  -2704  -3543  -2321       N
ATOM    335  CA  CYS C  46     -49.031-103.972 -44.091  1.00213.95           C
ANISOU  335  CA  CYS C  46    27783  26813  26695  -2706  -3661  -2211       C
ATOM    336  C   CYS C  46     -50.316-103.714 -44.867  1.00223.40           C
ANISOU  336  C   CYS C  46    29034  27996  27851  -2794  -3775  -2091       C
ATOM    337  O   CYS C  46     -50.409-102.757 -45.640  1.00227.53           O
ANISOU  337  O   CYS C  46    29614  28542  28294  -2846  -3757  -2080       O
ATOM    338  CB  CYS C  46     -49.259-103.683 -42.605  1.00209.98           C
ANISOU  338  CB  CYS C  46    27127  26354  26300  -2609  -3645  -2130       C
ATOM    339  SG  CYS C  46     -49.120-105.127 -41.524  1.00186.33           S
ANISOU  339  SG  CYS C  46    24043  23329  23424  -2540  -3672  -2146       S
ATOM    340  N   THR C  47     -51.301-104.583 -44.662  1.00219.18           N
ANISOU  340  N   THR C  47    28479  27425  27373  -2812  -3894  -1997       N
ATOM    341  CA  THR C  47     -52.570-104.486 -45.376  1.00215.03           C
ANISOU  341  CA  THR C  47    28005  26880  26816  -2900  -4013  -1873       C
ATOM    342  C   THR C  47     -53.482-103.293 -45.008  1.00207.78           C
ANISOU  342  C   THR C  47    27017  26018  25913  -2894  -4032  -1723       C
ATOM    343  O   THR C  47     -53.979-102.618 -45.909  1.00209.54           O
ANISOU  343  O   THR C  47    27309  26246  26062  -2972  -4060  -1677       O
ATOM    344  CB  THR C  47     -53.351-105.828 -45.354  1.00176.23           C
ANISOU  344  CB  THR C  47    23100  21904  21954  -2929  -4145  -1813       C
ATOM    345  OG1 THR C  47     -52.866-106.660 -44.293  1.00137.81           O
ANISOU  345  OG1 THR C  47    18145  17032  17182  -2843  -4123  -1854       O
ATOM    346  CG2 THR C  47     -53.167-106.566 -46.669  1.00191.52           C
ANISOU  346  CG2 THR C  47    25190  23774  23805  -3020  -4188  -1901       C
ATOM    347  N   HIS C  48     -53.694-102.999 -43.723  1.00191.14           N
ANISOU  347  N   HIS C  48    24775  23953  23895  -2802  -4016  -1647       N
ATOM    348  CA  HIS C  48     -53.108-103.711 -42.590  1.00185.16           C
ANISOU  348  CA  HIS C  48    23924  23198  23229  -2707  -3978  -1695       C
ATOM    349  C   HIS C  48     -53.842-105.007 -42.239  1.00177.51           C
ANISOU  349  C   HIS C  48    22923  22186  22337  -2709  -4095  -1624       C
ATOM    350  O   HIS C  48     -53.217-106.044 -42.038  1.00183.20           O
ANISOU  350  O   HIS C  48    23645  22872  23092  -2686  -4085  -1717       O
ATOM    351  CB  HIS C  48     -53.045-102.779 -41.377  1.00196.77           C
ANISOU  351  CB  HIS C  48    25267  24737  24760  -2608  -3912  -1641       C
ATOM    352  CG  HIS C  48     -52.296-101.502 -41.630  1.00212.60           C
ANISOU  352  CG  HIS C  48    27297  26783  26697  -2600  -3800  -1707       C
ATOM    353  ND1 HIS C  48     -51.353-101.374 -42.629  1.00207.69           N
ANISOU  353  ND1 HIS C  48    26783  26145  25986  -2650  -3733  -1843       N
ATOM    354  CD2 HIS C  48     -52.356-100.298 -41.016  1.00207.32           C
ANISOU  354  CD2 HIS C  48    26559  26173  26039  -2545  -3748  -1653       C
ATOM    355  CE1 HIS C  48     -50.862-100.147 -42.616  1.00175.23           C
ANISOU  355  CE1 HIS C  48    22663  22081  21835  -2630  -3647  -1867       C
ATOM    356  NE2 HIS C  48     -51.455 -99.473 -41.648  1.00191.51           N
ANISOU  356  NE2 HIS C  48    24622  24186  23957  -2568  -3655  -1755       N
ATOM    357  N   THR C  49     -55.167-104.934 -42.151  1.00178.10           N
ANISOU  357  N   THR C  49    22965  22265  22440  -2736  -4207  -1455       N
ATOM    358  CA  THR C  49     -56.025-106.123 -42.053  1.00190.32           C
ANISOU  358  CA  THR C  49    24499  23766  24046  -2761  -4342  -1368       C
ATOM    359  C   THR C  49     -55.583-107.197 -41.044  1.00175.28           C
ANISOU  359  C   THR C  49    22506  21851  22243  -2681  -4340  -1410       C
ATOM    360  O   THR C  49     -55.709-108.395 -41.313  1.00162.43           O
ANISOU  360  O   THR C  49    20916  20164  20637  -2716  -4420  -1428       O
ATOM    361  CB  THR C  49     -56.209-106.807 -43.441  1.00208.54           C
ANISOU  361  CB  THR C  49    26960  26001  26275  -2878  -4420  -1409       C
ATOM    362  OG1 THR C  49     -56.229-105.816 -44.476  1.00200.76           O
ANISOU  362  OG1 THR C  49    26070  25027  25183  -2951  -4387  -1422       O
ATOM    363  CG2 THR C  49     -57.504-107.616 -43.485  1.00198.54           C
ANISOU  363  CG2 THR C  49    25686  24696  25054  -2925  -4584  -1257       C
ATOM    364  N   GLY C  50     -55.087-106.786 -39.882  1.00152.33           N
ANISOU  364  N   GLY C  50    19480  18999  19400  -2576  -4252  -1423       N
ATOM    365  CA  GLY C  50     -54.659-107.756 -38.886  1.00143.10           C
ANISOU  365  CA  GLY C  50    18216  17826  18331  -2501  -4245  -1460       C
ATOM    366  C   GLY C  50     -54.860-107.256 -37.472  1.00169.59           C
ANISOU  366  C   GLY C  50    21411  21250  21775  -2391  -4212  -1373       C
ATOM    367  O   GLY C  50     -55.016-106.052 -37.250  1.00198.54           O
ANISOU  367  O   GLY C  50    25050  24970  25417  -2363  -4162  -1322       O
ATOM    368  N   THR C  51     -54.851-108.174 -36.509  1.00164.85           N
ANISOU  368  N   THR C  51    20706  20651  21279  -2327  -4240  -1355       N
ATOM    369  CA  THR C  51     -55.121-107.800 -35.122  1.00190.66           C
ANISOU  369  CA  THR C  51    23816  23987  24639  -2220  -4221  -1262       C
ATOM    370  C   THR C  51     -54.185-106.676 -34.685  1.00206.27           C
ANISOU  370  C   THR C  51    25769  26015  26590  -2156  -4072  -1346       C
ATOM    371  O   THR C  51     -53.020-106.640 -35.083  1.00230.19           O
ANISOU  371  O   THR C  51    28866  29026  29572  -2168  -3973  -1505       O
ATOM    372  CB  THR C  51     -55.028-109.016 -34.156  1.00128.09           C
ANISOU  372  CB  THR C  51    15781  16057  16831  -2159  -4257  -1257       C
ATOM    373  OG1 THR C  51     -53.775-109.014 -33.459  1.00143.17           O
ANISOU  373  OG1 THR C  51    17639  17988  18773  -2086  -4127  -1392       O
ATOM    374  CG2 THR C  51     -55.174-110.321 -34.925  1.00109.98           C
ANISOU  374  CG2 THR C  51    13567  13685  14536  -2239  -4355  -1289       C
ATOM    375  N   GLY C  52     -54.708-105.745 -33.893  1.00187.15           N
ANISOU  375  N   GLY C  52    23256  23656  24195  -2088  -4060  -1236       N
ATOM    376  CA  GLY C  52     -53.930-104.601 -33.454  1.00188.67           C
ANISOU  376  CA  GLY C  52    23426  23896  24363  -2028  -3932  -1299       C
ATOM    377  C   GLY C  52     -52.878-104.938 -32.408  1.00169.91           C
ANISOU  377  C   GLY C  52    20961  21540  22058  -1938  -3838  -1398       C
ATOM    378  O   GLY C  52     -51.957-104.152 -32.155  1.00106.62           O
ANISOU  378  O   GLY C  52    12944  13550  14016  -1898  -3721  -1486       O
ATOM    379  N   GLN C  53     -53.003-106.110 -31.799  1.00161.74           N
ANISOU  379  N   GLN C  53    19847  20493  21114  -1908  -3890  -1380       N
ATOM    380  CA  GLN C  53     -52.124-106.470 -30.702  1.00174.64           C
ANISOU  380  CA  GLN C  53    21377  22150  22826  -1820  -3808  -1454       C
ATOM    381  C   GLN C  53     -50.688-106.736 -31.148  1.00208.74           C
ANISOU  381  C   GLN C  53    25772  26435  27105  -1844  -3700  -1645       C
ATOM    382  O   GLN C  53     -50.449-107.326 -32.205  1.00196.86           O
ANISOU  382  O   GLN C  53    24381  24872  25545  -1927  -3722  -1720       O
ATOM    383  CB  GLN C  53     -52.698-107.661 -29.933  1.00172.77           C
ANISOU  383  CB  GLN C  53    21030  21913  22702  -1783  -3900  -1375       C
ATOM    384  CG  GLN C  53     -51.737-108.809 -29.701  1.00156.14           C
ANISOU  384  CG  GLN C  53    18904  19774  20649  -1775  -3860  -1502       C
ATOM    385  CD  GLN C  53     -52.295-110.116 -30.210  1.00171.65           C
ANISOU  385  CD  GLN C  53    20897  21681  22642  -1838  -3984  -1472       C
ATOM    386  OE1 GLN C  53     -52.807-110.186 -31.332  1.00170.05           O
ANISOU  386  OE1 GLN C  53    20811  21432  22367  -1929  -4056  -1453       O
ATOM    387  NE2 GLN C  53     -52.219-111.161 -29.383  1.00154.82           N
ANISOU  387  NE2 GLN C  53    18656  19550  20616  -1791  -4012  -1466       N
ATOM    388  N   ALA C  54     -49.743-106.255 -30.342  1.00236.07           N
ANISOU  388  N   ALA C  54    29173  29933  30591  -1769  -3582  -1717       N
ATOM    389  CA  ALA C  54     -48.330-106.585 -30.484  1.00202.66           C
ANISOU  389  CA  ALA C  54    24981  25678  26343  -1772  -3472  -1885       C
ATOM    390  C   ALA C  54     -48.003-107.446 -29.269  1.00207.41           C
ANISOU  390  C   ALA C  54    25448  26296  27063  -1695  -3455  -1894       C
ATOM    391  O   ALA C  54     -48.625-107.282 -28.221  1.00210.34           O
ANISOU  391  O   ALA C  54    25695  26715  27511  -1621  -3486  -1785       O
ATOM    392  CB  ALA C  54     -47.478-105.312 -30.505  1.00135.36           C
ANISOU  392  CB  ALA C  54    16491  17184  17755  -1751  -3351  -1953       C
ATOM    393  N   ILE C  55     -47.044-108.359 -29.396  1.00187.57           N
ANISOU  393  N   ILE C  55    22956  23747  24566  -1709  -3405  -2018       N
ATOM    394  CA  ILE C  55     -46.219-108.461 -30.588  1.00164.10           C
ANISOU  394  CA  ILE C  55    20128  20724  21497  -1783  -3354  -2150       C
ATOM    395  C   ILE C  55     -46.383-109.777 -31.341  1.00172.94           C
ANISOU  395  C   ILE C  55    21316  21778  22617  -1850  -3433  -2186       C
ATOM    396  O   ILE C  55     -46.050-110.859 -30.845  1.00150.49           O
ANISOU  396  O   ILE C  55    18412  18916  19850  -1827  -3435  -2225       O
ATOM    397  CB  ILE C  55     -44.752-108.218 -30.254  1.00151.57           C
ANISOU  397  CB  ILE C  55    18537  19151  19904  -1745  -3205  -2282       C
ATOM    398  CG1 ILE C  55     -44.441-108.673 -28.823  1.00147.34           C
ANISOU  398  CG1 ILE C  55    17845  18649  19489  -1655  -3168  -2272       C
ATOM    399  CG2 ILE C  55     -44.459-106.752 -30.365  1.00152.42           C
ANISOU  399  CG2 ILE C  55    18677  19295  19939  -1733  -3131  -2284       C
ATOM    400  CD1 ILE C  55     -44.641-110.154 -28.572  1.00162.57           C
ANISOU  400  CD1 ILE C  55    19721  20545  21502  -1658  -3235  -2273       C
ATOM    401  N   THR C  56     -46.890-109.652 -32.561  1.00179.31           N
ANISOU  401  N   THR C  56    22249  22547  23333  -1936  -3497  -2174       N
ATOM    402  CA  THR C  56     -47.199-110.788 -33.412  1.00181.06           C
ANISOU  402  CA  THR C  56    22554  22700  23539  -2008  -3588  -2196       C
ATOM    403  C   THR C  56     -45.946-111.525 -33.869  1.00175.05           C
ANISOU  403  C   THR C  56    21865  21895  22749  -2025  -3507  -2362       C
ATOM    404  O   THR C  56     -44.835-111.011 -33.741  1.00192.97           O
ANISOU  404  O   THR C  56    24143  24188  24990  -1994  -3376  -2460       O
ATOM    405  CB  THR C  56     -47.991-110.330 -34.644  1.00203.84           C
ANISOU  405  CB  THR C  56    25566  25560  26324  -2097  -3666  -2146       C
ATOM    406  OG1 THR C  56     -47.141-109.578 -35.520  1.00183.88           O
ANISOU  406  OG1 THR C  56    23153  23029  23685  -2132  -3569  -2253       O
ATOM    407  CG2 THR C  56     -49.159-109.452 -34.218  1.00224.24           C
ANISOU  407  CG2 THR C  56    28083  28192  28927  -2078  -3731  -1982       C
ATOM    408  N   VAL C  57     -46.126-112.754 -34.346  1.00171.35           N
ANISOU  408  N   VAL C  57    21445  21365  22293  -2069  -3586  -2389       N
ATOM    409  CA  VAL C  57     -45.062-113.472 -35.049  1.00172.93           C
ANISOU  409  CA  VAL C  57    21747  21515  22445  -2098  -3524  -2543       C
ATOM    410  C   VAL C  57     -44.969-112.972 -36.496  1.00145.80           C
ANISOU  410  C   VAL C  57    18480  18048  18868  -2178  -3520  -2596       C
ATOM    411  O   VAL C  57     -43.884-112.810 -37.054  1.00131.81           O
ANISOU  411  O   VAL C  57    16791  16268  17023  -2186  -3415  -2722       O
ATOM    412  CB  VAL C  57     -45.278-115.006 -35.020  1.00142.33           C
ANISOU  412  CB  VAL C  57    17863  17580  18635  -2113  -3614  -2556       C
ATOM    413  CG1 VAL C  57     -44.579-115.662 -36.184  1.00106.30           C
ANISOU  413  CG1 VAL C  57    13455  12950  13986  -2171  -3594  -2690       C
ATOM    414  CG2 VAL C  57     -44.792-115.600 -33.694  1.00108.56           C
ANISOU  414  CG2 VAL C  57    13433  13330  14485  -2032  -3567  -2568       C
ATOM    415  N   THR C  58     -46.129-112.710 -37.084  1.00124.06           N
ANISOU  415  N   THR C  58    15775  15282  16079  -2236  -3634  -2492       N
ATOM    416  CA  THR C  58     -46.225-112.119 -38.411  1.00147.00           C
ANISOU  416  CA  THR C  58    18830  18168  18857  -2314  -3642  -2518       C
ATOM    417  C   THR C  58     -46.914-110.759 -38.293  1.00156.01           C
ANISOU  417  C   THR C  58    19938  19365  19973  -2314  -3647  -2407       C
ATOM    418  O   THR C  58     -47.776-110.577 -37.435  1.00167.87           O
ANISOU  418  O   THR C  58    21329  20901  21555  -2277  -3707  -2278       O
ATOM    419  CB  THR C  58     -47.043-113.020 -39.351  1.00169.57           C
ANISOU  419  CB  THR C  58    21789  20955  21684  -2396  -3781  -2490       C
ATOM    420  OG1 THR C  58     -47.998-112.226 -40.064  1.00182.29           O
ANISOU  420  OG1 THR C  58    23461  22573  23229  -2460  -3852  -2393       O
ATOM    421  CG2 THR C  58     -47.789-114.085 -38.554  1.00148.16           C
ANISOU  421  CG2 THR C  58    18979  18223  19093  -2374  -3893  -2403       C
ATOM    422  N   PRO C  59     -46.543-109.799 -39.157  1.00145.32           N
ANISOU  422  N   PRO C  59    18680  18025  18511  -2352  -3586  -2454       N
ATOM    423  CA  PRO C  59     -47.039-108.422 -38.985  1.00142.70           C
ANISOU  423  CA  PRO C  59    18313  17750  18157  -2344  -3573  -2361       C
ATOM    424  C   PRO C  59     -48.563-108.368 -38.945  1.00191.97           C
ANISOU  424  C   PRO C  59    24523  23990  24426  -2375  -3711  -2196       C
ATOM    425  O   PRO C  59     -49.213-108.889 -39.852  1.00228.87           O
ANISOU  425  O   PRO C  59    29287  28613  29058  -2454  -3811  -2169       O
ATOM    426  CB  PRO C  59     -46.553-107.705 -40.248  1.00125.86           C
ANISOU  426  CB  PRO C  59    16317  15613  15893  -2409  -3521  -2437       C
ATOM    427  CG  PRO C  59     -45.507-108.587 -40.846  1.00124.29           C
ANISOU  427  CG  PRO C  59    16205  15368  15653  -2424  -3469  -2587       C
ATOM    428  CD  PRO C  59     -45.791-109.983 -40.411  1.00126.54           C
ANISOU  428  CD  PRO C  59    16452  15606  16022  -2412  -3544  -2581       C
ATOM    429  N   GLU C  60     -49.123-107.738 -37.919  1.00169.16           N
ANISOU  429  N   GLU C  60    21512  21155  21605  -2314  -3718  -2083       N
ATOM    430  CA  GLU C  60     -50.568-107.571 -37.830  1.00161.55           C
ANISOU  430  CA  GLU C  60    20512  20200  20668  -2336  -3842  -1913       C
ATOM    431  C   GLU C  60     -50.869-106.151 -37.383  1.00161.67           C
ANISOU  431  C   GLU C  60    20472  20282  20674  -2296  -3799  -1832       C
ATOM    432  O   GLU C  60     -50.493-105.754 -36.292  1.00188.24           O
ANISOU  432  O   GLU C  60    23730  23694  24099  -2207  -3730  -1829       O
ATOM    433  CB  GLU C  60     -51.166-108.576 -36.843  1.00149.21           C
ANISOU  433  CB  GLU C  60    18834  18633  19226  -2287  -3925  -1829       C
ATOM    434  CG  GLU C  60     -51.033-110.037 -37.274  1.00170.45           C
ANISOU  434  CG  GLU C  60    21577  21253  21934  -2329  -3990  -1891       C
ATOM    435  CD  GLU C  60     -51.434-111.020 -36.182  1.00175.18           C
ANISOU  435  CD  GLU C  60    22045  21853  22661  -2271  -4057  -1822       C
ATOM    436  OE1 GLU C  60     -51.106-112.218 -36.314  1.00164.87           O
ANISOU  436  OE1 GLU C  60    20762  20496  21386  -2286  -4088  -1891       O
ATOM    437  OE2 GLU C  60     -52.077-110.602 -35.195  1.00181.33           O
ANISOU  437  OE2 GLU C  60    22699  22688  23512  -2208  -4079  -1698       O
ATOM    438  N   ALA C  61     -51.557-105.379 -38.209  1.00185.42           N
ANISOU  438  N   ALA C  61    23551  23293  23606  -2362  -3841  -1765       N
ATOM    439  CA  ALA C  61     -51.763-103.978 -37.868  1.00183.66           C
ANISOU  439  CA  ALA C  61    23286  23130  23365  -2328  -3794  -1699       C
ATOM    440  C   ALA C  61     -53.219-103.524 -37.902  1.00206.00           C
ANISOU  440  C   ALA C  61    26093  25978  26201  -2353  -3900  -1519       C
ATOM    441  O   ALA C  61     -53.929-103.731 -38.887  1.00205.50           O
ANISOU  441  O   ALA C  61    26116  25879  26086  -2445  -3986  -1471       O
ATOM    442  CB  ALA C  61     -50.895-103.077 -38.753  1.00137.16           C
ANISOU  442  CB  ALA C  61    17498  17247  17371  -2369  -3698  -1809       C
ATOM    443  N   ASN C  62     -53.657-102.927 -36.799  1.00199.59           N
ANISOU  443  N   ASN C  62    25162  25221  25452  -2268  -3893  -1417       N
ATOM    444  CA  ASN C  62     -54.862-102.120 -36.790  1.00191.31           C
ANISOU  444  CA  ASN C  62    24091  24205  24395  -2277  -3959  -1254       C
ATOM    445  C   ASN C  62     -54.598-100.922 -37.707  1.00206.90           C
ANISOU  445  C   ASN C  62    26159  26189  26264  -2334  -3901  -1294       C
ATOM    446  O   ASN C  62     -53.460-100.476 -37.821  1.00208.09           O
ANISOU  446  O   ASN C  62    26340  26347  26376  -2319  -3793  -1427       O
ATOM    447  CB  ASN C  62     -55.188-101.699 -35.354  1.00174.11           C
ANISOU  447  CB  ASN C  62    21765  22086  22302  -2159  -3943  -1158       C
ATOM    448  CG  ASN C  62     -55.882-100.353 -35.276  1.00196.40           C
ANISOU  448  CG  ASN C  62    24573  24958  25092  -2144  -3941  -1045       C
ATOM    449  OD1 ASN C  62     -55.310 -99.374 -34.790  1.00156.06           O
ANISOU  449  OD1 ASN C  62    19434  19889  19973  -2083  -3848  -1085       O
ATOM    450  ND2 ASN C  62     -57.126-100.298 -35.748  1.00225.67           N
ANISOU  450  ND2 ASN C  62    28301  28661  28784  -2200  -4046   -900       N
ATOM    451  N   MET C  63     -55.629-100.417 -38.379  1.00221.70           N
ANISOU  451  N   MET C  63    28077  28065  28092  -2401  -3974  -1179       N
ATOM    452  CA  MET C  63     -55.430 -99.421 -39.441  1.00215.31           C
ANISOU  452  CA  MET C  63    27369  27259  27180  -2474  -3934  -1218       C
ATOM    453  C   MET C  63     -54.594 -98.207 -39.004  1.00200.67           C
ANISOU  453  C   MET C  63    25486  25454  25307  -2410  -3813  -1283       C
ATOM    454  O   MET C  63     -53.883 -97.606 -39.815  1.00137.10           O
ANISOU  454  O   MET C  63    17516  17399  17175  -2458  -3749  -1380       O
ATOM    455  CB  MET C  63     -56.776 -98.980 -40.044  1.00185.46           C
ANISOU  455  CB  MET C  63    23618  23481  23366  -2545  -4032  -1060       C
ATOM    456  CG  MET C  63     -56.730 -98.759 -41.550  1.00170.02           C
ANISOU  456  CG  MET C  63    21801  21494  21305  -2669  -4043  -1109       C
ATOM    457  SD  MET C  63     -55.954-100.144 -42.421  1.00247.30           S
ANISOU  457  SD  MET C  63    31694  31208  31060  -2736  -4055  -1263       S
ATOM    458  CE  MET C  63     -56.324 -99.739 -44.128  1.00180.12           C
ANISOU  458  CE  MET C  63    23333  22672  22431  -2880  -4095  -1263       C
ATOM    459  N   ASP C  64     -54.679 -97.860 -37.721  1.00227.58           N
ANISOU  459  N   ASP C  64    28777  28905  28788  -2302  -3787  -1227       N
ATOM    460  CA  ASP C  64     -53.931 -96.735 -37.155  1.00228.22           C
ANISOU  460  CA  ASP C  64    28823  29031  28861  -2231  -3680  -1278       C
ATOM    461  C   ASP C  64     -52.458 -97.081 -36.971  1.00220.71           C
ANISOU  461  C   ASP C  64    27880  28068  27913  -2200  -3579  -1450       C
ATOM    462  O   ASP C  64     -51.569 -96.287 -37.278  1.00225.55           O
ANISOU  462  O   ASP C  64    28535  28692  28470  -2204  -3492  -1542       O
ATOM    463  CB  ASP C  64     -54.523 -96.332 -35.802  1.00215.83           C
ANISOU  463  CB  ASP C  64    27126  27510  27371  -2120  -3690  -1160       C
ATOM    464  CG  ASP C  64     -55.905 -95.730 -35.926  1.00183.75           C
ANISOU  464  CG  ASP C  64    23051  23470  23298  -2139  -3772   -985       C
ATOM    465  OD1 ASP C  64     -56.091 -94.848 -36.793  1.00168.12           O
ANISOU  465  OD1 ASP C  64    21144  21492  21240  -2206  -3767   -973       O
ATOM    466  OD2 ASP C  64     -56.803 -96.141 -35.159  1.00158.63           O
ANISOU  466  OD2 ASP C  64    19783  20305  20185  -2087  -3841   -857       O
ATOM    467  N   GLN C  65     -52.221 -98.276 -36.448  1.00187.51           N
ANISOU  467  N   GLN C  65    23631  23840  23774  -2167  -3593  -1485       N
ATOM    468  CA  GLN C  65     -50.885 -98.794 -36.223  1.00151.68           C
ANISOU  468  CA  GLN C  65    19094  19287  19249  -2137  -3503  -1639       C
ATOM    469  C   GLN C  65     -50.067 -98.974 -37.505  1.00189.80           C
ANISOU  469  C   GLN C  65    24051  24077  23986  -2225  -3465  -1770       C
ATOM    470  O   GLN C  65     -50.582 -99.414 -38.535  1.00205.53           O
ANISOU  470  O   GLN C  65    26129  26033  25930  -2315  -3535  -1755       O
ATOM    471  CB  GLN C  65     -50.992-100.150 -35.533  1.00 95.09           C
ANISOU  471  CB  GLN C  65    11859  12099  12173  -2099  -3546  -1633       C
ATOM    472  CG  GLN C  65     -51.771-100.115 -34.241  1.00130.53           C
ANISOU  472  CG  GLN C  65    16213  16628  16756  -2007  -3587  -1504       C
ATOM    473  CD  GLN C  65     -51.803-101.462 -33.554  1.00151.03           C
ANISOU  473  CD  GLN C  65    18734  19206  19444  -1970  -3627  -1503       C
ATOM    474  OE1 GLN C  65     -51.599-102.500 -34.196  1.00150.70           O
ANISOU  474  OE1 GLN C  65    18752  19113  19393  -2031  -3660  -1567       O
ATOM    475  NE2 GLN C  65     -52.048-101.456 -32.233  1.00103.49           N
ANISOU  475  NE2 GLN C  65    12581  13228  13514  -1868  -3625  -1432       N
ATOM    476  N   GLU C  66     -48.783 -98.638 -37.420  1.00195.44           N
ANISOU  476  N   GLU C  66    24779  24802  24678  -2196  -3353  -1895       N
ATOM    477  CA  GLU C  66     -47.804 -99.034 -38.423  1.00158.11           C
ANISOU  477  CA  GLU C  66    20155  20040  19878  -2257  -3303  -2034       C
ATOM    478  C   GLU C  66     -47.002-100.179 -37.791  1.00178.78           C
ANISOU  478  C   GLU C  66    22731  22636  22560  -2207  -3263  -2123       C
ATOM    479  O   GLU C  66     -46.845-100.232 -36.564  1.00170.95           O
ANISOU  479  O   GLU C  66    21630  21670  21653  -2119  -3233  -2103       O
ATOM    480  CB  GLU C  66     -46.895 -97.863 -38.796  1.00 98.06           C
ANISOU  480  CB  GLU C  66    12592  12464  12202  -2260  -3206  -2106       C
ATOM    481  CG  GLU C  66     -46.315 -97.960 -40.185  1.00128.97           C
ANISOU  481  CG  GLU C  66    16634  16354  16016  -2348  -3184  -2203       C
ATOM    482  CD  GLU C  66     -47.356 -97.717 -41.270  1.00172.99           C
ANISOU  482  CD  GLU C  66    22286  21916  21527  -2443  -3273  -2128       C
ATOM    483  OE1 GLU C  66     -48.406 -97.127 -40.942  1.00198.46           O
ANISOU  483  OE1 GLU C  66    25465  25163  24777  -2437  -3333  -1999       O
ATOM    484  OE2 GLU C  66     -47.135 -98.114 -42.445  1.00170.34           O
ANISOU  484  OE2 GLU C  66    22057  21549  21115  -2522  -3284  -2193       O
ATOM    485  N   SER C  67     -46.526-101.119 -38.603  1.00170.25           N
ANISOU  485  N   SER C  67    21735  21510  21443  -2261  -3264  -2218       N
ATOM    486  CA  SER C  67     -45.843-102.281 -38.038  1.00159.77           C
ANISOU  486  CA  SER C  67    20369  20158  20178  -2219  -3234  -2296       C
ATOM    487  C   SER C  67     -44.333-102.301 -38.319  1.00187.63           C
ANISOU  487  C   SER C  67    23945  23683  23662  -2210  -3113  -2448       C
ATOM    488  O   SER C  67     -43.886-102.028 -39.448  1.00138.42           O
ANISOU  488  O   SER C  67    17823  17439  17331  -2272  -3085  -2516       O
ATOM    489  CB  SER C  67     -46.514-103.592 -38.463  1.00116.20           C
ANISOU  489  CB  SER C  67    14887  14585  14680  -2268  -3339  -2276       C
ATOM    490  OG  SER C  67     -46.250-103.898 -39.815  1.00147.85           O
ANISOU  490  OG  SER C  67    19033  18553  18593  -2353  -3348  -2354       O
ATOM    491  N   PHE C  68     -43.569-102.614 -37.267  1.00199.00           N
ANISOU  491  N   PHE C  68    25299  25137  25176  -2131  -3041  -2493       N
ATOM    492  CA  PHE C  68     -42.107-102.617 -37.297  1.00166.62           C
ANISOU  492  CA  PHE C  68    21220  21039  21048  -2108  -2920  -2623       C
ATOM    493  C   PHE C  68     -41.515-103.970 -36.905  1.00158.79           C
ANISOU  493  C   PHE C  68    20203  20015  20117  -2082  -2897  -2698       C
ATOM    494  O   PHE C  68     -42.183-104.785 -36.242  1.00120.70           O
ANISOU  494  O   PHE C  68    15306  15177  15379  -2057  -2966  -2642       O
ATOM    495  CB  PHE C  68     -41.566-101.580 -36.323  1.00155.56           C
ANISOU  495  CB  PHE C  68    19735  19690  19679  -2034  -2836  -2612       C
ATOM    496  CG  PHE C  68     -41.881-100.168 -36.696  1.00157.88           C
ANISOU  496  CG  PHE C  68    20059  20019  19911  -2055  -2836  -2558       C
ATOM    497  CD1 PHE C  68     -41.323 -99.593 -37.833  1.00154.76           C
ANISOU  497  CD1 PHE C  68    19769  19623  19410  -2114  -2796  -2621       C
ATOM    498  CD2 PHE C  68     -42.712 -99.398 -35.894  1.00156.58           C
ANISOU  498  CD2 PHE C  68    19812  19888  19793  -2010  -2874  -2444       C
ATOM    499  CE1 PHE C  68     -41.603 -98.281 -38.171  1.00164.10           C
ANISOU  499  CE1 PHE C  68    20974  20839  20539  -2134  -2798  -2570       C
ATOM    500  CE2 PHE C  68     -42.995 -98.087 -36.225  1.00181.29           C
ANISOU  500  CE2 PHE C  68    22967  23047  22866  -2027  -2874  -2396       C
ATOM    501  CZ  PHE C  68     -42.440 -97.528 -37.366  1.00188.36           C
ANISOU  501  CZ  PHE C  68    23967  23942  23661  -2091  -2837  -2459       C
ATOM    502  N   GLY C  69     -40.260-104.192 -37.309  1.00160.70           N
ANISOU  502  N   GLY C  69    20500  20245  20312  -2084  -2801  -2822       N
ATOM    503  CA  GLY C  69     -39.517-105.385 -36.932  1.00164.60           C
ANISOU  503  CA  GLY C  69    20971  20712  20857  -2055  -2760  -2904       C
ATOM    504  C   GLY C  69     -39.014-105.373 -35.497  1.00178.73           C
ANISOU  504  C   GLY C  69    22627  22534  22750  -1967  -2693  -2898       C
ATOM    505  O   GLY C  69     -38.458-104.375 -35.030  1.00183.12           O
ANISOU  505  O   GLY C  69    23145  23132  23300  -1928  -2615  -2899       O
ATOM    506  N   GLY C  70     -39.182-106.498 -34.808  1.00179.72           N
ANISOU  506  N   GLY C  70    22679  22638  22967  -1937  -2724  -2894       N
ATOM    507  CA  GLY C  70     -38.920-106.575 -33.379  1.00166.93           C
ANISOU  507  CA  GLY C  70    20918  21050  21456  -1855  -2680  -2871       C
ATOM    508  C   GLY C  70     -37.585-106.036 -32.912  1.00138.07           C
ANISOU  508  C   GLY C  70    17238  17425  17797  -1809  -2542  -2945       C
ATOM    509  O   GLY C  70     -37.530-105.220 -31.996  1.00110.60           O
ANISOU  509  O   GLY C  70    13674  13990  14359  -1754  -2506  -2899       O
ATOM    510  N   ALA C  71     -36.511-106.498 -33.543  1.00145.13           N
ANISOU  510  N   ALA C  71    18209  18295  18640  -1832  -2466  -3058       N
ATOM    511  CA  ALA C  71     -35.166-106.056 -33.204  1.00139.81           C
ANISOU  511  CA  ALA C  71    17520  17646  17954  -1795  -2333  -3129       C
ATOM    512  C   ALA C  71     -35.015-104.546 -33.341  1.00131.56           C
ANISOU  512  C   ALA C  71    16497  16642  16847  -1794  -2296  -3099       C
ATOM    513  O   ALA C  71     -34.554-103.873 -32.420  1.00122.13           O
ANISOU  513  O   ALA C  71    15225  15485  15695  -1739  -2234  -3082       O
ATOM    514  CB  ALA C  71     -34.148-106.760 -34.083  1.00155.84           C
ANISOU  514  CB  ALA C  71    19648  19643  19919  -1828  -2268  -3245       C
ATOM    515  N   SER C  72     -35.411-104.023 -34.498  1.00129.77           N
ANISOU  515  N   SER C  72    16376  16408  16521  -1856  -2339  -3091       N
ATOM    516  CA  SER C  72     -35.216-102.611 -34.815  1.00130.72           C
ANISOU  516  CA  SER C  72    16531  16564  16572  -1865  -2306  -3071       C
ATOM    517  C   SER C  72     -35.860-101.676 -33.795  1.00125.52           C
ANISOU  517  C   SER C  72    15774  15943  15972  -1815  -2333  -2972       C
ATOM    518  O   SER C  72     -35.512-100.495 -33.715  1.00114.21           O
ANISOU  518  O   SER C  72    14344  14544  14505  -1802  -2289  -2958       O
ATOM    519  CB  SER C  72     -35.768-102.304 -36.202  1.00142.82           C
ANISOU  519  CB  SER C  72    18183  18082  18000  -1944  -2368  -3065       C
ATOM    520  OG  SER C  72     -37.163-102.552 -36.257  1.00149.23           O
ANISOU  520  OG  SER C  72    18984  18877  18838  -1968  -2489  -2978       O
ATOM    521  N   CYS C  73     -36.802-102.206 -33.018  1.00127.43           N
ANISOU  521  N   CYS C  73    15933  16183  16304  -1785  -2407  -2900       N
ATOM    522  CA  CYS C  73     -37.529-101.395 -32.044  1.00156.28           C
ANISOU  522  CA  CYS C  73    19493  19873  20013  -1732  -2440  -2798       C
ATOM    523  C   CYS C  73     -36.905-101.413 -30.656  1.00148.13           C
ANISOU  523  C   CYS C  73    18344  18867  19072  -1648  -2370  -2804       C
ATOM    524  O   CYS C  73     -37.273-100.626 -29.785  1.00153.58           O
ANISOU  524  O   CYS C  73    18959  19591  19802  -1593  -2377  -2733       O
ATOM    525  CB  CYS C  73     -38.976-101.871 -31.938  1.00173.15           C
ANISOU  525  CB  CYS C  73    21595  21999  22193  -1741  -2565  -2699       C
ATOM    526  SG  CYS C  73     -39.961-101.557 -33.416  1.00202.54           S
ANISOU  526  SG  CYS C  73    25442  25700  25814  -1837  -2661  -2657       S
ATOM    527  N   CYS C  74     -35.934-102.293 -30.466  1.00149.39           N
ANISOU  527  N   CYS C  74    18490  19010  19261  -1637  -2300  -2889       N
ATOM    528  CA  CYS C  74     -35.378-102.551 -29.141  1.00142.33           C
ANISOU  528  CA  CYS C  74    17479  18136  18465  -1563  -2239  -2896       C
ATOM    529  C   CYS C  74     -34.022-101.882 -28.929  1.00144.83           C
ANISOU  529  C   CYS C  74    17804  18472  18755  -1541  -2117  -2961       C
ATOM    530  O   CYS C  74     -33.035-102.207 -29.598  1.00142.13           O
ANISOU  530  O   CYS C  74    17531  18111  18360  -1574  -2048  -3049       O
ATOM    531  CB  CYS C  74     -35.273-104.056 -28.911  1.00128.35           C
ANISOU  531  CB  CYS C  74    15668  16336  16763  -1561  -2246  -2936       C
ATOM    532  SG  CYS C  74     -34.165-104.527 -27.614  1.00 96.26           S
ANISOU  532  SG  CYS C  74    11489  12290  12797  -1491  -2140  -2984       S
ATOM    533  N   LEU C  75     -34.002-100.940 -27.993  1.00127.64           N
ANISOU  533  N   LEU C  75    15557  16330  16611  -1483  -2095  -2911       N
ATOM    534  CA  LEU C  75     -32.811-100.186 -27.632  1.00113.95           C
ANISOU  534  CA  LEU C  75    13820  14616  14861  -1457  -1991  -2953       C
ATOM    535  C   LEU C  75     -31.605-101.068 -27.353  1.00131.66           C
ANISOU  535  C   LEU C  75    16039  16847  17139  -1447  -1895  -3038       C
ATOM    536  O   LEU C  75     -30.512-100.819 -27.870  1.00138.27           O
ANISOU  536  O   LEU C  75    16940  17680  17915  -1470  -1814  -3103       O
ATOM    537  CB  LEU C  75     -33.118 -99.371 -26.386  1.00114.99           C
ANISOU  537  CB  LEU C  75    13853  14782  15054  -1383  -1995  -2881       C
ATOM    538  CG  LEU C  75     -32.059 -98.400 -25.904  1.00118.19           C
ANISOU  538  CG  LEU C  75    14251  15208  15446  -1351  -1905  -2903       C
ATOM    539  CD1 LEU C  75     -31.575 -97.523 -27.062  1.00 86.33           C
ANISOU  539  CD1 LEU C  75    10335  11170  11297  -1408  -1883  -2935       C
ATOM    540  CD2 LEU C  75     -32.655 -97.575 -24.772  1.00113.01           C
ANISOU  540  CD2 LEU C  75    13511  14584  14844  -1279  -1935  -2821       C
ATOM    541  N   TYR C  76     -31.802-102.089 -26.523  1.00124.34           N
ANISOU  541  N   TYR C  76    15018  15916  16311  -1412  -1905  -3033       N
ATOM    542  CA  TYR C  76     -30.708-102.973 -26.116  1.00149.28           C
ANISOU  542  CA  TYR C  76    18138  19065  19517  -1398  -1814  -3106       C
ATOM    543  C   TYR C  76     -30.264-103.884 -27.264  1.00146.93           C
ANISOU  543  C   TYR C  76    17938  18728  19160  -1458  -1797  -3187       C
ATOM    544  O   TYR C  76     -29.211-104.532 -27.220  1.00124.83           O
ANISOU  544  O   TYR C  76    15138  15918  16373  -1458  -1711  -3259       O
ATOM    545  CB  TYR C  76     -31.147-103.784 -24.906  1.00134.73           C
ANISOU  545  CB  TYR C  76    16161  17231  17799  -1344  -1838  -3070       C
ATOM    546  CG  TYR C  76     -31.760-102.923 -23.830  1.00132.65           C
ANISOU  546  CG  TYR C  76    15806  17007  17588  -1280  -1869  -2982       C
ATOM    547  CD1 TYR C  76     -31.031-102.554 -22.707  1.00169.83           C
ANISOU  547  CD1 TYR C  76    20431  21743  22354  -1221  -1792  -2983       C
ATOM    548  CD2 TYR C  76     -33.060-102.460 -23.947  1.00110.58           C
ANISOU  548  CD2 TYR C  76    13013  14222  14783  -1277  -1975  -2896       C
ATOM    549  CE1 TYR C  76     -31.587-101.761 -21.729  1.00185.40           C
ANISOU  549  CE1 TYR C  76    22325  23749  24368  -1158  -1821  -2906       C
ATOM    550  CE2 TYR C  76     -33.627-101.667 -22.971  1.00100.53           C
ANISOU  550  CE2 TYR C  76    11661  12985  13553  -1213  -2001  -2815       C
ATOM    551  CZ  TYR C  76     -32.890-101.321 -21.868  1.00156.38           C
ANISOU  551  CZ  TYR C  76    18655  20084  20680  -1152  -1925  -2822       C
ATOM    552  OH  TYR C  76     -33.450-100.528 -20.894  1.00178.65           O
ANISOU  552  OH  TYR C  76    21400  22939  23539  -1083  -1953  -2744       O
ATOM    553  N   CYS C  77     -31.118-103.946 -28.277  1.00139.16           N
ANISOU  553  N   CYS C  77    17037  17724  18115  -1510  -1884  -3172       N
ATOM    554  CA  CYS C  77     -30.786-104.536 -29.561  1.00112.02           C
ANISOU  554  CA  CYS C  77    13717  14251  14595  -1572  -1878  -3244       C
ATOM    555  C   CYS C  77     -30.051-103.549 -30.468  1.00121.22           C
ANISOU  555  C   CYS C  77    14986  15427  15646  -1604  -1822  -3279       C
ATOM    556  O   CYS C  77     -29.101-103.919 -31.160  1.00108.38           O
ANISOU  556  O   CYS C  77    13430  13786  13963  -1629  -1753  -3357       O
ATOM    557  CB  CYS C  77     -32.060-105.032 -30.239  1.00 93.83           C
ANISOU  557  CB  CYS C  77    11456  11918  12276  -1615  -2003  -3206       C
ATOM    558  SG  CYS C  77     -32.435-106.746 -29.879  1.00126.17           S
ANISOU  558  SG  CYS C  77    15495  15978  16467  -1609  -2051  -3223       S
ATOM    559  N   ARG C  78     -30.510-102.300 -30.471  1.00133.47           N
ANISOU  559  N   ARG C  78    16544  17005  17164  -1603  -1853  -3217       N
ATOM    560  CA  ARG C  78     -29.970-101.278 -31.359  1.00125.40           C
ANISOU  560  CA  ARG C  78    15615  15997  16036  -1637  -1817  -3236       C
ATOM    561  C   ARG C  78     -28.556-100.879 -30.971  1.00132.41           C
ANISOU  561  C   ARG C  78    16487  16904  16918  -1609  -1697  -3280       C
ATOM    562  O   ARG C  78     -27.706-100.660 -31.831  1.00138.23           O
ANISOU  562  O   ARG C  78    17308  17643  17571  -1640  -1640  -3332       O
ATOM    563  CB  ARG C  78     -30.867-100.040 -31.360  1.00129.60           C
ANISOU  563  CB  ARG C  78    16148  16552  16544  -1639  -1885  -3152       C
ATOM    564  CG  ARG C  78     -32.239-100.252 -31.973  1.00124.03           C
ANISOU  564  CG  ARG C  78    15477  15829  15820  -1680  -2003  -3101       C
ATOM    565  CD  ARG C  78     -32.136-100.783 -33.394  1.00140.19           C
ANISOU  565  CD  ARG C  78    17645  17847  17776  -1752  -2016  -3161       C
ATOM    566  NE  ARG C  78     -31.287 -99.948 -34.236  1.00148.10           N
ANISOU  566  NE  ARG C  78    18729  18864  18677  -1782  -1955  -3202       N
ATOM    567  CZ  ARG C  78     -31.735 -98.933 -34.963  1.00143.28           C
ANISOU  567  CZ  ARG C  78    18178  18270  17994  -1820  -1996  -3164       C
ATOM    568  NH1 ARG C  78     -33.025 -98.631 -34.947  1.00132.13           N
ANISOU  568  NH1 ARG C  78    16751  16857  16595  -1834  -2095  -3084       N
ATOM    569  NH2 ARG C  78     -30.892 -98.221 -35.698  1.00127.68           N
ANISOU  569  NH2 ARG C  78    16269  16311  15931  -1845  -1939  -3201       N
ATOM    570  N   CYS C  79     -28.310-100.774 -29.670  1.00140.88           N
ANISOU  570  N   CYS C  79    17452  17994  18081  -1548  -1661  -3254       N
ATOM    571  CA  CYS C  79     -27.011-100.342 -29.180  1.00126.98           C
ANISOU  571  CA  CYS C  79    15669  16253  16325  -1520  -1552  -3283       C
ATOM    572  C   CYS C  79     -26.094-101.528 -28.928  1.00119.16           C
ANISOU  572  C   CYS C  79    14652  15246  15377  -1510  -1472  -3351       C
ATOM    573  O   CYS C  79     -24.921-101.362 -28.607  1.00121.96           O
ANISOU  573  O   CYS C  79    14994  15614  15733  -1492  -1373  -3380       O
ATOM    574  CB  CYS C  79     -27.189 -99.512 -27.916  1.00117.84           C
ANISOU  574  CB  CYS C  79    14415  15122  15236  -1461  -1554  -3219       C
ATOM    575  SG  CYS C  79     -28.076 -97.969 -28.206  1.00132.11           S
ANISOU  575  SG  CYS C  79    16259  16950  16986  -1469  -1633  -3141       S
ATOM    576  N   HIS C  80     -26.638-102.727 -29.097  1.00131.59           N
ANISOU  576  N   HIS C  80    16221  16792  16985  -1522  -1516  -3373       N
ATOM    577  CA  HIS C  80     -25.890-103.960 -28.875  1.00119.00           C
ANISOU  577  CA  HIS C  80    14601  15179  15437  -1514  -1450  -3437       C
ATOM    578  C   HIS C  80     -25.353-104.054 -27.456  1.00110.43           C
ANISOU  578  C   HIS C  80    13390  14113  14456  -1456  -1385  -3422       C
ATOM    579  O   HIS C  80     -24.140-104.129 -27.241  1.00 97.28           O
ANISOU  579  O   HIS C  80    11717  12454  12791  -1444  -1280  -3463       O
ATOM    580  CB  HIS C  80     -24.730-104.054 -29.856  1.00124.57           C
ANISOU  580  CB  HIS C  80    15406  15877  16049  -1545  -1364  -3510       C
ATOM    581  CG  HIS C  80     -25.136-103.892 -31.287  1.00102.65           C
ANISOU  581  CG  HIS C  80    12756  13085  13160  -1601  -1418  -3528       C
ATOM    582  ND1 HIS C  80     -25.508-104.959 -32.081  1.00106.84           N
ANISOU  582  ND1 HIS C  80    13350  13579  13666  -1635  -1460  -3573       N
ATOM    583  CD2 HIS C  80     -25.228-102.793 -32.063  1.00 87.88           C
ANISOU  583  CD2 HIS C  80    10960  11232  11197  -1631  -1437  -3507       C
ATOM    584  CE1 HIS C  80     -25.810-104.520 -33.287  1.00103.67           C
ANISOU  584  CE1 HIS C  80    13057  13173  13158  -1683  -1502  -3579       C
ATOM    585  NE2 HIS C  80     -25.650-103.210 -33.307  1.00132.45           N
ANISOU  585  NE2 HIS C  80    16710  16853  16762  -1682  -1488  -3539       N
ATOM    586  N   ILE C  81     -26.274-104.091 -26.499  1.00122.80           N
ANISOU  586  N   ILE C  81    14857  15689  16112  -1419  -1451  -3361       N
ATOM    587  CA  ILE C  81     -25.948-104.087 -25.078  1.00105.44           C
ANISOU  587  CA  ILE C  81    12532  13514  14018  -1360  -1404  -3335       C
ATOM    588  C   ILE C  81     -26.706-105.214 -24.358  1.00134.57           C
ANISOU  588  C   ILE C  81    16120  17194  17815  -1335  -1459  -3316       C
ATOM    589  O   ILE C  81     -27.577-105.868 -24.949  1.00154.30           O
ANISOU  589  O   ILE C  81    18652  19670  20307  -1363  -1545  -3313       O
ATOM    590  CB  ILE C  81     -26.274-102.712 -24.456  1.00 88.45           C
ANISOU  590  CB  ILE C  81    10346  11394  11865  -1325  -1426  -3264       C
ATOM    591  CG1 ILE C  81     -27.738-102.623 -24.032  1.00125.80           C
ANISOU  591  CG1 ILE C  81    15021  16133  16643  -1301  -1540  -3188       C
ATOM    592  CG2 ILE C  81     -25.996-101.607 -25.446  1.00 81.12           C
ANISOU  592  CG2 ILE C  81     9531  10469  10820  -1362  -1419  -3268       C
ATOM    593  CD1 ILE C  81     -28.212-101.202 -23.799  1.00138.34           C
ANISOU  593  CD1 ILE C  81    16615  17747  18202  -1278  -1577  -3120       C
ATOM    594  N   ASP C  82     -26.360-105.465 -23.099  1.00119.62           N
ANISOU  594  N   ASP C  82    14105  15321  16023  -1284  -1413  -3303       N
ATOM    595  CA  ASP C  82     -27.066-106.480 -22.322  1.00119.69           C
ANISOU  595  CA  ASP C  82    14005  15330  16142  -1256  -1465  -3278       C
ATOM    596  C   ASP C  82     -28.543-106.152 -22.251  1.00125.26           C
ANISOU  596  C   ASP C  82    14689  16044  16859  -1244  -1592  -3195       C
ATOM    597  O   ASP C  82     -28.938-104.979 -22.277  1.00 89.01           O
ANISOU  597  O   ASP C  82    10124  11473  12222  -1233  -1621  -3145       O
ATOM    598  CB  ASP C  82     -26.542-106.542 -20.901  1.00 96.69           C
ANISOU  598  CB  ASP C  82    10957  12446  13333  -1198  -1400  -3262       C
ATOM    599  CG  ASP C  82     -25.062-106.499 -20.837  1.00121.82           C
ANISOU  599  CG  ASP C  82    14157  15629  16500  -1204  -1269  -3322       C
ATOM    600  OD1 ASP C  82     -24.497-105.435 -21.166  1.00152.40           O
ANISOU  600  OD1 ASP C  82    18098  19510  20296  -1213  -1226  -3324       O
ATOM    601  OD2 ASP C  82     -24.468-107.520 -20.441  1.00126.07           O
ANISOU  601  OD2 ASP C  82    14636  16160  17104  -1200  -1212  -3363       O
ATOM    602  N   HIS C  83     -29.359-107.192 -22.156  1.00110.05           N
ANISOU  602  N   HIS C  83    12715  14105  14995  -1245  -1669  -3176       N
ATOM    603  CA  HIS C  83     -30.787-106.997 -22.070  1.00 94.72           C
ANISOU  603  CA  HIS C  83    10747  12173  13071  -1234  -1793  -3089       C
ATOM    604  C   HIS C  83     -31.281-106.947 -20.637  1.00152.82           C
ANISOU  604  C   HIS C  83    17952  19572  20540  -1160  -1815  -3015       C
ATOM    605  O   HIS C  83     -30.864-107.755 -19.808  1.00154.46           O
ANISOU  605  O   HIS C  83    18059  19789  20842  -1130  -1774  -3033       O
ATOM    606  CB  HIS C  83     -31.518-108.044 -22.901  1.00126.95           C
ANISOU  606  CB  HIS C  83    14875  16215  17143  -1282  -1882  -3097       C
ATOM    607  CG  HIS C  83     -31.725-107.625 -24.324  1.00154.53           C
ANISOU  607  CG  HIS C  83    18521  19679  20513  -1347  -1917  -3118       C
ATOM    608  ND1 HIS C  83     -32.326-106.429 -24.662  1.00147.52           N
ANISOU  608  ND1 HIS C  83    17684  18809  19559  -1353  -1960  -3061       N
ATOM    609  CD2 HIS C  83     -31.400-108.224 -25.491  1.00148.92           C
ANISOU  609  CD2 HIS C  83    17924  18926  19732  -1407  -1912  -3190       C
ATOM    610  CE1 HIS C  83     -32.370-106.318 -25.975  1.00106.29           C
ANISOU  610  CE1 HIS C  83    12594  13557  14233  -1417  -1982  -3096       C
ATOM    611  NE2 HIS C  83     -31.820-107.391 -26.503  1.00135.54           N
ANISOU  611  NE2 HIS C  83    16341  17225  17931  -1450  -1955  -3174       N
ATOM    612  N   PRO C  84     -32.170-105.980 -20.342  1.00157.23           N
ANISOU  612  N   PRO C  84    18494  20159  21088  -1128  -1879  -2929       N
ATOM    613  CA  PRO C  84     -32.658-105.750 -18.977  1.00130.62           C
ANISOU  613  CA  PRO C  84    14985  16835  17811  -1048  -1899  -2852       C
ATOM    614  C   PRO C  84     -33.174-107.031 -18.343  1.00127.54           C
ANISOU  614  C   PRO C  84    14478  16450  17533  -1026  -1948  -2826       C
ATOM    615  O   PRO C  84     -32.974-107.239 -17.152  1.00126.93           O
ANISOU  615  O   PRO C  84    14274  16406  17549   -967  -1915  -2807       O
ATOM    616  CB  PRO C  84     -33.806-104.761 -19.180  1.00141.85           C
ANISOU  616  CB  PRO C  84    16439  18273  19185  -1036  -1989  -2763       C
ATOM    617  CG  PRO C  84     -33.471-104.053 -20.453  1.00108.02           C
ANISOU  617  CG  PRO C  84    12307  13960  14775  -1101  -1973  -2807       C
ATOM    618  CD  PRO C  84     -32.794-105.063 -21.319  1.00 95.86           C
ANISOU  618  CD  PRO C  84    10834  12377  13210  -1164  -1937  -2899       C
ATOM    619  N   ASN C  85     -33.823-107.881 -19.132  1.00147.20           N
ANISOU  619  N   ASN C  85    17010  18907  20013  -1074  -2029  -2825       N
ATOM    620  CA  ASN C  85     -34.272-109.171 -18.630  1.00151.93           C
ANISOU  620  CA  ASN C  85    17505  19505  20716  -1061  -2082  -2803       C
ATOM    621  C   ASN C  85     -33.118-109.895 -17.923  1.00184.71           C
ANISOU  621  C   ASN C  85    21578  23660  24943  -1043  -1977  -2875       C
ATOM    622  O   ASN C  85     -31.968-109.788 -18.347  1.00201.50           O
ANISOU  622  O   ASN C  85    23777  25766  27020  -1074  -1876  -2963       O
ATOM    623  CB  ASN C  85     -34.808-110.021 -19.782  1.00119.35           C
ANISOU  623  CB  ASN C  85    13467  15328  16552  -1131  -2165  -2820       C
ATOM    624  CG  ASN C  85     -35.332-111.361 -19.313  1.00155.35           C
ANISOU  624  CG  ASN C  85    17922  19883  21220  -1121  -2234  -2792       C
ATOM    625  OD1 ASN C  85     -34.557-112.267 -18.985  1.00149.05           O
ANISOU  625  OD1 ASN C  85    17074  19074  20483  -1121  -2175  -2856       O
ATOM    626  ND2 ASN C  85     -36.658-111.495 -19.268  1.00152.83           N
ANISOU  626  ND2 ASN C  85    17567  19575  20928  -1112  -2362  -2690       N
ATOM    627  N   PRO C  86     -33.412-110.608 -16.823  1.00203.09           N
ANISOU  627  N   PRO C  86    23754  26018  27394   -993  -1999  -2832       N
ATOM    628  CA  PRO C  86     -32.343-111.292 -16.079  1.00204.22           C
ANISOU  628  CA  PRO C  86    23810  26168  27615   -976  -1898  -2894       C
ATOM    629  C   PRO C  86     -31.708-112.419 -16.891  1.00194.31           C
ANISOU  629  C   PRO C  86    22619  24860  26350  -1039  -1870  -2987       C
ATOM    630  O   PRO C  86     -30.499-112.687 -16.752  1.00148.19           O
ANISOU  630  O   PRO C  86    16776  19010  20518  -1047  -1756  -3065       O
ATOM    631  CB  PRO C  86     -33.072-111.858 -14.856  1.00200.95           C
ANISOU  631  CB  PRO C  86    23221  25799  27333   -912  -1957  -2813       C
ATOM    632  CG  PRO C  86     -34.500-111.963 -15.282  1.00203.25           C
ANISOU  632  CG  PRO C  86    23526  26087  27614   -919  -2102  -2726       C
ATOM    633  CD  PRO C  86     -34.732-110.806 -16.202  1.00202.14           C
ANISOU  633  CD  PRO C  86    23529  25930  27344   -948  -2116  -2720       C
ATOM    634  N   LYS C  87     -32.529-113.071 -17.715  1.00193.49           N
ANISOU  634  N   LYS C  87    22571  24721  26226  -1082  -1975  -2973       N
ATOM    635  CA  LYS C  87     -32.055-114.111 -18.616  1.00170.17           C
ANISOU  635  CA  LYS C  87    19699  21711  23248  -1142  -1964  -3059       C
ATOM    636  C   LYS C  87     -31.371-113.426 -19.800  1.00162.73           C
ANISOU  636  C   LYS C  87    18928  20736  22167  -1193  -1903  -3131       C
ATOM    637  O   LYS C  87     -30.535-114.016 -20.496  1.00149.00           O
ANISOU  637  O   LYS C  87    17268  18957  20388  -1234  -1843  -3223       O
ATOM    638  CB  LYS C  87     -33.216-114.993 -19.067  1.00140.12           C
ANISOU  638  CB  LYS C  87    15895  17876  19467  -1169  -2106  -3013       C
ATOM    639  CG  LYS C  87     -32.791-116.364 -19.570  1.00170.02           C
ANISOU  639  CG  LYS C  87    19710  21611  23278  -1212  -2105  -3091       C
ATOM    640  CD  LYS C  87     -31.902-117.088 -18.560  1.00179.53           C
ANISOU  640  CD  LYS C  87    20787  22834  24590  -1178  -2014  -3132       C
ATOM    641  CE  LYS C  87     -30.623-117.610 -19.214  1.00177.58           C
ANISOU  641  CE  LYS C  87    20630  22544  24297  -1218  -1905  -3254       C
ATOM    642  NZ  LYS C  87     -29.658-116.516 -19.554  1.00152.45           N
ANISOU  642  NZ  LYS C  87    17540  19370  21015  -1223  -1787  -3303       N
ATOM    643  N   GLY C  88     -31.722-112.159 -20.001  1.00155.56           N
ANISOU  643  N   GLY C  88    18072  19847  21185  -1186  -1917  -3087       N
ATOM    644  CA  GLY C  88     -30.966-111.288 -20.880  1.00146.83           C
ANISOU  644  CA  GLY C  88    17103  18727  19958  -1220  -1845  -3144       C
ATOM    645  C   GLY C  88     -31.300-111.556 -22.316  1.00148.91           C
ANISOU  645  C   GLY C  88    17513  18941  20124  -1289  -1904  -3178       C
ATOM    646  O   GLY C  88     -30.674-111.010 -23.227  1.00161.80           O
ANISOU  646  O   GLY C  88    19269  20557  21650  -1326  -1850  -3233       O
ATOM    647  N   PHE C  89     -32.288-112.422 -22.509  1.00155.84           N
ANISOU  647  N   PHE C  89    18374  19797  21041  -1306  -2017  -3142       N
ATOM    648  CA  PHE C  89     -32.828-112.673 -23.831  1.00152.15           C
ANISOU  648  CA  PHE C  89    18042  19282  20487  -1370  -2096  -3157       C
ATOM    649  C   PHE C  89     -33.875-111.614 -24.109  1.00128.33           C
ANISOU  649  C   PHE C  89    15061  16284  17416  -1375  -2180  -3069       C
ATOM    650  O   PHE C  89     -34.603-111.184 -23.208  1.00135.77           O
ANISOU  650  O   PHE C  89    15898  17268  18421  -1326  -2225  -2976       O
ATOM    651  CB  PHE C  89     -33.421-114.076 -23.922  1.00142.70           C
ANISOU  651  CB  PHE C  89    16814  18048  19356  -1390  -2187  -3153       C
ATOM    652  CG  PHE C  89     -32.427-115.165 -23.647  1.00146.06           C
ANISOU  652  CG  PHE C  89    17203  18454  19839  -1385  -2109  -3239       C
ATOM    653  CD1 PHE C  89     -31.103-115.015 -24.020  1.00150.09           C
ANISOU  653  CD1 PHE C  89    17784  18955  20290  -1397  -1978  -3336       C
ATOM    654  CD2 PHE C  89     -32.809-116.329 -23.000  1.00163.17           C
ANISOU  654  CD2 PHE C  89    19261  20615  22123  -1369  -2165  -3217       C
ATOM    655  CE1 PHE C  89     -30.179-116.008 -23.764  1.00167.19           C
ANISOU  655  CE1 PHE C  89    19915  21103  22508  -1392  -1901  -3411       C
ATOM    656  CE2 PHE C  89     -31.890-117.327 -22.741  1.00174.62           C
ANISOU  656  CE2 PHE C  89    20674  22046  23628  -1365  -2091  -3295       C
ATOM    657  CZ  PHE C  89     -30.572-117.167 -23.123  1.00175.68           C
ANISOU  657  CZ  PHE C  89    20882  22169  23699  -1377  -1957  -3393       C
ATOM    658  N   CYS C  90     -33.918-111.173 -25.357  1.00 98.20           N
ANISOU  658  N   CYS C  90    11390  12439  13481  -1432  -2195  -3098       N
ATOM    659  CA  CYS C  90     -34.821-110.112 -25.757  1.00120.57           C
ANISOU  659  CA  CYS C  90    14272  15288  16251  -1445  -2264  -3021       C
ATOM    660  C   CYS C  90     -36.231-110.661 -26.032  1.00143.60           C
ANISOU  660  C   CYS C  90    17184  18185  19190  -1469  -2414  -2940       C
ATOM    661  O   CYS C  90     -36.406-111.796 -26.480  1.00128.06           O
ANISOU  661  O   CYS C  90    15244  16174  17239  -1504  -2466  -2969       O
ATOM    662  CB  CYS C  90     -34.258-109.386 -26.978  1.00111.50           C
ANISOU  662  CB  CYS C  90    13277  14122  14967  -1497  -2216  -3083       C
ATOM    663  SG  CYS C  90     -35.290-108.068 -27.623  1.00103.46           S
ANISOU  663  SG  CYS C  90    12330  13119  13861  -1524  -2296  -2998       S
ATOM    664  N   ASP C  91     -37.238-109.862 -25.703  1.00147.16           N
ANISOU  664  N   ASP C  91    17596  18670  19648  -1446  -2484  -2832       N
ATOM    665  CA  ASP C  91     -38.624-110.221 -25.975  1.00121.03           C
ANISOU  665  CA  ASP C  91    14285  15348  16354  -1470  -2627  -2737       C
ATOM    666  C   ASP C  91     -39.163-109.579 -27.257  1.00122.80           C
ANISOU  666  C   ASP C  91    14651  15548  16459  -1538  -2681  -2721       C
ATOM    667  O   ASP C  91     -40.349-109.702 -27.570  1.00133.70           O
ANISOU  667  O   ASP C  91    16043  16919  17839  -1564  -2800  -2633       O
ATOM    668  CB  ASP C  91     -39.537-109.977 -24.755  1.00157.34           C
ANISOU  668  CB  ASP C  91    18736  19998  21047  -1399  -2685  -2612       C
ATOM    669  CG  ASP C  91     -39.238-108.664 -24.025  1.00184.03           C
ANISOU  669  CG  ASP C  91    22072  23433  24420  -1339  -2611  -2586       C
ATOM    670  OD1 ASP C  91     -38.161-108.069 -24.256  1.00215.51           O
ANISOU  670  OD1 ASP C  91    26117  27418  28348  -1346  -2503  -2670       O
ATOM    671  OD2 ASP C  91     -40.085-108.238 -23.199  1.00136.07           O
ANISOU  671  OD2 ASP C  91    15901  17401  18398  -1283  -2664  -2477       O
ATOM    672  N   LEU C  92     -38.286-108.892 -27.988  1.00116.47           N
ANISOU  672  N   LEU C  92    13954  14739  15559  -1567  -2594  -2803       N
ATOM    673  CA  LEU C  92     -38.653-108.251 -29.263  1.00133.29           C
ANISOU  673  CA  LEU C  92    16223  16850  17571  -1635  -2632  -2800       C
ATOM    674  C   LEU C  92     -38.050-108.904 -30.507  1.00120.86           C
ANISOU  674  C   LEU C  92    14783  15222  15916  -1704  -2613  -2907       C
ATOM    675  O   LEU C  92     -38.760-109.355 -31.400  1.00128.54           O
ANISOU  675  O   LEU C  92    15836  16156  16847  -1763  -2706  -2891       O
ATOM    676  CB  LEU C  92     -38.259-106.779 -29.267  1.00140.64           C
ANISOU  676  CB  LEU C  92    17178  17819  18438  -1620  -2562  -2796       C
ATOM    677  CG  LEU C  92     -39.124-105.794 -28.496  1.00132.87           C
ANISOU  677  CG  LEU C  92    16115  16883  17486  -1571  -2604  -2679       C
ATOM    678  CD1 LEU C  92     -39.324-104.542 -29.346  1.00117.21           C
ANISOU  678  CD1 LEU C  92    14231  14909  15396  -1611  -2607  -2660       C
ATOM    679  CD2 LEU C  92     -40.454-106.434 -28.141  1.00137.77           C
ANISOU  679  CD2 LEU C  92    16668  17502  18178  -1563  -2730  -2571       C
ATOM    680  N   LYS C  93     -36.725-108.904 -30.573  1.00128.48           N
ANISOU  680  N   LYS C  93    15776  16187  16854  -1694  -2492  -3012       N
ATOM    681  CA  LYS C  93     -36.007-109.434 -31.724  1.00146.74           C
ANISOU  681  CA  LYS C  93    18218  18456  19083  -1749  -2456  -3118       C
ATOM    682  C   LYS C  93     -36.464-110.862 -32.045  1.00143.61           C
ANISOU  682  C   LYS C  93    17839  18004  18720  -1779  -2540  -3134       C
ATOM    683  O   LYS C  93     -36.473-111.740 -31.164  1.00136.24           O
ANISOU  683  O   LYS C  93    16803  17068  17892  -1741  -2549  -3126       O
ATOM    684  CB  LYS C  93     -34.485-109.376 -31.472  1.00124.43           C
ANISOU  684  CB  LYS C  93    15387  15642  16248  -1718  -2308  -3216       C
ATOM    685  CG  LYS C  93     -33.714-110.612 -31.935  1.00126.20           C
ANISOU  685  CG  LYS C  93    15664  15821  16465  -1737  -2269  -3319       C
ATOM    686  CD  LYS C  93     -32.418-110.283 -32.696  1.00108.45           C
ANISOU  686  CD  LYS C  93    13515  13572  14117  -1752  -2151  -3419       C
ATOM    687  CE  LYS C  93     -31.259-109.939 -31.764  1.00124.76           C
ANISOU  687  CE  LYS C  93    15499  15676  16228  -1696  -2021  -3448       C
ATOM    688  NZ  LYS C  93     -29.956-109.892 -32.493  1.00119.84           N
ANISOU  688  NZ  LYS C  93    14969  15048  15518  -1709  -1909  -3545       N
ATOM    689  N   GLY C  94     -36.837-111.091 -33.304  1.00 98.27           N
ANISOU  689  N   GLY C  94    12229  12220  12889  -1847  -2602  -3155       N
ATOM    690  CA  GLY C  94     -37.263-112.410 -33.725  1.00131.87           C
ANISOU  690  CA  GLY C  94    16522  16418  17166  -1882  -2688  -3174       C
ATOM    691  C   GLY C  94     -38.757-112.428 -33.932  1.00133.18           C
ANISOU  691  C   GLY C  94    16689  16571  17344  -1917  -2839  -3061       C
ATOM    692  O   GLY C  94     -39.309-113.386 -34.473  1.00132.48           O
ANISOU  692  O   GLY C  94    16652  16430  17256  -1959  -2935  -3061       O
ATOM    693  N   LYS C  95     -39.408-111.350 -33.505  1.00132.93           N
ANISOU  693  N   LYS C  95    16601  16586  17319  -1899  -2861  -2962       N
ATOM    694  CA  LYS C  95     -40.843-111.178 -33.703  1.00151.64           C
ANISOU  694  CA  LYS C  95    18970  18952  19693  -1931  -2998  -2841       C
ATOM    695  C   LYS C  95     -41.117-109.779 -34.258  1.00149.79           C
ANISOU  695  C   LYS C  95    18796  18749  19367  -1956  -2987  -2800       C
ATOM    696  O   LYS C  95     -40.214-108.950 -34.311  1.00146.78           O
ANISOU  696  O   LYS C  95    18436  18396  18936  -1940  -2878  -2859       O
ATOM    697  CB  LYS C  95     -41.615-111.444 -32.401  1.00136.69           C
ANISOU  697  CB  LYS C  95    16918  17090  17929  -1871  -3059  -2731       C
ATOM    698  CG  LYS C  95     -41.453-112.877 -31.892  1.00152.70           C
ANISOU  698  CG  LYS C  95    18881  19086  20052  -1852  -3085  -2762       C
ATOM    699  CD  LYS C  95     -42.710-113.398 -31.203  1.00164.24           C
ANISOU  699  CD  LYS C  95    20237  20554  21614  -1835  -3217  -2629       C
ATOM    700  CE  LYS C  95     -42.737-114.929 -31.177  1.00153.63           C
ANISOU  700  CE  LYS C  95    18878  19159  20337  -1848  -3280  -2660       C
ATOM    701  NZ  LYS C  95     -41.467-115.557 -30.702  1.00110.32           N
ANISOU  701  NZ  LYS C  95    13353  13668  14895  -1811  -3167  -2778       N
ATOM    702  N   TYR C  96     -42.345-109.538 -34.707  1.00143.00           N
ANISOU  702  N   TYR C  96    17967  17882  18486  -2000  -3102  -2699       N
ATOM    703  CA  TYR C  96     -42.744-108.242 -35.254  1.00114.37           C
ANISOU  703  CA  TYR C  96    14394  14283  14777  -2030  -3105  -2648       C
ATOM    704  C   TYR C  96     -43.428-107.424 -34.171  1.00122.56           C
ANISOU  704  C   TYR C  96    15308  15378  15882  -1969  -3123  -2527       C
ATOM    705  O   TYR C  96     -44.043-107.983 -33.260  1.00135.71           O
ANISOU  705  O   TYR C  96    16865  17052  17648  -1926  -3183  -2451       O
ATOM    706  CB  TYR C  96     -43.674-108.411 -36.459  1.00143.23           C
ANISOU  706  CB  TYR C  96    18162  17897  18360  -2119  -3217  -2607       C
ATOM    707  CG  TYR C  96     -42.959-108.712 -37.766  1.00158.56           C
ANISOU  707  CG  TYR C  96    20255  19795  20194  -2184  -3183  -2727       C
ATOM    708  CD1 TYR C  96     -42.260-107.718 -38.438  1.00141.78           C
ANISOU  708  CD1 TYR C  96    18205  17693  17971  -2203  -3096  -2787       C
ATOM    709  CD2 TYR C  96     -42.995-109.984 -38.334  1.00139.34           C
ANISOU  709  CD2 TYR C  96    17888  17298  17756  -2224  -3241  -2779       C
ATOM    710  CE1 TYR C  96     -41.608-107.979 -39.618  1.00137.40           C
ANISOU  710  CE1 TYR C  96    17784  17105  17317  -2256  -3064  -2892       C
ATOM    711  CE2 TYR C  96     -42.337-110.253 -39.523  1.00120.40           C
ANISOU  711  CE2 TYR C  96    15630  14862  15256  -2276  -3209  -2889       C
ATOM    712  CZ  TYR C  96     -41.646-109.241 -40.159  1.00136.51           C
ANISOU  712  CZ  TYR C  96    17738  16930  17197  -2291  -3118  -2944       C
ATOM    713  OH  TYR C  96     -40.983-109.480 -41.340  1.00121.30           O
ANISOU  713  OH  TYR C  96    15949  14973  15167  -2337  -3083  -3050       O
ATOM    714  N   VAL C  97     -43.275-106.105 -34.229  1.00140.95           N
ANISOU  714  N   VAL C  97    17650  17747  18157  -1960  -3069  -2512       N
ATOM    715  CA  VAL C  97     -43.850-105.236 -33.201  1.00182.93           C
ANISOU  715  CA  VAL C  97    22857  23118  23529  -1896  -3076  -2403       C
ATOM    716  C   VAL C  97     -44.785-104.204 -33.801  1.00194.58           C
ANISOU  716  C   VAL C  97    24382  24609  24939  -1937  -3136  -2310       C
ATOM    717  O   VAL C  97     -44.462-103.574 -34.821  1.00184.39           O
ANISOU  717  O   VAL C  97    23200  23312  23549  -1994  -3106  -2359       O
ATOM    718  CB  VAL C  97     -42.763-104.487 -32.394  1.00228.73           C
ANISOU  718  CB  VAL C  97    28599  28961  29345  -1825  -2948  -2460       C
ATOM    719  CG1 VAL C  97     -43.403-103.580 -31.353  1.00236.91           C
ANISOU  719  CG1 VAL C  97    29531  30051  30434  -1756  -2962  -2348       C
ATOM    720  CG2 VAL C  97     -41.807-105.471 -31.733  1.00250.01           C
ANISOU  720  CG2 VAL C  97    31236  31644  32110  -1783  -2881  -2548       C
ATOM    721  N   GLN C  98     -45.932-104.016 -33.153  1.00193.49           N
ANISOU  721  N   GLN C  98    24162  24497  24858  -1905  -3218  -2173       N
ATOM    722  CA  GLN C  98     -46.945-103.116 -33.677  1.00178.32           C
ANISOU  722  CA  GLN C  98    22280  22589  22883  -1944  -3284  -2068       C
ATOM    723  C   GLN C  98     -47.094-101.871 -32.789  1.00177.82           C
ANISOU  723  C   GLN C  98    22137  22586  22840  -1870  -3243  -1999       C
ATOM    724  O   GLN C  98     -47.232-101.986 -31.558  1.00133.46           O
ANISOU  724  O   GLN C  98    16397  17000  17312  -1784  -3239  -1949       O
ATOM    725  CB  GLN C  98     -48.261-103.876 -33.830  1.00160.80           C
ANISOU  725  CB  GLN C  98    20049  20348  20699  -1978  -3423  -1952       C
ATOM    726  CG  GLN C  98     -48.082-105.401 -34.012  1.00173.18           C
ANISOU  726  CG  GLN C  98    21630  21863  22306  -2005  -3465  -2009       C
ATOM    727  CD  GLN C  98     -47.665-105.819 -35.432  1.00180.05           C
ANISOU  727  CD  GLN C  98    22653  22677  23081  -2101  -3468  -2110       C
ATOM    728  OE1 GLN C  98     -47.507-107.009 -35.715  1.00166.18           O
ANISOU  728  OE1 GLN C  98    20927  20872  21343  -2129  -3504  -2163       O
ATOM    729  NE2 GLN C  98     -47.502-104.846 -36.326  1.00144.23           N
ANISOU  729  NE2 GLN C  98    18212  18147  18443  -2151  -3433  -2136       N
ATOM    730  N   ILE C  99     -47.042-100.694 -33.423  1.00201.66           N
ANISOU  730  N   ILE C  99    25226  25621  25775  -1902  -3214  -1999       N
ATOM    731  CA  ILE C  99     -47.047 -99.406 -32.722  1.00215.37           C
ANISOU  731  CA  ILE C  99    26907  27408  27514  -1838  -3168  -1950       C
ATOM    732  C   ILE C  99     -48.013 -98.415 -33.369  1.00209.92           C
ANISOU  732  C   ILE C  99    26267  26732  26762  -1884  -3226  -1851       C
ATOM    733  O   ILE C  99     -48.081 -98.330 -34.594  1.00232.02           O
ANISOU  733  O   ILE C  99    29174  29505  29479  -1975  -3247  -1878       O
ATOM    734  CB  ILE C  99     -45.646 -98.741 -32.770  1.00172.59           C
ANISOU  734  CB  ILE C  99    21522  21999  22053  -1823  -3043  -2074       C
ATOM    735  CG1 ILE C  99     -44.571 -99.652 -32.178  1.00165.20           C
ANISOU  735  CG1 ILE C  99    20544  21052  21174  -1782  -2972  -2178       C
ATOM    736  CG2 ILE C  99     -45.655 -97.379 -32.078  1.00175.58           C
ANISOU  736  CG2 ILE C  99    21854  22426  22433  -1759  -3003  -2025       C
ATOM    737  CD1 ILE C  99     -43.909-100.552 -33.197  1.00180.22           C
ANISOU  737  CD1 ILE C  99    22542  22906  23027  -1855  -2956  -2289       C
ATOM    738  N   PRO C 100     -48.747 -97.643 -32.545  1.00179.60           N
ANISOU  738  N   PRO C 100    22347  22934  22957  -1818  -3249  -1736       N
ATOM    739  CA  PRO C 100     -49.611 -96.534 -32.979  1.00171.22           C
ANISOU  739  CA  PRO C 100    21320  21895  21843  -1845  -3290  -1637       C
ATOM    740  C   PRO C 100     -48.889 -95.535 -33.890  1.00169.66           C
ANISOU  740  C   PRO C 100    21220  21696  21549  -1900  -3225  -1718       C
ATOM    741  O   PRO C 100     -47.702 -95.295 -33.699  1.00178.71           O
ANISOU  741  O   PRO C 100    22371  22845  22685  -1873  -3131  -1827       O
ATOM    742  CB  PRO C 100     -49.994 -95.868 -31.660  1.00159.96           C
ANISOU  742  CB  PRO C 100    19781  20518  20480  -1734  -3282  -1547       C
ATOM    743  CG  PRO C 100     -50.035 -97.003 -30.694  1.00167.64           C
ANISOU  743  CG  PRO C 100    20655  21490  21551  -1672  -3301  -1535       C
ATOM    744  CD  PRO C 100     -48.926 -97.941 -31.112  1.00163.91           C
ANISOU  744  CD  PRO C 100    20228  20978  21074  -1712  -3250  -1682       C
ATOM    745  N   THR C 101     -49.598 -94.967 -34.865  1.00182.22           N
ANISOU  745  N   THR C 101    22883  23283  23070  -1976  -3276  -1659       N
ATOM    746  CA  THR C 101     -48.972 -94.113 -35.883  1.00193.62           C
ANISOU  746  CA  THR C 101    24423  24725  24419  -2041  -3225  -1733       C
ATOM    747  C   THR C 101     -48.545 -92.732 -35.378  1.00186.25           C
ANISOU  747  C   THR C 101    23463  23832  23473  -1984  -3158  -1733       C
ATOM    748  O   THR C 101     -47.608 -92.135 -35.917  1.00165.27           O
ANISOU  748  O   THR C 101    20863  21177  20756  -2012  -3090  -1825       O
ATOM    749  CB  THR C 101     -49.874 -93.945 -37.142  1.00181.13           C
ANISOU  749  CB  THR C 101    22927  23127  22766  -2149  -3302  -1670       C
ATOM    750  OG1 THR C 101     -50.029 -95.210 -37.798  1.00174.75           O
ANISOU  750  OG1 THR C 101    22170  22274  21954  -2214  -3355  -1699       O
ATOM    751  CG2 THR C 101     -49.254 -92.958 -38.130  1.00163.63           C
ANISOU  751  CG2 THR C 101    20798  20918  20455  -2210  -3249  -1737       C
ATOM    752  N   THR C 102     -49.226 -92.227 -34.352  1.00195.37           N
ANISOU  752  N   THR C 102    24530  25019  24681  -1903  -3180  -1628       N
ATOM    753  CA  THR C 102     -48.938 -90.890 -33.829  1.00206.31           C
ANISOU  753  CA  THR C 102    25892  26440  26056  -1844  -3128  -1617       C
ATOM    754  C   THR C 102     -47.526 -90.802 -33.243  1.00211.71           C
ANISOU  754  C   THR C 102    26556  27127  26756  -1789  -3026  -1739       C
ATOM    755  O   THR C 102     -46.750 -89.906 -33.585  1.00188.45           O
ANISOU  755  O   THR C 102    23655  24189  23758  -1803  -2967  -1801       O
ATOM    756  CB  THR C 102     -49.972 -90.453 -32.758  1.00205.67           C
ANISOU  756  CB  THR C 102    25720  26393  26033  -1756  -3173  -1478       C
ATOM    757  OG1 THR C 102     -49.611 -90.988 -31.478  1.00218.36           O
ANISOU  757  OG1 THR C 102    27231  28012  27724  -1655  -3143  -1494       O
ATOM    758  CG2 THR C 102     -51.366 -90.934 -33.127  1.00200.66           C
ANISOU  758  CG2 THR C 102    25083  25753  25405  -1799  -3278  -1350       C
ATOM    759  N   CYS C 103     -47.201 -91.746 -32.367  1.00220.89           N
ANISOU  759  N   CYS C 103    27650  28285  27995  -1729  -3009  -1768       N
ATOM    760  CA  CYS C 103     -45.892 -91.796 -31.727  1.00208.50           C
ANISOU  760  CA  CYS C 103    26053  26717  26451  -1675  -2914  -1876       C
ATOM    761  C   CYS C 103     -44.913 -92.639 -32.544  1.00189.81           C
ANISOU  761  C   CYS C 103    23753  24316  24050  -1742  -2871  -2002       C
ATOM    762  O   CYS C 103     -43.774 -92.859 -32.138  1.00198.31           O
ANISOU  762  O   CYS C 103    24813  25390  25145  -1709  -2791  -2096       O
ATOM    763  CB  CYS C 103     -46.017 -92.345 -30.303  1.00221.66           C
ANISOU  763  CB  CYS C 103    27602  28400  28218  -1571  -2912  -1841       C
ATOM    764  SG  CYS C 103     -46.843 -93.947 -30.199  1.00192.45           S
ANISOU  764  SG  CYS C 103    23857  24680  24585  -1584  -2994  -1792       S
ATOM    765  N   ALA C 104     -45.361 -93.087 -33.710  1.00183.41           N
ANISOU  765  N   ALA C 104    23020  23480  23187  -1835  -2924  -2000       N
ATOM    766  CA  ALA C 104     -44.570 -93.958 -34.569  1.00163.73           C
ANISOU  766  CA  ALA C 104    20601  20953  20657  -1900  -2894  -2113       C
ATOM    767  C   ALA C 104     -43.295 -93.268 -35.029  1.00158.00           C
ANISOU  767  C   ALA C 104    19931  20234  19868  -1916  -2801  -2217       C
ATOM    768  O   ALA C 104     -42.488 -93.860 -35.744  1.00173.31           O
ANISOU  768  O   ALA C 104    21933  22150  21766  -1962  -2761  -2316       O
ATOM    769  CB  ALA C 104     -45.387 -94.425 -35.761  1.00180.18           C
ANISOU  769  CB  ALA C 104    22764  23009  22688  -1997  -2976  -2081       C
ATOM    770  N   ASN C 105     -43.137 -92.000 -34.665  1.00151.18           N
ANISOU  770  N   ASN C 105    19049  19402  18991  -1880  -2770  -2190       N
ATOM    771  CA  ASN C 105     -41.860 -91.329 -34.868  1.00171.77           C
ANISOU  771  CA  ASN C 105    21691  22019  21553  -1880  -2680  -2280       C
ATOM    772  C   ASN C 105     -40.733 -92.032 -34.091  1.00179.28           C
ANISOU  772  C   ASN C 105    22597  22963  22558  -1823  -2601  -2367       C
ATOM    773  O   ASN C 105     -39.644 -92.290 -34.629  1.00145.39           O
ANISOU  773  O   ASN C 105    18355  18661  18225  -1853  -2536  -2466       O
ATOM    774  CB  ASN C 105     -41.943 -89.857 -34.455  1.00163.17           C
ANISOU  774  CB  ASN C 105    20581  20963  20454  -1841  -2670  -2227       C
ATOM    775  CG  ASN C 105     -40.951 -88.981 -35.219  1.00183.42           C
ANISOU  775  CG  ASN C 105    23214  23537  22941  -1883  -2612  -2295       C
ATOM    776  OD1 ASN C 105     -40.077 -89.485 -35.931  1.00177.83           O
ANISOU  776  OD1 ASN C 105    22560  22815  22191  -1928  -2566  -2387       O
ATOM    777  ND2 ASN C 105     -41.080 -87.666 -35.072  1.00186.55           N
ANISOU  777  ND2 ASN C 105    23605  23958  23317  -1865  -2614  -2248       N
ATOM    778  N   ASP C 106     -41.018 -92.362 -32.833  1.00185.47           N
ANISOU  778  N   ASP C 106    23283  23755  23432  -1741  -2608  -2324       N
ATOM    779  CA  ASP C 106     -40.035 -92.962 -31.931  1.00190.00           C
ANISOU  779  CA  ASP C 106    23797  24326  24067  -1680  -2534  -2393       C
ATOM    780  C   ASP C 106     -40.504 -94.342 -31.459  1.00172.30           C
ANISOU  780  C   ASP C 106    21499  22067  21901  -1661  -2572  -2380       C
ATOM    781  O   ASP C 106     -41.040 -94.477 -30.355  1.00158.57           O
ANISOU  781  O   ASP C 106    19665  20345  20242  -1589  -2597  -2315       O
ATOM    782  CB  ASP C 106     -39.808 -92.028 -30.733  1.00192.41           C
ANISOU  782  CB  ASP C 106    24028  24662  24417  -1591  -2498  -2359       C
ATOM    783  CG  ASP C 106     -38.689 -92.487 -29.824  1.00170.11           C
ANISOU  783  CG  ASP C 106    21147  21838  21650  -1532  -2414  -2430       C
ATOM    784  OD1 ASP C 106     -37.710 -91.730 -29.680  1.00174.57           O
ANISOU  784  OD1 ASP C 106    21726  22413  22191  -1516  -2345  -2475       O
ATOM    785  OD2 ASP C 106     -38.795 -93.584 -29.238  1.00155.65           O
ANISOU  785  OD2 ASP C 106    19253  19997  19889  -1503  -2420  -2435       O
ATOM    786  N   PRO C 107     -40.306 -95.374 -32.301  1.00162.36           N
ANISOU  786  N   PRO C 107    20298  20776  20617  -1725  -2580  -2442       N
ATOM    787  CA  PRO C 107     -40.758 -96.734 -31.967  1.00156.78           C
ANISOU  787  CA  PRO C 107    19545  20046  19978  -1716  -2625  -2432       C
ATOM    788  C   PRO C 107     -40.005 -97.311 -30.770  1.00158.52           C
ANISOU  788  C   PRO C 107    19671  20273  20286  -1639  -2560  -2473       C
ATOM    789  O   PRO C 107     -40.565 -98.037 -29.934  1.00117.01           O
ANISOU  789  O   PRO C 107    14325  15018  15115  -1593  -2600  -2424       O
ATOM    790  CB  PRO C 107     -40.439 -97.539 -33.238  1.00129.49           C
ANISOU  790  CB  PRO C 107    16192  16550  16457  -1802  -2629  -2510       C
ATOM    791  CG  PRO C 107     -39.421 -96.732 -33.981  1.00132.41           C
ANISOU  791  CG  PRO C 107    16642  16929  16740  -1835  -2552  -2586       C
ATOM    792  CD  PRO C 107     -39.669 -95.298 -33.631  1.00134.90           C
ANISOU  792  CD  PRO C 107    16935  17280  17042  -1806  -2550  -2521       C
ATOM    793  N   VAL C 108     -38.725 -96.968 -30.710  1.00168.57           N
ANISOU  793  N   VAL C 108    20961  21551  21536  -1627  -2460  -2560       N
ATOM    794  CA  VAL C 108     -37.820 -97.435 -29.677  1.00159.43           C
ANISOU  794  CA  VAL C 108    19725  20400  20451  -1563  -2383  -2610       C
ATOM    795  C   VAL C 108     -38.237 -96.966 -28.284  1.00159.10           C
ANISOU  795  C   VAL C 108    19569  20392  20491  -1472  -2392  -2533       C
ATOM    796  O   VAL C 108     -38.369 -97.777 -27.351  1.00138.12           O
ANISOU  796  O   VAL C 108    16817  17738  17924  -1420  -2397  -2518       O
ATOM    797  CB  VAL C 108     -36.413 -96.930 -29.985  1.00159.42           C
ANISOU  797  CB  VAL C 108    19775  20401  20396  -1574  -2278  -2702       C
ATOM    798  CG1 VAL C 108     -35.658 -97.950 -30.816  1.00177.77           C
ANISOU  798  CG1 VAL C 108    22165  22693  22686  -1627  -2239  -2800       C
ATOM    799  CG2 VAL C 108     -36.504 -95.598 -30.733  1.00147.01           C
ANISOU  799  CG2 VAL C 108    18278  18844  18735  -1610  -2287  -2679       C
ATOM    800  N   GLY C 109     -38.437 -95.658 -28.145  1.00160.25           N
ANISOU  800  N   GLY C 109    19722  20562  20603  -1451  -2394  -2484       N
ATOM    801  CA  GLY C 109     -38.832 -95.101 -26.869  1.00159.20           C
ANISOU  801  CA  GLY C 109    19492  20462  20536  -1361  -2402  -2411       C
ATOM    802  C   GLY C 109     -40.119 -95.755 -26.442  1.00151.71           C
ANISOU  802  C   GLY C 109    18475  19519  19650  -1335  -2493  -2318       C
ATOM    803  O   GLY C 109     -40.314 -96.090 -25.272  1.00143.82           O
ANISOU  803  O   GLY C 109    17368  18540  18737  -1258  -2495  -2280       O
ATOM    804  N   PHE C 110     -40.988 -95.962 -27.422  1.00153.03           N
ANISOU  804  N   PHE C 110    18704  19669  19772  -1403  -2571  -2278       N
ATOM    805  CA  PHE C 110     -42.298 -96.532 -27.179  1.00158.32           C
ANISOU  805  CA  PHE C 110    19321  20344  20491  -1391  -2671  -2175       C
ATOM    806  C   PHE C 110     -42.235 -97.888 -26.473  1.00158.54           C
ANISOU  806  C   PHE C 110    19262  20365  20613  -1358  -2676  -2189       C
ATOM    807  O   PHE C 110     -43.022 -98.143 -25.556  1.00163.00           O
ANISOU  807  O   PHE C 110    19726  20954  21252  -1294  -2727  -2100       O
ATOM    808  CB  PHE C 110     -43.067 -96.645 -28.489  1.00162.25           C
ANISOU  808  CB  PHE C 110    19913  20816  20918  -1484  -2746  -2146       C
ATOM    809  CG  PHE C 110     -44.513 -96.984 -28.306  1.00177.93           C
ANISOU  809  CG  PHE C 110    21852  22810  22942  -1476  -2856  -2019       C
ATOM    810  CD1 PHE C 110     -44.928 -98.305 -28.257  1.00177.57           C
ANISOU  810  CD1 PHE C 110    21772  22744  22953  -1489  -2913  -2005       C
ATOM    811  CD2 PHE C 110     -45.456 -95.983 -28.167  1.00174.24           C
ANISOU  811  CD2 PHE C 110    21374  22371  22457  -1453  -2905  -1909       C
ATOM    812  CE1 PHE C 110     -46.247 -98.622 -28.080  1.00173.91           C
ANISOU  812  CE1 PHE C 110    21262  22289  22526  -1482  -3018  -1879       C
ATOM    813  CE2 PHE C 110     -46.782 -96.295 -27.990  1.00194.51           C
ANISOU  813  CE2 PHE C 110    23896  24948  25059  -1443  -3005  -1782       C
ATOM    814  CZ  PHE C 110     -47.179 -97.617 -27.948  1.00201.65           C
ANISOU  814  CZ  PHE C 110    24764  25833  26019  -1458  -3063  -1765       C
ATOM    815  N   THR C 111     -41.304 -98.748 -26.893  1.00141.88           N
ANISOU  815  N   THR C 111    17188  18224  18498  -1399  -2625  -2297       N
ATOM    816  CA  THR C 111     -41.185-100.094 -26.320  1.00140.83           C
ANISOU  816  CA  THR C 111    16978  18079  18452  -1376  -2630  -2318       C
ATOM    817  C   THR C 111     -40.714-100.037 -24.891  1.00139.53           C
ANISOU  817  C   THR C 111    16693  17949  18374  -1281  -2572  -2316       C
ATOM    818  O   THR C 111     -41.091-100.884 -24.066  1.00117.93           O
ANISOU  818  O   THR C 111    13853  15223  15730  -1235  -2604  -2277       O
ATOM    819  CB  THR C 111     -40.171-100.962 -27.054  1.00137.48           C
ANISOU  819  CB  THR C 111    16621  17614  18000  -1435  -2575  -2442       C
ATOM    820  OG1 THR C 111     -40.334-100.812 -28.471  1.00127.27           O
ANISOU  820  OG1 THR C 111    15458  16291  16607  -1525  -2606  -2466       O
ATOM    821  CG2 THR C 111     -40.356-102.430 -26.631  1.00 99.80           C
ANISOU  821  CG2 THR C 111    11778  12824  13315  -1425  -2610  -2445       C
ATOM    822  N   LEU C 112     -39.851 -99.056 -24.628  1.00124.19           N
ANISOU  822  N   LEU C 112    14765  16021  16400  -1254  -2487  -2359       N
ATOM    823  CA  LEU C 112     -39.419 -98.745 -23.277  1.00141.45           C
ANISOU  823  CA  LEU C 112    16848  18242  18657  -1162  -2431  -2351       C
ATOM    824  C   LEU C 112     -40.606 -98.223 -22.470  1.00161.66           C
ANISOU  824  C   LEU C 112    19328  20840  21256  -1091  -2503  -2224       C
ATOM    825  O   LEU C 112     -40.952 -98.775 -21.416  1.00132.96           O
ANISOU  825  O   LEU C 112    15576  17229  17712  -1023  -2522  -2176       O
ATOM    826  CB  LEU C 112     -38.323 -97.677 -23.317  1.00150.83           C
ANISOU  826  CB  LEU C 112    18087  19434  19789  -1158  -2338  -2414       C
ATOM    827  CG  LEU C 112     -36.856 -98.083 -23.507  1.00164.39           C
ANISOU  827  CG  LEU C 112    19835  21130  21496  -1185  -2235  -2534       C
ATOM    828  CD1 LEU C 112     -35.999 -96.913 -24.047  1.00119.02           C
ANISOU  828  CD1 LEU C 112    14178  15383  15663  -1211  -2171  -2581       C
ATOM    829  CD2 LEU C 112     -36.270 -98.656 -22.201  1.00133.67           C
ANISOU  829  CD2 LEU C 112    15826  17257  17707  -1114  -2177  -2553       C
ATOM    830  N   ARG C 113     -41.234 -97.177 -23.011  1.00174.07           N
ANISOU  830  N   ARG C 113    20964  22417  22757  -1109  -2544  -2167       N
ATOM    831  CA  ARG C 113     -42.274 -96.381 -22.352  1.00149.59           C
ANISOU  831  CA  ARG C 113    17810  19354  19672  -1041  -2601  -2048       C
ATOM    832  C   ARG C 113     -43.441 -97.180 -21.764  1.00177.27           C
ANISOU  832  C   ARG C 113    21219  22880  23256  -1000  -2689  -1943       C
ATOM    833  O   ARG C 113     -43.875 -96.911 -20.642  1.00175.76           O
ANISOU  833  O   ARG C 113    20929  22730  23122   -906  -2701  -1869       O
ATOM    834  CB  ARG C 113     -42.819 -95.350 -23.345  1.00141.29           C
ANISOU  834  CB  ARG C 113    16862  18296  18525  -1094  -2641  -2009       C
ATOM    835  CG  ARG C 113     -42.918 -93.938 -22.801  1.00154.65           C
ANISOU  835  CG  ARG C 113    18548  20017  20194  -1031  -2624  -1962       C
ATOM    836  CD  ARG C 113     -41.718 -93.101 -23.196  1.00137.57           C
ANISOU  836  CD  ARG C 113    16463  17841  17968  -1059  -2540  -2058       C
ATOM    837  NE  ARG C 113     -41.501 -93.074 -24.641  1.00155.25           N
ANISOU  837  NE  ARG C 113    18818  20048  20121  -1167  -2544  -2110       N
ATOM    838  CZ  ARG C 113     -40.846 -92.104 -25.279  1.00159.98           C
ANISOU  838  CZ  ARG C 113    19502  20641  20644  -1206  -2501  -2158       C
ATOM    839  NH1 ARG C 113     -40.679 -92.159 -26.602  1.00136.70           N
ANISOU  839  NH1 ARG C 113    16653  17667  17619  -1302  -2507  -2202       N
ATOM    840  NH2 ARG C 113     -40.356 -91.073 -24.591  1.00140.80           N
ANISOU  840  NH2 ARG C 113    17056  18229  18214  -1146  -2457  -2159       N
ATOM    841  N   ASN C 114     -43.929 -98.169 -22.516  1.00180.95           N
ANISOU  841  N   ASN C 114    21712  23319  23723  -1068  -2752  -1934       N
ATOM    842  CA  ASN C 114     -45.172 -98.873 -22.188  1.00151.56           C
ANISOU  842  CA  ASN C 114    17913  19612  20060  -1045  -2855  -1819       C
ATOM    843  C   ASN C 114     -44.938-100.366 -22.011  1.00155.05           C
ANISOU  843  C   ASN C 114    18300  20036  20577  -1059  -2866  -1859       C
ATOM    844  O   ASN C 114     -43.842-100.867 -22.295  1.00142.96           O
ANISOU  844  O   ASN C 114    16804  18475  19041  -1096  -2795  -1979       O
ATOM    845  CB  ASN C 114     -46.234 -98.641 -23.262  1.00115.13           C
ANISOU  845  CB  ASN C 114    13382  14982  15380  -1116  -2947  -1742       C
ATOM    846  CG  ASN C 114     -46.208 -97.227 -23.810  1.00148.90           C
ANISOU  846  CG  ASN C 114    17748  19264  19565  -1135  -2923  -1739       C
ATOM    847  OD1 ASN C 114     -45.446 -96.922 -24.732  1.00158.23           O
ANISOU  847  OD1 ASN C 114    19033  20415  20673  -1205  -2874  -1833       O
ATOM    848  ND2 ASN C 114     -47.044 -96.354 -23.248  1.00142.37           N
ANISOU  848  ND2 ASN C 114    16878  18475  18741  -1070  -2958  -1627       N
ATOM    849  N   THR C 115     -45.941-101.063 -21.478  1.00151.90           N
ANISOU  849  N   THR C 115    17807  19658  20252  -1023  -2953  -1754       N
ATOM    850  CA  THR C 115     -45.848-102.512 -21.310  1.00172.86           C
ANISOU  850  CA  THR C 115    20402  22294  22983  -1037  -2980  -1778       C
ATOM    851  C   THR C 115     -47.064-103.219 -21.904  1.00169.43           C
ANISOU  851  C   THR C 115    19978  21843  22554  -1086  -3109  -1681       C
ATOM    852  O   THR C 115     -48.116-102.609 -22.077  1.00189.99           O
ANISOU  852  O   THR C 115    22594  24465  25128  -1082  -3180  -1566       O
ATOM    853  CB  THR C 115     -45.667-102.902 -19.830  1.00161.78           C
ANISOU  853  CB  THR C 115    18842  20936  21690   -934  -2952  -1755       C
ATOM    854  OG1 THR C 115     -44.433-102.357 -19.344  1.00154.91           O
ANISOU  854  OG1 THR C 115    17971  20074  20814   -900  -2831  -1855       O
ATOM    855  CG2 THR C 115     -45.650-104.417 -19.663  1.00123.14           C
ANISOU  855  CG2 THR C 115    13881  16025  16880   -951  -2989  -1771       C
ATOM    856  N   VAL C 116     -46.903-104.498 -22.241  1.00174.12           N
ANISOU  856  N   VAL C 116    20573  22399  23185  -1135  -3139  -1726       N
ATOM    857  CA  VAL C 116     -47.979-105.286 -22.843  1.00178.99           C
ANISOU  857  CA  VAL C 116    21206  22991  23810  -1190  -3266  -1641       C
ATOM    858  C   VAL C 116     -48.863-105.988 -21.817  1.00182.26           C
ANISOU  858  C   VAL C 116    21471  23446  24336  -1121  -3350  -1517       C
ATOM    859  O   VAL C 116     -48.381-106.479 -20.791  1.00185.82           O
ANISOU  859  O   VAL C 116    21807  23923  24874  -1054  -3308  -1542       O
ATOM    860  CB  VAL C 116     -47.441-106.359 -23.815  1.00164.23           C
ANISOU  860  CB  VAL C 116    19424  21055  21920  -1283  -3272  -1748       C
ATOM    861  CG1 VAL C 116     -47.031-105.729 -25.139  1.00118.73           C
ANISOU  861  CG1 VAL C 116    13826  15251  16034  -1370  -3237  -1827       C
ATOM    862  CG2 VAL C 116     -46.292-107.137 -23.180  1.00167.31           C
ANISOU  862  CG2 VAL C 116    19751  21440  22378  -1252  -3187  -1860       C
ATOM    863  N   CYS C 117     -50.157-106.038 -22.117  1.00155.58           N
ANISOU  863  N   CYS C 117    18091  20071  20952  -1139  -3469  -1380       N
ATOM    864  CA  CYS C 117     -51.129-106.727 -21.283  1.00171.41           C
ANISOU  864  CA  CYS C 117    19959  22113  23055  -1082  -3566  -1243       C
ATOM    865  C   CYS C 117     -50.888-108.238 -21.314  1.00160.53           C
ANISOU  865  C   CYS C 117    18545  20700  21751  -1116  -3607  -1289       C
ATOM    866  O   CYS C 117     -50.768-108.831 -22.385  1.00161.80           O
ANISOU  866  O   CYS C 117    18813  20796  21868  -1213  -3641  -1349       O
ATOM    867  CB  CYS C 117     -52.537-106.405 -21.801  1.00198.68           C
ANISOU  867  CB  CYS C 117    23444  25573  26472  -1110  -3686  -1086       C
ATOM    868  SG  CYS C 117     -53.945-106.782 -20.709  1.00172.52           S
ANISOU  868  SG  CYS C 117    19961  22327  23261  -1019  -3806   -872       S
ATOM    869  N   THR C 118     -50.813-108.859 -20.142  1.00140.35           N
ANISOU  869  N   THR C 118    15837  18184  19304  -1037  -3606  -1261       N
ATOM    870  CA  THR C 118     -50.794-110.316 -20.066  1.00148.20           C
ANISOU  870  CA  THR C 118    16776  19151  20382  -1062  -3665  -1275       C
ATOM    871  C   THR C 118     -52.231-110.829 -20.141  1.00180.34           C
ANISOU  871  C   THR C 118    20801  23231  24490  -1072  -3825  -1104       C
ATOM    872  O   THR C 118     -52.498-112.027 -20.001  1.00176.74           O
ANISOU  872  O   THR C 118    20282  22760  24113  -1086  -3905  -1074       O
ATOM    873  CB  THR C 118     -50.186-110.804 -18.771  1.00142.07           C
ANISOU  873  CB  THR C 118    15847  18420  19716   -976  -3606  -1304       C
ATOM    874  OG1 THR C 118     -49.302-109.800 -18.255  1.00141.03           O
ANISOU  874  OG1 THR C 118    15713  18318  19554   -922  -3472  -1381       O
ATOM    875  CG2 THR C 118     -49.453-112.122 -19.010  1.00125.53           C
ANISOU  875  CG2 THR C 118    13754  16272  17669  -1028  -3599  -1414       C
ATOM    876  N   VAL C 119     -53.155-109.891 -20.322  1.00173.84           N
ANISOU  876  N   VAL C 119    20003  22434  23612  -1061  -3870   -985       N
ATOM    877  CA  VAL C 119     -54.543-110.208 -20.597  1.00141.58           C
ANISOU  877  CA  VAL C 119    15903  18352  19540  -1084  -4019   -816       C
ATOM    878  C   VAL C 119     -54.738-110.292 -22.112  1.00143.41           C
ANISOU  878  C   VAL C 119    16307  18507  19676  -1211  -4070   -849       C
ATOM    879  O   VAL C 119     -54.858-111.390 -22.654  1.00145.78           O
ANISOU  879  O   VAL C 119    16637  18753  19998  -1279  -4149   -864       O
ATOM    880  CB  VAL C 119     -55.496-109.163 -19.974  1.00142.20           C
ANISOU  880  CB  VAL C 119    15914  18503  19610  -1001  -4044   -656       C
ATOM    881  CG1 VAL C 119     -56.945-109.614 -20.080  1.00128.51           C
ANISOU  881  CG1 VAL C 119    14137  16782  17908  -1013  -4202   -463       C
ATOM    882  CG2 VAL C 119     -55.123-108.918 -18.516  1.00146.32           C
ANISOU  882  CG2 VAL C 119    16285  19100  20211   -873  -3971   -650       C
ATOM    883  N   CYS C 120     -54.685-109.148 -22.798  1.00160.56           N
ANISOU  883  N   CYS C 120    18594  20672  21741  -1243  -4021   -873       N
ATOM    884  CA  CYS C 120     -55.074-109.066 -24.215  1.00189.18           C
ANISOU  884  CA  CYS C 120    22375  24235  25270  -1359  -4079   -874       C
ATOM    885  C   CYS C 120     -54.453-110.170 -25.100  1.00210.05           C
ANISOU  885  C   CYS C 120    25111  26797  27900  -1453  -4094  -1001       C
ATOM    886  O   CYS C 120     -55.193-110.887 -25.773  1.00214.23           O
ANISOU  886  O   CYS C 120    25685  27284  28428  -1524  -4214   -937       O
ATOM    887  CB  CYS C 120     -54.790-107.667 -24.803  1.00187.96           C
ANISOU  887  CB  CYS C 120    22330  24084  25004  -1379  -3996   -920       C
ATOM    888  SG  CYS C 120     -55.719-106.251 -24.107  1.00133.38           S
ANISOU  888  SG  CYS C 120    15350  17251  18076  -1291  -3998   -758       S
ATOM    889  N   GLY C 121     -53.125-110.308 -25.128  1.00216.99           N
ANISOU  889  N   GLY C 121    26024  27654  28769  -1455  -3977  -1176       N
ATOM    890  CA  GLY C 121     -52.195-109.335 -24.584  1.00193.62           C
ANISOU  890  CA  GLY C 121    23047  24733  25788  -1393  -3834  -1262       C
ATOM    891  C   GLY C 121     -51.994-108.180 -25.549  1.00191.78           C
ANISOU  891  C   GLY C 121    22954  24483  25429  -1447  -3781  -1308       C
ATOM    892  O   GLY C 121     -51.960-108.371 -26.767  1.00177.58           O
ANISOU  892  O   GLY C 121    21291  22627  23555  -1545  -3808  -1360       O
ATOM    893  N   MET C 122     -51.892-106.971 -25.010  1.00199.71           N
ANISOU  893  N   MET C 122    23929  25539  26411  -1382  -3709  -1286       N
ATOM    894  CA  MET C 122     -51.795-105.785 -25.852  1.00191.25           C
ANISOU  894  CA  MET C 122    22978  24460  25227  -1427  -3666  -1313       C
ATOM    895  C   MET C 122     -51.214-104.580 -25.123  1.00197.08           C
ANISOU  895  C   MET C 122    23681  25249  25952  -1347  -3556  -1342       C
ATOM    896  O   MET C 122     -51.078-104.574 -23.890  1.00128.63           O
ANISOU  896  O   MET C 122    14885  16627  17361  -1249  -3523  -1316       O
ATOM    897  CB  MET C 122     -53.150-105.428 -26.442  1.00159.32           C
ANISOU  897  CB  MET C 122    18974  20418  21144  -1470  -3779  -1163       C
ATOM    898  CG  MET C 122     -53.082-104.794 -27.809  1.00150.84           C
ANISOU  898  CG  MET C 122    18060  19304  19950  -1570  -3770  -1211       C
ATOM    899  SD  MET C 122     -54.745-104.831 -28.514  1.00298.74           S
ANISOU  899  SD  MET C 122    36827  38025  38656  -1635  -3927  -1027       S
ATOM    900  CE  MET C 122     -55.392-106.321 -27.738  1.00 88.98           C
ANISOU  900  CE  MET C 122    10135  11460  12215  -1600  -4038   -934       C
ATOM    901  N   TRP C 123     -50.861-103.563 -25.900  1.00223.02           N
ANISOU  901  N   TRP C 123    27078  28522  29138  -1391  -3501  -1396       N
ATOM    902  CA  TRP C 123     -50.351-102.326 -25.337  1.00222.29           C
ANISOU  902  CA  TRP C 123    26968  28470  29021  -1325  -3406  -1419       C
ATOM    903  C   TRP C 123     -51.316-101.743 -24.306  1.00202.28           C
ANISOU  903  C   TRP C 123    24324  26000  26535  -1229  -3448  -1267       C
ATOM    904  O   TRP C 123     -52.489-101.509 -24.596  1.00215.77           O
ANISOU  904  O   TRP C 123    26040  27718  28226  -1245  -3539  -1135       O
ATOM    905  CB  TRP C 123     -50.085-101.311 -26.454  1.00231.52           C
ANISOU  905  CB  TRP C 123    28277  29619  30073  -1397  -3369  -1471       C
ATOM    906  CG  TRP C 123     -48.742-101.491 -27.131  1.00236.33           C
ANISOU  906  CG  TRP C 123    28976  30187  30633  -1453  -3277  -1642       C
ATOM    907  CD1 TRP C 123     -48.451-101.310 -28.457  1.00213.84           C
ANISOU  907  CD1 TRP C 123    26265  27297  27688  -1551  -3269  -1712       C
ATOM    908  CD2 TRP C 123     -47.514-101.884 -26.505  1.00220.62           C
ANISOU  908  CD2 TRP C 123    26943  28197  28686  -1411  -3180  -1760       C
ATOM    909  NE1 TRP C 123     -47.120-101.564 -28.690  1.00187.88           N
ANISOU  909  NE1 TRP C 123    23022  23986  24380  -1568  -3172  -1863       N
ATOM    910  CE2 TRP C 123     -46.523-101.917 -27.504  1.00195.91           C
ANISOU  910  CE2 TRP C 123    23929  25025  25481  -1485  -3116  -1893       C
ATOM    911  CE3 TRP C 123     -47.156-102.211 -25.191  1.00202.50           C
ANISOU  911  CE3 TRP C 123    24520  25935  26487  -1317  -3139  -1761       C
ATOM    912  CZ2 TRP C 123     -45.207-102.264 -27.234  1.00186.04           C
ANISOU  912  CZ2 TRP C 123    22672  23765  24248  -1468  -3013  -2022       C
ATOM    913  CZ3 TRP C 123     -45.855-102.552 -24.927  1.00190.94           C
ANISOU  913  CZ3 TRP C 123    23049  24459  25041  -1305  -3038  -1891       C
ATOM    914  CH2 TRP C 123     -44.894-102.578 -25.941  1.00192.00           C
ANISOU  914  CH2 TRP C 123    23302  24552  25099  -1380  -2976  -2018       C
ATOM    915  N   LYS C 124     -50.809-101.520 -23.097  1.00179.40           N
ANISOU  915  N   LYS C 124    21323  23143  23697  -1127  -3380  -1285       N
ATOM    916  CA  LYS C 124     -51.574-100.866 -22.046  1.00170.78           C
ANISOU  916  CA  LYS C 124    20130  22116  22645  -1022  -3402  -1155       C
ATOM    917  C   LYS C 124     -51.568 -99.368 -22.323  1.00191.85           C
ANISOU  917  C   LYS C 124    22871  24797  25227  -1015  -3359  -1148       C
ATOM    918  O   LYS C 124     -50.555 -98.811 -22.745  1.00183.78           O
ANISOU  918  O   LYS C 124    21928  23752  24147  -1047  -3271  -1271       O
ATOM    919  CB  LYS C 124     -50.968-101.155 -20.669  1.00167.31           C
ANISOU  919  CB  LYS C 124    19559  21715  22297   -917  -3342  -1185       C
ATOM    920  CG  LYS C 124     -51.812-102.045 -19.762  1.00170.52           C
ANISOU  920  CG  LYS C 124    19823  22160  22807   -851  -3424  -1065       C
ATOM    921  CD  LYS C 124     -51.244-103.458 -19.654  1.00173.38           C
ANISOU  921  CD  LYS C 124    20139  22495  23243   -878  -3425  -1142       C
ATOM    922  CE  LYS C 124     -51.538-104.084 -18.289  1.00169.92           C
ANISOU  922  CE  LYS C 124    19527  22113  22922   -775  -3449  -1066       C
ATOM    923  NZ  LYS C 124     -50.952-105.452 -18.123  1.00139.94           N
ANISOU  923  NZ  LYS C 124    15676  18291  19203   -798  -3447  -1142       N
ATOM    924  N   GLY C 125     -52.708 -98.721 -22.112  1.00212.49           N
ANISOU  924  N   GLY C 125    25456  27447  27831   -975  -3422  -1001       N
ATOM    925  CA  GLY C 125     -52.836 -97.303 -22.387  1.00216.40           C
ANISOU  925  CA  GLY C 125    26019  27956  28248   -968  -3392   -980       C
ATOM    926  C   GLY C 125     -53.087 -97.070 -23.863  1.00211.76           C
ANISOU  926  C   GLY C 125    25567  27324  27569  -1092  -3426   -991       C
ATOM    927  O   GLY C 125     -53.529 -95.995 -24.268  1.00216.29           O
ANISOU  927  O   GLY C 125    26196  27907  28077  -1104  -3432   -939       O
ATOM    928  N   TYR C 126     -52.783 -98.081 -24.672  1.00211.85           N
ANISOU  928  N   TYR C 126    25633  27286  27576  -1185  -3447  -1063       N
ATOM    929  CA  TYR C 126     -53.064 -98.034 -26.102  1.00224.80           C
ANISOU  929  CA  TYR C 126    27399  28881  29133  -1307  -3489  -1072       C
ATOM    930  C   TYR C 126     -53.729 -99.320 -26.579  1.00234.75           C
ANISOU  930  C   TYR C 126    28659  30109  30425  -1371  -3591  -1022       C
ATOM    931  O   TYR C 126     -53.102-100.381 -26.603  1.00243.06           O
ANISOU  931  O   TYR C 126    29705  31131  31515  -1392  -3580  -1112       O
ATOM    932  CB  TYR C 126     -51.774 -97.812 -26.891  1.00210.50           C
ANISOU  932  CB  TYR C 126    25694  27032  27256  -1373  -3397  -1243       C
ATOM    933  CG  TYR C 126     -51.201 -96.417 -26.781  1.00199.85           C
ANISOU  933  CG  TYR C 126    24377  25703  25852  -1341  -3313  -1286       C
ATOM    934  CD1 TYR C 126     -50.460 -96.033 -25.668  1.00192.72           C
ANISOU  934  CD1 TYR C 126    23402  24831  24992  -1243  -3232  -1331       C
ATOM    935  CD2 TYR C 126     -51.388 -95.489 -27.799  1.00188.26           C
ANISOU  935  CD2 TYR C 126    23014  24225  24291  -1412  -3316  -1281       C
ATOM    936  CE1 TYR C 126     -49.927 -94.759 -25.569  1.00188.53           C
ANISOU  936  CE1 TYR C 126    22905  24316  24412  -1215  -3162  -1369       C
ATOM    937  CE2 TYR C 126     -50.860 -94.216 -27.710  1.00197.14           C
ANISOU  937  CE2 TYR C 126    24168  25368  25369  -1384  -3245  -1318       C
ATOM    938  CZ  TYR C 126     -50.130 -93.855 -26.594  1.00196.37           C
ANISOU  938  CZ  TYR C 126    24001  25297  25314  -1286  -3170  -1362       C
ATOM    939  OH  TYR C 126     -49.601 -92.586 -26.504  1.00180.73           O
ANISOU  939  OH  TYR C 126    22052  23330  23287  -1260  -3106  -1397       O
ATOM    940  N   GLY C 127     -54.986 -99.212 -26.995  1.00212.99           N
ANISOU  940  N   GLY C 127    25917  27359  27651  -1404  -3691   -878       N
ATOM    941  CA  GLY C 127     -55.723-100.360 -27.487  1.00191.38           C
ANISOU  941  CA  GLY C 127    23186  24589  24940  -1469  -3800   -814       C
ATOM    942  C   GLY C 127     -55.860-101.521 -26.513  1.00176.68           C
ANISOU  942  C   GLY C 127    21200  22742  23190  -1405  -3842   -777       C
ATOM    943  O   GLY C 127     -55.849-102.680 -26.920  1.00189.68           O
ANISOU  943  O   GLY C 127    22863  24346  24863  -1463  -3897   -804       O
ATOM    944  N   CYS C 128     -55.971-101.228 -25.225  1.00145.68           N
ANISOU  944  N   CYS C 128    17148  18875  19329  -1285  -3818   -717       N
ATOM    945  CA  CYS C 128     -56.346-102.255 -24.262  1.00132.68           C
ANISOU  945  CA  CYS C 128    15368  17254  17791  -1219  -3875   -645       C
ATOM    946  C   CYS C 128     -57.329-101.733 -23.212  1.00195.39           C
ANISOU  946  C   CYS C 128    23192  25270  25779  -1108  -3914   -474       C
ATOM    947  O   CYS C 128     -57.067-100.747 -22.520  1.00205.93           O
ANISOU  947  O   CYS C 128    24493  26647  27104  -1023  -3840   -479       O
ATOM    948  CB  CYS C 128     -55.124-102.879 -23.594  1.00111.84           C
ANISOU  948  CB  CYS C 128    12674  14610  15211  -1177  -3789   -787       C
ATOM    949  SG  CYS C 128     -55.370-103.325 -21.837  1.00184.66           S
ANISOU  949  SG  CYS C 128    21693  23905  24564  -1030  -3798   -699       S
ATOM    950  N   SER C 129     -58.461-102.418 -23.104  1.00210.88           N
ANISOU  950  N   SER C 129    25092  27244  27789  -1108  -4034   -319       N
ATOM    951  CA  SER C 129     -59.462-102.130 -22.090  1.00200.79           C
ANISOU  951  CA  SER C 129    23689  26038  26562  -1000  -4085   -141       C
ATOM    952  C   SER C 129     -59.596-103.376 -21.220  1.00200.27           C
ANISOU  952  C   SER C 129    23488  25994  26612   -946  -4140    -98       C
ATOM    953  O   SER C 129     -59.862-104.464 -21.731  1.00183.29           O
ANISOU  953  O   SER C 129    21350  23803  24490  -1020  -4225    -83       O
ATOM    954  CB  SER C 129     -60.796-101.798 -22.755  1.00188.53           C
ANISOU  954  CB  SER C 129    22179  24488  24965  -1048  -4188     29       C
ATOM    955  OG  SER C 129     -60.593-100.943 -23.867  1.00178.52           O
ANISOU  955  OG  SER C 129    21057  23181  23590  -1136  -4150    -34       O
ATOM    956  N   CYS C 130     -59.400-103.222 -19.913  1.00214.86           N
ANISOU  956  N   CYS C 130    25205  27905  28526   -819  -4093    -79       N
ATOM    957  CA  CYS C 130     -59.357-104.359 -18.988  1.00228.13           C
ANISOU  957  CA  CYS C 130    26746  29613  30321   -760  -4128    -57       C
ATOM    958  C   CYS C 130     -59.606-103.919 -17.541  1.00230.66           C
ANISOU  958  C   CYS C 130    26918  30022  30702   -606  -4101     33       C
ATOM    959  O   CYS C 130     -60.015-102.781 -17.290  1.00217.33           O
ANISOU  959  O   CYS C 130    25236  28374  28966   -545  -4076    103       O
ATOM    960  CB  CYS C 130     -58.007-105.091 -19.076  1.00239.07           C
ANISOU  960  CB  CYS C 130    28154  30950  31733   -801  -4050   -255       C
ATOM    961  SG  CYS C 130     -57.729-106.144 -20.541  1.00226.12           S
ANISOU  961  SG  CYS C 130    26647  29210  30059   -964  -4104   -352       S
ATOM    962  N   ASP C 131     -59.381-104.839 -16.602  1.00234.45           N
ANISOU  962  N   ASP C 131    27262  30532  31286   -544  -4110     32       N
ATOM    963  CA  ASP C 131     -59.472-104.547 -15.171  1.00205.61           C
ANISOU  963  CA  ASP C 131    23460  26964  27698   -395  -4078     98       C
ATOM    964  C   ASP C 131     -58.084-104.400 -14.554  1.00172.93           C
ANISOU  964  C   ASP C 131    19303  22824  23578   -354  -3944    -80       C
ATOM    965  O   ASP C 131     -57.582-103.291 -14.369  1.00172.01           O
ANISOU  965  O   ASP C 131    19233  22718  23405   -313  -3849   -143       O
ATOM    966  CB  ASP C 131     -60.235-105.658 -14.442  1.00211.70           C
ANISOU  966  CB  ASP C 131    24074  27782  28580   -344  -4184    237       C
ATOM    967  CG  ASP C 131     -61.602-105.926 -15.049  1.00221.18           C
ANISOU  967  CG  ASP C 131    25300  28981  29757   -388  -4302    418       C
ATOM    968  OD1 ASP C 131     -62.228-104.973 -15.564  1.00234.56           O
ANISOU  968  OD1 ASP C 131    27064  30678  31381   -404  -4338    497       O
ATOM    969  OD2 ASP C 131     -62.051-107.093 -15.013  1.00196.78           O
ANISOU  969  OD2 ASP C 131    22190  25885  26695   -402  -4309    475       O
TER     970      ASP C 131
ATOM    971  N   ALA D   1     -29.498 -94.644 -49.892  1.00197.90           N
ANISOU  971  N   ALA D   1    26173  25361  23661  -2459  -2004  -3452       N
ATOM    972  CA  ALA D   1     -28.951 -95.425 -48.784  1.00186.00           C
ANISOU  972  CA  ALA D   1    24610  23826  22235  -2390  -1949  -3483       C
ATOM    973  C   ALA D   1     -27.549 -94.945 -48.415  1.00212.22           C
ANISOU  973  C   ALA D   1    27895  27188  25551  -2337  -1843  -3503       C
ATOM    974  O   ALA D   1     -26.614 -95.744 -48.330  1.00215.08           O
ANISOU  974  O   ALA D   1    28272  27541  25906  -2298  -1768  -3567       O
ATOM    975  CB  ALA D   1     -28.932 -96.915 -49.131  1.00147.46           C
ANISOU  975  CB  ALA D   1    19794  18894  17339  -2389  -1950  -3557       C
ATOM    976  N   GLU D   2     -27.413 -93.642 -48.182  1.00230.00           N
ANISOU  976  N   GLU D   2    30099  29485  27808  -2337  -1839  -3445       N
ATOM    977  CA  GLU D   2     -26.111 -93.038 -47.904  1.00237.29           C
ANISOU  977  CA  GLU D   2    30989  30451  28721  -2295  -1748  -3451       C
ATOM    978  C   GLU D   2     -26.216 -91.901 -46.882  1.00230.17           C
ANISOU  978  C   GLU D   2    29996  29568  27890  -2269  -1757  -3377       C
ATOM    979  O   GLU D   2     -27.283 -91.313 -46.703  1.00224.65           O
ANISOU  979  O   GLU D   2    29272  28864  27220  -2295  -1835  -3317       O
ATOM    980  CB  GLU D   2     -25.509 -92.497 -49.202  1.00233.66           C
ANISOU  980  CB  GLU D   2    30597  30039  28143  -2331  -1725  -3467       C
ATOM    981  CG  GLU D   2     -26.145 -91.187 -49.653  1.00226.24           C
ANISOU  981  CG  GLU D   2    29650  29135  27176  -2382  -1789  -3399       C
ATOM    982  CD  GLU D   2     -26.137 -91.016 -51.156  1.00208.59           C
ANISOU  982  CD  GLU D   2    27499  26932  24825  -2440  -1805  -3419       C
ATOM    983  OE1 GLU D   2     -26.516 -89.925 -51.631  1.00201.94           O
ANISOU  983  OE1 GLU D   2    26650  26126  23950  -2484  -1849  -3366       O
ATOM    984  OE2 GLU D   2     -25.761 -91.976 -51.862  1.00199.40           O
ANISOU  984  OE2 GLU D   2    26406  25756  23600  -2442  -1775  -3487       O
ATOM    985  N   ASN D   3     -25.116 -91.629 -46.186  1.00227.54           N
ANISOU  985  N   ASN D   3    29614  29254  27585  -2217  -1678  -3380       N
ATOM    986  CA  ASN D   3     -23.957 -92.511 -46.216  1.00230.53           C
ANISOU  986  CA  ASN D   3    30014  29630  27946  -2180  -1586  -3447       C
ATOM    987  C   ASN D   3     -23.687 -93.101 -44.841  1.00225.84           C
ANISOU  987  C   ASN D   3    29345  29006  27458  -2119  -1545  -3453       C
ATOM    988  O   ASN D   3     -23.275 -92.404 -43.914  1.00239.90           O
ANISOU  988  O   ASN D   3    31055  30801  29294  -2083  -1517  -3413       O
ATOM    989  CB  ASN D   3     -22.702 -91.837 -46.794  1.00221.87           C
ANISOU  989  CB  ASN D   3    28938  28589  26775  -2175  -1515  -3451       C
ATOM    990  CG  ASN D   3     -22.824 -90.333 -46.881  1.00197.34           C
ANISOU  990  CG  ASN D   3    25802  25524  23654  -2198  -1552  -3380       C
ATOM    991  OD1 ASN D   3     -23.156 -89.659 -45.897  1.00167.54           O
ANISOU  991  OD1 ASN D   3    21957  21744  19955  -2178  -1577  -3326       O
ATOM    992  ND2 ASN D   3     -22.556 -89.793 -48.074  1.00177.99           N
ANISOU  992  ND2 ASN D   3    23405  23117  21104  -2239  -1555  -3378       N
ATOM    993  N   VAL D   4     -23.903 -94.400 -44.738  1.00203.89           N
ANISOU  993  N   VAL D   4    26583  26183  24704  -2108  -1542  -3505       N
ATOM    994  CA  VAL D   4     -23.785 -95.132 -43.492  1.00200.21           C
ANISOU  994  CA  VAL D   4    26045  25684  24340  -2056  -1511  -3514       C
ATOM    995  C   VAL D   4     -22.463 -94.902 -42.758  1.00191.43           C
ANISOU  995  C   VAL D   4    24882  24596  23258  -2003  -1410  -3517       C
ATOM    996  O   VAL D   4     -21.403 -94.794 -43.380  1.00187.03           O
ANISOU  996  O   VAL D   4    24366  24069  22630  -2001  -1341  -3543       O
ATOM    997  CB  VAL D   4     -23.919 -96.626 -43.770  1.00203.26           C
ANISOU  997  CB  VAL D   4    26476  26027  24727  -2056  -1508  -3583       C
ATOM    998  CG1 VAL D   4     -25.335 -96.946 -44.218  1.00206.79           C
ANISOU  998  CG1 VAL D   4    26958  26441  25171  -2103  -1618  -3568       C
ATOM    999  CG2 VAL D   4     -22.900 -97.046 -44.830  1.00163.51           C
ANISOU  999  CG2 VAL D   4    21527  21009  19592  -2062  -1438  -3648       C
ATOM   1000  N   THR D   5     -22.544 -94.807 -41.432  1.00164.54           N
ANISOU 1000  N   THR D   5    21384  21177  19954  -1961  -1403  -3485       N
ATOM   1001  CA  THR D   5     -21.362 -94.782 -40.569  1.00154.97           C
ANISOU 1001  CA  THR D   5    20117  19979  18788  -1910  -1309  -3488       C
ATOM   1002  C   THR D   5     -20.779 -96.180 -40.367  1.00136.32           C
ANISOU 1002  C   THR D   5    17756  17588  16450  -1882  -1242  -3554       C
ATOM   1003  O   THR D   5     -21.490 -97.175 -40.494  1.00149.73           O
ANISOU 1003  O   THR D   5    19473  19249  18168  -1892  -1282  -3588       O
ATOM   1004  CB  THR D   5     -21.689 -94.187 -39.185  1.00179.56           C
ANISOU 1004  CB  THR D   5    23132  23089  22004  -1872  -1329  -3430       C
ATOM   1005  OG1 THR D   5     -20.923 -94.861 -38.181  1.00179.72           O
ANISOU 1005  OG1 THR D   5    23091  23097  22099  -1822  -1252  -3451       O
ATOM   1006  CG2 THR D   5     -23.166 -94.354 -38.863  1.00182.02           C
ANISOU 1006  CG2 THR D   5    23419  23372  22369  -1882  -1428  -3401       C
ATOM   1007  N   GLY D   6     -19.488 -96.255 -40.051  1.00136.94           N
ANISOU 1007  N   GLY D   6    17816  17685  16531  -1848  -1141  -3569       N
ATOM   1008  CA  GLY D   6     -18.838 -97.538 -39.825  1.00157.18           C
ANISOU 1008  CA  GLY D   6    20377  20224  19119  -1820  -1067  -3629       C
ATOM   1009  C   GLY D   6     -19.078 -98.026 -38.410  1.00138.41           C
ANISOU 1009  C   GLY D   6    17901  17819  16869  -1780  -1062  -3618       C
ATOM   1010  O   GLY D   6     -18.487 -99.021 -37.971  1.00108.36           O
ANISOU 1010  O   GLY D   6    14071  13995  13105  -1751   -996  -3658       O
ATOM   1011  N   LEU D   7     -19.980 -97.329 -37.718  1.00121.44           N
ANISOU 1011  N   LEU D   7    15695  15669  14779  -1778  -1135  -3561       N
ATOM   1012  CA  LEU D   7     -20.175 -97.484 -36.281  1.00122.89           C
ANISOU 1012  CA  LEU D   7    15773  15838  15082  -1735  -1132  -3534       C
ATOM   1013  C   LEU D   7     -20.376 -98.926 -35.886  1.00113.52           C
ANISOU 1013  C   LEU D   7    14560  14614  13960  -1718  -1122  -3581       C
ATOM   1014  O   LEU D   7     -19.508 -99.531 -35.272  1.00172.75           O
ANISOU 1014  O   LEU D   7    22019  22111  21508  -1686  -1038  -3607       O
ATOM   1015  CB  LEU D   7     -21.370 -96.658 -35.802  1.00138.59           C
ANISOU 1015  CB  LEU D   7    17720  17827  17113  -1738  -1230  -3469       C
ATOM   1016  CG  LEU D   7     -21.530 -96.370 -34.297  1.00133.63           C
ANISOU 1016  CG  LEU D   7    16982  17197  16595  -1689  -1230  -3423       C
ATOM   1017  CD1 LEU D   7     -21.363 -97.626 -33.445  1.00112.98           C
ANISOU 1017  CD1 LEU D   7    14301  14556  14070  -1653  -1189  -3457       C
ATOM   1018  CD2 LEU D   7     -20.591 -95.252 -33.815  1.00 91.64           C
ANISOU 1018  CD2 LEU D   7    11637  11909  11274  -1667  -1176  -3386       C
ATOM   1019  N   PHE D   8     -21.523 -99.480 -36.224  1.00 90.54           N
ANISOU 1019  N   PHE D   8    11671  11674  11055  -1742  -1209  -3589       N
ATOM   1020  CA  PHE D   8     -21.794-100.853 -35.832  1.00110.10           C
ANISOU 1020  CA  PHE D   8    14120  14114  13599  -1727  -1212  -3630       C
ATOM   1021  C   PHE D   8     -21.490-101.946 -36.876  1.00114.41           C
ANISOU 1021  C   PHE D   8    14757  14635  14079  -1750  -1190  -3706       C
ATOM   1022  O   PHE D   8     -21.823-103.116 -36.660  1.00 98.04           O
ANISOU 1022  O   PHE D   8    12669  12525  12056  -1743  -1208  -3741       O
ATOM   1023  CB  PHE D   8     -23.201-100.996 -35.278  1.00 98.12           C
ANISOU 1023  CB  PHE D   8    12550  12576  12156  -1727  -1318  -3586       C
ATOM   1024  CG  PHE D   8     -23.376-100.407 -33.902  1.00123.34           C
ANISOU 1024  CG  PHE D   8    15630  15786  15447  -1682  -1320  -3525       C
ATOM   1025  CD1 PHE D   8     -22.809-101.009 -32.792  1.00 94.09           C
ANISOU 1025  CD1 PHE D   8    11836  12077  11836  -1636  -1256  -3537       C
ATOM   1026  CD2 PHE D   8     -24.142 -99.263 -33.716  1.00149.92           C
ANISOU 1026  CD2 PHE D   8    18979  19171  18812  -1685  -1387  -3456       C
ATOM   1027  CE1 PHE D   8     -22.992-100.470 -31.534  1.00124.86           C
ANISOU 1027  CE1 PHE D   8    15632  15990  15820  -1594  -1261  -3482       C
ATOM   1028  CE2 PHE D   8     -24.330 -98.721 -32.455  1.00 91.37           C
ANISOU 1028  CE2 PHE D   8    11464  11769  11482  -1639  -1392  -3401       C
ATOM   1029  CZ  PHE D   8     -23.754 -99.326 -31.370  1.00121.09           C
ANISOU 1029  CZ  PHE D   8    15143  15530  15336  -1593  -1329  -3415       C
ATOM   1030  N   LYS D   9     -20.838-101.590 -37.980  1.00 90.46           N
ANISOU 1030  N   LYS D   9    11815  11621  10933  -1774  -1153  -3732       N
ATOM   1031  CA  LYS D   9     -20.899-102.427 -39.182  1.00135.58           C
ANISOU 1031  CA  LYS D   9    17636  17313  16566  -1804  -1166  -3796       C
ATOM   1032  C   LYS D   9     -20.692-103.909 -38.879  1.00123.90           C
ANISOU 1032  C   LYS D   9    16145  15792  15138  -1781  -1135  -3856       C
ATOM   1033  O   LYS D   9     -19.871-104.276 -38.048  1.00120.52           O
ANISOU 1033  O   LYS D   9    15652  15367  14772  -1741  -1051  -3867       O
ATOM   1034  CB  LYS D   9     -19.930-101.931 -40.282  1.00120.01           C
ANISOU 1034  CB  LYS D   9    15752  15376  14471  -1817  -1102  -3820       C
ATOM   1035  CG  LYS D   9     -18.479-102.339 -40.129  1.00128.81           C
ANISOU 1035  CG  LYS D   9    16862  16505  15575  -1780   -975  -3856       C
ATOM   1036  CD  LYS D   9     -17.643-101.883 -41.319  1.00143.03           C
ANISOU 1036  CD  LYS D   9    18754  18343  17247  -1793   -924  -3873       C
ATOM   1037  CE  LYS D   9     -16.142-101.967 -41.075  1.00141.99           C
ANISOU 1037  CE  LYS D   9    18605  18239  17104  -1753   -795  -3882       C
ATOM   1038  NZ  LYS D   9     -15.642-103.377 -41.057  1.00125.86           N
ANISOU 1038  NZ  LYS D   9    16582  16163  15075  -1726   -733  -3951       N
ATOM   1039  N   ASP D  10     -21.489-104.744 -39.540  1.00100.87           N
ANISOU 1039  N   ASP D  10    13291  12835  12199  -1810  -1208  -3892       N
ATOM   1040  CA  ASP D  10     -21.475-106.175 -39.305  1.00114.26           C
ANISOU 1040  CA  ASP D  10    14983  14486  13947  -1794  -1201  -3947       C
ATOM   1041  C   ASP D  10     -20.256-106.790 -39.998  1.00124.86           C
ANISOU 1041  C   ASP D  10    16400  15828  15213  -1779  -1099  -4021       C
ATOM   1042  O   ASP D  10     -20.126-106.767 -41.226  1.00124.41           O
ANISOU 1042  O   ASP D  10    16455  15773  15042  -1805  -1103  -4056       O
ATOM   1043  CB  ASP D  10     -22.788-106.772 -39.822  1.00111.48           C
ANISOU 1043  CB  ASP D  10    14678  14089  13591  -1833  -1326  -3951       C
ATOM   1044  CG  ASP D  10     -22.792-108.293 -39.835  1.00125.42           C
ANISOU 1044  CG  ASP D  10    16463  15801  15390  -1824  -1331  -4015       C
ATOM   1045  OD1 ASP D  10     -21.730-108.904 -40.095  1.00 96.39           O
ANISOU 1045  OD1 ASP D  10    12824  12121  11680  -1801  -1237  -4079       O
ATOM   1046  OD2 ASP D  10     -23.875-108.877 -39.590  1.00102.71           O
ANISOU 1046  OD2 ASP D  10    13564  12887  12574  -1840  -1431  -3998       O
ATOM   1047  N   CYS D  11     -19.372-107.354 -39.182  1.00 98.42           N
ANISOU 1047  N   CYS D  11    12986  12478  11930  -1736  -1006  -4041       N
ATOM   1048  CA  CYS D  11     -18.057-107.798 -39.627  1.00107.81           C
ANISOU 1048  CA  CYS D  11    14227  13679  13059  -1712   -890  -4096       C
ATOM   1049  C   CYS D  11     -18.000-109.286 -39.923  1.00116.86           C
ANISOU 1049  C   CYS D  11    15420  14774  14209  -1704   -884  -4172       C
ATOM   1050  O   CYS D  11     -16.937-109.829 -40.246  1.00117.82           O
ANISOU 1050  O   CYS D  11    15582  14898  14286  -1678   -786  -4222       O
ATOM   1051  CB  CYS D  11     -17.010-107.422 -38.583  1.00 90.96           C
ANISOU 1051  CB  CYS D  11    11995  11579  10988  -1672   -783  -4064       C
ATOM   1052  SG  CYS D  11     -16.979-105.657 -38.263  1.00132.06           S
ANISOU 1052  SG  CYS D  11    17154  16839  16182  -1680   -790  -3977       S
ATOM   1053  N   SER D  12     -19.150-109.940 -39.793  1.00 95.92           N
ANISOU 1053  N   SER D  12    12759  12075  11611  -1724   -991  -4177       N
ATOM   1054  CA  SER D  12     -19.246-111.366 -40.043  1.00127.35           C
ANISOU 1054  CA  SER D  12    16783  16000  15603  -1719  -1006  -4246       C
ATOM   1055  C   SER D  12     -18.993-111.551 -41.513  1.00114.74           C
ANISOU 1055  C   SER D  12    15338  14395  13864  -1738  -1002  -4305       C
ATOM   1056  O   SER D  12     -19.094-110.587 -42.280  1.00114.06           O
ANISOU 1056  O   SER D  12    15310  14341  13686  -1763  -1021  -4281       O
ATOM   1057  CB  SER D  12     -20.653-111.868 -39.732  1.00140.77           C
ANISOU 1057  CB  SER D  12    18452  17655  17379  -1745  -1141  -4225       C
ATOM   1058  OG  SER D  12     -21.440-111.885 -40.911  1.00 93.25           O
ANISOU 1058  OG  SER D  12    12551  11612  11269  -1790  -1235  -4242       O
ATOM   1059  N   LYS D  13     -18.649-112.770 -41.914  1.00107.51           N
ANISOU 1059  N   LYS D  13    14485  13437  12928  -1723   -978  -4380       N
ATOM   1060  CA  LYS D  13     -18.722-113.086 -43.324  1.00124.37           C
ANISOU 1060  CA  LYS D  13    16770  15550  14933  -1744  -1007  -4438       C
ATOM   1061  C   LYS D  13     -19.991-113.913 -43.514  1.00138.40           C
ANISOU 1061  C   LYS D  13    18581  17261  16743  -1779  -1144  -4454       C
ATOM   1062  O   LYS D  13     -20.006-115.125 -43.297  1.00150.74           O
ANISOU 1062  O   LYS D  13    20147  18773  18355  -1763  -1153  -4503       O
ATOM   1063  CB  LYS D  13     -17.503-113.911 -43.718  1.00130.58           C
ANISOU 1063  CB  LYS D  13    17618  16331  15665  -1701   -893  -4512       C
ATOM   1064  CG  LYS D  13     -16.196-113.444 -43.082  1.00131.23           C
ANISOU 1064  CG  LYS D  13    17628  16468  15767  -1658   -750  -4489       C
ATOM   1065  CD  LYS D  13     -15.323-114.632 -42.709  1.00121.94           C
ANISOU 1065  CD  LYS D  13    16438  15264  14628  -1612   -657  -4545       C
ATOM   1066  CE  LYS D  13     -13.940-114.534 -43.332  1.00112.42           C
ANISOU 1066  CE  LYS D  13    15297  14099  13319  -1575   -524  -4572       C
ATOM   1067  NZ  LYS D  13     -13.239-115.852 -43.273  1.00112.54           N
ANISOU 1067  NZ  LYS D  13    15336  14077  13348  -1534   -450  -4641       N
ATOM   1068  N   ILE D  14     -21.054-113.248 -43.951  1.00138.02           N
ANISOU 1068  N   ILE D  14    18561  17215  16666  -1827  -1253  -4410       N
ATOM   1069  CA  ILE D  14     -22.294-113.915 -44.312  1.00135.96           C
ANISOU 1069  CA  ILE D  14    18348  16893  16417  -1868  -1391  -4416       C
ATOM   1070  C   ILE D  14     -22.874-113.177 -45.487  1.00150.18           C
ANISOU 1070  C   ILE D  14    20253  18706  18103  -1919  -1459  -4402       C
ATOM   1071  O   ILE D  14     -23.130-111.972 -45.397  1.00166.74           O
ANISOU 1071  O   ILE D  14    22310  20850  20191  -1938  -1470  -4336       O
ATOM   1072  CB  ILE D  14     -23.345-113.844 -43.209  1.00138.01           C
ANISOU 1072  CB  ILE D  14    18485  17143  16811  -1880  -1480  -4342       C
ATOM   1073  CG1 ILE D  14     -22.926-114.670 -42.000  1.00121.64           C
ANISOU 1073  CG1 ILE D  14    16299  15054  14864  -1835  -1429  -4352       C
ATOM   1074  CG2 ILE D  14     -24.674-114.344 -43.742  1.00159.59           C
ANISOU 1074  CG2 ILE D  14    21279  19820  19539  -1931  -1632  -4332       C
ATOM   1075  CD1 ILE D  14     -24.071-114.964 -41.061  1.00 84.93           C
ANISOU 1075  CD1 ILE D  14    11546  10381  10343  -1846  -1537  -4291       C
ATOM   1076  N   ILE D  15     -23.136-113.900 -46.566  1.00128.97           N
ANISOU 1076  N   ILE D  15    17698  15973  15332  -1942  -1511  -4463       N
ATOM   1077  CA  ILE D  15     -23.568-113.274 -47.802  1.00115.94           C
ANISOU 1077  CA  ILE D  15    16158  14334  13559  -1990  -1566  -4460       C
ATOM   1078  C   ILE D  15     -25.013-112.843 -47.680  1.00118.86           C
ANISOU 1078  C   ILE D  15    16499  14690  13974  -2047  -1704  -4384       C
ATOM   1079  O   ILE D  15     -25.459-111.914 -48.342  1.00135.60           O
ANISOU 1079  O   ILE D  15    18659  16839  16025  -2089  -1745  -4346       O
ATOM   1080  CB  ILE D  15     -23.386-114.224 -48.983  1.00124.34           C
ANISOU 1080  CB  ILE D  15    17376  15352  14517  -1994  -1579  -4550       C
ATOM   1081  CG1 ILE D  15     -23.672-115.674 -48.563  1.00133.66           C
ANISOU 1081  CG1 ILE D  15    18556  16454  15774  -1981  -1626  -4595       C
ATOM   1082  CG2 ILE D  15     -21.966-114.111 -49.519  1.00106.56           C
ANISOU 1082  CG2 ILE D  15    15179  13142  12168  -1947  -1439  -4607       C
ATOM   1083  CD1 ILE D  15     -22.550-116.354 -47.765  1.00126.96           C
ANISOU 1083  CD1 ILE D  15    17644  15607  14988  -1914  -1506  -4638       C
ATOM   1084  N   THR D  16     -25.722-113.523 -46.791  1.00123.63           N
ANISOU 1084  N   THR D  16    17026  15252  14697  -2046  -1773  -4357       N
ATOM   1085  CA  THR D  16     -27.149-113.325 -46.557  1.00 95.48           C
ANISOU 1085  CA  THR D  16    13424  11664  11188  -2094  -1911  -4279       C
ATOM   1086  C   THR D  16     -27.452-112.316 -45.434  1.00117.87           C
ANISOU 1086  C   THR D  16    16116  14552  14119  -2083  -1905  -4184       C
ATOM   1087  O   THR D  16     -26.611-111.493 -45.064  1.00125.90           O
ANISOU 1087  O   THR D  16    17079  15626  15132  -2051  -1802  -4174       O
ATOM   1088  CB  THR D  16     -27.812-114.667 -46.208  1.00144.13           C
ANISOU 1088  CB  THR D  16    19579  17752  17430  -2098  -2000  -4294       C
ATOM   1089  OG1 THR D  16     -27.799-114.852 -44.788  1.00165.08           O
ANISOU 1089  OG1 THR D  16    22081  20414  20226  -2058  -1980  -4253       O
ATOM   1090  CG2 THR D  16     -27.059-115.811 -46.854  1.00 84.80           C
ANISOU 1090  CG2 THR D  16    12170  10192   9857  -2076  -1957  -4402       C
ATOM   1091  N   GLY D  17     -28.696-112.352 -44.963  1.00133.87           N
ANISOU 1091  N   GLY D  17    18086  16556  16223  -2111  -2023  -4111       N
ATOM   1092  CA  GLY D  17     -29.111-111.732 -43.715  1.00 87.21           C
ANISOU 1092  CA  GLY D  17    12030  10680  10426  -2090  -2032  -4023       C
ATOM   1093  C   GLY D  17     -29.388-110.258 -43.891  1.00131.72           C
ANISOU 1093  C   GLY D  17    17655  16373  16021  -2113  -2035  -3955       C
ATOM   1094  O   GLY D  17     -28.753-109.612 -44.726  1.00153.32           O
ANISOU 1094  O   GLY D  17    20464  19139  18650  -2124  -1976  -3987       O
ATOM   1095  N   LEU D  18     -30.293-109.702 -43.088  1.00125.49           N
ANISOU 1095  N   LEU D  18    16768  15601  15313  -2115  -2100  -3860       N
ATOM   1096  CA  LEU D  18     -31.000-110.427 -42.040  1.00117.15           C
ANISOU 1096  CA  LEU D  18    15611  14516  14385  -2095  -2165  -3816       C
ATOM   1097  C   LEU D  18     -32.504-110.248 -42.200  1.00124.03           C
ANISOU 1097  C   LEU D  18    16484  15370  15272  -2144  -2309  -3726       C
ATOM   1098  O   LEU D  18     -32.961-109.259 -42.773  1.00131.36           O
ANISOU 1098  O   LEU D  18    17451  16324  16135  -2183  -2340  -3681       O
ATOM   1099  CB  LEU D  18     -30.578-109.890 -40.663  1.00107.74           C
ANISOU 1099  CB  LEU D  18    14273  13371  13292  -2035  -2093  -3774       C
ATOM   1100  CG  LEU D  18     -29.455-110.602 -39.903  1.00122.76           C
ANISOU 1100  CG  LEU D  18    16116  15272  15255  -1977  -1986  -3836       C
ATOM   1101  CD1 LEU D  18     -28.868-109.727 -38.813  1.00104.45           C
ANISOU 1101  CD1 LEU D  18    13680  13009  12996  -1927  -1899  -3798       C
ATOM   1102  CD2 LEU D  18     -29.954-111.913 -39.323  1.00151.57           C
ANISOU 1102  CD2 LEU D  18    19714  18873  19004  -1966  -2050  -3839       C
ATOM   1103  N   HIS D  19     -33.265-111.205 -41.678  1.00121.77           N
ANISOU 1103  N   HIS D  19    16151  15042  15075  -2142  -2396  -3697       N
ATOM   1104  CA  HIS D  19     -34.721-111.109 -41.617  1.00135.39           C
ANISOU 1104  CA  HIS D  19    17853  16752  16835  -2181  -2535  -3596       C
ATOM   1105  C   HIS D  19     -35.088-109.801 -40.932  1.00136.59           C
ANISOU 1105  C   HIS D  19    17913  16966  17021  -2163  -2525  -3502       C
ATOM   1106  O   HIS D  19     -34.379-109.349 -40.040  1.00151.29           O
ANISOU 1106  O   HIS D  19    19683  18868  18931  -2107  -2433  -3504       O
ATOM   1107  CB  HIS D  19     -35.268-112.288 -40.815  1.00142.73           C
ANISOU 1107  CB  HIS D  19    18707  17642  17882  -2161  -2607  -3571       C
ATOM   1108  CG  HIS D  19     -36.723-112.579 -41.068  1.00126.49           C
ANISOU 1108  CG  HIS D  19    16666  15551  15844  -2211  -2765  -3483       C
ATOM   1109  ND1 HIS D  19     -37.626-112.748 -40.031  1.00137.83           N
ANISOU 1109  ND1 HIS D  19    17979  16994  17397  -2189  -2842  -3382       N
ATOM   1110  CD2 HIS D  19     -37.402-112.767 -42.202  1.00141.18           C
ANISOU 1110  CD2 HIS D  19    18648  17371  17625  -2281  -2858  -3479       C
ATOM   1111  CE1 HIS D  19     -38.812-113.012 -40.544  1.00139.63           C
ANISOU 1111  CE1 HIS D  19    18253  17186  17614  -2245  -2979  -3314       C
ATOM   1112  NE2 HIS D  19     -38.720-113.032 -41.853  1.00157.95           N
ANISOU 1112  NE2 HIS D  19    20722  19476  19818  -2304  -2993  -3370       N
ATOM   1113  N   PRO D  20     -36.185-109.173 -41.365  1.00111.26           N
ANISOU 1113  N   PRO D  20    14731  13762  13782  -2211  -2621  -3418       N
ATOM   1114  CA  PRO D  20     -36.653-107.898 -40.812  1.00126.74           C
ANISOU 1114  CA  PRO D  20    16613  15776  15765  -2198  -2623  -3324       C
ATOM   1115  C   PRO D  20     -36.886-107.939 -39.312  1.00146.96           C
ANISOU 1115  C   PRO D  20    19020  18361  18457  -2132  -2622  -3259       C
ATOM   1116  O   PRO D  20     -36.687-106.922 -38.645  1.00156.10           O
ANISOU 1116  O   PRO D  20    20105  19569  19636  -2094  -2570  -3220       O
ATOM   1117  CB  PRO D  20     -37.963-107.670 -41.552  1.00146.72           C
ANISOU 1117  CB  PRO D  20    19202  18290  18255  -2267  -2750  -3244       C
ATOM   1118  CG  PRO D  20     -37.694-108.258 -42.882  1.00148.19           C
ANISOU 1118  CG  PRO D  20    19534  18432  18339  -2324  -2762  -3327       C
ATOM   1119  CD  PRO D  20     -36.881-109.503 -42.615  1.00106.30           C
ANISOU 1119  CD  PRO D  20    14229  13090  13070  -2287  -2715  -3421       C
ATOM   1120  N   THR D  21     -37.323-109.081 -38.792  1.00148.42           N
ANISOU 1120  N   THR D  21    19157  18510  18728  -2118  -2684  -3246       N
ATOM   1121  CA  THR D  21     -37.249-109.319 -37.358  1.00162.88           C
ANISOU 1121  CA  THR D  21    20840  20363  20684  -2047  -2660  -3211       C
ATOM   1122  C   THR D  21     -35.902-109.951 -37.128  1.00163.34           C
ANISOU 1122  C   THR D  21    20893  20414  20754  -2010  -2545  -3322       C
ATOM   1123  O   THR D  21     -35.482-110.789 -37.922  1.00205.48           O
ANISOU 1123  O   THR D  21    26324  25706  26041  -2039  -2540  -3406       O
ATOM   1124  CB  THR D  21     -38.286-110.330 -36.890  1.00162.96           C
ANISOU 1124  CB  THR D  21    20791  20341  20786  -2048  -2779  -3145       C
ATOM   1125  OG1 THR D  21     -38.027-111.596 -37.512  1.00137.00           O
ANISOU 1125  OG1 THR D  21    17581  16993  17482  -2077  -2803  -3225       O
ATOM   1126  CG2 THR D  21     -39.679-109.859 -37.249  1.00187.75           C
ANISOU 1126  CG2 THR D  21    23949  23480  23908  -2093  -2904  -3030       C
ATOM   1127  N   GLN D  22     -35.223-109.567 -36.056  1.00120.62           N
ANISOU 1127  N   GLN D  22    15376  15045  15408  -1946  -2455  -3322       N
ATOM   1128  CA  GLN D  22     -33.899-110.127 -35.763  1.00152.10           C
ANISOU 1128  CA  GLN D  22    19351  19029  19412  -1910  -2337  -3420       C
ATOM   1129  C   GLN D  22     -32.773-109.407 -36.520  1.00141.06           C
ANISOU 1129  C   GLN D  22    18042  17650  17904  -1920  -2228  -3494       C
ATOM   1130  O   GLN D  22     -31.593-109.677 -36.299  1.00133.89           O
ANISOU 1130  O   GLN D  22    17125  16748  16999  -1889  -2118  -3567       O
ATOM   1131  CB  GLN D  22     -33.870-111.661 -35.963  1.00145.79           C
ANISOU 1131  CB  GLN D  22    18577  18171  18644  -1921  -2373  -3478       C
ATOM   1132  CG  GLN D  22     -33.101-112.177 -37.177  1.00153.88           C
ANISOU 1132  CG  GLN D  22    19745  19158  19564  -1957  -2330  -3587       C
ATOM   1133  CD  GLN D  22     -33.179-113.702 -37.339  1.00146.65           C
ANISOU 1133  CD  GLN D  22    18856  18180  18685  -1966  -2379  -3639       C
ATOM   1134  OE1 GLN D  22     -32.803-114.254 -38.390  1.00140.29           O
ANISOU 1134  OE1 GLN D  22    18176  17333  17794  -1998  -2373  -3719       O
ATOM   1135  NE2 GLN D  22     -33.668-114.387 -36.301  1.00 95.08           N
ANISOU 1135  NE2 GLN D  22    12205  11642  12280  -1936  -2430  -3591       N
ATOM   1136  N   ALA D  23     -33.147-108.491 -37.407  1.00137.93           N
ANISOU 1136  N   ALA D  23    17728  17266  17413  -1965  -2259  -3469       N
ATOM   1137  CA  ALA D  23     -32.196-107.532 -37.951  1.00109.19           C
ANISOU 1137  CA  ALA D  23    14147  13660  13681  -1969  -2162  -3511       C
ATOM   1138  C   ALA D  23     -32.268-106.219 -37.170  1.00111.37           C
ANISOU 1138  C   ALA D  23    14339  13991  13986  -1937  -2137  -3438       C
ATOM   1139  O   ALA D  23     -33.356-105.703 -36.902  1.00132.01           O
ANISOU 1139  O   ALA D  23    16914  16615  16628  -1944  -2222  -3348       O
ATOM   1140  CB  ALA D  23     -32.445-107.293 -39.419  1.00100.61           C
ANISOU 1140  CB  ALA D  23    13201  12558  12469  -2036  -2203  -3534       C
ATOM   1141  N   PRO D  24     -31.102-105.677 -36.803  1.00127.10           N
ANISOU 1141  N   PRO D  24    16304  16016  15970  -1900  -2020  -3475       N
ATOM   1142  CA  PRO D  24     -31.022-104.467 -35.980  1.00141.86           C
ANISOU 1142  CA  PRO D  24    18095  17935  17872  -1863  -1988  -3414       C
ATOM   1143  C   PRO D  24     -31.512-103.241 -36.726  1.00132.32           C
ANISOU 1143  C   PRO D  24    16947  16749  16580  -1903  -2029  -3367       C
ATOM   1144  O   PRO D  24     -31.976-102.275 -36.120  1.00123.88           O
ANISOU 1144  O   PRO D  24    15816  15711  15540  -1883  -2051  -3292       O
ATOM   1145  CB  PRO D  24     -29.517-104.326 -35.721  1.00139.88           C
ANISOU 1145  CB  PRO D  24    17834  17705  17611  -1828  -1854  -3479       C
ATOM   1146  CG  PRO D  24     -28.867-105.009 -36.884  1.00117.50           C
ANISOU 1146  CG  PRO D  24    15115  14844  14687  -1864  -1818  -3567       C
ATOM   1147  CD  PRO D  24     -29.769-106.158 -37.217  1.00128.85           C
ANISOU 1147  CD  PRO D  24    16580  16231  16145  -1893  -1913  -3574       C
ATOM   1148  N   THR D  25     -31.406-103.283 -38.045  1.00124.66           N
ANISOU 1148  N   THR D  25    16096  15765  15503  -1960  -2038  -3411       N
ATOM   1149  CA  THR D  25     -31.576-102.070 -38.813  1.00135.25           C
ANISOU 1149  CA  THR D  25    17496  17134  16757  -1998  -2052  -3380       C
ATOM   1150  C   THR D  25     -32.019-102.334 -40.246  1.00159.70           C
ANISOU 1150  C   THR D  25    20717  20207  19755  -2071  -2111  -3406       C
ATOM   1151  O   THR D  25     -31.885-103.447 -40.768  1.00142.38           O
ANISOU 1151  O   THR D  25    18583  17974  17542  -2088  -2119  -3468       O
ATOM   1152  CB  THR D  25     -30.259-101.294 -38.854  1.00127.88           C
ANISOU 1152  CB  THR D  25    16572  16240  15778  -1977  -1939  -3420       C
ATOM   1153  OG1 THR D  25     -30.517 -99.907 -39.103  1.00158.13           O
ANISOU 1153  OG1 THR D  25    20412  20108  19564  -1995  -1957  -3364       O
ATOM   1154  CG2 THR D  25     -29.361-101.854 -39.949  1.00121.90           C
ANISOU 1154  CG2 THR D  25    15918  15469  14928  -2003  -1882  -3512       C
ATOM   1155  N   HIS D  26     -32.554-101.289 -40.868  1.00165.27           N
ANISOU 1155  N   HIS D  26    21461  20935  20397  -2112  -2154  -3356       N
ATOM   1156  CA  HIS D  26     -32.907-101.318 -42.272  1.00153.33           C
ANISOU 1156  CA  HIS D  26    20067  19409  18782  -2184  -2203  -3375       C
ATOM   1157  C   HIS D  26     -31.745-101.870 -43.083  1.00125.00           C
ANISOU 1157  C   HIS D  26    16564  15813  15116  -2189  -2122  -3481       C
ATOM   1158  O   HIS D  26     -31.855-102.942 -43.680  1.00133.01           O
ANISOU 1158  O   HIS D  26    17648  16785  16105  -2213  -2151  -3532       O
ATOM   1159  CB  HIS D  26     -33.280 -99.914 -42.737  1.00166.30           C
ANISOU 1159  CB  HIS D  26    21727  21092  20368  -2218  -2226  -3315       C
ATOM   1160  CG  HIS D  26     -34.073 -99.882 -44.009  1.00180.33           C
ANISOU 1160  CG  HIS D  26    23603  22854  22060  -2298  -2306  -3303       C
ATOM   1161  ND1 HIS D  26     -33.883-100.801 -45.023  1.00181.60           N
ANISOU 1161  ND1 HIS D  26    23867  22981  22153  -2336  -2314  -3375       N
ATOM   1162  CD2 HIS D  26     -35.051 -99.055 -44.420  1.00152.43           C
ANISOU 1162  CD2 HIS D  26    20083  19335  18499  -2346  -2381  -3225       C
ATOM   1163  CE1 HIS D  26     -34.717-100.525 -46.010  1.00157.81           C
ANISOU 1163  CE1 HIS D  26    20925  19961  19073  -2407  -2393  -3343       C
ATOM   1164  NE2 HIS D  26     -35.437 -99.476 -45.676  1.00159.38           N
ANISOU 1164  NE2 HIS D  26    21071  20190  19296  -2416  -2433  -3251       N
ATOM   1165  N   LEU D  27     -30.622-101.163 -43.074  1.00 80.81           N
ANISOU 1165  N   LEU D  27    10963  10258   9483  -2164  -2023  -3510       N
ATOM   1166  CA  LEU D  27     -29.457-101.594 -43.845  1.00140.13           C
ANISOU 1166  CA  LEU D  27    18554  17771  16916  -2162  -1940  -3601       C
ATOM   1167  C   LEU D  27     -29.190-103.091 -43.692  1.00152.64           C
ANISOU 1167  C   LEU D  27    20153  19308  18535  -2141  -1925  -3670       C
ATOM   1168  O   LEU D  27     -28.784-103.766 -44.659  1.00124.95           O
ANISOU 1168  O   LEU D  27    16746  15780  14951  -2161  -1908  -3742       O
ATOM   1169  CB  LEU D  27     -28.217-100.842 -43.376  1.00148.47           C
ANISOU 1169  CB  LEU D  27    19564  18875  17972  -2117  -1828  -3612       C
ATOM   1170  CG  LEU D  27     -27.956 -99.436 -43.901  1.00138.60           C
ANISOU 1170  CG  LEU D  27    18334  17677  16651  -2139  -1811  -3578       C
ATOM   1171  CD1 LEU D  27     -27.426 -99.478 -45.334  1.00138.26           C
ANISOU 1171  CD1 LEU D  27    18406  17645  16480  -2178  -1786  -3635       C
ATOM   1172  CD2 LEU D  27     -29.230 -98.604 -43.793  1.00155.78           C
ANISOU 1172  CD2 LEU D  27    20482  19860  18848  -2172  -1910  -3489       C
ATOM   1173  N   SER D  28     -29.405-103.592 -42.474  1.00142.86           N
ANISOU 1173  N   SER D  28    18814  18052  17413  -2098  -1931  -3646       N
ATOM   1174  CA  SER D  28     -29.090-104.974 -42.116  1.00146.55           C
ANISOU 1174  CA  SER D  28    19273  18478  17933  -2069  -1911  -3705       C
ATOM   1175  C   SER D  28     -29.914-105.989 -42.885  1.00166.59           C
ANISOU 1175  C   SER D  28    21893  20960  20445  -2115  -2006  -3728       C
ATOM   1176  O   SER D  28     -29.428-107.069 -43.228  1.00178.83           O
ANISOU 1176  O   SER D  28    23497  22474  21977  -2109  -1980  -3805       O
ATOM   1177  CB  SER D  28     -29.323-105.196 -40.628  1.00150.76           C
ANISOU 1177  CB  SER D  28    19671  19010  18602  -2018  -1912  -3660       C
ATOM   1178  OG  SER D  28     -29.415-106.582 -40.348  1.00172.21           O
ANISOU 1178  OG  SER D  28    22376  21679  21376  -2005  -1931  -3700       O
ATOM   1179  N   VAL D  29     -31.169-105.639 -43.139  1.00157.53           N
ANISOU 1179  N   VAL D  29    20755  19804  19296  -2161  -2117  -3657       N
ATOM   1180  CA  VAL D  29     -32.100-106.555 -43.781  1.00139.25           C
ANISOU 1180  CA  VAL D  29    18510  17433  16966  -2208  -2224  -3661       C
ATOM   1181  C   VAL D  29     -31.667-106.867 -45.214  1.00150.01           C
ANISOU 1181  C   VAL D  29    20018  18778  18201  -2249  -2211  -3741       C
ATOM   1182  O   VAL D  29     -31.133-106.001 -45.916  1.00146.68           O
ANISOU 1182  O   VAL D  29    19647  18397  17689  -2264  -2159  -3756       O
ATOM   1183  CB  VAL D  29     -33.519-105.990 -43.750  1.00125.17           C
ANISOU 1183  CB  VAL D  29    16703  15651  15205  -2250  -2342  -3556       C
ATOM   1184  CG1 VAL D  29     -34.519-107.058 -44.118  1.00135.42           C
ANISOU 1184  CG1 VAL D  29    18048  16888  16517  -2291  -2459  -3545       C
ATOM   1185  CG2 VAL D  29     -33.819-105.454 -42.361  1.00121.92           C
ANISOU 1185  CG2 VAL D  29    16149  15270  14904  -2200  -2339  -3476       C
ATOM   1186  N   ASP D  30     -31.881-108.114 -45.627  1.00147.02           N
ANISOU 1186  N   ASP D  30    19704  18340  17815  -2265  -2259  -3791       N
ATOM   1187  CA  ASP D  30     -31.455-108.599 -46.935  1.00143.82           C
ANISOU 1187  CA  ASP D  30    19443  17911  17293  -2295  -2248  -3876       C
ATOM   1188  C   ASP D  30     -32.187-107.861 -48.049  1.00147.25           C
ANISOU 1188  C   ASP D  30    19962  18355  17632  -2367  -2319  -3840       C
ATOM   1189  O   ASP D  30     -33.340-107.472 -47.867  1.00161.75           O
ANISOU 1189  O   ASP D  30    21765  20188  19506  -2404  -2416  -3751       O
ATOM   1190  CB  ASP D  30     -31.757-110.093 -47.040  1.00135.72           C
ANISOU 1190  CB  ASP D  30    18463  16811  16295  -2300  -2309  -3924       C
ATOM   1191  CG  ASP D  30     -30.730-110.844 -47.866  1.00157.06           C
ANISOU 1191  CG  ASP D  30    21275  19491  18908  -2285  -2238  -4039       C
ATOM   1192  OD1 ASP D  30     -29.914-110.190 -48.554  1.00152.07           O
ANISOU 1192  OD1 ASP D  30    20699  18901  18179  -2282  -2156  -4076       O
ATOM   1193  OD2 ASP D  30     -30.743-112.096 -47.821  1.00161.33           O
ANISOU 1193  OD2 ASP D  30    21846  19973  19478  -2274  -2267  -4089       O
ATOM   1194  N   ILE D  31     -31.542-107.690 -49.203  1.00128.90           N
ANISOU 1194  N   ILE D  31    17747  16043  15184  -2386  -2273  -3905       N
ATOM   1195  CA  ILE D  31     -32.205-107.054 -50.338  1.00139.15           C
ANISOU 1195  CA  ILE D  31    19132  17352  16387  -2458  -2340  -3876       C
ATOM   1196  C   ILE D  31     -33.575-107.696 -50.500  1.00141.21           C
ANISOU 1196  C   ILE D  31    19423  17553  16679  -2512  -2483  -3830       C
ATOM   1197  O   ILE D  31     -34.560-107.033 -50.855  1.00146.86           O
ANISOU 1197  O   ILE D  31    20146  18276  17377  -2570  -2565  -3753       O
ATOM   1198  CB  ILE D  31     -31.432-107.286 -51.665  1.00128.53           C
ANISOU 1198  CB  ILE D  31    17923  16008  14904  -2471  -2292  -3969       C
ATOM   1199  CG1 ILE D  31     -30.350-108.352 -51.480  1.00169.36           C
ANISOU 1199  CG1 ILE D  31    23117  21154  20079  -2409  -2208  -4066       C
ATOM   1200  CG2 ILE D  31     -30.834-105.993 -52.204  1.00 95.98           C
ANISOU 1200  CG2 ILE D  31    13807  11959  10700  -2478  -2223  -3958       C
ATOM   1201  CD1 ILE D  31     -30.883-109.766 -51.443  1.00179.20           C
ANISOU 1201  CD1 ILE D  31    24406  22318  21363  -2416  -2286  -4101       C
ATOM   1202  N   LYS D  32     -33.624-108.993 -50.212  1.00119.28           N
ANISOU 1202  N   LYS D  32    16658  14714  13949  -2493  -2513  -3872       N
ATOM   1203  CA  LYS D  32     -34.795-109.819 -50.483  1.00124.05           C
ANISOU 1203  CA  LYS D  32    17309  15251  14573  -2544  -2650  -3841       C
ATOM   1204  C   LYS D  32     -36.106-109.345 -49.851  1.00120.55           C
ANISOU 1204  C   LYS D  32    16779  14811  14214  -2575  -2754  -3713       C
ATOM   1205  O   LYS D  32     -37.171-109.681 -50.350  1.00141.77           O
ANISOU 1205  O   LYS D  32    19521  17456  16890  -2636  -2874  -3668       O
ATOM   1206  CB  LYS D  32     -34.508-111.267 -50.095  1.00113.75           C
ANISOU 1206  CB  LYS D  32    16012  13884  13323  -2507  -2656  -3906       C
ATOM   1207  CG  LYS D  32     -33.336-111.882 -50.842  1.00100.06           C
ANISOU 1207  CG  LYS D  32    14383  12136  11498  -2480  -2569  -4032       C
ATOM   1208  CD  LYS D  32     -32.851-113.152 -50.159  1.00111.36           C
ANISOU 1208  CD  LYS D  32    15786  13521  13005  -2426  -2544  -4092       C
ATOM   1209  CE  LYS D  32     -32.226-114.142 -51.147  1.00116.34           C
ANISOU 1209  CE  LYS D  32    16561  14104  13541  -2422  -2525  -4207       C
ATOM   1210  NZ  LYS D  32     -30.739-113.986 -51.306  1.00118.04           N
ANISOU 1210  NZ  LYS D  32    16794  14360  13695  -2363  -2370  -4291       N
ATOM   1211  N   PHE D  33     -36.046-108.610 -48.743  1.00104.63           N
ANISOU 1211  N   PHE D  33    14630  12843  12281  -2531  -2710  -3651       N
ATOM   1212  CA  PHE D  33     -37.269-108.060 -48.149  1.00126.78           C
ANISOU 1212  CA  PHE D  33    17353  15659  15159  -2553  -2801  -3525       C
ATOM   1213  C   PHE D  33     -37.542-106.569 -48.449  1.00143.02           C
ANISOU 1213  C   PHE D  33    19397  17776  17168  -2584  -2791  -3459       C
ATOM   1214  O   PHE D  33     -38.597-106.035 -48.057  1.00109.93           O
ANISOU 1214  O   PHE D  33    15146  13596  13025  -2605  -2867  -3349       O
ATOM   1215  CB  PHE D  33     -37.298-108.296 -46.632  1.00132.66           C
ANISOU 1215  CB  PHE D  33    17951  16413  16042  -2485  -2786  -3482       C
ATOM   1216  CG  PHE D  33     -36.970-109.706 -46.218  1.00131.73           C
ANISOU 1216  CG  PHE D  33    17826  16242  15983  -2451  -2788  -3543       C
ATOM   1217  CD1 PHE D  33     -35.679-110.055 -45.866  1.00136.70           C
ANISOU 1217  CD1 PHE D  33    18438  16882  16621  -2391  -2668  -3636       C
ATOM   1218  CD2 PHE D  33     -37.952-110.674 -46.162  1.00147.71           C
ANISOU 1218  CD2 PHE D  33    19858  18207  18058  -2479  -2911  -3504       C
ATOM   1219  CE1 PHE D  33     -35.372-111.345 -45.473  1.00135.20           C
ANISOU 1219  CE1 PHE D  33    18238  16643  16488  -2359  -2668  -3692       C
ATOM   1220  CE2 PHE D  33     -37.648-111.969 -45.769  1.00153.60           C
ANISOU 1220  CE2 PHE D  33    20594  18905  18863  -2447  -2917  -3560       C
ATOM   1221  CZ  PHE D  33     -36.355-112.302 -45.424  1.00123.79           C
ANISOU 1221  CZ  PHE D  33    16800  15139  15094  -2387  -2793  -3656       C
ATOM   1222  N   LYS D  34     -36.611-105.912 -49.147  1.00157.52           N
ANISOU 1222  N   LYS D  34    21289  19652  18910  -2585  -2700  -3520       N
ATOM   1223  CA  LYS D  34     -36.618-104.445 -49.269  1.00184.31           C
ANISOU 1223  CA  LYS D  34    24651  23109  22268  -2599  -2669  -3467       C
ATOM   1224  C   LYS D  34     -37.186-103.913 -50.599  1.00190.67           C
ANISOU 1224  C   LYS D  34    25560  23921  22967  -2684  -2727  -3447       C
ATOM   1225  O   LYS D  34     -36.627-104.172 -51.682  1.00130.26           O
ANISOU 1225  O   LYS D  34    18018  16262  15212  -2709  -2700  -3528       O
ATOM   1226  CB  LYS D  34     -35.203-103.885 -49.043  1.00209.92           C
ANISOU 1226  CB  LYS D  34    27867  26404  25488  -2541  -2530  -3530       C
ATOM   1227  CG  LYS D  34     -34.585-104.225 -47.679  1.00212.35           C
ANISOU 1227  CG  LYS D  34    28064  26716  25903  -2459  -2462  -3541       C
ATOM   1228  CD  LYS D  34     -33.065-104.014 -47.653  1.00193.91           C
ANISOU 1228  CD  LYS D  34    25730  24417  23531  -2408  -2325  -3622       C
ATOM   1229  CE  LYS D  34     -32.681-102.598 -47.256  1.00157.79           C
ANISOU 1229  CE  LYS D  34    21087  19908  18958  -2388  -2267  -3574       C
ATOM   1230  NZ  LYS D  34     -31.280-102.535 -46.747  1.00136.31           N
ANISOU 1230  NZ  LYS D  34    18328  17216  16248  -2324  -2140  -3631       N
ATOM   1231  N   THR D  35     -38.295-103.171 -50.499  1.00229.82           N
ANISOU 1231  N   THR D  35    30480  28892  27948  -2725  -2805  -3338       N
ATOM   1232  CA  THR D  35     -39.002-102.606 -51.657  1.00228.86           C
ANISOU 1232  CA  THR D  35    30441  28778  27739  -2812  -2870  -3299       C
ATOM   1233  C   THR D  35     -39.472-101.182 -51.366  1.00218.72           C
ANISOU 1233  C   THR D  35    29083  27550  26471  -2824  -2873  -3201       C
ATOM   1234  O   THR D  35     -40.182-100.956 -50.384  1.00204.65           O
ANISOU 1234  O   THR D  35    27206  25771  24781  -2800  -2913  -3112       O
ATOM   1235  CB  THR D  35     -40.267-103.412 -51.986  1.00204.03           C
ANISOU 1235  CB  THR D  35    27343  25570  24608  -2873  -3005  -3246       C
ATOM   1236  OG1 THR D  35     -41.329-102.995 -51.118  1.00158.58           O
ANISOU 1236  OG1 THR D  35    21488  19821  18942  -2872  -3072  -3120       O
ATOM   1237  CG2 THR D  35     -40.022-104.894 -51.793  1.00227.45           C
ANISOU 1237  CG2 THR D  35    30341  28472  27606  -2845  -3021  -3316       C
ATOM   1238  N   GLU D  36     -39.090-100.224 -52.206  1.00210.81           N
ANISOU 1238  N   GLU D  36    28124  26595  25380  -2858  -2832  -3216       N
ATOM   1239  CA  GLU D  36     -39.508 -98.834 -51.992  1.00213.56           C
ANISOU 1239  CA  GLU D  36    28408  26997  25739  -2871  -2835  -3125       C
ATOM   1240  C   GLU D  36     -39.394 -98.414 -50.514  1.00192.43           C
ANISOU 1240  C   GLU D  36    25600  24343  23171  -2792  -2798  -3077       C
ATOM   1241  O   GLU D  36     -40.394 -98.054 -49.864  1.00137.38           O
ANISOU 1241  O   GLU D  36    18560  17372  16266  -2793  -2861  -2974       O
ATOM   1242  CB  GLU D  36     -40.847 -98.458 -52.675  1.00221.21           C
ANISOU 1242  CB  GLU D  36    29413  27958  26680  -2961  -2944  -3031       C
ATOM   1243  CG  GLU D  36     -42.136 -99.011 -52.083  1.00224.58           C
ANISOU 1243  CG  GLU D  36    29801  28340  27188  -2974  -3051  -2936       C
ATOM   1244  CD  GLU D  36     -43.389 -98.479 -52.793  1.00192.99           C
ANISOU 1244  CD  GLU D  36    25835  24341  23154  -3065  -3149  -2834       C
ATOM   1245  OE1 GLU D  36     -43.286 -97.469 -53.526  1.00170.99           O
ANISOU 1245  OE1 GLU D  36    23073  21597  20297  -3108  -3126  -2825       O
ATOM   1246  OE2 GLU D  36     -44.478 -99.076 -52.621  1.00158.38           O
ANISOU 1246  OE2 GLU D  36    21449  19915  18815  -3094  -3249  -2759       O
ATOM   1247  N   GLY D  37     -38.179 -98.566 -49.981  1.00175.14           N
ANISOU 1247  N   GLY D  37    23379  22168  20999  -2721  -2697  -3154       N
ATOM   1248  CA  GLY D  37     -37.840 -98.111 -48.644  1.00151.81           C
ANISOU 1248  CA  GLY D  37    20307  19239  18135  -2643  -2645  -3124       C
ATOM   1249  C   GLY D  37     -38.683 -98.751 -47.561  1.00167.08           C
ANISOU 1249  C   GLY D  37    22164  21139  20180  -2610  -2707  -3061       C
ATOM   1250  O   GLY D  37     -38.982 -98.126 -46.543  1.00170.83           O
ANISOU 1250  O   GLY D  37    22540  21638  20729  -2566  -2707  -2990       O
ATOM   1251  N   LEU D  38     -39.065-100.003 -47.785  1.00175.78           N
ANISOU 1251  N   LEU D  38    23310  22185  21291  -2630  -2764  -3086       N
ATOM   1252  CA  LEU D  38     -39.899-100.731 -46.842  1.00176.68           C
ANISOU 1252  CA  LEU D  38    23355  22267  21510  -2603  -2833  -3023       C
ATOM   1253  C   LEU D  38     -39.469-102.192 -46.776  1.00151.40           C
ANISOU 1253  C   LEU D  38    20182  19013  18331  -2582  -2829  -3105       C
ATOM   1254  O   LEU D  38     -38.898-102.723 -47.732  1.00141.34           O
ANISOU 1254  O   LEU D  38    19011  17717  16977  -2612  -2806  -3195       O
ATOM   1255  CB  LEU D  38     -41.367-100.623 -47.253  1.00183.37           C
ANISOU 1255  CB  LEU D  38    24223  23096  22354  -2671  -2958  -2918       C
ATOM   1256  CG  LEU D  38     -42.319-100.042 -46.208  1.00153.55           C
ANISOU 1256  CG  LEU D  38    20335  19341  18666  -2641  -3006  -2791       C
ATOM   1257  CD1 LEU D  38     -42.330-100.921 -44.980  1.00122.03           C
ANISOU 1257  CD1 LEU D  38    16253  15329  14785  -2569  -3011  -2783       C
ATOM   1258  CD2 LEU D  38     -41.921 -98.619 -45.850  1.00145.43           C
ANISOU 1258  CD2 LEU D  38    19252  18373  17630  -2609  -2937  -2766       C
ATOM   1259  N   CYS D  39     -39.738-102.841 -45.648  1.00106.84           N
ANISOU 1259  N   CYS D  39    14448  13351  12795  -2530  -2850  -3074       N
ATOM   1260  CA  CYS D  39     -39.330-104.230 -45.465  1.00136.78           C
ANISOU 1260  CA  CYS D  39    18254  17094  16621  -2505  -2845  -3148       C
ATOM   1261  C   CYS D  39     -40.550-105.082 -45.154  1.00129.74           C
ANISOU 1261  C   CYS D  39    17339  16157  15800  -2525  -2970  -3071       C
ATOM   1262  O   CYS D  39     -41.283-104.769 -44.217  1.00135.30           O
ANISOU 1262  O   CYS D  39    17940  16879  16588  -2496  -3012  -2971       O
ATOM   1263  CB  CYS D  39     -38.302-104.343 -44.331  1.00160.45           C
ANISOU 1263  CB  CYS D  39    21157  20113  19692  -2417  -2741  -3194       C
ATOM   1264  SG  CYS D  39     -36.649-103.639 -44.676  1.00168.47           S
ANISOU 1264  SG  CYS D  39    22206  21174  20630  -2388  -2587  -3297       S
ATOM   1265  N   VAL D  40     -40.773-106.145 -45.935  1.00121.18           N
ANISOU 1265  N   VAL D  40    16349  15013  14679  -2571  -3033  -3114       N
ATOM   1266  CA  VAL D  40     -42.000-106.951 -45.799  1.00152.21           C
ANISOU 1266  CA  VAL D  40    20270  18896  18666  -2603  -3168  -3033       C
ATOM   1267  C   VAL D  40     -41.814-108.448 -45.518  1.00142.99           C
ANISOU 1267  C   VAL D  40    19106  17670  17553  -2581  -3196  -3089       C
ATOM   1268  O   VAL D  40     -41.047-109.127 -46.204  1.00125.67           O
ANISOU 1268  O   VAL D  40    17006  15442  15299  -2590  -3159  -3201       O
ATOM   1269  CB  VAL D  40     -42.900-106.836 -47.042  1.00152.40           C
ANISOU 1269  CB  VAL D  40    20406  18893  18604  -2699  -3267  -2992       C
ATOM   1270  CG1 VAL D  40     -42.251-107.538 -48.235  1.00161.07           C
ANISOU 1270  CG1 VAL D  40    21648  19949  19602  -2739  -3251  -3113       C
ATOM   1271  CG2 VAL D  40     -44.272-107.431 -46.748  1.00134.63           C
ANISOU 1271  CG2 VAL D  40    18126  16605  16423  -2729  -3410  -2877       C
ATOM   1272  N   ASP D  41     -42.577-108.962 -44.553  1.00125.84           N
ANISOU 1272  N   ASP D  41    16836  15486  15492  -2554  -3270  -3005       N
ATOM   1273  CA  ASP D  41     -42.440-110.341 -44.111  1.00114.15           C
ANISOU 1273  CA  ASP D  41    15334  13955  14082  -2527  -3300  -3046       C
ATOM   1274  C   ASP D  41     -42.860-111.326 -45.195  1.00141.03           C
ANISOU 1274  C   ASP D  41    18871  17286  17430  -2597  -3398  -3078       C
ATOM   1275  O   ASP D  41     -43.997-111.317 -45.672  1.00157.09           O
ANISOU 1275  O   ASP D  41    20943  19296  19448  -2661  -3518  -2989       O
ATOM   1276  CB  ASP D  41     -43.315-110.575 -42.887  1.00114.84           C
ANISOU 1276  CB  ASP D  41    15283  14052  14300  -2488  -3373  -2929       C
ATOM   1277  CG  ASP D  41     -43.144-111.967 -42.306  1.00139.78           C
ANISOU 1277  CG  ASP D  41    18400  17166  17545  -2454  -3401  -2965       C
ATOM   1278  OD1 ASP D  41     -42.098-112.599 -42.563  1.00140.64           O
ANISOU 1278  OD1 ASP D  41    18560  17249  17626  -2438  -3327  -3091       O
ATOM   1279  OD2 ASP D  41     -44.051-112.424 -41.577  1.00147.03           O
ANISOU 1279  OD2 ASP D  41    19230  18076  18559  -2442  -3497  -2865       O
ATOM   1280  N   ILE D  42     -41.926-112.183 -45.573  1.00129.55           N
ANISOU 1280  N   ILE D  42    17487  15794  15942  -2585  -3347  -3204       N
ATOM   1281  CA  ILE D  42     -42.181-113.228 -46.542  1.00113.07           C
ANISOU 1281  CA  ILE D  42    15529  13631  13802  -2641  -3432  -3252       C
ATOM   1282  C   ILE D  42     -41.920-114.587 -45.899  1.00126.01           C
ANISOU 1282  C   ILE D  42    17128  15221  15529  -2599  -3451  -3297       C
ATOM   1283  O   ILE D  42     -40.773-114.952 -45.655  1.00153.57           O
ANISOU 1283  O   ILE D  42    20611  18714  19023  -2546  -3343  -3402       O
ATOM   1284  CB  ILE D  42     -41.272-113.014 -47.759  1.00123.80           C
ANISOU 1284  CB  ILE D  42    17028  14986  15023  -2666  -3353  -3372       C
ATOM   1285  CG1 ILE D  42     -41.462-111.584 -48.289  1.00 95.22           C
ANISOU 1285  CG1 ILE D  42    13428  11425  11327  -2703  -3324  -3324       C
ATOM   1286  CG2 ILE D  42     -41.532-114.073 -48.810  1.00151.17           C
ANISOU 1286  CG2 ILE D  42    20640  18373  18426  -2723  -3442  -3425       C
ATOM   1287  CD1 ILE D  42     -40.646-111.262 -49.515  1.00100.23           C
ANISOU 1287  CD1 ILE D  42    14193  12066  11824  -2730  -3252  -3427       C
ATOM   1288  N   PRO D  43     -42.976-115.351 -45.621  1.00126.48           N
ANISOU 1288  N   PRO D  43    17159  15236  15661  -2623  -3590  -3213       N
ATOM   1289  CA  PRO D  43     -42.669-116.703 -45.150  1.00133.58           C
ANISOU 1289  CA  PRO D  43    18035  16083  16634  -2589  -3611  -3267       C
ATOM   1290  C   PRO D  43     -41.985-117.453 -46.285  1.00148.89           C
ANISOU 1290  C   PRO D  43    20137  17961  18472  -2617  -3594  -3401       C
ATOM   1291  O   PRO D  43     -41.985-116.956 -47.417  1.00151.94           O
ANISOU 1291  O   PRO D  43    20647  18344  18738  -2670  -3592  -3430       O
ATOM   1292  CB  PRO D  43     -44.051-117.295 -44.855  1.00158.01           C
ANISOU 1292  CB  PRO D  43    21088  19140  19808  -2625  -3782  -3139       C
ATOM   1293  CG  PRO D  43     -45.001-116.478 -45.670  1.00160.06           C
ANISOU 1293  CG  PRO D  43    21418  19407  19993  -2700  -3858  -3051       C
ATOM   1294  CD  PRO D  43     -44.421-115.095 -45.716  1.00137.26           C
ANISOU 1294  CD  PRO D  43    18513  16595  17047  -2680  -3730  -3068       C
ATOM   1295  N   GLY D  44     -41.370-118.593 -45.992  1.00135.99           N
ANISOU 1295  N   GLY D  44    18501  16284  16882  -2579  -3576  -3485       N
ATOM   1296  CA  GLY D  44     -40.795-119.405 -47.050  1.00159.93           C
ANISOU 1296  CA  GLY D  44    21692  19252  19821  -2601  -3572  -3608       C
ATOM   1297  C   GLY D  44     -39.457-118.865 -47.527  1.00144.81           C
ANISOU 1297  C   GLY D  44    19836  17376  17808  -2568  -3408  -3727       C
ATOM   1298  O   GLY D  44     -38.774-119.471 -48.367  1.00 95.40           O
ANISOU 1298  O   GLY D  44    13707  11076  11466  -2571  -3376  -3842       O
ATOM   1299  N   ILE D  45     -39.103-117.693 -47.013  1.00147.13           N
ANISOU 1299  N   ILE D  45    20040  17751  18110  -2537  -3308  -3695       N
ATOM   1300  CA  ILE D  45     -37.712-117.262 -46.967  1.00144.85           C
ANISOU 1300  CA  ILE D  45    19749  17509  17777  -2482  -3139  -3792       C
ATOM   1301  C   ILE D  45     -37.434-116.940 -45.507  1.00121.12           C
ANISOU 1301  C   ILE D  45    16565  14559  14896  -2414  -3070  -3745       C
ATOM   1302  O   ILE D  45     -37.191-115.791 -45.154  1.00104.70           O
ANISOU 1302  O   ILE D  45    14421  12548  12812  -2395  -2993  -3710       O
ATOM   1303  CB  ILE D  45     -37.449-116.064 -47.899  1.00122.46           C
ANISOU 1303  CB  ILE D  45    16994  14721  14816  -2513  -3080  -3804       C
ATOM   1304  CG1 ILE D  45     -36.041-115.512 -47.697  1.00101.11           C
ANISOU 1304  CG1 ILE D  45    14262  12074  12079  -2452  -2907  -3882       C
ATOM   1305  CG2 ILE D  45     -38.520-114.991 -47.730  1.00118.95           C
ANISOU 1305  CG2 ILE D  45    16490  14316  14389  -2553  -3148  -3673       C
ATOM   1306  CD1 ILE D  45     -35.557-114.716 -48.883  1.00144.28           C
ANISOU 1306  CD1 ILE D  45    19846  17572  17403  -2481  -2850  -3930       C
ATOM   1307  N   PRO D  46     -37.484-117.979 -44.652  1.00120.47           N
ANISOU 1307  N   PRO D  46    16403  14444  14926  -2380  -3101  -3745       N
ATOM   1308  CA  PRO D  46     -37.585-117.819 -43.198  1.00139.41           C
ANISOU 1308  CA  PRO D  46    18622  16887  17461  -2325  -3078  -3674       C
ATOM   1309  C   PRO D  46     -36.410-117.106 -42.545  1.00145.83           C
ANISOU 1309  C   PRO D  46    19357  17767  18285  -2261  -2913  -3716       C
ATOM   1310  O   PRO D  46     -35.282-117.075 -43.070  1.00123.79           O
ANISOU 1310  O   PRO D  46    16639  14980  15414  -2244  -2801  -3820       O
ATOM   1311  CB  PRO D  46     -37.677-119.265 -42.686  1.00120.95           C
ANISOU 1311  CB  PRO D  46    16247  14491  15219  -2306  -3138  -3695       C
ATOM   1312  CG  PRO D  46     -37.053-120.084 -43.745  1.00133.33           C
ANISOU 1312  CG  PRO D  46    17968  15996  16693  -2325  -3124  -3817       C
ATOM   1313  CD  PRO D  46     -37.390-119.398 -45.037  1.00116.08           C
ANISOU 1313  CD  PRO D  46    15927  13808  14372  -2388  -3157  -3818       C
ATOM   1314  N   LYS D  47     -36.697-116.542 -41.377  1.00138.68           N
ANISOU 1314  N   LYS D  47    18300  16913  17478  -2223  -2902  -3630       N
ATOM   1315  CA  LYS D  47     -35.671-115.922 -40.573  1.00144.52           C
ANISOU 1315  CA  LYS D  47    18949  17714  18249  -2160  -2758  -3656       C
ATOM   1316  C   LYS D  47     -34.666-116.993 -40.166  1.00136.83           C
ANISOU 1316  C   LYS D  47    17952  16714  17322  -2115  -2681  -3751       C
ATOM   1317  O   LYS D  47     -34.950-118.195 -40.261  1.00116.23           O
ANISOU 1317  O   LYS D  47    15367  14046  14750  -2126  -2755  -3775       O
ATOM   1318  CB  LYS D  47     -36.276-115.233 -39.349  1.00144.86           C
ANISOU 1318  CB  LYS D  47    18834  17810  18395  -2126  -2776  -3542       C
ATOM   1319  CG  LYS D  47     -37.094-116.123 -38.442  1.00133.57           C
ANISOU 1319  CG  LYS D  47    17295  16358  17096  -2109  -2876  -3473       C
ATOM   1320  CD  LYS D  47     -37.348-115.439 -37.111  1.00129.82           C
ANISOU 1320  CD  LYS D  47    16655  15947  16723  -2055  -2854  -3381       C
ATOM   1321  CE  LYS D  47     -38.073-116.367 -36.151  1.00148.59           C
ANISOU 1321  CE  LYS D  47    18913  18310  19235  -2030  -2946  -3312       C
ATOM   1322  NZ  LYS D  47     -37.451-117.725 -36.120  1.00156.18           N
ANISOU 1322  NZ  LYS D  47    19885  19221  20236  -2020  -2930  -3402       N
ATOM   1323  N   ASP D  48     -33.473-116.556 -39.774  1.00126.64           N
ANISOU 1323  N   ASP D  48    16624  15469  16026  -2067  -2533  -3805       N
ATOM   1324  CA  ASP D  48     -32.400-117.480 -39.460  1.00126.99           C
ANISOU 1324  CA  ASP D  48    16654  15494  16104  -2025  -2443  -3897       C
ATOM   1325  C   ASP D  48     -32.568-118.151 -38.089  1.00144.72           C
ANISOU 1325  C   ASP D  48    18740  17742  18505  -1981  -2457  -3857       C
ATOM   1326  O   ASP D  48     -32.818-117.477 -37.078  1.00121.20           O
ANISOU 1326  O   ASP D  48    15630  14815  15603  -1950  -2445  -3779       O
ATOM   1327  CB  ASP D  48     -31.071-116.745 -39.547  1.00124.64           C
ANISOU 1327  CB  ASP D  48    16372  15245  15742  -1992  -2281  -3959       C
ATOM   1328  CG  ASP D  48     -30.326-117.060 -40.811  1.00134.30           C
ANISOU 1328  CG  ASP D  48    17754  16438  16836  -2011  -2233  -4062       C
ATOM   1329  OD1 ASP D  48     -29.841-118.207 -40.939  1.00126.71           O
ANISOU 1329  OD1 ASP D  48    16829  15430  15884  -1997  -2215  -4139       O
ATOM   1330  OD2 ASP D  48     -30.221-116.160 -41.671  1.00169.39           O
ANISOU 1330  OD2 ASP D  48    22285  20907  21169  -2038  -2212  -4066       O
ATOM   1331  N   MET D  49     -32.431-119.477 -38.062  1.00135.67           N
ANISOU 1331  N   MET D  49    17604  16541  17403  -1976  -2485  -3911       N
ATOM   1332  CA  MET D  49     -32.587-120.239 -36.823  1.00135.66           C
ANISOU 1332  CA  MET D  49    17453  16540  17551  -1937  -2505  -3877       C
ATOM   1333  C   MET D  49     -31.620-119.781 -35.733  1.00131.76           C
ANISOU 1333  C   MET D  49    16833  16108  17123  -1876  -2364  -3884       C
ATOM   1334  O   MET D  49     -32.037-119.429 -34.628  1.00110.88           O
ANISOU 1334  O   MET D  49    14044  13505  14579  -1846  -2378  -3801       O
ATOM   1335  CB  MET D  49     -32.409-121.730 -37.093  1.00160.13           C
ANISOU 1335  CB  MET D  49    20599  19568  20675  -1942  -2543  -3950       C
ATOM   1336  CG  MET D  49     -33.685-122.441 -37.513  1.00175.33           C
ANISOU 1336  CG  MET D  49    22568  21433  22617  -1991  -2722  -3900       C
ATOM   1337  SD  MET D  49     -34.828-122.652 -36.133  1.00188.25           S
ANISOU 1337  SD  MET D  49    24010  23093  24424  -1972  -2835  -3763       S
ATOM   1338  CE  MET D  49     -33.676-123.179 -34.842  1.00136.62           C
ANISOU 1338  CE  MET D  49    17319  16586  18004  -1899  -2699  -3813       C
ATOM   1339  N   THR D  50     -30.327-119.809 -36.048  1.00144.51           N
ANISOU 1339  N   THR D  50    18502  17727  18677  -1856  -2228  -3980       N
ATOM   1340  CA  THR D  50     -29.297-119.283 -35.158  1.00123.26           C
ANISOU 1340  CA  THR D  50    15712  15094  16029  -1804  -2085  -3989       C
ATOM   1341  C   THR D  50     -28.190-118.635 -35.971  1.00116.63           C
ANISOU 1341  C   THR D  50    14980  14272  15061  -1804  -1961  -4060       C
ATOM   1342  O   THR D  50     -27.852-119.100 -37.061  1.00140.04           O
ANISOU 1342  O   THR D  50    18083  17197  17929  -1827  -1956  -4137       O
ATOM   1343  CB  THR D  50     -28.650-120.382 -34.305  1.00139.15           C
ANISOU 1343  CB  THR D  50    17630  17092  18148  -1764  -2029  -4032       C
ATOM   1344  OG1 THR D  50     -27.853-121.233 -35.140  1.00166.90           O
ANISOU 1344  OG1 THR D  50    21262  20559  21595  -1771  -1979  -4139       O
ATOM   1345  CG2 THR D  50     -29.702-121.203 -33.574  1.00146.39           C
ANISOU 1345  CG2 THR D  50    18443  17986  19192  -1765  -2156  -3968       C
ATOM   1346  N   TYR D  51     -27.626-117.557 -35.444  1.00122.24           N
ANISOU 1346  N   TYR D  51    15629  15046  15772  -1777  -1866  -4032       N
ATOM   1347  CA  TYR D  51     -26.549-116.865 -36.132  1.00112.64           C
ANISOU 1347  CA  TYR D  51    14501  13856  14442  -1774  -1749  -4086       C
ATOM   1348  C   TYR D  51     -25.662-116.118 -35.143  1.00116.53           C
ANISOU 1348  C   TYR D  51    14884  14408  14982  -1729  -1626  -4065       C
ATOM   1349  O   TYR D  51     -26.139-115.688 -34.085  1.00101.72           O
ANISOU 1349  O   TYR D  51    12883  12565  13202  -1708  -1650  -3990       O
ATOM   1350  CB  TYR D  51     -27.133-115.901 -37.171  1.00128.07           C
ANISOU 1350  CB  TYR D  51    16563  15819  16281  -1820  -1808  -4059       C
ATOM   1351  CG  TYR D  51     -27.901-114.734 -36.578  1.00140.43           C
ANISOU 1351  CG  TYR D  51    18045  17429  17881  -1821  -1854  -3957       C
ATOM   1352  CD1 TYR D  51     -29.227-114.869 -36.192  1.00124.60           C
ANISOU 1352  CD1 TYR D  51    15984  15412  15946  -1837  -1987  -3878       C
ATOM   1353  CD2 TYR D  51     -27.299-113.496 -36.411  1.00154.94           C
ANISOU 1353  CD2 TYR D  51    19864  19325  19682  -1805  -1768  -3935       C
ATOM   1354  CE1 TYR D  51     -29.930-113.805 -35.657  1.00 89.66           C
ANISOU 1354  CE1 TYR D  51    11486  11029  11550  -1833  -2027  -3782       C
ATOM   1355  CE2 TYR D  51     -27.997-112.426 -35.874  1.00138.15           C
ANISOU 1355  CE2 TYR D  51    17667  17238  17586  -1803  -1812  -3844       C
ATOM   1356  CZ  TYR D  51     -29.311-112.589 -35.501  1.00 97.98           C
ANISOU 1356  CZ  TYR D  51    12527  12137  12566  -1816  -1938  -3769       C
ATOM   1357  OH  TYR D  51     -30.000-111.526 -34.964  1.00119.52           O
ANISOU 1357  OH  TYR D  51    15187  14906  15321  -1808  -1978  -3677       O
ATOM   1358  N   ARG D  52     -24.375-115.980 -35.475  1.00129.91           N
ANISOU 1358  N   ARG D  52    16628  16119  16611  -1712  -1495  -4127       N
ATOM   1359  CA  ARG D  52     -23.455-115.131 -34.695  1.00115.40           C
ANISOU 1359  CA  ARG D  52    14709  14340  14799  -1675  -1375  -4105       C
ATOM   1360  C   ARG D  52     -22.763-114.114 -35.606  1.00109.51           C
ANISOU 1360  C   ARG D  52    14065  13625  13920  -1687  -1307  -4121       C
ATOM   1361  O   ARG D  52     -22.112-114.478 -36.602  1.00105.18           O
ANISOU 1361  O   ARG D  52    13631  13058  13273  -1696  -1260  -4191       O
ATOM   1362  CB  ARG D  52     -22.416-115.959 -33.925  1.00 98.69           C
ANISOU 1362  CB  ARG D  52    12516  12221  12758  -1635  -1266  -4148       C
ATOM   1363  CG  ARG D  52     -22.943-117.277 -33.335  1.00138.52           C
ANISOU 1363  CG  ARG D  52    17490  17223  17916  -1628  -1330  -4158       C
ATOM   1364  CD  ARG D  52     -22.696-117.418 -31.826  1.00115.72           C
ANISOU 1364  CD  ARG D  52    14430  14365  15172  -1587  -1281  -4120       C
ATOM   1365  NE  ARG D  52     -21.290-117.295 -31.451  1.00117.16           N
ANISOU 1365  NE  ARG D  52    14584  14577  15355  -1556  -1125  -4152       N
ATOM   1366  CZ  ARG D  52     -20.879-116.758 -30.304  1.00134.82           C
ANISOU 1366  CZ  ARG D  52    16694  16860  17671  -1525  -1058  -4106       C
ATOM   1367  NH1 ARG D  52     -21.769-116.297 -29.434  1.00139.41           N
ANISOU 1367  NH1 ARG D  52    17170  17464  18336  -1516  -1132  -4029       N
ATOM   1368  NH2 ARG D  52     -19.584-116.673 -30.024  1.00124.98           N
ANISOU 1368  NH2 ARG D  52    15429  15637  16420  -1502   -918  -4133       N
ATOM   1369  N   ARG D  53     -22.918-112.838 -35.269  1.00 99.34           N
ANISOU 1369  N   ARG D  53    12733  12383  12627  -1686  -1305  -4055       N
ATOM   1370  CA  ARG D  53     -22.452-111.765 -36.139  1.00114.47           C
ANISOU 1370  CA  ARG D  53    14740  14332  14421  -1703  -1264  -4056       C
ATOM   1371  C   ARG D  53     -21.679-110.735 -35.348  1.00112.74           C
ANISOU 1371  C   ARG D  53    14441  14168  14228  -1673  -1172  -4014       C
ATOM   1372  O   ARG D  53     -22.200-110.142 -34.400  1.00107.87           O
ANISOU 1372  O   ARG D  53    13722  13573  13689  -1659  -1205  -3946       O
ATOM   1373  CB  ARG D  53     -23.629-111.071 -36.826  1.00116.13           C
ANISOU 1373  CB  ARG D  53    15009  14541  14576  -1748  -1383  -4010       C
ATOM   1374  CG  ARG D  53     -24.218-111.810 -38.005  1.00108.57           C
ANISOU 1374  CG  ARG D  53    14174  13534  13544  -1789  -1465  -4055       C
ATOM   1375  CD  ARG D  53     -25.569-111.216 -38.402  1.00124.55           C
ANISOU 1375  CD  ARG D  53    16225  15554  15547  -1834  -1596  -3992       C
ATOM   1376  NE  ARG D  53     -26.133-111.933 -39.539  1.00116.38           N
ANISOU 1376  NE  ARG D  53    15311  14468  14439  -1878  -1677  -4033       N
ATOM   1377  CZ  ARG D  53     -25.928-111.588 -40.804  1.00121.97           C
ANISOU 1377  CZ  ARG D  53    16147  15178  15017  -1911  -1672  -4069       C
ATOM   1378  NH1 ARG D  53     -25.197-110.516 -41.084  1.00118.55           N
ANISOU 1378  NH1 ARG D  53    15732  14797  14515  -1905  -1592  -4063       N
ATOM   1379  NH2 ARG D  53     -26.460-112.306 -41.786  1.00118.07           N
ANISOU 1379  NH2 ARG D  53    15764  14635  14463  -1949  -1750  -4107       N
ATOM   1380  N   LEU D  54     -20.441-110.508 -35.762  1.00 98.63           N
ANISOU 1380  N   LEU D  54    12702  12402  12369  -1661  -1058  -4052       N
ATOM   1381  CA  LEU D  54     -19.573-109.573 -35.077  1.00121.57           C
ANISOU 1381  CA  LEU D  54    15541  15357  15292  -1634   -966  -4014       C
ATOM   1382  C   LEU D  54     -19.925-108.118 -35.395  1.00109.05           C
ANISOU 1382  C   LEU D  54    13980  13808  13646  -1654  -1005  -3955       C
ATOM   1383  O   LEU D  54     -19.919-107.702 -36.545  1.00 97.29           O
ANISOU 1383  O   LEU D  54    12598  12325  12044  -1684  -1021  -3971       O
ATOM   1384  CB  LEU D  54     -18.128-109.869 -35.456  1.00 73.96           C
ANISOU 1384  CB  LEU D  54     9559   9339   9205  -1616   -834  -4067       C
ATOM   1385  CG  LEU D  54     -17.124-108.912 -34.833  1.00 94.50           C
ANISOU 1385  CG  LEU D  54    12101  11989  11815  -1591   -735  -4024       C
ATOM   1386  CD1 LEU D  54     -17.282-108.922 -33.324  1.00 80.69           C
ANISOU 1386  CD1 LEU D  54    10206  10247  10206  -1563   -730  -3980       C
ATOM   1387  CD2 LEU D  54     -15.713-109.300 -35.232  1.00119.36           C
ANISOU 1387  CD2 LEU D  54    15296  15149  14907  -1573   -606  -4070       C
ATOM   1388  N   ILE D  55     -20.216-107.334 -34.372  1.00 72.70           N
ANISOU 1388  N   ILE D  55     9275   9230   9117  -1637  -1020  -3888       N
ATOM   1389  CA  ILE D  55     -20.572-105.943 -34.593  1.00100.62           C
ANISOU 1389  CA  ILE D  55    12829  12799  12604  -1653  -1059  -3830       C
ATOM   1390  C   ILE D  55     -19.424-105.012 -34.209  1.00102.68           C
ANISOU 1390  C   ILE D  55    13061  13103  12850  -1630   -959  -3807       C
ATOM   1391  O   ILE D  55     -18.909-105.070 -33.096  1.00124.77           O
ANISOU 1391  O   ILE D  55    15762  15911  15735  -1594   -900  -3789       O
ATOM   1392  CB  ILE D  55     -21.850-105.564 -33.818  1.00 99.51           C
ANISOU 1392  CB  ILE D  55    12609  12657  12544  -1650  -1163  -3762       C
ATOM   1393  CG1 ILE D  55     -23.094-106.078 -34.546  1.00 75.18           C
ANISOU 1393  CG1 ILE D  55     9585   9540   9439  -1688  -1282  -3766       C
ATOM   1394  CG2 ILE D  55     -21.960-104.051 -33.639  1.00 96.67           C
ANISOU 1394  CG2 ILE D  55    12233  12336  12160  -1649  -1177  -3696       C
ATOM   1395  CD1 ILE D  55     -23.055-107.547 -34.843  1.00 77.58           C
ANISOU 1395  CD1 ILE D  55     9919   9800   9757  -1692  -1284  -3832       C
ATOM   1396  N   SER D  56     -19.025-104.148 -35.136  1.00107.60           N
ANISOU 1396  N   SER D  56    13767  13752  13365  -1653   -943  -3802       N
ATOM   1397  CA  SER D  56     -17.878-103.264 -34.926  1.00118.79           C
ANISOU 1397  CA  SER D  56    15169  15210  14756  -1636   -852  -3777       C
ATOM   1398  C   SER D  56     -18.147-102.219 -33.858  1.00108.65           C
ANISOU 1398  C   SER D  56    13794  13948  13542  -1617   -875  -3704       C
ATOM   1399  O   SER D  56     -19.212-101.606 -33.830  1.00122.36           O
ANISOU 1399  O   SER D  56    15523  15683  15284  -1631   -970  -3663       O
ATOM   1400  CB  SER D  56     -17.467-102.584 -36.239  1.00132.72           C
ANISOU 1400  CB  SER D  56    17042  16999  16385  -1666   -842  -3785       C
ATOM   1401  OG  SER D  56     -16.312-101.777 -36.059  1.00111.48           O
ANISOU 1401  OG  SER D  56    14338  14348  13671  -1650   -755  -3756       O
ATOM   1402  N   MET D  57     -17.196-102.043 -32.951  1.00102.37           N
ANISOU 1402  N   MET D  57    12928  13169  12799  -1584   -789  -3687       N
ATOM   1403  CA  MET D  57     -17.316-100.978 -31.959  1.00110.31           C
ANISOU 1403  CA  MET D  57    13857  14196  13861  -1563   -804  -3619       C
ATOM   1404  C   MET D  57     -16.556 -99.695 -32.299  1.00118.29           C
ANISOU 1404  C   MET D  57    14903  15243  14800  -1572   -770  -3581       C
ATOM   1405  O   MET D  57     -16.393 -98.831 -31.430  1.00101.94           O
ANISOU 1405  O   MET D  57    12771  13188  12774  -1551   -766  -3528       O
ATOM   1406  CB  MET D  57     -17.032-101.468 -30.544  1.00 95.55           C
ANISOU 1406  CB  MET D  57    11870  12320  12113  -1522   -757  -3609       C
ATOM   1407  CG  MET D  57     -18.234-101.327 -29.633  1.00 76.40           C
ANISOU 1407  CG  MET D  57     9364   9886   9777  -1503   -846  -3567       C
ATOM   1408  SD  MET D  57     -19.679-102.223 -30.238  1.00119.47           S
ANISOU 1408  SD  MET D  57    14852  15308  15233  -1527   -959  -3592       S
ATOM   1409  CE  MET D  57     -20.924-101.800 -28.989  1.00 91.61           C
ANISOU 1409  CE  MET D  57    11212  11783  11812  -1493  -1050  -3520       C
ATOM   1410  N   MET D  58     -16.038 -99.615 -33.531  1.00110.94           N
ANISOU 1410  N   MET D  58    14070  14325  13759  -1600   -744  -3607       N
ATOM   1411  CA  MET D  58     -15.143 -98.531 -33.943  1.00128.41           C
ANISOU 1411  CA  MET D  58    16317  16575  15899  -1607   -702  -3573       C
ATOM   1412  C   MET D  58     -15.832 -97.182 -34.251  1.00142.34           C
ANISOU 1412  C   MET D  58    18103  18358  17623  -1630   -789  -3519       C
ATOM   1413  O   MET D  58     -16.974 -97.132 -34.720  1.00 80.60           O
ANISOU 1413  O   MET D  58    10313  10525   9784  -1654   -881  -3521       O
ATOM   1414  CB  MET D  58     -14.269 -99.000 -35.101  1.00 71.34           C
ANISOU 1414  CB  MET D  58     9177   9358   8570  -1622   -636  -3618       C
ATOM   1415  CG  MET D  58     -13.815-100.445 -34.910  1.00168.78           C
ANISOU 1415  CG  MET D  58    21507  21673  20947  -1602   -565  -3678       C
ATOM   1416  SD  MET D  58     -12.324-100.992 -35.792  1.00110.01           S
ANISOU 1416  SD  MET D  58    14136  14251  13412  -1595   -442  -3716       S
ATOM   1417  CE  MET D  58     -11.116 -99.767 -35.271  1.00125.86           C
ANISOU 1417  CE  MET D  58    16101  16305  15416  -1581   -370  -3639       C
ATOM   1418  N   GLY D  59     -15.137 -96.081 -33.957  1.00169.81           N
ANISOU 1418  N   GLY D  59    21564  21866  21091  -1623   -762  -3467       N
ATOM   1419  CA  GLY D  59     -15.635 -94.765 -34.331  1.00156.61           C
ANISOU 1419  CA  GLY D  59    19918  20214  19373  -1645   -836  -3417       C
ATOM   1420  C   GLY D  59     -16.888 -94.305 -33.616  1.00133.00           C
ANISOU 1420  C   GLY D  59    16877  17207  16448  -1637   -931  -3381       C
ATOM   1421  O   GLY D  59     -17.942 -94.185 -34.246  1.00119.94           O
ANISOU 1421  O   GLY D  59    15262  15547  14762  -1665  -1014  -3382       O
ATOM   1422  N   PHE D  60     -16.807 -94.130 -32.300  1.00111.87           N
ANISOU 1422  N   PHE D  60    14115  14524  13865  -1597   -917  -3350       N
ATOM   1423  CA  PHE D  60     -18.012 -93.865 -31.497  1.00128.30           C
ANISOU 1423  CA  PHE D  60    16140  16590  16018  -1577  -1001  -3317       C
ATOM   1424  C   PHE D  60     -18.636 -92.456 -31.563  1.00122.29           C
ANISOU 1424  C   PHE D  60    15391  15843  15231  -1586  -1081  -3258       C
ATOM   1425  O   PHE D  60     -19.818 -92.293 -31.270  1.00113.21           O
ANISOU 1425  O   PHE D  60    14218  14682  14114  -1579  -1162  -3234       O
ATOM   1426  CB  PHE D  60     -17.784 -94.273 -30.045  1.00153.66           C
ANISOU 1426  CB  PHE D  60    19252  19790  19342  -1527   -961  -3309       C
ATOM   1427  CG  PHE D  60     -18.396 -95.595 -29.687  1.00132.29           C
ANISOU 1427  CG  PHE D  60    16504  17058  16702  -1514   -969  -3347       C
ATOM   1428  CD1 PHE D  60     -19.777 -95.734 -29.599  1.00132.05           C
ANISOU 1428  CD1 PHE D  60    16457  17014  16701  -1513  -1064  -3333       C
ATOM   1429  CD2 PHE D  60     -17.595 -96.697 -29.427  1.00112.19           C
ANISOU 1429  CD2 PHE D  60    13932  14503  14192  -1502   -883  -3392       C
ATOM   1430  CE1 PHE D  60     -20.346 -96.950 -29.266  1.00143.34           C
ANISOU 1430  CE1 PHE D  60    17845  18421  18195  -1502  -1079  -3362       C
ATOM   1431  CE2 PHE D  60     -18.161 -97.915 -29.094  1.00144.40           C
ANISOU 1431  CE2 PHE D  60    17971  18559  18337  -1491   -895  -3426       C
ATOM   1432  CZ  PHE D  60     -19.537 -98.040 -29.014  1.00162.73           C
ANISOU 1432  CZ  PHE D  60    20275  20867  20688  -1491   -996  -3410       C
ATOM   1433  N   LYS D  61     -17.843 -91.441 -31.891  1.00135.55           N
ANISOU 1433  N   LYS D  61    17101  17546  16854  -1598  -1059  -3229       N
ATOM   1434  CA  LYS D  61     -18.393 -90.135 -32.275  1.00171.71           C
ANISOU 1434  CA  LYS D  61    21711  22141  21389  -1617  -1136  -3179       C
ATOM   1435  C   LYS D  61     -19.463 -89.545 -31.345  1.00181.62           C
ANISOU 1435  C   LYS D  61    22913  23385  22711  -1587  -1214  -3133       C
ATOM   1436  O   LYS D  61     -20.571 -89.268 -31.805  1.00195.18           O
ANISOU 1436  O   LYS D  61    24653  25099  24405  -1607  -1295  -3118       O
ATOM   1437  CB  LYS D  61     -18.952 -90.207 -33.704  1.00174.33           C
ANISOU 1437  CB  LYS D  61    22125  22482  21631  -1671  -1183  -3201       C
ATOM   1438  CG  LYS D  61     -18.256 -89.287 -34.695  1.00163.41           C
ANISOU 1438  CG  LYS D  61    20803  21132  20153  -1706  -1174  -3183       C
ATOM   1439  CD  LYS D  61     -19.094 -88.061 -35.006  1.00146.95           C
ANISOU 1439  CD  LYS D  61    18736  19059  18039  -1729  -1266  -3132       C
ATOM   1440  CE  LYS D  61     -18.238 -86.964 -35.628  1.00169.40           C
ANISOU 1440  CE  LYS D  61    21615  21937  20811  -1752  -1254  -3099       C
ATOM   1441  NZ  LYS D  61     -17.269 -86.384 -34.649  1.00168.14           N
ANISOU 1441  NZ  LYS D  61    21407  21780  20696  -1715  -1210  -3063       N
ATOM   1442  N   MET D  62     -19.165 -89.362 -30.058  1.00173.86           N
ANISOU 1442  N   MET D  62    21857  22393  21807  -1537  -1189  -3109       N
ATOM   1443  CA  MET D  62     -20.193 -88.851 -29.139  1.00181.21           C
ANISOU 1443  CA  MET D  62    22737  23315  22800  -1499  -1261  -3065       C
ATOM   1444  C   MET D  62     -20.193 -87.342 -28.952  1.00173.33           C
ANISOU 1444  C   MET D  62    21749  22328  21782  -1492  -1305  -3007       C
ATOM   1445  O   MET D  62     -19.332 -86.785 -28.268  1.00117.26           O
ANISOU 1445  O   MET D  62    14623  15228  14702  -1467  -1267  -2985       O
ATOM   1446  CB  MET D  62     -20.031 -89.481 -27.773  1.00140.49           C
ANISOU 1446  CB  MET D  62    17490  18143  17745  -1444  -1220  -3068       C
ATOM   1447  CG  MET D  62     -18.601 -89.623 -27.367  1.00 95.98           C
ANISOU 1447  CG  MET D  62    11836  12511  12123  -1434  -1123  -3081       C
ATOM   1448  SD  MET D  62     -18.493 -91.269 -26.704  1.00180.83           S
ANISOU 1448  SD  MET D  62    22514  23241  22952  -1409  -1060  -3131       S
ATOM   1449  CE  MET D  62     -20.130 -91.436 -25.997  1.00 88.35           C
ANISOU 1449  CE  MET D  62    10742  11517  11310  -1372  -1156  -3106       C
ATOM   1450  N   ASN D  63     -21.204 -86.702 -29.528  1.00176.18           N
ANISOU 1450  N   ASN D  63    22145  22693  22104  -1514  -1389  -2980       N
ATOM   1451  CA  ASN D  63     -21.341 -85.260 -29.477  1.00143.22           C
ANISOU 1451  CA  ASN D  63    17986  18527  17903  -1511  -1443  -2925       C
ATOM   1452  C   ASN D  63     -22.332 -84.820 -28.415  1.00123.06           C
ANISOU 1452  C   ASN D  63    15381  15962  15416  -1457  -1504  -2881       C
ATOM   1453  O   ASN D  63     -22.534 -83.621 -28.218  1.00115.78           O
ANISOU 1453  O   ASN D  63    14467  15042  14481  -1444  -1552  -2834       O
ATOM   1454  CB  ASN D  63     -21.820 -84.728 -30.835  1.00158.62           C
ANISOU 1454  CB  ASN D  63    20009  20494  19765  -1571  -1497  -2917       C
ATOM   1455  CG  ASN D  63     -20.825 -84.983 -31.969  1.00171.34           C
ANISOU 1455  CG  ASN D  63    21679  22124  21299  -1622  -1442  -2954       C
ATOM   1456  OD1 ASN D  63     -19.834 -85.692 -31.809  1.00192.43           O
ANISOU 1456  OD1 ASN D  63    24339  24794  23981  -1614  -1361  -2988       O
ATOM   1457  ND2 ASN D  63     -21.106 -84.404 -33.131  1.00168.54           N
ANISOU 1457  ND2 ASN D  63    21385  21789  20865  -1674  -1486  -2943       N
ATOM   1458  N   TYR D  64     -22.950 -85.776 -27.726  1.00141.19           N
ANISOU 1458  N   TYR D  64    17621  18245  17781  -1422  -1503  -2894       N
ATOM   1459  CA  TYR D  64     -24.216 -85.508 -27.025  1.00154.29           C
ANISOU 1459  CA  TYR D  64    19238  19898  19487  -1378  -1577  -2850       C
ATOM   1460  C   TYR D  64     -24.159 -84.278 -26.139  1.00163.44           C
ANISOU 1460  C   TYR D  64    20376  21056  20667  -1329  -1603  -2799       C
ATOM   1461  O   TYR D  64     -23.295 -84.168 -25.272  1.00194.55           O
ANISOU 1461  O   TYR D  64    24282  24992  24648  -1292  -1553  -2801       O
ATOM   1462  CB  TYR D  64     -24.620 -86.710 -26.170  1.00152.22           C
ANISOU 1462  CB  TYR D  64    18901  19626  19309  -1335  -1560  -2866       C
ATOM   1463  CG  TYR D  64     -23.552 -87.141 -25.193  1.00163.04           C
ANISOU 1463  CG  TYR D  64    20216  20992  20740  -1297  -1478  -2890       C
ATOM   1464  CD1 TYR D  64     -22.420 -87.831 -25.628  1.00149.83           C
ANISOU 1464  CD1 TYR D  64    18562  19318  19048  -1331  -1395  -2941       C
ATOM   1465  CD2 TYR D  64     -23.668 -86.856 -23.839  1.00172.25           C
ANISOU 1465  CD2 TYR D  64    21312  22156  21981  -1227  -1481  -2858       C
ATOM   1466  CE1 TYR D  64     -21.442 -88.227 -24.744  1.00152.73           C
ANISOU 1466  CE1 TYR D  64    18878  19683  19472  -1300  -1317  -2958       C
ATOM   1467  CE2 TYR D  64     -22.690 -87.252 -22.941  1.00178.16           C
ANISOU 1467  CE2 TYR D  64    22007  22900  22785  -1196  -1405  -2877       C
ATOM   1468  CZ  TYR D  64     -21.581 -87.935 -23.400  1.00173.07           C
ANISOU 1468  CZ  TYR D  64    21381  22254  22123  -1235  -1323  -2926       C
ATOM   1469  OH  TYR D  64     -20.612 -88.324 -22.508  1.00174.54           O
ANISOU 1469  OH  TYR D  64    21513  22437  22366  -1207  -1246  -2939       O
ATOM   1470  N   GLN D  65     -25.094 -83.360 -26.346  1.00147.11           N
ANISOU 1470  N   GLN D  65    18331  18992  18573  -1327  -1683  -2752       N
ATOM   1471  CA  GLN D  65     -25.104 -82.131 -25.563  1.00165.26           C
ANISOU 1471  CA  GLN D  65    20618  21287  20885  -1279  -1716  -2703       C
ATOM   1472  C   GLN D  65     -26.079 -82.204 -24.386  1.00153.20           C
ANISOU 1472  C   GLN D  65    19025  19755  19431  -1202  -1754  -2667       C
ATOM   1473  O   GLN D  65     -26.218 -81.242 -23.628  1.00158.18           O
ANISOU 1473  O   GLN D  65    19644  20380  20077  -1150  -1786  -2626       O
ATOM   1474  CB  GLN D  65     -25.397 -80.916 -26.455  1.00170.57           C
ANISOU 1474  CB  GLN D  65    21357  21968  21484  -1320  -1776  -2669       C
ATOM   1475  CG  GLN D  65     -24.429 -79.752 -26.251  1.00192.62           C
ANISOU 1475  CG  GLN D  65    24174  24758  24256  -1315  -1769  -2651       C
ATOM   1476  CD  GLN D  65     -22.965 -80.146 -26.448  1.00184.40           C
ANISOU 1476  CD  GLN D  65    23142  23719  23203  -1343  -1685  -2690       C
ATOM   1477  OE1 GLN D  65     -22.657 -81.068 -27.202  1.00177.46           O
ANISOU 1477  OE1 GLN D  65    22278  22849  22299  -1388  -1641  -2733       O
ATOM   1478  NE2 GLN D  65     -22.059 -79.447 -25.761  1.00145.59           N
ANISOU 1478  NE2 GLN D  65    18220  18795  18303  -1316  -1665  -2672       N
ATOM   1479  N   VAL D  66     -26.721 -83.359 -24.223  1.00136.55           N
ANISOU 1479  N   VAL D  66    16873  17647  17365  -1191  -1752  -2681       N
ATOM   1480  CA  VAL D  66     -27.838 -83.506 -23.290  1.00158.70           C
ANISOU 1480  CA  VAL D  66    19614  20454  20231  -1122  -1799  -2637       C
ATOM   1481  C   VAL D  66     -27.566 -82.990 -21.871  1.00155.70           C
ANISOU 1481  C   VAL D  66    19179  20070  19910  -1038  -1787  -2613       C
ATOM   1482  O   VAL D  66     -26.499 -83.199 -21.305  1.00130.78           O
ANISOU 1482  O   VAL D  66    15999  16907  16784  -1024  -1721  -2643       O
ATOM   1483  CB  VAL D  66     -28.334 -84.970 -23.232  1.00173.45           C
ANISOU 1483  CB  VAL D  66    21433  22324  22147  -1123  -1788  -2660       C
ATOM   1484  CG1 VAL D  66     -27.152 -85.931 -23.227  1.00192.37           C
ANISOU 1484  CG1 VAL D  66    23815  24713  24563  -1146  -1699  -2726       C
ATOM   1485  CG2 VAL D  66     -29.239 -85.195 -22.020  1.00153.47           C
ANISOU 1485  CG2 VAL D  66    18818  19799  19694  -1039  -1822  -2614       C
ATOM   1486  N   ASN D  67     -28.559 -82.311 -21.311  1.00177.34           N
ANISOU 1486  N   ASN D  67    21902  22815  22665   -980  -1853  -2554       N
ATOM   1487  CA  ASN D  67     -28.464 -81.730 -19.979  1.00184.59           C
ANISOU 1487  CA  ASN D  67    22775  23730  23633   -893  -1854  -2526       C
ATOM   1488  C   ASN D  67     -28.409 -82.791 -18.882  1.00179.00           C
ANISOU 1488  C   ASN D  67    21973  23027  23011   -836  -1812  -2539       C
ATOM   1489  O   ASN D  67     -29.048 -83.846 -18.990  1.00158.21           O
ANISOU 1489  O   ASN D  67    19299  20405  20410   -841  -1818  -2543       O
ATOM   1490  CB  ASN D  67     -29.646 -80.781 -19.741  1.00203.46           C
ANISOU 1490  CB  ASN D  67    25171  26124  26008   -843  -1937  -2457       C
ATOM   1491  CG  ASN D  67     -29.686 -80.230 -18.326  1.00208.69           C
ANISOU 1491  CG  ASN D  67    25787  26785  26721   -742  -1944  -2425       C
ATOM   1492  OD1 ASN D  67     -28.661 -80.148 -17.646  1.00228.81           O
ANISOU 1492  OD1 ASN D  67    28319  29322  29296   -720  -1893  -2452       O
ATOM   1493  ND2 ASN D  67     -30.877 -79.847 -17.878  1.00173.97           N
ANISOU 1493  ND2 ASN D  67    21368  22399  22335   -678  -2007  -2365       N
ATOM   1494  N   GLY D  68     -27.645 -82.498 -17.830  1.00178.07           N
ANISOU 1494  N   GLY D  68    21822  22903  22935   -783  -1773  -2544       N
ATOM   1495  CA  GLY D  68     -27.484 -83.403 -16.705  1.00163.39           C
ANISOU 1495  CA  GLY D  68    19869  21051  21161   -727  -1729  -2556       C
ATOM   1496  C   GLY D  68     -26.235 -84.253 -16.858  1.00160.71           C
ANISOU 1496  C   GLY D  68    19520  20704  20839   -776  -1640  -2618       C
ATOM   1497  O   GLY D  68     -25.854 -85.006 -15.954  1.00153.54           O
ANISOU 1497  O   GLY D  68    18536  19801  20003   -740  -1590  -2635       O
ATOM   1498  N   TYR D  69     -25.587 -84.120 -18.011  1.00146.85           N
ANISOU 1498  N   TYR D  69    17840  18941  19017   -857  -1619  -2649       N
ATOM   1499  CA  TYR D  69     -24.464 -84.977 -18.339  1.00140.61           C
ANISOU 1499  CA  TYR D  69    17048  18145  18232   -908  -1535  -2706       C
ATOM   1500  C   TYR D  69     -23.211 -84.170 -18.652  1.00142.66           C
ANISOU 1500  C   TYR D  69    17368  18393  18443   -944  -1497  -2716       C
ATOM   1501  O   TYR D  69     -23.264 -83.155 -19.344  1.00129.68           O
ANISOU 1501  O   TYR D  69    15796  16745  16731   -973  -1540  -2696       O
ATOM   1502  CB  TYR D  69     -24.838 -85.884 -19.523  1.00149.38           C
ANISOU 1502  CB  TYR D  69    18188  19260  19309   -975  -1539  -2737       C
ATOM   1503  CG  TYR D  69     -25.913 -86.908 -19.182  1.00146.50           C
ANISOU 1503  CG  TYR D  69    17755  18906  19003   -945  -1568  -2729       C
ATOM   1504  CD1 TYR D  69     -25.633 -87.954 -18.315  1.00166.77           C
ANISOU 1504  CD1 TYR D  69    20236  21476  21652   -911  -1518  -2750       C
ATOM   1505  CD2 TYR D  69     -27.204 -86.830 -19.721  1.00116.45           C
ANISOU 1505  CD2 TYR D  69    13968  15106  15172   -951  -1649  -2694       C
ATOM   1506  CE1 TYR D  69     -26.595 -88.895 -17.984  1.00161.12           C
ANISOU 1506  CE1 TYR D  69    19453  20772  20994   -884  -1549  -2738       C
ATOM   1507  CE2 TYR D  69     -28.177 -87.776 -19.392  1.00138.71           C
ANISOU 1507  CE2 TYR D  69    16722  17935  18046   -924  -1681  -2677       C
ATOM   1508  CZ  TYR D  69     -27.860 -88.808 -18.519  1.00143.01           C
ANISOU 1508  CZ  TYR D  69    17179  18484  18674   -889  -1632  -2699       C
ATOM   1509  OH  TYR D  69     -28.782 -89.766 -18.153  1.00103.06           O
ANISOU 1509  OH  TYR D  69    12047  13435  13675   -861  -1666  -2679       O
ATOM   1510  N   PRO D  70     -22.074 -84.628 -18.117  1.00150.37           N
ANISOU 1510  N   PRO D  70    18312  19365  19457   -943  -1416  -2743       N
ATOM   1511  CA  PRO D  70     -20.733 -84.072 -18.312  1.00127.54           C
ANISOU 1511  CA  PRO D  70    15465  16463  16531   -978  -1366  -2750       C
ATOM   1512  C   PRO D  70     -20.191 -84.460 -19.672  1.00129.89           C
ANISOU 1512  C   PRO D  70    15823  16766  16762  -1059  -1333  -2785       C
ATOM   1513  O   PRO D  70     -20.352 -85.609 -20.081  1.00139.10           O
ANISOU 1513  O   PRO D  70    16972  17939  17940  -1083  -1302  -2824       O
ATOM   1514  CB  PRO D  70     -19.925 -84.763 -17.223  1.00142.64           C
ANISOU 1514  CB  PRO D  70    17303  18373  18521   -946  -1289  -2766       C
ATOM   1515  CG  PRO D  70     -20.620 -86.076 -17.023  1.00143.11           C
ANISOU 1515  CG  PRO D  70    17293  18444  18638   -931  -1277  -2792       C
ATOM   1516  CD  PRO D  70     -22.072 -85.788 -17.208  1.00148.00           C
ANISOU 1516  CD  PRO D  70    17918  19070  19244   -906  -1369  -2763       C
ATOM   1517  N   ASN D  71     -19.532 -83.535 -20.356  1.00120.44           N
ANISOU 1517  N   ASN D  71    14698  15567  15497  -1100  -1339  -2771       N
ATOM   1518  CA  ASN D  71     -19.059 -83.818 -21.705  1.00144.94           C
ANISOU 1518  CA  ASN D  71    17862  18681  18529  -1173  -1312  -2800       C
ATOM   1519  C   ASN D  71     -17.720 -84.530 -21.655  1.00134.12           C
ANISOU 1519  C   ASN D  71    16477  17310  17170  -1196  -1211  -2829       C
ATOM   1520  O   ASN D  71     -16.757 -83.991 -21.122  1.00151.97           O
ANISOU 1520  O   ASN D  71    18735  19565  19441  -1186  -1179  -2807       O
ATOM   1521  CB  ASN D  71     -18.962 -82.530 -22.535  1.00167.01           C
ANISOU 1521  CB  ASN D  71    20734  21479  21243  -1209  -1366  -2768       C
ATOM   1522  CG  ASN D  71     -20.293 -81.786 -22.629  1.00171.90           C
ANISOU 1522  CG  ASN D  71    21369  22097  21847  -1190  -1464  -2735       C
ATOM   1523  OD1 ASN D  71     -21.125 -81.862 -21.725  1.00185.30           O
ANISOU 1523  OD1 ASN D  71    23017  23788  23600  -1131  -1497  -2719       O
ATOM   1524  ND2 ASN D  71     -20.494 -81.063 -23.727  1.00151.13           N
ANISOU 1524  ND2 ASN D  71    18806  19476  19140  -1238  -1511  -2721       N
ATOM   1525  N   MET D  72     -17.650 -85.732 -22.223  1.00132.08           N
ANISOU 1525  N   MET D  72    16214  17059  16910  -1225  -1163  -2877       N
ATOM   1526  CA  MET D  72     -16.429 -86.543 -22.115  1.00148.51           C
ANISOU 1526  CA  MET D  72    18275  19142  19010  -1241  -1061  -2905       C
ATOM   1527  C   MET D  72     -15.201 -85.845 -22.689  1.00154.57           C
ANISOU 1527  C   MET D  72    19100  19917  19714  -1280  -1025  -2886       C
ATOM   1528  O   MET D  72     -14.066 -86.250 -22.423  1.00132.89           O
ANISOU 1528  O   MET D  72    16336  17172  16985  -1286   -941  -2891       O
ATOM   1529  CB  MET D  72     -16.585 -87.916 -22.780  1.00120.14           C
ANISOU 1529  CB  MET D  72    14681  15553  15414  -1269  -1022  -2962       C
ATOM   1530  CG  MET D  72     -17.784 -88.715 -22.306  1.00129.60           C
ANISOU 1530  CG  MET D  72    15822  16746  16675  -1236  -1061  -2978       C
ATOM   1531  SD  MET D  72     -17.556 -90.496 -22.465  1.00143.60           S
ANISOU 1531  SD  MET D  72    17559  18516  18487  -1251   -987  -3042       S
ATOM   1532  CE  MET D  72     -16.148 -90.594 -23.558  1.00114.84           C
ANISOU 1532  CE  MET D  72    13990  14881  14761  -1308   -904  -3069       C
ATOM   1533  N   PHE D  73     -15.423 -84.799 -23.474  1.00154.92           N
ANISOU 1533  N   PHE D  73    19209  19968  19687  -1306  -1088  -2859       N
ATOM   1534  CA  PHE D  73     -14.302 -84.030 -23.992  1.00145.54           C
ANISOU 1534  CA  PHE D  73    18070  18789  18440  -1340  -1065  -2829       C
ATOM   1535  C   PHE D  73     -14.343 -82.592 -23.502  1.00153.61           C
ANISOU 1535  C   PHE D  73    19106  19801  19459  -1320  -1132  -2771       C
ATOM   1536  O   PHE D  73     -15.428 -82.018 -23.315  1.00163.34           O
ANISOU 1536  O   PHE D  73    20339  21025  20697  -1296  -1214  -2757       O
ATOM   1537  CB  PHE D  73     -14.246 -84.119 -25.513  1.00129.20           C
ANISOU 1537  CB  PHE D  73    16070  16742  16279  -1398  -1068  -2849       C
ATOM   1538  CG  PHE D  73     -13.795 -85.462 -26.013  1.00130.11           C
ANISOU 1538  CG  PHE D  73    16183  16866  16387  -1419   -986  -2902       C
ATOM   1539  CD1 PHE D  73     -14.695 -86.512 -26.124  1.00116.21           C
ANISOU 1539  CD1 PHE D  73    14404  15099  14651  -1414   -992  -2951       C
ATOM   1540  CD2 PHE D  73     -12.462 -85.686 -26.355  1.00125.04           C
ANISOU 1540  CD2 PHE D  73    15557  16237  15714  -1442   -903  -2899       C
ATOM   1541  CE1 PHE D  73     -14.275 -87.767 -26.580  1.00115.70           C
ANISOU 1541  CE1 PHE D  73    14341  15038  14580  -1432   -919  -3002       C
ATOM   1542  CE2 PHE D  73     -12.036 -86.938 -26.817  1.00 89.64           C
ANISOU 1542  CE2 PHE D  73    11076  11761  11222  -1457   -824  -2950       C
ATOM   1543  CZ  PHE D  73     -12.942 -87.979 -26.926  1.00 79.56           C
ANISOU 1543  CZ  PHE D  73     9784  10474   9970  -1451   -833  -3004       C
ATOM   1544  N   ILE D  74     -13.157 -82.025 -23.284  1.00123.34           N
ANISOU 1544  N   ILE D  74    15282  15966  15616  -1328  -1099  -2735       N
ATOM   1545  CA  ILE D  74     -13.036 -80.736 -22.616  1.00141.50           C
ANISOU 1545  CA  ILE D  74    17590  18250  17926  -1304  -1156  -2680       C
ATOM   1546  C   ILE D  74     -12.013 -79.847 -23.299  1.00151.12           C
ANISOU 1546  C   ILE D  74    18861  19478  19078  -1347  -1160  -2635       C
ATOM   1547  O   ILE D  74     -11.028 -80.336 -23.862  1.00163.92           O
ANISOU 1547  O   ILE D  74    20494  21119  20671  -1382  -1088  -2639       O
ATOM   1548  CB  ILE D  74     -12.594 -80.919 -21.158  1.00165.02           C
ANISOU 1548  CB  ILE D  74    20506  21205  20988  -1255  -1117  -2668       C
ATOM   1549  CG1 ILE D  74     -11.377 -81.855 -21.099  1.00172.35           C
ANISOU 1549  CG1 ILE D  74    21409  22143  21934  -1276  -1006  -2682       C
ATOM   1550  CG2 ILE D  74     -13.742 -81.447 -20.310  1.00157.58           C
ANISOU 1550  CG2 ILE D  74    19507  20253  20114  -1200  -1141  -2695       C
ATOM   1551  CD1 ILE D  74     -10.768 -82.031 -19.720  1.00139.23           C
ANISOU 1551  CD1 ILE D  74    17154  17929  17820  -1238   -958  -2666       C
ATOM   1552  N   THR D  75     -12.232 -78.539 -23.206  1.00144.49           N
ANISOU 1552  N   THR D  75    18051  18628  18219  -1340  -1243  -2588       N
ATOM   1553  CA  THR D  75     -11.359 -77.560 -23.847  1.00165.80           C
ANISOU 1553  CA  THR D  75    20800  21338  20859  -1380  -1264  -2537       C
ATOM   1554  C   THR D  75      -9.946 -77.651 -23.269  1.00143.58           C
ANISOU 1554  C   THR D  75    17968  18518  18069  -1382  -1195  -2504       C
ATOM   1555  O   THR D  75      -9.757 -78.184 -22.181  1.00169.05           O
ANISOU 1555  O   THR D  75    21143  21722  21364  -1345  -1149  -2514       O
ATOM   1556  CB  THR D  75     -11.924 -76.127 -23.699  1.00174.84           C
ANISOU 1556  CB  THR D  75    21976  22466  21990  -1366  -1374  -2493       C
ATOM   1557  OG1 THR D  75     -10.905 -75.246 -23.204  1.00193.39           O
ANISOU 1557  OG1 THR D  75    24337  24799  24344  -1365  -1386  -2433       O
ATOM   1558  CG2 THR D  75     -13.136 -76.115 -22.745  1.00129.62           C
ANISOU 1558  CG2 THR D  75    16217  16713  16320  -1305  -1421  -2510       C
ATOM   1559  N   ARG D  76      -8.953 -77.169 -24.009  1.00126.07           N
ANISOU 1559  N   ARG D  76    15786  16319  15794  -1426  -1185  -2461       N
ATOM   1560  CA  ARG D  76      -7.563 -77.280 -23.566  1.00166.46           C
ANISOU 1560  CA  ARG D  76    20887  21432  20926  -1433  -1116  -2420       C
ATOM   1561  C   ARG D  76      -7.329 -76.548 -22.241  1.00175.79           C
ANISOU 1561  C   ARG D  76    22049  22574  22168  -1395  -1150  -2377       C
ATOM   1562  O   ARG D  76      -6.513 -76.975 -21.420  1.00131.20           O
ANISOU 1562  O   ARG D  76    16367  16914  16569  -1384  -1083  -2362       O
ATOM   1563  CB  ARG D  76      -6.584 -76.790 -24.646  1.00173.79           C
ANISOU 1563  CB  ARG D  76    21860  22394  21779  -1485  -1111  -2370       C
ATOM   1564  CG  ARG D  76      -6.563 -75.280 -24.856  1.00181.52           C
ANISOU 1564  CG  ARG D  76    22878  23367  22724  -1498  -1214  -2305       C
ATOM   1565  CD  ARG D  76      -5.142 -74.730 -24.791  1.00176.75           C
ANISOU 1565  CD  ARG D  76    22284  22767  22105  -1521  -1197  -2223       C
ATOM   1566  NE  ARG D  76      -4.285 -75.236 -25.865  1.00186.09           N
ANISOU 1566  NE  ARG D  76    23479  23998  23228  -1563  -1128  -2210       N
ATOM   1567  CZ  ARG D  76      -2.953 -75.226 -25.829  1.00192.73           C
ANISOU 1567  CZ  ARG D  76    24317  24852  24060  -1581  -1075  -2147       C
ATOM   1568  NH1 ARG D  76      -2.253 -75.708 -26.849  1.00163.19           N
ANISOU 1568  NH1 ARG D  76    20587  21157  20259  -1612  -1013  -2136       N
ATOM   1569  NH2 ARG D  76      -2.316 -74.742 -24.768  1.00201.57           N
ANISOU 1569  NH2 ARG D  76    25421  25937  25230  -1567  -1084  -2090       N
ATOM   1570  N   GLU D  77      -8.055 -75.453 -22.032  1.00200.89           N
ANISOU 1570  N   GLU D  77    25253  25732  25343  -1376  -1253  -2356       N
ATOM   1571  CA  GLU D  77      -7.938 -74.693 -20.792  1.00229.90           C
ANISOU 1571  CA  GLU D  77    28918  29365  29069  -1335  -1297  -2318       C
ATOM   1572  C   GLU D  77      -8.498 -75.486 -19.611  1.00220.17           C
ANISOU 1572  C   GLU D  77    27627  28111  27916  -1278  -1260  -2363       C
ATOM   1573  O   GLU D  77      -7.955 -75.440 -18.502  1.00205.88           O
ANISOU 1573  O   GLU D  77    25789  26275  26161  -1250  -1238  -2340       O
ATOM   1574  CB  GLU D  77      -8.635 -73.333 -20.926  1.00247.79           C
ANISOU 1574  CB  GLU D  77    31229  31614  31306  -1325  -1419  -2288       C
ATOM   1575  CG  GLU D  77      -9.558 -72.966 -19.772  1.00245.20           C
ANISOU 1575  CG  GLU D  77    30884  31247  31032  -1257  -1475  -2300       C
ATOM   1576  CD  GLU D  77     -11.024 -73.183 -20.109  1.00225.80           C
ANISOU 1576  CD  GLU D  77    28424  28802  28568  -1236  -1515  -2348       C
ATOM   1577  OE1 GLU D  77     -11.844 -72.294 -19.795  1.00197.28           O
ANISOU 1577  OE1 GLU D  77    24832  25168  24956  -1201  -1603  -2334       O
ATOM   1578  OE2 GLU D  77     -11.356 -74.241 -20.687  1.00228.82           O
ANISOU 1578  OE2 GLU D  77    28785  29212  28944  -1254  -1459  -2397       O
ATOM   1579  N   GLU D  78      -9.582 -76.218 -19.867  1.00205.91           N
ANISOU 1579  N   GLU D  78    25801  26319  26117  -1263  -1257  -2423       N
ATOM   1580  CA  GLU D  78     -10.185 -77.098 -18.870  1.00187.14           C
ANISOU 1580  CA  GLU D  78    23361  23931  23814  -1211  -1221  -2466       C
ATOM   1581  C   GLU D  78      -9.258 -78.290 -18.618  1.00164.27           C
ANISOU 1581  C   GLU D  78    20417  21045  20954  -1225  -1104  -2486       C
ATOM   1582  O   GLU D  78      -9.344 -78.946 -17.581  1.00188.30           O
ANISOU 1582  O   GLU D  78    23399  24076  24069  -1186  -1062  -2506       O
ATOM   1583  CB  GLU D  78     -11.582 -77.560 -19.325  1.00204.02           C
ANISOU 1583  CB  GLU D  78    25491  26082  25945  -1197  -1254  -2516       C
ATOM   1584  CG  GLU D  78     -12.510 -78.061 -18.201  1.00201.28           C
ANISOU 1584  CG  GLU D  78    25083  25722  25672  -1130  -1259  -2544       C
ATOM   1585  CD  GLU D  78     -13.918 -78.412 -18.691  1.00197.23           C
ANISOU 1585  CD  GLU D  78    24567  25222  25148  -1118  -1304  -2579       C
ATOM   1586  OE1 GLU D  78     -14.689 -79.011 -17.906  1.00178.26           O
ANISOU 1586  OE1 GLU D  78    22108  22817  22805  -1067  -1301  -2602       O
ATOM   1587  OE2 GLU D  78     -14.255 -78.089 -19.855  1.00194.24           O
ANISOU 1587  OE2 GLU D  78    24240  24860  24703  -1161  -1342  -2580       O
ATOM   1588  N   ALA D  79      -8.369 -78.561 -19.571  1.00131.13           N
ANISOU 1588  N   ALA D  79    16246  16872  16707  -1281  -1052  -2476       N
ATOM   1589  CA  ALA D  79      -7.337 -79.576 -19.397  1.00119.10           C
ANISOU 1589  CA  ALA D  79    14686  15359  15209  -1298   -939  -2483       C
ATOM   1590  C   ALA D  79      -6.216 -78.991 -18.565  1.00142.40           C
ANISOU 1590  C   ALA D  79    17630  18288  18187  -1296   -923  -2419       C
ATOM   1591  O   ALA D  79      -5.629 -79.666 -17.720  1.00140.68           O
ANISOU 1591  O   ALA D  79    17360  18062  18029  -1284   -847  -2420       O
ATOM   1592  CB  ALA D  79      -6.801 -80.029 -20.736  1.00116.55           C
ANISOU 1592  CB  ALA D  79    14397  15071  14816  -1351   -891  -2492       C
ATOM   1593  N   ILE D  80      -5.926 -77.720 -18.818  1.00169.14           N
ANISOU 1593  N   ILE D  80    21070  21665  21530  -1311   -997  -2360       N
ATOM   1594  CA  ILE D  80      -4.907 -76.999 -18.071  1.00179.11           C
ANISOU 1594  CA  ILE D  80    22338  22903  22813  -1313  -1002  -2289       C
ATOM   1595  C   ILE D  80      -5.232 -76.997 -16.591  1.00182.32           C
ANISOU 1595  C   ILE D  80    22699  23274  23301  -1257  -1011  -2296       C
ATOM   1596  O   ILE D  80      -4.368 -77.279 -15.757  1.00193.29           O
ANISOU 1596  O   ILE D  80    24054  24649  24738  -1254   -951  -2270       O
ATOM   1597  CB  ILE D  80      -4.766 -75.555 -18.571  1.00164.74           C
ANISOU 1597  CB  ILE D  80    20583  21075  20935  -1333  -1103  -2227       C
ATOM   1598  CG1 ILE D  80      -3.980 -75.545 -19.875  1.00168.92           C
ANISOU 1598  CG1 ILE D  80    21148  21644  21390  -1393  -1076  -2196       C
ATOM   1599  CG2 ILE D  80      -4.050 -74.702 -17.549  1.00158.05           C
ANISOU 1599  CG2 ILE D  80    19743  20189  20122  -1320  -1136  -2160       C
ATOM   1600  CD1 ILE D  80      -2.705 -76.353 -19.790  1.00159.17           C
ANISOU 1600  CD1 ILE D  80    19885  20424  20168  -1418   -963  -2171       C
ATOM   1601  N   ARG D  81      -6.479 -76.680 -16.262  1.00154.70           N
ANISOU 1601  N   ARG D  81    19200  19762  19818  -1210  -1084  -2329       N
ATOM   1602  CA  ARG D  81      -6.898 -76.709 -14.870  1.00157.77           C
ANISOU 1602  CA  ARG D  81    19543  20121  20280  -1148  -1094  -2340       C
ATOM   1603  C   ARG D  81      -6.596 -78.081 -14.251  1.00152.34           C
ANISOU 1603  C   ARG D  81    18777  19445  19660  -1139   -984  -2376       C
ATOM   1604  O   ARG D  81      -6.069 -78.178 -13.129  1.00135.20           O
ANISOU 1604  O   ARG D  81    16567  17254  17550  -1116   -950  -2356       O
ATOM   1605  CB  ARG D  81      -8.384 -76.347 -14.738  1.00139.31           C
ANISOU 1605  CB  ARG D  81    17210  17777  17945  -1097  -1180  -2373       C
ATOM   1606  CG  ARG D  81      -8.722 -74.884 -15.072  1.00128.96           C
ANISOU 1606  CG  ARG D  81    15971  16447  16581  -1094  -1295  -2333       C
ATOM   1607  CD  ARG D  81     -10.023 -74.417 -14.401  1.00127.97           C
ANISOU 1607  CD  ARG D  81    15841  16303  16478  -1023  -1375  -2350       C
ATOM   1608  NE  ARG D  81     -11.174 -74.433 -15.307  1.00172.49           N
ANISOU 1608  NE  ARG D  81    21499  21965  22077  -1027  -1420  -2381       N
ATOM   1609  CZ  ARG D  81     -12.059 -75.426 -15.392  1.00177.53           C
ANISOU 1609  CZ  ARG D  81    22091  22625  22737  -1008  -1390  -2432       C
ATOM   1610  NH1 ARG D  81     -11.933 -76.501 -14.627  1.00183.38           N
ANISOU 1610  NH1 ARG D  81    22761  23371  23544   -984  -1314  -2462       N
ATOM   1611  NH2 ARG D  81     -13.075 -75.349 -16.246  1.00147.99           N
ANISOU 1611  NH2 ARG D  81    18373  18901  18955  -1017  -1438  -2451       N
ATOM   1612  N   HIS D  82      -6.883 -79.133 -15.012  1.00123.94           N
ANISOU 1612  N   HIS D  82    15160  15879  16051  -1160   -929  -2427       N
ATOM   1613  CA  HIS D  82      -6.869 -80.498 -14.483  1.00132.93           C
ANISOU 1613  CA  HIS D  82    16221  17030  17257  -1146   -836  -2473       C
ATOM   1614  C   HIS D  82      -5.587 -81.322 -14.631  1.00138.47           C
ANISOU 1614  C   HIS D  82    16899  17745  17967  -1190   -722  -2462       C
ATOM   1615  O   HIS D  82      -5.596 -82.532 -14.405  1.00162.39           O
ANISOU 1615  O   HIS D  82    19868  20788  21044  -1185   -642  -2505       O
ATOM   1616  CB  HIS D  82      -8.111 -81.274 -14.917  1.00109.52           C
ANISOU 1616  CB  HIS D  82    13234  14084  14295  -1128   -848  -2539       C
ATOM   1617  CG  HIS D  82      -9.315 -80.979 -14.071  1.00123.50           C
ANISOU 1617  CG  HIS D  82    14975  15841  16108  -1062   -919  -2553       C
ATOM   1618  ND1 HIS D  82     -10.269 -80.046 -14.435  1.00127.94           N
ANISOU 1618  ND1 HIS D  82    15587  16397  16627  -1044  -1022  -2545       N
ATOM   1619  CD2 HIS D  82      -9.691 -81.459 -12.869  1.00117.13           C
ANISOU 1619  CD2 HIS D  82    14094  15028  15382  -1007   -902  -2568       C
ATOM   1620  CE1 HIS D  82     -11.194 -79.991 -13.496  1.00134.64           C
ANISOU 1620  CE1 HIS D  82    16395  17236  17526   -977  -1063  -2554       C
ATOM   1621  NE2 HIS D  82     -10.876 -80.834 -12.535  1.00148.78           N
ANISOU 1621  NE2 HIS D  82    18110  19028  19393   -953   -994  -2569       N
ATOM   1622  N   VAL D  83      -4.502 -80.667 -15.021  1.00120.93           N
ANISOU 1622  N   VAL D  83    14725  15522  15701  -1231   -715  -2401       N
ATOM   1623  CA  VAL D  83      -3.252 -81.341 -15.344  1.00138.53           C
ANISOU 1623  CA  VAL D  83    16943  17769  17923  -1276   -611  -2379       C
ATOM   1624  C   VAL D  83      -2.780 -82.313 -14.262  1.00144.46           C
ANISOU 1624  C   VAL D  83    17612  18514  18761  -1261   -516  -2390       C
ATOM   1625  O   VAL D  83      -1.900 -83.157 -14.503  1.00111.05           O
ANISOU 1625  O   VAL D  83    13359  14301  14534  -1292   -414  -2386       O
ATOM   1626  CB  VAL D  83      -2.144 -80.308 -15.572  1.00128.44           C
ANISOU 1626  CB  VAL D  83    15718  16483  16599  -1312   -632  -2291       C
ATOM   1627  CG1 VAL D  83      -0.878 -81.002 -16.032  1.00135.82           C
ANISOU 1627  CG1 VAL D  83    16645  17443  17517  -1357   -523  -2261       C
ATOM   1628  CG2 VAL D  83      -2.609 -79.275 -16.578  1.00119.72           C
ANISOU 1628  CG2 VAL D  83    14689  15386  15415  -1327   -732  -2276       C
ATOM   1629  N   ARG D  84      -3.333 -82.167 -13.062  1.00147.97           N
ANISOU 1629  N   ARG D  84    18013  18936  19275  -1211   -548  -2399       N
ATOM   1630  CA  ARG D  84      -3.055 -83.114 -11.998  1.00137.28           C
ANISOU 1630  CA  ARG D  84    16573  17580  18009  -1192   -465  -2415       C
ATOM   1631  C   ARG D  84      -3.606 -84.483 -12.408  1.00143.37           C
ANISOU 1631  C   ARG D  84    17295  18378  18801  -1190   -404  -2490       C
ATOM   1632  O   ARG D  84      -3.057 -85.524 -12.041  1.00135.83           O
ANISOU 1632  O   ARG D  84    16278  17433  17898  -1200   -305  -2505       O
ATOM   1633  CB  ARG D  84      -3.695 -82.637 -10.691  1.00106.15           C
ANISOU 1633  CB  ARG D  84    12593  13610  14129  -1132   -523  -2414       C
ATOM   1634  CG  ARG D  84      -2.817 -82.797  -9.460  1.00110.00           C
ANISOU 1634  CG  ARG D  84    13025  14081  14688  -1127   -463  -2377       C
ATOM   1635  CD  ARG D  84      -2.065 -81.507  -9.110  1.00144.85           C
ANISOU 1635  CD  ARG D  84    17497  18462  19078  -1139   -516  -2297       C
ATOM   1636  NE  ARG D  84      -2.892 -80.573  -8.347  1.00160.50           N
ANISOU 1636  NE  ARG D  84    19494  20415  21073  -1080   -619  -2295       N
ATOM   1637  CZ  ARG D  84      -2.417 -79.690  -7.472  1.00132.70           C
ANISOU 1637  CZ  ARG D  84    15992  16859  17569  -1067   -659  -2240       C
ATOM   1638  NH1 ARG D  84      -1.116 -79.631  -7.237  1.00125.70           N
ANISOU 1638  NH1 ARG D  84    15108  15961  16690  -1112   -605  -2178       N
ATOM   1639  NH2 ARG D  84      -3.245 -78.883  -6.818  1.00129.23           N
ANISOU 1639  NH2 ARG D  84    15570  16394  17137  -1007   -754  -2245       N
ATOM   1640  N   ALA D  85      -4.671 -84.454 -13.206  1.00146.08           N
ANISOU 1640  N   ALA D  85    17671  18732  19101  -1181   -466  -2535       N
ATOM   1641  CA  ALA D  85      -5.450 -85.640 -13.559  1.00137.30           C
ANISOU 1641  CA  ALA D  85    16520  17640  18009  -1173   -437  -2607       C
ATOM   1642  C   ALA D  85      -4.998 -86.385 -14.822  1.00149.05           C
ANISOU 1642  C   ALA D  85    18041  19152  19440  -1222   -374  -2632       C
ATOM   1643  O   ALA D  85      -5.519 -87.452 -15.128  1.00126.10           O
ANISOU 1643  O   ALA D  85    15104  16258  16550  -1219   -343  -2691       O
ATOM   1644  CB  ALA D  85      -6.909 -85.256 -13.695  1.00149.61           C
ANISOU 1644  CB  ALA D  85    18093  19196  19555  -1135   -539  -2637       C
ATOM   1645  N   TRP D  86      -4.040 -85.827 -15.554  1.00163.92           N
ANISOU 1645  N   TRP D  86    19987  21042  21255  -1264   -359  -2585       N
ATOM   1646  CA  TRP D  86      -3.657 -86.362 -16.859  1.00133.35           C
ANISOU 1646  CA  TRP D  86    16160  17196  17313  -1306   -312  -2604       C
ATOM   1647  C   TRP D  86      -3.064 -87.769 -16.835  1.00117.51           C
ANISOU 1647  C   TRP D  86    14103  15203  15343  -1318   -192  -2637       C
ATOM   1648  O   TRP D  86      -2.119 -88.032 -16.104  1.00126.06           O
ANISOU 1648  O   TRP D  86    15143  16282  16474  -1323   -117  -2603       O
ATOM   1649  CB  TRP D  86      -2.691 -85.403 -17.561  1.00138.61           C
ANISOU 1649  CB  TRP D  86    16895  17869  17900  -1344   -322  -2534       C
ATOM   1650  CG  TRP D  86      -3.337 -84.122 -17.972  1.00129.46           C
ANISOU 1650  CG  TRP D  86    15798  16704  16688  -1341   -441  -2511       C
ATOM   1651  CD1 TRP D  86      -4.596 -83.712 -17.658  1.00117.45           C
ANISOU 1651  CD1 TRP D  86    14274  15168  15185  -1306   -532  -2540       C
ATOM   1652  CD2 TRP D  86      -2.769 -83.086 -18.781  1.00135.99           C
ANISOU 1652  CD2 TRP D  86    16696  17540  17436  -1375   -483  -2451       C
ATOM   1653  NE1 TRP D  86      -4.852 -82.484 -18.212  1.00125.71           N
ANISOU 1653  NE1 TRP D  86    15385  16210  16168  -1316   -626  -2505       N
ATOM   1654  CE2 TRP D  86      -3.740 -82.069 -18.917  1.00123.64           C
ANISOU 1654  CE2 TRP D  86    15168  15963  15846  -1359   -601  -2451       C
ATOM   1655  CE3 TRP D  86      -1.523 -82.909 -19.413  1.00108.07           C
ANISOU 1655  CE3 TRP D  86    13192  14024  13846  -1415   -434  -2392       C
ATOM   1656  CZ2 TRP D  86      -3.529 -80.900 -19.635  1.00 89.91           C
ANISOU 1656  CZ2 TRP D  86    10962  11697  11503  -1385   -673  -2398       C
ATOM   1657  CZ3 TRP D  86      -1.302 -81.749 -20.133  1.00115.08           C
ANISOU 1657  CZ3 TRP D  86    14143  14920  14662  -1439   -507  -2336       C
ATOM   1658  CH2 TRP D  86      -2.300 -80.756 -20.237  1.00131.04           C
ANISOU 1658  CH2 TRP D  86    16198  16927  16663  -1425   -626  -2341       C
ATOM   1659  N   ILE D  87      -3.618 -88.659 -17.657  1.00131.93           N
ANISOU 1659  N   ILE D  87    15938  17043  17144  -1324   -177  -2702       N
ATOM   1660  CA  ILE D  87      -3.038 -89.985 -17.885  1.00133.39           C
ANISOU 1660  CA  ILE D  87    16093  17242  17346  -1338    -67  -2737       C
ATOM   1661  C   ILE D  87      -2.937 -90.283 -19.383  1.00136.37           C
ANISOU 1661  C   ILE D  87    16545  17643  17628  -1369    -54  -2764       C
ATOM   1662  O   ILE D  87      -3.922 -90.111 -20.119  1.00126.23           O
ANISOU 1662  O   ILE D  87    15303  16360  16298  -1368   -130  -2801       O
ATOM   1663  CB  ILE D  87      -3.879 -91.103 -17.241  1.00118.33           C
ANISOU 1663  CB  ILE D  87    14108  15327  15523  -1308    -53  -2804       C
ATOM   1664  CG1 ILE D  87      -4.322 -90.704 -15.841  1.00101.98           C
ANISOU 1664  CG1 ILE D  87    11969  13239  13540  -1269    -93  -2785       C
ATOM   1665  CG2 ILE D  87      -3.090 -92.400 -17.193  1.00100.10           C
ANISOU 1665  CG2 ILE D  87    11756  13028  13250  -1322     68  -2828       C
ATOM   1666  CD1 ILE D  87      -3.194 -90.562 -14.889  1.00 94.05           C
ANISOU 1666  CD1 ILE D  87    10921  12229  12586  -1273    -24  -2730       C
ATOM   1667  N   GLY D  88      -1.760 -90.714 -19.839  1.00123.67           N
ANISOU 1667  N   GLY D  88    14952  16051  15986  -1395     42  -2741       N
ATOM   1668  CA  GLY D  88      -1.579 -91.038 -21.247  1.00127.15           C
ANISOU 1668  CA  GLY D  88    15462  16516  16333  -1419     63  -2765       C
ATOM   1669  C   GLY D  88      -2.122 -92.407 -21.593  1.00113.85           C
ANISOU 1669  C   GLY D  88    13762  14832  14665  -1411    101  -2852       C
ATOM   1670  O   GLY D  88      -1.926 -93.363 -20.833  1.00 92.64           O
ANISOU 1670  O   GLY D  88    11006  12136  12057  -1398    171  -2876       O
ATOM   1671  N   PHE D  89      -2.792 -92.500 -22.740  1.00113.34           N
ANISOU 1671  N   PHE D  89    13762  14777  14527  -1421     54  -2897       N
ATOM   1672  CA  PHE D  89      -3.506 -93.718 -23.123  1.00109.05           C
ANISOU 1672  CA  PHE D  89    13213  14227  13994  -1414     66  -2981       C
ATOM   1673  C   PHE D  89      -3.380 -94.085 -24.605  1.00103.41           C
ANISOU 1673  C   PHE D  89    12583  13532  13175  -1435     81  -3015       C
ATOM   1674  O   PHE D  89      -3.874 -93.353 -25.473  1.00 99.29           O
ANISOU 1674  O   PHE D  89    12127  13021  12577  -1449      5  -3012       O
ATOM   1675  CB  PHE D  89      -4.990 -93.534 -22.777  1.00 98.87           C
ANISOU 1675  CB  PHE D  89    11904  12919  12745  -1395    -42  -3016       C
ATOM   1676  CG  PHE D  89      -5.797 -94.787 -22.870  1.00106.92           C
ANISOU 1676  CG  PHE D  89    12898  13926  13801  -1385    -40  -3094       C
ATOM   1677  CD1 PHE D  89      -5.240 -96.018 -22.547  1.00111.24           C
ANISOU 1677  CD1 PHE D  89    13397  14469  14399  -1380     57  -3125       C
ATOM   1678  CD2 PHE D  89      -7.115 -94.737 -23.301  1.00102.75           C
ANISOU 1678  CD2 PHE D  89    12395  13390  13257  -1382   -138  -3131       C
ATOM   1679  CE1 PHE D  89      -5.987 -97.179 -22.644  1.00109.37           C
ANISOU 1679  CE1 PHE D  89    13138  14220  14198  -1371     52  -3195       C
ATOM   1680  CE2 PHE D  89      -7.869 -95.885 -23.407  1.00 91.48           C
ANISOU 1680  CE2 PHE D  89    10946  11950  11863  -1374   -144  -3196       C
ATOM   1681  CZ  PHE D  89      -7.302 -97.116 -23.073  1.00108.38           C
ANISOU 1681  CZ  PHE D  89    13039  14085  14055  -1369    -51  -3230       C
ATOM   1682  N   ASP D  90      -2.774 -95.232 -24.899  1.00111.70           N
ANISOU 1682  N   ASP D  90    13631  14588  14222  -1436    177  -3050       N
ATOM   1683  CA  ASP D  90      -2.729 -95.738 -26.278  1.00139.95           C
ANISOU 1683  CA  ASP D  90    17290  18182  17703  -1449    194  -3093       C
ATOM   1684  C   ASP D  90      -2.938 -97.252 -26.261  1.00146.76           C
ANISOU 1684  C   ASP D  90    18128  19027  18606  -1438    249  -3171       C
ATOM   1685  O   ASP D  90      -2.406 -97.951 -25.400  1.00142.94           O
ANISOU 1685  O   ASP D  90    17575  18534  18200  -1426    327  -3170       O
ATOM   1686  CB  ASP D  90      -1.409 -95.370 -26.981  1.00130.37           C
ANISOU 1686  CB  ASP D  90    16126  17003  16405  -1463    265  -3036       C
ATOM   1687  CG  ASP D  90      -1.537 -95.309 -28.512  1.00148.71           C
ANISOU 1687  CG  ASP D  90    18546  19350  18606  -1477    241  -3061       C
ATOM   1688  OD1 ASP D  90      -2.176 -94.361 -29.042  1.00133.11           O
ANISOU 1688  OD1 ASP D  90    16614  17383  16581  -1491    145  -3048       O
ATOM   1689  OD2 ASP D  90      -0.969 -96.199 -29.190  1.00145.17           O
ANISOU 1689  OD2 ASP D  90    18131  18914  18111  -1473    321  -3092       O
ATOM   1690  N   VAL D  91      -3.744 -97.754 -27.191  1.00139.97           N
ANISOU 1690  N   VAL D  91    17325  18162  17696  -1443    203  -3237       N
ATOM   1691  CA  VAL D  91      -3.995 -99.187 -27.268  1.00121.62           C
ANISOU 1691  CA  VAL D  91    14988  15818  15404  -1433    243  -3312       C
ATOM   1692  C   VAL D  91      -3.545 -99.743 -28.610  1.00122.01           C
ANISOU 1692  C   VAL D  91    15129  15883  15348  -1441    289  -3349       C
ATOM   1693  O   VAL D  91      -3.802 -99.151 -29.677  1.00 87.00           O
ANISOU 1693  O   VAL D  91    10776  11465  10815  -1456    235  -3349       O
ATOM   1694  CB  VAL D  91      -5.481 -99.526 -27.074  1.00125.70           C
ANISOU 1694  CB  VAL D  91    15484  16307  15970  -1428    143  -3366       C
ATOM   1695  CG1 VAL D  91      -5.706-101.046 -27.198  1.00103.72           C
ANISOU 1695  CG1 VAL D  91    12689  13500  13218  -1420    180  -3442       C
ATOM   1696  CG2 VAL D  91      -5.964 -99.014 -25.732  1.00128.55           C
ANISOU 1696  CG2 VAL D  91    15753  16656  16434  -1413     99  -3329       C
ATOM   1697  N   GLU D  92      -2.856-100.877 -28.555  1.00115.37           N
ANISOU 1697  N   GLU D  92    14273  15036  14525  -1429    389  -3380       N
ATOM   1698  CA  GLU D  92      -2.540-101.588 -29.775  1.00138.94           C
ANISOU 1698  CA  GLU D  92    17345  18031  17417  -1429    431  -3428       C
ATOM   1699  C   GLU D  92      -3.543-102.737 -29.903  1.00135.82           C
ANISOU 1699  C   GLU D  92    16952  17598  17056  -1424    391  -3519       C
ATOM   1700  O   GLU D  92      -3.653-103.592 -29.003  1.00 94.57           O
ANISOU 1700  O   GLU D  92    11650  12349  11933  -1412    420  -3544       O
ATOM   1701  CB  GLU D  92      -1.080-102.067 -29.789  1.00128.98           C
ANISOU 1701  CB  GLU D  92    16080  16789  16136  -1417    569  -3400       C
ATOM   1702  CG  GLU D  92      -0.040-100.975 -29.469  1.00156.62           C
ANISOU 1702  CG  GLU D  92    19563  20324  19621  -1423    610  -3298       C
ATOM   1703  CD  GLU D  92      -0.051 -99.791 -30.439  1.00170.53           C
ANISOU 1703  CD  GLU D  92    21402  22119  21274  -1438    549  -3255       C
ATOM   1704  OE1 GLU D  92      -0.407 -99.988 -31.618  1.00170.09           O
ANISOU 1704  OE1 GLU D  92    21429  22071  21126  -1440    519  -3301       O
ATOM   1705  OE2 GLU D  92       0.297 -98.660 -30.018  1.00153.54           O
ANISOU 1705  OE2 GLU D  92    19227  19983  19129  -1448    527  -3175       O
ATOM   1706  N   GLY D  93      -4.290-102.723 -31.009  1.00122.75           N
ANISOU 1706  N   GLY D  93    15383  15939  15317  -1436    317  -3562       N
ATOM   1707  CA  GLY D  93      -5.340-103.695 -31.239  1.00109.56           C
ANISOU 1707  CA  GLY D  93    13727  14232  13670  -1437    259  -3642       C
ATOM   1708  C   GLY D  93      -4.902-104.938 -31.982  1.00101.98           C
ANISOU 1708  C   GLY D  93    12824  13260  12663  -1426    327  -3708       C
ATOM   1709  O   GLY D  93      -3.768-105.034 -32.427  1.00113.05           O
ANISOU 1709  O   GLY D  93    14264  14688  14004  -1415    423  -3692       O
ATOM   1710  N   CYS D  94      -5.803-105.907 -32.093  1.00110.52           N
ANISOU 1710  N   CYS D  94    13914  14303  13777  -1426    275  -3778       N
ATOM   1711  CA  CYS D  94      -5.611-107.029 -33.009  1.00116.50           C
ANISOU 1711  CA  CYS D  94    14750  15044  14472  -1418    312  -3851       C
ATOM   1712  C   CYS D  94      -6.844-107.116 -33.911  1.00124.34           C
ANISOU 1712  C   CYS D  94    15820  16012  15410  -1438    193  -3901       C
ATOM   1713  O   CYS D  94      -7.906-106.613 -33.545  1.00157.61           O
ANISOU 1713  O   CYS D  94    20001  20216  19669  -1455     90  -3885       O
ATOM   1714  CB  CYS D  94      -5.335-108.347 -32.267  1.00123.19           C
ANISOU 1714  CB  CYS D  94    15532  15861  15415  -1398    379  -3891       C
ATOM   1715  SG  CYS D  94      -6.541-108.846 -30.993  1.00112.90           S
ANISOU 1715  SG  CYS D  94    14110  14518  14270  -1401    294  -3906       S
ATOM   1716  N   HIS D  95      -6.707-107.722 -35.090  1.00118.97           N
ANISOU 1716  N   HIS D  95    15247  15326  14631  -1436    206  -3957       N
ATOM   1717  CA  HIS D  95      -7.807-107.768 -36.057  1.00121.53           C
ANISOU 1717  CA  HIS D  95    15656  15629  14890  -1459     95  -4002       C
ATOM   1718  C   HIS D  95      -8.625-109.044 -35.913  1.00111.52           C
ANISOU 1718  C   HIS D  95    14384  14306  13684  -1458     46  -4072       C
ATOM   1719  O   HIS D  95      -8.066-110.116 -35.679  1.00 96.59           O
ANISOU 1719  O   HIS D  95    12479  12395  11827  -1435    120  -4112       O
ATOM   1720  CB  HIS D  95      -7.273-107.702 -37.489  1.00157.47           C
ANISOU 1720  CB  HIS D  95    20335  20205  19293  -1457    126  -4026       C
ATOM   1721  CG  HIS D  95      -6.527-106.447 -37.808  1.00164.19           C
ANISOU 1721  CG  HIS D  95    21200  21114  20072  -1459    161  -3955       C
ATOM   1722  ND1 HIS D  95      -7.160-105.284 -38.196  1.00163.94           N
ANISOU 1722  ND1 HIS D  95    21190  21104  19997  -1489     72  -3917       N
ATOM   1723  CD2 HIS D  95      -5.200-106.181 -37.829  1.00144.11           C
ANISOU 1723  CD2 HIS D  95    18654  18611  17490  -1437    273  -3912       C
ATOM   1724  CE1 HIS D  95      -6.254-104.351 -38.423  1.00159.21           C
ANISOU 1724  CE1 HIS D  95    20597  20555  19339  -1485    125  -3854       C
ATOM   1725  NE2 HIS D  95      -5.057-104.867 -38.206  1.00157.97           N
ANISOU 1725  NE2 HIS D  95    20426  20413  19184  -1454    245  -3848       N
ATOM   1726  N   ALA D  96      -9.943-108.934 -36.064  1.00117.71           N
ANISOU 1726  N   ALA D  96    15179  15063  14481  -1484    -81  -4084       N
ATOM   1727  CA  ALA D  96     -10.805-110.112 -36.047  1.00116.21           C
ANISOU 1727  CA  ALA D  96    14994  14820  14340  -1489   -145  -4145       C
ATOM   1728  C   ALA D  96     -10.491-110.932 -37.290  1.00122.60           C
ANISOU 1728  C   ALA D  96    15929  15610  15042  -1484   -121  -4217       C
ATOM   1729  O   ALA D  96     -10.293-110.353 -38.364  1.00123.41           O
ANISOU 1729  O   ALA D  96    16129  15738  15023  -1493   -122  -4217       O
ATOM   1730  CB  ALA D  96     -12.258-109.693 -36.040  1.00111.05           C
ANISOU 1730  CB  ALA D  96    14334  14148  13711  -1520   -288  -4128       C
ATOM   1731  N   THR D  97     -10.420-112.258 -37.175  1.00 99.39           N
ANISOU 1731  N   THR D  97    12992  12629  12143  -1467    -97  -4278       N
ATOM   1732  CA  THR D  97      -9.984-113.012 -38.350  1.00143.12           C
ANISOU 1732  CA  THR D  97    18656  18151  17573  -1455    -62  -4347       C
ATOM   1733  C   THR D  97     -10.893-114.120 -38.920  1.00157.88           C
ANISOU 1733  C   THR D  97    20596  19957  19433  -1467   -152  -4423       C
ATOM   1734  O   THR D  97     -11.561-113.908 -39.936  1.00186.38           O
ANISOU 1734  O   THR D  97    24306  23557  22954  -1492   -235  -4444       O
ATOM   1735  CB  THR D  97      -8.519-113.513 -38.208  1.00129.65           C
ANISOU 1735  CB  THR D  97    16943  16464  15854  -1414     92  -4358       C
ATOM   1736  OG1 THR D  97      -8.109-114.160 -39.424  1.00154.95           O
ANISOU 1736  OG1 THR D  97    20279  19657  18939  -1397    125  -4422       O
ATOM   1737  CG2 THR D  97      -8.388-114.475 -37.039  1.00108.87           C
ANISOU 1737  CG2 THR D  97    14203  13801  13360  -1397    132  -4371       C
ATOM   1738  N   ARG D  98     -10.932-115.288 -38.290  1.00105.81           N
ANISOU 1738  N   ARG D  98    13951  13321  12932  -1452   -140  -4461       N
ATOM   1739  CA  ARG D  98     -11.504-116.441 -38.987  1.00111.09           C
ANISOU 1739  CA  ARG D  98    14708  13929  13573  -1456   -205  -4540       C
ATOM   1740  C   ARG D  98     -13.027-116.412 -39.156  1.00127.70           C
ANISOU 1740  C   ARG D  98    16826  15995  15699  -1498   -368  -4538       C
ATOM   1741  O   ARG D  98     -13.526-116.468 -40.274  1.00102.64           O
ANISOU 1741  O   ARG D  98    13773  12801  12426  -1518   -437  -4574       O
ATOM   1742  CB  ARG D  98     -11.035-117.762 -38.370  1.00 96.66           C
ANISOU 1742  CB  ARG D  98    12832  12064  11830  -1427   -144  -4585       C
ATOM   1743  CG  ARG D  98     -11.071-117.800 -36.863  1.00169.92           C
ANISOU 1743  CG  ARG D  98    21944  21349  21267  -1423   -125  -4538       C
ATOM   1744  CD  ARG D  98     -11.752-119.062 -36.377  1.00174.08           C
ANISOU 1744  CD  ARG D  98    22428  21818  21899  -1425   -191  -4580       C
ATOM   1745  NE  ARG D  98     -11.458-120.176 -37.261  1.00143.97           N
ANISOU 1745  NE  ARG D  98    18727  17958  18016  -1409   -173  -4664       N
ATOM   1746  CZ  ARG D  98     -10.309-120.832 -37.266  1.00153.78           C
ANISOU 1746  CZ  ARG D  98    19982  19203  19246  -1373    -47  -4700       C
ATOM   1747  NH1 ARG D  98     -10.135-121.829 -38.116  1.00178.36           N
ANISOU 1747  NH1 ARG D  98    23207  22270  22290  -1356    -42  -4779       N
ATOM   1748  NH2 ARG D  98      -9.339-120.483 -36.429  1.00129.93           N
ANISOU 1748  NH2 ARG D  98    16863  16227  16277  -1352     74  -4654       N
ATOM   1749  N   ASP D  99     -13.764-116.290 -38.057  1.00156.94           N
ANISOU 1749  N   ASP D  99    20406  19692  19530  -1510   -429  -4491       N
ATOM   1750  CA  ASP D  99     -15.218-116.261 -38.144  1.00102.64           C
ANISOU 1750  CA  ASP D  99    13533  12784  12682  -1548   -583  -4477       C
ATOM   1751  C   ASP D  99     -15.672-114.979 -38.826  1.00 91.86           C
ANISOU 1751  C   ASP D  99    12225  11453  11227  -1578   -637  -4434       C
ATOM   1752  O   ASP D  99     -16.698-114.965 -39.491  1.00125.98           O
ANISOU 1752  O   ASP D  99    16613  15748  15508  -1613   -753  -4440       O
ATOM   1753  CB  ASP D  99     -15.902-116.443 -36.764  1.00240.43           C
ANISOU 1753  CB  ASP D  99    30833  30227  30294  -1548   -635  -4431       C
ATOM   1754  CG  ASP D  99     -15.133-115.780 -35.596  1.00213.62           C
ANISOU 1754  CG  ASP D  99    27308  26882  26976  -1522   -535  -4374       C
ATOM   1755  OD1 ASP D  99     -14.117-116.354 -35.150  1.00189.28           O
ANISOU 1755  OD1 ASP D  99    24185  23804  23930  -1491   -423  -4397       O
ATOM   1756  OD2 ASP D  99     -15.561-114.714 -35.089  1.00180.84           O
ANISOU 1756  OD2 ASP D  99    23093  22764  22853  -1531   -571  -4305       O
ATOM   1757  N   ALA D 100     -14.906-113.903 -38.667  1.00 87.02           N
ANISOU 1757  N   ALA D 100    11584  10899  10583  -1567   -556  -4388       N
ATOM   1758  CA  ALA D 100     -15.301-112.598 -39.203  1.00 91.66           C
ANISOU 1758  CA  ALA D 100    12208  11523  11095  -1596   -606  -4340       C
ATOM   1759  C   ALA D 100     -14.115-111.658 -39.399  1.00112.01           C
ANISOU 1759  C   ALA D 100    14796  14160  13602  -1578   -495  -4311       C
ATOM   1760  O   ALA D 100     -12.986-111.989 -39.042  1.00110.40           O
ANISOU 1760  O   ALA D 100    14564  13972  13413  -1544   -377  -4321       O
ATOM   1761  CB  ALA D 100     -16.357-111.938 -38.319  1.00108.13           C
ANISOU 1761  CB  ALA D 100    14194  13613  13277  -1615   -699  -4270       C
ATOM   1762  N   VAL D 101     -14.390-110.482 -39.967  1.00119.49           N
ANISOU 1762  N   VAL D 101    15782  15142  14475  -1604   -535  -4269       N
ATOM   1763  CA  VAL D 101     -13.350-109.571 -40.460  1.00 91.72           C
ANISOU 1763  CA  VAL D 101    12300  11683  10867  -1594   -449  -4243       C
ATOM   1764  C   VAL D 101     -13.847-108.128 -40.483  1.00 95.08           C
ANISOU 1764  C   VAL D 101    12705  12147  11274  -1623   -510  -4172       C
ATOM   1765  O   VAL D 101     -15.033-107.895 -40.658  1.00 96.71           O
ANISOU 1765  O   VAL D 101    12923  12335  11488  -1657   -624  -4161       O
ATOM   1766  CB  VAL D 101     -12.977-109.922 -41.914  1.00 95.20           C
ANISOU 1766  CB  VAL D 101    12883  12124  11164  -1594   -429  -4301       C
ATOM   1767  CG1 VAL D 101     -11.851-109.040 -42.419  1.00126.70           C
ANISOU 1767  CG1 VAL D 101    16902  16177  15059  -1579   -338  -4269       C
ATOM   1768  CG2 VAL D 101     -12.599-111.396 -42.059  1.00100.85           C
ANISOU 1768  CG2 VAL D 101    13641  12795  11884  -1566   -383  -4380       C
ATOM   1769  N   GLY D 102     -12.943-107.160 -40.348  1.00108.53           N
ANISOU 1769  N   GLY D 102    14383  13904  12950  -1610   -436  -4122       N
ATOM   1770  CA  GLY D 102     -13.305-105.761 -40.542  1.00119.76           C
ANISOU 1770  CA  GLY D 102    15801  15364  14336  -1637   -490  -4059       C
ATOM   1771  C   GLY D 102     -13.360-104.839 -39.336  1.00119.67           C
ANISOU 1771  C   GLY D 102    15676  15374  14420  -1632   -494  -3984       C
ATOM   1772  O   GLY D 102     -13.760-103.672 -39.462  1.00116.16           O
ANISOU 1772  O   GLY D 102    15227  14956  13951  -1655   -549  -3931       O
ATOM   1773  N   THR D 103     -12.977-105.352 -38.168  1.00130.67           N
ANISOU 1773  N   THR D 103    16975  16754  15920  -1602   -439  -3979       N
ATOM   1774  CA  THR D 103     -12.949-104.541 -36.949  1.00133.36           C
ANISOU 1774  CA  THR D 103    17205  17112  16353  -1591   -435  -3911       C
ATOM   1775  C   THR D 103     -11.790-104.934 -36.039  1.00122.16           C
ANISOU 1775  C   THR D 103    15714  15702  14999  -1555   -317  -3904       C
ATOM   1776  O   THR D 103     -11.238-106.041 -36.154  1.00111.91           O
ANISOU 1776  O   THR D 103    14433  14386  13703  -1537   -249  -3956       O
ATOM   1777  CB  THR D 103     -14.271-104.640 -36.156  1.00121.04           C
ANISOU 1777  CB  THR D 103    15576  15521  14894  -1599   -539  -3896       C
ATOM   1778  OG1 THR D 103     -14.445-103.464 -35.356  1.00107.09           O
ANISOU 1778  OG1 THR D 103    13736  13779  13174  -1596   -563  -3823       O
ATOM   1779  CG2 THR D 103     -14.265-105.866 -35.252  1.00107.53           C
ANISOU 1779  CG2 THR D 103    13791  13774  13290  -1574   -510  -3928       C
ATOM   1780  N   ASN D 104     -11.441-104.025 -35.128  1.00106.38           N
ANISOU 1780  N   ASN D 104    13635  13730  13055  -1545   -294  -3838       N
ATOM   1781  CA  ASN D 104     -10.274-104.198 -34.270  1.00127.45           C
ANISOU 1781  CA  ASN D 104    16234  16411  15778  -1516   -181  -3816       C
ATOM   1782  C   ASN D 104     -10.572-104.331 -32.777  1.00119.42           C
ANISOU 1782  C   ASN D 104    15093  15380  14903  -1498   -187  -3790       C
ATOM   1783  O   ASN D 104     -11.145-103.432 -32.163  1.00115.25           O
ANISOU 1783  O   ASN D 104    14514  14860  14417  -1501   -249  -3740       O
ATOM   1784  CB  ASN D 104      -9.306-103.039 -34.478  1.00132.87           C
ANISOU 1784  CB  ASN D 104    16937  17146  16401  -1516   -129  -3755       C
ATOM   1785  CG  ASN D 104      -8.123-103.422 -35.326  1.00173.63           C
ANISOU 1785  CG  ASN D 104    22169  22330  21472  -1506    -28  -3775       C
ATOM   1786  OD1 ASN D 104      -7.951-104.587 -35.685  1.00165.03           O
ANISOU 1786  OD1 ASN D 104    21115  21219  20371  -1494     13  -3838       O
ATOM   1787  ND2 ASN D 104      -7.285-102.444 -35.640  1.00221.28           N
ANISOU 1787  ND2 ASN D 104    28225  28410  27443  -1507     12  -3718       N
ATOM   1788  N   LEU D 105     -10.168-105.458 -32.201  1.00112.86           N
ANISOU 1788  N   LEU D 105    14212  14528  14142  -1477   -121  -3825       N
ATOM   1789  CA  LEU D 105     -10.261-105.665 -30.763  1.00119.71           C
ANISOU 1789  CA  LEU D 105    14954  15387  15143  -1457   -108  -3800       C
ATOM   1790  C   LEU D 105      -8.988-105.202 -30.072  1.00128.61           C
ANISOU 1790  C   LEU D 105    16028  16543  16294  -1441      0  -3750       C
ATOM   1791  O   LEU D 105      -7.899-105.366 -30.613  1.00151.05           O
ANISOU 1791  O   LEU D 105    18918  19401  19071  -1438     93  -3756       O
ATOM   1792  CB  LEU D 105     -10.507-107.139 -30.454  1.00118.88           C
ANISOU 1792  CB  LEU D 105    14814  15246  15111  -1446    -97  -3859       C
ATOM   1793  CG  LEU D 105     -11.786-107.705 -31.061  1.00 99.90           C
ANISOU 1793  CG  LEU D 105    12457  12807  12694  -1463   -209  -3904       C
ATOM   1794  CD1 LEU D 105     -12.706-106.557 -31.448  1.00 88.82           C
ANISOU 1794  CD1 LEU D 105    11089  11416  11244  -1485   -315  -3865       C
ATOM   1795  CD2 LEU D 105     -11.449-108.581 -32.252  1.00 80.39           C
ANISOU 1795  CD2 LEU D 105    10095  10317  10133  -1470   -180  -3974       C
ATOM   1796  N   PRO D 106      -9.118-104.633 -28.866  1.00108.38           N
ANISOU 1796  N   PRO D 106    13366  13988  13824  -1430    -12  -3698       N
ATOM   1797  CA  PRO D 106      -7.924-104.189 -28.143  1.00 99.99           C
ANISOU 1797  CA  PRO D 106    12252  12951  12790  -1418     87  -3646       C
ATOM   1798  C   PRO D 106      -7.158-105.402 -27.604  1.00112.72           C
ANISOU 1798  C   PRO D 106    13808  14552  14470  -1402    191  -3676       C
ATOM   1799  O   PRO D 106      -7.803-106.412 -27.282  1.00129.28           O
ANISOU 1799  O   PRO D 106    15864  16621  16637  -1395    165  -3723       O
ATOM   1800  CB  PRO D 106      -8.499-103.331 -27.016  1.00 90.49           C
ANISOU 1800  CB  PRO D 106    10962  11751  11669  -1409     26  -3592       C
ATOM   1801  CG  PRO D 106      -9.879-103.845 -26.812  1.00 83.26           C
ANISOU 1801  CG  PRO D 106    10017  10809  10810  -1405    -73  -3625       C
ATOM   1802  CD  PRO D 106     -10.358-104.403 -28.108  1.00103.25           C
ANISOU 1802  CD  PRO D 106    12650  13325  13256  -1425   -115  -3682       C
ATOM   1803  N   LEU D 107      -5.824-105.315 -27.545  1.00102.16           N
ANISOU 1803  N   LEU D 107    12470  13236  13110  -1397    305  -3646       N
ATOM   1804  CA  LEU D 107      -4.981-106.413 -27.043  1.00108.36           C
ANISOU 1804  CA  LEU D 107    13202  14014  13955  -1383    417  -3666       C
ATOM   1805  C   LEU D 107      -4.121-105.986 -25.848  1.00123.75           C
ANISOU 1805  C   LEU D 107    15056  15981  15982  -1376    492  -3599       C
ATOM   1806  O   LEU D 107      -4.237-106.542 -24.748  1.00129.44           O
ANISOU 1806  O   LEU D 107    15673  16690  16819  -1365    511  -3601       O
ATOM   1807  CB  LEU D 107      -4.085-107.001 -28.141  1.00106.52           C
ANISOU 1807  CB  LEU D 107    13062  13788  13622  -1382    501  -3698       C
ATOM   1808  CG  LEU D 107      -3.113-108.087 -27.639  1.00105.15           C
ANISOU 1808  CG  LEU D 107    12836  13610  13507  -1366    627  -3712       C
ATOM   1809  CD1 LEU D 107      -3.850-109.234 -26.956  1.00124.68           C
ANISOU 1809  CD1 LEU D 107    15234  16047  16092  -1359    600  -3768       C
ATOM   1810  CD2 LEU D 107      -2.232-108.626 -28.739  1.00 74.60           C
ANISOU 1810  CD2 LEU D 107     9062   9749   9532  -1358    711  -3740       C
ATOM   1811  N   GLN D 108      -3.235-105.021 -26.081  1.00105.78           N
ANISOU 1811  N   GLN D 108    12815  13735  13641  -1382    535  -3536       N
ATOM   1812  CA  GLN D 108      -2.429-104.453 -25.007  1.00106.40           C
ANISOU 1812  CA  GLN D 108    12815  13830  13782  -1380    595  -3463       C
ATOM   1813  C   GLN D 108      -2.788-102.974 -24.823  1.00120.48           C
ANISOU 1813  C   GLN D 108    14606  15626  15545  -1388    511  -3402       C
ATOM   1814  O   GLN D 108      -2.915-102.213 -25.809  1.00 92.36           O
ANISOU 1814  O   GLN D 108    11133  12078  11880  -1400    462  -3391       O
ATOM   1815  CB  GLN D 108      -0.942-104.625 -25.305  1.00 83.97           C
ANISOU 1815  CB  GLN D 108     9999  11011  10894  -1381    725  -3428       C
ATOM   1816  CG  GLN D 108      -0.014-104.333 -24.147  1.00115.21           C
ANISOU 1816  CG  GLN D 108    13867  14979  14927  -1381    803  -3356       C
ATOM   1817  CD  GLN D 108       1.392-103.974 -24.605  1.00136.49           C
ANISOU 1817  CD  GLN D 108    16607  17706  17547  -1387    903  -3292       C
ATOM   1818  OE1 GLN D 108       1.647-102.841 -25.037  1.00114.65           O
ANISOU 1818  OE1 GLN D 108    13892  14962  14707  -1397    870  -3234       O
ATOM   1819  NE2 GLN D 108       2.316-104.937 -24.509  1.00128.18           N
ANISOU 1819  NE2 GLN D 108    15532  16657  16513  -1381   1023  -3296       N
ATOM   1820  N   LEU D 109      -2.973-102.590 -23.559  1.00 95.68           N
ANISOU 1820  N   LEU D 109    11371  12480  12504  -1379    494  -3365       N
ATOM   1821  CA  LEU D 109      -3.386-101.245 -23.197  1.00 82.64           C
ANISOU 1821  CA  LEU D 109     9715  10835  10848  -1381    411  -3310       C
ATOM   1822  C   LEU D 109      -2.287-100.559 -22.396  1.00116.90           C
ANISOU 1822  C   LEU D 109    14011  15189  15217  -1383    477  -3230       C
ATOM   1823  O   LEU D 109      -1.963-100.990 -21.279  1.00 95.85           O
ANISOU 1823  O   LEU D 109    11252  12517  12651  -1373    531  -3217       O
ATOM   1824  CB  LEU D 109      -4.636-101.327 -22.339  1.00 86.32           C
ANISOU 1824  CB  LEU D 109    10109  11282  11407  -1363    323  -3332       C
ATOM   1825  CG  LEU D 109      -5.920-101.771 -23.025  1.00 91.87           C
ANISOU 1825  CG  LEU D 109    10851  11968  12087  -1363    229  -3394       C
ATOM   1826  CD1 LEU D 109      -6.382-103.139 -22.525  1.00 94.98           C
ANISOU 1826  CD1 LEU D 109    11174  12342  12573  -1350    243  -3451       C
ATOM   1827  CD2 LEU D 109      -7.001-100.708 -22.841  1.00 97.56           C
ANISOU 1827  CD2 LEU D 109    11575  12688  12806  -1357    108  -3368       C
ATOM   1828  N   GLY D 110      -1.685 -99.517 -22.967  1.00149.75           N
ANISOU 1828  N   GLY D 110    18238  19370  19292  -1397    474  -3173       N
ATOM   1829  CA  GLY D 110      -0.674 -98.763 -22.244  1.00152.52           C
ANISOU 1829  CA  GLY D 110    18555  19732  19665  -1403    522  -3088       C
ATOM   1830  C   GLY D 110      -1.128 -97.468 -21.598  1.00132.94           C
ANISOU 1830  C   GLY D 110    16059  17247  17206  -1399    431  -3037       C
ATOM   1831  O   GLY D 110      -1.989 -96.748 -22.143  1.00107.03           O
ANISOU 1831  O   GLY D 110    12829  13964  13873  -1400    329  -3046       O
ATOM   1832  N   PHE D 111      -0.456 -97.125 -20.496  1.00120.99           N
ANISOU 1832  N   PHE D 111    14479  15730  15760  -1397    472  -2977       N
ATOM   1833  CA  PHE D 111      -0.797 -95.958 -19.686  1.00115.63           C
ANISOU 1833  CA  PHE D 111    13777  15043  15114  -1389    394  -2927       C
ATOM   1834  C   PHE D 111       0.437 -95.132 -19.313  1.00132.72           C
ANISOU 1834  C   PHE D 111    15944  17216  17268  -1405    440  -2833       C
ATOM   1835  O   PHE D 111       1.546 -95.667 -19.246  1.00141.64           O
ANISOU 1835  O   PHE D 111    17056  18356  18404  -1417    548  -2805       O
ATOM   1836  CB  PHE D 111      -1.497 -96.411 -18.410  1.00104.07           C
ANISOU 1836  CB  PHE D 111    12212  13559  13769  -1362    377  -2954       C
ATOM   1837  CG  PHE D 111      -2.859 -96.995 -18.642  1.00110.23           C
ANISOU 1837  CG  PHE D 111    12986  14330  14567  -1344    306  -3030       C
ATOM   1838  CD1 PHE D 111      -3.949 -96.169 -18.874  1.00110.07           C
ANISOU 1838  CD1 PHE D 111    13001  14304  14516  -1333    186  -3034       C
ATOM   1839  CD2 PHE D 111      -3.052 -98.370 -18.630  1.00100.79           C
ANISOU 1839  CD2 PHE D 111    11747  13130  13419  -1338    356  -3093       C
ATOM   1840  CE1 PHE D 111      -5.206 -96.703 -19.092  1.00110.71           C
ANISOU 1840  CE1 PHE D 111    13076  14376  14613  -1318    119  -3095       C
ATOM   1841  CE2 PHE D 111      -4.309 -98.909 -18.843  1.00104.42           C
ANISOU 1841  CE2 PHE D 111    12201  13580  13896  -1324    283  -3156       C
ATOM   1842  CZ  PHE D 111      -5.387 -98.074 -19.074  1.00 99.94           C
ANISOU 1842  CZ  PHE D 111    11669  13007  13297  -1314    165  -3154       C
ATOM   1843  N   SER D 112       0.238 -93.839 -19.053  1.00105.35           N
ANISOU 1843  N   SER D 112    12498  13743  13786  -1404    356  -2781       N
ATOM   1844  CA  SER D 112       1.332 -92.950 -18.659  1.00118.72           C
ANISOU 1844  CA  SER D 112    14197  15440  15471  -1420    381  -2686       C
ATOM   1845  C   SER D 112       2.224 -93.571 -17.570  1.00125.10           C
ANISOU 1845  C   SER D 112    14922  16243  16368  -1422    485  -2655       C
ATOM   1846  O   SER D 112       3.444 -93.471 -17.622  1.00128.68           O
ANISOU 1846  O   SER D 112    15384  16709  16800  -1444    560  -2588       O
ATOM   1847  CB  SER D 112       0.772 -91.603 -18.195  1.00127.48           C
ANISOU 1847  CB  SER D 112    15320  16534  16583  -1410    266  -2648       C
ATOM   1848  OG  SER D 112       1.681 -90.921 -17.346  1.00153.05           O
ANISOU 1848  OG  SER D 112    18535  19763  19854  -1418    288  -2564       O
ATOM   1849  N   THR D 113       1.612 -94.213 -16.585  1.00117.32           N
ANISOU 1849  N   THR D 113    13853  15241  15481  -1398    488  -2701       N
ATOM   1850  CA  THR D 113       2.353 -95.025 -15.627  1.00108.00           C
ANISOU 1850  CA  THR D 113    12587  14059  14389  -1401    594  -2686       C
ATOM   1851  C   THR D 113       2.925 -96.261 -16.315  1.00123.00           C
ANISOU 1851  C   THR D 113    14489  15975  16269  -1414    701  -2721       C
ATOM   1852  O   THR D 113       2.551 -96.588 -17.448  1.00118.37           O
ANISOU 1852  O   THR D 113    13967  15399  15611  -1415    685  -2771       O
ATOM   1853  CB  THR D 113       1.475 -95.470 -14.444  1.00144.11           C
ANISOU 1853  CB  THR D 113    17064  18617  19075  -1370    567  -2730       C
ATOM   1854  OG1 THR D 113       0.279 -96.085 -14.937  1.00107.47           O
ANISOU 1854  OG1 THR D 113    12428  13975  14431  -1350    514  -2816       O
ATOM   1855  CG2 THR D 113       1.109 -94.276 -13.565  1.00177.59           C
ANISOU 1855  CG2 THR D 113    21294  22840  23343  -1352    479  -2686       C
ATOM   1856  N   GLY D 114       3.856 -96.936 -15.654  1.00113.45           N
ANISOU 1856  N   GLY D 114    13216  14770  15122  -1425    812  -2693       N
ATOM   1857  CA  GLY D 114       4.531 -98.050 -16.295  1.00148.56           C
ANISOU 1857  CA  GLY D 114    17668  19231  19545  -1436    922  -2716       C
ATOM   1858  C   GLY D 114       3.643 -99.149 -16.867  1.00132.65           C
ANISOU 1858  C   GLY D 114    15656  17214  17532  -1419    913  -2821       C
ATOM   1859  O   GLY D 114       4.068 -99.907 -17.738  1.00110.12           O
ANISOU 1859  O   GLY D 114    12842  14372  14627  -1425    980  -2848       O
ATOM   1860  N   VAL D 115       2.404 -99.226 -16.395  1.00131.78           N
ANISOU 1860  N   VAL D 115    15506  17087  17478  -1397    827  -2877       N
ATOM   1861  CA  VAL D 115       1.557-100.394 -16.644  1.00127.10           C
ANISOU 1861  CA  VAL D 115    14890  16488  16916  -1381    820  -2970       C
ATOM   1862  C   VAL D 115       1.067-100.581 -18.093  1.00137.13           C
ANISOU 1862  C   VAL D 115    16261  17761  18082  -1383    779  -3025       C
ATOM   1863  O   VAL D 115       0.683 -99.616 -18.798  1.00 93.20           O
ANISOU 1863  O   VAL D 115    10776  12201  12435  -1386    696  -3012       O
ATOM   1864  CB  VAL D 115       0.374-100.500 -15.602  1.00114.20           C
ANISOU 1864  CB  VAL D 115    13168  14838  15384  -1353    743  -3005       C
ATOM   1865  CG1 VAL D 115      -0.171 -99.131 -15.202  1.00 74.27           C
ANISOU 1865  CG1 VAL D 115     8128   9776  10317  -1341    637  -2963       C
ATOM   1866  CG2 VAL D 115      -0.738-101.414 -16.109  1.00 99.88           C
ANISOU 1866  CG2 VAL D 115    11356  13017  13577  -1338    694  -3094       C
ATOM   1867  N   ASN D 116       1.147-101.840 -18.527  1.00144.45           N
ANISOU 1867  N   ASN D 116    17184  18687  19014  -1382    842  -3085       N
ATOM   1868  CA  ASN D 116       0.514-102.323 -19.748  1.00128.56           C
ANISOU 1868  CA  ASN D 116    15251  16671  16925  -1379    802  -3156       C
ATOM   1869  C   ASN D 116      -0.306-103.542 -19.360  1.00126.24           C
ANISOU 1869  C   ASN D 116    14891  16358  16716  -1364    792  -3233       C
ATOM   1870  O   ASN D 116       0.131-104.355 -18.532  1.00114.37           O
ANISOU 1870  O   ASN D 116    13299  14852  15304  -1361    871  -3235       O
ATOM   1871  CB  ASN D 116       1.556-102.763 -20.780  1.00102.00           C
ANISOU 1871  CB  ASN D 116    11960  13323  13472  -1391    898  -3152       C
ATOM   1872  CG  ASN D 116       2.497-101.652 -21.180  1.00125.71           C
ANISOU 1872  CG  ASN D 116    15021  16350  16392  -1406    918  -3066       C
ATOM   1873  OD1 ASN D 116       2.211-100.876 -22.094  1.00121.32           O
ANISOU 1873  OD1 ASN D 116    14551  15804  15740  -1411    849  -3059       O
ATOM   1874  ND2 ASN D 116       3.642-101.580 -20.509  1.00147.78           N
ANISOU 1874  ND2 ASN D 116    17769  19156  19224  -1415   1012  -2995       N
ATOM   1875  N   LEU D 117      -1.484-103.686 -19.953  1.00111.07           N
ANISOU 1875  N   LEU D 117    13010  14424  14768  -1356    695  -3292       N
ATOM   1876  CA  LEU D 117      -2.303-104.855 -19.680  1.00 99.70           C
ANISOU 1876  CA  LEU D 117    11513  12966  13403  -1343    674  -3362       C
ATOM   1877  C   LEU D 117      -2.706-105.523 -20.998  1.00113.17           C
ANISOU 1877  C   LEU D 117    13313  14661  15026  -1348    650  -3431       C
ATOM   1878  O   LEU D 117      -3.135-104.839 -21.940  1.00 96.04           O
ANISOU 1878  O   LEU D 117    11237  12495  12760  -1355    580  -3434       O
ATOM   1879  CB  LEU D 117      -3.534-104.444 -18.872  1.00109.94           C
ANISOU 1879  CB  LEU D 117    12745  14253  14772  -1325    563  -3362       C
ATOM   1880  CG  LEU D 117      -3.305-103.802 -17.499  1.00103.60           C
ANISOU 1880  CG  LEU D 117    11848  13460  14057  -1314    572  -3300       C
ATOM   1881  CD1 LEU D 117      -4.196-102.592 -17.300  1.00112.86           C
ANISOU 1881  CD1 LEU D 117    13037  14632  15213  -1300    455  -3270       C
ATOM   1882  CD2 LEU D 117      -3.528-104.816 -16.395  1.00109.86           C
ANISOU 1882  CD2 LEU D 117    12512  14247  14981  -1298    603  -3322       C
ATOM   1883  N   VAL D 118      -2.543-106.847 -21.076  1.00111.79           N
ANISOU 1883  N   VAL D 118    13114  14473  14887  -1345    710  -3486       N
ATOM   1884  CA  VAL D 118      -3.002-107.606 -22.249  1.00130.08           C
ANISOU 1884  CA  VAL D 118    15517  16773  17134  -1346    681  -3559       C
ATOM   1885  C   VAL D 118      -4.241-108.416 -21.935  1.00125.41           C
ANISOU 1885  C   VAL D 118    14875  16156  16621  -1337    598  -3616       C
ATOM   1886  O   VAL D 118      -4.305-109.152 -20.949  1.00131.99           O
ANISOU 1886  O   VAL D 118    15599  16982  17569  -1327    625  -3624       O
ATOM   1887  CB  VAL D 118      -1.952-108.579 -22.854  1.00126.44           C
ANISOU 1887  CB  VAL D 118    15097  16312  16633  -1347    801  -3587       C
ATOM   1888  CG1 VAL D 118      -0.846-107.811 -23.537  1.00121.84           C
ANISOU 1888  CG1 VAL D 118    14593  15758  15943  -1355    867  -3534       C
ATOM   1889  CG2 VAL D 118      -1.412-109.533 -21.792  1.00155.74           C
ANISOU 1889  CG2 VAL D 118    18693  20019  20464  -1341    892  -3588       C
ATOM   1890  N   ALA D 119      -5.227-108.289 -22.802  1.00 98.62           N
ANISOU 1890  N   ALA D 119    11558  12749  13162  -1341    495  -3652       N
ATOM   1891  CA  ALA D 119      -6.474-108.967 -22.577  1.00 98.06           C
ANISOU 1891  CA  ALA D 119    11447  12655  13158  -1334    402  -3696       C
ATOM   1892  C   ALA D 119      -6.709-109.914 -23.726  1.00101.66           C
ANISOU 1892  C   ALA D 119    11992  13086  13549  -1342    389  -3769       C
ATOM   1893  O   ALA D 119      -6.122-109.763 -24.795  1.00119.42           O
ANISOU 1893  O   ALA D 119    14349  15339  15684  -1351    428  -3781       O
ATOM   1894  CB  ALA D 119      -7.591-107.965 -22.481  1.00123.34           C
ANISOU 1894  CB  ALA D 119    14652  15859  16351  -1332    277  -3667       C
ATOM   1895  N   VAL D 120      -7.558-110.906 -23.503  1.00 96.33           N
ANISOU 1895  N   VAL D 120    11273  12384  12945  -1336    334  -3814       N
ATOM   1896  CA  VAL D 120      -7.935-111.800 -24.576  1.00112.92           C
ANISOU 1896  CA  VAL D 120    13462  14455  14987  -1344    301  -3885       C
ATOM   1897  C   VAL D 120      -8.636-110.981 -25.653  1.00126.33           C
ANISOU 1897  C   VAL D 120    15276  16153  16572  -1360    206  -3886       C
ATOM   1898  O   VAL D 120      -9.244-109.938 -25.373  1.00103.48           O
ANISOU 1898  O   VAL D 120    12366  13273  13679  -1362    133  -3839       O
ATOM   1899  CB  VAL D 120      -8.839-112.930 -24.068  1.00102.53           C
ANISOU 1899  CB  VAL D 120    12071  13109  13776  -1338    239  -3924       C
ATOM   1900  CG1 VAL D 120      -8.446-113.291 -22.649  1.00101.23           C
ANISOU 1900  CG1 VAL D 120    11756  12959  13750  -1323    302  -3895       C
ATOM   1901  CG2 VAL D 120     -10.291-112.507 -24.107  1.00152.29           C
ANISOU 1901  CG2 VAL D 120    18374  19403  20088  -1342     91  -3912       C
ATOM   1902  N   PRO D 121      -8.534-111.428 -26.906  1.00128.25           N
ANISOU 1902  N   PRO D 121    15638  16379  16713  -1369    208  -3939       N
ATOM   1903  CA  PRO D 121      -9.297-110.659 -27.880  1.00121.30           C
ANISOU 1903  CA  PRO D 121    14857  15499  15732  -1387    110  -3938       C
ATOM   1904  C   PRO D 121     -10.757-110.772 -27.479  1.00121.55           C
ANISOU 1904  C   PRO D 121    14841  15510  15834  -1391    -22  -3938       C
ATOM   1905  O   PRO D 121     -11.237-111.873 -27.232  1.00123.78           O
ANISOU 1905  O   PRO D 121    15084  15763  16186  -1387    -50  -3977       O
ATOM   1906  CB  PRO D 121      -9.031-111.406 -29.190  1.00139.78           C
ANISOU 1906  CB  PRO D 121    17322  17819  17969  -1394    130  -4005       C
ATOM   1907  CG  PRO D 121      -7.830-112.273 -28.927  1.00105.15           C
ANISOU 1907  CG  PRO D 121    12909  13433  13610  -1375    264  -4026       C
ATOM   1908  CD  PRO D 121      -7.909-112.624 -27.493  1.00113.49           C
ANISOU 1908  CD  PRO D 121    13818  14488  14815  -1364    281  -4002       C
ATOM   1909  N   THR D 122     -11.461-109.656 -27.380  1.00127.46           N
ANISOU 1909  N   THR D 122    15587  16274  16568  -1398   -103  -3889       N
ATOM   1910  CA  THR D 122     -12.869-109.741 -27.019  1.00124.09           C
ANISOU 1910  CA  THR D 122    15115  15830  16203  -1399   -229  -3880       C
ATOM   1911  C   THR D 122     -13.724-108.740 -27.787  1.00118.91           C
ANISOU 1911  C   THR D 122    14539  15179  15462  -1420   -331  -3857       C
ATOM   1912  O   THR D 122     -13.353-107.574 -27.944  1.00105.42           O
ANISOU 1912  O   THR D 122    12860  13499  13695  -1424   -315  -3815       O
ATOM   1913  CB  THR D 122     -13.069-109.563 -25.509  1.00124.71           C
ANISOU 1913  CB  THR D 122    15048  15925  16413  -1374   -230  -3830       C
ATOM   1914  OG1 THR D 122     -11.890-109.991 -24.826  1.00127.97           O
ANISOU 1914  OG1 THR D 122    15396  16348  16880  -1359   -106  -3832       O
ATOM   1915  CG2 THR D 122     -14.222-110.396 -25.035  1.00156.29           C
ANISOU 1915  CG2 THR D 122    18977  19900  20504  -1367   -322  -3841       C
ATOM   1916  N   GLY D 123     -14.872-109.203 -28.268  1.00 99.75           N
ANISOU 1916  N   GLY D 123    12146  12725  13030  -1435   -437  -3879       N
ATOM   1917  CA  GLY D 123     -15.744-108.352 -29.053  1.00112.78           C
ANISOU 1917  CA  GLY D 123    13873  14377  14599  -1459   -536  -3858       C
ATOM   1918  C   GLY D 123     -17.210-108.669 -28.878  1.00107.57           C
ANISOU 1918  C   GLY D 123    13183  13695  13993  -1465   -666  -3846       C
ATOM   1919  O   GLY D 123     -17.565-109.692 -28.289  1.00125.71           O
ANISOU 1919  O   GLY D 123    15410  15972  16383  -1452   -684  -3862       O
ATOM   1920  N   TYR D 124     -18.061-107.795 -29.404  1.00 93.31           N
ANISOU 1920  N   TYR D 124    11429  11896  12130  -1485   -756  -3812       N
ATOM   1921  CA  TYR D 124     -19.503-107.959 -29.270  1.00104.95           C
ANISOU 1921  CA  TYR D 124    12878  13353  13647  -1492   -885  -3785       C
ATOM   1922  C   TYR D 124     -20.117-108.717 -30.455  1.00105.54           C
ANISOU 1922  C   TYR D 124    13055  13388  13655  -1528   -954  -3833       C
ATOM   1923  O   TYR D 124     -19.925-108.356 -31.619  1.00 98.56           O
ANISOU 1923  O   TYR D 124    12288  12504  12655  -1558   -953  -3857       O
ATOM   1924  CB  TYR D 124     -20.164-106.595 -29.108  1.00 79.14           C
ANISOU 1924  CB  TYR D 124     9600  10110  10359  -1493   -949  -3715       C
ATOM   1925  CG  TYR D 124     -19.577-105.794 -27.979  1.00109.87           C
ANISOU 1925  CG  TYR D 124    13401  14036  14309  -1457   -887  -3669       C
ATOM   1926  CD1 TYR D 124     -18.364-105.138 -28.125  1.00107.39           C
ANISOU 1926  CD1 TYR D 124    13118  13745  13941  -1456   -790  -3672       C
ATOM   1927  CD2 TYR D 124     -20.231-105.699 -26.758  1.00138.13           C
ANISOU 1927  CD2 TYR D 124    16862  17625  17995  -1422   -930  -3618       C
ATOM   1928  CE1 TYR D 124     -17.819-104.400 -27.077  1.00108.35           C
ANISOU 1928  CE1 TYR D 124    13160  13894  14116  -1425   -738  -3627       C
ATOM   1929  CE2 TYR D 124     -19.693-104.961 -25.706  1.00137.33           C
ANISOU 1929  CE2 TYR D 124    16681  17553  17946  -1387   -876  -3576       C
ATOM   1930  CZ  TYR D 124     -18.488-104.319 -25.876  1.00111.13           C
ANISOU 1930  CZ  TYR D 124    13400  14252  14572  -1391   -782  -3582       C
ATOM   1931  OH  TYR D 124     -17.959-103.590 -24.842  1.00119.23           O
ANISOU 1931  OH  TYR D 124    14352  15302  15648  -1360   -734  -3539       O
ATOM   1932  N   VAL D 125     -20.869-109.768 -30.150  1.00 97.72           N
ANISOU 1932  N   VAL D 125    12022  12367  12740  -1526  -1019  -3843       N
ATOM   1933  CA  VAL D 125     -21.431-110.626 -31.186  1.00104.07           C
ANISOU 1933  CA  VAL D 125    12921  13128  13494  -1560  -1088  -3890       C
ATOM   1934  C   VAL D 125     -22.956-110.723 -31.113  1.00113.79           C
ANISOU 1934  C   VAL D 125    14130  14341  14764  -1575  -1233  -3843       C
ATOM   1935  O   VAL D 125     -23.509-111.222 -30.137  1.00131.05           O
ANISOU 1935  O   VAL D 125    16206  16523  17063  -1552  -1274  -3810       O
ATOM   1936  CB  VAL D 125     -20.841-112.045 -31.102  1.00 95.94           C
ANISOU 1936  CB  VAL D 125    11881  12066  12507  -1549  -1034  -3958       C
ATOM   1937  CG1 VAL D 125     -21.642-113.002 -31.967  1.00104.62           C
ANISOU 1937  CG1 VAL D 125    13062  13114  13576  -1580  -1131  -3997       C
ATOM   1938  CG2 VAL D 125     -19.379-112.028 -31.504  1.00 80.31           C
ANISOU 1938  CG2 VAL D 125     9956  10098  10460  -1540   -898  -4009       C
ATOM   1939  N   ASP D 126     -23.639-110.256 -32.150  1.00104.38           N
ANISOU 1939  N   ASP D 126    13040  13140  13480  -1615  -1310  -3834       N
ATOM   1940  CA  ASP D 126     -25.083-110.381 -32.186  1.00113.09           C
ANISOU 1940  CA  ASP D 126    14133  14224  14612  -1635  -1449  -3784       C
ATOM   1941  C   ASP D 126     -25.469-111.830 -32.481  1.00127.91           C
ANISOU 1941  C   ASP D 126    16032  16048  16519  -1650  -1504  -3829       C
ATOM   1942  O   ASP D 126     -24.872-112.470 -33.351  1.00110.71           O
ANISOU 1942  O   ASP D 126    13951  13841  14272  -1667  -1465  -3905       O
ATOM   1943  CB  ASP D 126     -25.692-109.431 -33.228  1.00138.05           C
ANISOU 1943  CB  ASP D 126    17397  17392  17664  -1677  -1514  -3758       C
ATOM   1944  CG  ASP D 126     -25.893-108.014 -32.691  1.00122.68           C
ANISOU 1944  CG  ASP D 126    15398  15492  15722  -1662  -1514  -3683       C
ATOM   1945  OD1 ASP D 126     -25.069-107.573 -31.864  1.00 94.06           O
ANISOU 1945  OD1 ASP D 126    11702  11898  12138  -1623  -1425  -3676       O
ATOM   1946  OD2 ASP D 126     -26.878-107.340 -33.091  1.00102.35           O
ANISOU 1946  OD2 ASP D 126    12855  12922  13112  -1689  -1605  -3629       O
ATOM   1947  N   THR D 127     -26.442-112.343 -31.725  1.00128.60           N
ANISOU 1947  N   THR D 127    16027  16125  16710  -1639  -1593  -3779       N
ATOM   1948  CA  THR D 127     -27.064-113.639 -31.990  1.00124.64           C
ANISOU 1948  CA  THR D 127    15543  15572  16244  -1657  -1677  -3802       C
ATOM   1949  C   THR D 127     -28.577-113.442 -32.044  1.00124.61           C
ANISOU 1949  C   THR D 127    15527  15560  16258  -1681  -1826  -3720       C
ATOM   1950  O   THR D 127     -29.058-112.316 -31.923  1.00139.34           O
ANISOU 1950  O   THR D 127    17378  17460  18103  -1681  -1852  -3653       O
ATOM   1951  CB  THR D 127     -26.747-114.661 -30.887  1.00135.62           C
ANISOU 1951  CB  THR D 127    16809  16957  17764  -1618  -1644  -3814       C
ATOM   1952  OG1 THR D 127     -27.199-114.155 -29.623  1.00145.44           O
ANISOU 1952  OG1 THR D 127    17908  18242  19109  -1580  -1661  -3732       O
ATOM   1953  CG2 THR D 127     -25.251-114.955 -30.821  1.00110.85           C
ANISOU 1953  CG2 THR D 127    13680  13825  14612  -1597  -1495  -3891       C
ATOM   1954  N   GLU D 128     -29.322-114.535 -32.204  1.00116.62           N
ANISOU 1954  N   GLU D 128    14521  14503  15288  -1700  -1924  -3720       N
ATOM   1955  CA  GLU D 128     -30.786-114.478 -32.280  1.00103.94           C
ANISOU 1955  CA  GLU D 128    12905  12886  13702  -1725  -2072  -3636       C
ATOM   1956  C   GLU D 128     -31.401-113.778 -31.079  1.00122.00           C
ANISOU 1956  C   GLU D 128    15051  15223  16080  -1684  -2098  -3534       C
ATOM   1957  O   GLU D 128     -32.230-112.886 -31.233  1.00132.51           O
ANISOU 1957  O   GLU D 128    16394  16574  17381  -1697  -2164  -3460       O
ATOM   1958  CB  GLU D 128     -31.399-115.878 -32.375  1.00 83.81           C
ANISOU 1958  CB  GLU D 128    10354  10280  11209  -1742  -2170  -3645       C
ATOM   1959  CG  GLU D 128     -30.552-116.908 -33.078  1.00117.53           C
ANISOU 1959  CG  GLU D 128    14716  14502  15437  -1757  -2120  -3756       C
ATOM   1960  CD  GLU D 128     -29.403-117.389 -32.220  1.00141.36           C
ANISOU 1960  CD  GLU D 128    17646  17536  18528  -1708  -1996  -3809       C
ATOM   1961  OE1 GLU D 128     -29.098-118.595 -32.259  1.00148.90           O
ANISOU 1961  OE1 GLU D 128    18607  18448  19519  -1707  -1994  -3868       O
ATOM   1962  OE2 GLU D 128     -28.805-116.563 -31.501  1.00150.85           O
ANISOU 1962  OE2 GLU D 128    18773  18791  19751  -1672  -1902  -3790       O
ATOM   1963  N   ASN D 129     -31.027-114.222 -29.880  1.00131.99           N
ANISOU 1963  N   ASN D 129    16182  16508  17460  -1633  -2051  -3528       N
ATOM   1964  CA  ASN D 129     -31.606-113.682 -28.656  1.00124.01           C
ANISOU 1964  CA  ASN D 129    15029  15546  16544  -1586  -2077  -3433       C
ATOM   1965  C   ASN D 129     -31.018-112.348 -28.205  1.00121.12           C
ANISOU 1965  C   ASN D 129    14636  15232  16152  -1554  -1985  -3416       C
ATOM   1966  O   ASN D 129     -31.764-111.419 -27.904  1.00152.20           O
ANISOU 1966  O   ASN D 129    18541  19201  20089  -1541  -2034  -3333       O
ATOM   1967  CB  ASN D 129     -31.524-114.704 -27.516  1.00133.64           C
ANISOU 1967  CB  ASN D 129    16107  16769  17902  -1544  -2072  -3427       C
ATOM   1968  CG  ASN D 129     -31.031-116.053 -27.979  1.00145.96           C
ANISOU 1968  CG  ASN D 129    17711  18276  19470  -1567  -2061  -3513       C
ATOM   1969  OD1 ASN D 129     -29.846-116.375 -27.845  1.00154.87           O
ANISOU 1969  OD1 ASN D 129    18838  19403  20602  -1552  -1944  -3590       O
ATOM   1970  ND2 ASN D 129     -31.938-116.856 -28.534  1.00140.45           N
ANISOU 1970  ND2 ASN D 129    17058  17533  18775  -1603  -2185  -3497       N
ATOM   1971  N   ASN D 130     -29.692-112.245 -28.166  1.00103.08           N
ANISOU 1971  N   ASN D 130    12367  12956  13842  -1542  -1853  -3490       N
ATOM   1972  CA  ASN D 130     -29.051-111.114 -27.495  1.00115.94           C
ANISOU 1972  CA  ASN D 130    13947  14634  15472  -1504  -1763  -3469       C
ATOM   1973  C   ASN D 130     -27.786-110.675 -28.185  1.00118.52           C
ANISOU 1973  C   ASN D 130    14369  14961  15702  -1521  -1648  -3545       C
ATOM   1974  O   ASN D 130     -27.469-111.162 -29.272  1.00119.27           O
ANISOU 1974  O   ASN D 130    14578  15021  15718  -1561  -1640  -3611       O
ATOM   1975  CB  ASN D 130     -28.710-111.494 -26.052  1.00 96.05           C
ANISOU 1975  CB  ASN D 130    11270  12142  13082  -1446  -1714  -3452       C
ATOM   1976  CG  ASN D 130     -27.708-112.638 -25.973  1.00119.95           C
ANISOU 1976  CG  ASN D 130    14285  15145  16146  -1446  -1631  -3535       C
ATOM   1977  OD1 ASN D 130     -27.598-113.451 -26.897  1.00111.26           O
ANISOU 1977  OD1 ASN D 130    13276  14000  14998  -1484  -1646  -3596       O
ATOM   1978  ND2 ASN D 130     -26.968-112.703 -24.869  1.00149.99           N
ANISOU 1978  ND2 ASN D 130    17976  18978  20034  -1401  -1543  -3538       N
ATOM   1979  N   THR D 131     -27.062-109.759 -27.543  1.00104.33           N
ANISOU 1979  N   THR D 131    12526  13204  13911  -1488  -1561  -3531       N
ATOM   1980  CA  THR D 131     -25.695-109.441 -27.957  1.00121.59           C
ANISOU 1980  CA  THR D 131    14776  15397  16027  -1494  -1437  -3596       C
ATOM   1981  C   THR D 131     -24.697-110.001 -26.942  1.00108.25           C
ANISOU 1981  C   THR D 131    12986  13719  14426  -1454  -1333  -3624       C
ATOM   1982  O   THR D 131     -24.657-109.570 -25.787  1.00105.50           O
ANISOU 1982  O   THR D 131    12525  13402  14156  -1412  -1310  -3576       O
ATOM   1983  CB  THR D 131     -25.468-107.933 -28.105  1.00114.60           C
ANISOU 1983  CB  THR D 131    13927  14546  15071  -1493  -1410  -3561       C
ATOM   1984  OG1 THR D 131     -26.450-107.381 -28.988  1.00100.34           O
ANISOU 1984  OG1 THR D 131    12202  12732  13189  -1531  -1509  -3528       O
ATOM   1985  CG2 THR D 131     -24.106-107.671 -28.683  1.00 73.82           C
ANISOU 1985  CG2 THR D 131     8837   9386   9826  -1505  -1294  -3622       C
ATOM   1986  N   GLU D 132     -23.897-110.962 -27.394  1.00106.70           N
ANISOU 1986  N   GLU D 132    12833  13494  14214  -1468  -1269  -3701       N
ATOM   1987  CA  GLU D 132     -22.941-111.670 -26.553  1.00 97.61           C
ANISOU 1987  CA  GLU D 132    11595  12348  13145  -1438  -1169  -3733       C
ATOM   1988  C   GLU D 132     -21.575-111.005 -26.556  1.00 97.30           C
ANISOU 1988  C   GLU D 132    11581  12333  13055  -1430  -1036  -3758       C
ATOM   1989  O   GLU D 132     -20.952-110.841 -27.604  1.00 94.75           O
ANISOU 1989  O   GLU D 132    11375  12001  12624  -1456   -992  -3803       O
ATOM   1990  CB  GLU D 132     -22.742-113.091 -27.056  1.00106.39           C
ANISOU 1990  CB  GLU D 132    12743  13415  14264  -1456  -1166  -3804       C
ATOM   1991  CG  GLU D 132     -23.758-114.083 -26.598  1.00124.74           C
ANISOU 1991  CG  GLU D 132    14992  15717  16687  -1452  -1268  -3783       C
ATOM   1992  CD  GLU D 132     -23.344-115.482 -26.966  1.00140.58           C
ANISOU 1992  CD  GLU D 132    17026  17679  18709  -1464  -1246  -3858       C
ATOM   1993  OE1 GLU D 132     -22.119-115.725 -27.063  1.00118.55           O
ANISOU 1993  OE1 GLU D 132    14259  14888  15896  -1458  -1125  -3916       O
ATOM   1994  OE2 GLU D 132     -24.239-116.327 -27.177  1.00143.19           O
ANISOU 1994  OE2 GLU D 132    17359  17974  19072  -1480  -1352  -3855       O
ATOM   1995  N   PHE D 133     -21.096-110.668 -25.367  1.00106.46           N
ANISOU 1995  N   PHE D 133    12628  13526  14296  -1392   -973  -3725       N
ATOM   1996  CA  PHE D 133     -19.778-110.097 -25.201  1.00 93.97           C
ANISOU 1996  CA  PHE D 133    11053  11967  12684  -1383   -847  -3737       C
ATOM   1997  C   PHE D 133     -18.846-111.272 -24.936  1.00101.10           C
ANISOU 1997  C   PHE D 133    11918  12855  13638  -1376   -753  -3793       C
ATOM   1998  O   PHE D 133     -18.873-111.854 -23.861  1.00115.37           O
ANISOU 1998  O   PHE D 133    13603  14670  15563  -1349   -739  -3780       O
ATOM   1999  CB  PHE D 133     -19.829-109.171 -23.991  1.00 91.92           C
ANISOU 1999  CB  PHE D 133    10687  11746  12491  -1346   -838  -3669       C
ATOM   2000  CG  PHE D 133     -18.530-108.496 -23.671  1.00102.46           C
ANISOU 2000  CG  PHE D 133    12018  13106  13806  -1335   -718  -3668       C
ATOM   2001  CD1 PHE D 133     -18.237-107.245 -24.185  1.00128.85           C
ANISOU 2001  CD1 PHE D 133    15438  16466  17054  -1347   -708  -3645       C
ATOM   2002  CD2 PHE D 133     -17.618-109.097 -22.830  1.00 85.99           C
ANISOU 2002  CD2 PHE D 133     9846  11027  11799  -1315   -620  -3683       C
ATOM   2003  CE1 PHE D 133     -17.047-106.621 -23.888  1.00125.21           C
ANISOU 2003  CE1 PHE D 133    14973  16026  16576  -1339   -605  -3636       C
ATOM   2004  CE2 PHE D 133     -16.429-108.480 -22.528  1.00101.39           C
ANISOU 2004  CE2 PHE D 133    11792  12999  13732  -1308   -513  -3674       C
ATOM   2005  CZ  PHE D 133     -16.139-107.241 -23.059  1.00 97.74           C
ANISOU 2005  CZ  PHE D 133    11412  12553  13174  -1320   -507  -3649       C
ATOM   2006  N   THR D 134     -18.007-111.613 -25.906  1.00 86.19           N
ANISOU 2006  N   THR D 134    10135  10950  11664  -1398   -686  -3854       N
ATOM   2007  CA  THR D 134     -17.221-112.843 -25.809  1.00112.90           C
ANISOU 2007  CA  THR D 134    13497  14313  15087  -1393   -605  -3911       C
ATOM   2008  C   THR D 134     -15.851-112.764 -26.469  1.00117.34           C
ANISOU 2008  C   THR D 134    14143  14879  15561  -1400   -481  -3953       C
ATOM   2009  O   THR D 134     -15.565-111.848 -27.238  1.00122.38           O
ANISOU 2009  O   THR D 134    14875  15532  16091  -1414   -468  -3945       O
ATOM   2010  CB  THR D 134     -17.961-114.058 -26.420  1.00128.58           C
ANISOU 2010  CB  THR D 134    15524  16252  17079  -1411   -686  -3959       C
ATOM   2011  OG1 THR D 134     -17.144-115.233 -26.287  1.00120.64           O
ANISOU 2011  OG1 THR D 134    14497  15226  16115  -1403   -603  -4016       O
ATOM   2012  CG2 THR D 134     -18.268-113.826 -27.902  1.00105.33           C
ANISOU 2012  CG2 THR D 134    12740  13284  13996  -1445   -739  -3991       C
ATOM   2013  N   ARG D 135     -14.996-113.729 -26.154  1.00 91.62           N
ANISOU 2013  N   ARG D 135    10847  11613  12352  -1388   -388  -3992       N
ATOM   2014  CA  ARG D 135     -13.773-113.880 -26.911  1.00 91.46           C
ANISOU 2014  CA  ARG D 135    10916  11592  12244  -1393   -276  -4036       C
ATOM   2015  C   ARG D 135     -14.158-114.158 -28.357  1.00127.78           C
ANISOU 2015  C   ARG D 135    15664  16160  16726  -1418   -334  -4087       C
ATOM   2016  O   ARG D 135     -15.199-114.761 -28.637  1.00117.03           O
ANISOU 2016  O   ARG D 135    14320  14765  15382  -1430   -441  -4107       O
ATOM   2017  CB  ARG D 135     -12.901-115.017 -26.365  1.00113.75           C
ANISOU 2017  CB  ARG D 135    13674  14404  15141  -1377   -175  -4071       C
ATOM   2018  CG  ARG D 135     -11.407-114.830 -26.677  1.00164.11           C
ANISOU 2018  CG  ARG D 135    20100  20802  21453  -1372    -29  -4082       C
ATOM   2019  CD  ARG D 135     -10.540-115.994 -26.198  1.00156.75           C
ANISOU 2019  CD  ARG D 135    19109  19859  20591  -1357     75  -4117       C
ATOM   2020  NE  ARG D 135     -10.807-116.354 -24.810  1.00160.73           N
ANISOU 2020  NE  ARG D 135    19453  20370  21247  -1344     70  -4087       N
ATOM   2021  CZ  ARG D 135      -9.870-116.497 -23.879  1.00162.69           C
ANISOU 2021  CZ  ARG D 135    19603  20641  21571  -1331    181  -4065       C
ATOM   2022  NH1 ARG D 135      -8.598-116.309 -24.194  1.00161.92           N
ANISOU 2022  NH1 ARG D 135    19554  20559  21410  -1329    306  -4065       N
ATOM   2023  NH2 ARG D 135     -10.205-116.835 -22.639  1.00173.97           N
ANISOU 2023  NH2 ARG D 135    20885  22077  23138  -1319    167  -4039       N
ATOM   2024  N   VAL D 136     -13.313-113.701 -29.271  1.00149.75           N
ANISOU 2024  N   VAL D 136    18554  18956  19390  -1424   -265  -4105       N
ATOM   2025  CA  VAL D 136     -13.496-113.959 -30.686  1.00148.61           C
ANISOU 2025  CA  VAL D 136    18556  18786  19124  -1444   -301  -4157       C
ATOM   2026  C   VAL D 136     -12.112-114.147 -31.303  1.00135.09           C
ANISOU 2026  C   VAL D 136    16915  17085  17328  -1432   -170  -4192       C
ATOM   2027  O   VAL D 136     -11.186-113.425 -30.961  1.00109.77           O
ANISOU 2027  O   VAL D 136    13679  13917  14110  -1421    -78  -4152       O
ATOM   2028  CB  VAL D 136     -14.265-112.795 -31.361  1.00131.47           C
ANISOU 2028  CB  VAL D 136    16454  16630  16869  -1469   -393  -4122       C
ATOM   2029  CG1 VAL D 136     -13.733-111.437 -30.888  1.00 91.52           C
ANISOU 2029  CG1 VAL D 136    11354  11621  11800  -1462   -344  -4055       C
ATOM   2030  CG2 VAL D 136     -14.233-112.923 -32.891  1.00151.37           C
ANISOU 2030  CG2 VAL D 136    19132  19133  19248  -1490   -411  -4174       C
ATOM   2031  N   ASN D 137     -11.964-115.124 -32.195  1.00134.32           N
ANISOU 2031  N   ASN D 137    16912  16953  17172  -1433   -161  -4263       N
ATOM   2032  CA  ASN D 137     -10.673-115.368 -32.833  1.00113.30           C
ANISOU 2032  CA  ASN D 137    14325  14302  14424  -1416    -37  -4296       C
ATOM   2033  C   ASN D 137     -10.146-114.096 -33.465  1.00119.55           C
ANISOU 2033  C   ASN D 137    15181  15139  15102  -1421     -2  -4256       C
ATOM   2034  O   ASN D 137     -10.892-113.344 -34.095  1.00130.24           O
ANISOU 2034  O   ASN D 137    16595  16498  16391  -1445    -92  -4241       O
ATOM   2035  CB  ASN D 137     -10.763-116.429 -33.928  1.00110.18           C
ANISOU 2035  CB  ASN D 137    14049  13861  13953  -1415    -55  -4379       C
ATOM   2036  CG  ASN D 137     -11.524-117.663 -33.502  1.00147.44           C
ANISOU 2036  CG  ASN D 137    18722  18527  18771  -1417   -124  -4421       C
ATOM   2037  OD1 ASN D 137     -10.925-118.703 -33.214  1.00147.24           O
ANISOU 2037  OD1 ASN D 137    18671  18481  18793  -1397    -54  -4460       O
ATOM   2038  ND2 ASN D 137     -12.855-117.571 -33.499  1.00143.63           N
ANISOU 2038  ND2 ASN D 137    18232  18021  18319  -1443   -266  -4409       N
ATOM   2039  N   ALA D 138      -8.852-113.862 -33.315  1.00109.14           N
ANISOU 2039  N   ALA D 138    13851  13855  13761  -1401    128  -4234       N
ATOM   2040  CA  ALA D 138      -8.263-112.689 -33.921  1.00123.86           C
ANISOU 2040  CA  ALA D 138    15775  15766  15520  -1404    163  -4191       C
ATOM   2041  C   ALA D 138      -6.768-112.870 -34.135  1.00139.66           C
ANISOU 2041  C   ALA D 138    17801  17794  17469  -1378    311  -4188       C
ATOM   2042  O   ALA D 138      -6.157-113.764 -33.546  1.00133.05           O
ANISOU 2042  O   ALA D 138    16910  16945  16700  -1357    394  -4206       O
ATOM   2043  CB  ALA D 138      -8.557-111.459 -33.082  1.00121.95           C
ANISOU 2043  CB  ALA D 138    15447  15555  15333  -1416    127  -4112       C
ATOM   2044  N   LYS D 139      -6.205-112.025 -35.001  1.00148.08           N
ANISOU 2044  N   LYS D 139    18949  18900  18415  -1378    341  -4162       N
ATOM   2045  CA  LYS D 139      -4.790-112.049 -35.359  1.00139.25           C
ANISOU 2045  CA  LYS D 139    17865  17815  17227  -1352    476  -4146       C
ATOM   2046  C   LYS D 139      -4.192-110.673 -35.085  1.00148.61           C
ANISOU 2046  C   LYS D 139    19016  19055  18392  -1358    508  -4054       C
ATOM   2047  O   LYS D 139      -4.916-109.669 -35.101  1.00124.35           O
ANISOU 2047  O   LYS D 139    15939  15994  15313  -1383    416  -4020       O
ATOM   2048  CB  LYS D 139      -4.627-112.358 -36.849  1.00146.83           C
ANISOU 2048  CB  LYS D 139    18972  18775  18041  -1342    480  -4199       C
ATOM   2049  CG  LYS D 139      -4.517-111.096 -37.732  1.00175.99           C
ANISOU 2049  CG  LYS D 139    22736  22518  21616  -1355    454  -4154       C
ATOM   2050  CD  LYS D 139      -5.080-111.306 -39.145  1.00193.68           C
ANISOU 2050  CD  LYS D 139    25112  24744  23732  -1361    387  -4215       C
ATOM   2051  CE  LYS D 139      -5.028-110.014 -39.967  1.00170.86           C
ANISOU 2051  CE  LYS D 139    22279  21906  20735  -1378    356  -4166       C
ATOM   2052  NZ  LYS D 139      -5.709-110.139 -41.297  1.00123.63           N
ANISOU 2052  NZ  LYS D 139    16422  15912  14640  -1391    277  -4222       N
ATOM   2053  N   PRO D 140      -2.878-110.619 -34.789  1.00152.46           N
ANISOU 2053  N   PRO D 140    19475  19575  18876  -1337    636  -4010       N
ATOM   2054  CA  PRO D 140      -2.147-109.347 -34.703  1.00138.34           C
ANISOU 2054  CA  PRO D 140    17672  17841  17051  -1341    673  -3919       C
ATOM   2055  C   PRO D 140      -1.816-108.842 -36.104  1.00128.62           C
ANISOU 2055  C   PRO D 140    16562  16645  15664  -1338    674  -3916       C
ATOM   2056  O   PRO D 140      -1.420-109.660 -36.932  1.00100.15           O
ANISOU 2056  O   PRO D 140    13035  13033  11982  -1314    725  -3968       O
ATOM   2057  CB  PRO D 140      -0.861-109.727 -33.962  1.00104.43           C
ANISOU 2057  CB  PRO D 140    13310  13563  12807  -1319    813  -3879       C
ATOM   2058  CG  PRO D 140      -1.018-111.212 -33.589  1.00112.26           C
ANISOU 2058  CG  PRO D 140    14273  14507  13873  -1304    844  -3954       C
ATOM   2059  CD  PRO D 140      -1.984-111.766 -34.575  1.00104.57           C
ANISOU 2059  CD  PRO D 140    13395  13498  12837  -1307    753  -4039       C
ATOM   2060  N   PRO D 141      -1.926-107.524 -36.359  1.00127.88           N
ANISOU 2060  N   PRO D 141    16479  16588  15522  -1358    623  -3855       N
ATOM   2061  CA  PRO D 141      -1.782-107.047 -37.739  1.00139.98           C
ANISOU 2061  CA  PRO D 141    18123  18153  16908  -1357    606  -3856       C
ATOM   2062  C   PRO D 141      -0.465-107.541 -38.326  1.00172.98           C
ANISOU 2062  C   PRO D 141    22353  22364  21006  -1320    735  -3849       C
ATOM   2063  O   PRO D 141       0.484-107.762 -37.568  1.00161.19           O
ANISOU 2063  O   PRO D 141    20796  20882  19568  -1302    838  -3807       O
ATOM   2064  CB  PRO D 141      -1.793-105.523 -37.596  1.00123.82           C
ANISOU 2064  CB  PRO D 141    16049  16148  14850  -1381    559  -3770       C
ATOM   2065  CG  PRO D 141      -2.480-105.274 -36.320  1.00125.58           C
ANISOU 2065  CG  PRO D 141    16168  16342  15206  -1399    503  -3751       C
ATOM   2066  CD  PRO D 141      -2.085-106.408 -35.417  1.00115.84           C
ANISOU 2066  CD  PRO D 141    14867  15078  14070  -1378    584  -3779       C
ATOM   2067  N   PRO D 142      -0.412-107.689 -39.661  1.00186.86           N
ANISOU 2067  N   PRO D 142    24226  24139  22633  -1307    731  -3887       N
ATOM   2068  CA  PRO D 142       0.466-108.587 -40.433  1.00197.82           C
ANISOU 2068  CA  PRO D 142    25690  25537  23934  -1263    832  -3922       C
ATOM   2069  C   PRO D 142       1.976-108.613 -40.144  1.00195.33           C
ANISOU 2069  C   PRO D 142    25342  25265  23608  -1229    977  -3851       C
ATOM   2070  O   PRO D 142       2.535-109.710 -40.056  1.00193.00           O
ANISOU 2070  O   PRO D 142    25055  24951  23324  -1195   1067  -3889       O
ATOM   2071  CB  PRO D 142       0.224-108.148 -41.889  1.00185.77           C
ANISOU 2071  CB  PRO D 142    24281  24041  22261  -1264    780  -3940       C
ATOM   2072  CG  PRO D 142      -0.450-106.808 -41.797  1.00161.28           C
ANISOU 2072  CG  PRO D 142    21149  20961  19170  -1308    677  -3886       C
ATOM   2073  CD  PRO D 142      -1.248-106.857 -40.545  1.00154.89           C
ANISOU 2073  CD  PRO D 142    20241  20103  18505  -1335    619  -3891       C
ATOM   2074  N   GLY D 143       2.626-107.462 -40.007  1.00178.67           N
ANISOU 2074  N   GLY D 143    23198  23209  21478  -1237    998  -3750       N
ATOM   2075  CA  GLY D 143       4.078-107.455 -40.023  1.00183.50           C
ANISOU 2075  CA  GLY D 143    23802  23869  22050  -1203   1131  -3677       C
ATOM   2076  C   GLY D 143       4.757-106.264 -39.381  1.00213.10           C
ANISOU 2076  C   GLY D 143    27475  27663  25831  -1220   1151  -3554       C
ATOM   2077  O   GLY D 143       4.123-105.477 -38.675  1.00248.77           O
ANISOU 2077  O   GLY D 143    31930  32167  30424  -1258   1069  -3527       O
ATOM   2078  N   ASP D 144       6.065-106.161 -39.606  1.00198.20           N
ANISOU 2078  N   ASP D 144    25594  25826  23885  -1190   1262  -3478       N
ATOM   2079  CA  ASP D 144       6.888-105.067 -39.083  1.00199.46           C
ANISOU 2079  CA  ASP D 144    25691  26033  24063  -1203   1291  -3350       C
ATOM   2080  C   ASP D 144       6.899-104.970 -37.549  1.00208.03           C
ANISOU 2080  C   ASP D 144    26659  27085  25299  -1229   1301  -3313       C
ATOM   2081  O   ASP D 144       7.210-105.954 -36.872  1.00162.51           O
ANISOU 2081  O   ASP D 144    20850  21290  19608  -1215   1380  -3340       O
ATOM   2082  CB  ASP D 144       6.590-103.711 -39.776  1.00223.75           C
ANISOU 2082  CB  ASP D 144    28801  29152  27063  -1227   1196  -3297       C
ATOM   2083  CG  ASP D 144       5.129-103.259 -39.644  1.00206.53           C
ANISOU 2083  CG  ASP D 144    26615  26932  24927  -1269   1051  -3356       C
ATOM   2084  OD1 ASP D 144       4.769-102.677 -38.598  1.00185.26           O
ANISOU 2084  OD1 ASP D 144    23839  24215  22336  -1300   1003  -3322       O
ATOM   2085  OD2 ASP D 144       4.346-103.453 -40.601  1.00200.75           O
ANISOU 2085  OD2 ASP D 144    25961  26191  24122  -1270    984  -3430       O
ATOM   2086  N   GLN D 145       6.576-103.794 -37.007  1.00239.83           N
ANISOU 2086  N   GLN D 145    30635  31119  29372  -1266   1222  -3252       N
ATOM   2087  CA  GLN D 145       6.686-103.550 -35.565  1.00221.87           C
ANISOU 2087  CA  GLN D 145    28251  28820  27231  -1288   1232  -3203       C
ATOM   2088  C   GLN D 145       5.636-104.315 -34.770  1.00200.10           C
ANISOU 2088  C   GLN D 145    25445  25998  24586  -1299   1186  -3296       C
ATOM   2089  O   GLN D 145       5.743-104.452 -33.549  1.00203.09           O
ANISOU 2089  O   GLN D 145    25730  26353  25082  -1310   1212  -3274       O
ATOM   2090  CB  GLN D 145       6.586-102.051 -35.252  1.00209.92           C
ANISOU 2090  CB  GLN D 145    26705  27328  25727  -1320   1152  -3115       C
ATOM   2091  CG  GLN D 145       6.515-101.156 -36.483  1.00199.09           C
ANISOU 2091  CG  GLN D 145    25413  26004  24229  -1323   1090  -3088       C
ATOM   2092  CD  GLN D 145       5.139-100.563 -36.706  1.00174.73           C
ANISOU 2092  CD  GLN D 145    22347  22895  21147  -1353    947  -3141       C
ATOM   2093  OE1 GLN D 145       4.546 -99.987 -35.792  1.00193.03           O
ANISOU 2093  OE1 GLN D 145    24602  25185  23555  -1379    878  -3127       O
ATOM   2094  NE2 GLN D 145       4.623-100.699 -37.927  1.00138.81           N
ANISOU 2094  NE2 GLN D 145    17886  18358  16497  -1347    902  -3200       N
ATOM   2095  N   PHE D 146       4.629-104.818 -35.474  1.00170.90           N
ANISOU 2095  N   PHE D 146    21809  22273  20852  -1298   1115  -3396       N
ATOM   2096  CA  PHE D 146       3.530-105.531 -34.845  1.00167.69           C
ANISOU 2096  CA  PHE D 146    21363  21807  20544  -1309   1055  -3482       C
ATOM   2097  C   PHE D 146       3.906-106.981 -34.556  1.00181.69           C
ANISOU 2097  C   PHE D 146    23119  23551  22362  -1282   1151  -3539       C
ATOM   2098  O   PHE D 146       3.158-107.711 -33.917  1.00191.55           O
ANISOU 2098  O   PHE D 146    24322  24752  23706  -1288   1118  -3603       O
ATOM   2099  CB  PHE D 146       2.301-105.494 -35.748  1.00172.53           C
ANISOU 2099  CB  PHE D 146    22054  22402  21099  -1320    937  -3559       C
ATOM   2100  CG  PHE D 146       1.908-104.110 -36.187  1.00178.73           C
ANISOU 2100  CG  PHE D 146    22864  23217  21827  -1346    843  -3509       C
ATOM   2101  CD1 PHE D 146       2.107-103.013 -35.361  1.00177.15           C
ANISOU 2101  CD1 PHE D 146    22593  23033  21683  -1365    822  -3421       C
ATOM   2102  CD2 PHE D 146       1.336-103.907 -37.435  1.00179.84           C
ANISOU 2102  CD2 PHE D 146    23101  23369  21859  -1351    774  -3549       C
ATOM   2103  CE1 PHE D 146       1.739-101.740 -35.774  1.00177.59           C
ANISOU 2103  CE1 PHE D 146    22673  23115  21689  -1389    733  -3375       C
ATOM   2104  CE2 PHE D 146       0.968-102.637 -37.851  1.00170.94           C
ANISOU 2104  CE2 PHE D 146    21994  22272  20684  -1376    688  -3502       C
ATOM   2105  CZ  PHE D 146       1.169-101.554 -37.019  1.00167.71           C
ANISOU 2105  CZ  PHE D 146    21512  21877  20332  -1395    667  -3415       C
ATOM   2106  N   LYS D 147       5.070-107.397 -35.035  1.00187.09           N
ANISOU 2106  N   LYS D 147    23841  24267  22980  -1252   1268  -3512       N
ATOM   2107  CA  LYS D 147       5.516-108.779 -34.880  1.00182.79           C
ANISOU 2107  CA  LYS D 147    23290  23697  22465  -1223   1367  -3565       C
ATOM   2108  C   LYS D 147       5.589-109.225 -33.418  1.00169.50           C
ANISOU 2108  C   LYS D 147    21484  21984  20936  -1236   1407  -3553       C
ATOM   2109  O   LYS D 147       5.407-110.399 -33.105  1.00144.08           O
ANISOU 2109  O   LYS D 147    18242  18726  17777  -1224   1439  -3623       O
ATOM   2110  CB  LYS D 147       6.870-108.977 -35.581  1.00181.97           C
ANISOU 2110  CB  LYS D 147    23241  23641  22260  -1186   1494  -3515       C
ATOM   2111  CG  LYS D 147       6.804-108.726 -37.078  1.00182.13           C
ANISOU 2111  CG  LYS D 147    23385  23692  22124  -1166   1463  -3537       C
ATOM   2112  CD  LYS D 147       8.164-108.704 -37.742  1.00172.52           C
ANISOU 2112  CD  LYS D 147    22214  22534  20803  -1126   1582  -3467       C
ATOM   2113  CE  LYS D 147       7.991-108.601 -39.251  1.00168.16           C
ANISOU 2113  CE  LYS D 147    21786  22009  20097  -1102   1547  -3504       C
ATOM   2114  NZ  LYS D 147       9.272-108.743 -39.988  1.00168.78           N
ANISOU 2114  NZ  LYS D 147    21917  22146  20065  -1052   1666  -3445       N
ATOM   2115  N   HIS D 148       5.845-108.279 -32.523  1.00173.83           N
ANISOU 2115  N   HIS D 148    21951  22548  21547  -1260   1400  -3466       N
ATOM   2116  CA  HIS D 148       6.080-108.601 -31.119  1.00178.78           C
ANISOU 2116  CA  HIS D 148    22459  23156  22315  -1271   1450  -3440       C
ATOM   2117  C   HIS D 148       4.791-108.831 -30.325  1.00164.86           C
ANISOU 2117  C   HIS D 148    20630  21345  20664  -1290   1348  -3504       C
ATOM   2118  O   HIS D 148       4.843-109.218 -29.151  1.00123.35           O
ANISOU 2118  O   HIS D 148    15269  16069  15530  -1298   1380  -3495       O
ATOM   2119  CB  HIS D 148       6.882-107.479 -30.464  1.00185.50           C
ANISOU 2119  CB  HIS D 148    23254  24043  23187  -1289   1480  -3317       C
ATOM   2120  CG  HIS D 148       6.081-106.244 -30.209  1.00168.07           C
ANISOU 2120  CG  HIS D 148    21030  21834  20994  -1317   1355  -3289       C
ATOM   2121  ND1 HIS D 148       5.330-106.071 -29.066  1.00175.64           N
ANISOU 2121  ND1 HIS D 148    21899  22761  22074  -1336   1292  -3298       N
ATOM   2122  CD2 HIS D 148       5.900-105.125 -30.951  1.00153.88           C
ANISOU 2122  CD2 HIS D 148    19295  20065  19106  -1326   1281  -3253       C
ATOM   2123  CE1 HIS D 148       4.728-104.895 -29.112  1.00196.98           C
ANISOU 2123  CE1 HIS D 148    24614  25471  24758  -1355   1186  -3268       C
ATOM   2124  NE2 HIS D 148       5.058-104.303 -30.245  1.00184.53           N
ANISOU 2124  NE2 HIS D 148    23128  23930  23056  -1351   1176  -3241       N
ATOM   2125  N   LEU D 149       3.649-108.559 -30.959  1.00175.77           N
ANISOU 2125  N   LEU D 149    22071  22711  22004  -1299   1226  -3560       N
ATOM   2126  CA  LEU D 149       2.338-108.711 -30.325  1.00126.00           C
ANISOU 2126  CA  LEU D 149    15713  16365  15794  -1315   1117  -3614       C
ATOM   2127  C   LEU D 149       1.850-110.147 -30.382  1.00125.73           C
ANISOU 2127  C   LEU D 149    15681  16289  15802  -1302   1122  -3712       C
ATOM   2128  O   LEU D 149       0.983-110.533 -29.610  1.00151.31           O
ANISOU 2128  O   LEU D 149    18849  19494  19147  -1311   1061  -3747       O
ATOM   2129  CB  LEU D 149       1.288-107.795 -30.966  1.00 91.22           C
ANISOU 2129  CB  LEU D 149    11368  11963  11330  -1332    981  -3625       C
ATOM   2130  CG  LEU D 149       1.409-106.275 -30.819  1.00113.22           C
ANISOU 2130  CG  LEU D 149    14145  14782  14092  -1351    937  -3537       C
ATOM   2131  CD1 LEU D 149       2.745-105.790 -31.322  1.00166.87           C
ANISOU 2131  CD1 LEU D 149    20979  21624  20799  -1342   1031  -3462       C
ATOM   2132  CD2 LEU D 149       0.317-105.566 -31.585  1.00100.44           C
ANISOU 2132  CD2 LEU D 149    12593  13161  12409  -1367    807  -3562       C
ATOM   2133  N   ILE D 150       2.404-110.940 -31.294  1.00138.33           N
ANISOU 2133  N   ILE D 150    17358  17886  17315  -1278   1191  -3753       N
ATOM   2134  CA  ILE D 150       1.929-112.313 -31.489  1.00166.43           C
ANISOU 2134  CA  ILE D 150    20936  21400  20901  -1264   1187  -3851       C
ATOM   2135  C   ILE D 150       2.017-113.210 -30.237  1.00164.90           C
ANISOU 2135  C   ILE D 150    20621  21180  20855  -1264   1237  -3862       C
ATOM   2136  O   ILE D 150       1.104-114.004 -29.985  1.00135.91           O
ANISOU 2136  O   ILE D 150    16923  17465  17252  -1267   1172  -3932       O
ATOM   2137  CB  ILE D 150       2.577-113.014 -32.740  1.00160.26           C
ANISOU 2137  CB  ILE D 150    20274  20624  19993  -1231   1257  -3894       C
ATOM   2138  CG1 ILE D 150       3.490-114.176 -32.325  1.00160.68           C
ANISOU 2138  CG1 ILE D 150    20289  20668  20096  -1206   1389  -3907       C
ATOM   2139  CG2 ILE D 150       3.283-112.001 -33.650  1.00111.82           C
ANISOU 2139  CG2 ILE D 150    14218  14543  13723  -1224   1284  -3830       C
ATOM   2140  CD1 ILE D 150       2.834-115.557 -32.426  1.00117.87           C
ANISOU 2140  CD1 ILE D 150    14881  15189  14715  -1195   1360  -4014       C
ATOM   2141  N   PRO D 151       3.108-113.092 -29.455  1.00152.69           N
ANISOU 2141  N   PRO D 151    18999  19659  19358  -1261   1350  -3791       N
ATOM   2142  CA  PRO D 151       3.255-113.915 -28.245  1.00107.13           C
ANISOU 2142  CA  PRO D 151    13107  13868  13730  -1264   1405  -3796       C
ATOM   2143  C   PRO D 151       2.248-113.547 -27.171  1.00127.47           C
ANISOU 2143  C   PRO D 151    15579  16427  16426  -1286   1306  -3790       C
ATOM   2144  O   PRO D 151       1.878-114.410 -26.369  1.00118.00           O
ANISOU 2144  O   PRO D 151    14291  15201  15342  -1287   1304  -3826       O
ATOM   2145  CB  PRO D 151       4.655-113.566 -27.757  1.00121.69           C
ANISOU 2145  CB  PRO D 151    14904  15750  15580  -1262   1538  -3702       C
ATOM   2146  CG  PRO D 151       4.913-112.199 -28.315  1.00162.42           C
ANISOU 2146  CG  PRO D 151    20125  20948  20638  -1269   1509  -3631       C
ATOM   2147  CD  PRO D 151       4.267-112.205 -29.657  1.00150.92           C
ANISOU 2147  CD  PRO D 151    18796  19485  19062  -1258   1432  -3696       C
ATOM   2148  N   LEU D 152       1.831-112.278 -27.165  1.00147.77           N
ANISOU 2148  N   LEU D 152    18160  19018  18969  -1302   1226  -3742       N
ATOM   2149  CA  LEU D 152       0.830-111.748 -26.234  1.00119.73           C
ANISOU 2149  CA  LEU D 152    14524  15456  15514  -1318   1123  -3729       C
ATOM   2150  C   LEU D 152      -0.465-112.531 -26.320  1.00117.51           C
ANISOU 2150  C   LEU D 152    14239  15133  15276  -1318   1020  -3814       C
ATOM   2151  O   LEU D 152      -1.042-112.906 -25.308  1.00135.14           O
ANISOU 2151  O   LEU D 152    16366  17349  17632  -1320    986  -3822       O
ATOM   2152  CB  LEU D 152       0.521-110.293 -26.574  1.00 99.53           C
ANISOU 2152  CB  LEU D 152    12012  12920  12885  -1331   1043  -3678       C
ATOM   2153  CG  LEU D 152       1.681-109.307 -26.483  1.00111.08           C
ANISOU 2153  CG  LEU D 152    13478  14424  14303  -1336   1119  -3582       C
ATOM   2154  CD1 LEU D 152       1.417-108.049 -27.305  1.00118.03           C
ANISOU 2154  CD1 LEU D 152    14444  15327  15076  -1346   1040  -3549       C
ATOM   2155  CD2 LEU D 152       1.959-108.951 -25.046  1.00 80.76           C
ANISOU 2155  CD2 LEU D 152     9514  10589  10583  -1345   1147  -3520       C
ATOM   2156  N   MET D 153      -0.892-112.787 -27.549  1.00 99.51           N
ANISOU 2156  N   MET D 153    12077  12839  12895  -1313    970  -3872       N
ATOM   2157  CA  MET D 153      -2.159-113.428 -27.839  1.00123.73           C
ANISOU 2157  CA  MET D 153    15165  15866  15982  -1317    858  -3947       C
ATOM   2158  C   MET D 153      -2.401-114.654 -26.965  1.00127.59           C
ANISOU 2158  C   MET D 153    15554  16324  16601  -1311    873  -3987       C
ATOM   2159  O   MET D 153      -3.516-114.881 -26.492  1.00153.42           O
ANISOU 2159  O   MET D 153    18770  19571  19950  -1317    771  -4009       O
ATOM   2160  CB  MET D 153      -2.182-113.840 -29.313  1.00135.66           C
ANISOU 2160  CB  MET D 153    16820  17364  17359  -1309    847  -4008       C
ATOM   2161  CG  MET D 153      -3.465-113.477 -30.074  1.00147.44           C
ANISOU 2161  CG  MET D 153    18387  18837  18795  -1324    702  -4043       C
ATOM   2162  SD  MET D 153      -3.467-111.791 -30.688  1.00111.96           S
ANISOU 2162  SD  MET D 153    13960  14388  14193  -1340    656  -3977       S
ATOM   2163  CE  MET D 153      -1.838-111.275 -30.200  1.00111.65           C
ANISOU 2163  CE  MET D 153    13878  14395  14151  -1328    807  -3895       C
ATOM   2164  N   TYR D 154      -1.354-115.438 -26.745  1.00114.60           N
ANISOU 2164  N   TYR D 154    13882  14681  14980  -1297    999  -3991       N
ATOM   2165  CA  TYR D 154      -1.465-116.666 -25.960  1.00147.81           C
ANISOU 2165  CA  TYR D 154    17992  18859  19309  -1292   1025  -4030       C
ATOM   2166  C   TYR D 154      -1.535-116.438 -24.438  1.00161.73           C
ANISOU 2166  C   TYR D 154    19595  20636  21218  -1301   1033  -3976       C
ATOM   2167  O   TYR D 154      -1.866-117.357 -23.679  1.00149.16           O
ANISOU 2167  O   TYR D 154    17907  19024  19743  -1299   1027  -4004       O
ATOM   2168  CB  TYR D 154      -0.322-117.627 -26.313  1.00148.09           C
ANISOU 2168  CB  TYR D 154    18060  18891  19316  -1274   1160  -4055       C
ATOM   2169  CG  TYR D 154      -0.494-118.345 -27.642  1.00128.37           C
ANISOU 2169  CG  TYR D 154    15700  16364  16710  -1259   1139  -4135       C
ATOM   2170  CD1 TYR D 154      -0.189-117.717 -28.846  1.00139.44           C
ANISOU 2170  CD1 TYR D 154    17237  17784  17959  -1252   1142  -4131       C
ATOM   2171  CD2 TYR D 154      -0.953-119.657 -27.689  1.00137.87           C
ANISOU 2171  CD2 TYR D 154    16899  17521  17964  -1252   1113  -4213       C
ATOM   2172  CE1 TYR D 154      -0.345-118.378 -30.063  1.00158.08           C
ANISOU 2172  CE1 TYR D 154    19728  20119  20218  -1235   1123  -4206       C
ATOM   2173  CE2 TYR D 154      -1.111-120.323 -28.898  1.00157.94           C
ANISOU 2173  CE2 TYR D 154    19574  20032  20406  -1237   1090  -4288       C
ATOM   2174  CZ  TYR D 154      -0.807-119.683 -30.080  1.00167.82           C
ANISOU 2174  CZ  TYR D 154    20960  21302  21502  -1228   1096  -4285       C
ATOM   2175  OH  TYR D 154      -0.969-120.358 -31.273  1.00182.01           O
ANISOU 2175  OH  TYR D 154    22890  23068  23197  -1210   1073  -4361       O
ATOM   2176  N   LYS D 155      -1.233-115.218 -23.996  1.00156.20           N
ANISOU 2176  N   LYS D 155    18868  19971  20511  -1309   1041  -3899       N
ATOM   2177  CA  LYS D 155      -1.351-114.873 -22.579  1.00148.12           C
ANISOU 2177  CA  LYS D 155    17702  18962  19616  -1315   1039  -3846       C
ATOM   2178  C   LYS D 155      -2.073-113.527 -22.379  1.00144.11           C
ANISOU 2178  C   LYS D 155    17194  18468  19091  -1322    936  -3799       C
ATOM   2179  O   LYS D 155      -1.545-112.465 -22.725  1.00150.64           O
ANISOU 2179  O   LYS D 155    18078  19321  19837  -1327    956  -3747       O
ATOM   2180  CB  LYS D 155       0.039-114.845 -21.925  1.00171.55           C
ANISOU 2180  CB  LYS D 155    20609  21955  22617  -1316   1186  -3787       C
ATOM   2181  CG  LYS D 155       1.060-113.944 -22.627  1.00166.46           C
ANISOU 2181  CG  LYS D 155    20056  21340  21850  -1319   1254  -3732       C
ATOM   2182  CD  LYS D 155       2.360-113.793 -21.822  1.00144.25           C
ANISOU 2182  CD  LYS D 155    17169  18554  19084  -1325   1388  -3656       C
ATOM   2183  CE  LYS D 155       2.978-115.141 -21.465  1.00146.08           C
ANISOU 2183  CE  LYS D 155    17342  18775  19388  -1319   1496  -3686       C
ATOM   2184  NZ  LYS D 155       3.299-115.973 -22.663  1.00147.93           N
ANISOU 2184  NZ  LYS D 155    17686  18995  19527  -1302   1539  -3746       N
ATOM   2185  N   GLY D 156      -3.268-113.566 -21.790  1.00112.60           N
ANISOU 2185  N   GLY D 156    13136  14465  15181  -1320    827  -3812       N
ATOM   2186  CA  GLY D 156      -4.077-112.362 -21.655  1.00 86.76           C
ANISOU 2186  CA  GLY D 156     9871  11204  11892  -1322    721  -3773       C
ATOM   2187  C   GLY D 156      -5.261-112.490 -20.701  1.00115.75           C
ANISOU 2187  C   GLY D 156    13435  14867  15678  -1314    622  -3773       C
ATOM   2188  O   GLY D 156      -5.809-113.580 -20.490  1.00107.52           O
ANISOU 2188  O   GLY D 156    12342  13803  14708  -1308    594  -3820       O
ATOM   2189  N   LEU D 157      -5.687-111.360 -20.146  1.00116.65           N
ANISOU 2189  N   LEU D 157    13517  14999  15806  -1310    562  -3719       N
ATOM   2190  CA  LEU D 157      -6.637-111.369 -19.031  1.00126.72           C
ANISOU 2190  CA  LEU D 157    14673  16277  17197  -1294    486  -3702       C
ATOM   2191  C   LEU D 157      -8.088-111.183 -19.418  1.00107.15           C
ANISOU 2191  C   LEU D 157    12227  13784  14701  -1289    340  -3719       C
ATOM   2192  O   LEU D 157      -8.416-110.277 -20.178  1.00113.75           O
ANISOU 2192  O   LEU D 157    13158  14622  15439  -1297    282  -3707       O
ATOM   2193  CB  LEU D 157      -6.255-110.316 -17.989  1.00144.39           C
ANISOU 2193  CB  LEU D 157    16841  18543  19478  -1286    510  -3628       C
ATOM   2194  CG  LEU D 157      -5.064-110.720 -17.128  1.00129.49           C
ANISOU 2194  CG  LEU D 157    14867  16669  17664  -1288    642  -3603       C
ATOM   2195  CD1 LEU D 157      -5.049-112.237 -17.069  1.00125.50           C
ANISOU 2195  CD1 LEU D 157    14310  16147  17229  -1288    682  -3660       C
ATOM   2196  CD2 LEU D 157      -3.749-110.178 -17.696  1.00114.13           C
ANISOU 2196  CD2 LEU D 157    13004  14735  15626  -1305    743  -3572       C
ATOM   2197  N   PRO D 158      -8.972-112.027 -18.869  1.00117.32           N
ANISOU 2197  N   PRO D 158    13428  15061  16087  -1277    279  -3741       N
ATOM   2198  CA  PRO D 158     -10.393-111.816 -19.142  1.00116.36           C
ANISOU 2198  CA  PRO D 158    13327  14928  15955  -1272    136  -3744       C
ATOM   2199  C   PRO D 158     -10.717-110.347 -18.917  1.00108.41           C
ANISOU 2199  C   PRO D 158    12335  13944  14913  -1263     85  -3684       C
ATOM   2200  O   PRO D 158     -10.130-109.736 -18.037  1.00105.99           O
ANISOU 2200  O   PRO D 158    11964  13659  14646  -1251    139  -3637       O
ATOM   2201  CB  PRO D 158     -11.079-112.707 -18.103  1.00118.92           C
ANISOU 2201  CB  PRO D 158    13511  15252  16421  -1252     97  -3745       C
ATOM   2202  CG  PRO D 158     -10.116-113.840 -17.925  1.00137.55           C
ANISOU 2202  CG  PRO D 158    15829  17603  18830  -1259    209  -3782       C
ATOM   2203  CD  PRO D 158      -8.739-113.215 -18.025  1.00128.03           C
ANISOU 2203  CD  PRO D 158    14666  16413  17565  -1269    333  -3760       C
ATOM   2204  N   TRP D 159     -11.605-109.768 -19.712  1.00131.13           N
ANISOU 2204  N   TRP D 159    15299  16813  17712  -1270    -18  -3684       N
ATOM   2205  CA  TRP D 159     -11.766-108.320 -19.663  1.00131.70           C
ANISOU 2205  CA  TRP D 159    15403  16904  17732  -1266    -57  -3630       C
ATOM   2206  C   TRP D 159     -12.217-107.805 -18.296  1.00121.32           C
ANISOU 2206  C   TRP D 159    13968  15611  16517  -1232    -90  -3574       C
ATOM   2207  O   TRP D 159     -11.812-106.723 -17.876  1.00118.35           O
ANISOU 2207  O   TRP D 159    13589  15253  16125  -1224    -70  -3527       O
ATOM   2208  CB  TRP D 159     -12.660-107.808 -20.804  1.00124.58           C
ANISOU 2208  CB  TRP D 159    14616  15991  16728  -1282   -160  -3639       C
ATOM   2209  CG  TRP D 159     -11.882-107.026 -21.828  1.00108.53           C
ANISOU 2209  CG  TRP D 159    12705  13964  14568  -1307   -118  -3639       C
ATOM   2210  CD1 TRP D 159     -11.487-107.451 -23.065  1.00126.20           C
ANISOU 2210  CD1 TRP D 159    15051  16187  16710  -1332    -90  -3686       C
ATOM   2211  CD2 TRP D 159     -11.379-105.697 -21.687  1.00 94.51           C
ANISOU 2211  CD2 TRP D 159    10952  12211  12747  -1306   -100  -3585       C
ATOM   2212  NE1 TRP D 159     -10.777-106.463 -23.705  1.00113.30           N
ANISOU 2212  NE1 TRP D 159    13502  14571  14976  -1345    -54  -3663       N
ATOM   2213  CE2 TRP D 159     -10.698-105.365 -22.871  1.00 88.58           C
ANISOU 2213  CE2 TRP D 159    10318  11461  11875  -1332    -62  -3599       C
ATOM   2214  CE3 TRP D 159     -11.438-104.739 -20.665  1.00109.91           C
ANISOU 2214  CE3 TRP D 159    12833  14179  14747  -1283   -115  -3524       C
ATOM   2215  CZ2 TRP D 159     -10.087-104.139 -23.075  1.00105.94           C
ANISOU 2215  CZ2 TRP D 159    12566  13682  14006  -1339    -42  -3552       C
ATOM   2216  CZ3 TRP D 159     -10.831-103.517 -20.863  1.00106.80           C
ANISOU 2216  CZ3 TRP D 159    12494  13802  14285  -1291    -96  -3482       C
ATOM   2217  CH2 TRP D 159     -10.165-103.226 -22.055  1.00104.17           C
ANISOU 2217  CH2 TRP D 159    12273  13470  13835  -1320    -62  -3494       C
ATOM   2218  N   ASN D 160     -13.036-108.586 -17.597  1.00122.09           N
ANISOU 2218  N   ASN D 160    13966  15707  16718  -1212   -141  -3579       N
ATOM   2219  CA  ASN D 160     -13.535-108.186 -16.280  1.00141.11           C
ANISOU 2219  CA  ASN D 160    16253  18139  19224  -1173   -176  -3527       C
ATOM   2220  C   ASN D 160     -12.395-107.983 -15.291  1.00138.02           C
ANISOU 2220  C   ASN D 160    15786  17767  18888  -1163    -65  -3501       C
ATOM   2221  O   ASN D 160     -12.481-107.165 -14.374  1.00155.41           O
ANISOU 2221  O   ASN D 160    17930  19990  21129  -1136    -78  -3450       O
ATOM   2222  CB  ASN D 160     -14.541-109.212 -15.738  1.00147.44           C
ANISOU 2222  CB  ASN D 160    16953  18939  20129  -1153   -244  -3535       C
ATOM   2223  CG  ASN D 160     -13.888-110.534 -15.340  1.00146.66           C
ANISOU 2223  CG  ASN D 160    16775  18835  20115  -1159   -161  -3573       C
ATOM   2224  OD1 ASN D 160     -13.614-111.394 -16.185  1.00140.37           O
ANISOU 2224  OD1 ASN D 160    16039  18012  19283  -1186   -136  -3627       O
ATOM   2225  ND2 ASN D 160     -13.661-110.707 -14.044  1.00133.96           N
ANISOU 2225  ND2 ASN D 160    15030  17251  18619  -1132   -120  -3544       N
ATOM   2226  N   VAL D 161     -11.329-108.746 -15.500  1.00112.89           N
ANISOU 2226  N   VAL D 161    12609  14577  15709  -1186     42  -3535       N
ATOM   2227  CA  VAL D 161     -10.109-108.653 -14.715  1.00115.16           C
ANISOU 2227  CA  VAL D 161    12837  14879  16040  -1187    160  -3511       C
ATOM   2228  C   VAL D 161      -9.259-107.460 -15.137  1.00112.24           C
ANISOU 2228  C   VAL D 161    12560  14515  15572  -1202    203  -3478       C
ATOM   2229  O   VAL D 161      -8.604-106.825 -14.316  1.00 98.55           O
ANISOU 2229  O   VAL D 161    10780  12797  13869  -1194    254  -3431       O
ATOM   2230  CB  VAL D 161      -9.277-109.922 -14.907  1.00125.33           C
ANISOU 2230  CB  VAL D 161    14107  16156  17358  -1207    260  -3557       C
ATOM   2231  CG1 VAL D 161      -7.833-109.726 -14.404  1.00 74.34           C
ANISOU 2231  CG1 VAL D 161     7621   9712  10913  -1218    394  -3528       C
ATOM   2232  CG2 VAL D 161      -9.987-111.105 -14.256  1.00 58.88           C
ANISOU 2232  CG2 VAL D 161     5573   7737   9060  -1191    226  -3581       C
ATOM   2233  N   VAL D 162      -9.273-107.175 -16.433  1.00121.51           N
ANISOU 2233  N   VAL D 162    13866  15676  16628  -1225    179  -3500       N
ATOM   2234  CA  VAL D 162      -8.515-106.074 -16.998  1.00111.92           C
ANISOU 2234  CA  VAL D 162    12747  14468  15312  -1242    211  -3469       C
ATOM   2235  C   VAL D 162      -9.144-104.774 -16.550  1.00106.69           C
ANISOU 2235  C   VAL D 162    12082  13816  14641  -1223    126  -3417       C
ATOM   2236  O   VAL D 162      -8.464-103.761 -16.434  1.00 97.84           O
ANISOU 2236  O   VAL D 162    10991  12704  13480  -1227    155  -3371       O
ATOM   2237  CB  VAL D 162      -8.517-106.122 -18.536  1.00108.83           C
ANISOU 2237  CB  VAL D 162    12492  14062  14794  -1269    194  -3508       C
ATOM   2238  CG1 VAL D 162      -7.563-105.075 -19.100  1.00102.13           C
ANISOU 2238  CG1 VAL D 162    11732  13226  13846  -1287    241  -3471       C
ATOM   2239  CG2 VAL D 162      -8.144-107.510 -19.020  1.00 98.54           C
ANISOU 2239  CG2 VAL D 162    11197  12744  13500  -1282    257  -3569       C
ATOM   2240  N   ARG D 163     -10.452-104.804 -16.315  1.00105.63           N
ANISOU 2240  N   ARG D 163    11912  13679  14543  -1200     20  -3420       N
ATOM   2241  CA  ARG D 163     -11.156-103.628 -15.824  1.00108.36           C
ANISOU 2241  CA  ARG D 163    12250  14035  14888  -1174    -64  -3371       C
ATOM   2242  C   ARG D 163     -10.645-103.249 -14.452  1.00115.83           C
ANISOU 2242  C   ARG D 163    13095  14996  15918  -1147    -18  -3325       C
ATOM   2243  O   ARG D 163     -10.170-102.138 -14.231  1.00106.11           O
ANISOU 2243  O   ARG D 163    11893  13771  14652  -1145    -10  -3280       O
ATOM   2244  CB  ARG D 163     -12.650-103.901 -15.726  1.00 80.09           C
ANISOU 2244  CB  ARG D 163     8635  10453  11345  -1149   -180  -3377       C
ATOM   2245  CG  ARG D 163     -13.409-103.653 -16.974  1.00 92.25           C
ANISOU 2245  CG  ARG D 163    10285  11979  12787  -1171   -263  -3396       C
ATOM   2246  CD  ARG D 163     -14.861-104.029 -16.784  1.00 84.43           C
ANISOU 2246  CD  ARG D 163     9249  10986  11843  -1147   -373  -3394       C
ATOM   2247  NE  ARG D 163     -15.485-104.244 -18.082  1.00105.54           N
ANISOU 2247  NE  ARG D 163    12025  13642  14434  -1178   -436  -3427       N
ATOM   2248  CZ  ARG D 163     -15.859-105.431 -18.536  1.00111.47           C
ANISOU 2248  CZ  ARG D 163    12776  14374  15203  -1193   -452  -3473       C
ATOM   2249  NH1 ARG D 163     -15.702-106.508 -17.781  1.00151.17           N
ANISOU 2249  NH1 ARG D 163    17702  19403  20333  -1179   -413  -3490       N
ATOM   2250  NH2 ARG D 163     -16.405-105.534 -19.729  1.00 92.33           N
ANISOU 2250  NH2 ARG D 163    10453  11932  12696  -1223   -512  -3499       N
ATOM   2251  N   ILE D 164     -10.755-104.192 -13.529  1.00121.20           N
ANISOU 2251  N   ILE D 164    13656  15684  16711  -1128      9  -3335       N
ATOM   2252  CA  ILE D 164     -10.424-103.937 -12.143  1.00117.87           C
ANISOU 2252  CA  ILE D 164    13125  15279  16380  -1099     45  -3293       C
ATOM   2253  C   ILE D 164      -9.044-103.304 -12.055  1.00109.97           C
ANISOU 2253  C   ILE D 164    12160  14279  15343  -1122    140  -3263       C
ATOM   2254  O   ILE D 164      -8.866-102.278 -11.388  1.00102.25           O
ANISOU 2254  O   ILE D 164    11172  13308  14369  -1104    129  -3213       O
ATOM   2255  CB  ILE D 164     -10.543-105.223 -11.308  1.00110.37           C
ANISOU 2255  CB  ILE D 164    12043  14339  15554  -1084     80  -3314       C
ATOM   2256  CG1 ILE D 164     -11.993-105.730 -11.367  1.00106.96           C
ANISOU 2256  CG1 ILE D 164    11575  13907  15156  -1058    -31  -3331       C
ATOM   2257  CG2 ILE D 164     -10.145-104.954  -9.874  1.00129.51           C
ANISOU 2257  CG2 ILE D 164    14353  16783  18071  -1056    122  -3271       C
ATOM   2258  CD1 ILE D 164     -12.203-107.104 -10.781  1.00114.75           C
ANISOU 2258  CD1 ILE D 164    12442  14902  16257  -1050    -11  -3357       C
ATOM   2259  N   LYS D 165      -8.088-103.897 -12.766  1.00 92.47           N
ANISOU 2259  N   LYS D 165     9990  12055  13088  -1160    230  -3290       N
ATOM   2260  CA  LYS D 165      -6.727-103.371 -12.844  1.00101.58           C
ANISOU 2260  CA  LYS D 165    11186  13210  14198  -1186    323  -3255       C
ATOM   2261  C   LYS D 165      -6.695-101.911 -13.306  1.00 87.39           C
ANISOU 2261  C   LYS D 165     9488  11411  12304  -1190    269  -3214       C
ATOM   2262  O   LYS D 165      -6.095-101.067 -12.652  1.00 94.42           O
ANISOU 2262  O   LYS D 165    10366  12306  13203  -1187    291  -3160       O
ATOM   2263  CB  LYS D 165      -5.859-104.251 -13.752  1.00123.62           C
ANISOU 2263  CB  LYS D 165    14029  15995  16945  -1222    415  -3292       C
ATOM   2264  CG  LYS D 165      -6.037-105.757 -13.515  1.00117.03           C
ANISOU 2264  CG  LYS D 165    13113  15157  16195  -1220    453  -3344       C
ATOM   2265  CD  LYS D 165      -4.809-106.410 -12.875  1.00107.70           C
ANISOU 2265  CD  LYS D 165    11859  13983  15079  -1234    586  -3331       C
ATOM   2266  CE  LYS D 165      -5.081-107.896 -12.594  1.00110.36           C
ANISOU 2266  CE  LYS D 165    12107  14316  15507  -1230    613  -3383       C
ATOM   2267  NZ  LYS D 165      -3.951-108.586 -11.892  1.00125.96           N
ANISOU 2267  NZ  LYS D 165    14000  16301  17559  -1245    743  -3369       N
ATOM   2268  N   ILE D 166      -7.340-101.609 -14.424  1.00 98.45           N
ANISOU 2268  N   ILE D 166    10987  12805  13614  -1199    196  -3236       N
ATOM   2269  CA  ILE D 166      -7.434-100.227 -14.896  1.00119.99           C
ANISOU 2269  CA  ILE D 166    13805  15532  16253  -1203    134  -3198       C
ATOM   2270  C   ILE D 166      -8.068 -99.270 -13.873  1.00115.30           C
ANISOU 2270  C   ILE D 166    13163  14941  15705  -1165     59  -3154       C
ATOM   2271  O   ILE D 166      -7.690 -98.090 -13.794  1.00 85.40           O
ANISOU 2271  O   ILE D 166     9421  11154  11873  -1166     43  -3106       O
ATOM   2272  CB  ILE D 166      -8.233-100.154 -16.205  1.00119.71           C
ANISOU 2272  CB  ILE D 166    13869  15491  16126  -1217     57  -3234       C
ATOM   2273  CG1 ILE D 166      -7.673-101.154 -17.207  1.00105.60           C
ANISOU 2273  CG1 ILE D 166    12132  13700  14293  -1249    126  -3282       C
ATOM   2274  CG2 ILE D 166      -8.234 -98.740 -16.769  1.00132.30           C
ANISOU 2274  CG2 ILE D 166    15556  17086  17625  -1226     -1  -3193       C
ATOM   2275  CD1 ILE D 166      -8.622-101.440 -18.330  1.00138.20           C
ANISOU 2275  CD1 ILE D 166    16335  17819  18357  -1259     49  -3329       C
ATOM   2276  N   VAL D 167      -9.054 -99.763 -13.120  1.00 99.76           N
ANISOU 2276  N   VAL D 167    11106  12977  13821  -1128     10  -3168       N
ATOM   2277  CA  VAL D 167      -9.648 -98.963 -12.051  1.00 99.50           C
ANISOU 2277  CA  VAL D 167    11017  12950  13837  -1082    -53  -3127       C
ATOM   2278  C   VAL D 167      -8.660 -98.840 -10.913  1.00 94.40           C
ANISOU 2278  C   VAL D 167    10299  12309  13259  -1076     27  -3090       C
ATOM   2279  O   VAL D 167      -8.296 -97.733 -10.526  1.00 97.53           O
ANISOU 2279  O   VAL D 167    10722  12703  13633  -1068     14  -3042       O
ATOM   2280  CB  VAL D 167     -10.986 -99.542 -11.534  1.00 91.24           C
ANISOU 2280  CB  VAL D 167     9890  11912  12865  -1040   -128  -3144       C
ATOM   2281  CG1 VAL D 167     -11.433 -98.811 -10.297  1.00 89.86           C
ANISOU 2281  CG1 VAL D 167     9645  11748  12748   -986   -174  -3099       C
ATOM   2282  CG2 VAL D 167     -12.066 -99.430 -12.611  1.00 76.91           C
ANISOU 2282  CG2 VAL D 167     8154  10091  10978  -1046   -225  -3166       C
ATOM   2283  N   GLN D 168      -8.197 -99.982 -10.413  1.00 88.76           N
ANISOU 2283  N   GLN D 168     9496  11602  12625  -1082    110  -3111       N
ATOM   2284  CA  GLN D 168      -7.229-100.000  -9.315  1.00124.92           C
ANISOU 2284  CA  GLN D 168    13998  16188  17277  -1080    195  -3077       C
ATOM   2285  C   GLN D 168      -5.994 -99.142  -9.609  1.00 93.63           C
ANISOU 2285  C   GLN D 168    10113  12217  13246  -1115    250  -3033       C
ATOM   2286  O   GLN D 168      -5.667 -98.221  -8.871  1.00 90.94           O
ANISOU 2286  O   GLN D 168     9765  11873  12915  -1102    241  -2982       O
ATOM   2287  CB  GLN D 168      -6.801-101.434  -9.000  1.00131.39           C
ANISOU 2287  CB  GLN D 168    14726  17016  18180  -1094    286  -3110       C
ATOM   2288  CG  GLN D 168      -5.764-101.559  -7.894  1.00 97.34           C
ANISOU 2288  CG  GLN D 168    10327  12711  13945  -1100    383  -3074       C
ATOM   2289  CD  GLN D 168      -5.556-102.999  -7.463  1.00165.66           C
ANISOU 2289  CD  GLN D 168    18872  21376  22696  -1107    459  -3108       C
ATOM   2290  OE1 GLN D 168      -5.272-103.874  -8.292  1.00185.41           O
ANISOU 2290  OE1 GLN D 168    21403  23871  25174  -1137    507  -3149       O
ATOM   2291  NE2 GLN D 168      -5.703-103.257  -6.160  1.00167.58           N
ANISOU 2291  NE2 GLN D 168    18987  21635  23050  -1077    471  -3090       N
ATOM   2292  N   MET D 169      -5.316 -99.434 -10.704  1.00 90.12           N
ANISOU 2292  N   MET D 169     9746  11767  12728  -1158    303  -3049       N
ATOM   2293  CA  MET D 169      -4.167 -98.634 -11.074  1.00110.54           C
ANISOU 2293  CA  MET D 169    12408  14349  15244  -1191    350  -3001       C
ATOM   2294  C   MET D 169      -4.535 -97.155 -11.046  1.00103.58           C
ANISOU 2294  C   MET D 169    11589  13460  14308  -1175    256  -2958       C
ATOM   2295  O   MET D 169      -3.825 -96.331 -10.469  1.00 99.86           O
ANISOU 2295  O   MET D 169    11121  12984  13839  -1179    272  -2900       O
ATOM   2296  CB  MET D 169      -3.649 -99.016 -12.463  1.00 74.75           C
ANISOU 2296  CB  MET D 169     7966   9815  10618  -1230    394  -3026       C
ATOM   2297  CG  MET D 169      -2.790 -97.918 -13.086  1.00 77.66           C
ANISOU 2297  CG  MET D 169     8434  10183  10890  -1258    401  -2971       C
ATOM   2298  SD  MET D 169      -3.273 -97.546 -14.780  1.00139.98           S
ANISOU 2298  SD  MET D 169    16461  18077  18649  -1276    334  -3000       S
ATOM   2299  CE  MET D 169      -2.526 -95.957 -15.058  1.00133.89           C
ANISOU 2299  CE  MET D 169    15772  17306  17792  -1294    308  -2919       C
ATOM   2300  N   LEU D 170      -5.658 -96.827 -11.666  1.00 79.19           N
ANISOU 2300  N   LEU D 170     8550  10368  11171  -1159    155  -2984       N
ATOM   2301  CA  LEU D 170      -6.006 -95.442 -11.909  1.00115.19           C
ANISOU 2301  CA  LEU D 170    13185  14919  15662  -1150     65  -2948       C
ATOM   2302  C   LEU D 170      -6.250 -94.723 -10.585  1.00118.27           C
ANISOU 2302  C   LEU D 170    13516  15305  16117  -1107     25  -2908       C
ATOM   2303  O   LEU D 170      -5.840 -93.564 -10.400  1.00 90.96           O
ANISOU 2303  O   LEU D 170    10103  11835  12622  -1108     -2  -2856       O
ATOM   2304  CB  LEU D 170      -7.232 -95.385 -12.828  1.00107.42           C
ANISOU 2304  CB  LEU D 170    12257  13935  14622  -1142    -31  -2987       C
ATOM   2305  CG  LEU D 170      -7.170 -94.382 -13.978  1.00 99.96           C
ANISOU 2305  CG  LEU D 170    11434  12986  13560  -1168    -81  -2969       C
ATOM   2306  CD1 LEU D 170      -5.778 -94.327 -14.570  1.00 80.48           C
ANISOU 2306  CD1 LEU D 170     9018  10522  11037  -1214      6  -2945       C
ATOM   2307  CD2 LEU D 170      -8.192 -94.755 -15.029  1.00101.12           C
ANISOU 2307  CD2 LEU D 170    11629  13135  13657  -1174   -143  -3019       C
ATOM   2308  N   SER D 171      -6.919 -95.429  -9.675  1.00106.72           N
ANISOU 2308  N   SER D 171    11949  13851  14750  -1069     20  -2930       N
ATOM   2309  CA  SER D 171      -7.245 -94.909  -8.349  1.00102.17           C
ANISOU 2309  CA  SER D 171    11304  13275  14243  -1019    -16  -2898       C
ATOM   2310  C   SER D 171      -5.987 -94.588  -7.564  1.00 99.98           C
ANISOU 2310  C   SER D 171    11002  12991  13996  -1035     61  -2850       C
ATOM   2311  O   SER D 171      -5.801 -93.455  -7.119  1.00 83.39           O
ANISOU 2311  O   SER D 171     8934  10877  11875  -1021     20  -2803       O
ATOM   2312  CB  SER D 171      -8.094 -95.918  -7.563  1.00 96.03           C
ANISOU 2312  CB  SER D 171    10406  12514  13565   -978    -22  -2930       C
ATOM   2313  OG  SER D 171      -9.209 -96.355  -8.314  1.00 96.31           O
ANISOU 2313  OG  SER D 171    10461  12556  13577   -969    -88  -2971       O
ATOM   2314  N   ASP D 172      -5.132 -95.594  -7.401  1.00102.55           N
ANISOU 2314  N   ASP D 172    11271  13325  14371  -1066    170  -2859       N
ATOM   2315  CA  ASP D 172      -3.873 -95.429  -6.701  1.00 97.03           C
ANISOU 2315  CA  ASP D 172    10543  12620  13703  -1089    254  -2810       C
ATOM   2316  C   ASP D 172      -3.166 -94.186  -7.205  1.00 87.95           C
ANISOU 2316  C   ASP D 172     9502  11452  12462  -1117    232  -2756       C
ATOM   2317  O   ASP D 172      -2.784 -93.311  -6.421  1.00103.70           O
ANISOU 2317  O   ASP D 172    11497  13434  14470  -1106    215  -2703       O
ATOM   2318  CB  ASP D 172      -2.977 -96.659  -6.905  1.00 97.35           C
ANISOU 2318  CB  ASP D 172    10539  12671  13777  -1131    377  -2828       C
ATOM   2319  CG  ASP D 172      -3.566 -97.917  -6.286  1.00135.01           C
ANISOU 2319  CG  ASP D 172    15189  17458  18649  -1107    403  -2876       C
ATOM   2320  OD1 ASP D 172      -4.629 -97.815  -5.615  1.00105.97           O
ANISOU 2320  OD1 ASP D 172    11456  13787  15020  -1056    327  -2888       O
ATOM   2321  OD2 ASP D 172      -2.953 -98.999  -6.461  1.00128.33           O
ANISOU 2321  OD2 ASP D 172    14303  16620  17835  -1138    498  -2898       O
ATOM   2322  N   THR D 173      -3.023 -94.100  -8.519  1.00 85.53           N
ANISOU 2322  N   THR D 173     9288  11145  12062  -1150    227  -2768       N
ATOM   2323  CA  THR D 173      -2.348 -92.973  -9.141  1.00 97.28           C
ANISOU 2323  CA  THR D 173    10880  12622  13460  -1179    205  -2715       C
ATOM   2324  C   THR D 173      -2.981 -91.614  -8.832  1.00108.83           C
ANISOU 2324  C   THR D 173    12388  14067  14894  -1146     90  -2685       C
ATOM   2325  O   THR D 173      -2.280 -90.646  -8.532  1.00 97.14           O
ANISOU 2325  O   THR D 173    10945  12572  13393  -1157     79  -2623       O
ATOM   2326  CB  THR D 173      -2.323 -93.140 -10.657  1.00 98.54           C
ANISOU 2326  CB  THR D 173    11128  12789  13523  -1212    205  -2741       C
ATOM   2327  OG1 THR D 173      -1.330 -94.112 -11.022  1.00127.11           O
ANISOU 2327  OG1 THR D 173    14732  16420  17146  -1250    323  -2745       O
ATOM   2328  CG2 THR D 173      -2.031 -91.801 -11.337  1.00 77.10           C
ANISOU 2328  CG2 THR D 173     8519  10065  10711  -1231    144  -2690       C
ATOM   2329  N   LEU D 174      -4.301 -91.532  -8.947  1.00 92.92           N
ANISOU 2329  N   LEU D 174    10373  12055  12877  -1106      1  -2725       N
ATOM   2330  CA  LEU D 174      -4.985 -90.250  -8.869  1.00 84.37           C
ANISOU 2330  CA  LEU D 174     9346  10957  11752  -1075   -112  -2701       C
ATOM   2331  C   LEU D 174      -5.577 -89.827  -7.515  1.00122.35           C
ANISOU 2331  C   LEU D 174    14094  15760  16634  -1014   -163  -2687       C
ATOM   2332  O   LEU D 174      -5.955 -88.653  -7.330  1.00 83.62           O
ANISOU 2332  O   LEU D 174     9239  10838  11695   -986   -250  -2657       O
ATOM   2333  CB  LEU D 174      -6.095 -90.266  -9.905  1.00 99.05           C
ANISOU 2333  CB  LEU D 174    11256  12824  13553  -1069   -186  -2745       C
ATOM   2334  CG  LEU D 174      -5.822 -89.510 -11.184  1.00 86.89           C
ANISOU 2334  CG  LEU D 174     9830  11280  11903  -1109   -220  -2728       C
ATOM   2335  CD1 LEU D 174      -4.344 -89.255 -11.281  1.00 91.68           C
ANISOU 2335  CD1 LEU D 174    10466  11883  12487  -1154   -146  -2677       C
ATOM   2336  CD2 LEU D 174      -6.347 -90.342 -12.332  1.00 80.59           C
ANISOU 2336  CD2 LEU D 174     9057  10498  11065  -1130   -214  -2785       C
ATOM   2337  N   LYS D 175      -5.658 -90.765  -6.573  1.00137.67           N
ANISOU 2337  N   LYS D 175    15925  17713  18670   -990   -109  -2707       N
ATOM   2338  CA  LYS D 175      -6.412 -90.510  -5.348  1.00107.35           C
ANISOU 2338  CA  LYS D 175    12017  13873  14897   -923   -160  -2701       C
ATOM   2339  C   LYS D 175      -5.866 -89.280  -4.648  1.00 94.93           C
ANISOU 2339  C   LYS D 175    10481  12275  13312   -911   -191  -2642       C
ATOM   2340  O   LYS D 175      -6.627 -88.452  -4.159  1.00132.22           O
ANISOU 2340  O   LYS D 175    15219  16988  18030   -857   -280  -2631       O
ATOM   2341  CB  LYS D 175      -6.466 -91.741  -4.426  1.00 72.59           C
ANISOU 2341  CB  LYS D 175     7482   9494  10605   -904    -91  -2727       C
ATOM   2342  CG  LYS D 175      -5.157 -92.142  -3.786  1.00 93.26           C
ANISOU 2342  CG  LYS D 175    10049  12109  13275   -940     18  -2699       C
ATOM   2343  CD  LYS D 175      -5.093 -93.647  -3.512  1.00102.68           C
ANISOU 2343  CD  LYS D 175    11132  13329  14555   -949    104  -2738       C
ATOM   2344  CE  LYS D 175      -6.325 -94.149  -2.779  1.00117.44           C
ANISOU 2344  CE  LYS D 175    12905  15220  16498   -884     55  -2769       C
ATOM   2345  NZ  LYS D 175      -6.217 -95.608  -2.479  1.00120.51           N
ANISOU 2345  NZ  LYS D 175    13180  15632  16975   -895    136  -2803       N
ATOM   2346  N   GLY D 176      -4.545 -89.145  -4.640  1.00109.24           N
ANISOU 2346  N   GLY D 176    12315  14075  15115   -962   -122  -2602       N
ATOM   2347  CA  GLY D 176      -3.904 -87.982  -4.055  1.00110.19           C
ANISOU 2347  CA  GLY D 176    12481  14167  15221   -961   -151  -2540       C
ATOM   2348  C   GLY D 176      -4.077 -86.704  -4.855  1.00106.87           C
ANISOU 2348  C   GLY D 176    12180  13725  14702   -967   -246  -2514       C
ATOM   2349  O   GLY D 176      -4.299 -85.641  -4.301  1.00138.93           O
ANISOU 2349  O   GLY D 176    16274  17761  18751   -932   -323  -2483       O
ATOM   2350  N   LEU D 177      -3.945 -86.805  -6.166  1.00120.66           N
ANISOU 2350  N   LEU D 177    13989  15479  16375  -1012   -240  -2526       N
ATOM   2351  CA  LEU D 177      -3.822 -85.630  -7.012  1.00105.97           C
ANISOU 2351  CA  LEU D 177    12241  13602  14421  -1034   -313  -2491       C
ATOM   2352  C   LEU D 177      -5.134 -84.965  -7.440  1.00110.59           C
ANISOU 2352  C   LEU D 177    12873  14184  14960   -993   -427  -2517       C
ATOM   2353  O   LEU D 177      -5.228 -83.729  -7.455  1.00 86.77           O
ANISOU 2353  O   LEU D 177     9926  11144  11897   -982   -512  -2480       O
ATOM   2354  CB  LEU D 177      -2.990 -85.977  -8.252  1.00112.99           C
ANISOU 2354  CB  LEU D 177    13179  14505  15247  -1102   -252  -2484       C
ATOM   2355  CG  LEU D 177      -1.580 -86.543  -8.117  1.00116.45           C
ANISOU 2355  CG  LEU D 177    13589  14947  15708  -1152   -137  -2447       C
ATOM   2356  CD1 LEU D 177      -1.489 -87.655  -7.082  1.00119.46           C
ANISOU 2356  CD1 LEU D 177    13858  15339  16193  -1135    -53  -2472       C
ATOM   2357  CD2 LEU D 177      -1.123 -87.037  -9.486  1.00159.95           C
ANISOU 2357  CD2 LEU D 177    19145  20479  21150  -1203    -86  -2458       C
ATOM   2358  N   SER D 178      -6.130 -85.772  -7.820  1.00104.75           N
ANISOU 2358  N   SER D 178    12101  13469  14232   -974   -433  -2576       N
ATOM   2359  CA  SER D 178      -7.350 -85.210  -8.427  1.00110.86           C
ANISOU 2359  CA  SER D 178    12925  14243  14954   -947   -535  -2596       C
ATOM   2360  C   SER D 178      -8.645 -85.969  -8.171  1.00114.28           C
ANISOU 2360  C   SER D 178    13292  14697  15434   -897   -559  -2646       C
ATOM   2361  O   SER D 178      -8.627 -87.118  -7.699  1.00113.19           O
ANISOU 2361  O   SER D 178    13065  14576  15367   -890   -491  -2675       O
ATOM   2362  CB  SER D 178      -7.188 -84.964  -9.934  1.00 91.00           C
ANISOU 2362  CB  SER D 178    10498  11734  12343  -1002   -550  -2599       C
ATOM   2363  OG  SER D 178      -8.219 -84.103 -10.409  1.00 88.28           O
ANISOU 2363  OG  SER D 178    10212  11384  11945   -979   -658  -2600       O
ATOM   2364  N   ASP D 179      -9.759 -85.291  -8.462  1.00111.95           N
ANISOU 2364  N   ASP D 179    13038  14399  15099   -862   -659  -2649       N
ATOM   2365  CA  ASP D 179     -11.090 -85.882  -8.377  1.00151.02           C
ANISOU 2365  CA  ASP D 179    17935  19366  20078   -817   -698  -2686       C
ATOM   2366  C   ASP D 179     -11.578 -86.378  -9.746  1.00143.74           C
ANISOU 2366  C   ASP D 179    17055  18459  19100   -859   -708  -2722       C
ATOM   2367  O   ASP D 179     -12.705 -86.857  -9.874  1.00138.49           O
ANISOU 2367  O   ASP D 179    16360  17809  18449   -831   -748  -2748       O
ATOM   2368  CB  ASP D 179     -12.083 -84.871  -7.819  1.00154.81           C
ANISOU 2368  CB  ASP D 179    18432  19837  20552   -748   -801  -2663       C
ATOM   2369  CG  ASP D 179     -12.202 -83.650  -8.700  1.00181.25           C
ANISOU 2369  CG  ASP D 179    21892  23168  23807   -769   -878  -2639       C
ATOM   2370  OD1 ASP D 179     -11.156 -83.230  -9.255  1.00163.43           O
ANISOU 2370  OD1 ASP D 179    19695  20898  21503   -826   -852  -2618       O
ATOM   2371  OD2 ASP D 179     -13.331 -83.125  -8.850  1.00191.79           O
ANISOU 2371  OD2 ASP D 179    23250  24504  25116   -730   -964  -2636       O
ATOM   2372  N   ARG D 180     -10.741 -86.255 -10.771  1.00111.72           N
ANISOU 2372  N   ARG D 180    13069  14400  14979   -925   -675  -2719       N
ATOM   2373  CA  ARG D 180     -11.110 -86.751 -12.091  1.00116.34           C
ANISOU 2373  CA  ARG D 180    13698  15000  15507   -967   -679  -2755       C
ATOM   2374  C   ARG D 180      -9.920 -87.266 -12.906  1.00115.45           C
ANISOU 2374  C   ARG D 180    13615  14892  15358  -1034   -591  -2763       C
ATOM   2375  O   ARG D 180      -8.775 -86.974 -12.598  1.00121.92           O
ANISOU 2375  O   ARG D 180    14441  15703  16181  -1054   -539  -2729       O
ATOM   2376  CB  ARG D 180     -11.848 -85.671 -12.872  1.00134.47           C
ANISOU 2376  CB  ARG D 180    16078  17290  17724   -968   -780  -2739       C
ATOM   2377  CG  ARG D 180     -10.962 -84.559 -13.370  1.00133.31           C
ANISOU 2377  CG  ARG D 180    16015  17129  17507  -1006   -794  -2697       C
ATOM   2378  CD  ARG D 180     -11.791 -83.519 -14.088  1.00128.02           C
ANISOU 2378  CD  ARG D 180    15419  16456  16767  -1004   -897  -2683       C
ATOM   2379  NE  ARG D 180     -12.777 -82.928 -13.192  1.00138.38           N
ANISOU 2379  NE  ARG D 180    16708  17758  18114   -935   -973  -2667       N
ATOM   2380  CZ  ARG D 180     -13.655 -82.004 -13.561  1.00165.19           C
ANISOU 2380  CZ  ARG D 180    20155  21147  21462   -919  -1068  -2651       C
ATOM   2381  NH1 ARG D 180     -13.662 -81.567 -14.819  1.00145.24           N
ANISOU 2381  NH1 ARG D 180    17703  18626  18854   -971  -1099  -2649       N
ATOM   2382  NH2 ARG D 180     -14.523 -81.521 -12.676  1.00181.33           N
ANISOU 2382  NH2 ARG D 180    22174  23183  23539   -849  -1130  -2635       N
ATOM   2383  N   VAL D 181     -10.201 -88.067 -13.929  1.00126.55           N
ANISOU 2383  N   VAL D 181    15040  16312  16731  -1066   -574  -2806       N
ATOM   2384  CA  VAL D 181      -9.169 -88.483 -14.865  1.00102.07           C
ANISOU 2384  CA  VAL D 181    11981  13219  13580  -1125   -499  -2815       C
ATOM   2385  C   VAL D 181      -9.343 -87.670 -16.114  1.00118.30           C
ANISOU 2385  C   VAL D 181    14138  15279  15534  -1158   -559  -2805       C
ATOM   2386  O   VAL D 181     -10.461 -87.423 -16.548  1.00118.64           O
ANISOU 2386  O   VAL D 181    14205  15323  15549  -1146   -639  -2821       O
ATOM   2387  CB  VAL D 181      -9.324 -89.940 -15.315  1.00106.72           C
ANISOU 2387  CB  VAL D 181    12537  13822  14191  -1141   -439  -2874       C
ATOM   2388  CG1 VAL D 181      -7.953 -90.558 -15.590  1.00 87.33           C
ANISOU 2388  CG1 VAL D 181    10083  11372  11726  -1182   -326  -2873       C
ATOM   2389  CG2 VAL D 181     -10.094 -90.744 -14.295  1.00136.14           C
ANISOU 2389  CG2 VAL D 181    16163  17549  18014  -1094   -442  -2899       C
ATOM   2390  N   VAL D 182      -8.237 -87.232 -16.690  1.00132.50           N
ANISOU 2390  N   VAL D 182    15989  17080  17274  -1200   -521  -2773       N
ATOM   2391  CA  VAL D 182      -8.286 -86.706 -18.037  1.00119.88           C
ANISOU 2391  CA  VAL D 182    14480  15493  15577  -1239   -561  -2769       C
ATOM   2392  C   VAL D 182      -7.352 -87.533 -18.896  1.00134.25           C
ANISOU 2392  C   VAL D 182    16320  17331  17358  -1282   -468  -2787       C
ATOM   2393  O   VAL D 182      -6.135 -87.567 -18.701  1.00119.69           O
ANISOU 2393  O   VAL D 182    14470  15490  15517  -1300   -394  -2753       O
ATOM   2394  CB  VAL D 182      -7.952 -85.214 -18.103  1.00117.38           C
ANISOU 2394  CB  VAL D 182    14220  15168  15212  -1246   -624  -2706       C
ATOM   2395  CG1 VAL D 182      -7.969 -84.737 -19.536  1.00128.45           C
ANISOU 2395  CG1 VAL D 182    15705  16587  16513  -1289   -660  -2702       C
ATOM   2396  CG2 VAL D 182      -8.958 -84.426 -17.291  1.00124.72           C
ANISOU 2396  CG2 VAL D 182    15134  16079  16176  -1197   -718  -2693       C
ATOM   2397  N   PHE D 183      -7.956 -88.246 -19.830  1.00133.03           N
ANISOU 2397  N   PHE D 183    16189  17188  17167  -1298   -473  -2841       N
ATOM   2398  CA  PHE D 183      -7.196 -89.075 -20.722  1.00131.95           C
ANISOU 2398  CA  PHE D 183    16080  17068  16986  -1333   -390  -2865       C
ATOM   2399  C   PHE D 183      -6.632 -88.232 -21.853  1.00156.90           C
ANISOU 2399  C   PHE D 183    19325  20246  20043  -1371   -408  -2830       C
ATOM   2400  O   PHE D 183      -7.349 -87.454 -22.494  1.00149.53           O
ANISOU 2400  O   PHE D 183    18444  19317  19056  -1379   -495  -2825       O
ATOM   2401  CB  PHE D 183      -8.077 -90.186 -21.262  1.00134.64           C
ANISOU 2401  CB  PHE D 183    16416  17411  17329  -1333   -393  -2938       C
ATOM   2402  CG  PHE D 183      -8.229 -91.340 -20.324  1.00120.93           C
ANISOU 2402  CG  PHE D 183    14592  15665  15690  -1306   -341  -2973       C
ATOM   2403  CD1 PHE D 183      -7.139 -92.140 -20.005  1.00120.66           C
ANISOU 2403  CD1 PHE D 183    14521  15635  15690  -1313   -231  -2976       C
ATOM   2404  CD2 PHE D 183      -9.461 -91.645 -19.773  1.00110.08           C
ANISOU 2404  CD2 PHE D 183    13169  14281  14375  -1273   -403  -3000       C
ATOM   2405  CE1 PHE D 183      -7.278 -93.224 -19.142  1.00118.85           C
ANISOU 2405  CE1 PHE D 183    14204  15398  15555  -1291   -183  -3009       C
ATOM   2406  CE2 PHE D 183      -9.607 -92.731 -18.908  1.00 98.12           C
ANISOU 2406  CE2 PHE D 183    11566  12761  12955  -1247   -358  -3030       C
ATOM   2407  CZ  PHE D 183      -8.513 -93.519 -18.594  1.00 83.59           C
ANISOU 2407  CZ  PHE D 183     9687  10923  11149  -1258   -248  -3036       C
ATOM   2408  N   VAL D 184      -5.333 -88.374 -22.071  1.00150.51           N
ANISOU 2408  N   VAL D 184    18528  19451  19210  -1393   -324  -2799       N
ATOM   2409  CA  VAL D 184      -4.685 -87.751 -23.202  1.00150.99           C
ANISOU 2409  CA  VAL D 184    18662  19536  19172  -1429   -327  -2763       C
ATOM   2410  C   VAL D 184      -4.289 -88.856 -24.162  1.00153.52           C
ANISOU 2410  C   VAL D 184    19007  19877  19445  -1448   -247  -2808       C
ATOM   2411  O   VAL D 184      -3.633 -89.830 -23.758  1.00148.30           O
ANISOU 2411  O   VAL D 184    18305  19216  18827  -1442   -151  -2823       O
ATOM   2412  CB  VAL D 184      -3.450 -86.988 -22.763  1.00134.47           C
ANISOU 2412  CB  VAL D 184    16567  17445  17079  -1438   -296  -2680       C
ATOM   2413  CG1 VAL D 184      -3.864 -85.699 -22.082  1.00129.48           C
ANISOU 2413  CG1 VAL D 184    15935  16792  16468  -1423   -393  -2633       C
ATOM   2414  CG2 VAL D 184      -2.617 -87.851 -21.839  1.00106.22           C
ANISOU 2414  CG2 VAL D 184    12924  13860  13575  -1428   -190  -2675       C
ATOM   2415  N   LEU D 185      -4.703 -88.714 -25.420  1.00122.16           N
ANISOU 2415  N   LEU D 185    15104  15925  15388  -1469   -288  -2831       N
ATOM   2416  CA  LEU D 185      -4.452 -89.739 -26.424  1.00145.51           C
ANISOU 2416  CA  LEU D 185    18095  18901  18291  -1484   -224  -2880       C
ATOM   2417  C   LEU D 185      -4.124 -89.130 -27.788  1.00165.53           C
ANISOU 2417  C   LEU D 185    20712  21472  20712  -1514   -245  -2856       C
ATOM   2418  O   LEU D 185      -4.755 -88.141 -28.188  1.00155.08           O
ANISOU 2418  O   LEU D 185    19421  20151  19350  -1525   -340  -2837       O
ATOM   2419  CB  LEU D 185      -5.649 -90.695 -26.518  1.00149.07           C
ANISOU 2419  CB  LEU D 185    18536  19335  18771  -1473   -252  -2964       C
ATOM   2420  CG  LEU D 185      -7.085 -90.225 -26.201  1.00136.51           C
ANISOU 2420  CG  LEU D 185    16934  17724  17212  -1460   -364  -2980       C
ATOM   2421  CD1 LEU D 185      -7.585 -90.765 -24.857  1.00104.23           C
ANISOU 2421  CD1 LEU D 185    12759  13608  13237  -1424   -361  -2998       C
ATOM   2422  CD2 LEU D 185      -7.259 -88.709 -26.285  1.00124.16           C
ANISOU 2422  CD2 LEU D 185    15399  16165  15611  -1468   -450  -2920       C
ATOM   2423  N   TRP D 186      -3.125 -89.689 -28.484  1.00160.37           N
ANISOU 2423  N   TRP D 186    20086  20845  20004  -1524   -157  -2852       N
ATOM   2424  CA  TRP D 186      -2.802 -89.201 -29.826  1.00181.49           C
ANISOU 2424  CA  TRP D 186    22834  23558  22567  -1549   -172  -2831       C
ATOM   2425  C   TRP D 186      -3.776 -89.674 -30.890  1.00164.65           C
ANISOU 2425  C   TRP D 186    20754  21430  20376  -1559   -214  -2905       C
ATOM   2426  O   TRP D 186      -4.394 -88.861 -31.581  1.00161.02           O
ANISOU 2426  O   TRP D 186    20335  20982  19862  -1578   -301  -2897       O
ATOM   2427  CB  TRP D 186      -1.367 -89.540 -30.248  1.00219.49           C
ANISOU 2427  CB  TRP D 186    27661  28404  27331  -1552    -66  -2790       C
ATOM   2428  CG  TRP D 186      -0.973 -88.877 -31.558  1.00230.71           C
ANISOU 2428  CG  TRP D 186    29150  29872  28638  -1573    -87  -2752       C
ATOM   2429  CD1 TRP D 186      -0.482 -89.488 -32.677  1.00239.17           C
ANISOU 2429  CD1 TRP D 186    30272  30979  29624  -1576    -28  -2772       C
ATOM   2430  CD2 TRP D 186      -1.072 -87.479 -31.879  1.00220.17           C
ANISOU 2430  CD2 TRP D 186    27838  28554  27263  -1593   -178  -2688       C
ATOM   2431  NE1 TRP D 186      -0.257 -88.558 -33.664  1.00240.34           N
ANISOU 2431  NE1 TRP D 186    30468  31169  29682  -1596    -74  -2722       N
ATOM   2432  CE2 TRP D 186      -0.612 -87.324 -33.201  1.00228.81           C
ANISOU 2432  CE2 TRP D 186    28990  29698  28249  -1609   -167  -2670       C
ATOM   2433  CE3 TRP D 186      -1.501 -86.351 -31.175  1.00204.74           C
ANISOU 2433  CE3 TRP D 186    25860  26578  25352  -1598   -267  -2645       C
ATOM   2434  CZ2 TRP D 186      -0.570 -86.080 -33.826  1.00228.01           C
ANISOU 2434  CZ2 TRP D 186    28918  29627  28088  -1632   -244  -2608       C
ATOM   2435  CZ3 TRP D 186      -1.454 -85.121 -31.801  1.00180.77           C
ANISOU 2435  CZ3 TRP D 186    22859  23569  22256  -1620   -344  -2585       C
ATOM   2436  CH2 TRP D 186      -0.994 -84.996 -33.110  1.00204.25           C
ANISOU 2436  CH2 TRP D 186    25884  26594  25128  -1638   -332  -2566       C
ATOM   2437  N   ALA D 187      -3.962 -90.984 -30.999  1.00143.60           N
ANISOU 2437  N   ALA D 187    18085  18752  17725  -1548   -159  -2978       N
ATOM   2438  CA  ALA D 187      -4.912 -91.461 -31.988  1.00131.27           C
ANISOU 2438  CA  ALA D 187    16577  17190  16111  -1560   -205  -3048       C
ATOM   2439  C   ALA D 187      -6.189 -91.489 -31.211  1.00136.75           C
ANISOU 2439  C   ALA D 187    17229  17846  16885  -1550   -282  -3079       C
ATOM   2440  O   ALA D 187      -6.424 -92.395 -30.411  1.00182.76           O
ANISOU 2440  O   ALA D 187    23003  23644  22792  -1530   -250  -3118       O
ATOM   2441  CB  ALA D 187      -4.541 -92.865 -32.445  1.00119.83           C
ANISOU 2441  CB  ALA D 187    15147  15740  14642  -1550   -116  -3111       C
ATOM   2442  N   HIS D 188      -7.036 -90.506 -31.466  1.00 97.13           N
ANISOU 2442  N   HIS D 188    12232  12829  11844  -1565   -385  -3061       N
ATOM   2443  CA  HIS D 188      -8.164 -90.289 -30.565  1.00136.34           C
ANISOU 2443  CA  HIS D 188    17151  17763  16890  -1550   -461  -3068       C
ATOM   2444  C   HIS D 188      -9.121 -91.474 -30.604  1.00130.65           C
ANISOU 2444  C   HIS D 188    16422  17017  16201  -1543   -472  -3144       C
ATOM   2445  O   HIS D 188      -9.605 -91.940 -29.572  1.00107.12           O
ANISOU 2445  O   HIS D 188    13377  14010  13314  -1518   -476  -3159       O
ATOM   2446  CB  HIS D 188      -8.860 -88.950 -30.874  1.00126.21           C
ANISOU 2446  CB  HIS D 188    15895  16486  15571  -1567   -569  -3027       C
ATOM   2447  CG  HIS D 188     -10.372 -88.985 -30.804  1.00114.67           C
ANISOU 2447  CG  HIS D 188    14430  15003  14137  -1565   -661  -3060       C
ATOM   2448  ND1 HIS D 188     -11.041 -89.521 -29.713  1.00120.41           N
ANISOU 2448  ND1 HIS D 188    15091  15698  14959  -1534   -671  -3080       N
ATOM   2449  CD2 HIS D 188     -11.289 -88.542 -31.652  1.00148.08           C
ANISOU 2449  CD2 HIS D 188    18709  19242  18313  -1591   -743  -3067       C
ATOM   2450  CE1 HIS D 188     -12.336 -89.400 -29.937  1.00140.26           C
ANISOU 2450  CE1 HIS D 188    17618  18202  17474  -1539   -759  -3096       C
ATOM   2451  NE2 HIS D 188     -12.542 -88.819 -31.084  1.00142.74           N
ANISOU 2451  NE2 HIS D 188    17999  18536  17699  -1575   -804  -3090       N
ATOM   2452  N   GLY D 189      -9.342 -91.978 -31.809  1.00128.46           N
ANISOU 2452  N   GLY D 189    16212  16751  15847  -1566   -475  -3189       N
ATOM   2453  CA  GLY D 189     -10.424 -92.899 -32.054  1.00135.49           C
ANISOU 2453  CA  GLY D 189    17111  17616  16752  -1569   -513  -3254       C
ATOM   2454  C   GLY D 189     -10.378 -94.290 -31.461  1.00120.55           C
ANISOU 2454  C   GLY D 189    15175  15699  14931  -1546   -453  -3307       C
ATOM   2455  O   GLY D 189     -11.250 -94.625 -30.669  1.00 96.42           O
ANISOU 2455  O   GLY D 189    12063  12615  11956  -1529   -496  -3320       O
ATOM   2456  N   PHE D 190      -9.371 -95.095 -31.795  1.00126.91           N
ANISOU 2456  N   PHE D 190    15998  16512  15709  -1542   -355  -3332       N
ATOM   2457  CA  PHE D 190      -9.447 -96.511 -31.430  1.00142.46           C
ANISOU 2457  CA  PHE D 190    17936  18455  17738  -1525   -306  -3392       C
ATOM   2458  C   PHE D 190      -9.472 -96.694 -29.928  1.00142.72           C
ANISOU 2458  C   PHE D 190    17864  18468  17893  -1496   -288  -3374       C
ATOM   2459  O   PHE D 190     -10.035 -97.659 -29.418  1.00116.32           O
ANISOU 2459  O   PHE D 190    14475  15099  14621  -1482   -293  -3415       O
ATOM   2460  CB  PHE D 190      -8.314 -97.349 -32.027  1.00153.16           C
ANISOU 2460  CB  PHE D 190    19329  19823  19043  -1523   -198  -3421       C
ATOM   2461  CG  PHE D 190      -8.363 -98.798 -31.605  1.00142.86           C
ANISOU 2461  CG  PHE D 190    17988  18488  17803  -1505   -148  -3481       C
ATOM   2462  CD1 PHE D 190      -9.451 -99.588 -31.939  1.00126.39           C
ANISOU 2462  CD1 PHE D 190    15922  16373  15726  -1511   -211  -3542       C
ATOM   2463  CD2 PHE D 190      -7.336 -99.364 -30.862  1.00137.81           C
ANISOU 2463  CD2 PHE D 190    17293  17849  17219  -1484    -42  -3473       C
ATOM   2464  CE1 PHE D 190      -9.507-100.914 -31.550  1.00110.34           C
ANISOU 2464  CE1 PHE D 190    13855  14313  13757  -1496   -172  -3596       C
ATOM   2465  CE2 PHE D 190      -7.390-100.695 -30.473  1.00109.14           C
ANISOU 2465  CE2 PHE D 190    13626  14191  13652  -1468      2  -3529       C
ATOM   2466  CZ  PHE D 190      -8.474-101.467 -30.818  1.00102.69           C
ANISOU 2466  CZ  PHE D 190    12829  13345  12843  -1474    -65  -3591       C
ATOM   2467  N   GLU D 191      -8.847 -95.768 -29.217  1.00148.72           N
ANISOU 2467  N   GLU D 191    18586  19242  18679  -1487   -270  -3309       N
ATOM   2468  CA  GLU D 191      -8.786 -95.882 -27.779  1.00119.29           C
ANISOU 2468  CA  GLU D 191    14762  15500  15065  -1458   -249  -3288       C
ATOM   2469  C   GLU D 191     -10.169 -95.655 -27.180  1.00110.03           C
ANISOU 2469  C   GLU D 191    13548  14307  13953  -1445   -351  -3290       C
ATOM   2470  O   GLU D 191     -10.547 -96.324 -26.209  1.00128.25           O
ANISOU 2470  O   GLU D 191    15777  16596  16357  -1420   -346  -3306       O
ATOM   2471  CB  GLU D 191      -7.705 -94.965 -27.208  1.00111.20           C
ANISOU 2471  CB  GLU D 191    13714  14492  14047  -1454   -202  -3217       C
ATOM   2472  CG  GLU D 191      -6.317 -95.619 -27.226  1.00 89.79           C
ANISOU 2472  CG  GLU D 191    10996  11791  11328  -1454    -77  -3214       C
ATOM   2473  CD  GLU D 191      -5.487 -95.230 -28.425  1.00132.47           C
ANISOU 2473  CD  GLU D 191    16485  17228  16618  -1476    -44  -3193       C
ATOM   2474  OE1 GLU D 191      -4.931 -96.130 -29.095  1.00142.57           O
ANISOU 2474  OE1 GLU D 191    17800  18516  17855  -1478     30  -3229       O
ATOM   2475  OE2 GLU D 191      -5.361 -94.015 -28.688  1.00177.12           O
ANISOU 2475  OE2 GLU D 191    22171  22902  22225  -1489    -91  -3137       O
ATOM   2476  N   LEU D 192     -10.938 -94.750 -27.787  1.00 89.30           N
ANISOU 2476  N   LEU D 192    10973  11688  11271  -1461   -444  -3273       N
ATOM   2477  CA  LEU D 192     -12.306 -94.488 -27.333  1.00 91.73           C
ANISOU 2477  CA  LEU D 192    11248  11978  11625  -1448   -545  -3268       C
ATOM   2478  C   LEU D 192     -13.110 -95.785 -27.434  1.00116.39           C
ANISOU 2478  C   LEU D 192    14358  15082  14785  -1445   -561  -3327       C
ATOM   2479  O   LEU D 192     -13.927 -96.101 -26.574  1.00124.39           O
ANISOU 2479  O   LEU D 192    15302  16080  15882  -1419   -602  -3327       O
ATOM   2480  CB  LEU D 192     -12.960 -93.391 -28.174  1.00 91.03           C
ANISOU 2480  CB  LEU D 192    11228  11901  11457  -1473   -636  -3242       C
ATOM   2481  CG  LEU D 192     -14.185 -92.629 -27.640  1.00114.16           C
ANISOU 2481  CG  LEU D 192    14129  14822  14424  -1457   -740  -3209       C
ATOM   2482  CD1 LEU D 192     -14.838 -91.798 -28.736  1.00122.73           C
ANISOU 2482  CD1 LEU D 192    15292  15920  15421  -1491   -822  -3196       C
ATOM   2483  CD2 LEU D 192     -15.225 -93.548 -27.002  1.00134.13           C
ANISOU 2483  CD2 LEU D 192    16598  17330  17035  -1432   -776  -3236       C
ATOM   2484  N   THR D 193     -12.850 -96.543 -28.489  1.00103.95           N
ANISOU 2484  N   THR D 193    12847  13506  13145  -1470   -528  -3377       N
ATOM   2485  CA  THR D 193     -13.503 -97.823 -28.698  1.00 95.12           C
ANISOU 2485  CA  THR D 193    11725  12364  12052  -1472   -542  -3436       C
ATOM   2486  C   THR D 193     -13.066 -98.804 -27.612  1.00107.20           C
ANISOU 2486  C   THR D 193    13164  13881  13686  -1441   -471  -3453       C
ATOM   2487  O   THR D 193     -13.866 -99.612 -27.129  1.00107.65           O
ANISOU 2487  O   THR D 193    13169  13917  13815  -1428   -507  -3476       O
ATOM   2488  CB  THR D 193     -13.220 -98.366 -30.119  1.00111.88           C
ANISOU 2488  CB  THR D 193    13948  14489  14073  -1503   -520  -3486       C
ATOM   2489  OG1 THR D 193     -13.874 -97.526 -31.086  1.00107.29           O
ANISOU 2489  OG1 THR D 193    13441  13918  13406  -1533   -602  -3471       O
ATOM   2490  CG2 THR D 193     -13.714 -99.803 -30.256  1.00 87.80           C
ANISOU 2490  CG2 THR D 193    10895  11409  11056  -1502   -523  -3550       C
ATOM   2491  N   SER D 194     -11.802 -98.716 -27.207  1.00124.01           N
ANISOU 2491  N   SER D 194    15270  16023  15824  -1432   -373  -3435       N
ATOM   2492  CA  SER D 194     -11.340 -99.485 -26.060  1.00122.62           C
ANISOU 2492  CA  SER D 194    14998  15839  15753  -1405   -303  -3440       C
ATOM   2493  C   SER D 194     -12.120 -99.043 -24.833  1.00120.61           C
ANISOU 2493  C   SER D 194    14654  15580  15593  -1375   -364  -3402       C
ATOM   2494  O   SER D 194     -12.664 -99.867 -24.097  1.00125.48           O
ANISOU 2494  O   SER D 194    15195  16183  16300  -1354   -375  -3421       O
ATOM   2495  CB  SER D 194      -9.854 -99.265 -25.821  1.00101.90           C
ANISOU 2495  CB  SER D 194    12366  13232  13118  -1404   -192  -3412       C
ATOM   2496  OG  SER D 194      -9.125 -99.430 -27.016  1.00117.47           O
ANISOU 2496  OG  SER D 194    14429  15217  14989  -1427   -142  -3433       O
ATOM   2497  N   MET D 195     -12.195 -97.731 -24.633  1.00115.18           N
ANISOU 2497  N   MET D 195    13976  14905  14883  -1372   -407  -3347       N
ATOM   2498  CA  MET D 195     -12.828 -97.172 -23.440  1.00119.63           C
ANISOU 2498  CA  MET D 195    14460  15467  15528  -1337   -459  -3305       C
ATOM   2499  C   MET D 195     -14.213 -97.754 -23.170  1.00119.70           C
ANISOU 2499  C   MET D 195    14426  15461  15592  -1320   -542  -3324       C
ATOM   2500  O   MET D 195     -14.598 -97.889 -22.008  1.00110.15           O
ANISOU 2500  O   MET D 195    13123  14250  14478  -1283   -555  -3305       O
ATOM   2501  CB  MET D 195     -12.868 -95.639 -23.493  1.00104.08           C
ANISOU 2501  CB  MET D 195    12528  13508  13509  -1339   -511  -3249       C
ATOM   2502  CG  MET D 195     -11.497 -94.978 -23.322  1.00115.35           C
ANISOU 2502  CG  MET D 195    13966  14949  14913  -1345   -436  -3211       C
ATOM   2503  SD  MET D 195     -11.588 -93.185 -23.341  1.00114.45           S
ANISOU 2503  SD  MET D 195    13894  14843  14748  -1346   -509  -3143       S
ATOM   2504  CE  MET D 195     -13.336 -92.984 -23.005  1.00126.13           C
ANISOU 2504  CE  MET D 195    15347  16312  16266  -1320   -631  -3143       C
ATOM   2505  N   LYS D 196     -14.944 -98.115 -24.228  1.00 96.82           N
ANISOU 2505  N   LYS D 196    11595  12556  12637  -1347   -597  -3357       N
ATOM   2506  CA  LYS D 196     -16.267 -98.721 -24.069  1.00100.64           C
ANISOU 2506  CA  LYS D 196    12045  13026  13169  -1335   -681  -3368       C
ATOM   2507  C   LYS D 196     -16.199 -99.962 -23.195  1.00108.11           C
ANISOU 2507  C   LYS D 196    12895  13962  14220  -1311   -638  -3394       C
ATOM   2508  O   LYS D 196     -17.186-100.344 -22.565  1.00101.87           O
ANISOU 2508  O   LYS D 196    12036  13166  13502  -1286   -700  -3383       O
ATOM   2509  CB  LYS D 196     -16.888 -99.085 -25.425  1.00112.83           C
ANISOU 2509  CB  LYS D 196    13682  14558  14631  -1375   -735  -3405       C
ATOM   2510  CG  LYS D 196     -17.779-100.349 -25.406  1.00104.85           C
ANISOU 2510  CG  LYS D 196    12640  13526  13674  -1373   -778  -3440       C
ATOM   2511  CD  LYS D 196     -19.259-100.055 -25.643  1.00115.10           C
ANISOU 2511  CD  LYS D 196    13950  14818  14965  -1377   -902  -3413       C
ATOM   2512  CE  LYS D 196     -20.108-101.328 -25.540  1.00128.75           C
ANISOU 2512  CE  LYS D 196    15640  16525  16756  -1375   -949  -3438       C
ATOM   2513  NZ  LYS D 196     -20.691-101.572 -24.178  1.00124.64           N
ANISOU 2513  NZ  LYS D 196    14993  16010  16354  -1326   -977  -3401       N
ATOM   2514  N   TYR D 197     -15.028-100.591 -23.162  1.00 99.73           N
ANISOU 2514  N   TYR D 197    11827  12901  13167  -1317   -532  -3424       N
ATOM   2515  CA  TYR D 197     -14.853-101.843 -22.432  1.00119.02           C
ANISOU 2515  CA  TYR D 197    14182  15334  15706  -1300   -482  -3454       C
ATOM   2516  C   TYR D 197     -14.753-101.680 -20.903  1.00115.81           C
ANISOU 2516  C   TYR D 197    13653  14940  15410  -1257   -461  -3414       C
ATOM   2517  O   TYR D 197     -15.289-102.495 -20.152  1.00110.21           O
ANISOU 2517  O   TYR D 197    12852  14227  14795  -1233   -478  -3421       O
ATOM   2518  CB  TYR D 197     -13.610-102.574 -22.931  1.00112.43           C
ANISOU 2518  CB  TYR D 197    13383  14496  14840  -1321   -371  -3497       C
ATOM   2519  CG  TYR D 197     -13.680-103.168 -24.325  1.00 99.54           C
ANISOU 2519  CG  TYR D 197    11856  12848  13116  -1355   -379  -3552       C
ATOM   2520  CD1 TYR D 197     -13.760-102.360 -25.458  1.00101.89           C
ANISOU 2520  CD1 TYR D 197    12263  13152  13298  -1382   -416  -3547       C
ATOM   2521  CD2 TYR D 197     -13.605-104.542 -24.507  1.00 92.40           C
ANISOU 2521  CD2 TYR D 197    10942  11923  12242  -1358   -347  -3608       C
ATOM   2522  CE1 TYR D 197     -13.794-102.914 -26.736  1.00 94.67           C
ANISOU 2522  CE1 TYR D 197    11446  12225  12298  -1411   -421  -3598       C
ATOM   2523  CE2 TYR D 197     -13.637-105.108 -25.774  1.00102.79           C
ANISOU 2523  CE2 TYR D 197    12360  13223  13473  -1386   -354  -3661       C
ATOM   2524  CZ  TYR D 197     -13.728-104.296 -26.887  1.00106.84           C
ANISOU 2524  CZ  TYR D 197    12983  13744  13869  -1412   -390  -3656       C
ATOM   2525  OH  TYR D 197     -13.749-104.878 -28.144  1.00 88.70           O
ANISOU 2525  OH  TYR D 197    10788  11431  11484  -1438   -396  -3710       O
ATOM   2526  N   PHE D 198     -13.974-100.700 -20.456  1.00 83.63           N
ANISOU 2526  N   PHE D 198     9574  10879  11323  -1249   -417  -3373       N
ATOM   2527  CA  PHE D 198     -13.875-100.357 -19.038  1.00 90.09           C
ANISOU 2527  CA  PHE D 198    10288  11708  12235  -1209   -403  -3331       C
ATOM   2528  C   PHE D 198     -14.640 -99.103 -18.529  1.00114.93           C
ANISOU 2528  C   PHE D 198    13425  14863  15380  -1179   -490  -3275       C
ATOM   2529  O   PHE D 198     -14.524 -98.732 -17.357  1.00 99.51           O
ANISOU 2529  O   PHE D 198    11393  12918  13496  -1142   -479  -3239       O
ATOM   2530  CB  PHE D 198     -12.408-100.290 -18.639  1.00 83.82           C
ANISOU 2530  CB  PHE D 198     9476  10920  11450  -1216   -287  -3321       C
ATOM   2531  CG  PHE D 198     -11.630 -99.278 -19.407  1.00 94.10           C
ANISOU 2531  CG  PHE D 198    10877  12228  12649  -1243   -265  -3298       C
ATOM   2532  CD1 PHE D 198     -11.788 -97.936 -19.146  1.00101.21           C
ANISOU 2532  CD1 PHE D 198    11797  13135  13524  -1232   -317  -3246       C
ATOM   2533  CD2 PHE D 198     -10.748 -99.664 -20.395  1.00104.04           C
ANISOU 2533  CD2 PHE D 198    12208  13486  13835  -1278   -195  -3327       C
ATOM   2534  CE1 PHE D 198     -11.082 -96.997 -19.846  1.00 95.12           C
ANISOU 2534  CE1 PHE D 198    11110  12370  12661  -1258   -303  -3221       C
ATOM   2535  CE2 PHE D 198     -10.035 -98.729 -21.094  1.00103.83           C
ANISOU 2535  CE2 PHE D 198    12266  13470  13716  -1302   -178  -3299       C
ATOM   2536  CZ  PHE D 198     -10.205 -97.392 -20.819  1.00102.68           C
ANISOU 2536  CZ  PHE D 198    12134  13331  13550  -1293   -234  -3245       C
ATOM   2537  N   VAL D 199     -15.383 -98.424 -19.393  1.00100.27           N
ANISOU 2537  N   VAL D 199    11650  13004  13445  -1194   -573  -3266       N
ATOM   2538  CA  VAL D 199     -15.987 -97.153 -18.980  1.00112.57           C
ANISOU 2538  CA  VAL D 199    13210  14569  14993  -1167   -647  -3212       C
ATOM   2539  C   VAL D 199     -17.493 -97.127 -19.106  1.00113.18           C
ANISOU 2539  C   VAL D 199    13283  14645  15076  -1151   -759  -3199       C
ATOM   2540  O   VAL D 199     -18.055 -97.702 -20.029  1.00110.05           O
ANISOU 2540  O   VAL D 199    12934  14240  14642  -1180   -796  -3230       O
ATOM   2541  CB  VAL D 199     -15.376 -95.931 -19.733  1.00108.48           C
ANISOU 2541  CB  VAL D 199    12791  14053  14372  -1196   -645  -3190       C
ATOM   2542  CG1 VAL D 199     -16.380 -94.793 -19.853  1.00 78.65           C
ANISOU 2542  CG1 VAL D 199     9047  10278  10558  -1182   -751  -3148       C
ATOM   2543  CG2 VAL D 199     -14.138 -95.464 -19.025  1.00142.83           C
ANISOU 2543  CG2 VAL D 199    17116  18409  18743  -1188   -565  -3163       C
ATOM   2544  N   LYS D 200     -18.136 -96.464 -18.155  1.00103.02           N
ANISOU 2544  N   LYS D 200    11939  13368  13837  -1102   -812  -3151       N
ATOM   2545  CA  LYS D 200     -19.567 -96.234 -18.203  1.00 95.79           C
ANISOU 2545  CA  LYS D 200    11019  12455  12923  -1081   -921  -3123       C
ATOM   2546  C   LYS D 200     -19.729 -94.732 -18.096  1.00103.99           C
ANISOU 2546  C   LYS D 200    12099  13499  13914  -1063   -967  -3074       C
ATOM   2547  O   LYS D 200     -18.746 -94.029 -17.918  1.00120.15           O
ANISOU 2547  O   LYS D 200    14168  15545  15939  -1067   -917  -3065       O
ATOM   2548  CB  LYS D 200     -20.261 -96.948 -17.042  1.00 87.01           C
ANISOU 2548  CB  LYS D 200     9784  11353  11922  -1027   -943  -3107       C
ATOM   2549  CG  LYS D 200     -21.357 -97.890 -17.483  1.00 99.42           C
ANISOU 2549  CG  LYS D 200    11343  12921  13512  -1035  -1009  -3118       C
ATOM   2550  CD  LYS D 200     -20.839 -99.226 -17.977  1.00 74.09           C
ANISOU 2550  CD  LYS D 200     8135   9699  10318  -1074   -952  -3180       C
ATOM   2551  CE  LYS D 200     -21.881 -99.877 -18.873  1.00101.30           C
ANISOU 2551  CE  LYS D 200    11620  13132  13737  -1102  -1031  -3193       C
ATOM   2552  NZ  LYS D 200     -21.955-101.348 -18.684  1.00 93.47           N
ANISOU 2552  NZ  LYS D 200    10563  12131  12818  -1105  -1015  -3228       N
ATOM   2553  N   ILE D 201     -20.952 -94.231 -18.202  1.00124.89           N
ANISOU 2553  N   ILE D 201    14757  16149  16546  -1044  -1065  -3038       N
ATOM   2554  CA  ILE D 201     -21.161 -92.790 -18.265  1.00128.10           C
ANISOU 2554  CA  ILE D 201    15215  16558  16898  -1033  -1115  -2994       C
ATOM   2555  C   ILE D 201     -22.560 -92.424 -17.797  1.00127.96           C
ANISOU 2555  C   ILE D 201    15161  16549  16907   -983  -1212  -2944       C
ATOM   2556  O   ILE D 201     -23.494 -93.208 -17.919  1.00127.00           O
ANISOU 2556  O   ILE D 201    15009  16432  16814   -979  -1257  -2943       O
ATOM   2557  CB  ILE D 201     -20.951 -92.257 -19.707  1.00118.80           C
ANISOU 2557  CB  ILE D 201    14156  15373  15608  -1097  -1129  -3009       C
ATOM   2558  CG1 ILE D 201     -20.670 -90.752 -19.705  1.00139.20           C
ANISOU 2558  CG1 ILE D 201    16791  17958  18139  -1092  -1152  -2969       C
ATOM   2559  CG2 ILE D 201     -22.164 -92.583 -20.593  1.00 89.40           C
ANISOU 2559  CG2 ILE D 201    10470  11648  11851  -1122  -1209  -3009       C
ATOM   2560  CD1 ILE D 201     -21.892 -89.898 -19.997  1.00167.05           C
ANISOU 2560  CD1 ILE D 201    20352  21488  21630  -1081  -1255  -2926       C
ATOM   2561  N   GLY D 202     -22.712 -91.220 -17.273  1.00113.99           N
ANISOU 2561  N   GLY D 202    13399  14784  15127   -944  -1246  -2898       N
ATOM   2562  CA  GLY D 202     -24.025 -90.765 -16.886  1.00102.54           C
ANISOU 2562  CA  GLY D 202    11924  13345  13692   -894  -1337  -2845       C
ATOM   2563  C   GLY D 202     -23.986 -89.442 -16.162  1.00120.63           C
ANISOU 2563  C   GLY D 202    14221  15638  15976   -843  -1361  -2800       C
ATOM   2564  O   GLY D 202     -23.000 -88.713 -16.239  1.00112.10           O
ANISOU 2564  O   GLY D 202    13188  14547  14859   -862  -1322  -2807       O
ATOM   2565  N   PRO D 203     -25.060 -89.139 -15.425  1.00135.37           N
ANISOU 2565  N   PRO D 203    16038  17517  17878   -776  -1427  -2749       N
ATOM   2566  CA  PRO D 203     -25.194 -87.866 -14.727  1.00113.50           C
ANISOU 2566  CA  PRO D 203    13278  14749  15100   -718  -1462  -2703       C
ATOM   2567  C   PRO D 203     -24.157 -87.814 -13.625  1.00129.98           C
ANISOU 2567  C   PRO D 203    15313  16832  17240   -682  -1393  -2714       C
ATOM   2568  O   PRO D 203     -23.874 -88.844 -13.010  1.00153.29           O
ANISOU 2568  O   PRO D 203    18184  19794  20266   -669  -1342  -2736       O
ATOM   2569  CB  PRO D 203     -26.591 -87.970 -14.120  1.00130.80           C
ANISOU 2569  CB  PRO D 203    15406  16960  17333   -649  -1535  -2651       C
ATOM   2570  CG  PRO D 203     -26.741 -89.432 -13.821  1.00111.35           C
ANISOU 2570  CG  PRO D 203    12854  14510  14944   -647  -1506  -2673       C
ATOM   2571  CD  PRO D 203     -26.055 -90.127 -14.965  1.00139.47           C
ANISOU 2571  CD  PRO D 203    16471  18055  18467   -739  -1460  -2733       C
ATOM   2572  N   GLU D 204     -23.588 -86.645 -13.372  1.00127.30           N
ANISOU 2572  N   GLU D 204    15021  16480  16868   -669  -1394  -2697       N
ATOM   2573  CA  GLU D 204     -22.624 -86.541 -12.293  1.00110.29           C
ANISOU 2573  CA  GLU D 204    12821  14320  14764   -636  -1334  -2701       C
ATOM   2574  C   GLU D 204     -23.259 -87.136 -11.041  1.00102.79           C
ANISOU 2574  C   GLU D 204    11759  13393  13906   -554  -1340  -2682       C
ATOM   2575  O   GLU D 204     -24.445 -86.940 -10.797  1.00126.06           O
ANISOU 2575  O   GLU D 204    14682  16354  16859   -501  -1411  -2643       O
ATOM   2576  CB  GLU D 204     -22.227 -85.081 -12.065  1.00105.82           C
ANISOU 2576  CB  GLU D 204    12319  13735  14152   -617  -1361  -2672       C
ATOM   2577  CG  GLU D 204     -21.154 -84.578 -13.005  1.00118.01           C
ANISOU 2577  CG  GLU D 204    13953  15260  15626   -694  -1330  -2691       C
ATOM   2578  CD  GLU D 204     -19.776 -85.086 -12.638  1.00136.57           C
ANISOU 2578  CD  GLU D 204    16277  17604  18011   -721  -1234  -2718       C
ATOM   2579  OE1 GLU D 204     -18.877 -84.234 -12.440  1.00144.07           O
ANISOU 2579  OE1 GLU D 204    17268  18535  18937   -729  -1220  -2703       O
ATOM   2580  OE2 GLU D 204     -19.590 -86.327 -12.556  1.00116.09           O
ANISOU 2580  OE2 GLU D 204    13621  15021  15467   -735  -1175  -2752       O
ATOM   2581  N   ARG D 205     -22.480 -87.889 -10.269  1.00126.83           N
ANISOU 2581  N   ARG D 205    14727  16441  17020   -546  -1265  -2705       N
ATOM   2582  CA  ARG D 205     -22.945 -88.405  -8.980  1.00115.40           C
ANISOU 2582  CA  ARG D 205    13165  15019  15664   -467  -1264  -2685       C
ATOM   2583  C   ARG D 205     -21.822 -88.395  -7.932  1.00118.08           C
ANISOU 2583  C   ARG D 205    13455  15352  16056   -447  -1190  -2695       C
ATOM   2584  O   ARG D 205     -20.652 -88.608  -8.257  1.00131.87           O
ANISOU 2584  O   ARG D 205    15228  17082  17792   -508  -1117  -2728       O
ATOM   2585  CB  ARG D 205     -23.569 -89.803  -9.142  1.00 92.67           C
ANISOU 2585  CB  ARG D 205    10209  12161  12839   -476  -1261  -2701       C
ATOM   2586  CG  ARG D 205     -24.970 -89.767  -9.766  1.00134.12           C
ANISOU 2586  CG  ARG D 205    15480  17423  18057   -466  -1352  -2669       C
ATOM   2587  CD  ARG D 205     -25.449 -91.107 -10.353  1.00164.95           C
ANISOU 2587  CD  ARG D 205    19347  21338  21991   -506  -1355  -2691       C
ATOM   2588  NE  ARG D 205     -26.402 -91.828  -9.502  1.00184.27           N
ANISOU 2588  NE  ARG D 205    21678  23816  24519   -439  -1390  -2655       N
ATOM   2589  CZ  ARG D 205     -27.718 -91.606  -9.459  1.00183.15           C
ANISOU 2589  CZ  ARG D 205    21522  23694  24373   -392  -1478  -2598       C
ATOM   2590  NH1 ARG D 205     -28.273 -90.654 -10.205  1.00189.13           N
ANISOU 2590  NH1 ARG D 205    22373  24440  25048   -404  -1538  -2572       N
ATOM   2591  NH2 ARG D 205     -28.483 -92.336  -8.653  1.00156.60           N
ANISOU 2591  NH2 ARG D 205    18046  20365  21090   -331  -1504  -2562       N
ATOM   2592  N   THR D 206     -22.177 -88.118  -6.682  1.00111.08           N
ANISOU 2592  N   THR D 206    12501  14481  15223   -360  -1209  -2662       N
ATOM   2593  CA  THR D 206     -21.205 -88.117  -5.595  1.00111.02           C
ANISOU 2593  CA  THR D 206    12441  14471  15271   -337  -1144  -2666       C
ATOM   2594  C   THR D 206     -20.882 -89.556  -5.201  1.00116.96           C
ANISOU 2594  C   THR D 206    13084  15245  16111   -351  -1072  -2695       C
ATOM   2595  O   THR D 206     -21.688 -90.457  -5.432  1.00116.98           O
ANISOU 2595  O   THR D 206    13032  15269  16144   -348  -1093  -2699       O
ATOM   2596  CB  THR D 206     -21.753 -87.379  -4.360  1.00131.37           C
ANISOU 2596  CB  THR D 206    14978  17060  17877   -233  -1190  -2621       C
ATOM   2597  OG1 THR D 206     -22.344 -88.322  -3.458  1.00138.26           O
ANISOU 2597  OG1 THR D 206    15721  17971  18839   -173  -1184  -2611       O
ATOM   2598  CG2 THR D 206     -22.804 -86.347  -4.774  1.00162.30           C
ANISOU 2598  CG2 THR D 206    18970  20973  21725   -196  -1288  -2584       C
ATOM   2599  N   CYS D 207     -19.700 -89.772  -4.622  1.00119.29           N
ANISOU 2599  N   CYS D 207    13346  15531  16446   -370   -989  -2712       N
ATOM   2600  CA  CYS D 207     -19.334 -91.072  -4.048  1.00 95.23           C
ANISOU 2600  CA  CYS D 207    10184  12506  13492   -376   -917  -2736       C
ATOM   2601  C   CYS D 207     -20.358 -91.363  -2.974  1.00110.22           C
ANISOU 2601  C   CYS D 207    11972  14443  15465   -283   -960  -2704       C
ATOM   2602  O   CYS D 207     -20.883 -90.430  -2.350  1.00148.45           O
ANISOU 2602  O   CYS D 207    16824  19288  20292   -211  -1017  -2665       O
ATOM   2603  CB  CYS D 207     -17.934 -91.012  -3.433  1.00108.83           C
ANISOU 2603  CB  CYS D 207    11893  14215  15245   -400   -827  -2745       C
ATOM   2604  SG  CYS D 207     -17.405 -92.455  -2.457  1.00 97.98           S
ANISOU 2604  SG  CYS D 207    10364  12868  13995   -398   -733  -2766       S
ATOM   2605  N   CYS D 208     -20.678 -92.632  -2.753  1.00 90.92           N
ANISOU 2605  N   CYS D 208     9422  12028  13097   -281   -938  -2717       N
ATOM   2606  CA  CYS D 208     -21.695 -92.928  -1.755  1.00124.01           C
ANISOU 2606  CA  CYS D 208    13500  16260  17358   -191   -985  -2679       C
ATOM   2607  C   CYS D 208     -21.154 -92.741  -0.338  1.00115.94           C
ANISOU 2607  C   CYS D 208    12397  15252  16402   -133   -942  -2664       C
ATOM   2608  O   CYS D 208     -21.845 -92.222   0.536  1.00110.19           O
ANISOU 2608  O   CYS D 208    11629  14548  15692    -42   -993  -2622       O
ATOM   2609  CB  CYS D 208     -22.289 -94.322  -1.957  1.00129.07           C
ANISOU 2609  CB  CYS D 208    14050  16929  18063   -204   -988  -2691       C
ATOM   2610  SG  CYS D 208     -21.116 -95.651  -1.931  1.00119.80           S
ANISOU 2610  SG  CYS D 208    12807  15753  16961   -275   -874  -2745       S
ATOM   2611  N   LEU D 209     -19.895 -93.106  -0.141  1.00109.46           N
ANISOU 2611  N   LEU D 209    11561  14418  15612   -185   -849  -2695       N
ATOM   2612  CA  LEU D 209     -19.243 -93.014   1.160  1.00 94.05           C
ANISOU 2612  CA  LEU D 209     9532  12478  13726   -145   -797  -2683       C
ATOM   2613  C   LEU D 209     -18.533 -91.678   1.420  1.00106.10           C
ANISOU 2613  C   LEU D 209    11152  13967  15193   -138   -797  -2668       C
ATOM   2614  O   LEU D 209     -17.886 -91.509   2.451  1.00129.67           O
ANISOU 2614  O   LEU D 209    14090  16955  18224   -112   -754  -2658       O
ATOM   2615  CB  LEU D 209     -18.236 -94.153   1.303  1.00100.79           C
ANISOU 2615  CB  LEU D 209    10310  13335  14651   -207   -693  -2718       C
ATOM   2616  CG  LEU D 209     -18.780 -95.443   1.897  1.00101.37           C
ANISOU 2616  CG  LEU D 209    10231  13456  14830   -177   -683  -2719       C
ATOM   2617  CD1 LEU D 209     -20.135 -95.747   1.313  1.00 95.88           C
ANISOU 2617  CD1 LEU D 209     9531  12779  14119   -151   -771  -2706       C
ATOM   2618  CD2 LEU D 209     -17.789 -96.559   1.635  1.00100.04           C
ANISOU 2618  CD2 LEU D 209    10019  13281  14710   -258   -583  -2762       C
ATOM   2619  N   CYS D 210     -18.629 -90.735   0.491  1.00 86.03           N
ANISOU 2619  N   CYS D 210     8744  11392  12552   -164   -845  -2666       N
ATOM   2620  CA  CYS D 210     -18.066 -89.409   0.727  1.00 91.38           C
ANISOU 2620  CA  CYS D 210     9513  12035  13173   -153   -861  -2647       C
ATOM   2621  C   CYS D 210     -18.811 -88.294  -0.003  1.00129.29           C
ANISOU 2621  C   CYS D 210    14430  16816  17879   -136   -954  -2627       C
ATOM   2622  O   CYS D 210     -19.945 -88.473  -0.477  1.00138.66           O
ANISOU 2622  O   CYS D 210    15614  18023  19050   -112  -1015  -2619       O
ATOM   2623  CB  CYS D 210     -16.569 -89.365   0.427  1.00 59.64           C
ANISOU 2623  CB  CYS D 210     5542   7980   9137   -239   -777  -2667       C
ATOM   2624  SG  CYS D 210     -16.077 -89.175  -1.291  1.00146.29           S
ANISOU 2624  SG  CYS D 210    16649  18921  20012   -344   -771  -2692       S
ATOM   2625  N   ASP D 211     -18.209 -87.113   0.009  1.00100.96           N
ANISOU 2625  N   ASP D 211    10938  13190  14232   -142   -969  -2613       N
ATOM   2626  CA  ASP D 211     -18.781 -85.976  -0.689  1.00126.97           C
ANISOU 2626  CA  ASP D 211    14347  16462  17436   -132  -1053  -2595       C
ATOM   2627  C   ASP D 211     -18.118 -85.663  -2.022  1.00114.31           C
ANISOU 2627  C   ASP D 211    12853  14825  15753   -230  -1042  -2614       C
ATOM   2628  O   ASP D 211     -18.541 -84.772  -2.759  1.00101.12           O
ANISOU 2628  O   ASP D 211    11279  13138  14006   -236  -1109  -2601       O
ATOM   2629  CB  ASP D 211     -18.835 -84.781   0.251  1.00149.38           C
ANISOU 2629  CB  ASP D 211    17216  19282  20258    -54  -1102  -2561       C
ATOM   2630  CG  ASP D 211     -19.907 -84.955   1.308  1.00173.19           C
ANISOU 2630  CG  ASP D 211    20138  22337  23327     58  -1141  -2535       C
ATOM   2631  OD1 ASP D 211     -20.987 -85.503   0.961  1.00148.01           O
ANISOU 2631  OD1 ASP D 211    16909  19182  20148     80  -1177  -2529       O
ATOM   2632  OD2 ASP D 211     -19.670 -84.575   2.475  1.00175.35           O
ANISOU 2632  OD2 ASP D 211    20379  22611  23635    122  -1137  -2518       O
ATOM   2633  N   LYS D 212     -17.089 -86.438  -2.331  1.00129.47           N
ANISOU 2633  N   LYS D 212    14754  16741  17696   -306   -955  -2643       N
ATOM   2634  CA  LYS D 212     -16.253 -86.210  -3.501  1.00108.09           C
ANISOU 2634  CA  LYS D 212    12143  14007  14919   -398   -928  -2658       C
ATOM   2635  C   LYS D 212     -16.933 -86.801  -4.717  1.00114.71           C
ANISOU 2635  C   LYS D 212    13005  14859  15723   -440   -948  -2683       C
ATOM   2636  O   LYS D 212     -17.541 -87.867  -4.640  1.00133.92           O
ANISOU 2636  O   LYS D 212    15355  17319  18207   -427   -936  -2701       O
ATOM   2637  CB  LYS D 212     -14.869 -86.853  -3.291  1.00109.38           C
ANISOU 2637  CB  LYS D 212    12273  14164  15124   -457   -821  -2673       C
ATOM   2638  CG  LYS D 212     -13.682 -85.901  -3.480  1.00146.87           C
ANISOU 2638  CG  LYS D 212    17111  18874  19819   -503   -804  -2651       C
ATOM   2639  CD  LYS D 212     -12.461 -86.318  -2.651  1.00130.11           C
ANISOU 2639  CD  LYS D 212    14931  16746  17758   -525   -712  -2645       C
ATOM   2640  CE  LYS D 212     -11.143 -85.907  -3.334  1.00148.61           C
ANISOU 2640  CE  LYS D 212    17357  19062  20047   -607   -667  -2631       C
ATOM   2641  NZ  LYS D 212     -11.020 -84.443  -3.573  1.00140.04           N
ANISOU 2641  NZ  LYS D 212    16380  17942  18885   -604   -743  -2594       N
ATOM   2642  N   ARG D 213     -16.838 -86.103  -5.840  1.00123.33           N
ANISOU 2642  N   ARG D 213    14205  15929  16725   -490   -982  -2682       N
ATOM   2643  CA  ARG D 213     -17.414 -86.587  -7.086  1.00129.30           C
ANISOU 2643  CA  ARG D 213    14996  16695  17438   -536  -1002  -2706       C
ATOM   2644  C   ARG D 213     -16.928 -88.001  -7.409  1.00114.90           C
ANISOU 2644  C   ARG D 213    13116  14885  15656   -589   -918  -2748       C
ATOM   2645  O   ARG D 213     -15.743 -88.299  -7.308  1.00133.75           O
ANISOU 2645  O   ARG D 213    15496  17263  18059   -630   -836  -2760       O
ATOM   2646  CB  ARG D 213     -17.053 -85.623  -8.209  1.00143.34           C
ANISOU 2646  CB  ARG D 213    16898  18449  19116   -593  -1032  -2699       C
ATOM   2647  CG  ARG D 213     -16.750 -86.299  -9.507  1.00122.14           C
ANISOU 2647  CG  ARG D 213    14252  15767  16389   -674   -996  -2734       C
ATOM   2648  CD  ARG D 213     -15.962 -85.402 -10.423  1.00117.08           C
ANISOU 2648  CD  ARG D 213    13718  15105  15662   -734   -999  -2724       C
ATOM   2649  NE  ARG D 213     -15.296 -86.217 -11.425  1.00136.62           N
ANISOU 2649  NE  ARG D 213    16214  17586  18111   -809   -933  -2759       N
ATOM   2650  CZ  ARG D 213     -15.886 -86.676 -12.522  1.00142.75           C
ANISOU 2650  CZ  ARG D 213    17022  18371  18844   -845   -954  -2786       C
ATOM   2651  NH1 ARG D 213     -17.155 -86.382 -12.763  1.00116.06           N
ANISOU 2651  NH1 ARG D 213    13655  14998  15445   -816  -1039  -2777       N
ATOM   2652  NH2 ARG D 213     -15.200 -87.426 -13.378  1.00162.59           N
ANISOU 2652  NH2 ARG D 213    19556  20888  21333   -907   -889  -2819       N
ATOM   2653  N   ALA D 214     -17.854 -88.866  -7.807  1.00122.01           N
ANISOU 2653  N   ALA D 214    13978  15806  16574   -586   -940  -2767       N
ATOM   2654  CA  ALA D 214     -17.558 -90.282  -8.062  1.00122.69           C
ANISOU 2654  CA  ALA D 214    14006  15905  16707   -627   -871  -2808       C
ATOM   2655  C   ALA D 214     -16.917 -90.560  -9.426  1.00119.83           C
ANISOU 2655  C   ALA D 214    13725  15528  16275   -714   -833  -2842       C
ATOM   2656  O   ALA D 214     -17.483 -90.188 -10.462  1.00123.36           O
ANISOU 2656  O   ALA D 214    14251  15970  16649   -739   -891  -2844       O
ATOM   2657  CB  ALA D 214     -18.827 -91.105  -7.917  1.00 93.47           C
ANISOU 2657  CB  ALA D 214    10231  12230  13054   -588   -919  -2809       C
ATOM   2658  N   THR D 215     -15.726 -91.170  -9.419  1.00 82.66           N
ANISOU 2658  N   THR D 215     9001  10816  11589   -758   -736  -2865       N
ATOM   2659  CA  THR D 215     -15.061 -91.576 -10.659  1.00108.97           C
ANISOU 2659  CA  THR D 215    12403  14140  14861   -834   -690  -2898       C
ATOM   2660  C   THR D 215     -15.162 -93.037 -11.055  1.00110.12           C
ANISOU 2660  C   THR D 215    12502  14295  15043   -861   -645  -2945       C
ATOM   2661  O   THR D 215     -14.721 -93.413 -12.151  1.00 96.86           O
ANISOU 2661  O   THR D 215    10886  12610  13308   -920   -612  -2976       O
ATOM   2662  CB  THR D 215     -13.570 -91.299 -10.618  1.00120.98           C
ANISOU 2662  CB  THR D 215    13952  15648  16366   -874   -606  -2890       C
ATOM   2663  OG1 THR D 215     -13.188 -90.992  -9.279  1.00 85.56           O
ANISOU 2663  OG1 THR D 215     9401  11162  11947   -830   -584  -2860       O
ATOM   2664  CG2 THR D 215     -13.218 -90.146 -11.559  1.00176.97           C
ANISOU 2664  CG2 THR D 215    21163  22724  23353   -911   -640  -2869       C
ATOM   2665  N   CYS D 216     -15.729 -93.865 -10.189  1.00107.48           N
ANISOU 2665  N   CYS D 216    12059  13978  14800   -819   -646  -2950       N
ATOM   2666  CA  CYS D 216     -15.743 -95.290 -10.461  1.00105.29           C
ANISOU 2666  CA  CYS D 216    11731  13708  14568   -844   -602  -2993       C
ATOM   2667  C   CYS D 216     -17.093 -95.873 -10.138  1.00102.30           C
ANISOU 2667  C   CYS D 216    11279  13346  14243   -799   -674  -2989       C
ATOM   2668  O   CYS D 216     -17.798 -95.368  -9.271  1.00132.33           O
ANISOU 2668  O   CYS D 216    15033  17163  18082   -737   -729  -2951       O
ATOM   2669  CB  CYS D 216     -14.657 -95.983  -9.659  1.00 84.29           C
ANISOU 2669  CB  CYS D 216     8990  11052  11983   -850   -496  -3003       C
ATOM   2670  SG  CYS D 216     -13.111 -95.085  -9.723  1.00116.92           S
ANISOU 2670  SG  CYS D 216    13193  15168  16063   -888   -421  -2983       S
ATOM   2671  N   PHE D 217     -17.447 -96.940 -10.839  1.00 84.71           N
ANISOU 2671  N   PHE D 217     9048  11117  12019   -830   -676  -3027       N
ATOM   2672  CA  PHE D 217     -18.760 -97.537 -10.702  1.00 91.51           C
ANISOU 2672  CA  PHE D 217     9851  11994  12925   -797   -753  -3019       C
ATOM   2673  C   PHE D 217     -18.624 -99.041 -10.562  1.00117.47           C
ANISOU 2673  C   PHE D 217    13055  15287  16290   -812   -706  -3056       C
ATOM   2674  O   PHE D 217     -17.698 -99.643 -11.116  1.00121.08           O
ANISOU 2674  O   PHE D 217    13544  15730  16732   -864   -629  -3100       O
ATOM   2675  CB  PHE D 217     -19.591 -97.180 -11.922  1.00 89.24           C
ANISOU 2675  CB  PHE D 217     9665  11694  12548   -824   -835  -3019       C
ATOM   2676  CG  PHE D 217     -20.875 -97.959 -12.054  1.00115.56           C
ANISOU 2676  CG  PHE D 217    12953  15037  15916   -808   -912  -3013       C
ATOM   2677  CD1 PHE D 217     -20.865 -99.265 -12.514  1.00117.59           C
ANISOU 2677  CD1 PHE D 217    13189  15288  16202   -843   -891  -3056       C
ATOM   2678  CD2 PHE D 217     -22.092 -97.368 -11.771  1.00130.23           C
ANISOU 2678  CD2 PHE D 217    14798  16910  17774   -758  -1009  -2961       C
ATOM   2679  CE1 PHE D 217     -22.031 -99.976 -12.660  1.00 83.43           C
ANISOU 2679  CE1 PHE D 217     8826  10968  11907   -832   -969  -3046       C
ATOM   2680  CE2 PHE D 217     -23.260 -98.078 -11.913  1.00140.24           C
ANISOU 2680  CE2 PHE D 217    16025  18187  19072   -745  -1083  -2946       C
ATOM   2681  CZ  PHE D 217     -23.225 -99.385 -12.359  1.00129.37           C
ANISOU 2681  CZ  PHE D 217    14626  16803  17727   -784  -1065  -2988       C
ATOM   2682  N   SER D 218     -19.535 -99.645  -9.803  1.00 93.97           N
ANISOU 2682  N   SER D 218     9972  12333  13399   -763   -753  -3035       N
ATOM   2683  CA  SER D 218     -19.523-101.091  -9.615  1.00109.47           C
ANISOU 2683  CA  SER D 218    11846  14303  15445   -774   -721  -3066       C
ATOM   2684  C   SER D 218     -20.775-101.733 -10.189  1.00112.35           C
ANISOU 2684  C   SER D 218    12209  14668  15811   -775   -815  -3064       C
ATOM   2685  O   SER D 218     -21.893-101.240 -10.017  1.00 94.46           O
ANISOU 2685  O   SER D 218     9933  12416  13540   -733   -908  -3016       O
ATOM   2686  CB  SER D 218     -19.390-101.476  -8.142  1.00 91.60           C
ANISOU 2686  CB  SER D 218     9435  12070  13299   -721   -686  -3043       C
ATOM   2687  OG  SER D 218     -19.273-102.887  -8.022  1.00122.01           O
ANISOU 2687  OG  SER D 218    13203  15926  17230   -738   -650  -3076       O
ATOM   2688  N   THR D 219     -20.573-102.823 -10.911  1.00114.79           N
ANISOU 2688  N   THR D 219    12533  14959  16121   -824   -791  -3113       N
ATOM   2689  CA  THR D 219     -21.677-103.643 -11.357  1.00121.63           C
ANISOU 2689  CA  THR D 219    13384  15824  17006   -828   -875  -3112       C
ATOM   2690  C   THR D 219     -22.088-104.620 -10.259  1.00129.52           C
ANISOU 2690  C   THR D 219    14226  16851  18136   -784   -884  -3093       C
ATOM   2691  O   THR D 219     -23.263-104.924 -10.087  1.00145.21           O
ANISOU 2691  O   THR D 219    16160  18853  20159   -753   -978  -3054       O
ATOM   2692  CB  THR D 219     -21.304-104.378 -12.638  1.00120.87           C
ANISOU 2692  CB  THR D 219    13380  15692  16851   -898   -852  -3174       C
ATOM   2693  OG1 THR D 219     -19.891-104.621 -12.641  1.00107.25           O
ANISOU 2693  OG1 THR D 219    11668  13957  15124   -928   -732  -3220       O
ATOM   2694  CG2 THR D 219     -21.643-103.508 -13.827  1.00 97.33           C
ANISOU 2694  CG2 THR D 219    10542  12692  13746   -930   -905  -3173       C
ATOM   2695  N   SER D 220     -21.095-105.095  -9.513  1.00129.42           N
ANISOU 2695  N   SER D 220    14135  16846  18191   -783   -787  -3115       N
ATOM   2696  CA  SER D 220     -21.286-106.112  -8.487  1.00 97.98           C
ANISOU 2696  CA  SER D 220     9998  12892  14338   -749   -779  -3104       C
ATOM   2697  C   SER D 220     -22.404-105.710  -7.565  1.00113.83           C
ANISOU 2697  C   SER D 220    11915  14938  16397   -675   -866  -3033       C
ATOM   2698  O   SER D 220     -23.348-106.470  -7.340  1.00153.55           O
ANISOU 2698  O   SER D 220    16864  19987  21493   -651   -937  -3007       O
ATOM   2699  CB  SER D 220     -19.987-106.293  -7.705  1.00130.11           C
ANISOU 2699  CB  SER D 220    14004  16969  18462   -754   -656  -3126       C
ATOM   2700  OG  SER D 220     -18.869-106.296  -8.594  1.00143.31           O
ANISOU 2700  OG  SER D 220    15783  18607  20061   -817   -572  -3180       O
ATOM   2701  N   SER D 221     -22.273-104.515  -7.009  1.00138.14           N
ANISOU 2701  N   SER D 221    15007  18031  19448   -635   -859  -2998       N
ATOM   2702  CA  SER D 221     -23.317-103.913  -6.190  1.00149.95           C
ANISOU 2702  CA  SER D 221    16438  19563  20974   -557   -940  -2927       C
ATOM   2703  C   SER D 221     -23.525-102.518  -6.710  1.00108.77           C
ANISOU 2703  C   SER D 221    11347  14332  15648   -552   -979  -2906       C
ATOM   2704  O   SER D 221     -22.674-101.663  -6.477  1.00154.81           O
ANISOU 2704  O   SER D 221    17222  20154  21444   -552   -920  -2913       O
ATOM   2705  CB  SER D 221     -22.830-103.809  -4.744  1.00173.64           C
ANISOU 2705  CB  SER D 221    19316  22598  24062   -501   -883  -2905       C
ATOM   2706  OG  SER D 221     -21.675-102.975  -4.637  1.00126.40           O
ANISOU 2706  OG  SER D 221    13396  16597  18033   -519   -800  -2926       O
ATOM   2707  N   ASP D 222     -24.647-102.243  -7.352  1.00 96.14           N
ANISOU 2707  N   ASP D 222     9801  12730  13999   -546  -1079  -2874       N
ATOM   2708  CA  ASP D 222     -24.755-100.959  -8.024  1.00 94.80           C
ANISOU 2708  CA  ASP D 222     9761  12540  13717   -556  -1109  -2862       C
ATOM   2709  C   ASP D 222     -24.428 -99.904  -6.959  1.00112.26           C
ANISOU 2709  C   ASP D 222    11942  14770  15940   -493  -1085  -2828       C
ATOM   2710  O   ASP D 222     -25.079 -99.834  -5.928  1.00129.12           O
ANISOU 2710  O   ASP D 222    13978  16942  18138   -418  -1122  -2777       O
ATOM   2711  CB  ASP D 222     -26.177-100.787  -8.567  1.00 99.39           C
ANISOU 2711  CB  ASP D 222    10374  13128  14264   -541  -1228  -2813       C
ATOM   2712  CG  ASP D 222     -26.363 -99.498  -9.347  1.00141.76           C
ANISOU 2712  CG  ASP D 222    15874  18473  19514   -556  -1264  -2800       C
ATOM   2713  OD1 ASP D 222     -25.719 -98.489  -8.989  1.00173.05           O
ANISOU 2713  OD1 ASP D 222    19872  22434  23447   -538  -1224  -2799       O
ATOM   2714  OD2 ASP D 222     -27.160 -99.493 -10.317  1.00116.13           O
ANISOU 2714  OD2 ASP D 222    12699  15215  16212   -587  -1336  -2789       O
ATOM   2715  N   THR D 223     -23.375 -99.127  -7.206  1.00133.30           N
ANISOU 2715  N   THR D 223    14693  17411  18544   -525  -1020  -2857       N
ATOM   2716  CA  THR D 223     -22.883 -98.059  -6.323  1.00108.19           C
ANISOU 2716  CA  THR D 223    11509  14238  15362   -479   -993  -2832       C
ATOM   2717  C   THR D 223     -21.944 -97.152  -7.114  1.00115.59           C
ANISOU 2717  C   THR D 223    12581  15139  16201   -534   -952  -2860       C
ATOM   2718  O   THR D 223     -21.468 -97.522  -8.179  1.00133.45           O
ANISOU 2718  O   THR D 223    14916  17375  18412   -606   -922  -2904       O
ATOM   2719  CB  THR D 223     -22.114 -98.598  -5.101  1.00124.79           C
ANISOU 2719  CB  THR D 223    13490  16360  17564   -452   -913  -2839       C
ATOM   2720  OG1 THR D 223     -21.196 -99.627  -5.503  1.00132.07           O
ANISOU 2720  OG1 THR D 223    14402  17267  18512   -520   -829  -2895       O
ATOM   2721  CG2 THR D 223     -23.070 -99.160  -4.079  1.00146.66           C
ANISOU 2721  CG2 THR D 223    16119  19175  20430   -377   -961  -2796       C
ATOM   2722  N   TYR D 224     -21.658 -95.971  -6.594  1.00104.42           N
ANISOU 2722  N   TYR D 224    11197  13721  14757   -499   -953  -2833       N
ATOM   2723  CA  TYR D 224     -20.645 -95.113  -7.201  1.00104.22           C
ANISOU 2723  CA  TYR D 224    11286  13664  14650   -549   -910  -2852       C
ATOM   2724  C   TYR D 224     -19.499 -94.851  -6.201  1.00115.55           C
ANISOU 2724  C   TYR D 224    12679  15098  16128   -536   -830  -2851       C
ATOM   2725  O   TYR D 224     -19.669 -94.999  -4.994  1.00136.17           O
ANISOU 2725  O   TYR D 224    15187  17734  18819   -474   -825  -2827       O
ATOM   2726  CB  TYR D 224     -21.270 -93.801  -7.690  1.00125.40           C
ANISOU 2726  CB  TYR D 224    14069  16335  17243   -534   -992  -2819       C
ATOM   2727  CG  TYR D 224     -22.218 -93.943  -8.872  1.00121.83           C
ANISOU 2727  CG  TYR D 224    13681  15877  16731   -566  -1063  -2821       C
ATOM   2728  CD1 TYR D 224     -23.275 -94.844  -8.850  1.00120.04           C
ANISOU 2728  CD1 TYR D 224    13386  15671  16552   -545  -1113  -2809       C
ATOM   2729  CD2 TYR D 224     -22.067 -93.147 -10.000  1.00126.64           C
ANISOU 2729  CD2 TYR D 224    14417  16463  17237   -617  -1085  -2829       C
ATOM   2730  CE1 TYR D 224     -24.144 -94.957  -9.933  1.00132.11           C
ANISOU 2730  CE1 TYR D 224    14977  17193  18025   -578  -1181  -2806       C
ATOM   2731  CE2 TYR D 224     -22.922 -93.251 -11.076  1.00136.95           C
ANISOU 2731  CE2 TYR D 224    15783  17764  18488   -649  -1149  -2829       C
ATOM   2732  CZ  TYR D 224     -23.960 -94.154 -11.044  1.00134.52           C
ANISOU 2732  CZ  TYR D 224    15411  17474  18227   -631  -1197  -2818       C
ATOM   2733  OH  TYR D 224     -24.813 -94.248 -12.130  1.00107.56           O
ANISOU 2733  OH  TYR D 224    12059  14051  14756   -667  -1264  -2814       O
ATOM   2734  N   ALA D 225     -18.325 -94.488  -6.704  1.00113.40           N
ANISOU 2734  N   ALA D 225    12485  14799  15804   -594   -766  -2873       N
ATOM   2735  CA  ALA D 225     -17.188 -94.238  -5.832  1.00100.61           C
ANISOU 2735  CA  ALA D 225    10832  13175  14220   -590   -690  -2867       C
ATOM   2736  C   ALA D 225     -16.128 -93.293  -6.411  1.00109.70           C
ANISOU 2736  C   ALA D 225    12097  14295  15288   -640   -657  -2866       C
ATOM   2737  O   ALA D 225     -15.929 -93.223  -7.621  1.00124.11           O
ANISOU 2737  O   ALA D 225    14015  16104  17037   -698   -658  -2887       O
ATOM   2738  CB  ALA D 225     -16.562 -95.546  -5.416  1.00 97.18           C
ANISOU 2738  CB  ALA D 225    10299  12753  13872   -612   -601  -2897       C
ATOM   2739  N   CYS D 226     -15.459 -92.565  -5.522  1.00 92.34           N
ANISOU 2739  N   CYS D 226     9889  12090  13107   -616   -633  -2838       N
ATOM   2740  CA  CYS D 226     -14.253 -91.810  -5.848  1.00111.33           C
ANISOU 2740  CA  CYS D 226    12380  14468  15455   -664   -588  -2829       C
ATOM   2741  C   CYS D 226     -13.095 -92.770  -5.708  1.00119.64           C
ANISOU 2741  C   CYS D 226    13381  15521  16555   -712   -474  -2851       C
ATOM   2742  O   CYS D 226     -13.286 -93.930  -5.358  1.00143.52           O
ANISOU 2742  O   CYS D 226    16310  18566  19655   -705   -437  -2875       O
ATOM   2743  CB  CYS D 226     -14.041 -90.681  -4.856  1.00110.26           C
ANISOU 2743  CB  CYS D 226    12249  14321  15324   -615   -614  -2786       C
ATOM   2744  SG  CYS D 226     -13.534 -91.324  -3.261  1.00115.91           S
ANISOU 2744  SG  CYS D 226    12827  15055  16160   -576   -542  -2777       S
ATOM   2745  N   TRP D 227     -11.888 -92.282  -5.940  1.00 95.03           N
ANISOU 2745  N   TRP D 227    10325  12384  13398   -759   -420  -2838       N
ATOM   2746  CA  TRP D 227     -10.734 -93.158  -5.962  1.00106.94           C
ANISOU 2746  CA  TRP D 227    11799  13894  14940   -811   -307  -2854       C
ATOM   2747  C   TRP D 227     -10.319 -93.739  -4.614  1.00128.45           C
ANISOU 2747  C   TRP D 227    14400  16631  17772   -785   -243  -2845       C
ATOM   2748  O   TRP D 227      -9.509 -94.669  -4.553  1.00110.05           O
ANISOU 2748  O   TRP D 227    12020  14307  15487   -823   -148  -2861       O
ATOM   2749  CB  TRP D 227      -9.584 -92.443  -6.629  1.00 83.86           C
ANISOU 2749  CB  TRP D 227     8975  10947  11939   -867   -271  -2833       C
ATOM   2750  CG  TRP D 227      -9.786 -92.415  -8.092  1.00146.62           C
ANISOU 2750  CG  TRP D 227    17020  18891  19796   -910   -297  -2857       C
ATOM   2751  CD1 TRP D 227     -10.057 -93.483  -8.918  1.00145.10           C
ANISOU 2751  CD1 TRP D 227    16823  18709  19598   -938   -273  -2904       C
ATOM   2752  CD2 TRP D 227      -9.748 -91.263  -8.926  1.00147.87           C
ANISOU 2752  CD2 TRP D 227    17294  19035  19856   -930   -355  -2834       C
ATOM   2753  NE1 TRP D 227     -10.179 -93.057 -10.223  1.00 86.01           N
ANISOU 2753  NE1 TRP D 227     9448  11218  12014   -974   -311  -2914       N
ATOM   2754  CE2 TRP D 227      -9.995 -91.705 -10.253  1.00129.56           C
ANISOU 2754  CE2 TRP D 227    15034  16720  17473   -970   -360  -2870       C
ATOM   2755  CE3 TRP D 227      -9.526 -89.907  -8.683  1.00 94.93           C
ANISOU 2755  CE3 TRP D 227    10648  12312  13110   -917   -405  -2787       C
ATOM   2756  CZ2 TRP D 227     -10.017 -90.827 -11.327  1.00113.24           C
ANISOU 2756  CZ2 TRP D 227    13078  14645  15305   -999   -410  -2859       C
ATOM   2757  CZ3 TRP D 227      -9.551 -89.040  -9.757  1.00125.97           C
ANISOU 2757  CZ3 TRP D 227    14688  16233  16942   -947   -457  -2775       C
ATOM   2758  CH2 TRP D 227      -9.793 -89.504 -11.064  1.00135.69           C
ANISOU 2758  CH2 TRP D 227    15970  17472  18113   -988   -458  -2810       C
ATOM   2759  N   ASN D 228     -10.883 -93.198  -3.540  1.00124.31           N
ANISOU 2759  N   ASN D 228    13828  16114  17290   -718   -295  -2818       N
ATOM   2760  CA  ASN D 228     -10.603 -93.714  -2.208  1.00113.53           C
ANISOU 2760  CA  ASN D 228    12340  14767  16030   -686   -242  -2807       C
ATOM   2761  C   ASN D 228     -11.420 -94.954  -1.829  1.00111.33           C
ANISOU 2761  C   ASN D 228    11940  14522  15837   -655   -240  -2836       C
ATOM   2762  O   ASN D 228     -10.895 -95.909  -1.268  1.00132.35           O
ANISOU 2762  O   ASN D 228    14505  17201  18582   -669   -160  -2847       O
ATOM   2763  CB  ASN D 228     -10.762 -92.609  -1.165  1.00115.25           C
ANISOU 2763  CB  ASN D 228    12556  14977  16254   -625   -294  -2765       C
ATOM   2764  CG  ASN D 228      -9.719 -91.508  -1.314  1.00133.96           C
ANISOU 2764  CG  ASN D 228    15027  17312  18561   -661   -282  -2730       C
ATOM   2765  OD1 ASN D 228     -10.062 -90.338  -1.512  1.00117.13           O
ANISOU 2765  OD1 ASN D 228    12983  15161  16362   -638   -362  -2707       O
ATOM   2766  ND2 ASN D 228      -8.434 -91.878  -1.210  1.00113.70           N
ANISOU 2766  ND2 ASN D 228    12447  14739  16017   -718   -183  -2721       N
ATOM   2767  N   HIS D 229     -12.706 -94.956  -2.148  1.00129.08           N
ANISOU 2767  N   HIS D 229    14191  16782  18069   -615   -329  -2844       N
ATOM   2768  CA  HIS D 229     -13.556 -96.065  -1.721  1.00154.52           C
ANISOU 2768  CA  HIS D 229    17294  20039  21376   -580   -341  -2861       C
ATOM   2769  C   HIS D 229     -13.690 -97.166  -2.771  1.00122.35           C
ANISOU 2769  C   HIS D 229    13228  15965  17295   -632   -321  -2906       C
ATOM   2770  O   HIS D 229     -14.478 -98.095  -2.589  1.00 98.04           O
ANISOU 2770  O   HIS D 229    10062  12911  14279   -608   -344  -2919       O
ATOM   2771  CB  HIS D 229     -14.941 -95.560  -1.282  1.00159.85           C
ANISOU 2771  CB  HIS D 229    17948  20734  22056   -497   -450  -2834       C
ATOM   2772  CG  HIS D 229     -14.923 -94.183  -0.713  1.00138.09           C
ANISOU 2772  CG  HIS D 229    15243  17965  19261   -450   -493  -2795       C
ATOM   2773  ND1 HIS D 229     -15.210 -93.071  -1.468  1.00137.04           N
ANISOU 2773  ND1 HIS D 229    15236  17806  19027   -454   -561  -2782       N
ATOM   2774  CD2 HIS D 229     -14.617 -93.722   0.534  1.00 88.79           C
ANISOU 2774  CD2 HIS D 229     8946  11728  13064   -401   -480  -2765       C
ATOM   2775  CE1 HIS D 229     -15.097 -91.985  -0.721  1.00135.58           C
ANISOU 2775  CE1 HIS D 229    15076  17611  18829   -407   -590  -2747       C
ATOM   2776  NE2 HIS D 229     -14.735 -92.359   0.494  1.00104.35           N
ANISOU 2776  NE2 HIS D 229    11015  13673  14959   -374   -542  -2737       N
ATOM   2777  N   SER D 230     -12.933 -97.058  -3.863  1.00139.10           N
ANISOU 2777  N   SER D 230    15453  18059  19338   -701   -282  -2926       N
ATOM   2778  CA  SER D 230     -13.145 -97.928  -5.021  1.00131.62           C
ANISOU 2778  CA  SER D 230    14541  17108  18362   -748   -278  -2970       C
ATOM   2779  C   SER D 230     -12.150 -99.054  -5.082  1.00120.26           C
ANISOU 2779  C   SER D 230    13055  15668  16969   -798   -167  -3002       C
ATOM   2780  O   SER D 230     -11.007 -98.880  -5.488  1.00146.44           O
ANISOU 2780  O   SER D 230    16430  18966  20243   -848    -93  -3003       O
ATOM   2781  CB  SER D 230     -13.006 -97.122  -6.296  1.00115.03           C
ANISOU 2781  CB  SER D 230    12589  14980  16138   -789   -308  -2975       C
ATOM   2782  OG  SER D 230     -11.681 -96.642  -6.405  1.00119.10           O
ANISOU 2782  OG  SER D 230    13158  15477  16616   -832   -233  -2963       O
ATOM   2783  N   VAL D 231     -12.625-100.230  -4.733  1.00110.58           N
ANISOU 2783  N   VAL D 231    11724  14463  15829   -784   -161  -3024       N
ATOM   2784  CA  VAL D 231     -11.772-101.385  -4.601  1.00126.10           C
ANISOU 2784  CA  VAL D 231    13623  16433  17858   -823    -57  -3052       C
ATOM   2785  C   VAL D 231     -12.597-102.531  -5.128  1.00 98.39           C
ANISOU 2785  C   VAL D 231    10079  12929  14376   -827    -93  -3091       C
ATOM   2786  O   VAL D 231     -13.730-102.723  -4.713  1.00108.80           O
ANISOU 2786  O   VAL D 231    11331  14267  15740   -779   -173  -3080       O
ATOM   2787  CB  VAL D 231     -11.335-101.600  -3.125  1.00 99.72           C
ANISOU 2787  CB  VAL D 231    10148  13114  14626   -793     -1  -3026       C
ATOM   2788  CG1 VAL D 231     -10.593-102.900  -2.962  1.00 90.63           C
ANISOU 2788  CG1 VAL D 231     8913  11971  13552   -831    101  -3054       C
ATOM   2789  CG2 VAL D 231     -10.472-100.449  -2.672  1.00 77.89           C
ANISOU 2789  CG2 VAL D 231     7430  10337  11827   -795     31  -2985       C
ATOM   2790  N   GLY D 232     -12.032-103.285  -6.056  1.00131.12           N
ANISOU 2790  N   GLY D 232    14272  17056  18490   -883    -37  -3134       N
ATOM   2791  CA  GLY D 232     -12.808-104.273  -6.776  1.00147.25           C
ANISOU 2791  CA  GLY D 232    16314  19096  20538   -893    -81  -3174       C
ATOM   2792  C   GLY D 232     -13.898-103.590  -7.579  1.00131.77           C
ANISOU 2792  C   GLY D 232    14448  17126  18494   -880   -197  -3168       C
ATOM   2793  O   GLY D 232     -14.883-104.218  -7.971  1.00120.22           O
ANISOU 2793  O   GLY D 232    12972  15664  17042   -873   -267  -3184       O
ATOM   2794  N   PHE D 233     -13.730-102.288  -7.798  1.00130.32           N
ANISOU 2794  N   PHE D 233    14355  16933  18228   -878   -219  -3140       N
ATOM   2795  CA  PHE D 233     -14.586-101.558  -8.719  1.00123.32           C
ANISOU 2795  CA  PHE D 233    13574  16034  17247   -877   -316  -3135       C
ATOM   2796  C   PHE D 233     -14.090-101.771 -10.148  1.00128.04           C
ANISOU 2796  C   PHE D 233    14292  16607  17751   -940   -287  -3177       C
ATOM   2797  O   PHE D 233     -12.883-101.694 -10.415  1.00106.05           O
ANISOU 2797  O   PHE D 233    11549  13812  14932   -978   -197  -3186       O
ATOM   2798  CB  PHE D 233     -14.647-100.081  -8.345  1.00109.19           C
ANISOU 2798  CB  PHE D 233    11828  14245  15413   -846   -356  -3087       C
ATOM   2799  CG  PHE D 233     -15.718 -99.772  -7.356  1.00114.98           C
ANISOU 2799  CG  PHE D 233    12480  15003  16205   -774   -435  -3047       C
ATOM   2800  CD1 PHE D 233     -15.782-100.462  -6.157  1.00119.03           C
ANISOU 2800  CD1 PHE D 233    12851  15541  16832   -735   -409  -3037       C
ATOM   2801  CD2 PHE D 233     -16.678 -98.804  -7.621  1.00118.30           C
ANISOU 2801  CD2 PHE D 233    12960  15422  16567   -744   -536  -3018       C
ATOM   2802  CE1 PHE D 233     -16.790-100.188  -5.234  1.00137.18           C
ANISOU 2802  CE1 PHE D 233    15071  17867  19185   -663   -482  -2997       C
ATOM   2803  CE2 PHE D 233     -17.687 -98.523  -6.691  1.00118.94           C
ANISOU 2803  CE2 PHE D 233    12964  15527  16699   -670   -608  -2976       C
ATOM   2804  CZ  PHE D 233     -17.741 -99.214  -5.504  1.00114.64           C
ANISOU 2804  CZ  PHE D 233    12281  15011  16267   -628   -581  -2965       C
ATOM   2805  N   ASP D 234     -15.022-102.106 -11.040  1.00122.64           N
ANISOU 2805  N   ASP D 234    13656  15914  17026   -950   -362  -3199       N
ATOM   2806  CA  ASP D 234     -14.683-102.472 -12.406  1.00 95.96           C
ANISOU 2806  CA  ASP D 234    10384  12513  13562  -1006   -342  -3244       C
ATOM   2807  C   ASP D 234     -14.873-101.409 -13.492  1.00 99.70           C
ANISOU 2807  C   ASP D 234    10995  12974  13912  -1029   -395  -3236       C
ATOM   2808  O   ASP D 234     -14.481-101.636 -14.629  1.00105.02           O
ANISOU 2808  O   ASP D 234    11762  13633  14509  -1074   -371  -3272       O
ATOM   2809  CB  ASP D 234     -15.435-103.741 -12.795  1.00101.14           C
ANISOU 2809  CB  ASP D 234    11011  13163  14255  -1014   -379  -3283       C
ATOM   2810  CG  ASP D 234     -16.941-103.593 -12.644  1.00122.06           C
ANISOU 2810  CG  ASP D 234    13632  15822  16923   -977   -504  -3254       C
ATOM   2811  OD1 ASP D 234     -17.376-102.799 -11.774  1.00111.15           O
ANISOU 2811  OD1 ASP D 234    12201  14459  15571   -929   -544  -3204       O
ATOM   2812  OD2 ASP D 234     -17.684-104.275 -13.390  1.00110.88           O
ANISOU 2812  OD2 ASP D 234    12244  14392  15491   -995   -562  -3279       O
ATOM   2813  N   TYR D 235     -15.438-100.252 -13.173  1.00 74.15           N
ANISOU 2813  N   TYR D 235     7774   9745  10654   -997   -464  -3190       N
ATOM   2814  CA  TYR D 235     -15.709 -99.281 -14.237  1.00109.80           C
ANISOU 2814  CA  TYR D 235    12414  14250  15055  -1021   -521  -3182       C
ATOM   2815  C   TYR D 235     -15.371 -97.830 -13.892  1.00111.81           C
ANISOU 2815  C   TYR D 235    12706  14508  15271  -1004   -532  -3135       C
ATOM   2816  O   TYR D 235     -15.632 -97.380 -12.782  1.00121.13           O
ANISOU 2816  O   TYR D 235    13816  15699  16510   -955   -552  -3097       O
ATOM   2817  CB  TYR D 235     -17.176 -99.380 -14.697  1.00107.68           C
ANISOU 2817  CB  TYR D 235    12160  13981  14772  -1009   -634  -3179       C
ATOM   2818  CG  TYR D 235     -17.477-100.451 -15.753  1.00 96.43           C
ANISOU 2818  CG  TYR D 235    10778  12542  13321  -1051   -645  -3229       C
ATOM   2819  CD1 TYR D 235     -17.691-101.775 -15.390  1.00115.28           C
ANISOU 2819  CD1 TYR D 235    13081  14928  15791  -1044   -631  -3256       C
ATOM   2820  CD2 TYR D 235     -17.556-100.126 -17.105  1.00100.50           C
ANISOU 2820  CD2 TYR D 235    11417  13043  13727  -1095   -673  -3249       C
ATOM   2821  CE1 TYR D 235     -17.966-102.743 -16.337  1.00142.20           C
ANISOU 2821  CE1 TYR D 235    16534  18320  19176  -1080   -646  -3303       C
ATOM   2822  CE2 TYR D 235     -17.827-101.084 -18.058  1.00112.55           C
ANISOU 2822  CE2 TYR D 235    12987  14553  15225  -1131   -686  -3296       C
ATOM   2823  CZ  TYR D 235     -18.038-102.397 -17.675  1.00123.43           C
ANISOU 2823  CZ  TYR D 235    14286  15927  16686  -1123   -674  -3324       C
ATOM   2824  OH  TYR D 235     -18.323-103.369 -18.630  1.00 83.93           O
ANISOU 2824  OH  TYR D 235     9333  10903  11655  -1159   -693  -3371       O
ATOM   2825  N   VAL D 236     -14.802 -97.102 -14.852  1.00 88.42           N
ANISOU 2825  N   VAL D 236     9853  11535  12208  -1045   -521  -3135       N
ATOM   2826  CA  VAL D 236     -14.501 -95.682 -14.671  1.00 90.15           C
ANISOU 2826  CA  VAL D 236    10119  11753  12381  -1035   -543  -3089       C
ATOM   2827  C   VAL D 236     -15.717 -94.818 -15.017  1.00123.69           C
ANISOU 2827  C   VAL D 236    14414  16002  16583  -1016   -658  -3064       C
ATOM   2828  O   VAL D 236     -16.180 -94.845 -16.156  1.00138.68           O
ANISOU 2828  O   VAL D 236    16387  17894  18409  -1050   -700  -3083       O
ATOM   2829  CB  VAL D 236     -13.357 -95.264 -15.591  1.00 98.79           C
ANISOU 2829  CB  VAL D 236    11308  12840  13388  -1087   -485  -3094       C
ATOM   2830  CG1 VAL D 236     -13.112 -93.762 -15.476  1.00113.69           C
ANISOU 2830  CG1 VAL D 236    13248  14725  15225  -1080   -522  -3043       C
ATOM   2831  CG2 VAL D 236     -12.095 -96.067 -15.278  1.00 62.19           C
ANISOU 2831  CG2 VAL D 236     6631   8206   8792  -1107   -366  -3110       C
ATOM   2832  N   TYR D 237     -16.238 -94.046 -14.060  1.00108.24           N
ANISOU 2832  N   TYR D 237    12415  14050  14662   -962   -710  -3021       N
ATOM   2833  CA  TYR D 237     -17.591 -93.499 -14.255  1.00130.38           C
ANISOU 2833  CA  TYR D 237    15240  16858  17442   -935   -819  -2996       C
ATOM   2834  C   TYR D 237     -17.788 -92.306 -15.174  1.00142.46           C
ANISOU 2834  C   TYR D 237    16880  18379  18869   -959   -879  -2976       C
ATOM   2835  O   TYR D 237     -18.647 -92.350 -16.054  1.00184.66           O
ANISOU 2835  O   TYR D 237    22272  23723  24166   -979   -941  -2983       O
ATOM   2836  CB  TYR D 237     -18.339 -93.242 -12.949  1.00 98.82           C
ANISOU 2836  CB  TYR D 237    11153  12874  13521   -859   -865  -2957       C
ATOM   2837  CG  TYR D 237     -19.708 -92.631 -13.205  1.00118.26           C
ANISOU 2837  CG  TYR D 237    13643  15341  15951   -830   -975  -2925       C
ATOM   2838  CD1 TYR D 237     -20.720 -93.374 -13.785  1.00101.40           C
ANISOU 2838  CD1 TYR D 237    11502  13210  13816   -840  -1027  -2936       C
ATOM   2839  CD2 TYR D 237     -19.973 -91.301 -12.892  1.00149.96           C
ANISOU 2839  CD2 TYR D 237    17694  19353  19933   -794  -1029  -2880       C
ATOM   2840  CE1 TYR D 237     -21.961 -92.818 -14.034  1.00133.50           C
ANISOU 2840  CE1 TYR D 237    15593  17281  17851   -817  -1126  -2899       C
ATOM   2841  CE2 TYR D 237     -21.210 -90.738 -13.136  1.00127.18           C
ANISOU 2841  CE2 TYR D 237    14834  16473  17016   -768  -1126  -2847       C
ATOM   2842  CZ  TYR D 237     -22.200 -91.500 -13.706  1.00131.94           C
ANISOU 2842  CZ  TYR D 237    15427  17084  17622   -780  -1172  -2854       C
ATOM   2843  OH  TYR D 237     -23.437 -90.944 -13.945  1.00131.87           O
ANISOU 2843  OH  TYR D 237    15442  17080  17582   -756  -1267  -2814       O
ATOM   2844  N   ASN D 238     -17.042 -91.233 -14.978  1.00 72.45           N
ANISOU 2844  N   ASN D 238     8052   9505   9969   -959   -865  -2948       N
ATOM   2845  CA  ASN D 238     -17.255 -90.090 -15.859  1.00 76.44           C
ANISOU 2845  CA  ASN D 238     8658  10005  10381   -983   -926  -2927       C
ATOM   2846  C   ASN D 238     -15.918 -89.549 -16.240  1.00 94.58           C
ANISOU 2846  C   ASN D 238    11014  12295  12627  -1024   -867  -2923       C
ATOM   2847  O   ASN D 238     -15.537 -88.453 -15.839  1.00135.59           O
ANISOU 2847  O   ASN D 238    16232  17482  17806  -1009   -884  -2884       O
ATOM   2848  CB  ASN D 238     -18.119 -89.003 -15.202  1.00137.72           C
ANISOU 2848  CB  ASN D 238    16413  17765  18147   -926  -1012  -2878       C
ATOM   2849  CG  ASN D 238     -19.569 -89.013 -15.696  1.00128.96           C
ANISOU 2849  CG  ASN D 238    15318  16663  17017   -915  -1103  -2870       C
ATOM   2850  OD1 ASN D 238     -19.885 -89.634 -16.711  1.00115.94           O
ANISOU 2850  OD1 ASN D 238    13704  15016  15333   -961  -1110  -2899       O
ATOM   2851  ND2 ASN D 238     -20.451 -88.314 -14.979  1.00104.82           N
ANISOU 2851  ND2 ASN D 238    12236  13610  13982   -853  -1173  -2827       N
ATOM   2852  N   PRO D 239     -15.175 -90.338 -17.002  1.00 97.03           N
ANISOU 2852  N   PRO D 239    11347  12607  12911  -1075   -797  -2960       N
ATOM   2853  CA  PRO D 239     -13.824 -89.923 -17.357  1.00116.74           C
ANISOU 2853  CA  PRO D 239    13893  15101  15362  -1113   -733  -2949       C
ATOM   2854  C   PRO D 239     -13.919 -88.745 -18.302  1.00108.41           C
ANISOU 2854  C   PRO D 239    12934  14045  14210  -1142   -795  -2924       C
ATOM   2855  O   PRO D 239     -14.900 -88.603 -19.020  1.00133.54           O
ANISOU 2855  O   PRO D 239    16156  17231  17352  -1150   -865  -2933       O
ATOM   2856  CB  PRO D 239     -13.266 -91.143 -18.079  1.00 74.76           C
ANISOU 2856  CB  PRO D 239     8582   9790  10035  -1155   -654  -2999       C
ATOM   2857  CG  PRO D 239     -14.475 -91.744 -18.710  1.00 86.33           C
ANISOU 2857  CG  PRO D 239    10057  11257  11489  -1158   -714  -3032       C
ATOM   2858  CD  PRO D 239     -15.609 -91.526 -17.746  1.00 73.79           C
ANISOU 2858  CD  PRO D 239     8404   9667   9964  -1101   -787  -3009       C
ATOM   2859  N   PHE D 240     -12.908 -87.893 -18.277  1.00116.40           N
ANISOU 2859  N   PHE D 240    13982  15054  15191  -1157   -771  -2888       N
ATOM   2860  CA  PHE D 240     -12.795 -86.807 -19.226  1.00103.91           C
ANISOU 2860  CA  PHE D 240    12489  13475  13517  -1190   -821  -2861       C
ATOM   2861  C   PHE D 240     -11.554 -87.133 -20.024  1.00139.61           C
ANISOU 2861  C   PHE D 240    17049  18007  17988  -1241   -740  -2868       C
ATOM   2862  O   PHE D 240     -10.710 -87.938 -19.602  1.00122.68           O
ANISOU 2862  O   PHE D 240    14863  15864  15887  -1243   -649  -2880       O
ATOM   2863  CB  PHE D 240     -12.612 -85.461 -18.533  1.00116.13           C
ANISOU 2863  CB  PHE D 240    14048  15009  15067  -1164   -870  -2804       C
ATOM   2864  CG  PHE D 240     -13.732 -85.088 -17.621  1.00134.99           C
ANISOU 2864  CG  PHE D 240    16395  17387  17505  -1104   -943  -2792       C
ATOM   2865  CD1 PHE D 240     -13.901 -85.732 -16.406  1.00117.97           C
ANISOU 2865  CD1 PHE D 240    14153  15229  15442  -1055   -913  -2800       C
ATOM   2866  CD2 PHE D 240     -14.606 -84.073 -17.969  1.00157.41           C
ANISOU 2866  CD2 PHE D 240    19284  20225  20301  -1095  -1040  -2768       C
ATOM   2867  CE1 PHE D 240     -14.933 -85.385 -15.572  1.00127.18           C
ANISOU 2867  CE1 PHE D 240    15281  16391  16651   -993   -980  -2784       C
ATOM   2868  CE2 PHE D 240     -15.644 -83.717 -17.126  1.00150.44           C
ANISOU 2868  CE2 PHE D 240    18365  19334  19460  -1033  -1106  -2752       C
ATOM   2869  CZ  PHE D 240     -15.805 -84.376 -15.929  1.00126.34           C
ANISOU 2869  CZ  PHE D 240    15226  16281  16496   -981  -1076  -2759       C
ATOM   2870  N   MET D 241     -11.462 -86.542 -21.202  1.00152.34           N
ANISOU 2870  N   MET D 241    18742  19631  19511  -1282   -771  -2859       N
ATOM   2871  CA  MET D 241     -10.331 -86.808 -22.057  1.00133.18           C
ANISOU 2871  CA  MET D 241    16356  17220  17026  -1326   -699  -2861       C
ATOM   2872  C   MET D 241     -10.131 -85.641 -22.995  1.00153.11           C
ANISOU 2872  C   MET D 241    18958  19756  19460  -1359   -752  -2822       C
ATOM   2873  O   MET D 241     -11.026 -84.787 -23.150  1.00118.79           O
ANISOU 2873  O   MET D 241    14638  15406  15092  -1353   -846  -2807       O
ATOM   2874  CB  MET D 241     -10.563 -88.097 -22.836  1.00123.05           C
ANISOU 2874  CB  MET D 241    15079  15946  15726  -1346   -656  -2924       C
ATOM   2875  CG  MET D 241     -11.917 -88.145 -23.527  1.00154.79           C
ANISOU 2875  CG  MET D 241    19131  19967  19717  -1352   -739  -2955       C
ATOM   2876  SD  MET D 241     -12.745 -89.740 -23.365  1.00120.69           S
ANISOU 2876  SD  MET D 241    14760  15639  15457  -1337   -721  -3022       S
ATOM   2877  CE  MET D 241     -13.716 -89.445 -21.891  1.00167.38           C
ANISOU 2877  CE  MET D 241    20591  21537  21469  -1276   -781  -2998       C
ATOM   2878  N   ILE D 242      -8.947 -85.589 -23.598  1.00168.83           N
ANISOU 2878  N   ILE D 242    20983  21764  21400  -1393   -692  -2801       N
ATOM   2879  CA  ILE D 242      -8.671 -84.571 -24.592  1.00164.87           C
ANISOU 2879  CA  ILE D 242    20551  21281  20811  -1428   -737  -2762       C
ATOM   2880  C   ILE D 242      -7.801 -85.154 -25.705  1.00164.68           C
ANISOU 2880  C   ILE D 242    20566  21286  20717  -1466   -664  -2775       C
ATOM   2881  O   ILE D 242      -6.855 -85.913 -25.425  1.00146.91           O
ANISOU 2881  O   ILE D 242    18290  19040  18490  -1464   -568  -2777       O
ATOM   2882  CB  ILE D 242      -8.032 -83.319 -23.941  1.00126.12           C
ANISOU 2882  CB  ILE D 242    15644  16363  15912  -1420   -769  -2687       C
ATOM   2883  CG1 ILE D 242      -8.153 -82.112 -24.875  1.00158.15           C
ANISOU 2883  CG1 ILE D 242    19766  20435  19888  -1450   -849  -2648       C
ATOM   2884  CG2 ILE D 242      -6.580 -83.598 -23.526  1.00 79.01           C
ANISOU 2884  CG2 ILE D 242     9656  10400   9964  -1427   -674  -2652       C
ATOM   2885  CD1 ILE D 242      -9.440 -82.089 -25.694  1.00161.00           C
ANISOU 2885  CD1 ILE D 242    20159  20803  20210  -1460   -920  -2688       C
ATOM   2886  N   ASP D 243      -8.148 -84.833 -26.956  1.00150.95           N
ANISOU 2886  N   ASP D 243    18890  19571  18894  -1497   -708  -2783       N
ATOM   2887  CA  ASP D 243      -7.337 -85.248 -28.094  1.00172.48           C
ANISOU 2887  CA  ASP D 243    21661  22330  21542  -1530   -647  -2789       C
ATOM   2888  C   ASP D 243      -6.285 -84.199 -28.396  1.00173.17           C
ANISOU 2888  C   ASP D 243    21776  22439  21580  -1550   -649  -2711       C
ATOM   2889  O   ASP D 243      -6.616 -83.031 -28.636  1.00173.96           O
ANISOU 2889  O   ASP D 243    21903  22544  21651  -1562   -736  -2671       O
ATOM   2890  CB  ASP D 243      -8.191 -85.487 -29.338  1.00177.00           C
ANISOU 2890  CB  ASP D 243    22288  22920  22046  -1555   -690  -2836       C
ATOM   2891  CG  ASP D 243      -7.361 -85.953 -30.532  1.00190.70           C
ANISOU 2891  CG  ASP D 243    24071  24690  23695  -1583   -625  -2846       C
ATOM   2892  OD1 ASP D 243      -6.507 -86.856 -30.361  1.00180.56           O
ANISOU 2892  OD1 ASP D 243    22769  23409  22425  -1573   -527  -2860       O
ATOM   2893  OD2 ASP D 243      -7.557 -85.411 -31.643  1.00203.89           O
ANISOU 2893  OD2 ASP D 243    25797  26388  25284  -1612   -672  -2838       O
ATOM   2894  N   VAL D 244      -5.022 -84.621 -28.387  1.00153.36           N
ANISOU 2894  N   VAL D 244    19260  19946  19063  -1554   -555  -2685       N
ATOM   2895  CA  VAL D 244      -3.911 -83.695 -28.575  1.00182.56           C
ANISOU 2895  CA  VAL D 244    22977  23667  22722  -1572   -552  -2600       C
ATOM   2896  C   VAL D 244      -3.810 -83.207 -30.026  1.00220.64           C
ANISOU 2896  C   VAL D 244    27862  28533  27439  -1605   -583  -2583       C
ATOM   2897  O   VAL D 244      -3.281 -82.123 -30.294  1.00233.84           O
ANISOU 2897  O   VAL D 244    29553  30223  29073  -1623   -625  -2509       O
ATOM   2898  CB  VAL D 244      -2.569 -84.330 -28.148  1.00179.00           C
ANISOU 2898  CB  VAL D 244    22497  23223  22294  -1566   -437  -2569       C
ATOM   2899  CG1 VAL D 244      -1.862 -83.465 -27.105  1.00176.75           C
ANISOU 2899  CG1 VAL D 244    22180  22918  22057  -1560   -449  -2487       C
ATOM   2900  CG2 VAL D 244      -2.791 -85.743 -27.614  1.00169.54           C
ANISOU 2900  CG2 VAL D 244    21257  22005  21156  -1544   -360  -2641       C
ATOM   2901  N   GLN D 245      -4.324 -84.004 -30.956  1.00213.78           N
ANISOU 2901  N   GLN D 245    27023  27680  26523  -1614   -567  -2650       N
ATOM   2902  CA  GLN D 245      -4.211 -83.688 -32.372  1.00182.76           C
ANISOU 2902  CA  GLN D 245    23152  23796  22491  -1645   -587  -2642       C
ATOM   2903  C   GLN D 245      -5.237 -82.650 -32.825  1.00190.38           C
ANISOU 2903  C   GLN D 245    24144  24762  23428  -1664   -707  -2635       C
ATOM   2904  O   GLN D 245      -5.095 -82.072 -33.900  1.00209.79           O
ANISOU 2904  O   GLN D 245    26644  27261  25807  -1693   -739  -2608       O
ATOM   2905  CB  GLN D 245      -4.350 -84.962 -33.213  1.00179.29           C
ANISOU 2905  CB  GLN D 245    22742  23371  22008  -1646   -524  -2718       C
ATOM   2906  CG  GLN D 245      -3.764 -84.858 -34.614  1.00183.18           C
ANISOU 2906  CG  GLN D 245    23290  23918  22391  -1669   -504  -2701       C
ATOM   2907  CD  GLN D 245      -4.478 -85.746 -35.615  1.00176.77           C
ANISOU 2907  CD  GLN D 245    22525  23115  21526  -1678   -500  -2785       C
ATOM   2908  OE1 GLN D 245      -5.704 -85.692 -35.740  1.00153.85           O
ANISOU 2908  OE1 GLN D 245    19632  20191  18632  -1688   -574  -2830       O
ATOM   2909  NE2 GLN D 245      -3.714 -86.571 -36.333  1.00168.72           N
ANISOU 2909  NE2 GLN D 245    21534  22124  20447  -1673   -413  -2804       N
ATOM   2910  N   GLN D 246      -6.265 -82.410 -32.013  1.00197.22           N
ANISOU 2910  N   GLN D 246    24985  25589  24361  -1648   -771  -2656       N
ATOM   2911  CA  GLN D 246      -7.342 -81.491 -32.401  1.00198.54           C
ANISOU 2911  CA  GLN D 246    25176  25755  24506  -1665   -882  -2652       C
ATOM   2912  C   GLN D 246      -6.946 -80.008 -32.346  1.00198.87           C
ANISOU 2912  C   GLN D 246    25224  25805  24531  -1677   -950  -2567       C
ATOM   2913  O   GLN D 246      -7.681 -79.145 -32.835  1.00181.86           O
ANISOU 2913  O   GLN D 246    23094  23659  22348  -1697  -1041  -2554       O
ATOM   2914  CB  GLN D 246      -8.626 -81.753 -31.599  1.00184.22           C
ANISOU 2914  CB  GLN D 246    23333  23898  22763  -1639   -929  -2698       C
ATOM   2915  CG  GLN D 246      -9.286 -83.103 -31.896  1.00158.54           C
ANISOU 2915  CG  GLN D 246    20084  20639  19516  -1636   -891  -2781       C
ATOM   2916  CD  GLN D 246     -10.736 -83.176 -31.434  1.00162.72           C
ANISOU 2916  CD  GLN D 246    20595  21137  20095  -1620   -962  -2815       C
ATOM   2917  OE1 GLN D 246     -11.375 -82.152 -31.180  1.00185.32           O
ANISOU 2917  OE1 GLN D 246    23456  23990  22967  -1618  -1046  -2781       O
ATOM   2918  NE2 GLN D 246     -11.262 -84.393 -31.329  1.00129.05           N
ANISOU 2918  NE2 GLN D 246    16316  16858  15861  -1608   -929  -2879       N
ATOM   2919  N   TRP D 247      -5.807 -79.715 -31.723  1.00207.84           N
ANISOU 2919  N   TRP D 247    26338  26940  25691  -1668   -911  -2507       N
ATOM   2920  CA  TRP D 247      -5.186 -78.400 -31.855  1.00208.64           C
ANISOU 2920  CA  TRP D 247    26451  27056  25765  -1685   -967  -2419       C
ATOM   2921  C   TRP D 247      -4.389 -78.368 -33.150  1.00209.67           C
ANISOU 2921  C   TRP D 247    26616  27246  25804  -1718   -937  -2388       C
ATOM   2922  O   TRP D 247      -4.247 -77.321 -33.784  1.00201.79           O
ANISOU 2922  O   TRP D 247    25639  26275  24756  -1744  -1004  -2332       O
ATOM   2923  CB  TRP D 247      -4.276 -78.101 -30.670  1.00216.17           C
ANISOU 2923  CB  TRP D 247    27370  27983  26780  -1664   -941  -2360       C
ATOM   2924  CG  TRP D 247      -4.964 -78.251 -29.356  1.00229.34           C
ANISOU 2924  CG  TRP D 247    29002  29598  28539  -1627   -958  -2391       C
ATOM   2925  CD1 TRP D 247      -6.123 -77.644 -28.962  1.00220.94           C
ANISOU 2925  CD1 TRP D 247    27937  28505  27504  -1612  -1049  -2408       C
ATOM   2926  CD2 TRP D 247      -4.533 -79.055 -28.248  1.00227.70           C
ANISOU 2926  CD2 TRP D 247    28748  29363  28406  -1596   -880  -2405       C
ATOM   2927  NE1 TRP D 247      -6.444 -78.026 -27.680  1.00212.18           N
ANISOU 2927  NE1 TRP D 247    26785  27354  26480  -1570  -1033  -2432       N
ATOM   2928  CE2 TRP D 247      -5.486 -78.889 -27.219  1.00216.07           C
ANISOU 2928  CE2 TRP D 247    27247  27846  27003  -1562   -931  -2432       C
ATOM   2929  CE3 TRP D 247      -3.438 -79.898 -28.028  1.00200.44           C
ANISOU 2929  CE3 TRP D 247    25273  25919  24965  -1594   -770  -2396       C
ATOM   2930  CZ2 TRP D 247      -5.372 -79.538 -25.986  1.00187.33           C
ANISOU 2930  CZ2 TRP D 247    23556  24175  23447  -1527   -878  -2450       C
ATOM   2931  CZ3 TRP D 247      -3.329 -80.540 -26.805  1.00165.01           C
ANISOU 2931  CZ3 TRP D 247    20735  21399  20564  -1563   -717  -2414       C
ATOM   2932  CH2 TRP D 247      -4.291 -80.357 -25.800  1.00164.81           C
ANISOU 2932  CH2 TRP D 247    20680  21332  20609  -1530   -771  -2442       C
ATOM   2933  N   GLY D 248      -3.863 -79.533 -33.521  1.00220.47           N
ANISOU 2933  N   GLY D 248    27987  28634  27149  -1713   -836  -2425       N
ATOM   2934  CA  GLY D 248      -3.185 -79.736 -34.791  1.00220.72           C
ANISOU 2934  CA  GLY D 248    28053  28723  27088  -1735   -795  -2410       C
ATOM   2935  C   GLY D 248      -1.670 -79.696 -34.709  1.00214.78           C
ANISOU 2935  C   GLY D 248    27288  27997  26320  -1732   -724  -2332       C
ATOM   2936  O   GLY D 248      -1.105 -78.921 -33.938  1.00218.41           O
ANISOU 2936  O   GLY D 248    27724  28442  26821  -1729   -748  -2257       O
ATOM   2937  N   PHE D 249      -1.016 -80.522 -35.526  1.00211.58           N
ANISOU 2937  N   PHE D 249    26903  27634  25854  -1731   -638  -2345       N
ATOM   2938  CA  PHE D 249       0.449 -80.622 -35.548  1.00201.75           C
ANISOU 2938  CA  PHE D 249    25648  26421  24586  -1725   -558  -2268       C
ATOM   2939  C   PHE D 249       0.985 -81.175 -36.865  1.00209.68           C
ANISOU 2939  C   PHE D 249    26690  27489  25492  -1729   -497  -2273       C
ATOM   2940  O   PHE D 249       0.238 -81.719 -37.685  1.00175.47           O
ANISOU 2940  O   PHE D 249    22391  23166  21112  -1733   -501  -2352       O
ATOM   2941  CB  PHE D 249       0.983 -81.454 -34.381  1.00203.32           C
ANISOU 2941  CB  PHE D 249    25806  26582  24863  -1698   -468  -2276       C
ATOM   2942  CG  PHE D 249       0.650 -80.887 -33.039  1.00225.73           C
ANISOU 2942  CG  PHE D 249    28606  29364  27796  -1690   -520  -2259       C
ATOM   2943  CD1 PHE D 249      -0.433 -81.368 -32.317  1.00227.66           C
ANISOU 2943  CD1 PHE D 249    28832  29559  28109  -1673   -538  -2342       C
ATOM   2944  CD2 PHE D 249       1.407 -79.861 -32.504  1.00219.53           C
ANISOU 2944  CD2 PHE D 249    27805  28576  27031  -1698   -555  -2156       C
ATOM   2945  CE1 PHE D 249      -0.748 -80.841 -31.087  1.00210.13           C
ANISOU 2945  CE1 PHE D 249    26577  27290  25971  -1660   -586  -2325       C
ATOM   2946  CE2 PHE D 249       1.094 -79.331 -31.271  1.00213.37           C
ANISOU 2946  CE2 PHE D 249    26995  27742  26334  -1688   -606  -2142       C
ATOM   2947  CZ  PHE D 249       0.015 -79.823 -30.563  1.00207.34           C
ANISOU 2947  CZ  PHE D 249    26212  26932  25635  -1666   -619  -2228       C
ATOM   2948  N   THR D 250       2.292 -81.028 -37.053  1.00235.60           N
ANISOU 2948  N   THR D 250    29966  30812  28740  -1726   -441  -2184       N
ATOM   2949  CA  THR D 250       2.928 -81.348 -38.323  1.00243.85           C
ANISOU 2949  CA  THR D 250    31044  31926  29682  -1725   -390  -2167       C
ATOM   2950  C   THR D 250       2.690 -82.784 -38.805  1.00221.53           C
ANISOU 2950  C   THR D 250    28246  29101  26825  -1704   -301  -2269       C
ATOM   2951  O   THR D 250       2.461 -83.004 -39.993  1.00237.09           O
ANISOU 2951  O   THR D 250    30260  31113  28710  -1708   -303  -2304       O
ATOM   2952  CB  THR D 250       4.456 -81.049 -38.295  1.00186.58           C
ANISOU 2952  CB  THR D 250    23772  24715  22405  -1719   -333  -2044       C
ATOM   2953  OG1 THR D 250       4.783 -80.281 -37.128  1.00166.28           O
ANISOU 2953  OG1 THR D 250    21161  22105  19914  -1726   -372  -1971       O
ATOM   2954  CG2 THR D 250       4.864 -80.274 -39.544  1.00183.90           C
ANISOU 2954  CG2 THR D 250    23456  24451  21967  -1735   -375  -1972       C
ATOM   2955  N   GLY D 251       2.740 -83.753 -37.895  1.00181.52           N
ANISOU 2955  N   GLY D 251    23155  23987  21827  -1681   -228  -2317       N
ATOM   2956  CA  GLY D 251       2.801 -85.151 -38.291  1.00154.69           C
ANISOU 2956  CA  GLY D 251    19781  20591  18401  -1657   -130  -2398       C
ATOM   2957  C   GLY D 251       2.590 -86.135 -37.157  1.00172.39           C
ANISOU 2957  C   GLY D 251    21989  22774  20739  -1637    -72  -2460       C
ATOM   2958  O   GLY D 251       2.027 -85.777 -36.121  1.00206.87           O
ANISOU 2958  O   GLY D 251    26317  27091  25193  -1642   -123  -2465       O
ATOM   2959  N   ASN D 252       3.021 -87.381 -37.361  1.00147.30           N
ANISOU 2959  N   ASN D 252    18824  19601  17544  -1612     34  -2507       N
ATOM   2960  CA  ASN D 252       2.885 -88.424 -36.339  1.00174.81           C
ANISOU 2960  CA  ASN D 252    22270  23031  21117  -1593     98  -2566       C
ATOM   2961  C   ASN D 252       3.549 -88.035 -35.015  1.00215.63           C
ANISOU 2961  C   ASN D 252    27375  28177  26377  -1591    121  -2491       C
ATOM   2962  O   ASN D 252       4.558 -87.330 -34.998  1.00233.64           O
ANISOU 2962  O   ASN D 252    29646  30489  28637  -1597    135  -2385       O
ATOM   2963  CB  ASN D 252       3.440 -89.761 -36.838  1.00146.76           C
ANISOU 2963  CB  ASN D 252    18744  19495  17524  -1566    215  -2614       C
ATOM   2964  CG  ASN D 252       4.953 -89.794 -36.854  1.00161.86           C
ANISOU 2964  CG  ASN D 252    20645  21449  19407  -1550    314  -2519       C
ATOM   2965  OD1 ASN D 252       5.597 -88.788 -37.135  1.00175.06           O
ANISOU 2965  OD1 ASN D 252    22316  23161  21036  -1562    287  -2418       O
ATOM   2966  ND2 ASN D 252       5.530 -90.952 -36.545  1.00167.95           N
ANISOU 2966  ND2 ASN D 252    21404  22210  20200  -1524    427  -2546       N
ATOM   2967  N   LEU D 253       2.975 -88.493 -33.907  1.00209.85           N
ANISOU 2967  N   LEU D 253    26598  27388  25746  -1584    121  -2542       N
ATOM   2968  CA  LEU D 253       3.437 -88.070 -32.591  1.00206.67           C
ANISOU 2968  CA  LEU D 253    26134  26957  25434  -1583    128  -2478       C
ATOM   2969  C   LEU D 253       4.890 -88.482 -32.282  1.00200.88           C
ANISOU 2969  C   LEU D 253    25376  26244  24705  -1573    246  -2405       C
ATOM   2970  O   LEU D 253       5.561 -87.826 -31.482  1.00222.30           O
ANISOU 2970  O   LEU D 253    28052  28950  27463  -1581    246  -2317       O
ATOM   2971  CB  LEU D 253       2.442 -88.497 -31.488  1.00189.40           C
ANISOU 2971  CB  LEU D 253    23901  24710  23353  -1574    101  -2551       C
ATOM   2972  CG  LEU D 253       2.268 -89.961 -31.063  1.00191.64           C
ANISOU 2972  CG  LEU D 253    24157  24966  23690  -1552    184  -2635       C
ATOM   2973  CD1 LEU D 253       2.505 -90.926 -32.232  1.00202.95           C
ANISOU 2973  CD1 LEU D 253    25643  26429  25039  -1544    252  -2686       C
ATOM   2974  CD2 LEU D 253       3.167 -90.303 -29.874  1.00174.29           C
ANISOU 2974  CD2 LEU D 253    21894  22751  21576  -1542    270  -2589       C
ATOM   2975  N   GLN D 254       5.378 -89.542 -32.926  1.00156.81           N
ANISOU 2975  N   GLN D 254    19819  20687  19075  -1556    345  -2439       N
ATOM   2976  CA  GLN D 254       6.758 -89.993 -32.715  1.00175.77           C
ANISOU 2976  CA  GLN D 254    22199  23111  21473  -1544    464  -2367       C
ATOM   2977  C   GLN D 254       7.774 -88.900 -33.051  1.00179.14           C
ANISOU 2977  C   GLN D 254    22635  23585  21846  -1557    450  -2233       C
ATOM   2978  O   GLN D 254       8.844 -88.823 -32.442  1.00150.53           O
ANISOU 2978  O   GLN D 254    18976  19968  18252  -1558    514  -2142       O
ATOM   2979  CB  GLN D 254       7.062 -91.251 -33.540  1.00197.08           C
ANISOU 2979  CB  GLN D 254    24936  25835  24113  -1519    564  -2427       C
ATOM   2980  CG  GLN D 254       8.522 -91.725 -33.480  1.00191.86           C
ANISOU 2980  CG  GLN D 254    24260  25205  23434  -1503    693  -2347       C
ATOM   2981  CD  GLN D 254       8.776 -92.762 -32.390  1.00182.48           C
ANISOU 2981  CD  GLN D 254    23015  23977  22344  -1491    787  -2378       C
ATOM   2982  OE1 GLN D 254       8.772 -92.447 -31.197  1.00157.59           O
ANISOU 2982  OE1 GLN D 254    19801  20788  19287  -1504    772  -2347       O
ATOM   2983  NE2 GLN D 254       9.004 -94.007 -32.800  1.00181.58           N
ANISOU 2983  NE2 GLN D 254    22919  23868  22204  -1465    884  -2439       N
ATOM   2984  N   SER D 255       7.448 -88.071 -34.037  1.00198.18           N
ANISOU 2984  N   SER D 255    25092  26031  24177  -1570    367  -2217       N
ATOM   2985  CA  SER D 255       8.280 -86.921 -34.366  1.00190.52           C
ANISOU 2985  CA  SER D 255    24127  25106  23158  -1585    332  -2088       C
ATOM   2986  C   SER D 255       8.142 -85.836 -33.305  1.00202.47           C
ANISOU 2986  C   SER D 255    25599  26580  24750  -1608    246  -2028       C
ATOM   2987  O   SER D 255       9.130 -85.409 -32.695  1.00199.90           O
ANISOU 2987  O   SER D 255    25243  26257  24452  -1615    272  -1920       O
ATOM   2988  CB  SER D 255       7.864 -86.332 -35.713  1.00165.99           C
ANISOU 2988  CB  SER D 255    21074  22046  19948  -1594    258  -2094       C
ATOM   2989  OG  SER D 255       6.628 -85.635 -35.611  1.00151.20           O
ANISOU 2989  OG  SER D 255    19207  20141  18102  -1615    135  -2145       O
ATOM   2990  N   ASN D 256       6.898 -85.419 -33.077  1.00187.48           N
ANISOU 2990  N   ASN D 256    23704  24643  22886  -1618    144  -2097       N
ATOM   2991  CA  ASN D 256       6.607 -84.276 -32.219  1.00174.25           C
ANISOU 2991  CA  ASN D 256    22002  22932  21272  -1636     45  -2047       C
ATOM   2992  C   ASN D 256       7.169 -84.429 -30.810  1.00184.61           C
ANISOU 2992  C   ASN D 256    23259  24202  22682  -1632     93  -2006       C
ATOM   2993  O   ASN D 256       7.753 -83.491 -30.266  1.00151.80           O
ANISOU 2993  O   ASN D 256    19087  20040  18550  -1647     54  -1906       O
ATOM   2994  CB  ASN D 256       5.106 -83.992 -32.187  1.00134.32           C
ANISOU 2994  CB  ASN D 256    16957  17840  16238  -1640    -58  -2139       C
ATOM   2995  CG  ASN D 256       4.540 -83.726 -33.571  1.00156.43           C
ANISOU 2995  CG  ASN D 256    19812  20682  18943  -1651   -114  -2171       C
ATOM   2996  OD1 ASN D 256       5.050 -84.239 -34.572  1.00151.83           O
ANISOU 2996  OD1 ASN D 256    19260  20148  18281  -1645    -52  -2171       O
ATOM   2997  ND2 ASN D 256       3.485 -82.918 -33.636  1.00157.84           N
ANISOU 2997  ND2 ASN D 256    20002  20843  19128  -1666   -230  -2197       N
ATOM   2998  N   HIS D 257       6.986 -85.601 -30.208  1.00197.17           N
ANISOU 2998  N   HIS D 257    24820  25763  24332  -1613    174  -2082       N
ATOM   2999  CA  HIS D 257       7.673 -85.873 -28.954  1.00173.39           C
ANISOU 2999  CA  HIS D 257    21753  22721  21407  -1610    239  -2038       C
ATOM   3000  C   HIS D 257       9.184 -85.921 -29.143  1.00191.21           C
ANISOU 3000  C   HIS D 257    24005  25017  23627  -1615    328  -1925       C
ATOM   3001  O   HIS D 257       9.905 -85.142 -28.526  1.00251.89           O
ANISOU 3001  O   HIS D 257    31670  32696  31340  -1632    309  -1819       O
ATOM   3002  CB  HIS D 257       7.225 -87.173 -28.289  1.00144.62           C
ANISOU 3002  CB  HIS D 257    18071  19042  17835  -1590    313  -2139       C
ATOM   3003  CG  HIS D 257       8.108 -87.588 -27.135  1.00171.61           C
ANISOU 3003  CG  HIS D 257    21430  22439  21334  -1588    401  -2088       C
ATOM   3004  ND1 HIS D 257       8.365 -86.728 -26.078  1.00179.62           N
ANISOU 3004  ND1 HIS D 257    22411  23423  22412  -1601    356  -2014       N
ATOM   3005  CD2 HIS D 257       8.786 -88.715 -26.893  1.00150.36           C
ANISOU 3005  CD2 HIS D 257    18710  19753  18668  -1578    528  -2096       C
ATOM   3006  CE1 HIS D 257       9.166 -87.344 -25.227  1.00168.07           C
ANISOU 3006  CE1 HIS D 257    20898  21949  21012  -1600    453  -1980       C
ATOM   3007  NE2 HIS D 257       9.434 -88.548 -25.667  1.00150.11           N
ANISOU 3007  NE2 HIS D 257    18621  19695  18719  -1587    560  -2027       N
ATOM   3008  N   ASP D 258       9.667 -86.822 -29.997  1.00133.41           N
ANISOU 3008  N   ASP D 258    16708  17739  16244  -1601    424  -1943       N
ATOM   3009  CA  ASP D 258      11.100 -87.106 -30.031  1.00181.12           C
ANISOU 3009  CA  ASP D 258    22738  23816  22263  -1599    530  -1840       C
ATOM   3010  C   ASP D 258      11.935 -85.847 -30.260  1.00213.60           C
ANISOU 3010  C   ASP D 258    26860  27963  26334  -1621    476  -1695       C
ATOM   3011  O   ASP D 258      13.110 -85.789 -29.879  1.00216.00           O
ANISOU 3011  O   ASP D 258    27141  28282  26650  -1627    540  -1583       O
ATOM   3012  CB  ASP D 258      11.434 -88.203 -31.046  1.00191.41           C
ANISOU 3012  CB  ASP D 258    24073  25163  23491  -1574    633  -1883       C
ATOM   3013  CG  ASP D 258      11.309 -89.601 -30.458  1.00192.10           C
ANISOU 3013  CG  ASP D 258    24129  25218  23642  -1554    735  -1972       C
ATOM   3014  OD1 ASP D 258      10.616 -90.438 -31.071  1.00221.97           O
ANISOU 3014  OD1 ASP D 258    27943  29001  27396  -1535    751  -2084       O
ATOM   3015  OD2 ASP D 258      11.904 -89.867 -29.388  1.00148.98           O
ANISOU 3015  OD2 ASP D 258    18613  19731  18260  -1559    798  -1929       O
ATOM   3016  N   GLN D 259      11.315 -84.839 -30.864  1.00213.36           N
ANISOU 3016  N   GLN D 259    26864  27944  26259  -1633    356  -1693       N
ATOM   3017  CA  GLN D 259      11.946 -83.536 -31.042  1.00207.97           C
ANISOU 3017  CA  GLN D 259    26188  27287  25544  -1657    281  -1560       C
ATOM   3018  C   GLN D 259      12.210 -82.853 -29.691  1.00209.25           C
ANISOU 3018  C   GLN D 259    26310  27396  25799  -1676    239  -1490       C
ATOM   3019  O   GLN D 259      13.341 -82.453 -29.392  1.00213.62           O
ANISOU 3019  O   GLN D 259    26846  27963  26355  -1690    264  -1360       O
ATOM   3020  CB  GLN D 259      11.066 -82.663 -31.943  1.00170.01           C
ANISOU 3020  CB  GLN D 259    21421  22497  20677  -1667    157  -1589       C
ATOM   3021  CG  GLN D 259      11.343 -81.171 -31.894  1.00168.08           C
ANISOU 3021  CG  GLN D 259    21179  22259  20425  -1694     43  -1475       C
ATOM   3022  CD  GLN D 259      10.074 -80.369 -31.652  1.00183.98           C
ANISOU 3022  CD  GLN D 259    23203  24230  22471  -1706    -89  -1539       C
ATOM   3023  OE1 GLN D 259       9.083 -80.900 -31.148  1.00207.91           O
ANISOU 3023  OE1 GLN D 259    26227  27215  25556  -1693    -92  -1654       O
ATOM   3024  NE2 GLN D 259      10.095 -79.091 -32.013  1.00174.53           N
ANISOU 3024  NE2 GLN D 259    22022  23049  21243  -1728   -201  -1463       N
ATOM   3025  N   HIS D 260      11.164 -82.758 -28.870  1.00166.72           N
ANISOU 3025  N   HIS D 260    20909  21950  20488  -1675    178  -1576       N
ATOM   3026  CA  HIS D 260      11.215 -82.021 -27.610  1.00114.11           C
ANISOU 3026  CA  HIS D 260    14215  15232  13909  -1689    120  -1525       C
ATOM   3027  C   HIS D 260      11.629 -82.849 -26.386  1.00159.61           C
ANISOU 3027  C   HIS D 260    19925  20957  19763  -1682    217  -1532       C
ATOM   3028  O   HIS D 260      11.597 -82.347 -25.264  1.00184.96           O
ANISOU 3028  O   HIS D 260    23109  24119  23050  -1690    174  -1503       O
ATOM   3029  CB  HIS D 260       9.870 -81.355 -27.334  1.00107.57           C
ANISOU 3029  CB  HIS D 260    13398  14362  13112  -1687     -5  -1603       C
ATOM   3030  CG  HIS D 260       9.569 -80.196 -28.234  1.00163.93           C
ANISOU 3030  CG  HIS D 260    20579  21526  20179  -1703   -122  -1566       C
ATOM   3031  ND1 HIS D 260       8.289 -79.899 -28.660  1.00167.48           N
ANISOU 3031  ND1 HIS D 260    21054  21967  20614  -1698   -210  -1656       N
ATOM   3032  CD2 HIS D 260      10.374 -79.254 -28.768  1.00197.68           C
ANISOU 3032  CD2 HIS D 260    24872  25838  24400  -1724   -167  -1444       C
ATOM   3033  CE1 HIS D 260       8.327 -78.825 -29.427  1.00184.82           C
ANISOU 3033  CE1 HIS D 260    23282  24193  22749  -1717   -302  -1594       C
ATOM   3034  NE2 HIS D 260       9.577 -78.411 -29.510  1.00206.51           N
ANISOU 3034  NE2 HIS D 260    26023  26968  25471  -1733   -281  -1466       N
ATOM   3035  N   CYS D 261      11.978 -84.118 -26.584  1.00163.37           N
ANISOU 3035  N   CYS D 261    20386  21453  20234  -1666    344  -1573       N
ATOM   3036  CA  CYS D 261      12.526 -84.933 -25.494  1.00162.81           C
ANISOU 3036  CA  CYS D 261    20261  21354  20247  -1664    447  -1566       C
ATOM   3037  C   CYS D 261      13.550 -85.948 -25.993  1.00145.52           C
ANISOU 3037  C   CYS D 261    18065  19209  18018  -1656    590  -1533       C
ATOM   3038  O   CYS D 261      13.331 -86.607 -27.007  1.00147.40           O
ANISOU 3038  O   CYS D 261    18334  19482  18188  -1637    631  -1596       O
ATOM   3039  CB  CYS D 261      11.400 -85.643 -24.738  1.00188.16           C
ANISOU 3039  CB  CYS D 261    23439  24516  23537  -1645    447  -1701       C
ATOM   3040  SG  CYS D 261      11.939 -86.896 -23.532  1.00222.35           S
ANISOU 3040  SG  CYS D 261    27695  28819  27970  -1639    586  -1717       S
ATOM   3041  N   GLN D 262      14.678 -86.061 -25.298  1.00183.38           N
ANISOU 3041  N   GLN D 262    22824  24002  22851  -1670    666  -1430       N
ATOM   3042  CA  GLN D 262      15.679 -87.069 -25.653  1.00211.26           C
ANISOU 3042  CA  GLN D 262    26344  27573  26353  -1660    811  -1393       C
ATOM   3043  C   GLN D 262      15.497 -88.373 -24.869  1.00170.41           C
ANISOU 3043  C   GLN D 262    21120  22368  21261  -1646    916  -1483       C
ATOM   3044  O   GLN D 262      16.015 -89.426 -25.256  1.00120.33           O
ANISOU 3044  O   GLN D 262    14773  16054  14895  -1630   1036  -1497       O
ATOM   3045  CB  GLN D 262      17.096 -86.532 -25.392  1.00224.07           C
ANISOU 3045  CB  GLN D 262    27952  29217  27968  -1684    847  -1218       C
ATOM   3046  CG  GLN D 262      17.256 -85.011 -25.476  1.00214.38           C
ANISOU 3046  CG  GLN D 262    26749  27990  26714  -1710    716  -1111       C
ATOM   3047  CD  GLN D 262      17.491 -84.506 -26.889  1.00213.44           C
ANISOU 3047  CD  GLN D 262    26682  27938  26479  -1704    679  -1060       C
ATOM   3048  OE1 GLN D 262      16.604 -84.574 -27.744  1.00220.11           O
ANISOU 3048  OE1 GLN D 262    27562  28797  27270  -1686    634  -1160       O
ATOM   3049  NE2 GLN D 262      18.691 -83.988 -27.140  1.00204.31           N
ANISOU 3049  NE2 GLN D 262    25527  26821  25280  -1720    694   -900       N
ATOM   3050  N   VAL D 263      14.709 -88.313 -23.800  1.00170.45           N
ANISOU 3050  N   VAL D 263    21087  22316  21360  -1650    867  -1548       N
ATOM   3051  CA  VAL D 263      14.799 -89.329 -22.748  1.00194.46           C
ANISOU 3051  CA  VAL D 263    24062  25326  24499  -1646    962  -1590       C
ATOM   3052  C   VAL D 263      13.983 -90.582 -22.997  1.00206.22           C
ANISOU 3052  C   VAL D 263    25542  26810  26002  -1618   1014  -1737       C
ATOM   3053  O   VAL D 263      14.534 -91.637 -23.321  1.00224.52           O
ANISOU 3053  O   VAL D 263    27852  29151  28304  -1606   1133  -1749       O
ATOM   3054  CB  VAL D 263      14.375 -88.768 -21.376  1.00186.51           C
ANISOU 3054  CB  VAL D 263    23009  24263  23595  -1659    894  -1589       C
ATOM   3055  CG1 VAL D 263      14.452 -89.855 -20.310  1.00132.43           C
ANISOU 3055  CG1 VAL D 263    16084  17386  16847  -1655    994  -1634       C
ATOM   3056  CG2 VAL D 263      15.238 -87.579 -20.995  1.00219.62           C
ANISOU 3056  CG2 VAL D 263    27209  28452  27784  -1690    845  -1440       C
ATOM   3057  N   HIS D 264      12.668 -90.467 -22.844  1.00187.04           N
ANISOU 3057  N   HIS D 264    23116  24350  23602  -1606    922  -1845       N
ATOM   3058  CA  HIS D 264      11.808 -91.632 -22.988  1.00195.82           C
ANISOU 3058  CA  HIS D 264    24216  25451  24737  -1581    956  -1982       C
ATOM   3059  C   HIS D 264      11.486 -91.907 -24.467  1.00195.07           C
ANISOU 3059  C   HIS D 264    24192  25392  24533  -1565    949  -2037       C
ATOM   3060  O   HIS D 264      11.100 -91.004 -25.219  1.00190.46           O
ANISOU 3060  O   HIS D 264    23663  24825  23880  -1569    852  -2026       O
ATOM   3061  CB  HIS D 264      10.560 -91.550 -22.080  1.00189.44           C
ANISOU 3061  CB  HIS D 264    23368  24593  24016  -1573    873  -2070       C
ATOM   3062  CG  HIS D 264       9.696 -90.334 -22.310  1.00178.06           C
ANISOU 3062  CG  HIS D 264    21969  23141  22544  -1575    726  -2075       C
ATOM   3063  ND1 HIS D 264       9.510 -89.363 -21.344  1.00112.25           N
ANISOU 3063  ND1 HIS D 264    13611  14774  14267  -1584    646  -2030       N
ATOM   3064  CD2 HIS D 264       8.955 -89.966 -23.363  1.00210.13           C
ANISOU 3064  CD2 HIS D 264    26093  27219  26529  -1569    647  -2121       C
ATOM   3065  CE1 HIS D 264       8.694 -88.443 -21.807  1.00102.43           C
ANISOU 3065  CE1 HIS D 264    12414  13526  12980  -1581    524  -2049       C
ATOM   3066  NE2 HIS D 264       8.335 -88.770 -23.030  1.00178.14           N
ANISOU 3066  NE2 HIS D 264    22053  23144  22488  -1575    522  -2102       N
ATOM   3067  N   GLY D 265      11.678 -93.155 -24.885  1.00161.95           N
ANISOU 3067  N   GLY D 265    19998  21212  20324  -1547   1052  -2095       N
ATOM   3068  CA  GLY D 265      11.540 -93.497 -26.286  1.00174.16           C
ANISOU 3068  CA  GLY D 265    21615  22796  21763  -1529   1060  -2140       C
ATOM   3069  C   GLY D 265      10.999 -94.895 -26.507  1.00201.64           C
ANISOU 3069  C   GLY D 265    25093  26263  25258  -1505   1120  -2264       C
ATOM   3070  O   GLY D 265      11.048 -95.746 -25.610  1.00190.29           O
ANISOU 3070  O   GLY D 265    23592  24798  23911  -1502   1188  -2297       O
ATOM   3071  N   ASN D 266      10.508 -95.127 -27.724  1.00213.40           N
ANISOU 3071  N   ASN D 266    26652  27774  26657  -1489   1095  -2330       N
ATOM   3072  CA  ASN D 266       9.694 -96.298 -28.041  1.00202.56           C
ANISOU 3072  CA  ASN D 266    25291  26382  25292  -1468   1112  -2462       C
ATOM   3073  C   ASN D 266      10.403 -97.615 -27.744  1.00182.85           C
ANISOU 3073  C   ASN D 266    22760  23883  22831  -1452   1252  -2479       C
ATOM   3074  O   ASN D 266      11.522 -97.849 -28.203  1.00161.87           O
ANISOU 3074  O   ASN D 266    20124  21264  20117  -1443   1348  -2412       O
ATOM   3075  CB  ASN D 266       9.258 -96.241 -29.516  1.00200.26           C
ANISOU 3075  CB  ASN D 266    25090  26120  24879  -1456   1067  -2509       C
ATOM   3076  CG  ASN D 266       7.956 -96.998 -29.787  1.00194.47           C
ANISOU 3076  CG  ASN D 266    24377  25354  24160  -1446   1017  -2648       C
ATOM   3077  OD1 ASN D 266       7.271 -97.443 -28.864  1.00202.90           O
ANISOU 3077  OD1 ASN D 266    25387  26378  25328  -1447    999  -2707       O
ATOM   3078  ND2 ASN D 266       7.605 -97.128 -31.067  1.00148.54           N
ANISOU 3078  ND2 ASN D 266    18640  19560  18240  -1435    990  -2698       N
ATOM   3079  N   ALA D 267       9.758 -98.447 -26.929  1.00179.44           N
ANISOU 3079  N   ALA D 267    22272  23409  22498  -1448   1262  -2562       N
ATOM   3080  CA  ALA D 267      10.141 -99.844 -26.749  1.00151.27           C
ANISOU 3080  CA  ALA D 267    18675  19832  18967  -1431   1379  -2609       C
ATOM   3081  C   ALA D 267       9.248-100.726 -27.622  1.00171.81           C
ANISOU 3081  C   ALA D 267    21331  22422  21525  -1409   1355  -2736       C
ATOM   3082  O   ALA D 267       9.277-101.956 -27.527  1.00145.89           O
ANISOU 3082  O   ALA D 267    18031  19124  18277  -1393   1429  -2801       O
ATOM   3083  CB  ALA D 267      10.044-100.254 -25.291  1.00103.12           C
ANISOU 3083  CB  ALA D 267    12474  13697  13010  -1442   1407  -2617       C
ATOM   3084  N   HIS D 268       8.422-100.079 -28.441  1.00200.20           N
ANISOU 3084  N   HIS D 268    24992  26024  25051  -1411   1246  -2769       N
ATOM   3085  CA  HIS D 268       7.390-100.770 -29.204  1.00204.54           C
ANISOU 3085  CA  HIS D 268    25594  26556  25565  -1397   1198  -2888       C
ATOM   3086  C   HIS D 268       6.465-101.477 -28.218  1.00193.57           C
ANISOU 3086  C   HIS D 268    24133  25116  24297  -1399   1169  -2968       C
ATOM   3087  O   HIS D 268       6.135-102.649 -28.371  1.00201.77           O
ANISOU 3087  O   HIS D 268    25175  26134  25354  -1383   1202  -3054       O
ATOM   3088  CB  HIS D 268       7.994-101.752 -30.217  1.00220.62           C
ANISOU 3088  CB  HIS D 268    27694  28615  27516  -1370   1292  -2921       C
ATOM   3089  CG  HIS D 268       8.700-101.088 -31.360  1.00220.68           C
ANISOU 3089  CG  HIS D 268    27779  28676  27391  -1362   1304  -2854       C
ATOM   3090  ND1 HIS D 268       8.057-100.250 -32.247  1.00223.57           N
ANISOU 3090  ND1 HIS D 268    28211  29060  27677  -1370   1198  -2864       N
ATOM   3091  CD2 HIS D 268       9.989-101.148 -31.767  1.00203.79           C
ANISOU 3091  CD2 HIS D 268    25661  26582  25188  -1346   1408  -2773       C
ATOM   3092  CE1 HIS D 268       8.923 -99.818 -33.146  1.00210.17           C
ANISOU 3092  CE1 HIS D 268    26568  27417  25872  -1360   1236  -2793       C
ATOM   3093  NE2 HIS D 268      10.102-100.347 -32.878  1.00205.63           N
ANISOU 3093  NE2 HIS D 268    25967  26859  25303  -1343   1362  -2735       N
ATOM   3094  N   VAL D 269       6.075-100.741 -27.185  1.00188.71           N
ANISOU 3094  N   VAL D 269    23453  24482  23766  -1416   1107  -2935       N
ATOM   3095  CA  VAL D 269       5.103-101.200 -26.205  1.00186.47           C
ANISOU 3095  CA  VAL D 269    23096  24156  23597  -1415   1062  -2999       C
ATOM   3096  C   VAL D 269       4.098-100.067 -26.002  1.00168.93           C
ANISOU 3096  C   VAL D 269    20877  21924  21385  -1427    925  -2992       C
ATOM   3097  O   VAL D 269       4.483 -98.891 -25.929  1.00123.13           O
ANISOU 3097  O   VAL D 269    15086  16141  15556  -1440    892  -2910       O
ATOM   3098  CB  VAL D 269       5.785-101.636 -24.880  1.00106.60           C
ANISOU 3098  CB  VAL D 269    12878  14030  13597  -1418   1150  -2959       C
ATOM   3099  CG1 VAL D 269       4.791-101.700 -23.764  1.00100.99           C
ANISOU 3099  CG1 VAL D 269    12084  13284  13002  -1418   1082  -2999       C
ATOM   3100  CG2 VAL D 269       6.447-102.992 -25.060  1.00123.26           C
ANISOU 3100  CG2 VAL D 269    14979  16141  15712  -1404   1274  -2994       C
ATOM   3101  N   ALA D 270       2.817-100.430 -25.940  1.00157.67           N
ANISOU 3101  N   ALA D 270    19443  20470  19996  -1421    843  -3076       N
ATOM   3102  CA  ALA D 270       1.723 -99.466 -25.994  1.00121.15           C
ANISOU 3102  CA  ALA D 270    14835  15834  15360  -1429    709  -3082       C
ATOM   3103  C   ALA D 270       1.909 -98.304 -25.028  1.00122.22           C
ANISOU 3103  C   ALA D 270    14921  15970  15546  -1437    673  -3000       C
ATOM   3104  O   ALA D 270       1.672 -97.148 -25.393  1.00131.57           O
ANISOU 3104  O   ALA D 270    16149  17166  16677  -1447    592  -2961       O
ATOM   3105  CB  ALA D 270       0.407-100.156 -25.752  1.00100.97           C
ANISOU 3105  CB  ALA D 270    12253  13246  12865  -1419    641  -3171       C
ATOM   3106  N   SER D 271       2.334 -98.611 -23.804  1.00101.81           N
ANISOU 3106  N   SER D 271    12247  13372  13063  -1433    730  -2974       N
ATOM   3107  CA  SER D 271       2.551 -97.583 -22.787  1.00130.73           C
ANISOU 3107  CA  SER D 271    15861  17030  16780  -1439    700  -2898       C
ATOM   3108  C   SER D 271       3.447 -96.430 -23.234  1.00127.07           C
ANISOU 3108  C   SER D 271    15450  16593  16238  -1456    699  -2802       C
ATOM   3109  O   SER D 271       3.076 -95.269 -23.098  1.00112.09           O
ANISOU 3109  O   SER D 271    13568  14693  14329  -1462    606  -2764       O
ATOM   3110  CB  SER D 271       3.113 -98.207 -21.512  1.00133.82           C
ANISOU 3110  CB  SER D 271    16153  17410  17284  -1435    785  -2879       C
ATOM   3111  OG  SER D 271       3.889 -99.348 -21.812  1.00111.91           O
ANISOU 3111  OG  SER D 271    13374  14645  14504  -1434    904  -2898       O
ATOM   3112  N   CYS D 272       4.621 -96.745 -23.770  1.00141.26           N
ANISOU 3112  N   CYS D 272    17275  18418  17982  -1463    798  -2760       N
ATOM   3113  CA  CYS D 272       5.533 -95.704 -24.223  1.00150.82           C
ANISOU 3113  CA  CYS D 272    18531  19658  19117  -1479    799  -2660       C
ATOM   3114  C   CYS D 272       4.766 -94.697 -25.072  1.00152.50           C
ANISOU 3114  C   CYS D 272    18813  19879  19250  -1485    678  -2666       C
ATOM   3115  O   CYS D 272       4.900 -93.488 -24.877  1.00140.96           O
ANISOU 3115  O   CYS D 272    17360  18420  17777  -1497    614  -2594       O
ATOM   3116  CB  CYS D 272       6.705 -96.295 -25.014  1.00142.61           C
ANISOU 3116  CB  CYS D 272    17527  18652  18006  -1478    914  -2628       C
ATOM   3117  SG  CYS D 272       7.705 -97.481 -24.095  1.00182.67           S
ANISOU 3117  SG  CYS D 272    22520  23720  23167  -1474   1067  -2612       S
ATOM   3118  N   ASP D 273       3.948 -95.200 -25.993  1.00137.74           N
ANISOU 3118  N   ASP D 273    16994  18012  17330  -1477    644  -2752       N
ATOM   3119  CA  ASP D 273       3.148 -94.336 -26.855  1.00157.47           C
ANISOU 3119  CA  ASP D 273    19558  20519  19755  -1485    532  -2764       C
ATOM   3120  C   ASP D 273       2.291 -93.370 -26.043  1.00135.93           C
ANISOU 3120  C   ASP D 273    16798  17765  17085  -1488    422  -2751       C
ATOM   3121  O   ASP D 273       2.059 -92.224 -26.445  1.00117.52           O
ANISOU 3121  O   ASP D 273    14507  15443  14703  -1500    336  -2711       O
ATOM   3122  CB  ASP D 273       2.266 -95.174 -27.780  1.00183.17           C
ANISOU 3122  CB  ASP D 273    22860  23770  22965  -1477    511  -2867       C
ATOM   3123  CG  ASP D 273       2.725 -95.122 -29.224  1.00177.08           C
ANISOU 3123  CG  ASP D 273    22176  23040  22067  -1481    531  -2860       C
ATOM   3124  OD1 ASP D 273       3.645 -95.892 -29.585  1.00175.86           O
ANISOU 3124  OD1 ASP D 273    22034  22905  21880  -1471    637  -2855       O
ATOM   3125  OD2 ASP D 273       2.167 -94.307 -29.994  1.00149.55           O
ANISOU 3125  OD2 ASP D 273    18742  19567  18512  -1494    440  -2858       O
ATOM   3126  N   ALA D 274       1.819 -93.844 -24.897  1.00143.27           N
ANISOU 3126  N   ALA D 274    17654  18661  18121  -1474    424  -2784       N
ATOM   3127  CA  ALA D 274       0.994 -93.027 -24.023  1.00140.70           C
ANISOU 3127  CA  ALA D 274    17293  18309  17857  -1468    327  -2775       C
ATOM   3128  C   ALA D 274       1.848 -91.980 -23.330  1.00139.93           C
ANISOU 3128  C   ALA D 274    17177  18214  17778  -1477    327  -2673       C
ATOM   3129  O   ALA D 274       1.547 -90.785 -23.396  1.00102.58           O
ANISOU 3129  O   ALA D 274    12474  13481  13019  -1484    234  -2633       O
ATOM   3130  CB  ALA D 274       0.279 -93.900 -23.004  1.00112.53           C
ANISOU 3130  CB  ALA D 274    13647  14711  14398  -1446    335  -2836       C
ATOM   3131  N   ILE D 275       2.925 -92.442 -22.691  1.00162.65           N
ANISOU 3131  N   ILE D 275    20007  21092  20699  -1480    430  -2630       N
ATOM   3132  CA  ILE D 275       3.837 -91.571 -21.952  1.00144.40           C
ANISOU 3132  CA  ILE D 275    17674  18779  18413  -1492    440  -2528       C
ATOM   3133  C   ILE D 275       4.245 -90.404 -22.819  1.00133.15           C
ANISOU 3133  C   ILE D 275    16322  17379  16892  -1511    384  -2457       C
ATOM   3134  O   ILE D 275       4.262 -89.253 -22.364  1.00102.78           O
ANISOU 3134  O   ILE D 275    12477  13520  13054  -1518    311  -2395       O
ATOM   3135  CB  ILE D 275       5.148 -92.279 -21.553  1.00102.45           C
ANISOU 3135  CB  ILE D 275    12321  13477  13129  -1500    574  -2480       C
ATOM   3136  CG1 ILE D 275       4.913 -93.727 -21.126  1.00129.51           C
ANISOU 3136  CG1 ILE D 275    15689  16892  16627  -1485    654  -2560       C
ATOM   3137  CG2 ILE D 275       5.813 -91.525 -20.443  1.00123.60           C
ANISOU 3137  CG2 ILE D 275    14957  16139  15865  -1511    573  -2390       C
ATOM   3138  CD1 ILE D 275       6.159 -94.395 -20.547  1.00110.20           C
ANISOU 3138  CD1 ILE D 275    13191  14453  14226  -1494    785  -2509       C
ATOM   3139  N   MET D 276       4.584 -90.722 -24.069  1.00129.10           N
ANISOU 3139  N   MET D 276    15865  16900  16286  -1519    420  -2465       N
ATOM   3140  CA  MET D 276       4.999 -89.724 -25.046  1.00135.32           C
ANISOU 3140  CA  MET D 276    16720  17721  16975  -1537    374  -2398       C
ATOM   3141  C   MET D 276       3.899 -88.697 -25.276  1.00127.27           C
ANISOU 3141  C   MET D 276    15733  16690  15935  -1539    236  -2417       C
ATOM   3142  O   MET D 276       4.161 -87.504 -25.465  1.00124.43           O
ANISOU 3142  O   MET D 276    15401  16339  15536  -1554    169  -2342       O
ATOM   3143  CB  MET D 276       5.385 -90.398 -26.370  1.00136.45           C
ANISOU 3143  CB  MET D 276    16917  17906  17024  -1537    437  -2421       C
ATOM   3144  CG  MET D 276       6.500 -91.424 -26.221  1.00141.17           C
ANISOU 3144  CG  MET D 276    17488  18518  17635  -1531    579  -2400       C
ATOM   3145  SD  MET D 276       7.214 -91.993 -27.778  1.00172.48           S
ANISOU 3145  SD  MET D 276    21523  22538  21474  -1525    656  -2398       S
ATOM   3146  CE  MET D 276       8.164 -93.386 -27.177  1.00109.83           C
ANISOU 3146  CE  MET D 276    13535  14599  13596  -1512    817  -2401       C
ATOM   3147  N   THR D 277       2.663 -89.171 -25.246  1.00 95.55           N
ANISOU 3147  N   THR D 277    11709  12651  11944  -1524    192  -2513       N
ATOM   3148  CA  THR D 277       1.536 -88.336 -25.572  1.00109.66           C
ANISOU 3148  CA  THR D 277    13529  14429  13707  -1525     67  -2537       C
ATOM   3149  C   THR D 277       1.283 -87.348 -24.442  1.00139.12           C
ANISOU 3149  C   THR D 277    17225  18128  17504  -1519     -6  -2493       C
ATOM   3150  O   THR D 277       0.685 -86.289 -24.653  1.00156.62           O
ANISOU 3150  O   THR D 277    19474  20341  19694  -1523   -112  -2475       O
ATOM   3151  CB  THR D 277       0.318 -89.203 -25.800  1.00122.41           C
ANISOU 3151  CB  THR D 277    15142  16030  15337  -1511     46  -2645       C
ATOM   3152  OG1 THR D 277       0.741 -90.422 -26.430  1.00108.95           O
ANISOU 3152  OG1 THR D 277    13450  14344  13604  -1510    142  -2690       O
ATOM   3153  CG2 THR D 277      -0.708 -88.466 -26.666  1.00117.84           C
ANISOU 3153  CG2 THR D 277    14620  15458  14696  -1520    -67  -2668       C
ATOM   3154  N   ARG D 278       1.709 -87.713 -23.235  1.00120.41           N
ANISOU 3154  N   ARG D 278    14792  15736  15224  -1506     49  -2476       N
ATOM   3155  CA  ARG D 278       1.781 -86.754 -22.145  1.00134.41           C
ANISOU 3155  CA  ARG D 278    16536  17481  17053  -1501     -5  -2417       C
ATOM   3156  C   ARG D 278       2.968 -85.816 -22.364  1.00154.37           C
ANISOU 3156  C   ARG D 278    19096  20026  19534  -1527     -4  -2307       C
ATOM   3157  O   ARG D 278       2.812 -84.592 -22.416  1.00139.79           O
ANISOU 3157  O   ARG D 278    17280  18172  17661  -1534   -100  -2258       O
ATOM   3158  CB  ARG D 278       1.901 -87.464 -20.790  1.00138.26           C
ANISOU 3158  CB  ARG D 278    16943  17941  17649  -1481     56  -2432       C
ATOM   3159  CG  ARG D 278       0.567 -87.732 -20.091  1.00114.28           C
ANISOU 3159  CG  ARG D 278    13865  14877  14681  -1448      0  -2508       C
ATOM   3160  CD  ARG D 278       0.730 -87.893 -18.585  1.00116.30           C
ANISOU 3160  CD  ARG D 278    14043  15105  15042  -1428     28  -2492       C
ATOM   3161  NE  ARG D 278       1.282 -86.687 -17.973  1.00145.57           N
ANISOU 3161  NE  ARG D 278    17760  18796  18755  -1433    -18  -2406       N
ATOM   3162  CZ  ARG D 278       2.457 -86.631 -17.352  1.00149.28           C
ANISOU 3162  CZ  ARG D 278    18204  19262  19255  -1449     48  -2334       C
ATOM   3163  NH1 ARG D 278       3.212 -87.719 -17.233  1.00133.82           N
ANISOU 3163  NH1 ARG D 278    16203  17316  17325  -1460    168  -2339       N
ATOM   3164  NH2 ARG D 278       2.877 -85.485 -16.841  1.00145.87           N
ANISOU 3164  NH2 ARG D 278    17789  18811  18824  -1455     -8  -2256       N
ATOM   3165  N   CYS D 279       4.149 -86.405 -22.534  1.00163.34           N
ANISOU 3165  N   CYS D 279    20222  21184  20656  -1541    104  -2264       N
ATOM   3166  CA  CYS D 279       5.394 -85.644 -22.648  1.00153.03           C
ANISOU 3166  CA  CYS D 279    18935  19895  19313  -1565    118  -2147       C
ATOM   3167  C   CYS D 279       5.311 -84.580 -23.745  1.00156.74           C
ANISOU 3167  C   CYS D 279    19474  20393  19689  -1582     29  -2106       C
ATOM   3168  O   CYS D 279       6.048 -83.599 -23.726  1.00152.08           O
ANISOU 3168  O   CYS D 279    18900  19807  19075  -1601     -6  -2006       O
ATOM   3169  CB  CYS D 279       6.589 -86.594 -22.843  1.00131.33           C
ANISOU 3169  CB  CYS D 279    16170  17175  16555  -1574    256  -2114       C
ATOM   3170  SG  CYS D 279       8.150 -85.877 -23.450  1.00123.20           S
ANISOU 3170  SG  CYS D 279    15175  16187  15450  -1604    288  -1968       S
ATOM   3171  N   LEU D 280       4.426 -84.790 -24.713  1.00174.80           N
ANISOU 3171  N   LEU D 280    21798  22697  21922  -1578     -7  -2182       N
ATOM   3172  CA  LEU D 280       4.065 -83.731 -25.643  1.00183.98           C
ANISOU 3172  CA  LEU D 280    23017  23880  23008  -1593   -109  -2157       C
ATOM   3173  C   LEU D 280       3.024 -82.821 -24.988  1.00160.71           C
ANISOU 3173  C   LEU D 280    20066  20891  20103  -1583   -229  -2174       C
ATOM   3174  O   LEU D 280       3.104 -81.597 -25.089  1.00151.17           O
ANISOU 3174  O   LEU D 280    18885  19682  18870  -1597   -317  -2109       O
ATOM   3175  CB  LEU D 280       3.527 -84.312 -26.964  1.00192.74           C
ANISOU 3175  CB  LEU D 280    24169  25024  24040  -1594   -100  -2230       C
ATOM   3176  CG  LEU D 280       3.641 -83.492 -28.263  1.00182.50           C
ANISOU 3176  CG  LEU D 280    22932  23771  22639  -1616   -159  -2188       C
ATOM   3177  CD1 LEU D 280       2.849 -84.147 -29.396  1.00182.56           C
ANISOU 3177  CD1 LEU D 280    22978  23802  22584  -1614   -159  -2279       C
ATOM   3178  CD2 LEU D 280       3.189 -82.048 -28.082  1.00171.73           C
ANISOU 3178  CD2 LEU D 280    21583  22392  21277  -1628   -289  -2140       C
ATOM   3179  N   ALA D 281       2.050 -83.430 -24.317  1.00166.65           N
ANISOU 3179  N   ALA D 281    20785  21613  20922  -1557   -233  -2259       N
ATOM   3180  CA  ALA D 281       0.910 -82.698 -23.771  1.00174.86           C
ANISOU 3180  CA  ALA D 281    21823  22618  21998  -1540   -342  -2286       C
ATOM   3181  C   ALA D 281       1.329 -81.552 -22.851  1.00192.88           C
ANISOU 3181  C   ALA D 281    24098  24871  24317  -1539   -401  -2203       C
ATOM   3182  O   ALA D 281       0.849 -80.425 -22.994  1.00185.21           O
ANISOU 3182  O   ALA D 281    23159  23890  23321  -1542   -509  -2178       O
ATOM   3183  CB  ALA D 281      -0.038 -83.656 -23.052  1.00164.03           C
ANISOU 3183  CB  ALA D 281    20403  21220  20701  -1508   -322  -2377       C
ATOM   3184  N   VAL D 282       2.221 -81.838 -21.908  1.00201.27           N
ANISOU 3184  N   VAL D 282    25118  25919  25437  -1537   -332  -2159       N
ATOM   3185  CA  VAL D 282       2.763 -80.789 -21.053  1.00195.90           C
ANISOU 3185  CA  VAL D 282    24436  25209  24787  -1540   -382  -2073       C
ATOM   3186  C   VAL D 282       3.449 -79.729 -21.917  1.00183.53           C
ANISOU 3186  C   VAL D 282    22923  23667  23141  -1573   -436  -1983       C
ATOM   3187  O   VAL D 282       3.046 -78.559 -21.923  1.00143.43           O
ANISOU 3187  O   VAL D 282    17877  18572  18048  -1574   -548  -1953       O
ATOM   3188  CB  VAL D 282       3.750 -81.361 -19.999  1.00234.14           C
ANISOU 3188  CB  VAL D 282    29226  30037  29700  -1540   -286  -2033       C
ATOM   3189  CG1 VAL D 282       4.604 -82.470 -20.597  1.00239.11           C
ANISOU 3189  CG1 VAL D 282    29842  30705  30305  -1557   -158  -2033       C
ATOM   3190  CG2 VAL D 282       4.624 -80.260 -19.411  1.00233.51           C
ANISOU 3190  CG2 VAL D 282    29158  29936  29630  -1556   -330  -1922       C
ATOM   3191  N   HIS D 283       4.435 -80.169 -22.692  1.00177.98           N
ANISOU 3191  N   HIS D 283    22231  23007  22388  -1598   -356  -1941       N
ATOM   3192  CA  HIS D 283       5.301 -79.294 -23.484  1.00151.69           C
ANISOU 3192  CA  HIS D 283    18942  19709  18986  -1629   -389  -1840       C
ATOM   3193  C   HIS D 283       4.552 -78.258 -24.324  1.00146.92           C
ANISOU 3193  C   HIS D 283    18386  19115  18322  -1638   -511  -1843       C
ATOM   3194  O   HIS D 283       5.022 -77.141 -24.505  1.00151.33           O
ANISOU 3194  O   HIS D 283    18971  19677  18850  -1658   -585  -1753       O
ATOM   3195  CB  HIS D 283       6.206 -80.131 -24.392  1.00159.28           C
ANISOU 3195  CB  HIS D 283    19906  20723  19890  -1644   -280  -1819       C
ATOM   3196  CG  HIS D 283       7.318 -79.359 -25.032  1.00186.78           C
ANISOU 3196  CG  HIS D 283    23416  24242  23309  -1673   -294  -1697       C
ATOM   3197  ND1 HIS D 283       8.640 -79.525 -24.682  1.00189.57           N
ANISOU 3197  ND1 HIS D 283    23749  24606  23674  -1687   -217  -1600       N
ATOM   3198  CD2 HIS D 283       7.303 -78.409 -26.002  1.00186.60           C
ANISOU 3198  CD2 HIS D 283    23436  24250  23212  -1692   -378  -1649       C
ATOM   3199  CE1 HIS D 283       9.394 -78.714 -25.404  1.00188.02           C
ANISOU 3199  CE1 HIS D 283    23582  24446  23413  -1711   -255  -1494       C
ATOM   3200  NE2 HIS D 283       8.603 -78.027 -26.213  1.00199.76           N
ANISOU 3200  NE2 HIS D 283    25106  25947  24848  -1714   -354  -1524       N
ATOM   3201  N   GLU D 284       3.389 -78.622 -24.853  1.00171.62           N
ANISOU 3201  N   GLU D 284    21527  22250  21432  -1625   -536  -1941       N
ATOM   3202  CA  GLU D 284       2.648 -77.686 -25.689  1.00175.95           C
ANISOU 3202  CA  GLU D 284    22119  22810  21923  -1636   -646  -1945       C
ATOM   3203  C   GLU D 284       1.950 -76.605 -24.871  1.00172.97           C
ANISOU 3203  C   GLU D 284    21746  22385  21590  -1622   -762  -1935       C
ATOM   3204  O   GLU D 284       1.652 -75.523 -25.378  1.00186.46           O
ANISOU 3204  O   GLU D 284    23491  24099  23259  -1636   -864  -1901       O
ATOM   3205  CB  GLU D 284       1.664 -78.425 -26.597  1.00165.78           C
ANISOU 3205  CB  GLU D 284    20846  21547  20597  -1631   -634  -2046       C
ATOM   3206  CG  GLU D 284       2.189 -78.596 -28.010  1.00162.67           C
ANISOU 3206  CG  GLU D 284    20486  21214  20108  -1657   -601  -2026       C
ATOM   3207  CD  GLU D 284       2.522 -77.262 -28.652  1.00192.67           C
ANISOU 3207  CD  GLU D 284    24318  25038  23851  -1684   -693  -1937       C
ATOM   3208  OE1 GLU D 284       3.621 -77.135 -29.235  1.00208.28           O
ANISOU 3208  OE1 GLU D 284    26303  27057  25777  -1703   -657  -1858       O
ATOM   3209  OE2 GLU D 284       1.681 -76.339 -28.568  1.00192.69           O
ANISOU 3209  OE2 GLU D 284    24336  25019  23860  -1685   -803  -1944       O
ATOM   3210  N   CYS D 285       1.714 -76.902 -23.599  1.00173.98           N
ANISOU 3210  N   CYS D 285    21837  22467  21801  -1592   -745  -1962       N
ATOM   3211  CA  CYS D 285       0.983 -76.007 -22.710  1.00190.14           C
ANISOU 3211  CA  CYS D 285    23887  24465  23894  -1568   -846  -1962       C
ATOM   3212  C   CYS D 285       1.931 -75.304 -21.756  1.00179.36           C
ANISOU 3212  C   CYS D 285    22516  23066  22567  -1571   -863  -1870       C
ATOM   3213  O   CYS D 285       1.993 -74.075 -21.696  1.00168.67           O
ANISOU 3213  O   CYS D 285    21195  21694  21199  -1579   -964  -1809       O
ATOM   3214  CB  CYS D 285      -0.051 -76.786 -21.902  1.00191.78           C
ANISOU 3214  CB  CYS D 285    24056  24643  24168  -1526   -825  -2057       C
ATOM   3215  SG  CYS D 285      -0.880 -78.110 -22.804  1.00144.53           S
ANISOU 3215  SG  CYS D 285    18063  18695  18158  -1523   -762  -2165       S
ATOM   3216  N   PHE D 286       2.632 -76.115 -20.975  1.00193.87           N
ANISOU 3216  N   PHE D 286    24310  24894  24458  -1565   -765  -1863       N
ATOM   3217  CA  PHE D 286       3.455 -75.635 -19.868  1.00224.89           C
ANISOU 3217  CA  PHE D 286    28225  28785  28437  -1566   -770  -1785       C
ATOM   3218  C   PHE D 286       4.833 -75.039 -20.190  1.00227.40           C
ANISOU 3218  C   PHE D 286    28565  29119  28719  -1607   -768  -1661       C
ATOM   3219  O   PHE D 286       5.169 -73.959 -19.698  1.00224.43           O
ANISOU 3219  O   PHE D 286    28211  28710  28353  -1614   -851  -1586       O
ATOM   3220  CB  PHE D 286       3.606 -76.758 -18.847  1.00228.09           C
ANISOU 3220  CB  PHE D 286    28571  29174  28921  -1544   -666  -1826       C
ATOM   3221  CG  PHE D 286       2.348 -77.045 -18.103  1.00193.60           C
ANISOU 3221  CG  PHE D 286    24175  24776  24609  -1497   -693  -1919       C
ATOM   3222  CD1 PHE D 286       1.371 -76.072 -17.999  1.00194.58           C
ANISOU 3222  CD1 PHE D 286    24331  24874  24725  -1473   -814  -1936       C
ATOM   3223  CD2 PHE D 286       2.134 -78.271 -17.513  1.00160.72           C
ANISOU 3223  CD2 PHE D 286    19951  20612  20505  -1475   -600  -1985       C
ATOM   3224  CE1 PHE D 286       0.210 -76.313 -17.316  1.00202.42           C
ANISOU 3224  CE1 PHE D 286    25299  25845  25768  -1426   -840  -2012       C
ATOM   3225  CE2 PHE D 286       0.975 -78.517 -16.831  1.00189.47           C
ANISOU 3225  CE2 PHE D 286    23563  24229  24197  -1429   -630  -2062       C
ATOM   3226  CZ  PHE D 286       0.010 -77.536 -16.731  1.00207.80           C
ANISOU 3226  CZ  PHE D 286    25919  26528  26509  -1403   -749  -2074       C
ATOM   3227  N   VAL D 287       5.622 -75.731 -21.008  1.00219.48           N
ANISOU 3227  N   VAL D 287    27555  28165  27672  -1633   -676  -1637       N
ATOM   3228  CA  VAL D 287       6.995 -75.300 -21.276  1.00198.14           C
ANISOU 3228  CA  VAL D 287    24864  25482  24937  -1669   -660  -1511       C
ATOM   3229  C   VAL D 287       7.050 -73.902 -21.905  1.00186.25           C
ANISOU 3229  C   VAL D 287    23408  23982  23376  -1691   -788  -1436       C
ATOM   3230  O   VAL D 287       8.104 -73.264 -21.926  1.00190.37           O
ANISOU 3230  O   VAL D 287    23942  24510  23882  -1720   -809  -1318       O
ATOM   3231  CB  VAL D 287       7.793 -76.334 -22.108  1.00165.23           C
ANISOU 3231  CB  VAL D 287    20681  21372  20725  -1686   -534  -1500       C
ATOM   3232  CG1 VAL D 287       8.573 -75.651 -23.220  1.00151.19           C
ANISOU 3232  CG1 VAL D 287    18938  19643  18864  -1719   -567  -1400       C
ATOM   3233  CG2 VAL D 287       8.722 -77.148 -21.204  1.00112.04           C
ANISOU 3233  CG2 VAL D 287    13898  14623  14048  -1688   -419  -1465       C
ATOM   3234  N   LYS D 288       5.917 -73.423 -22.409  1.00172.01           N
ANISOU 3234  N   LYS D 288    21632  22179  21546  -1679   -875  -1500       N
ATOM   3235  CA  LYS D 288       5.823 -72.021 -22.792  1.00190.19           C
ANISOU 3235  CA  LYS D 288    23977  24475  23811  -1696  -1009  -1436       C
ATOM   3236  C   LYS D 288       4.993 -71.227 -21.776  1.00216.71           C
ANISOU 3236  C   LYS D 288    27348  27767  27223  -1667  -1112  -1463       C
ATOM   3237  O   LYS D 288       3.764 -71.312 -21.775  1.00226.50           O
ANISOU 3237  O   LYS D 288    28591  28996  28472  -1639  -1146  -1557       O
ATOM   3238  CB  LYS D 288       5.143 -71.888 -24.160  1.00194.46           C
ANISOU 3238  CB  LYS D 288    24543  25065  24278  -1706  -1047  -1478       C
ATOM   3239  CG  LYS D 288       5.558 -72.904 -25.232  1.00215.55           C
ANISOU 3239  CG  LYS D 288    27204  27803  26893  -1720   -939  -1496       C
ATOM   3240  CD  LYS D 288       4.489 -72.977 -26.343  1.00204.05           C
ANISOU 3240  CD  LYS D 288    25770  26381  25380  -1720   -973  -1579       C
ATOM   3241  CE  LYS D 288       5.001 -73.594 -27.647  1.00154.70           C
ANISOU 3241  CE  LYS D 288    19526  20203  19052  -1739   -900  -1571       C
ATOM   3242  NZ  LYS D 288       5.486 -74.998 -27.489  1.00123.41           N
ANISOU 3242  NZ  LYS D 288    15535  16253  15104  -1726   -756  -1609       N
ATOM   3243  N   ARG D 289       5.664 -70.447 -20.931  1.00217.78           N
ANISOU 3243  N   ARG D 289    27493  27860  27393  -1673  -1164  -1376       N
ATOM   3244  CA  ARG D 289       5.042 -69.323 -20.221  1.00225.35           C
ANISOU 3244  CA  ARG D 289    28482  28760  28379  -1652  -1292  -1373       C
ATOM   3245  C   ARG D 289       3.916 -69.631 -19.208  1.00247.21           C
ANISOU 3245  C   ARG D 289    31236  31483  31210  -1598  -1297  -1475       C
ATOM   3246  O   ARG D 289       3.516 -68.750 -18.442  1.00246.10           O
ANISOU 3246  O   ARG D 289    31120  31289  31098  -1574  -1393  -1466       O
ATOM   3247  CB  ARG D 289       4.545 -68.294 -21.247  1.00227.59           C
ANISOU 3247  CB  ARG D 289    28808  29064  28601  -1668  -1406  -1357       C
ATOM   3248  CG  ARG D 289       5.647 -67.533 -21.997  1.00240.40           C
ANISOU 3248  CG  ARG D 289    30452  30718  30172  -1717  -1450  -1230       C
ATOM   3249  CD  ARG D 289       6.571 -68.441 -22.811  1.00249.08           C
ANISOU 3249  CD  ARG D 289    31525  31884  31231  -1745  -1332  -1196       C
ATOM   3250  NE  ARG D 289       7.539 -67.672 -23.594  1.00245.44           N
ANISOU 3250  NE  ARG D 289    31080  31459  30717  -1787  -1381  -1071       N
ATOM   3251  CZ  ARG D 289       8.693 -68.150 -24.051  1.00230.03           C
ANISOU 3251  CZ  ARG D 289    29110  29555  28736  -1813  -1298   -992       C
ATOM   3252  NH1 ARG D 289       9.504 -67.370 -24.753  1.00218.29           N
ANISOU 3252  NH1 ARG D 289    27636  28104  27202  -1848  -1355   -872       N
ATOM   3253  NH2 ARG D 289       9.044 -69.405 -23.803  1.00228.00           N
ANISOU 3253  NH2 ARG D 289    28819  29313  28499  -1803  -1159  -1028       N
ATOM   3254  N   VAL D 290       3.411 -70.862 -19.210  1.00270.75           N
ANISOU 3254  N   VAL D 290    34178  34486  34211  -1578  -1197  -1568       N
ATOM   3255  CA  VAL D 290       2.291 -71.276 -18.346  1.00281.81           C
ANISOU 3255  CA  VAL D 290    35555  35853  35667  -1525  -1196  -1665       C
ATOM   3256  C   VAL D 290       1.090 -70.315 -18.382  1.00273.10           C
ANISOU 3256  C   VAL D 290    34489  34724  34551  -1496  -1322  -1700       C
ATOM   3257  O   VAL D 290       0.759 -69.762 -19.430  1.00298.92           O
ANISOU 3257  O   VAL D 290    37793  38022  37762  -1518  -1383  -1694       O
ATOM   3258  CB  VAL D 290       2.739 -71.525 -16.869  1.00249.51           C
ANISOU 3258  CB  VAL D 290    31431  31715  31655  -1501  -1157  -1649       C
ATOM   3259  CG1 VAL D 290       3.926 -72.481 -16.818  1.00260.99           C
ANISOU 3259  CG1 VAL D 290    32846  33194  33124  -1531  -1029  -1611       C
ATOM   3260  CG2 VAL D 290       3.068 -70.221 -16.148  1.00223.13           C
ANISOU 3260  CG2 VAL D 290    28131  28321  28327  -1498  -1266  -1572       C
ATOM   3261  N   ASP D 291       0.446 -70.124 -17.233  1.00227.17           N
ANISOU 3261  N   ASP D 291    28665  28859  28791  -1446  -1358  -1735       N
ATOM   3262  CA  ASP D 291      -0.527 -69.051 -17.054  1.00207.30           C
ANISOU 3262  CA  ASP D 291    26188  26308  26267  -1414  -1484  -1748       C
ATOM   3263  C   ASP D 291      -0.668 -68.720 -15.575  1.00210.82           C
ANISOU 3263  C   ASP D 291    26630  26693  26777  -1363  -1517  -1747       C
ATOM   3264  O   ASP D 291      -0.463 -69.580 -14.717  1.00206.72           O
ANISOU 3264  O   ASP D 291    26064  26166  26315  -1342  -1433  -1772       O
ATOM   3265  CB  ASP D 291      -1.893 -69.408 -17.652  1.00205.47           C
ANISOU 3265  CB  ASP D 291    25952  26102  26017  -1391  -1494  -1839       C
ATOM   3266  CG  ASP D 291      -2.915 -68.294 -17.475  1.00208.22           C
ANISOU 3266  CG  ASP D 291    26340  26417  26356  -1355  -1621  -1848       C
ATOM   3267  OD1 ASP D 291      -2.504 -67.147 -17.198  1.00209.75           O
ANISOU 3267  OD1 ASP D 291    26576  26575  26544  -1360  -1711  -1780       O
ATOM   3268  OD2 ASP D 291      -4.130 -68.560 -17.615  1.00205.67           O
ANISOU 3268  OD2 ASP D 291    26008  26102  26033  -1323  -1634  -1919       O
ATOM   3269  N   TRP D 292      -1.011 -67.469 -15.284  1.00218.29           N
ANISOU 3269  N   TRP D 292    27627  27598  27715  -1343  -1640  -1717       N
ATOM   3270  CA  TRP D 292      -1.266 -67.031 -13.912  1.00217.96           C
ANISOU 3270  CA  TRP D 292    27593  27496  27726  -1287  -1687  -1720       C
ATOM   3271  C   TRP D 292      -2.681 -67.315 -13.417  1.00210.58           C
ANISOU 3271  C   TRP D 292    26638  26553  26818  -1217  -1698  -1810       C
ATOM   3272  O   TRP D 292      -2.868 -67.704 -12.265  1.00232.05           O
ANISOU 3272  O   TRP D 292    29326  29247  29595  -1167  -1668  -1838       O
ATOM   3273  CB  TRP D 292      -0.902 -65.555 -13.724  1.00223.90           C
ANISOU 3273  CB  TRP D 292    28412  28201  28460  -1293  -1815  -1641       C
ATOM   3274  CG  TRP D 292       0.540 -65.355 -13.366  1.00228.23           C
ANISOU 3274  CG  TRP D 292    28968  28729  29020  -1335  -1800  -1547       C
ATOM   3275  CD1 TRP D 292       1.030 -64.694 -12.277  1.00214.06           C
ANISOU 3275  CD1 TRP D 292    27200  26872  27259  -1317  -1855  -1495       C
ATOM   3276  CD2 TRP D 292       1.682 -65.847 -14.083  1.00239.64           C
ANISOU 3276  CD2 TRP D 292    30393  30216  30443  -1401  -1725  -1488       C
ATOM   3277  NE1 TRP D 292       2.404 -64.732 -12.278  1.00210.72           N
ANISOU 3277  NE1 TRP D 292    26776  26450  26839  -1373  -1820  -1404       N
ATOM   3278  CE2 TRP D 292       2.829 -65.435 -13.377  1.00226.63           C
ANISOU 3278  CE2 TRP D 292    28760  28530  28819  -1423  -1738  -1396       C
ATOM   3279  CE3 TRP D 292       1.845 -66.593 -15.260  1.00236.04           C
ANISOU 3279  CE3 TRP D 292    29911  29827  29947  -1442  -1647  -1502       C
ATOM   3280  CZ2 TRP D 292       4.120 -65.739 -13.803  1.00225.57           C
ANISOU 3280  CZ2 TRP D 292    28612  28424  28671  -1484  -1676  -1313       C
ATOM   3281  CZ3 TRP D 292       3.126 -66.895 -15.683  1.00222.33           C
ANISOU 3281  CZ3 TRP D 292    28162  28120  28195  -1497  -1584  -1424       C
ATOM   3282  CH2 TRP D 292       4.247 -66.467 -14.957  1.00225.20           C
ANISOU 3282  CH2 TRP D 292    28537  28446  28583  -1518  -1598  -1328       C
ATOM   3283  N   SER D 293      -3.673 -67.106 -14.282  1.00186.20           N
ANISOU 3283  N   SER D 293    23568  23491  23689  -1213  -1744  -1850       N
ATOM   3284  CA  SER D 293      -5.072 -67.309 -13.902  1.00181.15           C
ANISOU 3284  CA  SER D 293    22911  22847  23069  -1147  -1763  -1925       C
ATOM   3285  C   SER D 293      -5.311 -68.704 -13.331  1.00194.65           C
ANISOU 3285  C   SER D 293    24549  24578  24834  -1119  -1651  -1988       C
ATOM   3286  O   SER D 293      -6.137 -68.889 -12.431  1.00163.63           O
ANISOU 3286  O   SER D 293    20594  20630  20947  -1052  -1658  -2031       O
ATOM   3287  CB  SER D 293      -6.006 -67.056 -15.087  1.00158.38           C
ANISOU 3287  CB  SER D 293    20050  19996  20130  -1162  -1810  -1953       C
ATOM   3288  OG  SER D 293      -6.416 -65.701 -15.131  1.00139.27           O
ANISOU 3288  OG  SER D 293    17691  17544  17683  -1147  -1936  -1921       O
ATOM   3289  N   VAL D 294      -4.580 -69.683 -13.855  1.00214.56           N
ANISOU 3289  N   VAL D 294    27033  27136  27353  -1169  -1548  -1990       N
ATOM   3290  CA  VAL D 294      -4.719 -71.060 -13.398  1.00209.28           C
ANISOU 3290  CA  VAL D 294    26292  26488  26735  -1150  -1438  -2048       C
ATOM   3291  C   VAL D 294      -4.149 -71.256 -11.992  1.00202.46           C
ANISOU 3291  C   VAL D 294    25395  25591  25941  -1118  -1401  -2030       C
ATOM   3292  O   VAL D 294      -2.969 -71.007 -11.745  1.00214.51           O
ANISOU 3292  O   VAL D 294    26932  27100  27472  -1153  -1383  -1966       O
ATOM   3293  CB  VAL D 294      -4.039 -72.046 -14.371  1.00191.65           C
ANISOU 3293  CB  VAL D 294    24035  24304  24479  -1211  -1337  -2054       C
ATOM   3294  CG1 VAL D 294      -2.574 -71.681 -14.571  1.00174.65           C
ANISOU 3294  CG1 VAL D 294    21905  22148  22305  -1266  -1318  -1970       C
ATOM   3295  CG2 VAL D 294      -4.176 -73.464 -13.859  1.00195.00           C
ANISOU 3295  CG2 VAL D 294    24384  24746  24960  -1191  -1228  -2113       C
ATOM   3296  N   GLU D 295      -4.995 -71.724 -11.080  1.00179.21           N
ANISOU 3296  N   GLU D 295    22405  22638  23050  -1053  -1389  -2084       N
ATOM   3297  CA  GLU D 295      -4.602 -71.950  -9.696  1.00173.17           C
ANISOU 3297  CA  GLU D 295    21600  21843  22353  -1016  -1355  -2075       C
ATOM   3298  C   GLU D 295      -4.880 -73.401  -9.347  1.00150.59           C
ANISOU 3298  C   GLU D 295    18651  19016  19549   -999  -1247  -2135       C
ATOM   3299  O   GLU D 295      -5.611 -74.081 -10.055  1.00175.58           O
ANISOU 3299  O   GLU D 295    21794  22217  22701  -1001  -1222  -2188       O
ATOM   3300  CB  GLU D 295      -5.392 -71.027  -8.768  1.00179.28           C
ANISOU 3300  CB  GLU D 295    22402  22576  23142   -941  -1454  -2077       C
ATOM   3301  CG  GLU D 295      -4.595 -70.490  -7.589  1.00185.47           C
ANISOU 3301  CG  GLU D 295    23197  23310  23962   -923  -1471  -2026       C
ATOM   3302  CD  GLU D 295      -5.312 -69.351  -6.886  1.00177.03           C
ANISOU 3302  CD  GLU D 295    22179  22195  22887   -853  -1587  -2021       C
ATOM   3303  OE1 GLU D 295      -6.446 -69.016  -7.304  1.00152.64           O
ANISOU 3303  OE1 GLU D 295    19112  19116  19769   -817  -1648  -2055       O
ATOM   3304  OE2 GLU D 295      -4.742 -68.790  -5.919  1.00167.27           O
ANISOU 3304  OE2 GLU D 295    20966  20914  21676   -834  -1618  -1980       O
ATOM   3305  N   TYR D 296      -4.292 -73.888  -8.268  1.00135.91           N
ANISOU 3305  N   TYR D 296    16742  17144  17755   -985  -1185  -2126       N
ATOM   3306  CA  TYR D 296      -4.544 -75.261  -7.864  1.00130.37           C
ANISOU 3306  CA  TYR D 296    15949  16472  17113   -967  -1085  -2181       C
ATOM   3307  C   TYR D 296      -4.742 -75.358  -6.365  1.00174.22           C
ANISOU 3307  C   TYR D 296    21453  22003  22740   -902  -1081  -2189       C
ATOM   3308  O   TYR D 296      -4.073 -74.669  -5.591  1.00207.20           O
ANISOU 3308  O   TYR D 296    25654  26142  26932   -897  -1108  -2138       O
ATOM   3309  CB  TYR D 296      -3.401 -76.168  -8.315  1.00133.75           C
ANISOU 3309  CB  TYR D 296    16346  16925  17547  -1036   -972  -2166       C
ATOM   3310  CG  TYR D 296      -3.168 -76.102  -9.799  1.00140.12           C
ANISOU 3310  CG  TYR D 296    17202  17759  18279  -1096   -972  -2157       C
ATOM   3311  CD1 TYR D 296      -2.361 -75.121 -10.349  1.00153.29           C
ANISOU 3311  CD1 TYR D 296    18939  19412  19890  -1141  -1020  -2086       C
ATOM   3312  CD2 TYR D 296      -3.777 -77.006 -10.656  1.00177.51           C
ANISOU 3312  CD2 TYR D 296    21912  22535  22998  -1106   -930  -2218       C
ATOM   3313  CE1 TYR D 296      -2.155 -75.050 -11.710  1.00160.46           C
ANISOU 3313  CE1 TYR D 296    19888  20350  20728  -1193  -1021  -2076       C
ATOM   3314  CE2 TYR D 296      -3.580 -76.944 -12.016  1.00176.27           C
ANISOU 3314  CE2 TYR D 296    21802  22404  22769  -1158   -931  -2211       C
ATOM   3315  CZ  TYR D 296      -2.767 -75.965 -12.539  1.00174.06           C
ANISOU 3315  CZ  TYR D 296    21588  22114  22435  -1200   -975  -2141       C
ATOM   3316  OH  TYR D 296      -2.568 -75.904 -13.899  1.00181.09           O
ANISOU 3316  OH  TYR D 296    22518  23035  23252  -1249   -975  -2132       O
ATOM   3317  N   PRO D 297      -5.673 -76.217  -5.950  1.00146.12           N
ANISOU 3317  N   PRO D 297    17822  18469  19228   -852  -1050  -2249       N
ATOM   3318  CA  PRO D 297      -5.922 -76.452  -4.532  1.00148.93           C
ANISOU 3318  CA  PRO D 297    18115  18813  19657   -786  -1038  -2260       C
ATOM   3319  C   PRO D 297      -4.721 -77.128  -3.908  1.00130.81           C
ANISOU 3319  C   PRO D 297    15766  16517  17418   -823   -937  -2235       C
ATOM   3320  O   PRO D 297      -3.840 -77.626  -4.613  1.00137.37           O
ANISOU 3320  O   PRO D 297    16596  17364  18234   -895   -866  -2220       O
ATOM   3321  CB  PRO D 297      -7.118 -77.410  -4.541  1.00161.68           C
ANISOU 3321  CB  PRO D 297    19658  20467  21304   -741  -1016  -2326       C
ATOM   3322  CG  PRO D 297      -7.713 -77.270  -5.888  1.00129.33           C
ANISOU 3322  CG  PRO D 297    15612  16389  17139   -769  -1055  -2346       C
ATOM   3323  CD  PRO D 297      -6.558 -77.022  -6.797  1.00111.07           C
ANISOU 3323  CD  PRO D 297    13355  14071  14775   -854  -1029  -2307       C
ATOM   3324  N   ILE D 298      -4.685 -77.133  -2.586  1.00117.60           N
ANISOU 3324  N   ILE D 298    14048  14827  15806   -774   -931  -2229       N
ATOM   3325  CA  ILE D 298      -3.581 -77.745  -1.874  1.00136.78           C
ANISOU 3325  CA  ILE D 298    16421  17254  18294   -807   -837  -2203       C
ATOM   3326  C   ILE D 298      -3.824 -79.241  -1.678  1.00120.04           C
ANISOU 3326  C   ILE D 298    14189  15179  16241   -803   -733  -2255       C
ATOM   3327  O   ILE D 298      -4.786 -79.644  -1.022  1.00140.21           O
ANISOU 3327  O   ILE D 298    16681  17751  18841   -735   -742  -2298       O
ATOM   3328  CB  ILE D 298      -3.382 -77.050  -0.522  1.00143.44           C
ANISOU 3328  CB  ILE D 298    17269  18056  19174   -759   -878  -2170       C
ATOM   3329  CG1 ILE D 298      -4.270 -75.806  -0.449  1.00127.85           C
ANISOU 3329  CG1 ILE D 298    15373  16052  17152   -696  -1010  -2169       C
ATOM   3330  CG2 ILE D 298      -1.939 -76.656  -0.333  1.00137.08           C
ANISOU 3330  CG2 ILE D 298    16499  17219  18366   -823   -852  -2096       C
ATOM   3331  CD1 ILE D 298      -3.790 -74.760   0.529  1.00 93.30           C
ANISOU 3331  CD1 ILE D 298    11049  11621  12780   -670  -1074  -2119       C
ATOM   3332  N   ILE D 299      -2.955 -80.052  -2.270  1.00 94.81           N
ANISOU 3332  N   ILE D 299    10969  12004  13049   -874   -636  -2249       N
ATOM   3333  CA  ILE D 299      -2.993 -81.495  -2.118  1.00116.80           C
ANISOU 3333  CA  ILE D 299    13651  14829  15899   -881   -531  -2293       C
ATOM   3334  C   ILE D 299      -2.087 -81.925  -0.976  1.00125.62           C
ANISOU 3334  C   ILE D 299    14699  15939  17093   -890   -452  -2263       C
ATOM   3335  O   ILE D 299      -2.146 -83.064  -0.506  1.00130.12           O
ANISOU 3335  O   ILE D 299    15167  16538  17733   -884   -370  -2296       O
ATOM   3336  CB  ILE D 299      -2.428 -82.156  -3.374  1.00152.75           C
ANISOU 3336  CB  ILE D 299    18218  19406  20412   -954   -462  -2299       C
ATOM   3337  CG1 ILE D 299      -3.136 -81.634  -4.622  1.00119.16           C
ANISOU 3337  CG1 ILE D 299    14045  15158  16073   -959   -539  -2318       C
ATOM   3338  CG2 ILE D 299      -2.490 -83.679  -3.273  1.00175.67           C
ANISOU 3338  CG2 ILE D 299    21018  22347  23380   -961   -356  -2348       C
ATOM   3339  CD1 ILE D 299      -2.581 -82.245  -5.888  1.00161.16           C
ANISOU 3339  CD1 ILE D 299    19385  20503  21347  -1027   -474  -2324       C
ATOM   3340  N   GLY D 300      -1.264 -80.989  -0.521  1.00120.01           N
ANISOU 3340  N   GLY D 300    14042  15189  16368   -907   -482  -2197       N
ATOM   3341  CA  GLY D 300      -0.163 -81.281   0.382  1.00159.97           C
ANISOU 3341  CA  GLY D 300    19055  20238  21488   -937   -406  -2151       C
ATOM   3342  C   GLY D 300       0.154 -79.973   1.054  1.00149.91           C
ANISOU 3342  C   GLY D 300    17853  18913  20195   -920   -493  -2093       C
ATOM   3343  O   GLY D 300      -0.638 -79.040   0.935  1.00152.29           O
ANISOU 3343  O   GLY D 300    18219  19193  20450   -872   -602  -2103       O
ATOM   3344  N   ASP D 301       1.269 -79.860   1.767  1.00134.16           N
ANISOU 3344  N   ASP D 301    15849  16893  18233   -956   -451  -2030       N
ATOM   3345  CA  ASP D 301       1.469 -78.561   2.380  1.00150.03           C
ANISOU 3345  CA  ASP D 301    17936  18849  20220   -935   -549  -1978       C
ATOM   3346  C   ASP D 301       2.265 -77.693   1.428  1.00121.20           C
ANISOU 3346  C   ASP D 301    14389  15171  16490  -1000   -593  -1910       C
ATOM   3347  O   ASP D 301       3.485 -77.727   1.380  1.00 89.98           O
ANISOU 3347  O   ASP D 301    10444  11207  12539  -1068   -541  -1840       O
ATOM   3348  CB  ASP D 301       2.171 -78.686   3.739  1.00168.79           C
ANISOU 3348  CB  ASP D 301    20260  21204  22668   -934   -505  -1940       C
ATOM   3349  CG  ASP D 301       3.387 -79.587   3.688  1.00191.55           C
ANISOU 3349  CG  ASP D 301    23084  24105  25590  -1015   -376  -1898       C
ATOM   3350  OD1 ASP D 301       3.618 -80.191   2.617  1.00200.62           O
ANISOU 3350  OD1 ASP D 301    24229  25286  26712  -1064   -317  -1907       O
ATOM   3351  OD2 ASP D 301       4.101 -79.693   4.717  1.00174.19           O
ANISOU 3351  OD2 ASP D 301    20846  21889  23448  -1029   -333  -1856       O
ATOM   3352  N   GLU D 302       1.534 -76.847   0.719  1.00128.08           N
ANISOU 3352  N   GLU D 302    15340  16032  17293   -974   -698  -1926       N
ATOM   3353  CA  GLU D 302       2.125 -75.855  -0.146  1.00126.77           C
ANISOU 3353  CA  GLU D 302    15276  15840  17050  -1024   -764  -1862       C
ATOM   3354  C   GLU D 302       2.477 -74.698   0.763  1.00131.95           C
ANISOU 3354  C   GLU D 302    15994  16434  17707  -1005   -853  -1804       C
ATOM   3355  O   GLU D 302       3.581 -74.164   0.715  1.00136.10           O
ANISOU 3355  O   GLU D 302    16567  16930  18215  -1063   -863  -1719       O
ATOM   3356  CB  GLU D 302       1.131 -75.425  -1.238  1.00106.97           C
ANISOU 3356  CB  GLU D 302    12823  13346  14473  -1003   -841  -1905       C
ATOM   3357  CG  GLU D 302       1.150 -76.296  -2.507  1.00150.02           C
ANISOU 3357  CG  GLU D 302    18253  18851  19897  -1051   -768  -1935       C
ATOM   3358  CD  GLU D 302       0.165 -77.466  -2.475  1.00156.97           C
ANISOU 3358  CD  GLU D 302    19047  19774  20818  -1010   -708  -2025       C
ATOM   3359  OE1 GLU D 302      -0.571 -77.651  -3.473  1.00136.03           O
ANISOU 3359  OE1 GLU D 302    16410  17150  18123  -1008   -726  -2071       O
ATOM   3360  OE2 GLU D 302       0.139 -78.214  -1.470  1.00130.82           O
ANISOU 3360  OE2 GLU D 302    15652  16471  17584   -983   -644  -2048       O
ATOM   3361  N   LEU D 303       1.534 -74.361   1.636  1.00130.53           N
ANISOU 3361  N   LEU D 303    15809  16236  17550   -921   -916  -1848       N
ATOM   3362  CA  LEU D 303       1.635 -73.175   2.466  1.00134.14           C
ANISOU 3362  CA  LEU D 303    16337  16633  17999   -886  -1019  -1806       C
ATOM   3363  C   LEU D 303       2.871 -73.205   3.343  1.00128.15           C
ANISOU 3363  C   LEU D 303    15564  15843  17284   -930   -974  -1734       C
ATOM   3364  O   LEU D 303       3.556 -72.195   3.489  1.00 90.32           O
ANISOU 3364  O   LEU D 303    10855  10999  12464   -956  -1048  -1661       O
ATOM   3365  CB  LEU D 303       0.373 -73.017   3.311  1.00126.17           C
ANISOU 3365  CB  LEU D 303    15309  15619  17012   -780  -1074  -1872       C
ATOM   3366  CG  LEU D 303      -0.756 -72.170   2.710  1.00127.44           C
ANISOU 3366  CG  LEU D 303    15541  15772  17109   -725  -1188  -1906       C
ATOM   3367  CD1 LEU D 303      -0.618 -71.983   1.189  1.00116.93           C
ANISOU 3367  CD1 LEU D 303    14260  14458  15710   -790  -1203  -1892       C
ATOM   3368  CD2 LEU D 303      -2.101 -72.770   3.077  1.00112.72           C
ANISOU 3368  CD2 LEU D 303    13607  13946  15275   -638  -1178  -1988       C
ATOM   3369  N   ARG D 304       3.149 -74.364   3.927  1.00147.01           N
ANISOU 3369  N   ARG D 304    17847  18264  19744   -940   -855  -1753       N
ATOM   3370  CA  ARG D 304       4.321 -74.519   4.773  1.00144.49           C
ANISOU 3370  CA  ARG D 304    17503  17922  19474   -986   -798  -1685       C
ATOM   3371  C   ARG D 304       5.573 -74.297   3.941  1.00116.03           C
ANISOU 3371  C   ARG D 304    13947  14308  15831  -1084   -776  -1594       C
ATOM   3372  O   ARG D 304       6.461 -73.537   4.314  1.00105.79           O
ANISOU 3372  O   ARG D 304    12708  12962  14525  -1121   -820  -1508       O
ATOM   3373  CB  ARG D 304       4.320 -75.909   5.397  1.00162.83           C
ANISOU 3373  CB  ARG D 304    19695  20292  21882   -981   -666  -1727       C
ATOM   3374  CG  ARG D 304       3.172 -76.116   6.365  1.00178.23           C
ANISOU 3374  CG  ARG D 304    21589  22253  23879   -882   -687  -1802       C
ATOM   3375  CD  ARG D 304       3.675 -76.029   7.785  1.00191.19           C
ANISOU 3375  CD  ARG D 304    23198  23864  25581   -867   -674  -1769       C
ATOM   3376  NE  ARG D 304       4.563 -77.150   8.057  1.00180.90           N
ANISOU 3376  NE  ARG D 304    21797  22591  24344   -931   -536  -1746       N
ATOM   3377  CZ  ARG D 304       4.175 -78.275   8.644  1.00168.00           C
ANISOU 3377  CZ  ARG D 304    20041  21006  22787   -902   -446  -1800       C
ATOM   3378  NH1 ARG D 304       2.914 -78.419   9.044  1.00171.83           N
ANISOU 3378  NH1 ARG D 304    20485  21513  23289   -808   -483  -1876       N
ATOM   3379  NH2 ARG D 304       5.050 -79.251   8.839  1.00141.62           N
ANISOU 3379  NH2 ARG D 304    16616  17690  19506   -966   -321  -1773       N
ATOM   3380  N   VAL D 305       5.620 -74.954   2.792  1.00110.43           N
ANISOU 3380  N   VAL D 305    13216  13647  15095  -1126   -713  -1611       N
ATOM   3381  CA  VAL D 305       6.740 -74.816   1.877  1.00119.51           C
ANISOU 3381  CA  VAL D 305    14408  14800  16202  -1213   -687  -1527       C
ATOM   3382  C   VAL D 305       6.814 -73.402   1.274  1.00113.89           C
ANISOU 3382  C   VAL D 305    13816  14046  15411  -1223   -824  -1473       C
ATOM   3383  O   VAL D 305       7.881 -72.807   1.215  1.00111.53           O
ANISOU 3383  O   VAL D 305    13568  13717  15093  -1281   -849  -1371       O
ATOM   3384  CB  VAL D 305       6.675 -75.891   0.773  1.00106.80           C
ANISOU 3384  CB  VAL D 305    12747  13254  14578  -1245   -587  -1569       C
ATOM   3385  CG1 VAL D 305       7.757 -75.672  -0.271  1.00 89.00           C
ANISOU 3385  CG1 VAL D 305    10540  11007  12267  -1326   -569  -1481       C
ATOM   3386  CG2 VAL D 305       6.809 -77.270   1.405  1.00108.10           C
ANISOU 3386  CG2 VAL D 305    12793  13455  14824  -1246   -449  -1607       C
ATOM   3387  N   ASN D 306       5.681 -72.863   0.838  1.00120.71           N
ANISOU 3387  N   ASN D 306    14723  14909  16232  -1167   -916  -1535       N
ATOM   3388  CA  ASN D 306       5.642 -71.502   0.305  1.00115.14           C
ANISOU 3388  CA  ASN D 306    14128  14163  15456  -1171  -1053  -1490       C
ATOM   3389  C   ASN D 306       6.198 -70.471   1.268  1.00103.56           C
ANISOU 3389  C   ASN D 306    12723  12626  13999  -1167  -1140  -1417       C
ATOM   3390  O   ASN D 306       6.908 -69.555   0.861  1.00127.96           O
ANISOU 3390  O   ASN D 306    15892  15683  17045  -1214  -1215  -1331       O
ATOM   3391  CB  ASN D 306       4.214 -71.114  -0.094  1.00155.86           C
ANISOU 3391  CB  ASN D 306    19313  19328  20577  -1100  -1136  -1575       C
ATOM   3392  CG  ASN D 306       3.872 -71.540  -1.499  1.00150.07           C
ANISOU 3392  CG  ASN D 306    18574  18649  19796  -1127  -1106  -1608       C
ATOM   3393  OD1 ASN D 306       4.667 -72.216  -2.168  1.00125.12           O
ANISOU 3393  OD1 ASN D 306    15385  15525  16631  -1193  -1015  -1577       O
ATOM   3394  ND2 ASN D 306       2.681 -71.153  -1.960  1.00139.85           N
ANISOU 3394  ND2 ASN D 306    17309  17361  18465  -1076  -1180  -1671       N
ATOM   3395  N   SER D 307       5.853 -70.608   2.543  1.00122.46           N
ANISOU 3395  N   SER D 307    15083  14997  16449  -1110  -1136  -1451       N
ATOM   3396  CA  SER D 307       6.311 -69.664   3.554  1.00110.18           C
ANISOU 3396  CA  SER D 307    13588  13370  14904  -1099  -1221  -1391       C
ATOM   3397  C   SER D 307       7.777 -69.871   3.866  1.00110.41           C
ANISOU 3397  C   SER D 307    13604  13384  14962  -1183  -1158  -1288       C
ATOM   3398  O   SER D 307       8.556 -68.916   3.879  1.00123.68           O
ANISOU 3398  O   SER D 307    15365  15013  16614  -1224  -1239  -1193       O
ATOM   3399  CB  SER D 307       5.492 -69.800   4.831  1.00125.99           C
ANISOU 3399  CB  SER D 307    15554  15358  16957  -1009  -1229  -1460       C
ATOM   3400  OG  SER D 307       6.084 -69.031   5.858  1.00128.79           O
ANISOU 3400  OG  SER D 307    15962  15646  17328  -1006  -1294  -1398       O
ATOM   3401  N   ALA D 308       8.144 -71.124   4.121  1.00123.03           N
ANISOU 3401  N   ALA D 308    15100  15028  16618  -1209  -1014  -1302       N
ATOM   3402  CA  ALA D 308       9.525 -71.482   4.428  1.00132.69           C
ANISOU 3402  CA  ALA D 308    16297  16245  17875  -1290   -934  -1204       C
ATOM   3403  C   ALA D 308      10.461 -70.865   3.408  1.00136.80           C
ANISOU 3403  C   ALA D 308    16887  16756  18334  -1368   -973  -1100       C
ATOM   3404  O   ALA D 308      11.519 -70.346   3.759  1.00133.45           O
ANISOU 3404  O   ALA D 308    16503  16290  17912  -1422   -999   -990       O
ATOM   3405  CB  ALA D 308       9.693 -72.997   4.446  1.00128.34           C
ANISOU 3405  CB  ALA D 308    15624  15757  17381  -1311   -768  -1243       C
ATOM   3406  N   CYS D 309      10.063 -70.928   2.142  1.00138.93           N
ANISOU 3406  N   CYS D 309    17171  17068  18549  -1374   -977  -1131       N
ATOM   3407  CA  CYS D 309      10.847 -70.347   1.063  1.00112.11           C
ANISOU 3407  CA  CYS D 309    13836  13672  15088  -1441  -1017  -1036       C
ATOM   3408  C   CYS D 309      10.893 -68.824   1.144  1.00113.02           C
ANISOU 3408  C   CYS D 309    14063  13720  15159  -1435  -1185   -976       C
ATOM   3409  O   CYS D 309      11.975 -68.254   1.250  1.00146.61           O
ANISOU 3409  O   CYS D 309    18362  17939  19405  -1494  -1221   -856       O
ATOM   3410  CB  CYS D 309      10.347 -70.837  -0.303  1.00105.59           C
ANISOU 3410  CB  CYS D 309    12993  12911  14214  -1445   -978  -1092       C
ATOM   3411  SG  CYS D 309      10.775 -72.578  -0.624  1.00138.98           S
ANISOU 3411  SG  CYS D 309    17106  17216  18484  -1481   -778  -1120       S
ATOM   3412  N   ARG D 310       9.735 -68.168   1.146  1.00 80.79           N
ANISOU 3412  N   ARG D 310    10027   9617  11051  -1363  -1289  -1053       N
ATOM   3413  CA  ARG D 310       9.695 -66.701   1.222  1.00122.37           C
ANISOU 3413  CA  ARG D 310    15403  14817  16275  -1351  -1454  -1003       C
ATOM   3414  C   ARG D 310      10.452 -66.123   2.427  1.00138.69           C
ANISOU 3414  C   ARG D 310    17508  16812  18377  -1363  -1504   -924       C
ATOM   3415  O   ARG D 310      10.867 -64.959   2.405  1.00111.13           O
ANISOU 3415  O   ARG D 310    14109  13263  14851  -1382  -1631   -844       O
ATOM   3416  CB  ARG D 310       8.263 -66.173   1.231  1.00103.51           C
ANISOU 3416  CB  ARG D 310    13049  12416  13862  -1262  -1547  -1106       C
ATOM   3417  CG  ARG D 310       7.447 -66.496   0.005  1.00145.81           C
ANISOU 3417  CG  ARG D 310    18389  17835  19178  -1251  -1529  -1175       C
ATOM   3418  CD  ARG D 310       6.093 -65.832   0.129  1.00159.87           C
ANISOU 3418  CD  ARG D 310    20212  19594  20935  -1164  -1632  -1259       C
ATOM   3419  NE  ARG D 310       5.626 -65.862   1.513  1.00154.11           N
ANISOU 3419  NE  ARG D 310    19469  18829  20257  -1092  -1641  -1305       N
ATOM   3420  CZ  ARG D 310       4.900 -66.842   2.037  1.00131.65           C
ANISOU 3420  CZ  ARG D 310    16541  16021  17459  -1038  -1553  -1394       C
ATOM   3421  NH1 ARG D 310       4.546 -67.883   1.291  1.00119.47           N
ANISOU 3421  NH1 ARG D 310    14925  14548  15919  -1050  -1453  -1449       N
ATOM   3422  NH2 ARG D 310       4.524 -66.779   3.308  1.00119.72           N
ANISOU 3422  NH2 ARG D 310    15020  14477  15990   -970  -1570  -1426       N
ATOM   3423  N   LYS D 311      10.603 -66.918   3.487  1.00128.79           N
ANISOU 3423  N   LYS D 311    16185  15559  17191  -1349  -1411   -947       N
ATOM   3424  CA  LYS D 311      11.439 -66.509   4.611  1.00127.65           C
ANISOU 3424  CA  LYS D 311    16068  15351  17083  -1371  -1441   -866       C
ATOM   3425  C   LYS D 311      12.915 -66.671   4.239  1.00129.95           C
ANISOU 3425  C   LYS D 311    16353  15649  17374  -1477  -1387   -730       C
ATOM   3426  O   LYS D 311      13.702 -65.750   4.429  1.00137.86           O
ANISOU 3426  O   LYS D 311    17431  16592  18359  -1519  -1480   -621       O
ATOM   3427  CB  LYS D 311      11.095 -67.273   5.902  1.00127.79           C
ANISOU 3427  CB  LYS D 311    16011  15370  17174  -1321  -1362   -933       C
ATOM   3428  CG  LYS D 311      11.439 -66.500   7.194  1.00152.56           C
ANISOU 3428  CG  LYS D 311    19205  18425  20335  -1304  -1446   -885       C
ATOM   3429  CD  LYS D 311      10.854 -67.150   8.459  1.00148.90           C
ANISOU 3429  CD  LYS D 311    18670  17966  19938  -1234  -1385   -969       C
ATOM   3430  CE  LYS D 311      10.802 -66.167   9.638  1.00135.45           C
ANISOU 3430  CE  LYS D 311    17046  16179  18240  -1187  -1503   -950       C
ATOM   3431  NZ  LYS D 311       9.826 -65.044   9.408  1.00 99.14           N
ANISOU 3431  NZ  LYS D 311    12546  11541  13581  -1111  -1655   -998       N
ATOM   3432  N   VAL D 312      13.284 -67.829   3.693  1.00114.22           N
ANISOU 3432  N   VAL D 312    14274  13727  15399  -1519  -1240   -734       N
ATOM   3433  CA  VAL D 312      14.676 -68.083   3.310  1.00115.76           C
ANISOU 3433  CA  VAL D 312    14454  13935  15593  -1616  -1174   -603       C
ATOM   3434  C   VAL D 312      15.069 -67.223   2.119  1.00129.72           C
ANISOU 3434  C   VAL D 312    16298  15704  17286  -1658  -1266   -520       C
ATOM   3435  O   VAL D 312      16.220 -66.804   1.995  1.00111.62           O
ANISOU 3435  O   VAL D 312    14038  13390  14981  -1730  -1289   -382       O
ATOM   3436  CB  VAL D 312      14.930 -69.566   2.957  1.00113.90           C
ANISOU 3436  CB  VAL D 312    14107  13778  15390  -1644   -991   -633       C
ATOM   3437  CG1 VAL D 312      16.354 -69.775   2.421  1.00 81.53           C
ANISOU 3437  CG1 VAL D 312     9999   9699  11279  -1739   -926   -491       C
ATOM   3438  CG2 VAL D 312      14.692 -70.442   4.164  1.00104.97           C
ANISOU 3438  CG2 VAL D 312    12893  12650  14342  -1612   -897   -698       C
ATOM   3439  N   GLN D 313      14.108 -66.965   1.240  1.00141.35           N
ANISOU 3439  N   GLN D 313    17794  17202  18709  -1616  -1318   -601       N
ATOM   3440  CA  GLN D 313      14.344 -66.054   0.139  1.00159.42           C
ANISOU 3440  CA  GLN D 313    20155  19491  20927  -1649  -1420   -531       C
ATOM   3441  C   GLN D 313      14.812 -64.726   0.702  1.00150.15           C
ANISOU 3441  C   GLN D 313    19076  18231  19741  -1663  -1573   -434       C
ATOM   3442  O   GLN D 313      15.916 -64.273   0.409  1.00158.24           O
ANISOU 3442  O   GLN D 313    20135  19242  20749  -1733  -1606   -296       O
ATOM   3443  CB  GLN D 313      13.066 -65.821  -0.670  1.00201.98           C
ANISOU 3443  CB  GLN D 313    25565  24908  26271  -1590  -1475   -642       C
ATOM   3444  CG  GLN D 313      12.602 -66.993  -1.527  1.00234.75           C
ANISOU 3444  CG  GLN D 313    29636  29142  30414  -1584  -1347   -728       C
ATOM   3445  CD  GLN D 313      12.066 -66.528  -2.868  1.00222.37           C
ANISOU 3445  CD  GLN D 313    28107  27608  28775  -1581  -1411   -750       C
ATOM   3446  OE1 GLN D 313      12.123 -65.333  -3.186  1.00161.12           O
ANISOU 3446  OE1 GLN D 313    20430  19814  20974  -1590  -1549   -693       O
ATOM   3447  NE2 GLN D 313      11.562 -67.467  -3.671  1.00243.44           N
ANISOU 3447  NE2 GLN D 313    30719  30347  31430  -1572  -1315   -830       N
ATOM   3448  N   HIS D 314      13.984 -64.117   1.545  1.00126.16           N
ANISOU 3448  N   HIS D 314    16083  15135  16716  -1593  -1667   -503       N
ATOM   3449  CA  HIS D 314      14.261 -62.759   2.005  1.00119.09           C
ANISOU 3449  CA  HIS D 314    15292  14154  15803  -1595  -1832   -427       C
ATOM   3450  C   HIS D 314      15.522 -62.620   2.864  1.00115.61           C
ANISOU 3450  C   HIS D 314    14865  13663  15399  -1657  -1831   -298       C
ATOM   3451  O   HIS D 314      16.119 -61.551   2.932  1.00 91.86           O
ANISOU 3451  O   HIS D 314    11942  10593  12368  -1690  -1959   -192       O
ATOM   3452  CB  HIS D 314      13.050 -62.171   2.719  1.00100.89           C
ANISOU 3452  CB  HIS D 314    13034  11800  13499  -1499  -1929   -535       C
ATOM   3453  CG  HIS D 314      13.354 -60.924   3.490  1.00104.51           C
ANISOU 3453  CG  HIS D 314    13595  12161  13952  -1493  -2084   -466       C
ATOM   3454  ND1 HIS D 314      12.770 -59.707   3.201  1.00122.69           N
ANISOU 3454  ND1 HIS D 314    15992  14417  16206  -1456  -2246   -476       N
ATOM   3455  CD2 HIS D 314      14.175 -60.709   4.538  1.00 85.03           C
ANISOU 3455  CD2 HIS D 314    11152   9632  11521  -1520  -2103   -387       C
ATOM   3456  CE1 HIS D 314      13.221 -58.798   4.045  1.00141.38           C
ANISOU 3456  CE1 HIS D 314    18441  16696  18580  -1458  -2361   -407       C
ATOM   3457  NE2 HIS D 314      14.075 -59.375   4.867  1.00139.01           N
ANISOU 3457  NE2 HIS D 314    18102  16384  18330  -1497  -2279   -351       N
ATOM   3458  N   MET D 315      15.932 -63.689   3.529  1.00149.74           N
ANISOU 3458  N   MET D 315    19106  18010  19780  -1673  -1689   -304       N
ATOM   3459  CA  MET D 315      17.150 -63.611   4.326  1.00139.86           C
ANISOU 3459  CA  MET D 315    17861  16713  18565  -1738  -1679   -176       C
ATOM   3460  C   MET D 315      18.381 -63.611   3.423  1.00139.55           C
ANISOU 3460  C   MET D 315    17820  16704  18498  -1834  -1653    -27       C
ATOM   3461  O   MET D 315      19.238 -62.741   3.568  1.00173.89           O
ANISOU 3461  O   MET D 315    22238  20997  22834  -1885  -1753    107       O
ATOM   3462  CB  MET D 315      17.204 -64.703   5.416  1.00139.22           C
ANISOU 3462  CB  MET D 315    17692  16646  18560  -1726  -1540   -225       C
ATOM   3463  CG  MET D 315      18.400 -65.659   5.352  1.00152.76           C
ANISOU 3463  CG  MET D 315    19329  18403  20310  -1811  -1392   -128       C
ATOM   3464  SD  MET D 315      19.600 -65.440   6.692  1.00143.77           S
ANISOU 3464  SD  MET D 315    18207  17193  19226  -1871  -1399      4       S
ATOM   3465  CE  MET D 315      18.839 -64.026   7.506  1.00 92.00           C
ANISOU 3465  CE  MET D 315    11771  10535  12651  -1798  -1603    -37       C
ATOM   3466  N   VAL D 316      18.465 -64.545   2.473  1.00124.41           N
ANISOU 3466  N   VAL D 316    15828  14872  16568  -1856  -1526    -46       N
ATOM   3467  CA  VAL D 316      19.694 -64.662   1.673  1.00127.52           C
ANISOU 3467  CA  VAL D 316    16211  15302  16938  -1944  -1484    102       C
ATOM   3468  C   VAL D 316      19.853 -63.548   0.651  1.00113.97           C
ANISOU 3468  C   VAL D 316    14574  13577  15151  -1966  -1624    181       C
ATOM   3469  O   VAL D 316      20.959 -63.289   0.199  1.00132.71           O
ANISOU 3469  O   VAL D 316    16962  15958  17505  -2038  -1636    332       O
ATOM   3470  CB  VAL D 316      19.852 -66.014   0.949  1.00 97.16           C
ANISOU 3470  CB  VAL D 316    12265  11552  13097  -1963  -1302     69       C
ATOM   3471  CG1 VAL D 316      19.994 -67.146   1.937  1.00112.00           C
ANISOU 3471  CG1 VAL D 316    14059  13443  15053  -1961  -1155     27       C
ATOM   3472  CG2 VAL D 316      18.681 -66.253   0.037  1.00153.69           C
ANISOU 3472  CG2 VAL D 316    19412  18764  20219  -1904  -1295    -69       C
ATOM   3473  N   VAL D 317      18.763 -62.890   0.279  1.00 93.63           N
ANISOU 3473  N   VAL D 317    12047  10989  12538  -1905  -1730     84       N
ATOM   3474  CA  VAL D 317      18.889 -61.730  -0.598  1.00135.34           C
ANISOU 3474  CA  VAL D 317    17407  16257  17759  -1926  -1878    161       C
ATOM   3475  C   VAL D 317      19.324 -60.504   0.222  1.00143.81           C
ANISOU 3475  C   VAL D 317    18574  17228  18838  -1940  -2040    256       C
ATOM   3476  O   VAL D 317      20.432 -59.994   0.025  1.00150.15           O
ANISOU 3476  O   VAL D 317    19408  18013  19629  -2012  -2094    417       O
ATOM   3477  CB  VAL D 317      17.633 -61.497  -1.505  1.00143.57           C
ANISOU 3477  CB  VAL D 317    18463  17334  18754  -1866  -1926     36       C
ATOM   3478  CG1 VAL D 317      16.383 -61.297  -0.671  1.00183.16           C
ANISOU 3478  CG1 VAL D 317    23500  22303  23790  -1778  -1975   -108       C
ATOM   3479  CG2 VAL D 317      17.845 -60.321  -2.452  1.00 98.92           C
ANISOU 3479  CG2 VAL D 317    12879  11669  13038  -1895  -2075    125       C
ATOM   3480  N   LYS D 318      18.491 -60.075   1.174  1.00 87.21           N
ANISOU 3480  N   LYS D 318    11449   9995  11692  -1873  -2114    162       N
ATOM   3481  CA  LYS D 318      18.843 -58.945   2.045  1.00132.43           C
ANISOU 3481  CA  LYS D 318    17271  15620  17426  -1879  -2268    239       C
ATOM   3482  C   LYS D 318      20.261 -59.072   2.646  1.00121.53           C
ANISOU 3482  C   LYS D 318    15886  14210  16081  -1961  -2236    398       C
ATOM   3483  O   LYS D 318      20.936 -58.072   2.877  1.00100.25           O
ANISOU 3483  O   LYS D 318    13269  11445  13374  -2002  -2371    522       O
ATOM   3484  CB  LYS D 318      17.782 -58.752   3.147  1.00145.56           C
ANISOU 3484  CB  LYS D 318    18965  17226  19116  -1787  -2312    106       C
ATOM   3485  CG  LYS D 318      18.154 -57.771   4.279  1.00144.79           C
ANISOU 3485  CG  LYS D 318    18960  17018  19035  -1786  -2448    172       C
ATOM   3486  CD  LYS D 318      16.934 -57.425   5.171  1.00175.14           C
ANISOU 3486  CD  LYS D 318    22847  20811  22888  -1680  -2512     31       C
ATOM   3487  CE  LYS D 318      16.968 -58.108   6.552  1.00159.42           C
ANISOU 3487  CE  LYS D 318    20815  18796  20960  -1653  -2424    -12       C
ATOM   3488  NZ  LYS D 318      15.684 -57.963   7.335  1.00120.02           N
ANISOU 3488  NZ  LYS D 318    15846  13778  15977  -1539  -2460   -162       N
ATOM   3489  N   SER D 319      20.705 -60.306   2.879  1.00 97.44           N
ANISOU 3489  N   SER D 319    12740  11212  13071  -1988  -2060    397       N
ATOM   3490  CA  SER D 319      22.027 -60.584   3.439  1.00133.11           C
ANISOU 3490  CA  SER D 319    17239  15712  17627  -2068  -2005    543       C
ATOM   3491  C   SER D 319      23.182 -60.282   2.492  1.00157.95           C
ANISOU 3491  C   SER D 319    20393  18885  20735  -2155  -2027    721       C
ATOM   3492  O   SER D 319      24.144 -59.611   2.872  1.00156.05           O
ANISOU 3492  O   SER D 319    20206  18586  20500  -2215  -2113    874       O
ATOM   3493  CB  SER D 319      22.123 -62.047   3.898  1.00144.45           C
ANISOU 3493  CB  SER D 319    18562  17204  19118  -2070  -1801    486       C
ATOM   3494  OG  SER D 319      21.417 -62.261   5.111  1.00137.93           O
ANISOU 3494  OG  SER D 319    17729  16337  18341  -2008  -1788    372       O
ATOM   3495  N   ALA D 320      23.095 -60.804   1.272  1.00184.55           N
ANISOU 3495  N   ALA D 320    23709  22343  24067  -2162  -1949    704       N
ATOM   3496  CA  ALA D 320      24.139 -60.602   0.268  1.00184.90           C
ANISOU 3496  CA  ALA D 320    23752  22429  24071  -2236  -1957    867       C
ATOM   3497  C   ALA D 320      24.214 -59.139  -0.151  1.00174.91           C
ANISOU 3497  C   ALA D 320    22586  21112  22760  -2248  -2165    953       C
ATOM   3498  O   ALA D 320      25.297 -58.627  -0.447  1.00152.25           O
ANISOU 3498  O   ALA D 320    19742  18232  19874  -2319  -2226   1132       O
ATOM   3499  CB  ALA D 320      23.900 -61.495  -0.946  1.00159.68           C
ANISOU 3499  CB  ALA D 320    20483  19344  20844  -2228  -1828    810       C
ATOM   3500  N   LEU D 321      23.055 -58.483  -0.180  1.00146.20           N
ANISOU 3500  N   LEU D 321    19003  17443  19104  -2178  -2274    828       N
ATOM   3501  CA  LEU D 321      22.965 -57.053  -0.452  1.00125.36           C
ANISOU 3501  CA  LEU D 321    16462  14744  16426  -2179  -2481    887       C
ATOM   3502  C   LEU D 321      23.765 -56.247   0.554  1.00147.73           C
ANISOU 3502  C   LEU D 321    19369  17476  19285  -2220  -2599   1016       C
ATOM   3503  O   LEU D 321      24.409 -55.257   0.217  1.00140.89           O
ANISOU 3503  O   LEU D 321    18564  16575  18393  -2267  -2740   1157       O
ATOM   3504  CB  LEU D 321      21.519 -56.592  -0.371  1.00100.42           C
ANISOU 3504  CB  LEU D 321    13345  11557  13252  -2089  -2561    716       C
ATOM   3505  CG  LEU D 321      20.646 -56.990  -1.551  1.00129.49           C
ANISOU 3505  CG  LEU D 321    16981  15327  16894  -2052  -2505    604       C
ATOM   3506  CD1 LEU D 321      19.323 -56.235  -1.508  1.00127.25           C
ANISOU 3506  CD1 LEU D 321    16757  15003  16589  -1972  -2624    472       C
ATOM   3507  CD2 LEU D 321      21.395 -56.679  -2.826  1.00144.99           C
ANISOU 3507  CD2 LEU D 321    18937  17345  18808  -2115  -2536    737       C
ATOM   3508  N   LEU D 322      23.698 -56.667   1.808  1.00160.08           N
ANISOU 3508  N   LEU D 322    20927  18993  20903  -2200  -2544    965       N
ATOM   3509  CA  LEU D 322      24.441 -56.002   2.859  1.00130.45           C
ANISOU 3509  CA  LEU D 322    17243  15142  17178  -2238  -2644   1079       C
ATOM   3510  C   LEU D 322      25.935 -56.267   2.741  1.00115.60           C
ANISOU 3510  C   LEU D 322    15332  13280  15311  -2340  -2592   1279       C
ATOM   3511  O   LEU D 322      26.736 -55.341   2.853  1.00143.85           O
ANISOU 3511  O   LEU D 322    18980  16797  18879  -2395  -2730   1437       O
ATOM   3512  CB  LEU D 322      23.919 -56.419   4.237  1.00123.39           C
ANISOU 3512  CB  LEU D 322    16347  14199  16338  -2185  -2594    964       C
ATOM   3513  CG  LEU D 322      22.903 -55.447   4.852  1.00141.21           C
ANISOU 3513  CG  LEU D 322    18698  16370  18584  -2103  -2750    858       C
ATOM   3514  CD1 LEU D 322      21.655 -55.276   3.977  1.00104.58           C
ANISOU 3514  CD1 LEU D 322    14060  11775  13902  -2030  -2777    716       C
ATOM   3515  CD2 LEU D 322      22.540 -55.875   6.274  1.00133.92           C
ANISOU 3515  CD2 LEU D 322    17769  15401  17715  -2055  -2697    766       C
ATOM   3516  N   ALA D 323      26.309 -57.522   2.506  1.00116.01           N
ANISOU 3516  N   ALA D 323    15280  13415  15382  -2364  -2397   1278       N
ATOM   3517  CA  ALA D 323      27.719 -57.920   2.551  1.00157.90           C
ANISOU 3517  CA  ALA D 323    20548  18740  20706  -2457  -2323   1464       C
ATOM   3518  C   ALA D 323      28.537 -57.285   1.435  1.00174.81           C
ANISOU 3518  C   ALA D 323    22711  20912  22798  -2518  -2406   1637       C
ATOM   3519  O   ALA D 323      29.620 -56.728   1.662  1.00172.36           O
ANISOU 3519  O   ALA D 323    22439  20558  22492  -2590  -2485   1825       O
ATOM   3520  CB  ALA D 323      27.846 -59.431   2.485  1.00139.14           C
ANISOU 3520  CB  ALA D 323    18054  16451  18361  -2461  -2091   1411       C
ATOM   3521  N   ASP D 324      28.027 -57.438   0.221  1.00159.12           N
ANISOU 3521  N   ASP D 324    20691  19004  20762  -2490  -2379   1575       N
ATOM   3522  CA  ASP D 324      28.688 -56.950  -0.977  1.00119.73           C
ANISOU 3522  CA  ASP D 324    15707  14064  15721  -2537  -2441   1721       C
ATOM   3523  C   ASP D 324      28.140 -55.605  -1.516  1.00125.12           C
ANISOU 3523  C   ASP D 324    16474  14707  16358  -2513  -2651   1716       C
ATOM   3524  O   ASP D 324      28.499 -55.168  -2.601  1.00129.03           O
ANISOU 3524  O   ASP D 324    16969  15249  16807  -2542  -2709   1815       O
ATOM   3525  CB  ASP D 324      28.779 -58.084  -2.002  1.00 94.29           C
ANISOU 3525  CB  ASP D 324    12385  10966  12476  -2538  -2259   1695       C
ATOM   3526  CG  ASP D 324      29.583 -59.297  -1.462  1.00143.69           C
ANISOU 3526  CG  ASP D 324    18563  17255  18778  -2578  -2067   1745       C
ATOM   3527  OD1 ASP D 324      29.012 -60.155  -0.756  1.00138.20           O
ANISOU 3527  OD1 ASP D 324    17824  16558  18125  -2538  -1948   1602       O
ATOM   3528  OD2 ASP D 324      30.798 -59.391  -1.737  1.00129.81           O
ANISOU 3528  OD2 ASP D 324    16783  15525  17014  -2649  -2035   1934       O
ATOM   3529  N   LYS D 325      27.226 -54.999  -0.755  1.00147.24           N
ANISOU 3529  N   LYS D 325    19345  17426  19175  -2456  -2756   1595       N
ATOM   3530  CA  LYS D 325      26.724 -53.620  -0.951  1.00143.35           C
ANISOU 3530  CA  LYS D 325    18948  16868  18651  -2432  -2972   1593       C
ATOM   3531  C   LYS D 325      26.217 -53.279  -2.351  1.00138.68           C
ANISOU 3531  C   LYS D 325    18345  16347  18001  -2414  -3017   1564       C
ATOM   3532  O   LYS D 325      26.208 -52.107  -2.741  1.00145.48           O
ANISOU 3532  O   LYS D 325    19274  17169  18833  -2423  -3198   1629       O
ATOM   3533  CB  LYS D 325      27.767 -52.573  -0.529  1.00141.72           C
ANISOU 3533  CB  LYS D 325    18820  16577  18451  -2500  -3137   1793       C
ATOM   3534  CG  LYS D 325      28.163 -52.606   0.943  1.00138.07           C
ANISOU 3534  CG  LYS D 325    18397  16022  18043  -2515  -3142   1821       C
ATOM   3535  CD  LYS D 325      28.938 -51.353   1.316  1.00169.06           C
ANISOU 3535  CD  LYS D 325    22420  19848  21965  -2570  -3347   1994       C
ATOM   3536  CE  LYS D 325      29.754 -51.551   2.589  1.00168.97           C
ANISOU 3536  CE  LYS D 325    22429  19765  22006  -2616  -3324   2084       C
ATOM   3537  NZ  LYS D 325      30.890 -52.495   2.398  1.00144.71           N
ANISOU 3537  NZ  LYS D 325    19268  16763  18952  -2692  -3166   2222       N
ATOM   3538  N   PHE D 326      25.737 -54.288  -3.072  1.00132.74           N
ANISOU 3538  N   PHE D 326    17509  15693  17233  -2385  -2859   1457       N
ATOM   3539  CA  PHE D 326      25.396 -54.146  -4.482  1.00153.04           C
ANISOU 3539  CA  PHE D 326    20054  18345  19747  -2377  -2873   1442       C
ATOM   3540  C   PHE D 326      24.507 -52.931  -4.750  1.00179.45           C
ANISOU 3540  C   PHE D 326    23477  21642  23064  -2336  -3061   1382       C
ATOM   3541  O   PHE D 326      23.432 -52.803  -4.171  1.00170.79           O
ANISOU 3541  O   PHE D 326    22414  20498  21981  -2268  -3088   1224       O
ATOM   3542  CB  PHE D 326      24.715 -55.422  -4.967  1.00140.52           C
ANISOU 3542  CB  PHE D 326    18381  16853  18156  -2334  -2681   1289       C
ATOM   3543  CG  PHE D 326      25.636 -56.608  -5.047  1.00160.06           C
ANISOU 3543  CG  PHE D 326    20773  19396  20647  -2378  -2495   1361       C
ATOM   3544  CD1 PHE D 326      26.895 -56.488  -5.624  1.00178.19           C
ANISOU 3544  CD1 PHE D 326    23052  21730  22923  -2451  -2498   1562       C
ATOM   3545  CD2 PHE D 326      25.244 -57.845  -4.547  1.00139.12           C
ANISOU 3545  CD2 PHE D 326    18058  16772  18031  -2345  -2318   1233       C
ATOM   3546  CE1 PHE D 326      27.746 -57.580  -5.706  1.00180.35           C
ANISOU 3546  CE1 PHE D 326    23250  22067  23208  -2488  -2324   1632       C
ATOM   3547  CE2 PHE D 326      26.087 -58.945  -4.623  1.00131.55           C
ANISOU 3547  CE2 PHE D 326    17021  15874  17087  -2385  -2146   1298       C
ATOM   3548  CZ  PHE D 326      27.341 -58.811  -5.202  1.00169.65           C
ANISOU 3548  CZ  PHE D 326    21834  20737  21890  -2456  -2147   1497       C
ATOM   3549  N   PRO D 327      24.971 -52.030  -5.632  1.00193.57           N
ANISOU 3549  N   PRO D 327    25290  23443  24813  -2377  -3192   1513       N
ATOM   3550  CA  PRO D 327      24.302 -50.765  -5.960  1.00183.28           C
ANISOU 3550  CA  PRO D 327    24060  22093  23482  -2351  -3386   1488       C
ATOM   3551  C   PRO D 327      23.014 -50.983  -6.747  1.00183.95           C
ANISOU 3551  C   PRO D 327    24119  22239  23537  -2287  -3348   1311       C
ATOM   3552  O   PRO D 327      22.050 -50.231  -6.596  1.00183.44           O
ANISOU 3552  O   PRO D 327    24113  22121  23465  -2235  -3464   1211       O
ATOM   3553  CB  PRO D 327      25.339 -50.047  -6.825  1.00168.44           C
ANISOU 3553  CB  PRO D 327    22184  20242  21573  -2424  -3492   1696       C
ATOM   3554  CG  PRO D 327      26.069 -51.153  -7.497  1.00157.85           C
ANISOU 3554  CG  PRO D 327    20747  19010  20219  -2461  -3313   1761       C
ATOM   3555  CD  PRO D 327      26.154 -52.258  -6.482  1.00179.62           C
ANISOU 3555  CD  PRO D 327    23472  21754  23024  -2449  -3147   1693       C
ATOM   3556  N   VAL D 328      23.015 -52.007  -7.593  1.00177.10           N
ANISOU 3556  N   VAL D 328    23164  21480  22648  -2290  -3186   1276       N
ATOM   3557  CA  VAL D 328      21.864 -52.327  -8.425  1.00178.70           C
ANISOU 3557  CA  VAL D 328    23333  21747  22818  -2236  -3136   1117       C
ATOM   3558  C   VAL D 328      21.552 -53.817  -8.300  1.00148.30           C
ANISOU 3558  C   VAL D 328    19405  17959  18985  -2208  -2918    996       C
ATOM   3559  O   VAL D 328      22.442 -54.624  -8.028  1.00147.48           O
ANISOU 3559  O   VAL D 328    19254  17879  18901  -2245  -2796   1070       O
ATOM   3560  CB  VAL D 328      22.122 -51.972  -9.906  1.00226.72           C
ANISOU 3560  CB  VAL D 328    29386  27914  28844  -2270  -3178   1201       C
ATOM   3561  CG1 VAL D 328      22.813 -50.615 -10.020  1.00231.64           C
ANISOU 3561  CG1 VAL D 328    30071  28484  29457  -2318  -3380   1371       C
ATOM   3562  CG2 VAL D 328      22.962 -53.045 -10.581  1.00241.87           C
ANISOU 3562  CG2 VAL D 328    31219  29935  30747  -2309  -3010   1274       C
ATOM   3563  N   LEU D 329      20.289 -54.186  -8.482  1.00120.99           N
ANISOU 3563  N   LEU D 329    15931  14522  15518  -2142  -2870    814       N
ATOM   3564  CA  LEU D 329      19.906 -55.595  -8.382  1.00133.24           C
ANISOU 3564  CA  LEU D 329    17409  16130  17087  -2112  -2673    692       C
ATOM   3565  C   LEU D 329      18.913 -56.027  -9.460  1.00154.23           C
ANISOU 3565  C   LEU D 329    20027  18869  19705  -2075  -2615    563       C
ATOM   3566  O   LEU D 329      17.838 -55.428  -9.624  1.00118.70           O
ANISOU 3566  O   LEU D 329    15565  14347  15190  -2028  -2706    463       O
ATOM   3567  CB  LEU D 329      19.346 -55.908  -6.987  1.00165.37           C
ANISOU 3567  CB  LEU D 329    21495  20127  21211  -2062  -2641    582       C
ATOM   3568  CG  LEU D 329      18.638 -57.252  -6.766  1.00166.67           C
ANISOU 3568  CG  LEU D 329    21589  20339  21400  -2015  -2462    425       C
ATOM   3569  CD1 LEU D 329      18.760 -57.703  -5.325  1.00133.09           C
ANISOU 3569  CD1 LEU D 329    17332  16025  17209  -1998  -2405    396       C
ATOM   3570  CD2 LEU D 329      17.172 -57.189  -7.172  1.00199.19           C
ANISOU 3570  CD2 LEU D 329    25713  24473  25496  -1945  -2483    258       C
ATOM   3571  N   HIS D 330      19.279 -57.084 -10.181  1.00179.97           N
ANISOU 3571  N   HIS D 330    23213  22220  22948  -2094  -2461    567       N
ATOM   3572  CA  HIS D 330      18.433 -57.643 -11.230  1.00182.39           C
ANISOU 3572  CA  HIS D 330    23477  22607  23214  -2064  -2389    450       C
ATOM   3573  C   HIS D 330      17.629 -58.833 -10.699  1.00168.60           C
ANISOU 3573  C   HIS D 330    21686  20872  21501  -2012  -2241    285       C
ATOM   3574  O   HIS D 330      18.195 -59.746 -10.091  1.00153.74           O
ANISOU 3574  O   HIS D 330    19762  18995  19657  -2024  -2115    298       O
ATOM   3575  CB  HIS D 330      19.287 -58.098 -12.424  1.00180.70           C
ANISOU 3575  CB  HIS D 330    23212  22491  22955  -2112  -2311    551       C
ATOM   3576  CG  HIS D 330      20.277 -57.076 -12.904  1.00193.62           C
ANISOU 3576  CG  HIS D 330    24878  24126  24564  -2169  -2437    739       C
ATOM   3577  ND1 HIS D 330      19.915 -55.789 -13.248  1.00197.38           N
ANISOU 3577  ND1 HIS D 330    25410  24568  25016  -2169  -2618    767       N
ATOM   3578  CD2 HIS D 330      21.608 -57.165 -13.124  1.00192.26           C
ANISOU 3578  CD2 HIS D 330    24684  23984  24383  -2227  -2409    913       C
ATOM   3579  CE1 HIS D 330      20.989 -55.126 -13.642  1.00201.53           C
ANISOU 3579  CE1 HIS D 330    25945  25104  25523  -2226  -2700    950       C
ATOM   3580  NE2 HIS D 330      22.030 -55.936 -13.578  1.00194.22           N
ANISOU 3580  NE2 HIS D 330    24973  24218  24605  -2262  -2576   1044       N
ATOM   3581  N   ASP D 331      16.314 -58.827 -10.915  1.00165.06           N
ANISOU 3581  N   ASP D 331    21245  20429  21043  -1955  -2259    134       N
ATOM   3582  CA  ASP D 331      15.506 -60.012 -10.619  1.00177.29           C
ANISOU 3582  CA  ASP D 331    22742  22003  22617  -1907  -2118    -20       C
ATOM   3583  C   ASP D 331      14.956 -60.609 -11.920  1.00176.05           C
ANISOU 3583  C   ASP D 331    22544  21937  22411  -1900  -2046    -94       C
ATOM   3584  O   ASP D 331      14.024 -60.070 -12.535  1.00142.99           O
ANISOU 3584  O   ASP D 331    18381  17758  18190  -1874  -2126   -162       O
ATOM   3585  CB  ASP D 331      14.364 -59.669  -9.657  1.00180.42           C
ANISOU 3585  CB  ASP D 331    23175  22330  23048  -1840  -2182   -143       C
ATOM   3586  CG  ASP D 331      13.702 -60.907  -9.065  1.00179.71           C
ANISOU 3586  CG  ASP D 331    23027  22256  22998  -1793  -2039   -279       C
ATOM   3587  OD1 ASP D 331      14.185 -62.039  -9.311  1.00170.59           O
ANISOU 3587  OD1 ASP D 331    21806  21159  21851  -1815  -1889   -277       O
ATOM   3588  OD2 ASP D 331      12.701 -60.744  -8.336  1.00172.42           O
ANISOU 3588  OD2 ASP D 331    22124  21288  22101  -1731  -2078   -384       O
ATOM   3589  N   ILE D 332      15.529 -61.742 -12.317  1.00180.25           N
ANISOU 3589  N   ILE D 332    23013  22536  22939  -1923  -1892    -81       N
ATOM   3590  CA  ILE D 332      15.176 -62.393 -13.569  1.00163.51           C
ANISOU 3590  CA  ILE D 332    20854  20503  20769  -1920  -1814   -139       C
ATOM   3591  C   ILE D 332      14.182 -63.506 -13.275  1.00150.72           C
ANISOU 3591  C   ILE D 332    19193  18898  19177  -1869  -1699   -305       C
ATOM   3592  O   ILE D 332      14.522 -64.497 -12.637  1.00179.08           O
ANISOU 3592  O   ILE D 332    22740  22492  22812  -1867  -1574   -324       O
ATOM   3593  CB  ILE D 332      16.416 -63.004 -14.249  1.00157.30           C
ANISOU 3593  CB  ILE D 332    20026  19785  19956  -1972  -1711    -23       C
ATOM   3594  CG1 ILE D 332      17.693 -62.287 -13.805  1.00126.49           C
ANISOU 3594  CG1 ILE D 332    16148  15845  16065  -2023  -1778    157       C
ATOM   3595  CG2 ILE D 332      16.278 -62.953 -15.762  1.00177.69           C
ANISOU 3595  CG2 ILE D 332    22600  22449  22465  -1983  -1716    -19       C
ATOM   3596  CD1 ILE D 332      17.830 -60.903 -14.378  1.00127.93           C
ANISOU 3596  CD1 ILE D 332    16384  16015  16208  -2047  -1951    253       C
ATOM   3597  N   GLY D 333      12.962 -63.349 -13.768  1.00122.69           N
ANISOU 3597  N   GLY D 333    15655  15359  15603  -1830  -1741   -420       N
ATOM   3598  CA  GLY D 333      11.879 -64.265 -13.460  1.00134.43           C
ANISOU 3598  CA  GLY D 333    17108  16853  17117  -1777  -1658   -577       C
ATOM   3599  C   GLY D 333      10.823 -63.755 -12.498  1.00141.77           C
ANISOU 3599  C   GLY D 333    18069  17714  18084  -1721  -1741   -664       C
ATOM   3600  O   GLY D 333      10.006 -64.539 -12.021  1.00161.53           O
ANISOU 3600  O   GLY D 333    20537  20216  20619  -1675  -1671   -782       O
ATOM   3601  N   ASN D 334      10.828 -62.453 -12.213  1.00141.40           N
ANISOU 3601  N   ASN D 334    18085  17609  18031  -1721  -1893   -606       N
ATOM   3602  CA  ASN D 334       9.761 -61.858 -11.405  1.00180.44           C
ANISOU 3602  CA  ASN D 334    23068  22489  23000  -1661  -1985   -689       C
ATOM   3603  C   ASN D 334       8.775 -61.052 -12.249  1.00182.94           C
ANISOU 3603  C   ASN D 334    23423  22815  23269  -1641  -2094   -735       C
ATOM   3604  O   ASN D 334       9.066 -59.924 -12.642  1.00190.25           O
ANISOU 3604  O   ASN D 334    24400  23722  24165  -1667  -2220   -652       O
ATOM   3605  CB  ASN D 334      10.361 -60.962 -10.311  1.00212.80           C
ANISOU 3605  CB  ASN D 334    27218  26503  27132  -1664  -2083   -603       C
ATOM   3606  CG  ASN D 334       9.303 -60.211  -9.506  1.00213.42           C
ANISOU 3606  CG  ASN D 334    27348  26513  27228  -1598  -2191   -679       C
ATOM   3607  OD1 ASN D 334       8.182 -60.685  -9.335  1.00228.48           O
ANISOU 3607  OD1 ASN D 334    29234  28431  29148  -1540  -2154   -803       O
ATOM   3608  ND2 ASN D 334       9.664 -59.031  -9.006  1.00185.72           N
ANISOU 3608  ND2 ASN D 334    23909  22934  23722  -1604  -2329   -600       N
ATOM   3609  N   PRO D 335       7.593 -61.632 -12.512  1.00185.38           N
ANISOU 3609  N   PRO D 335    23707  23154  23574  -1597  -2047   -863       N
ATOM   3610  CA  PRO D 335       6.471 -60.994 -13.208  1.00174.01           C
ANISOU 3610  CA  PRO D 335    22297  21723  22095  -1571  -2137   -925       C
ATOM   3611  C   PRO D 335       5.801 -59.912 -12.370  1.00158.46           C
ANISOU 3611  C   PRO D 335    20389  19675  20143  -1522  -2272   -942       C
ATOM   3612  O   PRO D 335       5.360 -58.903 -12.917  1.00163.40           O
ANISOU 3612  O   PRO D 335    21060  20290  20733  -1521  -2391   -930       O
ATOM   3613  CB  PRO D 335       5.495 -62.151 -13.437  1.00184.15           C
ANISOU 3613  CB  PRO D 335    23529  23054  23386  -1535  -2026  -1054       C
ATOM   3614  CG  PRO D 335       6.326 -63.379 -13.345  1.00192.36           C
ANISOU 3614  CG  PRO D 335    24509  24132  24448  -1562  -1876  -1041       C
ATOM   3615  CD  PRO D 335       7.354 -63.069 -12.311  1.00196.90           C
ANISOU 3615  CD  PRO D 335    25098  24652  25063  -1578  -1891   -950       C
ATOM   3616  N   LYS D 336       5.716 -60.127 -11.062  1.00149.63           N
ANISOU 3616  N   LYS D 336    19271  18504  19079  -1478  -2252   -973       N
ATOM   3617  CA  LYS D 336       5.050 -59.175 -10.177  1.00162.64           C
ANISOU 3617  CA  LYS D 336    20977  20076  20742  -1420  -2371   -997       C
ATOM   3618  C   LYS D 336       5.884 -57.939  -9.870  1.00181.14           C
ANISOU 3618  C   LYS D 336    23390  22355  23079  -1450  -2504   -881       C
ATOM   3619  O   LYS D 336       7.119 -57.936  -9.990  1.00152.86           O
ANISOU 3619  O   LYS D 336    19804  18778  19499  -1512  -2489   -773       O
ATOM   3620  CB  LYS D 336       4.632 -59.831  -8.865  1.00157.36           C
ANISOU 3620  CB  LYS D 336    20283  19375  20131  -1358  -2307  -1071       C
ATOM   3621  CG  LYS D 336       3.154 -60.133  -8.771  1.00166.61           C
ANISOU 3621  CG  LYS D 336    21440  20560  21306  -1284  -2295  -1196       C
ATOM   3622  CD  LYS D 336       2.774 -61.228  -9.746  1.00176.97           C
ANISOU 3622  CD  LYS D 336    22686  21955  22602  -1302  -2181  -1258       C
ATOM   3623  CE  LYS D 336       1.384 -61.768  -9.459  1.00174.29           C
ANISOU 3623  CE  LYS D 336    22316  21627  22278  -1229  -2148  -1378       C
ATOM   3624  NZ  LYS D 336       1.330 -62.506  -8.158  1.00124.61           N
ANISOU 3624  NZ  LYS D 336    15983  15313  16049  -1180  -2074  -1420       N
ATOM   3625  N   ALA D 337       5.176 -56.889  -9.467  1.00185.47           N
ANISOU 3625  N   ALA D 337    24003  22843  23622  -1402  -2635   -901       N
ATOM   3626  CA  ALA D 337       5.781 -55.618  -9.100  1.00178.25           C
ANISOU 3626  CA  ALA D 337    23165  21857  22703  -1419  -2781   -804       C
ATOM   3627  C   ALA D 337       6.663 -55.760  -7.872  1.00179.00           C
ANISOU 3627  C   ALA D 337    23270  21896  22846  -1422  -2761   -750       C
ATOM   3628  O   ALA D 337       7.650 -55.041  -7.738  1.00151.77           O
ANISOU 3628  O   ALA D 337    19865  18406  19396  -1468  -2842   -635       O
ATOM   3629  CB  ALA D 337       4.692 -54.584  -8.845  1.00145.25           C
ANISOU 3629  CB  ALA D 337    19052  17624  18511  -1354  -2914   -857       C
ATOM   3630  N   ILE D 338       6.298 -56.705  -7.001  1.00213.66           N
ANISOU 3630  N   ILE D 338    27617  26287  27278  -1374  -2654   -831       N
ATOM   3631  CA  ILE D 338       6.815 -56.806  -5.627  1.00206.40           C
ANISOU 3631  CA  ILE D 338    26708  25305  26408  -1355  -2642   -809       C
ATOM   3632  C   ILE D 338       8.164 -57.512  -5.427  1.00170.82           C
ANISOU 3632  C   ILE D 338    22158  20815  21929  -1424  -2543   -720       C
ATOM   3633  O   ILE D 338       8.477 -58.509  -6.092  1.00145.34           O
ANISOU 3633  O   ILE D 338    18860  17661  18700  -1462  -2417   -724       O
ATOM   3634  CB  ILE D 338       5.769 -57.447  -4.677  1.00139.29           C
ANISOU 3634  CB  ILE D 338    18180  16798  17945  -1267  -2579   -934       C
ATOM   3635  CG1 ILE D 338       5.022 -58.596  -5.370  1.00131.53           C
ANISOU 3635  CG1 ILE D 338    17115  15901  16959  -1254  -2451  -1030       C
ATOM   3636  CG2 ILE D 338       4.773 -56.402  -4.199  1.00130.71           C
ANISOU 3636  CG2 ILE D 338    17168  15650  16846  -1189  -2713   -982       C
ATOM   3637  CD1 ILE D 338       5.793 -59.907  -5.420  1.00148.49           C
ANISOU 3637  CD1 ILE D 338    19179  18103  19137  -1301  -2290  -1017       C
ATOM   3638  N   LYS D 339       8.942 -56.991  -4.478  1.00153.44           N
ANISOU 3638  N   LYS D 339    20003  18542  19755  -1436  -2603   -641       N
ATOM   3639  CA  LYS D 339      10.310 -57.456  -4.249  1.00182.91           C
ANISOU 3639  CA  LYS D 339    23705  22279  23512  -1507  -2532   -533       C
ATOM   3640  C   LYS D 339      10.525 -57.993  -2.832  1.00205.28           C
ANISOU 3640  C   LYS D 339    26520  25070  26406  -1479  -2468   -553       C
ATOM   3641  O   LYS D 339      10.000 -57.429  -1.865  1.00216.67           O
ANISOU 3641  O   LYS D 339    28015  26446  27865  -1418  -2547   -594       O
ATOM   3642  CB  LYS D 339      11.302 -56.325  -4.544  1.00177.51           C
ANISOU 3642  CB  LYS D 339    23090  21553  22803  -1570  -2665   -385       C
ATOM   3643  CG  LYS D 339      10.878 -54.930  -4.059  1.00152.15           C
ANISOU 3643  CG  LYS D 339    19980  18252  19579  -1530  -2850   -377       C
ATOM   3644  CD  LYS D 339      11.921 -53.897  -4.502  1.00146.71           C
ANISOU 3644  CD  LYS D 339    19347  17530  18865  -1603  -2977   -221       C
ATOM   3645  CE  LYS D 339      11.662 -52.509  -3.925  1.00131.46           C
ANISOU 3645  CE  LYS D 339    17522  15500  16926  -1570  -3166   -200       C
ATOM   3646  NZ  LYS D 339      12.813 -51.604  -4.233  1.00123.11           N
ANISOU 3646  NZ  LYS D 339    16515  14408  15854  -1647  -3285    -34       N
ATOM   3647  N   CYS D 340      11.303 -59.068  -2.702  1.00188.78           N
ANISOU 3647  N   CYS D 340    24358  23022  24348  -1523  -2324   -522       N
ATOM   3648  CA  CYS D 340      11.471 -59.688  -1.387  1.00168.31           C
ANISOU 3648  CA  CYS D 340    21733  20399  21817  -1498  -2249   -547       C
ATOM   3649  C   CYS D 340      11.953 -58.728  -0.290  1.00150.46           C
ANISOU 3649  C   CYS D 340    19552  18040  19575  -1495  -2368   -475       C
ATOM   3650  O   CYS D 340      11.459 -58.792   0.829  1.00190.60           O
ANISOU 3650  O   CYS D 340    24643  23082  24694  -1433  -2370   -541       O
ATOM   3651  CB  CYS D 340      12.286 -60.997  -1.432  1.00175.57           C
ANISOU 3651  CB  CYS D 340    22560  21378  22770  -1551  -2075   -518       C
ATOM   3652  SG  CYS D 340      13.568 -61.135  -2.694  1.00179.41           S
ANISOU 3652  SG  CYS D 340    23027  21922  23219  -1655  -2033   -379       S
ATOM   3653  N   VAL D 341      12.885 -57.831  -0.596  1.00131.67           N
ANISOU 3653  N   VAL D 341    17234  15623  17170  -1558  -2472   -341       N
ATOM   3654  CA  VAL D 341      13.314 -56.856   0.407  1.00130.86           C
ANISOU 3654  CA  VAL D 341    17217  15421  17082  -1555  -2599   -272       C
ATOM   3655  C   VAL D 341      12.777 -55.468   0.106  1.00148.68           C
ANISOU 3655  C   VAL D 341    19574  17624  19294  -1525  -2786   -269       C
ATOM   3656  O   VAL D 341      13.351 -54.751  -0.708  1.00169.26           O
ANISOU 3656  O   VAL D 341    22217  20228  21865  -1583  -2874   -167       O
ATOM   3657  CB  VAL D 341      14.841 -56.722   0.416  1.00125.05           C
ANISOU 3657  CB  VAL D 341    16490  14669  16356  -1652  -2604   -103       C
ATOM   3658  CG1 VAL D 341      15.285 -55.907   1.619  1.00155.56           C
ANISOU 3658  CG1 VAL D 341    20435  18427  20243  -1649  -2716    -40       C
ATOM   3659  CG2 VAL D 341      15.499 -58.092   0.401  1.00 86.83           C
ANISOU 3659  CG2 VAL D 341    11545   9895  11549  -1697  -2414    -87       C
ATOM   3660  N   PRO D 342      11.723 -55.046   0.817  1.00168.81           N
ANISOU 3660  N   PRO D 342    22169  20125  21847  -1435  -2851   -372       N
ATOM   3661  CA  PRO D 342      11.200 -53.711   0.531  1.00177.74           C
ANISOU 3661  CA  PRO D 342    23396  21201  22935  -1404  -3030   -369       C
ATOM   3662  C   PRO D 342      12.173 -52.621   0.950  1.00173.08           C
ANISOU 3662  C   PRO D 342    22898  20523  22342  -1450  -3175   -235       C
ATOM   3663  O   PRO D 342      12.231 -51.570   0.318  1.00195.92           O
ANISOU 3663  O   PRO D 342    25856  23387  25196  -1471  -3316   -177       O
ATOM   3664  CB  PRO D 342       9.924 -53.645   1.381  1.00182.55           C
ANISOU 3664  CB  PRO D 342    24027  21779  23554  -1291  -3047   -506       C
ATOM   3665  CG  PRO D 342       9.509 -55.063   1.548  1.00183.61           C
ANISOU 3665  CG  PRO D 342    24053  21988  23722  -1265  -2866   -600       C
ATOM   3666  CD  PRO D 342      10.815 -55.810   1.687  1.00193.50           C
ANISOU 3666  CD  PRO D 342    25251  23262  25010  -1351  -2761   -504       C
ATOM   3667  N   GLN D 343      12.931 -52.869   2.007  1.00165.99           N
ANISOU 3667  N   GLN D 343    22004  19579  21485  -1469  -3145   -183       N
ATOM   3668  CA  GLN D 343      13.728 -51.805   2.601  1.00188.82           C
ANISOU 3668  CA  GLN D 343    24994  22372  24377  -1501  -3295    -67       C
ATOM   3669  C   GLN D 343      15.052 -51.498   1.899  1.00172.91           C
ANISOU 3669  C   GLN D 343    22983  20363  22350  -1612  -3333    105       C
ATOM   3670  O   GLN D 343      15.489 -50.350   1.895  1.00181.72           O
ANISOU 3670  O   GLN D 343    24190  21409  23448  -1639  -3498    201       O
ATOM   3671  CB  GLN D 343      13.926 -52.042   4.104  1.00212.82           C
ANISOU 3671  CB  GLN D 343    28050  25348  27463  -1469  -3270    -82       C
ATOM   3672  CG  GLN D 343      12.612 -52.043   4.896  1.00212.88           C
ANISOU 3672  CG  GLN D 343    28076  25332  27476  -1349  -3275   -236       C
ATOM   3673  CD  GLN D 343      11.720 -50.853   4.572  1.00186.71           C
ANISOU 3673  CD  GLN D 343    24855  21973  24114  -1287  -3438   -281       C
ATOM   3674  OE1 GLN D 343      10.648 -51.006   3.983  1.00157.64           O
ANISOU 3674  OE1 GLN D 343    21145  18342  20410  -1232  -3413   -384       O
ATOM   3675  NE2 GLN D 343      12.155 -49.661   4.969  1.00179.72           N
ANISOU 3675  NE2 GLN D 343    24082  20989  23214  -1297  -3608   -200       N
ATOM   3676  N   ALA D 344      15.682 -52.500   1.292  1.00177.96           N
ANISOU 3676  N   ALA D 344    23529  21089  23000  -1675  -3187    148       N
ATOM   3677  CA  ALA D 344      16.992 -52.281   0.668  1.00201.09           C
ANISOU 3677  CA  ALA D 344    26455  24030  25919  -1778  -3212    322       C
ATOM   3678  C   ALA D 344      16.952 -51.113  -0.321  1.00236.31           C
ANISOU 3678  C   ALA D 344    30977  28480  30329  -1798  -3374    385       C
ATOM   3679  O   ALA D 344      15.953 -50.916  -1.017  1.00258.07           O
ANISOU 3679  O   ALA D 344    33731  31269  33053  -1751  -3398    288       O
ATOM   3680  CB  ALA D 344      17.492 -53.551  -0.010  1.00170.04           C
ANISOU 3680  CB  ALA D 344    22409  20203  21994  -1828  -3025    340       C
ATOM   3681  N   GLU D 345      18.023 -50.324  -0.363  1.00221.96           N
ANISOU 3681  N   GLU D 345    29212  26615  28507  -1869  -3490    550       N
ATOM   3682  CA  GLU D 345      18.048 -49.130  -1.204  1.00207.92           C
ANISOU 3682  CA  GLU D 345    27495  24818  26686  -1891  -3662    623       C
ATOM   3683  C   GLU D 345      18.323 -49.452  -2.670  1.00215.50           C
ANISOU 3683  C   GLU D 345    28383  25886  27613  -1943  -3604    674       C
ATOM   3684  O   GLU D 345      17.998 -48.670  -3.569  1.00216.68           O
ANISOU 3684  O   GLU D 345    28557  26047  27723  -1945  -3714    688       O
ATOM   3685  CB  GLU D 345      19.061 -48.116  -0.668  1.00201.09           C
ANISOU 3685  CB  GLU D 345    26718  23857  25830  -1946  -3822    785       C
ATOM   3686  CG  GLU D 345      18.486 -47.195   0.399  1.00205.03           C
ANISOU 3686  CG  GLU D 345    27327  24238  26336  -1881  -3968    727       C
ATOM   3687  CD  GLU D 345      17.180 -46.546  -0.043  1.00215.72           C
ANISOU 3687  CD  GLU D 345    28720  25588  27656  -1803  -4055    601       C
ATOM   3688  OE1 GLU D 345      17.062 -46.172  -1.232  1.00200.50           O
ANISOU 3688  OE1 GLU D 345    26775  23711  25693  -1828  -4102    630       O
ATOM   3689  OE2 GLU D 345      16.265 -46.421   0.797  1.00226.57           O
ANISOU 3689  OE2 GLU D 345    30139  26909  29038  -1716  -4073    476       O
ATOM   3690  N   VAL D 346      18.891 -50.630  -2.895  1.00218.02           N
ANISOU 3690  N   VAL D 346    28610  26282  27946  -1981  -3428    697       N
ATOM   3691  CA  VAL D 346      19.342 -51.058  -4.217  1.00216.62           C
ANISOU 3691  CA  VAL D 346    28360  26208  27736  -2034  -3356    761       C
ATOM   3692  C   VAL D 346      18.253 -51.044  -5.297  1.00195.60           C
ANISOU 3692  C   VAL D 346    25674  23613  25033  -1992  -3352    646       C
ATOM   3693  O   VAL D 346      17.064 -51.227  -5.015  1.00213.16           O
ANISOU 3693  O   VAL D 346    27902  25829  27261  -1917  -3328    485       O
ATOM   3694  CB  VAL D 346      19.985 -52.459  -4.143  1.00206.30           C
ANISOU 3694  CB  VAL D 346    26960  24971  26455  -2066  -3149    777       C
ATOM   3695  CG1 VAL D 346      19.028 -53.444  -3.506  1.00204.21           C
ANISOU 3695  CG1 VAL D 346    26652  24719  26219  -1995  -3013    597       C
ATOM   3696  CG2 VAL D 346      20.410 -52.932  -5.517  1.00212.17           C
ANISOU 3696  CG2 VAL D 346    27631  25823  27160  -2112  -3070    836       C
ATOM   3697  N   GLU D 347      18.678 -50.806  -6.535  1.00145.88           N
ANISOU 3697  N   GLU D 347    19351  17381  18696  -2042  -3378    735       N
ATOM   3698  CA  GLU D 347      17.772 -50.748  -7.666  1.00165.15           C
ANISOU 3698  CA  GLU D 347    21766  19889  21094  -2015  -3380    647       C
ATOM   3699  C   GLU D 347      17.209 -52.121  -8.022  1.00147.13           C
ANISOU 3699  C   GLU D 347    19397  17696  18811  -1985  -3182    518       C
ATOM   3700  O   GLU D 347      17.964 -53.055  -8.300  1.00110.41           O
ANISOU 3700  O   GLU D 347    14678  13108  14163  -2025  -3045    571       O
ATOM   3701  CB  GLU D 347      18.513 -50.186  -8.871  1.00177.81           C
ANISOU 3701  CB  GLU D 347    23357  21545  22657  -2081  -3454    792       C
ATOM   3702  CG  GLU D 347      19.187 -48.854  -8.621  1.00194.68           C
ANISOU 3702  CG  GLU D 347    25573  23602  24796  -2120  -3653    940       C
ATOM   3703  CD  GLU D 347      19.754 -48.252  -9.897  1.00231.04           C
ANISOU 3703  CD  GLU D 347    30159  28267  29359  -2178  -3736   1072       C
ATOM   3704  OE1 GLU D 347      18.966 -47.943 -10.824  1.00221.90           O
ANISOU 3704  OE1 GLU D 347    28991  27155  28167  -2156  -3773   1005       O
ATOM   3705  OE2 GLU D 347      20.991 -48.090  -9.973  1.00252.39           O
ANISOU 3705  OE2 GLU D 347    32856  30973  32066  -2245  -3764   1249       O
ATOM   3706  N   TRP D 348      15.882 -52.234  -8.034  1.00135.41           N
ANISOU 3706  N   TRP D 348    17914  16214  17321  -1914  -3169    354       N
ATOM   3707  CA  TRP D 348      15.231 -53.494  -8.377  1.00198.79           C
ANISOU 3707  CA  TRP D 348    25864  24320  25347  -1883  -2995    225       C
ATOM   3708  C   TRP D 348      14.818 -53.575  -9.852  1.00208.30           C
ANISOU 3708  C   TRP D 348    27030  25615  26499  -1893  -2978    199       C
ATOM   3709  O   TRP D 348      14.100 -52.706 -10.363  1.00206.00           O
ANISOU 3709  O   TRP D 348    26777  25314  26179  -1874  -3097    168       O
ATOM   3710  CB  TRP D 348      14.010 -53.744  -7.481  1.00227.29           C
ANISOU 3710  CB  TRP D 348    29487  27888  28984  -1797  -2972     60       C
ATOM   3711  CG  TRP D 348      13.824 -55.196  -7.127  1.00222.27           C
ANISOU 3711  CG  TRP D 348    28773  27300  28379  -1775  -2780    -32       C
ATOM   3712  CD1 TRP D 348      13.163 -56.153  -7.855  1.00208.01           C
ANISOU 3712  CD1 TRP D 348    26899  25576  26558  -1755  -2656   -135       C
ATOM   3713  CD2 TRP D 348      14.319 -55.853  -5.958  1.00202.40           C
ANISOU 3713  CD2 TRP D 348    26237  24749  25915  -1773  -2695    -26       C
ATOM   3714  NE1 TRP D 348      13.220 -57.364  -7.206  1.00194.78           N
ANISOU 3714  NE1 TRP D 348    25164  23920  24924  -1740  -2501   -193       N
ATOM   3715  CE2 TRP D 348      13.924 -57.206  -6.041  1.00222.73           C
ANISOU 3715  CE2 TRP D 348    28728  27391  28507  -1751  -2520   -128       C
ATOM   3716  CE3 TRP D 348      15.059 -55.428  -4.851  1.00147.58           C
ANISOU 3716  CE3 TRP D 348    19339  17726  19008  -1790  -2751     58       C
ATOM   3717  CZ2 TRP D 348      14.244 -58.132  -5.050  1.00237.53           C
ANISOU 3717  CZ2 TRP D 348    30558  29257  30435  -1745  -2400   -148       C
ATOM   3718  CZ3 TRP D 348      15.375 -56.347  -3.876  1.00167.16           C
ANISOU 3718  CZ3 TRP D 348    21776  20198  21540  -1785  -2630     38       C
ATOM   3719  CH2 TRP D 348      14.968 -57.685  -3.979  1.00213.37           C
ANISOU 3719  CH2 TRP D 348    27541  26121  27410  -1762  -2455    -65       C
ATOM   3720  N   LYS D 349      15.261 -54.630 -10.528  1.00185.65           N
ANISOU 3720  N   LYS D 349    24086  22835  23619  -1924  -2829    211       N
ATOM   3721  CA  LYS D 349      14.851 -54.861 -11.900  1.00202.02           C
ANISOU 3721  CA  LYS D 349    26119  24999  25642  -1931  -2794    176       C
ATOM   3722  C   LYS D 349      14.061 -56.165 -11.995  1.00204.95           C
ANISOU 3722  C   LYS D 349    26427  25424  26018  -1889  -2628     25       C
ATOM   3723  O   LYS D 349      14.485 -57.193 -11.463  1.00174.92           O
ANISOU 3723  O   LYS D 349    22580  21634  22248  -1892  -2492     14       O
ATOM   3724  CB  LYS D 349      16.074 -54.884 -12.825  1.00214.57           C
ANISOU 3724  CB  LYS D 349    27676  26653  27199  -2003  -2777    332       C
ATOM   3725  CG  LYS D 349      17.063 -53.739 -12.584  1.00184.84           C
ANISOU 3725  CG  LYS D 349    23963  22831  23437  -2052  -2928    504       C
ATOM   3726  CD  LYS D 349      17.821 -53.336 -13.847  1.00170.09           C
ANISOU 3726  CD  LYS D 349    22072  21033  21519  -2109  -2973    641       C
ATOM   3727  CE  LYS D 349      16.922 -52.594 -14.835  1.00182.77           C
ANISOU 3727  CE  LYS D 349    23693  22668  23083  -2093  -3075    587       C
ATOM   3728  NZ  LYS D 349      16.264 -53.495 -15.832  1.00153.02           N
ANISOU 3728  NZ  LYS D 349    19865  18996  19279  -2074  -2948    477       N
ATOM   3729  N   PHE D 350      12.898 -56.113 -12.642  1.00232.78           N
ANISOU 3729  N   PHE D 350    29951  28980  29516  -1851  -2643    -90       N
ATOM   3730  CA  PHE D 350      12.093 -57.314 -12.846  1.00238.96           C
ANISOU 3730  CA  PHE D 350    30677  29817  30301  -1813  -2497   -230       C
ATOM   3731  C   PHE D 350      11.852 -57.596 -14.322  1.00212.42           C
ANISOU 3731  C   PHE D 350    27279  26548  26883  -1833  -2459   -248       C
ATOM   3732  O   PHE D 350      11.182 -56.817 -15.015  1.00172.30           O
ANISOU 3732  O   PHE D 350    22226  21475  21767  -1826  -2561   -269       O
ATOM   3733  CB  PHE D 350      10.729 -57.219 -12.147  1.00249.25           C
ANISOU 3733  CB  PHE D 350    32004  31073  31627  -1738  -2527   -374       C
ATOM   3734  CG  PHE D 350      10.610 -56.092 -11.161  1.00227.40           C
ANISOU 3734  CG  PHE D 350    29311  28206  28883  -1712  -2673   -348       C
ATOM   3735  CD1 PHE D 350      10.654 -54.773 -11.583  1.00217.13           C
ANISOU 3735  CD1 PHE D 350    28071  26876  27553  -1730  -2838   -277       C
ATOM   3736  CD2 PHE D 350      10.400 -56.356  -9.816  1.00200.10           C
ANISOU 3736  CD2 PHE D 350    25864  24687  25477  -1666  -2647   -400       C
ATOM   3737  CE1 PHE D 350      10.528 -53.743 -10.677  1.00209.25           C
ANISOU 3737  CE1 PHE D 350    27147  25783  26575  -1703  -2975   -257       C
ATOM   3738  CE2 PHE D 350      10.270 -55.330  -8.911  1.00187.36           C
ANISOU 3738  CE2 PHE D 350    24325  22982  23882  -1637  -2782   -381       C
ATOM   3739  CZ  PHE D 350      10.332 -54.023  -9.340  1.00198.63           C
ANISOU 3739  CZ  PHE D 350    25817  24375  25277  -1655  -2946   -311       C
ATOM   3740  N   TYR D 351      12.414 -58.697 -14.813  1.00225.09           N
ANISOU 3740  N   TYR D 351    28823  28223  28477  -1858  -2312   -236       N
ATOM   3741  CA  TYR D 351      11.957 -59.230 -16.089  1.00261.46           C
ANISOU 3741  CA  TYR D 351    33393  32917  33034  -1861  -2249   -294       C
ATOM   3742  C   TYR D 351      11.754 -60.748 -16.095  1.00270.56           C
ANISOU 3742  C   TYR D 351    34484  34118  34199  -1843  -2068   -390       C
ATOM   3743  O   TYR D 351      12.723 -61.510 -16.066  1.00292.08           O
ANISOU 3743  O   TYR D 351    37172  36874  36932  -1871  -1959   -329       O
ATOM   3744  CB  TYR D 351      12.942 -58.842 -17.190  1.00275.47           C
ANISOU 3744  CB  TYR D 351    35158  34750  34757  -1921  -2278   -156       C
ATOM   3745  CG  TYR D 351      14.230 -58.210 -16.694  1.00257.84           C
ANISOU 3745  CG  TYR D 351    32947  32478  32541  -1965  -2342     10       C
ATOM   3746  CD1 TYR D 351      14.246 -56.907 -16.211  1.00232.64           C
ANISOU 3746  CD1 TYR D 351    29817  29213  29362  -1969  -2510     72       C
ATOM   3747  CD2 TYR D 351      15.434 -58.906 -16.734  1.00240.24           C
ANISOU 3747  CD2 TYR D 351    30679  30287  30313  -2003  -2236    110       C
ATOM   3748  CE1 TYR D 351      15.417 -56.320 -15.772  1.00206.59           C
ANISOU 3748  CE1 TYR D 351    26541  25877  26079  -2012  -2576    229       C
ATOM   3749  CE2 TYR D 351      16.613 -58.324 -16.297  1.00212.81           C
ANISOU 3749  CE2 TYR D 351    27224  26779  26854  -2046  -2297    271       C
ATOM   3750  CZ  TYR D 351      16.598 -57.030 -15.818  1.00197.76           C
ANISOU 3750  CZ  TYR D 351    25381  24798  24962  -2052  -2470    331       C
ATOM   3751  OH  TYR D 351      17.766 -56.445 -15.383  1.00175.04           O
ANISOU 3751  OH  TYR D 351    22525  21883  22100  -2098  -2537    496       O
ATOM   3752  N   ASP D 352      10.496 -61.178 -16.154  1.00243.64           N
ANISOU 3752  N   ASP D 352    31065  30716  30792  -1795  -2039   -536       N
ATOM   3753  CA  ASP D 352      10.150 -62.552 -16.503  1.00214.55           C
ANISOU 3753  CA  ASP D 352    27325  27089  27105  -1780  -1884   -632       C
ATOM   3754  C   ASP D 352      10.083 -62.662 -18.016  1.00214.72           C
ANISOU 3754  C   ASP D 352    27332  27193  27058  -1806  -1870   -629       C
ATOM   3755  O   ASP D 352       9.899 -61.654 -18.694  1.00230.39           O
ANISOU 3755  O   ASP D 352    29351  29184  29004  -1821  -1987   -589       O
ATOM   3756  CB  ASP D 352       8.817 -62.963 -15.868  1.00201.44           C
ANISOU 3756  CB  ASP D 352    25659  25400  25480  -1717  -1866   -783       C
ATOM   3757  CG  ASP D 352       8.624 -64.477 -15.826  1.00186.51           C
ANISOU 3757  CG  ASP D 352    23706  23550  23609  -1701  -1702   -872       C
ATOM   3758  OD1 ASP D 352       9.588 -65.220 -16.120  1.00187.67           O
ANISOU 3758  OD1 ASP D 352    23818  23739  23749  -1736  -1597   -818       O
ATOM   3759  OD2 ASP D 352       7.508 -64.927 -15.488  1.00163.22           O
ANISOU 3759  OD2 ASP D 352    20743  20590  20682  -1652  -1679   -994       O
ATOM   3760  N   ALA D 353      10.243 -63.866 -18.554  1.00212.27           N
ANISOU 3760  N   ALA D 353    26975  26946  26732  -1810  -1728   -669       N
ATOM   3761  CA  ALA D 353       9.865 -64.093 -19.947  1.00218.08           C
ANISOU 3761  CA  ALA D 353    27700  27756  27403  -1821  -1708   -704       C
ATOM   3762  C   ALA D 353       8.425 -63.604 -20.191  1.00206.17           C
ANISOU 3762  C   ALA D 353    26218  26234  25884  -1788  -1794   -810       C
ATOM   3763  O   ALA D 353       8.105 -63.111 -21.265  1.00176.86           O
ANISOU 3763  O   ALA D 353    22518  22563  22118  -1804  -1853   -805       O
ATOM   3764  CB  ALA D 353      10.012 -65.561 -20.320  1.00216.32           C
ANISOU 3764  CB  ALA D 353    27429  27591  27173  -1817  -1542   -762       C
ATOM   3765  N   GLN D 354       7.562 -63.732 -19.188  1.00228.20           N
ANISOU 3765  N   GLN D 354    29013  28968  28726  -1741  -1801   -902       N
ATOM   3766  CA  GLN D 354       6.217 -63.160 -19.256  1.00217.63           C
ANISOU 3766  CA  GLN D 354    27702  27606  27382  -1706  -1892   -989       C
ATOM   3767  C   GLN D 354       6.060 -61.967 -18.314  1.00225.99           C
ANISOU 3767  C   GLN D 354    28809  28585  28473  -1686  -2026   -954       C
ATOM   3768  O   GLN D 354       5.984 -62.140 -17.097  1.00243.46           O
ANISOU 3768  O   GLN D 354    31022  30741  30741  -1652  -2011   -980       O
ATOM   3769  CB  GLN D 354       5.152 -64.210 -18.918  1.00213.63           C
ANISOU 3769  CB  GLN D 354    27165  27102  26904  -1659  -1804  -1129       C
ATOM   3770  CG  GLN D 354       4.619 -64.980 -20.111  1.00224.66           C
ANISOU 3770  CG  GLN D 354    28538  28570  28254  -1667  -1736  -1199       C
ATOM   3771  CD  GLN D 354       3.227 -65.544 -19.870  1.00241.80           C
ANISOU 3771  CD  GLN D 354    30696  30732  30445  -1618  -1713  -1332       C
ATOM   3772  OE1 GLN D 354       2.306 -65.299 -20.648  1.00248.98           O
ANISOU 3772  OE1 GLN D 354    31619  31664  31318  -1615  -1760  -1383       O
ATOM   3773  NE2 GLN D 354       3.068 -66.303 -18.789  1.00250.86           N
ANISOU 3773  NE2 GLN D 354    31815  31849  31654  -1581  -1643  -1385       N
ATOM   3774  N   PRO D 355       5.985 -60.752 -18.874  1.00205.96           N
ANISOU 3774  N   PRO D 355    26313  26042  25902  -1705  -2159   -897       N
ATOM   3775  CA  PRO D 355       5.769 -59.554 -18.055  1.00193.75           C
ANISOU 3775  CA  PRO D 355    24820  24416  24380  -1684  -2298   -868       C
ATOM   3776  C   PRO D 355       4.323 -59.502 -17.577  1.00191.86           C
ANISOU 3776  C   PRO D 355    24595  24143  24160  -1621  -2327   -990       C
ATOM   3777  O   PRO D 355       3.434 -59.954 -18.297  1.00185.77           O
ANISOU 3777  O   PRO D 355    23804  23417  23364  -1610  -2290  -1073       O
ATOM   3778  CB  PRO D 355       6.032 -58.416 -19.035  1.00190.75           C
ANISOU 3778  CB  PRO D 355    24469  24056  23951  -1727  -2420   -780       C
ATOM   3779  CG  PRO D 355       5.645 -58.987 -20.360  1.00217.92           C
ANISOU 3779  CG  PRO D 355    27876  27583  27341  -1746  -2357   -826       C
ATOM   3780  CD  PRO D 355       6.036 -60.441 -20.312  1.00208.66           C
ANISOU 3780  CD  PRO D 355    26652  26450  26178  -1746  -2189   -863       C
ATOM   3781  N   CYS D 356       4.086 -58.975 -16.379  1.00213.34           N
ANISOU 3781  N   CYS D 356    27351  26786  26923  -1578  -2392   -998       N
ATOM   3782  CA  CYS D 356       2.720 -58.881 -15.868  1.00236.84           C
ANISOU 3782  CA  CYS D 356    30342  29730  29918  -1511  -2423  -1105       C
ATOM   3783  C   CYS D 356       1.966 -57.777 -16.590  1.00217.88           C
ANISOU 3783  C   CYS D 356    27982  27327  27476  -1511  -2551  -1105       C
ATOM   3784  O   CYS D 356       2.483 -56.670 -16.779  1.00149.72           O
ANISOU 3784  O   CYS D 356    19391  18668  18826  -1540  -2666  -1016       O
ATOM   3785  CB  CYS D 356       2.685 -58.655 -14.351  1.00261.76           C
ANISOU 3785  CB  CYS D 356    33523  32806  33128  -1459  -2451  -1114       C
ATOM   3786  SG  CYS D 356       1.007 -58.686 -13.622  1.00238.79           S
ANISOU 3786  SG  CYS D 356    30624  29865  30242  -1364  -2472  -1244       S
ATOM   3787  N   SER D 357       0.739 -58.096 -16.987  1.00248.77           N
ANISOU 3787  N   SER D 357    31880  31266  31375  -1479  -2532  -1203       N
ATOM   3788  CA  SER D 357      -0.075 -57.206 -17.800  1.00258.36           C
ANISOU 3788  CA  SER D 357    33124  32491  32550  -1482  -2635  -1213       C
ATOM   3789  C   SER D 357      -0.271 -55.836 -17.161  1.00266.74           C
ANISOU 3789  C   SER D 357    34251  33476  33621  -1453  -2785  -1175       C
ATOM   3790  O   SER D 357      -0.130 -54.811 -17.827  1.00276.75           O
ANISOU 3790  O   SER D 357    35551  34745  34858  -1487  -2893  -1114       O
ATOM   3791  CB  SER D 357      -1.435 -57.850 -18.089  1.00251.09           C
ANISOU 3791  CB  SER D 357    32179  31602  31624  -1443  -2583  -1327       C
ATOM   3792  OG  SER D 357      -2.098 -58.204 -16.888  1.00244.72           O
ANISOU 3792  OG  SER D 357    31371  30749  30862  -1371  -2558  -1395       O
ATOM   3793  N   ASP D 358      -0.585 -55.817 -15.870  1.00257.29           N
ANISOU 3793  N   ASP D 358    33076  32215  32468  -1390  -2794  -1211       N
ATOM   3794  CA  ASP D 358      -1.013 -54.580 -15.228  1.00243.66           C
ANISOU 3794  CA  ASP D 358    31417  30415  30748  -1347  -2933  -1197       C
ATOM   3795  C   ASP D 358      -0.385 -54.346 -13.860  1.00228.79           C
ANISOU 3795  C   ASP D 358    29566  28455  28907  -1315  -2958  -1163       C
ATOM   3796  O   ASP D 358       0.225 -55.245 -13.282  1.00212.86           O
ANISOU 3796  O   ASP D 358    27512  26442  26921  -1318  -2856  -1164       O
ATOM   3797  CB  ASP D 358      -2.540 -54.561 -15.110  1.00232.65           C
ANISOU 3797  CB  ASP D 358    30029  29018  29352  -1279  -2947  -1296       C
ATOM   3798  CG  ASP D 358      -3.069 -53.225 -14.642  1.00221.57           C
ANISOU 3798  CG  ASP D 358    28697  27544  27945  -1235  -3095  -1282       C
ATOM   3799  OD1 ASP D 358      -2.512 -52.187 -15.057  1.00212.73           O
ANISOU 3799  OD1 ASP D 358    27618  26405  26805  -1277  -3205  -1202       O
ATOM   3800  OD2 ASP D 358      -4.038 -53.211 -13.856  1.00225.97           O
ANISOU 3800  OD2 ASP D 358    29270  28068  28520  -1155  -3104  -1350       O
ATOM   3801  N   LYS D 359      -0.548 -53.125 -13.355  1.00241.10           N
ANISOU 3801  N   LYS D 359    31196  29944  30468  -1286  -3097  -1132       N
ATOM   3802  CA  LYS D 359      -0.070 -52.744 -12.027  1.00265.66           C
ANISOU 3802  CA  LYS D 359    34352  32972  33614  -1249  -3143  -1102       C
ATOM   3803  C   LYS D 359       1.373 -53.181 -11.772  1.00302.51           C
ANISOU 3803  C   LYS D 359    38998  37639  38302  -1306  -3087  -1019       C
ATOM   3804  O   LYS D 359       1.633 -54.035 -10.919  1.00311.58           O
ANISOU 3804  O   LYS D 359    40117  38780  39489  -1284  -2990  -1045       O
ATOM   3805  CB  LYS D 359      -1.005 -53.275 -10.927  1.00246.71           C
ANISOU 3805  CB  LYS D 359    31945  30545  31247  -1157  -3091  -1202       C
ATOM   3806  CG  LYS D 359      -0.576 -52.900  -9.507  1.00231.07           C
ANISOU 3806  CG  LYS D 359    30012  28481  29303  -1112  -3136  -1178       C
ATOM   3807  CD  LYS D 359      -0.552 -51.388  -9.297  1.00212.20           C
ANISOU 3807  CD  LYS D 359    27715  26015  26896  -1098  -3310  -1124       C
ATOM   3808  CE  LYS D 359       0.616 -50.952  -8.417  1.00189.59           C
ANISOU 3808  CE  LYS D 359    24897  23081  24057  -1117  -3363  -1039       C
ATOM   3809  NZ  LYS D 359       1.906 -50.883  -9.174  1.00156.18           N
ANISOU 3809  NZ  LYS D 359    20651  18876  19815  -1219  -3366   -928       N
ATOM   3810  N   ALA D 360       2.312 -52.582 -12.499  1.00315.12           N
ANISOU 3810  N   ALA D 360    40610  39247  39876  -1379  -3150   -914       N
ATOM   3811  CA  ALA D 360       2.018 -51.570 -13.510  1.00308.66           C
ANISOU 3811  CA  ALA D 360    39820  38441  39015  -1408  -3266   -880       C
ATOM   3812  C   ALA D 360       3.274 -51.331 -14.329  1.00302.09           C
ANISOU 3812  C   ALA D 360    38976  37643  38163  -1496  -3288   -757       C
ATOM   3813  O   ALA D 360       4.290 -51.999 -14.124  1.00310.94           O
ANISOU 3813  O   ALA D 360    40065  38779  39300  -1532  -3205   -704       O
ATOM   3814  CB  ALA D 360       1.564 -50.272 -12.860  1.00312.45           C
ANISOU 3814  CB  ALA D 360    40384  38834  39499  -1360  -3424   -872       C
ATOM   3815  N   TYR D 361       3.204 -50.383 -15.258  1.00279.57           N
ANISOU 3815  N   TYR D 361    36144  34805  35276  -1531  -3398   -707       N
ATOM   3816  CA  TYR D 361       4.409 -49.860 -15.883  1.00259.56           C
ANISOU 3816  CA  TYR D 361    33610  32288  32725  -1608  -3459   -572       C
ATOM   3817  C   TYR D 361       5.309 -51.023 -16.264  1.00259.83           C
ANISOU 3817  C   TYR D 361    33575  32391  32756  -1655  -3312   -539       C
ATOM   3818  O   TYR D 361       6.484 -51.067 -15.874  1.00240.06           O
ANISOU 3818  O   TYR D 361    31074  29870  30270  -1690  -3306   -441       O
ATOM   3819  CB  TYR D 361       5.135 -48.923 -14.916  1.00230.38           C
ANISOU 3819  CB  TYR D 361    29981  28497  29055  -1607  -3581   -483       C
ATOM   3820  CG  TYR D 361       4.193 -48.112 -14.046  1.00229.57           C
ANISOU 3820  CG  TYR D 361    29950  28308  28967  -1533  -3686   -546       C
ATOM   3821  CD1 TYR D 361       3.021 -47.565 -14.568  1.00225.24           C
ANISOU 3821  CD1 TYR D 361    29417  27768  28395  -1502  -3749   -613       C
ATOM   3822  CD2 TYR D 361       4.464 -47.912 -12.698  1.00227.50           C
ANISOU 3822  CD2 TYR D 361    29741  27958  28742  -1493  -3719   -539       C
ATOM   3823  CE1 TYR D 361       2.154 -46.833 -13.774  1.00226.83           C
ANISOU 3823  CE1 TYR D 361    29685  27892  28606  -1429  -3841   -668       C
ATOM   3824  CE2 TYR D 361       3.601 -47.180 -11.893  1.00235.60           C
ANISOU 3824  CE2 TYR D 361    30835  28906  29777  -1418  -3814   -597       C
ATOM   3825  CZ  TYR D 361       2.448 -46.642 -12.435  1.00237.35           C
ANISOU 3825  CZ  TYR D 361    31072  29138  29972  -1385  -3873   -661       C
ATOM   3826  OH  TYR D 361       1.589 -45.913 -11.636  1.00227.51           O
ANISOU 3826  OH  TYR D 361    29896  27816  28733  -1306  -3965   -716       O
ATOM   3827  N   LYS D 362       4.735 -51.977 -16.996  1.00262.89           N
ANISOU 3827  N   LYS D 362    33906  32856  33124  -1653  -3194   -620       N
ATOM   3828  CA  LYS D 362       5.432 -53.205 -17.367  1.00247.48           C
ANISOU 3828  CA  LYS D 362    31890  30972  31168  -1686  -3041   -610       C
ATOM   3829  C   LYS D 362       6.765 -52.905 -18.057  1.00260.11           C
ANISOU 3829  C   LYS D 362    33477  32609  32745  -1760  -3067   -465       C
ATOM   3830  O   LYS D 362       6.826 -52.116 -19.004  1.00245.39           O
ANISOU 3830  O   LYS D 362    31617  30774  30844  -1796  -3160   -407       O
ATOM   3831  CB  LYS D 362       4.543 -54.073 -18.259  1.00198.05           C
ANISOU 3831  CB  LYS D 362    25581  24790  24879  -1677  -2940   -714       C
ATOM   3832  CG  LYS D 362       3.069 -54.034 -17.876  1.00187.70           C
ANISOU 3832  CG  LYS D 362    24288  23451  23580  -1610  -2956   -839       C
ATOM   3833  CD  LYS D 362       2.291 -53.109 -18.805  1.00197.89           C
ANISOU 3833  CD  LYS D 362    25599  24759  24831  -1619  -3064   -846       C
ATOM   3834  CE  LYS D 362       2.198 -53.676 -20.228  1.00170.85           C
ANISOU 3834  CE  LYS D 362    22123  21433  21360  -1664  -2995   -859       C
ATOM   3835  NZ  LYS D 362       1.545 -52.735 -21.188  1.00127.18           N
ANISOU 3835  NZ  LYS D 362    16607  15924  15792  -1683  -3103   -853       N
ATOM   3836  N   ILE D 363       7.826 -53.544 -17.570  1.00268.67           N
ANISOU 3836  N   ILE D 363    34540  33693  33851  -1782  -2985   -404       N
ATOM   3837  CA  ILE D 363       9.191 -53.237 -17.991  1.00239.69           C
ANISOU 3837  CA  ILE D 363    30861  30046  30166  -1847  -3013   -250       C
ATOM   3838  C   ILE D 363       9.934 -54.470 -18.511  1.00238.86           C
ANISOU 3838  C   ILE D 363    30689  30021  30045  -1877  -2851   -229       C
ATOM   3839  O   ILE D 363       9.659 -55.594 -18.083  1.00256.05           O
ANISOU 3839  O   ILE D 363    32836  32208  32244  -1848  -2715   -318       O
ATOM   3840  CB  ILE D 363      10.003 -52.622 -16.824  1.00200.94           C
ANISOU 3840  CB  ILE D 363    26001  25048  25299  -1852  -3092   -157       C
ATOM   3841  CG1 ILE D 363       9.794 -53.424 -15.528  1.00150.69           C
ANISOU 3841  CG1 ILE D 363    19636  18633  18984  -1804  -2997   -238       C
ATOM   3842  CG2 ILE D 363       9.614 -51.165 -16.608  1.00203.55           C
ANISOU 3842  CG2 ILE D 363    26402  25308  25631  -1840  -3282   -129       C
ATOM   3843  CD1 ILE D 363       8.533 -53.053 -14.750  1.00101.37           C
ANISOU 3843  CD1 ILE D 363    13434  12321  12759  -1731  -3054   -358       C
ATOM   3844  N   GLU D 364      10.864 -54.257 -19.443  1.00221.44           N
ANISOU 3844  N   GLU D 364    28461  27874  27803  -1934  -2866   -108       N
ATOM   3845  CA  GLU D 364      11.743 -55.334 -19.916  1.00224.04           C
ANISOU 3845  CA  GLU D 364    28732  28277  28115  -1963  -2720    -64       C
ATOM   3846  C   GLU D 364      10.999 -56.590 -20.373  1.00218.45           C
ANISOU 3846  C   GLU D 364    27979  27629  27391  -1935  -2569   -200       C
ATOM   3847  O   GLU D 364      10.320 -56.565 -21.397  1.00222.38           O
ANISOU 3847  O   GLU D 364    28464  28182  27846  -1935  -2576   -254       O
ATOM   3848  CB  GLU D 364      12.836 -55.667 -18.897  1.00236.79           C
ANISOU 3848  CB  GLU D 364    30348  29850  29772  -1977  -2672     21       C
ATOM   3849  CG  GLU D 364      14.186 -55.017 -19.212  1.00235.44           C
ANISOU 3849  CG  GLU D 364    30179  29692  29586  -2036  -2742    211       C
ATOM   3850  CD  GLU D 364      14.825 -55.561 -20.485  1.00224.47           C
ANISOU 3850  CD  GLU D 364    28734  28411  28142  -2072  -2659    275       C
ATOM   3851  OE1 GLU D 364      15.881 -55.033 -20.894  1.00224.49           O
ANISOU 3851  OE1 GLU D 364    28732  28439  28126  -2118  -2717    435       O
ATOM   3852  OE2 GLU D 364      14.278 -56.518 -21.075  1.00212.65           O
ANISOU 3852  OE2 GLU D 364    27199  26976  26620  -2052  -2538    169       O
ATOM   3853  N   GLU D 365      11.156 -57.676 -19.616  1.00218.59           N
ANISOU 3853  N   GLU D 365    27973  27636  27444  -1915  -2437   -251       N
ATOM   3854  CA  GLU D 365      10.559 -58.981 -19.924  1.00233.38           C
ANISOU 3854  CA  GLU D 365    29803  29561  29310  -1889  -2286   -375       C
ATOM   3855  C   GLU D 365      11.447 -59.930 -20.752  1.00231.19           C
ANISOU 3855  C   GLU D 365    29475  29370  28998  -1922  -2156   -324       C
ATOM   3856  O   GLU D 365      11.101 -61.099 -20.930  1.00256.23           O
ANISOU 3856  O   GLU D 365    32611  32579  32166  -1902  -2023   -418       O
ATOM   3857  CB  GLU D 365       9.188 -58.804 -20.614  1.00248.37           C
ANISOU 3857  CB  GLU D 365    31708  31480  31180  -1862  -2325   -492       C
ATOM   3858  CG  GLU D 365       9.205 -59.035 -22.143  1.00254.57           C
ANISOU 3858  CG  GLU D 365    32464  32362  31898  -1892  -2293   -483       C
ATOM   3859  CD  GLU D 365       8.284 -58.095 -22.933  1.00221.53           C
ANISOU 3859  CD  GLU D 365    28303  28189  27680  -1893  -2413   -513       C
ATOM   3860  OE1 GLU D 365       7.514 -57.329 -22.312  1.00234.57           O
ANISOU 3860  OE1 GLU D 365    29994  29774  29358  -1865  -2515   -553       O
ATOM   3861  OE2 GLU D 365       8.340 -58.124 -24.186  1.00154.15           O
ANISOU 3861  OE2 GLU D 365    19748  19733  19091  -1921  -2405   -493       O
ATOM   3862  N   LEU D 366      12.605 -59.460 -21.208  1.00197.69           N
ANISOU 3862  N   LEU D 366    25229  25155  24729  -1969  -2193   -172       N
ATOM   3863  CA  LEU D 366      13.408 -60.231 -22.166  1.00194.60           C
ANISOU 3863  CA  LEU D 366    24793  24855  24292  -1996  -2082   -116       C
ATOM   3864  C   LEU D 366      13.809 -61.643 -21.701  1.00183.65           C
ANISOU 3864  C   LEU D 366    23367  23482  22929  -1984  -1906   -155       C
ATOM   3865  O   LEU D 366      13.984 -61.903 -20.510  1.00169.42           O
ANISOU 3865  O   LEU D 366    21569  21619  21186  -1971  -1875   -164       O
ATOM   3866  CB  LEU D 366      14.636 -59.431 -22.630  1.00208.95           C
ANISOU 3866  CB  LEU D 366    26613  26699  26082  -2045  -2159     70       C
ATOM   3867  CG  LEU D 366      15.905 -59.332 -21.772  1.00216.94           C
ANISOU 3867  CG  LEU D 366    27627  27672  27130  -2073  -2155    210       C
ATOM   3868  CD1 LEU D 366      15.579 -59.254 -20.289  1.00220.07           C
ANISOU 3868  CD1 LEU D 366    28053  27966  27597  -2048  -2175    157       C
ATOM   3869  CD2 LEU D 366      16.859 -60.486 -22.048  1.00218.44           C
ANISOU 3869  CD2 LEU D 366    27768  27926  27303  -2086  -1991    261       C
ATOM   3870  N   PHE D 367      13.931 -62.549 -22.665  1.00189.33           N
ANISOU 3870  N   PHE D 367    24051  24285  23602  -1986  -1792   -181       N
ATOM   3871  CA  PHE D 367      14.296 -63.938 -22.407  1.00200.98           C
ANISOU 3871  CA  PHE D 367    25487  25784  25093  -1975  -1620   -221       C
ATOM   3872  C   PHE D 367      15.819 -64.067 -22.228  1.00181.25           C
ANISOU 3872  C   PHE D 367    22970  23302  22596  -2010  -1570    -61       C
ATOM   3873  O   PHE D 367      16.585 -63.342 -22.856  1.00168.87           O
ANISOU 3873  O   PHE D 367    21406  21767  20988  -2043  -1639     75       O
ATOM   3874  CB  PHE D 367      13.794 -64.818 -23.561  1.00200.89           C
ANISOU 3874  CB  PHE D 367    25451  25852  25026  -1961  -1526   -314       C
ATOM   3875  CG  PHE D 367      13.750 -66.281 -23.236  1.00218.04           C
ANISOU 3875  CG  PHE D 367    27589  28035  27221  -1937  -1360   -403       C
ATOM   3876  CD1 PHE D 367      14.833 -67.103 -23.514  1.00211.71           C
ANISOU 3876  CD1 PHE D 367    26755  27285  26399  -1952  -1237   -331       C
ATOM   3877  CD2 PHE D 367      12.625 -66.835 -22.650  1.00226.73           C
ANISOU 3877  CD2 PHE D 367    28688  29098  28363  -1899  -1329   -555       C
ATOM   3878  CE1 PHE D 367      14.796 -68.450 -23.211  1.00210.05           C
ANISOU 3878  CE1 PHE D 367    26513  27083  26213  -1931  -1086   -413       C
ATOM   3879  CE2 PHE D 367      12.580 -68.181 -22.343  1.00231.91           C
ANISOU 3879  CE2 PHE D 367    29308  29763  29044  -1879  -1182   -635       C
ATOM   3880  CZ  PHE D 367      13.668 -68.991 -22.624  1.00228.26           C
ANISOU 3880  CZ  PHE D 367    28815  29349  28563  -1896  -1061   -567       C
ATOM   3881  N   TYR D 368      16.260 -64.986 -21.375  1.00171.46           N
ANISOU 3881  N   TYR D 368    21705  22040  21403  -2004  -1452    -72       N
ATOM   3882  CA  TYR D 368      17.677 -65.074 -21.023  1.00158.85           C
ANISOU 3882  CA  TYR D 368    20092  20448  19817  -2038  -1408     84       C
ATOM   3883  C   TYR D 368      18.345 -66.410 -21.431  1.00169.25           C
ANISOU 3883  C   TYR D 368    21362  21833  21114  -2038  -1228     91       C
ATOM   3884  O   TYR D 368      17.808 -67.487 -21.172  1.00191.83           O
ANISOU 3884  O   TYR D 368    24197  24692  23996  -2009  -1114    -37       O
ATOM   3885  CB  TYR D 368      17.848 -64.800 -19.508  1.00120.73           C
ANISOU 3885  CB  TYR D 368    15279  15525  15068  -2041  -1442    104       C
ATOM   3886  CG  TYR D 368      19.276 -64.882 -18.993  1.00150.42           C
ANISOU 3886  CG  TYR D 368    19024  19279  18850  -2080  -1399    266       C
ATOM   3887  CD1 TYR D 368      19.920 -66.113 -18.874  1.00175.15           C
ANISOU 3887  CD1 TYR D 368    22109  22447  21992  -2082  -1230    274       C
ATOM   3888  CD2 TYR D 368      19.979 -63.734 -18.606  1.00119.31           C
ANISOU 3888  CD2 TYR D 368    15117  15294  14921  -2116  -1530    414       C
ATOM   3889  CE1 TYR D 368      21.226 -66.209 -18.401  1.00155.56           C
ANISOU 3889  CE1 TYR D 368    19612  19961  19531  -2120  -1186    427       C
ATOM   3890  CE2 TYR D 368      21.299 -63.823 -18.130  1.00112.69           C
ANISOU 3890  CE2 TYR D 368    14265  14450  14103  -2155  -1491    571       C
ATOM   3891  CZ  TYR D 368      21.906 -65.072 -18.030  1.00135.70           C
ANISOU 3891  CZ  TYR D 368    17130  17403  17026  -2157  -1316    577       C
ATOM   3892  OH  TYR D 368      23.188 -65.208 -17.571  1.00123.44           O
ANISOU 3892  OH  TYR D 368    15561  15848  15493  -2197  -1269    733       O
ATOM   3893  N   SER D 369      19.505 -66.332 -22.085  1.00141.07           N
ANISOU 3893  N   SER D 369    17778  18321  17499  -2069  -1205    242       N
ATOM   3894  CA  SER D 369      20.394 -67.496 -22.216  1.00161.83           C
ANISOU 3894  CA  SER D 369    20367  21003  20119  -2072  -1038    284       C
ATOM   3895  C   SER D 369      21.874 -67.120 -22.127  1.00188.47           C
ANISOU 3895  C   SER D 369    23731  24392  23486  -2113  -1043    495       C
ATOM   3896  O   SER D 369      22.275 -66.014 -22.507  1.00150.40           O
ANISOU 3896  O   SER D 369    18931  19577  18637  -2140  -1171    618       O
ATOM   3897  CB  SER D 369      20.155 -68.270 -23.507  1.00173.45           C
ANISOU 3897  CB  SER D 369    21821  22564  21519  -2050   -948    220       C
ATOM   3898  OG  SER D 369      21.123 -69.304 -23.632  1.00167.14           O
ANISOU 3898  OG  SER D 369    20986  21814  20707  -2052   -793    279       O
ATOM   3899  N   TYR D 370      22.685 -68.054 -21.634  1.00226.05           N
ANISOU 3899  N   TYR D 370    28458  29159  28272  -2120   -905    539       N
ATOM   3900  CA  TYR D 370      24.094 -67.773 -21.355  1.00229.29           C
ANISOU 3900  CA  TYR D 370    28858  29575  28688  -2162   -901    742       C
ATOM   3901  C   TYR D 370      24.807 -67.242 -22.590  1.00206.85           C
ANISOU 3901  C   TYR D 370    26014  26815  25764  -2178   -945    886       C
ATOM   3902  O   TYR D 370      25.402 -66.165 -22.548  1.00201.25           O
ANISOU 3902  O   TYR D 370    25322  26091  25052  -2212  -1070   1036       O
ATOM   3903  CB  TYR D 370      24.814 -69.012 -20.800  1.00229.38           C
ANISOU 3903  CB  TYR D 370    28827  29595  28733  -2163   -723    758       C
ATOM   3904  CG  TYR D 370      26.225 -68.751 -20.296  1.00189.65           C
ANISOU 3904  CG  TYR D 370    23784  24556  23720  -2209   -716    966       C
ATOM   3905  CD1 TYR D 370      26.589 -67.506 -19.790  1.00162.15           C
ANISOU 3905  CD1 TYR D 370    20334  21017  20260  -2246   -870   1090       C
ATOM   3906  CD2 TYR D 370      27.195 -69.745 -20.347  1.00175.39           C
ANISOU 3906  CD2 TYR D 370    21936  22797  21906  -2216   -557   1042       C
ATOM   3907  CE1 TYR D 370      27.882 -67.261 -19.345  1.00163.15           C
ANISOU 3907  CE1 TYR D 370    20450  21135  20402  -2292   -869   1288       C
ATOM   3908  CE2 TYR D 370      28.492 -69.511 -19.902  1.00178.00           C
ANISOU 3908  CE2 TYR D 370    22256  23123  22254  -2260   -549   1242       C
ATOM   3909  CZ  TYR D 370      28.832 -68.267 -19.402  1.00171.58           C
ANISOU 3909  CZ  TYR D 370    21475  22254  21464  -2299   -707   1366       C
ATOM   3910  OH  TYR D 370      30.123 -68.033 -18.962  1.00138.58           O
ANISOU 3910  OH  TYR D 370    17286  18069  17302  -2347   -703   1572       O
ATOM   3911  N   ALA D 371      24.725 -67.983 -23.692  1.00198.50           N
ANISOU 3911  N   ALA D 371    24936  25844  24641  -2151   -849    839       N
ATOM   3912  CA  ALA D 371      25.386 -67.583 -24.937  1.00202.47           C
ANISOU 3912  CA  ALA D 371    25432  26437  25061  -2159   -877    969       C
ATOM   3913  C   ALA D 371      25.039 -66.153 -25.380  1.00190.70           C
ANISOU 3913  C   ALA D 371    23970  24939  23548  -2176  -1071   1018       C
ATOM   3914  O   ALA D 371      25.902 -65.425 -25.877  1.00170.40           O
ANISOU 3914  O   ALA D 371    21394  22410  20941  -2203  -1142   1195       O
ATOM   3915  CB  ALA D 371      25.074 -68.580 -26.048  1.00198.29           C
ANISOU 3915  CB  ALA D 371    24885  25994  24463  -2119   -755    872       C
ATOM   3916  N   THR D 372      23.775 -65.766 -25.207  1.00188.21           N
ANISOU 3916  N   THR D 372    23684  24573  23255  -2161  -1155    866       N
ATOM   3917  CA  THR D 372      23.304 -64.421 -25.554  1.00171.90           C
ANISOU 3917  CA  THR D 372    21648  22492  21176  -2175  -1340    891       C
ATOM   3918  C   THR D 372      23.738 -63.335 -24.579  1.00183.60           C
ANISOU 3918  C   THR D 372    23155  23890  22713  -2212  -1476   1008       C
ATOM   3919  O   THR D 372      24.230 -62.277 -24.983  1.00179.23           O
ANISOU 3919  O   THR D 372    22611  23352  22137  -2241  -1605   1150       O
ATOM   3920  CB  THR D 372      21.760 -64.344 -25.557  1.00149.00           C
ANISOU 3920  CB  THR D 372    18772  19553  18288  -2145  -1386    688       C
ATOM   3921  OG1 THR D 372      21.216 -65.317 -26.455  1.00178.16           O
ANISOU 3921  OG1 THR D 372    22447  23314  21930  -2112  -1273    566       O
ATOM   3922  CG2 THR D 372      21.294 -62.940 -25.954  1.00 89.29           C
ANISOU 3922  CG2 THR D 372    11238  11976  10710  -2161  -1576    720       C
ATOM   3923  N   HIS D 373      23.479 -63.585 -23.298  1.00177.67           N
ANISOU 3923  N   HIS D 373    22419  23051  22036  -2208  -1454    940       N
ATOM   3924  CA  HIS D 373      23.516 -62.537 -22.282  1.00160.40           C
ANISOU 3924  CA  HIS D 373    20270  20769  19907  -2233  -1597    997       C
ATOM   3925  C   HIS D 373      24.741 -62.412 -21.346  1.00168.62           C
ANISOU 3925  C   HIS D 373    21309  21766  20992  -2272  -1593   1163       C
ATOM   3926  O   HIS D 373      24.755 -61.548 -20.467  1.00153.54           O
ANISOU 3926  O   HIS D 373    19437  19771  19129  -2292  -1715   1206       O
ATOM   3927  CB  HIS D 373      22.199 -62.538 -21.501  1.00141.37           C
ANISOU 3927  CB  HIS D 373    17889  18280  17547  -2200  -1627    808       C
ATOM   3928  CG  HIS D 373      20.991 -62.306 -22.356  1.00134.88           C
ANISOU 3928  CG  HIS D 373    17079  17485  16685  -2170  -1679    673       C
ATOM   3929  ND1 HIS D 373      20.724 -61.097 -22.958  1.00162.39           N
ANISOU 3929  ND1 HIS D 373    20589  20973  20139  -2184  -1840    719       N
ATOM   3930  CD2 HIS D 373      19.971 -63.132 -22.706  1.00116.69           C
ANISOU 3930  CD2 HIS D 373    14763  15206  14369  -2131  -1592    497       C
ATOM   3931  CE1 HIS D 373      19.597 -61.183 -23.643  1.00169.10           C
ANISOU 3931  CE1 HIS D 373    21442  21850  20959  -2155  -1846    578       C
ATOM   3932  NE2 HIS D 373      19.121 -62.409 -23.502  1.00152.24           N
ANISOU 3932  NE2 HIS D 373    19285  19726  18833  -2123  -1699    443       N
ATOM   3933  N   HIS D 374      25.757 -63.254 -21.513  1.00183.49           N
ANISOU 3933  N   HIS D 374    23152  23706  22859  -2284  -1456   1258       N
ATOM   3934  CA  HIS D 374      26.939 -63.168 -20.644  1.00182.95           C
ANISOU 3934  CA  HIS D 374    23081  23600  22833  -2325  -1446   1424       C
ATOM   3935  C   HIS D 374      27.626 -61.792 -20.681  1.00188.44           C
ANISOU 3935  C   HIS D 374    23803  24272  23522  -2370  -1625   1614       C
ATOM   3936  O   HIS D 374      28.446 -61.477 -19.822  1.00162.26           O
ANISOU 3936  O   HIS D 374    20499  20903  20250  -2408  -1659   1745       O
ATOM   3937  CB  HIS D 374      27.948 -64.293 -20.926  1.00187.85           C
ANISOU 3937  CB  HIS D 374    23651  24293  23432  -2329  -1267   1506       C
ATOM   3938  CG  HIS D 374      28.442 -64.332 -22.339  1.00204.68           C
ANISOU 3938  CG  HIS D 374    25756  26537  25477  -2325  -1244   1597       C
ATOM   3939  ND1 HIS D 374      28.886 -63.213 -23.009  1.00205.18           N
ANISOU 3939  ND1 HIS D 374    25829  26631  25500  -2350  -1387   1747       N
ATOM   3940  CD2 HIS D 374      28.570 -65.365 -23.211  1.00190.35           C
ANISOU 3940  CD2 HIS D 374    23904  24813  23607  -2295  -1094   1560       C
ATOM   3941  CE1 HIS D 374      29.258 -63.549 -24.232  1.00190.93           C
ANISOU 3941  CE1 HIS D 374    23993  24934  23619  -2335  -1325   1800       C
ATOM   3942  NE2 HIS D 374      29.077 -64.851 -24.377  1.00181.74           N
ANISOU 3942  NE2 HIS D 374    22803  23807  22443  -2300  -1147   1687       N
ATOM   3943  N   ASP D 375      27.331 -60.995 -21.704  1.00217.87           N
ANISOU 3943  N   ASP D 375    27540  28045  27196  -2368  -1738   1636       N
ATOM   3944  CA  ASP D 375      27.791 -59.606 -21.743  1.00216.79           C
ANISOU 3944  CA  ASP D 375    27432  27881  27059  -2407  -1929   1795       C
ATOM   3945  C   ASP D 375      26.760 -58.582 -21.238  1.00195.59           C
ANISOU 3945  C   ASP D 375    24803  25104  24408  -2400  -2096   1696       C
ATOM   3946  O   ASP D 375      27.100 -57.413 -21.029  1.00188.86           O
ANISOU 3946  O   ASP D 375    23984  24206  23569  -2433  -2262   1818       O
ATOM   3947  CB  ASP D 375      28.280 -59.234 -23.155  1.00226.85           C
ANISOU 3947  CB  ASP D 375    28676  29262  28255  -2415  -1967   1918       C
ATOM   3948  CG  ASP D 375      27.283 -59.606 -24.249  1.00222.12           C
ANISOU 3948  CG  ASP D 375    28061  28734  27601  -2372  -1923   1759       C
ATOM   3949  OD1 ASP D 375      26.291 -58.869 -24.435  1.00220.20           O
ANISOU 3949  OD1 ASP D 375    27847  28460  27357  -2361  -2043   1661       O
ATOM   3950  OD2 ASP D 375      27.500 -60.630 -24.935  1.00208.82           O
ANISOU 3950  OD2 ASP D 375    26337  27135  25871  -2349  -1770   1735       O
ATOM   3951  N   LYS D 376      25.519 -59.028 -21.020  1.00165.15           N
ANISOU 3951  N   LYS D 376    20959  21220  20569  -2356  -2051   1480       N
ATOM   3952  CA  LYS D 376      24.378 -58.114 -20.846  1.00170.43           C
ANISOU 3952  CA  LYS D 376    21677  21826  21253  -2338  -2198   1369       C
ATOM   3953  C   LYS D 376      24.321 -57.386 -19.505  1.00198.47           C
ANISOU 3953  C   LYS D 376    25283  25255  24872  -2349  -2310   1383       C
ATOM   3954  O   LYS D 376      24.030 -56.187 -19.469  1.00193.39           O
ANISOU 3954  O   LYS D 376    24683  24563  24232  -2359  -2486   1413       O
ATOM   3955  CB  LYS D 376      23.044 -58.829 -21.117  1.00168.14           C
ANISOU 3955  CB  LYS D 376    21380  21553  20954  -2285  -2116   1142       C
ATOM   3956  CG  LYS D 376      22.209 -58.210 -22.241  1.00173.75           C
ANISOU 3956  CG  LYS D 376    22095  22309  21613  -2272  -2207   1082       C
ATOM   3957  CD  LYS D 376      20.954 -57.492 -21.729  1.00174.25           C
ANISOU 3957  CD  LYS D 376    22208  22291  21707  -2246  -2325    948       C
ATOM   3958  CE  LYS D 376      19.694 -58.346 -21.912  1.00163.16           C
ANISOU 3958  CE  LYS D 376    20793  20903  20297  -2197  -2226    735       C
ATOM   3959  NZ  LYS D 376      18.500 -57.563 -22.372  1.00134.17           N
ANISOU 3959  NZ  LYS D 376    17149  17219  16609  -2177  -2344    636       N
ATOM   3960  N   PHE D 377      24.545 -58.114 -18.409  1.00218.87           N
ANISOU 3960  N   PHE D 377    27864  27789  27509  -2346  -2210   1352       N
ATOM   3961  CA  PHE D 377      24.680 -57.488 -17.094  1.00198.07           C
ANISOU 3961  CA  PHE D 377    25280  25041  24936  -2360  -2305   1387       C
ATOM   3962  C   PHE D 377      26.036 -57.808 -16.483  1.00202.58           C
ANISOU 3962  C   PHE D 377    25834  25602  25534  -2406  -2245   1554       C
ATOM   3963  O   PHE D 377      26.274 -58.931 -16.039  1.00194.98           O
ANISOU 3963  O   PHE D 377    24835  24653  24595  -2399  -2082   1515       O
ATOM   3964  CB  PHE D 377      23.616 -58.009 -16.127  1.00167.81           C
ANISOU 3964  CB  PHE D 377    21463  21145  21153  -2312  -2249   1189       C
ATOM   3965  CG  PHE D 377      22.228 -58.084 -16.708  1.00171.06           C
ANISOU 3965  CG  PHE D 377    21876  21578  21539  -2261  -2253   1003       C
ATOM   3966  CD1 PHE D 377      21.725 -59.290 -17.206  1.00135.14           C
ANISOU 3966  CD1 PHE D 377    17278  17097  16971  -2229  -2091    875       C
ATOM   3967  CD2 PHE D 377      21.409 -56.958 -16.732  1.00187.43           C
ANISOU 3967  CD2 PHE D 377    24003  23602  23610  -2245  -2420    957       C
ATOM   3968  CE1 PHE D 377      20.425 -59.362 -17.727  1.00122.39           C
ANISOU 3968  CE1 PHE D 377    15667  15500  15335  -2185  -2099    707       C
ATOM   3969  CE2 PHE D 377      20.111 -57.022 -17.252  1.00161.98           C
ANISOU 3969  CE2 PHE D 377    20781  20399  20365  -2200  -2424    791       C
ATOM   3970  CZ  PHE D 377      19.621 -58.223 -17.746  1.00134.34           C
ANISOU 3970  CZ  PHE D 377    17231  16966  16845  -2171  -2264    668       C
ATOM   3971  N   THR D 378      26.922 -56.821 -16.449  1.00218.95           N
ANISOU 3971  N   THR D 378    27933  27651  27605  -2455  -2380   1745       N
ATOM   3972  CA  THR D 378      28.152 -56.926 -15.674  1.00221.67           C
ANISOU 3972  CA  THR D 378    28276  27963  27985  -2503  -2356   1912       C
ATOM   3973  C   THR D 378      27.986 -56.240 -14.312  1.00189.40           C
ANISOU 3973  C   THR D 378    24256  23747  23962  -2511  -2470   1902       C
ATOM   3974  O   THR D 378      28.800 -56.416 -13.400  1.00142.08           O
ANISOU 3974  O   THR D 378    18268  17707  18010  -2545  -2441   2000       O
ATOM   3975  CB  THR D 378      29.350 -56.330 -16.452  1.00227.41           C
ANISOU 3975  CB  THR D 378    28988  28746  28672  -2555  -2428   2150       C
ATOM   3976  OG1 THR D 378      28.996 -55.037 -16.959  1.00238.12           O
ANISOU 3976  OG1 THR D 378    30384  30084  30006  -2560  -2626   2184       O
ATOM   3977  CG2 THR D 378      29.729 -57.227 -17.631  1.00206.16           C
ANISOU 3977  CG2 THR D 378    26226  26184  25922  -2546  -2279   2177       C
ATOM   3978  N   ASP D 379      26.889 -55.500 -14.177  1.00182.42           N
ANISOU 3978  N   ASP D 379    23422  22807  23082  -2475  -2593   1776       N
ATOM   3979  CA  ASP D 379      26.714 -54.545 -13.089  1.00165.97           C
ANISOU 3979  CA  ASP D 379    21414  20603  21044  -2480  -2746   1784       C
ATOM   3980  C   ASP D 379      25.831 -55.097 -11.981  1.00209.23           C
ANISOU 3980  C   ASP D 379    26910  26016  26572  -2431  -2676   1600       C
ATOM   3981  O   ASP D 379      24.875 -55.829 -12.243  1.00231.55           O
ANISOU 3981  O   ASP D 379    29707  28882  29391  -2380  -2574   1424       O
ATOM   3982  CB  ASP D 379      26.104 -53.240 -13.621  1.00172.03           C
ANISOU 3982  CB  ASP D 379    22233  21346  21785  -2471  -2945   1779       C
ATOM   3983  CG  ASP D 379      24.681 -53.423 -14.171  1.00180.28           C
ANISOU 3983  CG  ASP D 379    23271  22421  22806  -2409  -2921   1569       C
ATOM   3984  OD1 ASP D 379      24.467 -54.265 -15.081  1.00159.59           O
ANISOU 3984  OD1 ASP D 379    20591  19899  20149  -2393  -2790   1508       O
ATOM   3985  OD2 ASP D 379      23.770 -52.711 -13.689  1.00163.66           O
ANISOU 3985  OD2 ASP D 379    21225  20240  20718  -2375  -3035   1468       O
ATOM   3986  N   GLY D 380      26.159 -54.738 -10.742  1.00210.35           N
ANISOU 3986  N   GLY D 380    27100  26059  26765  -2447  -2736   1645       N
ATOM   3987  CA  GLY D 380      25.374 -55.135  -9.585  1.00194.27           C
ANISOU 3987  CA  GLY D 380    25083  23953  24778  -2400  -2690   1485       C
ATOM   3988  C   GLY D 380      25.184 -56.635  -9.464  1.00192.22           C
ANISOU 3988  C   GLY D 380    24748  23751  24535  -2376  -2469   1374       C
ATOM   3989  O   GLY D 380      26.131 -57.403  -9.664  1.00200.33           O
ANISOU 3989  O   GLY D 380    25721  24834  25562  -2414  -2344   1473       O
ATOM   3990  N   VAL D 381      23.961 -57.056  -9.140  1.00175.87           N
ANISOU 3990  N   VAL D 381    22675  21668  22481  -2311  -2421   1172       N
ATOM   3991  CA  VAL D 381      23.675 -58.477  -8.930  1.00143.83           C
ANISOU 3991  CA  VAL D 381    18547  17656  18445  -2283  -2221   1054       C
ATOM   3992  C   VAL D 381      22.356 -58.931  -9.548  1.00145.85           C
ANISOU 3992  C   VAL D 381    18780  17959  18677  -2220  -2170    861       C
ATOM   3993  O   VAL D 381      21.314 -58.270  -9.380  1.00 89.83           O
ANISOU 3993  O   VAL D 381    11733  10819  11581  -2174  -2277    755       O
ATOM   3994  CB  VAL D 381      23.657 -58.829  -7.431  1.00139.90           C
ANISOU 3994  CB  VAL D 381    18057  17082  18017  -2271  -2179   1008       C
ATOM   3995  CG1 VAL D 381      22.477 -58.149  -6.727  1.00112.46           C
ANISOU 3995  CG1 VAL D 381    14644  13527  14560  -2210  -2294    872       C
ATOM   3996  CG2 VAL D 381      23.626 -60.340  -7.243  1.00136.39           C
ANISOU 3996  CG2 VAL D 381    17531  16693  17601  -2257  -1966    923       C
ATOM   3997  N   CYS D 382      22.408 -60.053 -10.267  1.00178.20           N
ANISOU 3997  N   CYS D 382    22807  22147  22755  -2217  -2009    819       N
ATOM   3998  CA  CYS D 382      21.195 -60.659 -10.811  1.00195.44           C
ANISOU 3998  CA  CYS D 382    24962  24376  24919  -2160  -1943    636       C
ATOM   3999  C   CYS D 382      20.816 -61.905 -10.009  1.00187.62           C
ANISOU 3999  C   CYS D 382    23922  23385  23980  -2127  -1785    512       C
ATOM   4000  O   CYS D 382      21.691 -62.610  -9.473  1.00135.16           O
ANISOU 4000  O   CYS D 382    17239  16744  17370  -2158  -1676    580       O
ATOM   4001  CB  CYS D 382      21.293 -60.937 -12.326  1.00181.83           C
ANISOU 4001  CB  CYS D 382    23205  22755  23128  -2171  -1897    655       C
ATOM   4002  SG  CYS D 382      22.878 -61.569 -12.963  1.00200.24           S
ANISOU 4002  SG  CYS D 382    25482  25166  25433  -2233  -1781    839       S
ATOM   4003  N   LEU D 383      19.505 -62.142  -9.919  1.00192.98           N
ANISOU 4003  N   LEU D 383    24599  24058  24666  -2066  -1777    335       N
ATOM   4004  CA  LEU D 383      18.931 -63.157  -9.040  1.00169.83           C
ANISOU 4004  CA  LEU D 383    21625  21114  21789  -2025  -1659    203       C
ATOM   4005  C   LEU D 383      17.795 -63.944  -9.714  1.00163.10           C
ANISOU 4005  C   LEU D 383    20734  20320  20916  -1975  -1579     38       C
ATOM   4006  O   LEU D 383      16.838 -63.358 -10.252  1.00125.62           O
ANISOU 4006  O   LEU D 383    16020  15573  16135  -1942  -1671    -38       O
ATOM   4007  CB  LEU D 383      18.410 -62.483  -7.769  1.00164.30           C
ANISOU 4007  CB  LEU D 383    20975  20318  21136  -1991  -1761    159       C
ATOM   4008  CG  LEU D 383      17.072 -62.984  -7.218  1.00163.55           C
ANISOU 4008  CG  LEU D 383    20862  20209  21071  -1917  -1724    -27       C
ATOM   4009  CD1 LEU D 383      17.307 -64.032  -6.141  1.00152.48           C
ANISOU 4009  CD1 LEU D 383    19402  18796  19736  -1911  -1589    -62       C
ATOM   4010  CD2 LEU D 383      16.224 -61.829  -6.672  1.00127.46           C
ANISOU 4010  CD2 LEU D 383    16366  15561  16502  -1871  -1888    -76       C
ATOM   4011  N   PHE D 384      17.896 -65.271  -9.671  1.00162.03           N
ANISOU 4011  N   PHE D 384    20529  20231  20803  -1971  -1411    -17       N
ATOM   4012  CA  PHE D 384      16.861 -66.122 -10.247  1.00184.35           C
ANISOU 4012  CA  PHE D 384    23318  23111  23617  -1926  -1329   -171       C
ATOM   4013  C   PHE D 384      16.121 -66.913  -9.154  1.00162.90           C
ANISOU 4013  C   PHE D 384    20563  20364  20966  -1878  -1254   -301       C
ATOM   4014  O   PHE D 384      16.738 -67.737  -8.472  1.00154.02           O
ANISOU 4014  O   PHE D 384    19390  19241  19891  -1895  -1140   -279       O
ATOM   4015  CB  PHE D 384      17.471 -67.119 -11.254  1.00207.28           C
ANISOU 4015  CB  PHE D 384    26170  26103  26485  -1954  -1190   -143       C
ATOM   4016  CG  PHE D 384      18.500 -66.523 -12.211  1.00199.13           C
ANISOU 4016  CG  PHE D 384    25158  25108  25393  -2006  -1234     15       C
ATOM   4017  CD1 PHE D 384      18.120 -65.674 -13.246  1.00176.92           C
ANISOU 4017  CD1 PHE D 384    22386  22319  22517  -2005  -1345     25       C
ATOM   4018  CD2 PHE D 384      19.843 -66.861 -12.103  1.00183.87           C
ANISOU 4018  CD2 PHE D 384    23201  23194  23468  -2056  -1158    157       C
ATOM   4019  CE1 PHE D 384      19.071 -65.147 -14.130  1.00131.32           C
ANISOU 4019  CE1 PHE D 384    16623  16585  16689  -2051  -1386    174       C
ATOM   4020  CE2 PHE D 384      20.796 -66.342 -12.990  1.00155.80           C
ANISOU 4020  CE2 PHE D 384    19660  19680  19857  -2101  -1197    310       C
ATOM   4021  CZ  PHE D 384      20.409 -65.484 -14.000  1.00122.61           C
ANISOU 4021  CZ  PHE D 384    15493  15500  15592  -2097  -1312    319       C
ATOM   4022  N   TRP D 385      14.810 -66.704  -8.995  1.00146.85           N
ANISOU 4022  N   TRP D 385    18547  18311  18939  -1819  -1312   -433       N
ATOM   4023  CA  TRP D 385      14.050 -67.562  -8.075  1.00175.74           C
ANISOU 4023  CA  TRP D 385    22159  21956  22657  -1770  -1233   -559       C
ATOM   4024  C   TRP D 385      13.334 -68.647  -8.865  1.00162.01           C
ANISOU 4024  C   TRP D 385    20367  20286  20902  -1746  -1127   -675       C
ATOM   4025  O   TRP D 385      12.323 -68.383  -9.527  1.00137.62           O
ANISOU 4025  O   TRP D 385    17300  17213  17776  -1713  -1184   -757       O
ATOM   4026  CB  TRP D 385      13.023 -66.769  -7.249  1.00204.14           C
ANISOU 4026  CB  TRP D 385    25800  25487  26277  -1712  -1353   -633       C
ATOM   4027  CG  TRP D 385      13.542 -66.288  -5.899  1.00221.00           C
ANISOU 4027  CG  TRP D 385    27959  27547  28465  -1715  -1399   -570       C
ATOM   4028  CD1 TRP D 385      13.444 -65.022  -5.384  1.00217.29           C
ANISOU 4028  CD1 TRP D 385    27565  27005  27991  -1702  -1552   -529       C
ATOM   4029  CD2 TRP D 385      14.241 -67.067  -4.906  1.00178.19           C
ANISOU 4029  CD2 TRP D 385    22483  22113  23106  -1732  -1291   -542       C
ATOM   4030  NE1 TRP D 385      14.030 -64.969  -4.135  1.00180.50           N
ANISOU 4030  NE1 TRP D 385    22908  22290  23386  -1710  -1548   -479       N
ATOM   4031  CE2 TRP D 385      14.536 -66.206  -3.828  1.00167.02           C
ANISOU 4031  CE2 TRP D 385    21120  20620  21722  -1730  -1389   -483       C
ATOM   4032  CE3 TRP D 385      14.648 -68.405  -4.829  1.00119.02           C
ANISOU 4032  CE3 TRP D 385    14907  14668  15648  -1750  -1124   -560       C
ATOM   4033  CZ2 TRP D 385      15.218 -66.642  -2.692  1.00149.73           C
ANISOU 4033  CZ2 TRP D 385    18896  18399  19594  -1748  -1323   -441       C
ATOM   4034  CZ3 TRP D 385      15.319 -68.830  -3.699  1.00135.84           C
ANISOU 4034  CZ3 TRP D 385    17000  16769  17843  -1767  -1058   -517       C
ATOM   4035  CH2 TRP D 385      15.596 -67.953  -2.644  1.00135.49           C
ANISOU 4035  CH2 TRP D 385    17006  16648  17828  -1767  -1156   -458       C
ATOM   4036  N   ASN D 386      13.850 -69.872  -8.760  1.00170.95           N
ANISOU 4036  N   ASN D 386    21432  21457  22065  -1762   -973   -680       N
ATOM   4037  CA  ASN D 386      13.377 -70.972  -9.589  1.00209.47           C
ANISOU 4037  CA  ASN D 386    26263  26402  26924  -1749   -865   -774       C
ATOM   4038  C   ASN D 386      13.200 -70.539 -11.040  1.00227.82           C
ANISOU 4038  C   ASN D 386    28625  28772  29164  -1761   -917   -763       C
ATOM   4039  O   ASN D 386      12.147 -70.751 -11.642  1.00226.41           O
ANISOU 4039  O   ASN D 386    28446  28619  28960  -1727   -926   -871       O
ATOM   4040  CB  ASN D 386      12.096 -71.592  -9.035  1.00208.93           C
ANISOU 4040  CB  ASN D 386    26159  26326  26900  -1686   -839   -927       C
ATOM   4041  CG  ASN D 386      12.332 -72.972  -8.452  1.00197.26           C
ANISOU 4041  CG  ASN D 386    24598  24869  25483  -1684   -683   -970       C
ATOM   4042  OD1 ASN D 386      13.387 -73.573  -8.661  1.00160.80           O
ANISOU 4042  OD1 ASN D 386    19950  20281  20866  -1729   -582   -896       O
ATOM   4043  ND2 ASN D 386      11.350 -73.485  -7.724  1.00216.75           N
ANISOU 4043  ND2 ASN D 386    27027  27324  28003  -1632   -664  -1084       N
ATOM   4044  N   CYS D 387      14.240 -69.920 -11.586  1.00222.55           N
ANISOU 4044  N   CYS D 387    27987  28116  28454  -1811   -953   -626       N
ATOM   4045  CA  CYS D 387      14.220 -69.417 -12.952  1.00198.44           C
ANISOU 4045  CA  CYS D 387    24968  25110  25321  -1827  -1009   -595       C
ATOM   4046  C   CYS D 387      15.127 -70.273 -13.822  1.00170.06           C
ANISOU 4046  C   CYS D 387    21338  21588  21691  -1862   -884   -538       C
ATOM   4047  O   CYS D 387      16.119 -70.820 -13.345  1.00148.66           O
ANISOU 4047  O   CYS D 387    18594  18880  19011  -1889   -791   -464       O
ATOM   4048  CB  CYS D 387      14.686 -67.965 -12.980  1.00201.40           C
ANISOU 4048  CB  CYS D 387    25406  25446  25670  -1855  -1161   -475       C
ATOM   4049  SG  CYS D 387      13.696 -66.880 -13.999  1.00116.27           S
ANISOU 4049  SG  CYS D 387    14680  14673  14823  -1837  -1311   -516       S
ATOM   4050  N   ASN D 388      14.793 -70.387 -15.100  1.00175.18           N
ANISOU 4050  N   ASN D 388    21994  22295  22272  -1859   -880   -571       N
ATOM   4051  CA  ASN D 388      15.513 -71.307 -15.971  1.00201.68           C
ANISOU 4051  CA  ASN D 388    25317  25724  25588  -1880   -753   -538       C
ATOM   4052  C   ASN D 388      16.359 -70.617 -17.038  1.00185.42           C
ANISOU 4052  C   ASN D 388    23286  23710  23455  -1918   -802   -405       C
ATOM   4053  O   ASN D 388      15.853 -69.820 -17.833  1.00201.14           O
ANISOU 4053  O   ASN D 388    25314  25715  25395  -1915   -907   -412       O
ATOM   4054  CB  ASN D 388      14.535 -72.288 -16.628  1.00231.41           C
ANISOU 4054  CB  ASN D 388    29059  29532  29335  -1845   -678   -688       C
ATOM   4055  CG  ASN D 388      13.563 -72.904 -15.631  1.00219.54           C
ANISOU 4055  CG  ASN D 388    27525  27986  27903  -1803   -646   -821       C
ATOM   4056  OD1 ASN D 388      13.795 -72.873 -14.421  1.00214.35           O
ANISOU 4056  OD1 ASN D 388    26852  27279  27313  -1802   -642   -802       O
ATOM   4057  ND2 ASN D 388      12.472 -73.475 -16.139  1.00185.94           N
ANISOU 4057  ND2 ASN D 388    23262  23755  23633  -1769   -626   -954       N
ATOM   4058  N   VAL D 389      17.653 -70.917 -17.046  1.00149.89           N
ANISOU 4058  N   VAL D 389    18765  19235  18951  -1954   -726   -277       N
ATOM   4059  CA  VAL D 389      18.517 -70.462 -18.134  1.00182.27           C
ANISOU 4059  CA  VAL D 389    22881  23394  22979  -1985   -749   -146       C
ATOM   4060  C   VAL D 389      19.544 -71.524 -18.519  1.00185.67           C
ANISOU 4060  C   VAL D 389    23270  23886  23391  -2000   -591    -82       C
ATOM   4061  O   VAL D 389      19.867 -72.404 -17.716  1.00162.03           O
ANISOU 4061  O   VAL D 389    20237  20875  20452  -2000   -478    -99       O
ATOM   4062  CB  VAL D 389      19.242 -69.139 -17.809  1.00161.14           C
ANISOU 4062  CB  VAL D 389    20241  20679  20304  -2023   -883     11       C
ATOM   4063  CG1 VAL D 389      18.459 -68.337 -16.775  1.00133.04           C
ANISOU 4063  CG1 VAL D 389    16716  17033  16800  -2007  -1004    -46       C
ATOM   4064  CG2 VAL D 389      20.659 -69.415 -17.337  1.00157.70           C
ANISOU 4064  CG2 VAL D 389    19781  20246  19891  -2062   -808    163       C
ATOM   4065  N   ASP D 390      20.067 -71.416 -19.739  1.00180.55           N
ANISOU 4065  N   ASP D 390    22627  23309  22663  -2012   -584     -6       N
ATOM   4066  CA  ASP D 390      20.987 -72.413 -20.268  1.00187.53           C
ANISOU 4066  CA  ASP D 390    23477  24260  23516  -2018   -434     52       C
ATOM   4067  C   ASP D 390      22.072 -72.683 -19.235  1.00172.32           C
ANISOU 4067  C   ASP D 390    21522  22303  21648  -2048   -365    164       C
ATOM   4068  O   ASP D 390      22.251 -73.826 -18.789  1.00120.46           O
ANISOU 4068  O   ASP D 390    14913  15738  15117  -2039   -225    117       O
ATOM   4069  CB  ASP D 390      21.609 -71.909 -21.578  1.00207.58           C
ANISOU 4069  CB  ASP D 390    26032  26875  25963  -2032   -470    167       C
ATOM   4070  CG  ASP D 390      22.688 -72.838 -22.117  1.00219.03           C
ANISOU 4070  CG  ASP D 390    27449  28396  27375  -2035   -321    251       C
ATOM   4071  OD1 ASP D 390      22.620 -74.056 -21.839  1.00237.76           O
ANISOU 4071  OD1 ASP D 390    29791  30773  29774  -2016   -180    167       O
ATOM   4072  OD2 ASP D 390      23.604 -72.348 -22.819  1.00194.69           O
ANISOU 4072  OD2 ASP D 390    24372  25366  24236  -2056   -345    405       O
ATOM   4073  N   ARG D 391      22.752 -71.607 -18.837  1.00199.69           N
ANISOU 4073  N   ARG D 391    25012  25737  25125  -2085   -472    312       N
ATOM   4074  CA  ARG D 391      23.836 -71.635 -17.858  1.00174.99           C
ANISOU 4074  CA  ARG D 391    21865  22575  22050  -2122   -433    444       C
ATOM   4075  C   ARG D 391      23.829 -70.299 -17.104  1.00166.32           C
ANISOU 4075  C   ARG D 391    20807  21400  20985  -2147   -601    515       C
ATOM   4076  O   ARG D 391      23.571 -69.234 -17.690  1.00134.21           O
ANISOU 4076  O   ARG D 391    16782  17336  16876  -2150   -741    549       O
ATOM   4077  CB  ARG D 391      25.186 -71.866 -18.555  1.00158.67           C
ANISOU 4077  CB  ARG D 391    19778  20578  19931  -2149   -357    615       C
ATOM   4078  CG  ARG D 391      26.313 -72.329 -17.648  1.00161.10           C
ANISOU 4078  CG  ARG D 391    20052  20867  20291  -2183   -262    735       C
ATOM   4079  CD  ARG D 391      27.257 -73.317 -18.350  1.00192.16           C
ANISOU 4079  CD  ARG D 391    23948  24883  24180  -2184   -103    812       C
ATOM   4080  NE  ARG D 391      28.322 -72.695 -19.142  1.00198.45           N
ANISOU 4080  NE  ARG D 391    24755  25737  24912  -2210   -141   1009       N
ATOM   4081  CZ  ARG D 391      29.405 -73.342 -19.575  1.00181.95           C
ANISOU 4081  CZ  ARG D 391    22634  23712  22787  -2218    -18   1129       C
ATOM   4082  NH1 ARG D 391      29.577 -74.628 -19.287  1.00179.87           N
ANISOU 4082  NH1 ARG D 391    22330  23462  22550  -2203    153   1070       N
ATOM   4083  NH2 ARG D 391      30.322 -72.705 -20.290  1.00166.02           N
ANISOU 4083  NH2 ARG D 391    20624  21746  20709  -2238    -66   1313       N
ATOM   4084  N   TYR D 392      24.126 -70.367 -15.809  1.00162.00           N
ANISOU 4084  N   TYR D 392    20251  20787  20514  -2164   -586    540       N
ATOM   4085  CA  TYR D 392      23.984 -69.240 -14.890  1.00134.95           C
ANISOU 4085  CA  TYR D 392    16868  17276  17132  -2180   -735    578       C
ATOM   4086  C   TYR D 392      25.217 -68.317 -14.808  1.00166.25           C
ANISOU 4086  C   TYR D 392    20854  21227  21085  -2235   -819    797       C
ATOM   4087  O   TYR D 392      26.349 -68.800 -14.747  1.00163.05           O
ANISOU 4087  O   TYR D 392    20418  20851  20683  -2268   -723    925       O
ATOM   4088  CB  TYR D 392      23.698 -69.800 -13.507  1.00123.87           C
ANISOU 4088  CB  TYR D 392    15441  15809  15817  -2170   -676    496       C
ATOM   4089  CG  TYR D 392      22.260 -70.175 -13.295  1.00143.02           C
ANISOU 4089  CG  TYR D 392    17862  18214  18265  -2115   -674    288       C
ATOM   4090  CD1 TYR D 392      21.243 -69.287 -13.617  1.00125.58           C
ANISOU 4090  CD1 TYR D 392    15701  15982  16031  -2088   -814    212       C
ATOM   4091  CD2 TYR D 392      21.910 -71.417 -12.774  1.00150.74           C
ANISOU 4091  CD2 TYR D 392    18786  19196  19292  -2091   -534    173       C
ATOM   4092  CE1 TYR D 392      19.911 -69.620 -13.421  1.00119.45           C
ANISOU 4092  CE1 TYR D 392    14921  15190  15276  -2036   -814     30       C
ATOM   4093  CE2 TYR D 392      20.578 -71.762 -12.577  1.00129.19           C
ANISOU 4093  CE2 TYR D 392    16051  16451  16586  -2040   -537    -10       C
ATOM   4094  CZ  TYR D 392      19.585 -70.856 -12.907  1.00145.10           C
ANISOU 4094  CZ  TYR D 392    18115  18444  18571  -2012   -676    -78       C
ATOM   4095  OH  TYR D 392      18.259 -71.173 -12.730  1.00172.50           O
ANISOU 4095  OH  TYR D 392    21579  21901  22062  -1961   -682   -249       O
ATOM   4096  N   PRO D 393      24.996 -66.983 -14.779  1.00162.08           N
ANISOU 4096  N   PRO D 393    20382  20654  20548  -2245  -1000    843       N
ATOM   4097  CA  PRO D 393      26.087 -65.986 -14.631  1.00120.84           C
ANISOU 4097  CA  PRO D 393    15186  15407  15319  -2299  -1106   1052       C
ATOM   4098  C   PRO D 393      26.937 -66.192 -13.365  1.00155.41           C
ANISOU 4098  C   PRO D 393    19555  19729  19767  -2336  -1061   1146       C
ATOM   4099  O   PRO D 393      26.474 -66.847 -12.438  1.00209.07           O
ANISOU 4099  O   PRO D 393    26331  26484  26622  -2316   -988   1032       O
ATOM   4100  CB  PRO D 393      25.343 -64.634 -14.544  1.00 86.63           C
ANISOU 4100  CB  PRO D 393    10918  11014  10983  -2290  -1307   1025       C
ATOM   4101  CG  PRO D 393      23.824 -64.976 -14.528  1.00120.88           C
ANISOU 4101  CG  PRO D 393    15260  15341  15330  -2230  -1296    796       C
ATOM   4102  CD  PRO D 393      23.684 -66.367 -15.083  1.00106.39           C
ANISOU 4102  CD  PRO D 393    13366  13580  13477  -2206  -1114    704       C
ATOM   4103  N   ALA D 394      28.155 -65.655 -13.312  1.00172.22           N
ANISOU 4103  N   ALA D 394    21692  21855  21889  -2390  -1106   1354       N
ATOM   4104  CA  ALA D 394      28.946 -65.733 -12.078  1.00174.76           C
ANISOU 4104  CA  ALA D 394    22010  22114  22276  -2431  -1081   1452       C
ATOM   4105  C   ALA D 394      28.505 -64.632 -11.114  1.00150.71           C
ANISOU 4105  C   ALA D 394    19027  18962  19273  -2435  -1250   1437       C
ATOM   4106  O   ALA D 394      28.990 -64.546  -9.991  1.00125.07           O
ANISOU 4106  O   ALA D 394    15789  15649  16083  -2465  -1257   1500       O
ATOM   4107  CB  ALA D 394      30.452 -65.632 -12.380  1.00177.46           C
ANISOU 4107  CB  ALA D 394    22336  22495  22595  -2489  -1058   1690       C
ATOM   4108  N   ASN D 395      27.584 -63.797 -11.592  1.00141.62           N
ANISOU 4108  N   ASN D 395    17921  17797  18090  -2404  -1386   1356       N
ATOM   4109  CA  ASN D 395      27.004 -62.676 -10.852  1.00126.20           C
ANISOU 4109  CA  ASN D 395    16037  15749  16166  -2396  -1560   1324       C
ATOM   4110  C   ASN D 395      25.655 -63.016 -10.168  1.00183.39           C
ANISOU 4110  C   ASN D 395    23285  22947  23448  -2334  -1541   1103       C
ATOM   4111  O   ASN D 395      24.946 -62.135  -9.649  1.00140.39           O
ANISOU 4111  O   ASN D 395    17896  17428  18018  -2312  -1680   1044       O
ATOM   4112  CB  ASN D 395      26.866 -61.481 -11.800  1.00112.66           C
ANISOU 4112  CB  ASN D 395    14368  14046  14393  -2401  -1728   1386       C
ATOM   4113  CG  ASN D 395      26.044 -60.356 -11.214  1.00158.70           C
ANISOU 4113  CG  ASN D 395    20270  19785  20243  -2379  -1906   1321       C
ATOM   4114  OD1 ASN D 395      25.067 -59.915 -11.815  1.00199.85           O
ANISOU 4114  OD1 ASN D 395    25504  25007  25423  -2342  -1981   1216       O
ATOM   4115  ND2 ASN D 395      26.429 -59.888 -10.037  1.00147.24           N
ANISOU 4115  ND2 ASN D 395    18858  18244  18843  -2403  -1974   1385       N
ATOM   4116  N   ALA D 396      25.283 -64.293 -10.227  1.00182.01           N
ANISOU 4116  N   ALA D 396    23050  22821  23286  -2305  -1372    981       N
ATOM   4117  CA  ALA D 396      24.002 -64.784  -9.700  1.00145.08           C
ANISOU 4117  CA  ALA D 396    18363  18118  18644  -2244  -1335    773       C
ATOM   4118  C   ALA D 396      23.884 -65.125  -8.205  1.00154.05           C
ANISOU 4118  C   ALA D 396    19490  19183  19860  -2235  -1298    721       C
ATOM   4119  O   ALA D 396      24.874 -65.386  -7.505  1.00128.34           O
ANISOU 4119  O   ALA D 396    16215  15906  16642  -2279  -1242    832       O
ATOM   4120  CB  ALA D 396      23.503 -65.951 -10.534  1.00107.80           C
ANISOU 4120  CB  ALA D 396    13583  13481  13896  -2211  -1188    653       C
ATOM   4121  N   ILE D 397      22.640 -65.095  -7.737  1.00168.44           N
ANISOU 4121  N   ILE D 397    21325  20968  21705  -2176  -1331    553       N
ATOM   4122  CA  ILE D 397      22.223 -65.851  -6.562  1.00142.17           C
ANISOU 4122  CA  ILE D 397    17963  17606  18449  -2147  -1245    448       C
ATOM   4123  C   ILE D 397      20.955 -66.616  -6.919  1.00127.34           C
ANISOU 4123  C   ILE D 397    16048  15768  16567  -2083  -1175    254       C
ATOM   4124  O   ILE D 397      19.925 -66.010  -7.259  1.00114.53           O
ANISOU 4124  O   ILE D 397    14466  14134  14917  -2040  -1277    162       O
ATOM   4125  CB  ILE D 397      21.933 -64.954  -5.377  1.00139.13           C
ANISOU 4125  CB  ILE D 397    17635  17122  18104  -2133  -1374    442       C
ATOM   4126  CG1 ILE D 397      23.189 -64.168  -5.015  1.00158.78           C
ANISOU 4126  CG1 ILE D 397    20166  19565  20597  -2199  -1454    639       C
ATOM   4127  CG2 ILE D 397      21.476 -65.790  -4.220  1.00 92.83           C
ANISOU 4127  CG2 ILE D 397    11726  11233  12311  -2098  -1278    331       C
ATOM   4128  CD1 ILE D 397      23.113 -63.469  -3.677  1.00130.48           C
ANISOU 4128  CD1 ILE D 397    16634  15880  17062  -2193  -1556    647       C
ATOM   4129  N   VAL D 398      21.026 -67.944  -6.844  1.00122.25           N
ANISOU 4129  N   VAL D 398    15328  15171  15951  -2079  -1004    196       N
ATOM   4130  CA  VAL D 398      19.955 -68.768  -7.406  1.00156.13           C
ANISOU 4130  CA  VAL D 398    19581  19513  20230  -2027   -929     31       C
ATOM   4131  C   VAL D 398      19.545 -69.999  -6.583  1.00177.92           C
ANISOU 4131  C   VAL D 398    22269  22276  23057  -1997   -792    -84       C
ATOM   4132  O   VAL D 398      20.347 -70.568  -5.821  1.00122.24           O
ANISOU 4132  O   VAL D 398    15174  15214  16056  -2029   -699    -23       O
ATOM   4133  CB  VAL D 398      20.285 -69.211  -8.854  1.00129.33           C
ANISOU 4133  CB  VAL D 398    16167  16205  16767  -2044   -862     60       C
ATOM   4134  CG1 VAL D 398      21.151 -70.472  -8.855  1.00 97.70           C
ANISOU 4134  CG1 VAL D 398    12090  12248  12782  -2073   -681    101       C
ATOM   4135  CG2 VAL D 398      19.016 -69.445  -9.626  1.00158.39           C
ANISOU 4135  CG2 VAL D 398    19847  19920  20413  -1992   -869    -96       C
ATOM   4136  N   CYS D 399      18.277 -70.383  -6.745  1.00193.67           N
ANISOU 4136  N   CYS D 399    24248  24285  25052  -1938   -783   -247       N
ATOM   4137  CA  CYS D 399      17.745 -71.617  -6.175  1.00179.18           C
ANISOU 4137  CA  CYS D 399    22338  22466  23275  -1905   -655   -368       C
ATOM   4138  C   CYS D 399      16.961 -72.415  -7.230  1.00164.77           C
ANISOU 4138  C   CYS D 399    20484  20708  21413  -1873   -588   -485       C
ATOM   4139  O   CYS D 399      16.102 -71.860  -7.942  1.00134.73           O
ANISOU 4139  O   CYS D 399    16722  16910  17559  -1843   -679   -547       O
ATOM   4140  CB  CYS D 399      16.882 -71.313  -4.951  1.00179.46           C
ANISOU 4140  CB  CYS D 399    22380  22438  23367  -1855   -719   -455       C
ATOM   4141  SG  CYS D 399      15.194 -71.931  -5.038  1.00170.16           S
ANISOU 4141  SG  CYS D 399    21169  21283  22201  -1774   -703   -659       S
ATOM   4142  N   ARG D 400      17.284 -73.708  -7.335  1.00157.07           N
ANISOU 4142  N   ARG D 400    19438  19780  20461  -1883   -430   -512       N
ATOM   4143  CA  ARG D 400      16.693 -74.591  -8.340  1.00165.76           C
ANISOU 4143  CA  ARG D 400    20510  20945  21527  -1859   -352   -612       C
ATOM   4144  C   ARG D 400      15.916 -75.719  -7.692  1.00181.71           C
ANISOU 4144  C   ARG D 400    22459  22969  23612  -1818   -258   -748       C
ATOM   4145  O   ARG D 400      16.307 -76.227  -6.632  1.00195.38           O
ANISOU 4145  O   ARG D 400    24140  24679  25416  -1827   -188   -735       O
ATOM   4146  CB  ARG D 400      17.782 -75.229  -9.206  1.00178.48           C
ANISOU 4146  CB  ARG D 400    22099  22616  23099  -1903   -240   -524       C
ATOM   4147  CG  ARG D 400      18.092 -74.521 -10.511  1.00175.00           C
ANISOU 4147  CG  ARG D 400    21714  22211  22566  -1923   -307   -450       C
ATOM   4148  CD  ARG D 400      17.980 -75.474 -11.692  1.00147.61           C
ANISOU 4148  CD  ARG D 400    18222  18817  19047  -1914   -205   -506       C
ATOM   4149  NE  ARG D 400      16.614 -75.512 -12.203  1.00190.08           N
ANISOU 4149  NE  ARG D 400    23615  24205  24403  -1866   -254   -653       N
ATOM   4150  CZ  ARG D 400      16.152 -74.733 -13.181  1.00194.94           C
ANISOU 4150  CZ  ARG D 400    24284  24836  24947  -1859   -356   -659       C
ATOM   4151  NH1 ARG D 400      16.945 -73.846 -13.773  1.00167.83           N
ANISOU 4151  NH1 ARG D 400    20893  21415  21460  -1895   -423   -527       N
ATOM   4152  NH2 ARG D 400      14.892 -74.843 -13.575  1.00206.54           N
ANISOU 4152  NH2 ARG D 400    25762  26313  26402  -1818   -392   -793       N
ATOM   4153  N   PHE D 401      14.836 -76.137  -8.347  1.00162.12           N
ANISOU 4153  N   PHE D 401    19972  20518  21107  -1777   -256   -875       N
ATOM   4154  CA  PHE D 401      14.089 -77.291  -7.875  1.00158.01           C
ANISOU 4154  CA  PHE D 401    19381  20011  20646  -1739   -165  -1001       C
ATOM   4155  C   PHE D 401      14.715 -78.620  -8.325  1.00153.27           C
ANISOU 4155  C   PHE D 401    18721  19465  20051  -1763     -3  -1002       C
ATOM   4156  O   PHE D 401      14.937 -78.827  -9.524  1.00139.21           O
ANISOU 4156  O   PHE D 401    16961  17730  18201  -1776     27   -990       O
ATOM   4157  CB  PHE D 401      12.642 -77.226  -8.344  1.00159.87           C
ANISOU 4157  CB  PHE D 401    19633  20253  20856  -1685   -232  -1133       C
ATOM   4158  CG  PHE D 401      11.826 -78.362  -7.844  1.00171.86           C
ANISOU 4158  CG  PHE D 401    21079  21783  22436  -1644   -152  -1256       C
ATOM   4159  CD1 PHE D 401      11.179 -78.272  -6.630  1.00166.23           C
ANISOU 4159  CD1 PHE D 401    20337  21030  21792  -1604   -187  -1308       C
ATOM   4160  CD2 PHE D 401      11.755 -79.549  -8.555  1.00196.34           C
ANISOU 4160  CD2 PHE D 401    24137  24936  25528  -1646    -41  -1316       C
ATOM   4161  CE1 PHE D 401      10.454 -79.331  -6.145  1.00182.34           C
ANISOU 4161  CE1 PHE D 401    22302  23085  23893  -1567   -115  -1414       C
ATOM   4162  CE2 PHE D 401      11.026 -80.613  -8.073  1.00199.88           C
ANISOU 4162  CE2 PHE D 401    24515  25394  26037  -1611     28  -1424       C
ATOM   4163  CZ  PHE D 401      10.376 -80.503  -6.866  1.00186.56           C
ANISOU 4163  CZ  PHE D 401    22794  23670  24421  -1572    -10  -1471       C
ATOM   4164  N   ASP D 402      14.995 -79.515  -7.374  1.00139.38           N
ANISOU 4164  N   ASP D 402    16887  17699  18370  -1766    102  -1016       N
ATOM   4165  CA  ASP D 402      15.475 -80.851  -7.718  1.00126.63           C
ANISOU 4165  CA  ASP D 402    15211  16133  16769  -1782    258  -1032       C
ATOM   4166  C   ASP D 402      14.310 -81.774  -8.035  1.00147.01           C
ANISOU 4166  C   ASP D 402    17755  18740  19361  -1734    293  -1186       C
ATOM   4167  O   ASP D 402      13.492 -82.086  -7.167  1.00164.30           O
ANISOU 4167  O   ASP D 402    19899  20909  21618  -1698    286  -1273       O
ATOM   4168  CB  ASP D 402      16.287 -81.454  -6.576  1.00139.67           C
ANISOU 4168  CB  ASP D 402    16793  17769  18505  -1809    358   -979       C
ATOM   4169  CG  ASP D 402      16.701 -82.891  -6.857  1.00158.04           C
ANISOU 4169  CG  ASP D 402    19050  20144  20853  -1821    522  -1005       C
ATOM   4170  OD1 ASP D 402      17.102 -83.172  -8.011  1.00166.28           O
ANISOU 4170  OD1 ASP D 402    20119  21232  21829  -1835    568   -981       O
ATOM   4171  OD2 ASP D 402      16.615 -83.738  -5.935  1.00128.05           O
ANISOU 4171  OD2 ASP D 402    15173  16340  17140  -1814    604  -1051       O
ATOM   4172  N   THR D 403      14.267 -82.242  -9.278  1.00138.48           N
ANISOU 4172  N   THR D 403    16693  17707  18216  -1736    334  -1214       N
ATOM   4173  CA  THR D 403      13.121 -82.987  -9.784  1.00134.70           C
ANISOU 4173  CA  THR D 403    16197  17252  17732  -1694    347  -1354       C
ATOM   4174  C   THR D 403      13.076 -84.404  -9.223  1.00135.12           C
ANISOU 4174  C   THR D 403    16159  17319  17860  -1685    477  -1422       C
ATOM   4175  O   THR D 403      12.006 -84.994  -9.080  1.00134.40           O
ANISOU 4175  O   THR D 403    16034  17230  17803  -1645    474  -1540       O
ATOM   4176  CB  THR D 403      13.143 -83.046 -11.318  1.00135.74           C
ANISOU 4176  CB  THR D 403    16380  17429  17765  -1700    350  -1360       C
ATOM   4177  OG1 THR D 403      14.285 -83.794 -11.752  1.00154.08           O
ANISOU 4177  OG1 THR D 403    18683  19789  20071  -1734    477  -1293       O
ATOM   4178  CG2 THR D 403      13.208 -81.639 -11.911  1.00105.58           C
ANISOU 4178  CG2 THR D 403    12644  13600  13872  -1712    220  -1288       C
ATOM   4179  N   ARG D 404      14.245 -84.934  -8.883  1.00136.06           N
ANISOU 4179  N   ARG D 404    16238  17448  18010  -1723    588  -1340       N
ATOM   4180  CA  ARG D 404      14.371 -86.329  -8.465  1.00167.52           C
ANISOU 4180  CA  ARG D 404    20135  21451  22063  -1722    724  -1392       C
ATOM   4181  C   ARG D 404      13.582 -86.699  -7.193  1.00175.74           C
ANISOU 4181  C   ARG D 404    21103  22465  23206  -1691    718  -1472       C
ATOM   4182  O   ARG D 404      13.108 -87.830  -7.065  1.00134.94           O
ANISOU 4182  O   ARG D 404    15870  17316  18087  -1670    792  -1563       O
ATOM   4183  CB  ARG D 404      15.851 -86.708  -8.329  1.00176.18           C
ANISOU 4183  CB  ARG D 404    21207  22563  23171  -1773    841  -1272       C
ATOM   4184  CG  ARG D 404      16.134 -88.199  -8.389  1.00168.46           C
ANISOU 4184  CG  ARG D 404    20157  21619  22232  -1776    994  -1316       C
ATOM   4185  CD  ARG D 404      17.629 -88.470  -8.379  1.00178.02           C
ANISOU 4185  CD  ARG D 404    21352  22847  23441  -1826   1106  -1185       C
ATOM   4186  NE  ARG D 404      18.350 -87.566  -7.481  1.00210.27           N
ANISOU 4186  NE  ARG D 404    25442  26896  27556  -1861   1065  -1065       N
ATOM   4187  CZ  ARG D 404      18.360 -87.663  -6.151  1.00205.62           C
ANISOU 4187  CZ  ARG D 404    24790  26275  27063  -1868   1078  -1062       C
ATOM   4188  NH1 ARG D 404      19.057 -86.791  -5.428  1.00163.24           N
ANISOU 4188  NH1 ARG D 404    19438  20873  21713  -1903   1035   -946       N
ATOM   4189  NH2 ARG D 404      17.673 -88.625  -5.540  1.00203.95           N
ANISOU 4189  NH2 ARG D 404    24498  26064  26929  -1841   1132  -1172       N
ATOM   4190  N   VAL D 405      13.436 -85.757  -6.261  1.00203.75           N
ANISOU 4190  N   VAL D 405    24661  25970  26786  -1684    628  -1438       N
ATOM   4191  CA  VAL D 405      12.670 -86.018  -5.037  1.00198.05           C
ANISOU 4191  CA  VAL D 405    23871  25224  26156  -1648    614  -1509       C
ATOM   4192  C   VAL D 405      11.167 -85.938  -5.313  1.00178.39           C
ANISOU 4192  C   VAL D 405    21394  22734  23652  -1589    525  -1631       C
ATOM   4193  O   VAL D 405      10.712 -85.067  -6.058  1.00145.87           O
ANISOU 4193  O   VAL D 405    17356  18610  19459  -1576    422  -1634       O
ATOM   4194  CB  VAL D 405      13.052 -85.061  -3.881  1.00178.90           C
ANISOU 4194  CB  VAL D 405    21454  22752  23770  -1657    551  -1430       C
ATOM   4195  CG1 VAL D 405      12.227 -85.374  -2.647  1.00150.64           C
ANISOU 4195  CG1 VAL D 405    17801  19154  20282  -1613    540  -1507       C
ATOM   4196  CG2 VAL D 405      14.545 -85.161  -3.562  1.00159.70           C
ANISOU 4196  CG2 VAL D 405    19004  20317  21356  -1720    640  -1302       C
ATOM   4197  N   LEU D 406      10.408 -86.845  -4.701  1.00184.17           N
ANISOU 4197  N   LEU D 406    22044  23474  24459  -1554    564  -1724       N
ATOM   4198  CA  LEU D 406       9.001 -87.059  -5.054  1.00184.26           C
ANISOU 4198  CA  LEU D 406    22054  23495  24461  -1500    503  -1840       C
ATOM   4199  C   LEU D 406       7.970 -86.454  -4.089  1.00167.95           C
ANISOU 4199  C   LEU D 406    19975  21400  22438  -1446    400  -1883       C
ATOM   4200  O   LEU D 406       8.138 -86.489  -2.864  1.00139.33           O
ANISOU 4200  O   LEU D 406    16292  17757  18891  -1437    417  -1864       O
ATOM   4201  CB  LEU D 406       8.721 -88.557  -5.232  1.00180.87           C
ANISOU 4201  CB  LEU D 406    21546  23100  24076  -1493    608  -1922       C
ATOM   4202  CG  LEU D 406       9.409 -89.554  -4.289  1.00188.68           C
ANISOU 4202  CG  LEU D 406    22432  24097  25161  -1514    733  -1905       C
ATOM   4203  CD1 LEU D 406      10.835 -89.825  -4.738  1.00175.62           C
ANISOU 4203  CD1 LEU D 406    20791  22458  23479  -1573    837  -1815       C
ATOM   4204  CD2 LEU D 406       9.376 -89.098  -2.830  1.00202.89           C
ANISOU 4204  CD2 LEU D 406    24184  25868  27039  -1498    700  -1878       C
ATOM   4205  N   SER D 407       6.894 -85.914  -4.657  1.00156.66           N
ANISOU 4205  N   SER D 407    18598  19967  20957  -1407    295  -1939       N
ATOM   4206  CA  SER D 407       5.806 -85.352  -3.859  1.00152.03           C
ANISOU 4206  CA  SER D 407    18004  19357  20402  -1347    195  -1983       C
ATOM   4207  C   SER D 407       4.480 -85.340  -4.620  1.00166.90           C
ANISOU 4207  C   SER D 407    19917  21255  22244  -1305    121  -2070       C
ATOM   4208  O   SER D 407       4.459 -85.435  -5.852  1.00136.22           O
ANISOU 4208  O   SER D 407    16082  17389  18287  -1326    122  -2083       O
ATOM   4209  CB  SER D 407       6.154 -83.934  -3.398  1.00136.90           C
ANISOU 4209  CB  SER D 407    16158  17398  18461  -1349     99  -1905       C
ATOM   4210  OG  SER D 407       6.221 -83.032  -4.491  1.00132.74           O
ANISOU 4210  OG  SER D 407    15732  16865  17836  -1368     23  -1872       O
ATOM   4211  N   ASN D 408       3.378 -85.231  -3.877  1.00190.50           N
ANISOU 4211  N   ASN D 408    22871  24234  25275  -1243     57  -2124       N
ATOM   4212  CA  ASN D 408       2.053 -85.105  -4.477  1.00190.21           C
ANISOU 4212  CA  ASN D 408    22861  24207  25201  -1199    -25  -2196       C
ATOM   4213  C   ASN D 408       2.027 -83.896  -5.389  1.00169.30           C
ANISOU 4213  C   ASN D 408    20326  21543  22455  -1213   -121  -2161       C
ATOM   4214  O   ASN D 408       1.200 -83.798  -6.301  1.00171.88           O
ANISOU 4214  O   ASN D 408    20694  21883  22728  -1200   -174  -2207       O
ATOM   4215  CB  ASN D 408       0.972 -84.936  -3.405  1.00199.02           C
ANISOU 4215  CB  ASN D 408    23930  25313  26376  -1127    -89  -2237       C
ATOM   4216  CG  ASN D 408       1.475 -85.247  -2.005  1.00207.90           C
ANISOU 4216  CG  ASN D 408    24973  26429  27592  -1117    -33  -2212       C
ATOM   4217  OD1 ASN D 408       2.050 -84.389  -1.330  1.00198.56           O
ANISOU 4217  OD1 ASN D 408    23819  25212  26411  -1120    -65  -2150       O
ATOM   4218  ND2 ASN D 408       1.247 -86.475  -1.556  1.00217.07           N
ANISOU 4218  ND2 ASN D 408    26028  27618  28829  -1105     47  -2261       N
ATOM   4219  N   LEU D 409       2.933 -82.963  -5.113  1.00141.38           N
ANISOU 4219  N   LEU D 409    16839  17977  18900  -1240   -147  -2076       N
ATOM   4220  CA  LEU D 409       3.061 -81.747  -5.898  1.00131.90           C
ANISOU 4220  CA  LEU D 409    15744  16760  17613  -1258   -241  -2028       C
ATOM   4221  C   LEU D 409       3.932 -82.006  -7.111  1.00125.60           C
ANISOU 4221  C   LEU D 409    14982  15989  16752  -1320   -182  -1992       C
ATOM   4222  O   LEU D 409       3.912 -81.235  -8.069  1.00111.81           O
ANISOU 4222  O   LEU D 409    13313  14243  14926  -1337   -249  -1967       O
ATOM   4223  CB  LEU D 409       3.680 -80.627  -5.052  1.00123.22           C
ANISOU 4223  CB  LEU D 409    14681  15615  16521  -1260   -301  -1946       C
ATOM   4224  CG  LEU D 409       3.039 -80.261  -3.712  1.00142.65           C
ANISOU 4224  CG  LEU D 409    17112  18045  19043  -1198   -356  -1966       C
ATOM   4225  CD1 LEU D 409       1.514 -80.341  -3.779  1.00185.72           C
ANISOU 4225  CD1 LEU D 409    22556  23512  24498  -1131   -419  -2055       C
ATOM   4226  CD2 LEU D 409       3.577 -81.151  -2.600  1.00166.70           C
ANISOU 4226  CD2 LEU D 409    20063  21094  22180  -1201   -254  -1962       C
ATOM   4227  N   ASN D 410       4.688 -83.102  -7.057  1.00145.56           N
ANISOU 4227  N   ASN D 410    17450  18540  19317  -1351    -56  -1987       N
ATOM   4228  CA  ASN D 410       5.712 -83.413  -8.055  1.00140.15           C
ANISOU 4228  CA  ASN D 410    16791  17880  18578  -1408     17  -1939       C
ATOM   4229  C   ASN D 410       5.210 -84.383  -9.117  1.00121.74           C
ANISOU 4229  C   ASN D 410    14452  15590  16215  -1408     66  -2016       C
ATOM   4230  O   ASN D 410       4.847 -85.517  -8.797  1.00145.36           O
ANISOU 4230  O   ASN D 410    17370  18596  19264  -1391    137  -2083       O
ATOM   4231  CB  ASN D 410       6.938 -84.008  -7.357  1.00162.45           C
ANISOU 4231  CB  ASN D 410    19559  20706  21460  -1444    131  -1877       C
ATOM   4232  CG  ASN D 410       8.246 -83.542  -7.968  1.00179.88           C
ANISOU 4232  CG  ASN D 410    21819  22917  23608  -1502    156  -1767       C
ATOM   4233  OD1 ASN D 410       8.259 -82.709  -8.878  1.00164.25           O
ANISOU 4233  OD1 ASN D 410    19919  20941  21549  -1514     82  -1735       O
ATOM   4234  ND2 ASN D 410       9.358 -84.066  -7.458  1.00192.49           N
ANISOU 4234  ND2 ASN D 410    23370  24518  25249  -1538    260  -1704       N
ATOM   4235  N   LEU D 411       5.201 -83.949 -10.378  1.00124.71           N
ANISOU 4235  N   LEU D 411    14902  15982  16500  -1427     26  -2006       N
ATOM   4236  CA  LEU D 411       4.680 -84.780 -11.466  1.00142.90           C
ANISOU 4236  CA  LEU D 411    17211  18321  18762  -1426     60  -2080       C
ATOM   4237  C   LEU D 411       5.728 -85.013 -12.545  1.00165.72           C
ANISOU 4237  C   LEU D 411    20139  21243  21585  -1473    129  -2030       C
ATOM   4238  O   LEU D 411       6.399 -84.075 -12.966  1.00192.35           O
ANISOU 4238  O   LEU D 411    23570  24613  24899  -1500     88  -1946       O
ATOM   4239  CB  LEU D 411       3.494 -84.077 -12.127  1.00102.41           C
ANISOU 4239  CB  LEU D 411    12141  13190  13580  -1400    -60  -2128       C
ATOM   4240  CG  LEU D 411       2.315 -83.630 -11.263  1.00121.15           C
ANISOU 4240  CG  LEU D 411    14496  15536  16000  -1347   -151  -2172       C
ATOM   4241  CD1 LEU D 411       1.253 -82.909 -12.108  1.00101.43           C
ANISOU 4241  CD1 LEU D 411    12063  13040  13435  -1330   -262  -2207       C
ATOM   4242  CD2 LEU D 411       1.728 -84.829 -10.536  1.00115.58           C
ANISOU 4242  CD2 LEU D 411    13700  14838  15379  -1315    -89  -2247       C
ATOM   4243  N   PRO D 412       5.829 -86.251 -13.053  1.00156.16           N
ANISOU 4243  N   PRO D 412    18898  20062  20375  -1479    229  -2080       N
ATOM   4244  CA  PRO D 412       6.784 -86.448 -14.145  1.00176.60           C
ANISOU 4244  CA  PRO D 412    21527  22683  22888  -1516    293  -2033       C
ATOM   4245  C   PRO D 412       6.450 -85.574 -15.351  1.00163.40           C
ANISOU 4245  C   PRO D 412    19943  21027  21116  -1522    201  -2024       C
ATOM   4246  O   PRO D 412       5.345 -85.035 -15.439  1.00120.56           O
ANISOU 4246  O   PRO D 412    14541  15587  15679  -1498     99  -2074       O
ATOM   4247  CB  PRO D 412       6.655 -87.946 -14.478  1.00165.43           C
ANISOU 4247  CB  PRO D 412    20069  21294  21493  -1510    399  -2111       C
ATOM   4248  CG  PRO D 412       5.485 -88.438 -13.705  1.00135.72           C
ANISOU 4248  CG  PRO D 412    16248  17512  17807  -1471    370  -2203       C
ATOM   4249  CD  PRO D 412       5.327 -87.532 -12.533  1.00132.12           C
ANISOU 4249  CD  PRO D 412    15772  17021  17405  -1456    300  -2164       C
ATOM   4250  N   GLY D 413       7.425 -85.407 -16.240  1.00158.07           N
ANISOU 4250  N   GLY D 413    19311  20381  20369  -1555    238  -1954       N
ATOM   4251  CA  GLY D 413       7.277 -84.549 -17.399  1.00164.56           C
ANISOU 4251  CA  GLY D 413    20210  21222  21094  -1566    157  -1931       C
ATOM   4252  C   GLY D 413       8.480 -84.652 -18.319  1.00180.98           C
ANISOU 4252  C   GLY D 413    22319  23342  23102  -1598    227  -1852       C
ATOM   4253  O   GLY D 413       9.284 -85.585 -18.200  1.00161.64           O
ANISOU 4253  O   GLY D 413    19834  20909  20673  -1607    347  -1835       O
ATOM   4254  N   CYS D 414       8.604 -83.689 -19.232  1.00201.56           N
ANISOU 4254  N   CYS D 414    24990  25968  25626  -1613    151  -1799       N
ATOM   4255  CA  CYS D 414       9.676 -83.677 -20.227  1.00200.36           C
ANISOU 4255  CA  CYS D 414    24871  25862  25395  -1639    203  -1718       C
ATOM   4256  C   CYS D 414      10.851 -82.795 -19.809  1.00200.23           C
ANISOU 4256  C   CYS D 414    24859  25840  25379  -1669    189  -1574       C
ATOM   4257  O   CYS D 414      10.655 -81.697 -19.285  1.00228.99           O
ANISOU 4257  O   CYS D 414    28518  29449  29040  -1673     84  -1533       O
ATOM   4258  CB  CYS D 414       9.135 -83.176 -21.568  1.00203.84           C
ANISOU 4258  CB  CYS D 414    25375  26336  25740  -1640    128  -1742       C
ATOM   4259  SG  CYS D 414       8.484 -81.482 -21.529  1.00176.26           S
ANISOU 4259  SG  CYS D 414    21927  22817  22229  -1645    -48  -1706       S
ATOM   4260  N   ASP D 415      12.072 -83.282 -20.017  1.00169.38           N
ANISOU 4260  N   ASP D 415    20939  21963  21453  -1688    295  -1495       N
ATOM   4261  CA  ASP D 415      12.313 -84.651 -20.463  1.00170.92           C
ANISOU 4261  CA  ASP D 415    21112  22191  21639  -1678    426  -1547       C
ATOM   4262  C   ASP D 415      12.750 -85.515 -19.276  1.00171.89           C
ANISOU 4262  C   ASP D 415    21164  22289  21858  -1678    529  -1549       C
ATOM   4263  O   ASP D 415      12.029 -86.427 -18.857  1.00172.02           O
ANISOU 4263  O   ASP D 415    21141  22290  21931  -1656    568  -1657       O
ATOM   4264  CB  ASP D 415      13.353 -84.683 -21.589  1.00191.84           C
ANISOU 4264  CB  ASP D 415    23796  24899  24196  -1692    482  -1460       C
ATOM   4265  CG  ASP D 415      14.378 -83.566 -21.475  1.00199.64           C
ANISOU 4265  CG  ASP D 415    24800  25892  25163  -1723    437  -1303       C
ATOM   4266  OD1 ASP D 415      14.563 -83.041 -20.358  1.00218.46           O
ANISOU 4266  OD1 ASP D 415    27159  28230  27615  -1737    401  -1253       O
ATOM   4267  OD2 ASP D 415      14.999 -83.215 -22.506  1.00171.94           O
ANISOU 4267  OD2 ASP D 415    21329  22432  21568  -1733    435  -1226       O
ATOM   4268  N   GLY D 416      13.932 -85.226 -18.736  1.00159.14           N
ANISOU 4268  N   GLY D 416    19531  20672  20264  -1706    570  -1424       N
ATOM   4269  CA  GLY D 416      14.338 -85.782 -17.457  1.00156.14           C
ANISOU 4269  CA  GLY D 416    19084  20262  19982  -1713    646  -1410       C
ATOM   4270  C   GLY D 416      13.741 -84.933 -16.343  1.00154.99           C
ANISOU 4270  C   GLY D 416    18925  20060  19903  -1710    540  -1417       C
ATOM   4271  O   GLY D 416      13.847 -85.259 -15.153  1.00111.54           O
ANISOU 4271  O   GLY D 416    13365  14525  14490  -1711    579  -1418       O
ATOM   4272  N   GLY D 417      13.096 -83.839 -16.748  1.00162.47           N
ANISOU 4272  N   GLY D 417    19928  20997  20805  -1704    406  -1421       N
ATOM   4273  CA  GLY D 417      12.515 -82.886 -15.822  1.00158.67           C
ANISOU 4273  CA  GLY D 417    19450  20465  20372  -1696    292  -1422       C
ATOM   4274  C   GLY D 417      11.226 -83.351 -15.178  1.00169.35           C
ANISOU 4274  C   GLY D 417    20766  21789  21789  -1657    270  -1554       C
ATOM   4275  O   GLY D 417      10.673 -84.388 -15.540  1.00164.83           O
ANISOU 4275  O   GLY D 417    20170  21237  21220  -1637    331  -1652       O
ATOM   4276  N   SER D 418      10.749 -82.563 -14.218  1.00194.14           N
ANISOU 4276  N   SER D 418    23904  24882  24977  -1644    178  -1553       N
ATOM   4277  CA  SER D 418       9.564 -82.891 -13.432  1.00201.52           C
ANISOU 4277  CA  SER D 418    24799  25789  25979  -1602    150  -1661       C
ATOM   4278  C   SER D 418       8.619 -81.689 -13.332  1.00206.69           C
ANISOU 4278  C   SER D 418    25501  26413  26617  -1578     -1  -1680       C
ATOM   4279  O   SER D 418       9.065 -80.548 -13.219  1.00177.30           O
ANISOU 4279  O   SER D 418    21824  22670  22871  -1596    -81  -1592       O
ATOM   4280  CB  SER D 418       9.985 -83.346 -12.030  1.00208.47           C
ANISOU 4280  CB  SER D 418    25608  26642  26959  -1602    215  -1643       C
ATOM   4281  OG  SER D 418       8.871 -83.533 -11.174  1.00234.67           O
ANISOU 4281  OG  SER D 418    28885  29935  30344  -1559    177  -1735       O
ATOM   4282  N   LEU D 419       7.312 -81.943 -13.370  1.00227.05           N
ANISOU 4282  N   LEU D 419    28072  28988  29208  -1539    -43  -1789       N
ATOM   4283  CA  LEU D 419       6.342 -80.862 -13.219  1.00193.56           C
ANISOU 4283  CA  LEU D 419    23872  24718  24955  -1510   -181  -1810       C
ATOM   4284  C   LEU D 419       5.893 -80.692 -11.757  1.00187.17           C
ANISOU 4284  C   LEU D 419    23020  23864  24231  -1474   -213  -1829       C
ATOM   4285  O   LEU D 419       5.153 -81.520 -11.217  1.00154.36           O
ANISOU 4285  O   LEU D 419    18807  19710  20134  -1440   -177  -1912       O
ATOM   4286  CB  LEU D 419       5.121 -81.105 -14.101  1.00132.64           C
ANISOU 4286  CB  LEU D 419    16176  17023  17198  -1486   -222  -1908       C
ATOM   4287  CG  LEU D 419       4.222 -79.871 -14.077  1.00119.31           C
ANISOU 4287  CG  LEU D 419    14538  15309  15487  -1462   -366  -1914       C
ATOM   4288  CD1 LEU D 419       4.824 -78.801 -14.944  1.00130.29           C
ANISOU 4288  CD1 LEU D 419    16000  16707  16797  -1498   -431  -1829       C
ATOM   4289  CD2 LEU D 419       2.823 -80.178 -14.530  1.00102.43           C
ANISOU 4289  CD2 LEU D 419    12402  13181  13337  -1429   -407  -2016       C
ATOM   4290  N   TYR D 420       6.322 -79.595 -11.139  1.00173.04           N
ANISOU 4290  N   TYR D 420    21262  22038  22447  -1481   -286  -1751       N
ATOM   4291  CA  TYR D 420       6.001 -79.298  -9.748  1.00139.78           C
ANISOU 4291  CA  TYR D 420    17021  17782  18309  -1446   -323  -1758       C
ATOM   4292  C   TYR D 420       4.750 -78.429  -9.736  1.00147.20           C
ANISOU 4292  C   TYR D 420    18002  18699  19229  -1399   -453  -1807       C
ATOM   4293  O   TYR D 420       4.716 -77.368 -10.371  1.00126.91           O
ANISOU 4293  O   TYR D 420    15505  16121  16596  -1411   -549  -1767       O
ATOM   4294  CB  TYR D 420       7.190 -78.576  -9.095  1.00150.96           C
ANISOU 4294  CB  TYR D 420    18455  19166  19738  -1479   -333  -1641       C
ATOM   4295  CG  TYR D 420       7.084 -78.240  -7.610  1.00150.90           C
ANISOU 4295  CG  TYR D 420    18420  19109  19804  -1450   -365  -1633       C
ATOM   4296  CD1 TYR D 420       7.463 -79.162  -6.632  1.00153.29           C
ANISOU 4296  CD1 TYR D 420    18643  19413  20189  -1449   -263  -1641       C
ATOM   4297  CD2 TYR D 420       6.657 -76.980  -7.187  1.00105.18           C
ANISOU 4297  CD2 TYR D 420    12688  13274  14002  -1423   -498  -1612       C
ATOM   4298  CE1 TYR D 420       7.394 -78.850  -5.269  1.00116.60           C
ANISOU 4298  CE1 TYR D 420    13971  14723  15607  -1421   -292  -1631       C
ATOM   4299  CE2 TYR D 420       6.577 -76.661  -5.827  1.00104.82           C
ANISOU 4299  CE2 TYR D 420    12623  13184  14019  -1392   -528  -1605       C
ATOM   4300  CZ  TYR D 420       6.947 -77.602  -4.877  1.00130.70           C
ANISOU 4300  CZ  TYR D 420    15820  16465  17376  -1391   -424  -1614       C
ATOM   4301  OH  TYR D 420       6.868 -77.300  -3.534  1.00143.10           O
ANISOU 4301  OH  TYR D 420    17369  17994  19007  -1359   -453  -1607       O
ATOM   4302  N   VAL D 421       3.715 -78.898  -9.040  1.00159.12           N
ANISOU 4302  N   VAL D 421    19463  20202  20793  -1346   -456  -1891       N
ATOM   4303  CA  VAL D 421       2.474 -78.145  -8.899  1.00148.72           C
ANISOU 4303  CA  VAL D 421    18177  18864  19465  -1294   -573  -1938       C
ATOM   4304  C   VAL D 421       2.336 -77.673  -7.465  1.00169.02           C
ANISOU 4304  C   VAL D 421    20730  21392  22099  -1251   -615  -1925       C
ATOM   4305  O   VAL D 421       2.126 -78.480  -6.558  1.00192.52           O
ANISOU 4305  O   VAL D 421    23630  24370  25148  -1222   -553  -1965       O
ATOM   4306  CB  VAL D 421       1.234 -79.004  -9.220  1.00154.32           C
ANISOU 4306  CB  VAL D 421    18847  19602  20185  -1256   -557  -2043       C
ATOM   4307  CG1 VAL D 421       0.029 -78.107  -9.531  1.00134.24           C
ANISOU 4307  CG1 VAL D 421    16356  17046  17601  -1216   -682  -2075       C
ATOM   4308  CG2 VAL D 421       1.507 -79.946 -10.380  1.00163.33           C
ANISOU 4308  CG2 VAL D 421    19980  20788  21288  -1297   -473  -2068       C
ATOM   4309  N   ASN D 422       2.464 -76.366  -7.265  1.00168.69           N
ANISOU 4309  N   ASN D 422    20756  21309  22028  -1247   -721  -1868       N
ATOM   4310  CA  ASN D 422       2.313 -75.760  -5.945  1.00157.35           C
ANISOU 4310  CA  ASN D 422    19319  19827  20641  -1203   -777  -1853       C
ATOM   4311  C   ASN D 422       1.222 -74.713  -6.050  1.00159.33           C
ANISOU 4311  C   ASN D 422    19630  20054  20854  -1152   -910  -1880       C
ATOM   4312  O   ASN D 422       0.211 -74.753  -5.348  1.00167.13           O
ANISOU 4312  O   ASN D 422    20594  21034  21876  -1085   -942  -1937       O
ATOM   4313  CB  ASN D 422       3.624 -75.136  -5.485  1.00124.24           C
ANISOU 4313  CB  ASN D 422    15157  15599  16451  -1247   -782  -1749       C
ATOM   4314  CG  ASN D 422       3.484 -74.413  -4.185  1.00156.03           C
ANISOU 4314  CG  ASN D 422    19194  19571  20518  -1202   -851  -1731       C
ATOM   4315  OD1 ASN D 422       2.723 -73.445  -4.080  1.00158.07           O
ANISOU 4315  OD1 ASN D 422    19509  19800  20750  -1157   -967  -1745       O
ATOM   4316  ND2 ASN D 422       4.218 -74.871  -3.173  1.00168.33           N
ANISOU 4316  ND2 ASN D 422    20702  21117  22141  -1212   -780  -1700       N
ATOM   4317  N   LYS D 423       1.482 -73.734  -6.898  1.00132.57           N
ANISOU 4317  N   LYS D 423    16321  16655  17394  -1185   -988  -1829       N
ATOM   4318  CA  LYS D 423       0.433 -72.960  -7.517  1.00132.71           C
ANISOU 4318  CA  LYS D 423    16393  16670  17360  -1155  -1095  -1861       C
ATOM   4319  C   LYS D 423       0.950 -72.699  -8.920  1.00160.33           C
ANISOU 4319  C   LYS D 423    19937  20195  20784  -1220  -1102  -1821       C
ATOM   4320  O   LYS D 423       2.127 -72.408  -9.105  1.00130.91           O
ANISOU 4320  O   LYS D 423    16235  16464  17043  -1273  -1089  -1739       O
ATOM   4321  CB  LYS D 423       0.190 -71.660  -6.760  1.00161.85           C
ANISOU 4321  CB  LYS D 423    20144  20303  21049  -1114  -1217  -1829       C
ATOM   4322  CG  LYS D 423      -1.280 -71.332  -6.546  1.00163.36           C
ANISOU 4322  CG  LYS D 423    20344  20488  21237  -1038  -1293  -1898       C
ATOM   4323  CD  LYS D 423      -1.546 -70.897  -5.102  1.00166.29           C
ANISOU 4323  CD  LYS D 423    20713  20812  21658   -970  -1338  -1899       C
ATOM   4324  CE  LYS D 423      -0.651 -69.725  -4.695  1.00164.92           C
ANISOU 4324  CE  LYS D 423    20612  20582  21470   -991  -1417  -1813       C
ATOM   4325  NZ  LYS D 423      -0.544 -69.549  -3.211  1.00143.63           N
ANISOU 4325  NZ  LYS D 423    17902  17841  18829   -940  -1428  -1805       N
ATOM   4326  N   HIS D 424       0.086 -72.859  -9.913  1.00214.44           N
ANISOU 4326  N   HIS D 424    26801  27082  27595  -1215  -1119  -1876       N
ATOM   4327  CA  HIS D 424       0.435 -72.554 -11.299  1.00210.59           C
ANISOU 4327  CA  HIS D 424    26358  26625  27032  -1271  -1136  -1844       C
ATOM   4328  C   HIS D 424       1.422 -73.570 -11.897  1.00171.91           C
ANISOU 4328  C   HIS D 424    21424  21768  22127  -1326  -1013  -1825       C
ATOM   4329  O   HIS D 424       1.624 -73.606 -13.114  1.00148.20           O
ANISOU 4329  O   HIS D 424    18444  18802  19061  -1366  -1005  -1814       O
ATOM   4330  CB  HIS D 424       0.959 -71.117 -11.390  1.00216.73           C
ANISOU 4330  CB  HIS D 424    27210  27367  27771  -1292  -1247  -1757       C
ATOM   4331  CG  HIS D 424       0.197 -70.145 -10.535  1.00201.13           C
ANISOU 4331  CG  HIS D 424    25269  25339  25813  -1233  -1358  -1766       C
ATOM   4332  ND1 HIS D 424       0.514 -68.806 -10.463  1.00201.22           N
ANISOU 4332  ND1 HIS D 424    25349  25308  25796  -1241  -1472  -1697       N
ATOM   4333  CD2 HIS D 424      -0.864 -70.323  -9.711  1.00168.98           C
ANISOU 4333  CD2 HIS D 424    21171  21251  21781  -1163  -1374  -1835       C
ATOM   4334  CE1 HIS D 424      -0.322 -68.200  -9.637  1.00175.96           C
ANISOU 4334  CE1 HIS D 424    22171  22067  22618  -1177  -1552  -1726       C
ATOM   4335  NE2 HIS D 424      -1.168 -69.099  -9.167  1.00148.34           N
ANISOU 4335  NE2 HIS D 424    18615  18586  19160  -1127  -1492  -1808       N
ATOM   4336  N   ALA D 425       2.017 -74.393 -11.030  1.00148.95           N
ANISOU 4336  N   ALA D 425    18456  18856  19282  -1325   -918  -1822       N
ATOM   4337  CA  ALA D 425       2.698 -75.619 -11.449  1.00168.46           C
ANISOU 4337  CA  ALA D 425    20878  21368  21760  -1361   -785  -1828       C
ATOM   4338  C   ALA D 425       3.841 -75.464 -12.453  1.00182.01           C
ANISOU 4338  C   ALA D 425    22628  23112  23415  -1425   -756  -1749       C
ATOM   4339  O   ALA D 425       3.819 -76.080 -13.520  1.00230.76           O
ANISOU 4339  O   ALA D 425    28801  29332  29547  -1447   -705  -1777       O
ATOM   4340  CB  ALA D 425       1.676 -76.617 -11.984  1.00204.72           C
ANISOU 4340  CB  ALA D 425    25436  25997  26352  -1338   -742  -1931       C
ATOM   4341  N   PHE D 426       4.840 -74.659 -12.113  1.00160.98           N
ANISOU 4341  N   PHE D 426    19994  20421  20748  -1454   -790  -1647       N
ATOM   4342  CA  PHE D 426       5.967 -74.414 -13.013  1.00184.35           C
ANISOU 4342  CA  PHE D 426    22984  23409  23651  -1512   -772  -1555       C
ATOM   4343  C   PHE D 426       6.818 -75.669 -13.273  1.00181.86           C
ANISOU 4343  C   PHE D 426    22618  23134  23346  -1542   -622  -1546       C
ATOM   4344  O   PHE D 426       7.001 -76.506 -12.381  1.00171.31           O
ANISOU 4344  O   PHE D 426    21223  21790  22078  -1531   -536  -1569       O
ATOM   4345  CB  PHE D 426       6.827 -73.294 -12.436  1.00204.20           C
ANISOU 4345  CB  PHE D 426    25537  25879  26169  -1534   -846  -1441       C
ATOM   4346  CG  PHE D 426       6.031 -72.253 -11.702  1.00201.24           C
ANISOU 4346  CG  PHE D 426    25200  25450  25813  -1492   -973  -1459       C
ATOM   4347  CD1 PHE D 426       5.345 -71.263 -12.395  1.00206.80           C
ANISOU 4347  CD1 PHE D 426    25963  26150  26462  -1483  -1092  -1466       C
ATOM   4348  CD2 PHE D 426       5.938 -72.282 -10.321  1.00171.44           C
ANISOU 4348  CD2 PHE D 426    21401  21629  22109  -1458   -973  -1470       C
ATOM   4349  CE1 PHE D 426       4.596 -70.310 -11.718  1.00181.15           C
ANISOU 4349  CE1 PHE D 426    22751  22850  23228  -1440  -1208  -1482       C
ATOM   4350  CE2 PHE D 426       5.191 -71.334  -9.644  1.00157.57           C
ANISOU 4350  CE2 PHE D 426    19683  19823  20365  -1412  -1089  -1488       C
ATOM   4351  CZ  PHE D 426       4.518 -70.349 -10.341  1.00137.29           C
ANISOU 4351  CZ  PHE D 426    17175  17248  17740  -1402  -1206  -1494       C
ATOM   4352  N   HIS D 427       7.339 -75.796 -14.493  1.00157.56           N
ANISOU 4352  N   HIS D 427    19562  20104  20200  -1578   -592  -1511       N
ATOM   4353  CA  HIS D 427       8.153 -76.954 -14.837  1.00162.96           C
ANISOU 4353  CA  HIS D 427    20205  20829  20884  -1603   -452  -1501       C
ATOM   4354  C   HIS D 427       9.651 -76.632 -14.768  1.00164.88           C
ANISOU 4354  C   HIS D 427    20455  21075  21116  -1649   -420  -1363       C
ATOM   4355  O   HIS D 427      10.089 -75.527 -15.107  1.00142.22           O
ANISOU 4355  O   HIS D 427    17637  18198  18204  -1673   -509  -1273       O
ATOM   4356  CB  HIS D 427       7.773 -77.519 -16.216  1.00177.59           C
ANISOU 4356  CB  HIS D 427    22071  22736  22668  -1607   -418  -1558       C
ATOM   4357  CG  HIS D 427       8.536 -78.752 -16.590  1.00189.72           C
ANISOU 4357  CG  HIS D 427    23570  24315  24202  -1625   -274  -1556       C
ATOM   4358  ND1 HIS D 427       8.754 -79.791 -15.707  1.00182.92           N
ANISOU 4358  ND1 HIS D 427    22644  23444  23415  -1616   -169  -1587       N
ATOM   4359  CD2 HIS D 427       9.131 -79.117 -17.749  1.00166.10           C
ANISOU 4359  CD2 HIS D 427    20595  21375  21140  -1649   -216  -1528       C
ATOM   4360  CE1 HIS D 427       9.456 -80.736 -16.304  1.00142.05           C
ANISOU 4360  CE1 HIS D 427    17448  18309  18215  -1634    -53  -1577       C
ATOM   4361  NE2 HIS D 427       9.702 -80.350 -17.545  1.00123.22           N
ANISOU 4361  NE2 HIS D 427    15114  15962  15741  -1653    -78  -1541       N
ATOM   4362  N   THR D 428      10.438 -77.609 -14.335  1.00169.65           N
ANISOU 4362  N   THR D 428    21008  21691  21762  -1663   -293  -1343       N
ATOM   4363  CA  THR D 428      11.880 -77.436 -14.258  1.00175.04           C
ANISOU 4363  CA  THR D 428    21690  22379  22437  -1708   -249  -1208       C
ATOM   4364  C   THR D 428      12.614 -78.452 -15.135  1.00181.92           C
ANISOU 4364  C   THR D 428    22540  23310  23270  -1729   -119  -1191       C
ATOM   4365  O   THR D 428      12.182 -79.599 -15.260  1.00201.62           O
ANISOU 4365  O   THR D 428    24996  25826  25783  -1709    -28  -1287       O
ATOM   4366  CB  THR D 428      12.386 -77.590 -12.802  1.00180.04           C
ANISOU 4366  CB  THR D 428    22280  22967  23159  -1712   -211  -1170       C
ATOM   4367  OG1 THR D 428      12.677 -78.970 -12.528  1.00130.32           O
ANISOU 4367  OG1 THR D 428    15915  16694  16907  -1712    -62  -1210       O
ATOM   4368  CG2 THR D 428      11.346 -77.067 -11.810  1.00188.30           C
ANISOU 4368  CG2 THR D 428    23329  23960  24258  -1671   -305  -1239       C
ATOM   4369  N   PRO D 429      13.721 -78.021 -15.759  1.00169.14           N
ANISOU 4369  N   PRO D 429    20949  21720  21598  -1767   -114  -1065       N
ATOM   4370  CA  PRO D 429      14.701 -78.873 -16.448  1.00129.74           C
ANISOU 4370  CA  PRO D 429    15940  16784  16572  -1788     13  -1013       C
ATOM   4371  C   PRO D 429      15.394 -79.787 -15.443  1.00123.61           C
ANISOU 4371  C   PRO D 429    15100  15995  15872  -1798    137   -992       C
ATOM   4372  O   PRO D 429      15.260 -79.562 -14.243  1.00141.25           O
ANISOU 4372  O   PRO D 429    17312  18177  18180  -1796    110   -994       O
ATOM   4373  CB  PRO D 429      15.703 -77.868 -16.990  1.00135.89           C
ANISOU 4373  CB  PRO D 429    16761  17580  17291  -1825    -45   -860       C
ATOM   4374  CG  PRO D 429      14.910 -76.612 -17.165  1.00170.36           C
ANISOU 4374  CG  PRO D 429    21178  21919  21631  -1817   -207   -874       C
ATOM   4375  CD  PRO D 429      13.962 -76.590 -16.011  1.00170.93           C
ANISOU 4375  CD  PRO D 429    21233  21930  21781  -1787   -248   -969       C
ATOM   4376  N   ALA D 430      16.077 -80.829 -15.904  1.00118.40           N
ANISOU 4376  N   ALA D 430    14412  15380  15196  -1807    272   -978       N
ATOM   4377  CA  ALA D 430      16.791 -81.708 -14.975  1.00143.55           C
ANISOU 4377  CA  ALA D 430    17533  18555  18454  -1820    395   -951       C
ATOM   4378  C   ALA D 430      18.069 -81.017 -14.506  1.00164.91           C
ANISOU 4378  C   ALA D 430    20244  21247  21168  -1865    388   -780       C
ATOM   4379  O   ALA D 430      18.672 -80.242 -15.253  1.00142.76           O
ANISOU 4379  O   ALA D 430    17485  18465  18293  -1886    335   -674       O
ATOM   4380  CB  ALA D 430      17.109 -83.037 -15.627  1.00131.77           C
ANISOU 4380  CB  ALA D 430    16011  17114  16942  -1814    541   -989       C
ATOM   4381  N   PHE D 431      18.479 -81.267 -13.267  1.00207.60           N
ANISOU 4381  N   PHE D 431    25602  26616  26658  -1880    434   -749       N
ATOM   4382  CA  PHE D 431      19.680 -80.612 -12.762  1.00223.81           C
ANISOU 4382  CA  PHE D 431    27662  28651  28722  -1926    423   -583       C
ATOM   4383  C   PHE D 431      20.847 -80.965 -13.683  1.00221.94           C
ANISOU 4383  C   PHE D 431    27429  28475  28422  -1952    515   -470       C
ATOM   4384  O   PHE D 431      20.923 -82.085 -14.194  1.00194.87           O
ANISOU 4384  O   PHE D 431    23971  25090  24980  -1938    637   -522       O
ATOM   4385  CB  PHE D 431      19.945 -80.978 -11.292  1.00217.69           C
ANISOU 4385  CB  PHE D 431    26830  27832  28052  -1939    476   -573       C
ATOM   4386  CG  PHE D 431      21.327 -81.518 -11.027  1.00214.54           C
ANISOU 4386  CG  PHE D 431    26392  27451  27672  -1983    600   -445       C
ATOM   4387  CD1 PHE D 431      22.398 -80.664 -10.780  1.00170.21           C
ANISOU 4387  CD1 PHE D 431    20803  21821  22049  -2029    558   -274       C
ATOM   4388  CD2 PHE D 431      21.551 -82.887 -11.007  1.00226.46           C
ANISOU 4388  CD2 PHE D 431    27838  28993  29212  -1979    757   -491       C
ATOM   4389  CE1 PHE D 431      23.669 -81.172 -10.530  1.00149.27           C
ANISOU 4389  CE1 PHE D 431    18113  19187  19415  -2071    674   -148       C
ATOM   4390  CE2 PHE D 431      22.819 -83.400 -10.757  1.00210.35           C
ANISOU 4390  CE2 PHE D 431    25760  26971  27191  -2018    876   -370       C
ATOM   4391  CZ  PHE D 431      23.877 -82.541 -10.518  1.00178.02           C
ANISOU 4391  CZ  PHE D 431    21690  22862  23086  -2065    836   -196       C
ATOM   4392  N   ASP D 432      21.708 -79.984 -13.946  1.00231.29           N
ANISOU 4392  N   ASP D 432    28653  29663  29563  -1986    449   -315       N
ATOM   4393  CA  ASP D 432      22.873 -80.187 -14.800  1.00209.42           C
ANISOU 4393  CA  ASP D 432    25888  26952  26729  -2009    525   -186       C
ATOM   4394  C   ASP D 432      24.121 -79.553 -14.183  1.00202.08           C
ANISOU 4394  C   ASP D 432    24958  26003  25821  -2061    512      4       C
ATOM   4395  O   ASP D 432      24.190 -78.328 -14.033  1.00199.38           O
ANISOU 4395  O   ASP D 432    24659  25628  25467  -2080    374     82       O
ATOM   4396  CB  ASP D 432      22.612 -79.607 -16.191  1.00193.55           C
ANISOU 4396  CB  ASP D 432    23935  24990  24617  -1994    449   -182       C
ATOM   4397  CG  ASP D 432      23.569 -80.150 -17.238  1.00191.73           C
ANISOU 4397  CG  ASP D 432    23701  24835  24313  -1998    553    -94       C
ATOM   4398  OD1 ASP D 432      24.080 -81.277 -17.048  1.00194.44           O
ANISOU 4398  OD1 ASP D 432    23999  25199  24682  -1997    702    -96       O
ATOM   4399  OD2 ASP D 432      23.804 -79.453 -18.253  1.00170.10           O
ANISOU 4399  OD2 ASP D 432    21004  22136  21490  -2000    486    -21       O
ATOM   4400  N   LYS D 433      25.115 -80.377 -13.853  1.00188.53           N
ANISOU 4400  N   LYS D 433    23194  24306  24134  -2085    651     83       N
ATOM   4401  CA  LYS D 433      26.329 -79.876 -13.207  1.00172.87           C
ANISOU 4401  CA  LYS D 433    21205  22302  22175  -2138    649    269       C
ATOM   4402  C   LYS D 433      26.905 -78.683 -13.967  1.00154.38           C
ANISOU 4402  C   LYS D 433    18921  19980  19757  -2160    535    417       C
ATOM   4403  O   LYS D 433      27.557 -77.824 -13.380  1.00136.09           O
ANISOU 4403  O   LYS D 433    16621  17626  17462  -2201    459    554       O
ATOM   4404  CB  LYS D 433      27.387 -80.979 -13.073  1.00165.80           C
ANISOU 4404  CB  LYS D 433    20253  21444  21300  -2159    828    346       C
ATOM   4405  CG  LYS D 433      27.200 -81.873 -11.851  1.00185.10           C
ANISOU 4405  CG  LYS D 433    22631  23850  23849  -2163    923    267       C
ATOM   4406  CD  LYS D 433      28.499 -82.581 -11.490  1.00179.74           C
ANISOU 4406  CD  LYS D 433    21901  23192  23198  -2203   1069    401       C
ATOM   4407  CE  LYS D 433      28.513 -82.966 -10.019  1.00169.68           C
ANISOU 4407  CE  LYS D 433    20569  21864  22038  -2227   1115    379       C
ATOM   4408  NZ  LYS D 433      28.405 -81.765  -9.143  1.00138.26           N
ANISOU 4408  NZ  LYS D 433    16622  17816  18095  -2254    968    431       N
ATOM   4409  N   SER D 434      26.625 -78.634 -15.269  1.00174.91           N
ANISOU 4409  N   SER D 434    21552  22638  22270  -2131    517    387       N
ATOM   4410  CA  SER D 434      27.176 -77.626 -16.175  1.00187.67           C
ANISOU 4410  CA  SER D 434    23214  24289  23805  -2147    422    525       C
ATOM   4411  C   SER D 434      26.503 -76.252 -16.113  1.00181.96           C
ANISOU 4411  C   SER D 434    22544  23519  23073  -2150    228    515       C
ATOM   4412  O   SER D 434      27.093 -75.260 -16.521  1.00212.68           O
ANISOU 4412  O   SER D 434    26468  27421  26921  -2175    130    658       O
ATOM   4413  CB  SER D 434      27.147 -78.136 -17.624  1.00195.31           C
ANISOU 4413  CB  SER D 434    24190  25342  24678  -2113    483    496       C
ATOM   4414  OG  SER D 434      28.076 -79.189 -17.819  1.00207.53           O
ANISOU 4414  OG  SER D 434    25698  26940  26215  -2115    650    560       O
ATOM   4415  N   ALA D 435      25.279 -76.185 -15.607  1.00143.03           N
ANISOU 4415  N   ALA D 435    17621  18538  18186  -2122    169    353       N
ATOM   4416  CA  ALA D 435      24.553 -74.918 -15.598  1.00137.49           C
ANISOU 4416  CA  ALA D 435    16973  17794  17474  -2118    -12    331       C
ATOM   4417  C   ALA D 435      25.042 -74.000 -14.477  1.00147.05           C
ANISOU 4417  C   ALA D 435    18200  18932  18740  -2157   -106    442       C
ATOM   4418  O   ALA D 435      24.896 -72.775 -14.534  1.00136.59           O
ANISOU 4418  O   ALA D 435    16924  17575  17396  -2168   -262    494       O
ATOM   4419  CB  ALA D 435      23.060 -75.171 -15.472  1.00103.42           C
ANISOU 4419  CB  ALA D 435    12661  13454  13181  -2071    -39    124       C
ATOM   4420  N   PHE D 436      25.584 -74.614 -13.434  1.00137.24           N
ANISOU 4420  N   PHE D 436    16916  17660  17569  -2178    -12    473       N
ATOM   4421  CA  PHE D 436      26.023 -73.888 -12.248  1.00175.91           C
ANISOU 4421  CA  PHE D 436    21826  22484  22527  -2215    -88    566       C
ATOM   4422  C   PHE D 436      27.533 -73.641 -12.141  1.00174.37           C
ANISOU 4422  C   PHE D 436    21627  22300  22327  -2273    -64    787       C
ATOM   4423  O   PHE D 436      27.996 -73.039 -11.177  1.00198.09           O
ANISOU 4423  O   PHE D 436    24643  25241  25379  -2310   -127    880       O
ATOM   4424  CB  PHE D 436      25.509 -74.607 -10.988  1.00209.21           C
ANISOU 4424  CB  PHE D 436    26001  26652  26838  -2200    -19    449       C
ATOM   4425  CG  PHE D 436      24.042 -74.977 -11.047  1.00191.04           C
ANISOU 4425  CG  PHE D 436    23695  24344  24547  -2141    -30    237       C
ATOM   4426  CD1 PHE D 436      23.069 -73.996 -11.182  1.00157.64           C
ANISOU 4426  CD1 PHE D 436    19520  20081  20297  -2114   -184    168       C
ATOM   4427  CD2 PHE D 436      23.641 -76.303 -10.961  1.00166.57           C
ANISOU 4427  CD2 PHE D 436    20537  21272  21479  -2114    113    114       C
ATOM   4428  CE1 PHE D 436      21.735 -74.322 -11.239  1.00 92.95           C
ANISOU 4428  CE1 PHE D 436    11322  11884  12112  -2061   -194    -14       C
ATOM   4429  CE2 PHE D 436      22.299 -76.641 -11.016  1.00164.79           C
ANISOU 4429  CE2 PHE D 436    20306  21042  21264  -2061     99    -70       C
ATOM   4430  CZ  PHE D 436      21.344 -75.646 -11.157  1.00151.49           C
ANISOU 4430  CZ  PHE D 436    18676  19325  19557  -2035    -54   -132       C
ATOM   4431  N   THR D 437      28.295 -74.095 -13.127  1.00180.43           N
ANISOU 4431  N   THR D 437    22376  23145  23033  -2281     24    875       N
ATOM   4432  CA  THR D 437      29.746 -74.272 -12.965  1.00190.21           C
ANISOU 4432  CA  THR D 437    23590  24404  24275  -2331    100   1073       C
ATOM   4433  C   THR D 437      30.570 -73.014 -12.642  1.00200.55           C
ANISOU 4433  C   THR D 437    24941  25675  25584  -2383    -36   1268       C
ATOM   4434  O   THR D 437      31.726 -73.117 -12.203  1.00180.87           O
ANISOU 4434  O   THR D 437    22427  23181  23113  -2431     17   1433       O
ATOM   4435  CB  THR D 437      30.366 -74.993 -14.189  1.00155.17           C
ANISOU 4435  CB  THR D 437    19129  20065  19762  -2319    219   1129       C
ATOM   4436  OG1 THR D 437      31.745 -75.275 -13.928  1.00149.33           O
ANISOU 4436  OG1 THR D 437    18360  19346  19033  -2364    309   1317       O
ATOM   4437  CG2 THR D 437      30.239 -74.127 -15.442  1.00115.53           C
ANISOU 4437  CG2 THR D 437    14154  15091  14649  -2305    105   1172       C
ATOM   4438  N   ASN D 438      29.988 -71.844 -12.892  1.00207.50           N
ANISOU 4438  N   ASN D 438    25878  26525  26437  -2375   -211   1253       N
ATOM   4439  CA  ASN D 438      30.650 -70.567 -12.630  1.00194.42           C
ANISOU 4439  CA  ASN D 438    24267  24826  24778  -2422   -363   1427       C
ATOM   4440  C   ASN D 438      30.255 -69.887 -11.304  1.00185.67           C
ANISOU 4440  C   ASN D 438    23191  23611  23744  -2436   -472   1395       C
ATOM   4441  O   ASN D 438      30.675 -68.764 -11.018  1.00177.33           O
ANISOU 4441  O   ASN D 438    22182  22507  22689  -2471   -616   1522       O
ATOM   4442  CB  ASN D 438      30.417 -69.625 -13.799  1.00152.69           C
ANISOU 4442  CB  ASN D 438    19025  19578  19414  -2410   -495   1461       C
ATOM   4443  CG  ASN D 438      28.965 -69.341 -13.999  1.00152.94           C
ANISOU 4443  CG  ASN D 438    19085  19587  19438  -2360   -576   1262       C
ATOM   4444  OD1 ASN D 438      28.473 -68.283 -13.615  1.00153.24           O
ANISOU 4444  OD1 ASN D 438    19173  19561  19491  -2362   -735   1249       O
ATOM   4445  ND2 ASN D 438      28.247 -70.311 -14.552  1.00148.52           N
ANISOU 4445  ND2 ASN D 438    18496  19076  18858  -2314   -467   1104       N
ATOM   4446  N   LEU D 439      29.424 -70.549 -10.510  1.00158.04           N
ANISOU 4446  N   LEU D 439    19668  20075  20304  -2405   -410   1224       N
ATOM   4447  CA  LEU D 439      29.198 -70.102  -9.138  1.00153.08           C
ANISOU 4447  CA  LEU D 439    19061  19352  19751  -2417   -482   1203       C
ATOM   4448  C   LEU D 439      29.051 -71.252  -8.124  1.00136.33           C
ANISOU 4448  C   LEU D 439    16879  17214  17708  -2409   -334   1107       C
ATOM   4449  O   LEU D 439      29.131 -72.424  -8.488  1.00103.06           O
ANISOU 4449  O   LEU D 439    12606  13060  13493  -2395   -175   1056       O
ATOM   4450  CB  LEU D 439      28.051 -69.086  -9.037  1.00123.47           C
ANISOU 4450  CB  LEU D 439    15373  15546  15995  -2380   -654   1093       C
ATOM   4451  CG  LEU D 439      26.618 -69.288  -9.521  1.00113.10           C
ANISOU 4451  CG  LEU D 439    14063  14249  14662  -2313   -667    884       C
ATOM   4452  CD1 LEU D 439      26.005 -67.916  -9.825  1.00 72.15           C
ANISOU 4452  CD1 LEU D 439     8951   9024   9440  -2300   -865    877       C
ATOM   4453  CD2 LEU D 439      26.556 -70.180 -10.746  1.00179.96           C
ANISOU 4453  CD2 LEU D 439    22491  22812  23073  -2292   -547    837       C
ATOM   4454  N   LYS D 440      28.842 -70.910  -6.853  1.00133.05           N
ANISOU 4454  N   LYS D 440    16476  16716  17361  -2417   -391   1085       N
ATOM   4455  CA  LYS D 440      29.057 -71.868  -5.766  1.00115.24           C
ANISOU 4455  CA  LYS D 440    14159  14441  15186  -2429   -258   1054       C
ATOM   4456  C   LYS D 440      27.800 -72.329  -5.046  1.00143.59           C
ANISOU 4456  C   LYS D 440    17727  18001  18830  -2372   -240    844       C
ATOM   4457  O   LYS D 440      26.806 -71.592  -4.905  1.00110.20           O
ANISOU 4457  O   LYS D 440    13547  13729  14596  -2331   -370    744       O
ATOM   4458  CB  LYS D 440      30.092 -71.337  -4.747  1.00119.50           C
ANISOU 4458  CB  LYS D 440    14714  14918  15770  -2494   -300   1224       C
ATOM   4459  CG  LYS D 440      29.538 -70.401  -3.665  1.00 94.30           C
ANISOU 4459  CG  LYS D 440    11578  11630  12622  -2485   -448   1183       C
ATOM   4460  CD  LYS D 440      30.559 -69.349  -3.207  1.00138.51           C
ANISOU 4460  CD  LYS D 440    17233  17171  18225  -2550   -566   1386       C
ATOM   4461  CE  LYS D 440      31.556 -69.851  -2.158  1.00128.41           C
ANISOU 4461  CE  LYS D 440    15912  15866  17012  -2609   -470   1499       C
ATOM   4462  NZ  LYS D 440      32.487 -68.756  -1.731  1.00122.21           N
ANISOU 4462  NZ  LYS D 440    15189  15019  16228  -2673   -602   1696       N
ATOM   4463  N   GLN D 441      27.866 -73.574  -4.593  1.00155.83           N
ANISOU 4463  N   GLN D 441    19199  19575  20433  -2370    -76    784       N
ATOM   4464  CA  GLN D 441      26.839 -74.130  -3.738  1.00158.81           C
ANISOU 4464  CA  GLN D 441    19540  19926  20876  -2323    -42    608       C
ATOM   4465  C   GLN D 441      26.899 -73.394  -2.399  1.00164.46           C
ANISOU 4465  C   GLN D 441    20284  20554  21651  -2340   -138    645       C
ATOM   4466  O   GLN D 441      27.934 -73.400  -1.729  1.00144.73           O
ANISOU 4466  O   GLN D 441    17771  18031  19188  -2398   -103    782       O
ATOM   4467  CB  GLN D 441      27.169 -75.602  -3.515  1.00156.41           C
ANISOU 4467  CB  GLN D 441    19141  19667  20619  -2331    157    575       C
ATOM   4468  CG  GLN D 441      25.980 -76.535  -3.537  1.00160.64           C
ANISOU 4468  CG  GLN D 441    19627  20227  21180  -2268    227    369       C
ATOM   4469  CD  GLN D 441      26.397 -77.964  -3.817  1.00159.49           C
ANISOU 4469  CD  GLN D 441    19400  20146  21054  -2276    420    352       C
ATOM   4470  OE1 GLN D 441      27.516 -78.369  -3.499  1.00155.93           O
ANISOU 4470  OE1 GLN D 441    18912  19705  20629  -2329    516    479       O
ATOM   4471  NE2 GLN D 441      25.504 -78.733  -4.433  1.00170.39           N
ANISOU 4471  NE2 GLN D 441    20752  21569  22418  -2225    475    199       N
ATOM   4472  N   LEU D 442      25.788 -72.783  -1.991  1.00158.64           N
ANISOU 4472  N   LEU D 442    19586  19768  20922  -2288   -255    524       N
ATOM   4473  CA  LEU D 442      25.770 -71.972  -0.767  1.00119.31           C
ANISOU 4473  CA  LEU D 442    14646  14701  15987  -2295   -363    552       C
ATOM   4474  C   LEU D 442      25.365 -72.771   0.472  1.00122.32           C
ANISOU 4474  C   LEU D 442    14960  15061  16457  -2273   -275    451       C
ATOM   4475  O   LEU D 442      24.290 -73.363   0.515  1.00172.62           O
ANISOU 4475  O   LEU D 442    21292  21451  22845  -2212   -236    284       O
ATOM   4476  CB  LEU D 442      24.853 -70.760  -0.954  1.00 98.39           C
ANISOU 4476  CB  LEU D 442    12082  12004  13295  -2250   -548    492       C
ATOM   4477  CG  LEU D 442      24.431 -69.887   0.227  1.00108.32           C
ANISOU 4477  CG  LEU D 442    13393  13172  14592  -2229   -678    468       C
ATOM   4478  CD1 LEU D 442      23.847 -68.580  -0.283  1.00 96.99           C
ANISOU 4478  CD1 LEU D 442    12054  11702  13097  -2200   -864    459       C
ATOM   4479  CD2 LEU D 442      23.403 -70.587   1.096  1.00145.99           C
ANISOU 4479  CD2 LEU D 442    18111  17935  19424  -2167   -619    297       C
ATOM   4480  N   PRO D 443      26.231 -72.782   1.490  1.00106.32           N
ANISOU 4480  N   PRO D 443    12917  12994  14485  -2325   -247    558       N
ATOM   4481  CA  PRO D 443      26.049 -73.489   2.759  1.00117.06           C
ANISOU 4481  CA  PRO D 443    14209  14332  15934  -2316   -164    491       C
ATOM   4482  C   PRO D 443      25.055 -72.718   3.635  1.00151.15           C
ANISOU 4482  C   PRO D 443    18575  18581  20273  -2259   -298    391       C
ATOM   4483  O   PRO D 443      24.721 -71.577   3.297  1.00152.83           O
ANISOU 4483  O   PRO D 443    18880  18756  20433  -2240   -456    402       O
ATOM   4484  CB  PRO D 443      27.446 -73.454   3.359  1.00 99.59           C
ANISOU 4484  CB  PRO D 443    11988  12097  13755  -2401   -123    676       C
ATOM   4485  CG  PRO D 443      27.951 -72.118   2.933  1.00136.47           C
ANISOU 4485  CG  PRO D 443    16763  16726  18364  -2433   -283    812       C
ATOM   4486  CD  PRO D 443      27.356 -71.838   1.566  1.00117.80           C
ANISOU 4486  CD  PRO D 443    14434  14406  15918  -2393   -335    754       C
ATOM   4487  N   PHE D 444      24.568 -73.327   4.715  1.00128.96           N
ANISOU 4487  N   PHE D 444    15704  15758  17537  -2229   -238    294       N
ATOM   4488  CA  PHE D 444      23.602 -72.655   5.579  1.00135.95           C
ANISOU 4488  CA  PHE D 444    16631  16583  18442  -2166   -357    197       C
ATOM   4489  C   PHE D 444      24.182 -71.546   6.459  1.00122.47           C
ANISOU 4489  C   PHE D 444    15002  14789  16743  -2198   -483    311       C
ATOM   4490  O   PHE D 444      25.229 -71.715   7.081  1.00126.95           O
ANISOU 4490  O   PHE D 444    15547  15337  17350  -2266   -430    433       O
ATOM   4491  CB  PHE D 444      22.851 -73.663   6.451  1.00169.20           C
ANISOU 4491  CB  PHE D 444    20746  20814  22729  -2116   -256     56       C
ATOM   4492  CG  PHE D 444      22.146 -73.035   7.623  1.00147.41           C
ANISOU 4492  CG  PHE D 444    18019  17988  20002  -2062   -359     -9       C
ATOM   4493  CD1 PHE D 444      21.028 -72.228   7.431  1.00121.50           C
ANISOU 4493  CD1 PHE D 444    14807  14681  16677  -1986   -495   -107       C
ATOM   4494  CD2 PHE D 444      22.603 -73.245   8.915  1.00117.15           C
ANISOU 4494  CD2 PHE D 444    14148  14122  16242  -2086   -320     29       C
ATOM   4495  CE1 PHE D 444      20.386 -71.640   8.508  1.00116.74           C
ANISOU 4495  CE1 PHE D 444    14238  14019  16100  -1930   -590   -164       C
ATOM   4496  CE2 PHE D 444      21.966 -72.661   9.985  1.00118.98           C
ANISOU 4496  CE2 PHE D 444    14413  14296  16500  -2031   -415    -30       C
ATOM   4497  CZ  PHE D 444      20.854 -71.857   9.782  1.00125.81           C
ANISOU 4497  CZ  PHE D 444    15349  15134  17317  -1951   -550   -127       C
ATOM   4498  N   PHE D 445      23.477 -70.416   6.500  1.00123.21           N
ANISOU 4498  N   PHE D 445    15189  14829  16798  -2150   -651    270       N
ATOM   4499  CA  PHE D 445      23.847 -69.277   7.335  1.00 94.92           C
ANISOU 4499  CA  PHE D 445    11693  11154  13217  -2167   -793    358       C
ATOM   4500  C   PHE D 445      22.595 -68.501   7.771  1.00107.25           C
ANISOU 4500  C   PHE D 445    13318  12667  14766  -2076   -929    229       C
ATOM   4501  O   PHE D 445      21.630 -68.376   7.003  1.00120.28           O
ANISOU 4501  O   PHE D 445    14984  14345  16373  -2017   -968    124       O
ATOM   4502  CB  PHE D 445      24.818 -68.353   6.571  1.00 95.44           C
ANISOU 4502  CB  PHE D 445    11841  11199  13223  -2235   -889    529       C
ATOM   4503  CG  PHE D 445      24.137 -67.313   5.715  1.00104.20           C
ANISOU 4503  CG  PHE D 445    13040  12292  14258  -2193  -1044    494       C
ATOM   4504  CD1 PHE D 445      23.939 -66.021   6.195  1.00111.53           C
ANISOU 4504  CD1 PHE D 445    14074  13134  15167  -2175  -1226    519       C
ATOM   4505  CD2 PHE D 445      23.686 -67.622   4.436  1.00114.65           C
ANISOU 4505  CD2 PHE D 445    14345  13688  15531  -2171  -1009    436       C
ATOM   4506  CE1 PHE D 445      23.298 -65.045   5.416  1.00 96.90           C
ANISOU 4506  CE1 PHE D 445    12302  11266  13248  -2136  -1371    488       C
ATOM   4507  CE2 PHE D 445      23.043 -66.652   3.648  1.00120.79           C
ANISOU 4507  CE2 PHE D 445    15200  14451  16241  -2135  -1153    405       C
ATOM   4508  CZ  PHE D 445      22.852 -65.362   4.142  1.00102.91           C
ANISOU 4508  CZ  PHE D 445    13037  12101  13961  -2118  -1332    432       C
ATOM   4509  N   TYR D 446      22.592 -67.990   8.998  1.00 90.24           N
ANISOU 4509  N   TYR D 446    11200  10439  12648  -2063  -1000    238       N
ATOM   4510  CA  TYR D 446      21.529 -67.068   9.409  1.00113.70           C
ANISOU 4510  CA  TYR D 446    14250  13353  15597  -1978  -1149    141       C
ATOM   4511  C   TYR D 446      22.103 -65.726   9.904  1.00122.24           C
ANISOU 4511  C   TYR D 446    15452  14337  16657  -2007  -1318    258       C
ATOM   4512  O   TYR D 446      23.129 -65.716  10.617  1.00 87.69           O
ANISOU 4512  O   TYR D 446    11077   9924  12317  -2074  -1301    379       O
ATOM   4513  CB  TYR D 446      20.608 -67.694  10.470  1.00101.45           C
ANISOU 4513  CB  TYR D 446    12634  11807  14105  -1900  -1091     -3       C
ATOM   4514  CG  TYR D 446      19.647 -66.682  11.073  1.00 97.95           C
ANISOU 4514  CG  TYR D 446    12279  11297  13641  -1813  -1248    -82       C
ATOM   4515  CD1 TYR D 446      18.467 -66.332  10.424  1.00 69.42           C
ANISOU 4515  CD1 TYR D 446     8698   7700   9980  -1734  -1317   -196       C
ATOM   4516  CD2 TYR D 446      19.929 -66.066  12.288  1.00 86.57           C
ANISOU 4516  CD2 TYR D 446    10890   9775  12226  -1810  -1326    -39       C
ATOM   4517  CE1 TYR D 446      17.597 -65.387  10.978  1.00 95.39           C
ANISOU 4517  CE1 TYR D 446    12070  10928  13248  -1651  -1460   -264       C
ATOM   4518  CE2 TYR D 446      19.078 -65.127  12.842  1.00 82.92           C
ANISOU 4518  CE2 TYR D 446    10514   9250  11740  -1726  -1469   -109       C
ATOM   4519  CZ  TYR D 446      17.912 -64.789  12.195  1.00100.74           C
ANISOU 4519  CZ  TYR D 446    12801  11525  13950  -1645  -1535   -221       C
ATOM   4520  OH  TYR D 446      17.078 -63.853  12.780  1.00101.21           O
ANISOU 4520  OH  TYR D 446    12948  11522  13987  -1559  -1675   -286       O
ATOM   4521  N   TYR D 447      21.450 -64.614   9.527  1.00 72.80           N
ANISOU 4521  N   TYR D 447     9291   8033  10337  -1958  -1481    226       N
ATOM   4522  CA  TYR D 447      21.914 -63.270   9.897  1.00102.78           C
ANISOU 4522  CA  TYR D 447    13211  11733  14107  -1980  -1659    331       C
ATOM   4523  C   TYR D 447      20.772 -62.353  10.307  1.00 93.66           C
ANISOU 4523  C   TYR D 447    12141  10520  12926  -1883  -1806    221       C
ATOM   4524  O   TYR D 447      19.785 -62.230   9.589  1.00 81.70           O
ANISOU 4524  O   TYR D 447    10633   9037  11373  -1820  -1836    117       O
ATOM   4525  CB  TYR D 447      22.711 -62.632   8.738  1.00134.00           C
ANISOU 4525  CB  TYR D 447    17219  15692  18004  -2052  -1730    472       C
ATOM   4526  CG  TYR D 447      22.962 -61.134   8.856  1.00115.99           C
ANISOU 4526  CG  TYR D 447    15073  13317  15683  -2063  -1939    563       C
ATOM   4527  CD1 TYR D 447      24.112 -60.640   9.469  1.00 94.40           C
ANISOU 4527  CD1 TYR D 447    12387  10516  12966  -2140  -1997    725       C
ATOM   4528  CD2 TYR D 447      22.056 -60.213   8.336  1.00 76.96           C
ANISOU 4528  CD2 TYR D 447    10207   8350  10685  -2000  -2080    492       C
ATOM   4529  CE1 TYR D 447      24.342 -59.270   9.575  1.00 99.34           C
ANISOU 4529  CE1 TYR D 447    13138  11051  13556  -2151  -2196    810       C
ATOM   4530  CE2 TYR D 447      22.282 -58.843   8.435  1.00 97.52           C
ANISOU 4530  CE2 TYR D 447    12934  10866  13254  -2010  -2275    574       C
ATOM   4531  CZ  TYR D 447      23.424 -58.380   9.052  1.00119.04           C
ANISOU 4531  CZ  TYR D 447    15708  13523  15997  -2085  -2334    732       C
ATOM   4532  OH  TYR D 447      23.642 -57.026   9.143  1.00136.24           O
ANISOU 4532  OH  TYR D 447    18010  15611  18142  -2095  -2534    815       O
ATOM   4533  N   SER D 448      20.924 -61.681  11.446  1.00100.63           N
ANISOU 4533  N   SER D 448    13092  11315  13828  -1870  -1902    250       N
ATOM   4534  CA  SER D 448      19.903 -60.746  11.921  1.00113.33           C
ANISOU 4534  CA  SER D 448    14791  12859  15409  -1774  -2049    155       C
ATOM   4535  C   SER D 448      20.504 -59.410  12.376  1.00118.59           C
ANISOU 4535  C   SER D 448    15592  13415  16051  -1803  -2232    269       C
ATOM   4536  O   SER D 448      21.452 -59.376  13.188  1.00110.27           O
ANISOU 4536  O   SER D 448    14551  12313  15033  -1864  -2230    376       O
ATOM   4537  CB  SER D 448      19.095 -61.376  13.063  1.00123.33           C
ANISOU 4537  CB  SER D 448    16001  14133  16728  -1691  -1977     22       C
ATOM   4538  OG  SER D 448      17.973 -60.583  13.413  1.00138.19           O
ANISOU 4538  OG  SER D 448    17960  15968  18579  -1585  -2102    -84       O
ATOM   4539  N   ASP D 449      19.950 -58.321  11.839  1.00125.84           N
ANISOU 4539  N   ASP D 449    16609  14294  16910  -1762  -2390    250       N
ATOM   4540  CA  ASP D 449      20.344 -56.964  12.213  1.00166.78           C
ANISOU 4540  CA  ASP D 449    21932  19370  22067  -1775  -2584    342       C
ATOM   4541  C   ASP D 449      19.471 -56.472  13.365  1.00175.97           C
ANISOU 4541  C   ASP D 449    23161  20465  23237  -1672  -2668    234       C
ATOM   4542  O   ASP D 449      19.642 -55.361  13.864  1.00176.47           O
ANISOU 4542  O   ASP D 449    23344  20428  23277  -1664  -2832    285       O
ATOM   4543  CB  ASP D 449      20.197 -56.020  11.013  1.00186.67           C
ANISOU 4543  CB  ASP D 449    24524  21883  24519  -1783  -2717    378       C
ATOM   4544  CG  ASP D 449      21.509 -55.337  10.635  1.00214.88           C
ANISOU 4544  CG  ASP D 449    28155  25413  28075  -1892  -2808    576       C
ATOM   4545  OD1 ASP D 449      22.408 -55.230  11.503  1.00245.37           O
ANISOU 4545  OD1 ASP D 449    32043  29215  31970  -1947  -2825    681       O
ATOM   4546  OD2 ASP D 449      21.639 -54.897   9.469  1.00183.50           O
ANISOU 4546  OD2 ASP D 449    24200  21466  24057  -1924  -2866    631       O
ATOM   4547  N   SER D 450      18.534 -57.318  13.778  1.00180.42           N
ANISOU 4547  N   SER D 450    23642  21082  23829  -1591  -2555     87       N
ATOM   4548  CA  SER D 450      17.536 -56.966  14.781  1.00157.03           C
ANISOU 4548  CA  SER D 450    20725  18072  20867  -1476  -2617    -33       C
ATOM   4549  C   SER D 450      18.172 -56.700  16.132  1.00166.56           C
ANISOU 4549  C   SER D 450    21979  19197  22108  -1491  -2658     28       C
ATOM   4550  O   SER D 450      19.240 -57.236  16.436  1.00170.36           O
ANISOU 4550  O   SER D 450    22412  19684  22633  -1582  -2575    130       O
ATOM   4551  CB  SER D 450      16.527 -58.102  14.929  1.00165.26           C
ANISOU 4551  CB  SER D 450    21646  19203  21941  -1398  -2466   -185       C
ATOM   4552  OG  SER D 450      17.173 -59.276  15.393  1.00172.40           O
ANISOU 4552  OG  SER D 450    22436  20157  22911  -1454  -2300   -158       O
ATOM   4553  N   PRO D 451      17.517 -55.861  16.949  1.00176.26           N
ANISOU 4553  N   PRO D 451    23306  20348  23317  -1399  -2786    -34       N
ATOM   4554  CA  PRO D 451      17.951 -55.645  18.333  1.00165.04           C
ANISOU 4554  CA  PRO D 451    21931  18850  21926  -1395  -2822     -1       C
ATOM   4555  C   PRO D 451      17.816 -56.945  19.116  1.00121.07           C
ANISOU 4555  C   PRO D 451    16226  13349  16426  -1376  -2640    -68       C
ATOM   4556  O   PRO D 451      16.842 -57.657  18.918  1.00120.01           O
ANISOU 4556  O   PRO D 451    16005  13294  16301  -1302  -2544   -195       O
ATOM   4557  CB  PRO D 451      16.945 -54.612  18.862  1.00161.64           C
ANISOU 4557  CB  PRO D 451    21619  18346  21452  -1271  -2979    -93       C
ATOM   4558  CG  PRO D 451      16.359 -53.964  17.644  1.00153.50           C
ANISOU 4558  CG  PRO D 451    20637  17327  20361  -1249  -3068   -118       C
ATOM   4559  CD  PRO D 451      16.354 -55.030  16.589  1.00156.17           C
ANISOU 4559  CD  PRO D 451    20841  17782  20715  -1296  -2909   -133       C
ATOM   4560  N   CYS D 452      18.771 -57.264  19.979  1.00111.02           N
ANISOU 4560  N   CYS D 452    14933  12048  15202  -1444  -2592     18       N
ATOM   4561  CA  CYS D 452      18.629 -58.442  20.828  1.00109.31           C
ANISOU 4561  CA  CYS D 452    14589  11891  15054  -1423  -2427    -46       C
ATOM   4562  C   CYS D 452      18.054 -58.061  22.199  1.00151.20           C
ANISOU 4562  C   CYS D 452    19946  17135  20367  -1322  -2493   -121       C
ATOM   4563  O   CYS D 452      18.321 -56.967  22.699  1.00157.15           O
ANISOU 4563  O   CYS D 452    20837  17784  21088  -1316  -2651    -68       O
ATOM   4564  CB  CYS D 452      19.948 -59.212  20.962  1.00 97.23           C
ANISOU 4564  CB  CYS D 452    12979  10383  13580  -1554  -2306     82       C
ATOM   4565  SG  CYS D 452      19.728 -60.883  21.698  1.00147.70           S
ANISOU 4565  SG  CYS D 452    19181  16876  20063  -1537  -2073     -4       S
ATOM   4566  N   GLU D 453      17.244 -58.943  22.788  1.00177.51           N
ANISOU 4566  N   GLU D 453    23172  20534  23739  -1240  -2377   -245       N
ATOM   4567  CA  GLU D 453      16.547 -58.625  24.038  1.00199.14           C
ANISOU 4567  CA  GLU D 453    25952  23230  26481  -1126  -2433   -330       C
ATOM   4568  C   GLU D 453      17.199 -59.229  25.288  1.00180.03           C
ANISOU 4568  C   GLU D 453    23471  20803  24130  -1161  -2348   -292       C
ATOM   4569  O   GLU D 453      17.974 -60.186  25.213  1.00142.91           O
ANISOU 4569  O   GLU D 453    18657  16156  19486  -1258  -2205   -231       O
ATOM   4570  CB  GLU D 453      15.072 -59.038  23.955  1.00214.53           C
ANISOU 4570  CB  GLU D 453    27837  25252  28422   -991  -2388   -494       C
ATOM   4571  CG  GLU D 453      14.173 -58.353  24.987  1.00232.61           C
ANISOU 4571  CG  GLU D 453    30208  27488  30686   -852  -2494   -583       C
ATOM   4572  CD  GLU D 453      13.175 -57.399  24.350  1.00244.75           C
ANISOU 4572  CD  GLU D 453    31850  28999  32147   -758  -2629   -650       C
ATOM   4573  OE1 GLU D 453      12.404 -56.761  25.099  1.00235.70           O
ANISOU 4573  OE1 GLU D 453    30781  27806  30970   -637  -2724   -721       O
ATOM   4574  OE2 GLU D 453      13.160 -57.291  23.102  1.00252.39           O
ANISOU 4574  OE2 GLU D 453    32821  29992  33084   -803  -2639   -631       O
ATOM   4575  N   TYR D 465      19.005 -76.126  27.102  1.00174.24           N
ANISOU 4575  N   TYR D 465    20635  21184  24386  -1598    -99   -548       N
ATOM   4576  CA  TYR D 465      17.799 -75.329  27.334  1.00206.02           C
ANISOU 4576  CA  TYR D 465    24737  25183  28356  -1464   -236   -650       C
ATOM   4577  C   TYR D 465      17.667 -74.230  26.274  1.00195.01           C
ANISOU 4577  C   TYR D 465    23506  23733  26856  -1454   -373   -632       C
ATOM   4578  O   TYR D 465      17.804 -74.501  25.079  1.00156.12           O
ANISOU 4578  O   TYR D 465    18579  18836  21902  -1497   -335   -621       O
ATOM   4579  CB  TYR D 465      17.806 -74.727  28.748  1.00216.11           C
ANISOU 4579  CB  TYR D 465    26052  26406  29652  -1422   -309   -640       C
ATOM   4580  CG  TYR D 465      16.478 -74.809  29.478  1.00234.56           C
ANISOU 4580  CG  TYR D 465    28341  28780  32003  -1275   -342   -773       C
ATOM   4581  CD1 TYR D 465      15.381 -75.450  28.906  1.00239.39           C
ANISOU 4581  CD1 TYR D 465    28871  29470  32617  -1196   -302   -888       C
ATOM   4582  CD2 TYR D 465      16.322 -74.239  30.738  1.00232.05           C
ANISOU 4582  CD2 TYR D 465    28061  28417  31692  -1215   -416   -780       C
ATOM   4583  CE1 TYR D 465      14.163 -75.523  29.573  1.00233.82           C
ANISOU 4583  CE1 TYR D 465    28118  28801  31923  -1060   -334   -999       C
ATOM   4584  CE2 TYR D 465      15.109 -74.305  31.412  1.00223.21           C
ANISOU 4584  CE2 TYR D 465    26896  27335  30581  -1075   -446   -896       C
ATOM   4585  CZ  TYR D 465      14.035 -74.947  30.824  1.00217.64           C
ANISOU 4585  CZ  TYR D 465    26105  26710  29879   -998   -404  -1002       C
ATOM   4586  OH  TYR D 465      12.832 -75.011  31.487  1.00181.10           O
ANISOU 4586  OH  TYR D 465    21428  22122  25259   -857   -435  -1107       O
ATOM   4587  N   VAL D 466      17.413 -72.998  26.716  1.00201.31           N
ANISOU 4587  N   VAL D 466    24442  24450  27597  -1397   -531   -629       N
ATOM   4588  CA  VAL D 466      17.277 -71.856  25.804  1.00195.34           C
ANISOU 4588  CA  VAL D 466    23846  23634  26742  -1384   -676   -609       C
ATOM   4589  C   VAL D 466      18.518 -71.546  24.953  1.00211.05           C
ANISOU 4589  C   VAL D 466    25904  25586  28700  -1515   -679   -469       C
ATOM   4590  O   VAL D 466      18.383 -71.261  23.760  1.00211.57           O
ANISOU 4590  O   VAL D 466    26024  25656  28705  -1523   -717   -468       O
ATOM   4591  CB  VAL D 466      16.870 -70.555  26.542  1.00158.93           C
ANISOU 4591  CB  VAL D 466    19376  18933  22077  -1302   -849   -622       C
ATOM   4592  CG1 VAL D 466      16.886 -69.366  25.570  1.00127.64           C
ANISOU 4592  CG1 VAL D 466    15577  14904  18016  -1307   -998   -584       C
ATOM   4593  CG2 VAL D 466      15.505 -70.707  27.210  1.00119.22           C
ANISOU 4593  CG2 VAL D 466    14298  13941  17058  -1155   -867   -762       C
ATOM   4594  N   PRO D 467      19.723 -71.570  25.563  1.00209.71           N
ANISOU 4594  N   PRO D 467    25732  25379  28570  -1616   -643   -346       N
ATOM   4595  CA  PRO D 467      20.941 -71.169  24.847  1.00177.09           C
ANISOU 4595  CA  PRO D 467    21674  21206  24406  -1738   -660   -196       C
ATOM   4596  C   PRO D 467      21.399 -72.164  23.777  1.00174.13           C
ANISOU 4596  C   PRO D 467    21205  20908  24049  -1814   -517   -166       C
ATOM   4597  O   PRO D 467      21.512 -73.377  24.042  1.00132.48           O
ANISOU 4597  O   PRO D 467    15782  15704  18850  -1838   -357   -190       O
ATOM   4598  CB  PRO D 467      21.983 -71.089  25.962  1.00122.81           C
ANISOU 4598  CB  PRO D 467    14800  14281  17582  -1815   -644    -83       C
ATOM   4599  CG  PRO D 467      21.550 -72.105  26.913  1.00148.60           C
ANISOU 4599  CG  PRO D 467    17919  17608  20933  -1774   -525   -167       C
ATOM   4600  CD  PRO D 467      20.042 -72.004  26.936  1.00204.69           C
ANISOU 4600  CD  PRO D 467    25019  24741  28012  -1626   -580   -331       C
ATOM   4601  N   LEU D 468      21.701 -71.620  22.597  1.00164.30           N
ANISOU 4601  N   LEU D 468    20047  19646  22734  -1852   -577   -107       N
ATOM   4602  CA  LEU D 468      22.139 -72.397  21.442  1.00132.51           C
ANISOU 4602  CA  LEU D 468    15957  15687  18706  -1918   -461    -73       C
ATOM   4603  C   LEU D 468      23.515 -71.924  20.957  1.00135.04           C
ANISOU 4603  C   LEU D 468    16348  15964  18997  -2039   -482    108       C
ATOM   4604  O   LEU D 468      23.802 -70.720  20.957  1.00119.50           O
ANISOU 4604  O   LEU D 468    14517  13915  16974  -2050   -634    182       O
ATOM   4605  CB  LEU D 468      21.129 -72.253  20.306  1.00143.89           C
ANISOU 4605  CB  LEU D 468    17427  17162  20082  -1845   -508   -177       C
ATOM   4606  CG  LEU D 468      21.531 -71.398  19.092  1.00120.49           C
ANISOU 4606  CG  LEU D 468    14581  14168  17033  -1886   -604    -96       C
ATOM   4607  CD1 LEU D 468      21.481 -72.243  17.824  1.00 63.33           C
ANISOU 4607  CD1 LEU D 468     7272   7011   9779  -1909   -495   -121       C
ATOM   4608  CD2 LEU D 468      20.652 -70.148  18.952  1.00 92.87           C
ANISOU 4608  CD2 LEU D 468    11215  10612  13462  -1799   -790   -155       C
ATOM   4609  N   LYS D 469      24.367 -72.865  20.557  1.00121.39           N
ANISOU 4609  N   LYS D 469    14527  14290  17306  -2128   -332    183       N
ATOM   4610  CA  LYS D 469      25.645 -72.506  19.966  1.00119.91           C
ANISOU 4610  CA  LYS D 469    14396  14075  17088  -2239   -340    359       C
ATOM   4611  C   LYS D 469      25.690 -72.956  18.517  1.00133.75           C
ANISOU 4611  C   LYS D 469    16126  15894  18799  -2258   -275    359       C
ATOM   4612  O   LYS D 469      25.389 -74.108  18.203  1.00126.66           O
ANISOU 4612  O   LYS D 469    15111  15077  17938  -2245   -132    282       O
ATOM   4613  CB  LYS D 469      26.817 -73.129  20.733  1.00138.41           C
ANISOU 4613  CB  LYS D 469    16664  16419  19505  -2341   -222    482       C
ATOM   4614  CG  LYS D 469      28.189 -72.828  20.111  1.00156.54           C
ANISOU 4614  CG  LYS D 469    19011  18694  21772  -2460   -220    678       C
ATOM   4615  CD  LYS D 469      29.341 -73.433  20.919  1.00157.19           C
ANISOU 4615  CD  LYS D 469    19018  18776  21930  -2562   -102    806       C
ATOM   4616  CE  LYS D 469      30.696 -72.936  20.412  1.00166.77           C
ANISOU 4616  CE  LYS D 469    20300  19956  23109  -2675   -129   1018       C
ATOM   4617  NZ  LYS D 469      31.466 -72.172  21.445  1.00157.22           N
ANISOU 4617  NZ  LYS D 469    19186  18686  21862  -2669   -195   1103       N
ATOM   4618  N   SER D 470      26.033 -72.027  17.632  1.00168.04           N
ANISOU 4618  N   SER D 470    20582  20201  23063  -2284   -388    443       N
ATOM   4619  CA  SER D 470      26.321 -72.356  16.239  1.00170.93           C
ANISOU 4619  CA  SER D 470    20937  20625  23384  -2317   -332    478       C
ATOM   4620  C   SER D 470      27.321 -71.358  15.676  1.00142.73           C
ANISOU 4620  C   SER D 470    17477  17002  19753  -2392   -437    653       C
ATOM   4621  O   SER D 470      27.298 -70.158  16.001  1.00 95.11           O
ANISOU 4621  O   SER D 470    11563  10889  13685  -2381   -604    693       O
ATOM   4622  CB  SER D 470      25.050 -72.361  15.382  1.00153.71           C
ANISOU 4622  CB  SER D 470    18764  18484  21155  -2221   -368    322       C
ATOM   4623  OG  SER D 470      24.746 -71.061  14.894  1.00108.12           O
ANISOU 4623  OG  SER D 470    13125  12653  15301  -2191   -549    336       O
ATOM   4624  N   ALA D 471      28.211 -71.854  14.835  1.00115.39           N
ANISOU 4624  N   ALA D 471    13977  13588  16278  -2468   -340    761       N
ATOM   4625  CA  ALA D 471      29.132 -70.958  14.179  1.00116.71           C
ANISOU 4625  CA  ALA D 471    14241  13718  16386  -2536   -436    930       C
ATOM   4626  C   ALA D 471      28.346 -70.174  13.128  1.00112.94           C
ANISOU 4626  C   ALA D 471    13849  13240  15824  -2473   -565    863       C
ATOM   4627  O   ALA D 471      28.724 -69.083  12.723  1.00118.22           O
ANISOU 4627  O   ALA D 471    14624  13858  16436  -2498   -707    965       O
ATOM   4628  CB  ALA D 471      30.260 -71.735  13.553  1.00109.85           C
ANISOU 4628  CB  ALA D 471    13305  12909  15525  -2625   -293   1063       C
ATOM   4629  N   THR D 472      27.223 -70.727  12.705  1.00113.81           N
ANISOU 4629  N   THR D 472    13909  13405  15928  -2391   -518    691       N
ATOM   4630  CA  THR D 472      26.499 -70.149  11.586  1.00104.52           C
ANISOU 4630  CA  THR D 472    12798  12243  14674  -2338   -615    627       C
ATOM   4631  C   THR D 472      25.452 -69.108  12.015  1.00126.25           C
ANISOU 4631  C   THR D 472    15641  14928  17399  -2253   -786    528       C
ATOM   4632  O   THR D 472      24.721 -68.573  11.177  1.00100.78           O
ANISOU 4632  O   THR D 472    12470  11709  14112  -2201   -875    462       O
ATOM   4633  CB  THR D 472      25.924 -71.259  10.666  1.00103.67           C
ANISOU 4633  CB  THR D 472    12597  12232  14561  -2303   -478    514       C
ATOM   4634  OG1 THR D 472      24.601 -70.907  10.230  1.00125.13           O
ANISOU 4634  OG1 THR D 472    15350  14955  17238  -2209   -563    361       O
ATOM   4635  CG2 THR D 472      25.932 -72.618  11.395  1.00 91.20           C
ANISOU 4635  CG2 THR D 472    10884  10700  13069  -2307   -299    454       C
ATOM   4636  N   CYS D 473      25.398 -68.796  13.310  1.00126.68           N
ANISOU 4636  N   CYS D 473    15716  14919  17498  -2239   -834    521       N
ATOM   4637  CA  CYS D 473      24.453 -67.782  13.764  1.00127.16           C
ANISOU 4637  CA  CYS D 473    15870  14914  17531  -2155   -998    433       C
ATOM   4638  C   CYS D 473      25.092 -66.402  13.817  1.00115.12           C
ANISOU 4638  C   CYS D 473    14481  13298  15960  -2196  -1175    568       C
ATOM   4639  O   CYS D 473      25.918 -66.109  14.687  1.00108.07           O
ANISOU 4639  O   CYS D 473    13617  12346  15099  -2253  -1202    679       O
ATOM   4640  CB  CYS D 473      23.836 -68.137  15.119  1.00122.41           C
ANISOU 4640  CB  CYS D 473    15222  14294  16993  -2095   -968    328       C
ATOM   4641  SG  CYS D 473      22.458 -67.022  15.558  1.00 95.46           S
ANISOU 4641  SG  CYS D 473    11915  10817  13539  -1969  -1153    194       S
ATOM   4642  N   ILE D 474      24.672 -65.543  12.894  1.00 91.31           N
ANISOU 4642  N   ILE D 474    11551  10270  12873  -2167  -1301    557       N
ATOM   4643  CA  ILE D 474      25.317 -64.251  12.737  1.00122.46           C
ANISOU 4643  CA  ILE D 474    15622  14137  16771  -2212  -1471    695       C
ATOM   4644  C   ILE D 474      24.455 -63.126  13.318  1.00128.85           C
ANISOU 4644  C   ILE D 474    16541  14863  17554  -2131  -1650    617       C
ATOM   4645  O   ILE D 474      23.509 -62.638  12.691  1.00118.90           O
ANISOU 4645  O   ILE D 474    15325  13608  16245  -2060  -1733    521       O
ATOM   4646  CB  ILE D 474      25.634 -64.010  11.244  1.00112.85           C
ANISOU 4646  CB  ILE D 474    14423  12963  15490  -2250  -1494    766       C
ATOM   4647  CG1 ILE D 474      26.785 -64.920  10.811  1.00 88.97           C
ANISOU 4647  CG1 ILE D 474    11313  10002  12488  -2344  -1339    891       C
ATOM   4648  CG2 ILE D 474      25.972 -62.561  10.978  1.00123.36           C
ANISOU 4648  CG2 ILE D 474    15888  14216  16766  -2272  -1697    875       C
ATOM   4649  CD1 ILE D 474      26.707 -65.306   9.377  1.00110.66           C
ANISOU 4649  CD1 ILE D 474    14024  12835  15189  -2348  -1280    882       C
ATOM   4650  N   THR D 475      24.850 -62.673  14.502  1.00115.30           N
ANISOU 4650  N   THR D 475    14874  13065  15868  -2145  -1714    671       N
ATOM   4651  CA  THR D 475      24.083 -61.698  15.251  1.00103.91           C
ANISOU 4651  CA  THR D 475    13533  11539  14408  -2064  -1871    596       C
ATOM   4652  C   THR D 475      25.072 -60.965  16.155  1.00126.45           C
ANISOU 4652  C   THR D 475    16472  14296  17278  -2129  -1969    741       C
ATOM   4653  O   THR D 475      26.019 -61.597  16.659  1.00 82.37           O
ANISOU 4653  O   THR D 475    10829   8722  11746  -2208  -1865    838       O
ATOM   4654  CB  THR D 475      23.007 -62.431  16.075  1.00129.68           C
ANISOU 4654  CB  THR D 475    16724  14835  17716  -1966  -1784    420       C
ATOM   4655  OG1 THR D 475      23.449 -63.768  16.347  1.00117.92           O
ANISOU 4655  OG1 THR D 475    15096  13415  16292  -2011  -1588    424       O
ATOM   4656  CG2 THR D 475      21.723 -62.534  15.287  1.00156.45           C
ANISOU 4656  CG2 THR D 475    20096  18280  21068  -1873  -1786    266       C
ATOM   4657  N   ARG D 476      24.851 -59.666  16.391  1.00139.60           N
ANISOU 4657  N   ARG D 476    18275  15867  18899  -2096  -2167    755       N
ATOM   4658  CA  ARG D 476      25.842 -58.835  17.102  1.00128.18           C
ANISOU 4658  CA  ARG D 476    16926  14319  17458  -2165  -2286    909       C
ATOM   4659  C   ARG D 476      26.237 -59.483  18.414  1.00101.94           C
ANISOU 4659  C   ARG D 476    13549  10980  14205  -2186  -2191    918       C
ATOM   4660  O   ARG D 476      27.359 -59.358  18.904  1.00110.29           O
ANISOU 4660  O   ARG D 476    14627  11991  15287  -2279  -2201   1071       O
ATOM   4661  CB  ARG D 476      25.335 -57.401  17.341  1.00102.75           C
ANISOU 4661  CB  ARG D 476    13861  10994  14185  -2104  -2511    888       C
ATOM   4662  CG  ARG D 476      23.809 -57.218  17.410  1.00105.11           C
ANISOU 4662  CG  ARG D 476    14178  11302  14459  -1965  -2551    688       C
ATOM   4663  CD  ARG D 476      23.454 -55.722  17.376  1.00161.32           C
ANISOU 4663  CD  ARG D 476    21456  18321  21517  -1920  -2781    694       C
ATOM   4664  NE  ARG D 476      24.136 -55.019  16.283  1.00214.30           N
ANISOU 4664  NE  ARG D 476    28222  25018  28182  -1997  -2879    830       N
ATOM   4665  CZ  ARG D 476      23.551 -54.167  15.440  1.00218.30           C
ANISOU 4665  CZ  ARG D 476    28801  25511  28630  -1955  -3008    799       C
ATOM   4666  NH1 ARG D 476      22.258 -53.889  15.554  1.00227.11           N
ANISOU 4666  NH1 ARG D 476    29947  26623  29722  -1836  -3054    636       N
ATOM   4667  NH2 ARG D 476      24.262 -53.588  14.476  1.00190.90           N
ANISOU 4667  NH2 ARG D 476    25370  22036  25126  -2033  -3090    935       N
ATOM   4668  N   CYS D 477      25.301 -60.259  18.917  1.00107.76           N
ANISOU 4668  N   CYS D 477    14203  11766  14975  -2101  -2086    755       N
ATOM   4669  CA  CYS D 477      25.314 -60.798  20.258  1.00113.13           C
ANISOU 4669  CA  CYS D 477    14834  12432  15718  -2086  -2012    717       C
ATOM   4670  C   CYS D 477      26.044 -62.144  20.284  1.00 93.50           C
ANISOU 4670  C   CYS D 477    12199  10028  13298  -2166  -1801    768       C
ATOM   4671  O   CYS D 477      25.977 -62.874  21.262  1.00144.79           O
ANISOU 4671  O   CYS D 477    18616  16542  19857  -2154  -1698    720       O
ATOM   4672  CB  CYS D 477      23.856 -60.913  20.774  1.00 92.01           C
ANISOU 4672  CB  CYS D 477    12143   9773  13044  -1944  -2015    514       C
ATOM   4673  SG  CYS D 477      22.803 -59.379  20.553  1.00144.19           S
ANISOU 4673  SG  CYS D 477    18920  16299  19567  -1832  -2252    433       S
ATOM   4674  N   ASN D 478      26.693 -62.504  19.189  1.00 86.27           N
ANISOU 4674  N   ASN D 478    11241   9169  12370  -2243  -1733    860       N
ATOM   4675  CA  ASN D 478      27.409 -63.779  19.147  1.00114.61           C
ANISOU 4675  CA  ASN D 478    14692  12836  16018  -2318  -1531    912       C
ATOM   4676  C   ASN D 478      28.937 -63.682  19.229  1.00118.00           C
ANISOU 4676  C   ASN D 478    15137  13235  16465  -2453  -1521   1130       C
ATOM   4677  O   ASN D 478      29.582 -63.072  18.375  1.00105.15           O
ANISOU 4677  O   ASN D 478    13573  11591  14789  -2512  -1599   1258       O
ATOM   4678  CB  ASN D 478      27.019 -64.589  17.895  1.00103.47           C
ANISOU 4678  CB  ASN D 478    13191  11532  14590  -2304  -1413    846       C
ATOM   4679  CG  ASN D 478      27.756 -65.937  17.804  1.00116.14           C
ANISOU 4679  CG  ASN D 478    14654  13219  16254  -2378  -1201    898       C
ATOM   4680  OD1 ASN D 478      28.870 -66.110  18.342  1.00 86.25           O
ANISOU 4680  OD1 ASN D 478    10852   9411  12508  -2472  -1155   1040       O
ATOM   4681  ND2 ASN D 478      27.136 -66.897  17.109  1.00 81.23           N
ANISOU 4681  ND2 ASN D 478    10132   8893  11838  -2338  -1072    785       N
ATOM   4682  N   LEU D 479      29.510 -64.294  20.261  1.00121.77           N
ANISOU 4682  N   LEU D 479    15550  13706  17011  -2501  -1423   1175       N
ATOM   4683  CA  LEU D 479      30.938 -64.627  20.278  1.00127.38           C
ANISOU 4683  CA  LEU D 479    16227  14420  17753  -2632  -1347   1371       C
ATOM   4684  C   LEU D 479      31.076 -65.984  20.947  1.00138.10           C
ANISOU 4684  C   LEU D 479    17433  15843  19194  -2652  -1141   1330       C
ATOM   4685  O   LEU D 479      30.586 -66.185  22.056  1.00187.51           O
ANISOU 4685  O   LEU D 479    23666  22081  25497  -2604  -1125   1237       O
ATOM   4686  CB  LEU D 479      31.763 -63.571  21.018  1.00 77.01           C
ANISOU 4686  CB  LEU D 479     9968   7925  11366  -2695  -1500   1524       C
ATOM   4687  CG  LEU D 479      31.009 -62.828  22.119  1.00102.67           C
ANISOU 4687  CG  LEU D 479    13306  11088  14614  -2612  -1634   1422       C
ATOM   4688  CD1 LEU D 479      31.857 -62.765  23.373  1.00121.69           C
ANISOU 4688  CD1 LEU D 479    15731  13430  17076  -2684  -1638   1533       C
ATOM   4689  CD2 LEU D 479      30.544 -61.427  21.679  1.00 87.46           C
ANISOU 4689  CD2 LEU D 479    11537   9085  12609  -2560  -1858   1412       C
ATOM   4690  N   GLY D 480      31.745 -66.918  20.284  1.00100.27           N
ANISOU 4690  N   GLY D 480    12542  11132  14424  -2721   -983   1402       N
ATOM   4691  CA  GLY D 480      31.770 -68.292  20.756  1.00106.44           C
ANISOU 4691  CA  GLY D 480    13170  11989  15285  -2733   -777   1347       C
ATOM   4692  C   GLY D 480      30.379 -68.878  20.970  1.00142.83           C
ANISOU 4692  C   GLY D 480    17708  16647  19914  -2613   -724   1120       C
ATOM   4693  O   GLY D 480      29.523 -68.782  20.086  1.00185.71           O
ANISOU 4693  O   GLY D 480    23154  22114  25296  -2540   -756   1011       O
ATOM   4694  N   GLY D 481      30.147 -69.459  22.151  1.00123.84           N
ANISOU 4694  N   GLY D 481    15227  14246  17581  -2594   -649   1053       N
ATOM   4695  CA  GLY D 481      28.976 -70.293  22.412  1.00156.77           C
ANISOU 4695  CA  GLY D 481    19295  18482  21789  -2495   -559    856       C
ATOM   4696  C   GLY D 481      27.582 -69.740  22.703  1.00139.71           C
ANISOU 4696  C   GLY D 481    17188  16299  19598  -2360   -675    683       C
ATOM   4697  O   GLY D 481      26.586 -70.202  22.130  1.00110.89           O
ANISOU 4697  O   GLY D 481    13485  12711  15935  -2280   -634    541       O
ATOM   4698  N   ALA D 482      27.486 -68.765  23.599  1.00142.93           N
ANISOU 4698  N   ALA D 482    17699  16615  19993  -2333   -819    695       N
ATOM   4699  CA  ALA D 482      26.170 -68.304  24.043  1.00156.64           C
ANISOU 4699  CA  ALA D 482    19478  18332  21707  -2199   -917    532       C
ATOM   4700  C   ALA D 482      25.537 -67.455  22.963  1.00131.58           C
ANISOU 4700  C   ALA D 482    16409  15142  18445  -2143  -1048    488       C
ATOM   4701  O   ALA D 482      26.229 -66.699  22.280  1.00184.05           O
ANISOU 4701  O   ALA D 482    23150  21743  25038  -2206  -1139    611       O
ATOM   4702  CB  ALA D 482      26.278 -67.518  25.350  1.00184.15           C
ANISOU 4702  CB  ALA D 482    23046  21721  25201  -2183  -1031    557       C
ATOM   4703  N   VAL D 483      24.229 -67.576  22.795  1.00 93.46           N
ANISOU 4703  N   VAL D 483    11559  10351  13599  -2026  -1059    320       N
ATOM   4704  CA  VAL D 483      23.546 -66.744  21.811  1.00110.85           C
ANISOU 4704  CA  VAL D 483    13861  12538  15719  -1967  -1187    272       C
ATOM   4705  C   VAL D 483      22.349 -65.974  22.363  1.00125.46           C
ANISOU 4705  C   VAL D 483    15789  14343  17537  -1838  -1320    144       C
ATOM   4706  O   VAL D 483      21.500 -66.523  23.091  1.00 71.66           O
ANISOU 4706  O   VAL D 483     8900   7564  10762  -1753  -1263     19       O
ATOM   4707  CB  VAL D 483      23.100 -67.551  20.591  1.00123.70           C
ANISOU 4707  CB  VAL D 483    15403  14263  17335  -1956  -1081    203       C
ATOM   4708  CG1 VAL D 483      22.374 -66.654  19.625  1.00139.20           C
ANISOU 4708  CG1 VAL D 483    17469  16208  19214  -1896  -1217    154       C
ATOM   4709  CG2 VAL D 483      24.289 -68.177  19.921  1.00118.31           C
ANISOU 4709  CG2 VAL D 483    14663  13621  16669  -2077   -966    337       C
ATOM   4710  N   CYS D 484      22.284 -64.712  21.944  1.00125.88           N
ANISOU 4710  N   CYS D 484    15990  14322  17516  -1823  -1496    180       N
ATOM   4711  CA  CYS D 484      21.321 -63.709  22.401  1.00 86.84           C
ANISOU 4711  CA  CYS D 484    11155   9313  12526  -1710  -1655     90       C
ATOM   4712  C   CYS D 484      19.907 -64.240  22.376  1.00 75.32           C
ANISOU 4712  C   CYS D 484     9623   7922  11071  -1586  -1604    -91       C
ATOM   4713  O   CYS D 484      19.479 -64.806  21.371  1.00159.19           O
ANISOU 4713  O   CYS D 484    20181  18621  21683  -1578  -1531   -145       O
ATOM   4714  CB  CYS D 484      21.429 -62.540  21.428  1.00133.25           C
ANISOU 4714  CB  CYS D 484    17169  15136  18323  -1726  -1814    151       C
ATOM   4715  SG  CYS D 484      22.671 -62.833  20.087  1.00 84.58           S
ANISOU 4715  SG  CYS D 484    10977   9013  12148  -1870  -1749    311       S
ATOM   4716  N   ARG D 485      19.165 -64.076  23.464  1.00115.55           N
ANISOU 4716  N   ARG D 485    14729  12994  16181  -1488  -1643   -182       N
ATOM   4717  CA  ARG D 485      17.893 -64.798  23.595  1.00141.51           C
ANISOU 4717  CA  ARG D 485    17919  16360  19489  -1375  -1567   -343       C
ATOM   4718  C   ARG D 485      16.927 -64.638  22.409  1.00134.87           C
ANISOU 4718  C   ARG D 485    17095  15559  18591  -1313  -1602   -429       C
ATOM   4719  O   ARG D 485      16.539 -65.632  21.800  1.00100.59           O
ANISOU 4719  O   ARG D 485    12638  11310  14274  -1310  -1477   -490       O
ATOM   4720  CB  ARG D 485      17.206 -64.468  24.923  1.00170.96           C
ANISOU 4720  CB  ARG D 485    21675  20051  23231  -1267  -1627   -421       C
ATOM   4721  CG  ARG D 485      16.485 -63.123  24.975  1.00201.26           C
ANISOU 4721  CG  ARG D 485    25670  23809  26990  -1171  -1819   -463       C
ATOM   4722  CD  ARG D 485      15.219 -63.263  25.806  1.00213.77           C
ANISOU 4722  CD  ARG D 485    27221  25419  28582  -1022  -1822   -604       C
ATOM   4723  NE  ARG D 485      14.616 -64.577  25.585  1.00217.12           N
ANISOU 4723  NE  ARG D 485    27476  25961  29059   -995  -1659   -693       N
ATOM   4724  CZ  ARG D 485      13.740 -65.153  26.402  1.00179.82           C
ANISOU 4724  CZ  ARG D 485    22663  21288  24374   -893  -1602   -797       C
ATOM   4725  NH1 ARG D 485      13.355 -64.527  27.506  1.00193.55           N
ANISOU 4725  NH1 ARG D 485    24467  22972  26100   -803  -1691   -830       N
ATOM   4726  NH2 ARG D 485      13.253 -66.358  26.119  1.00104.72           N
ANISOU 4726  NH2 ARG D 485    12997  11881  14912   -880  -1458   -867       N
ATOM   4727  N   HIS D 486      16.563 -63.397  22.076  1.00132.85           N
ANISOU 4727  N   HIS D 486    16982  15234  18260  -1269  -1772   -430       N
ATOM   4728  CA  HIS D 486      15.693 -63.121  20.930  1.00 92.66           C
ANISOU 4728  CA  HIS D 486    11919  10175  13111  -1217  -1819   -499       C
ATOM   4729  C   HIS D 486      16.286 -63.747  19.673  1.00 98.19           C
ANISOU 4729  C   HIS D 486    12557  10938  13812  -1317  -1723   -442       C
ATOM   4730  O   HIS D 486      15.628 -64.496  18.962  1.00 93.77           O
ANISOU 4730  O   HIS D 486    11912  10462  13256  -1289  -1634   -524       O
ATOM   4731  CB  HIS D 486      15.541 -61.610  20.735  1.00 92.83           C
ANISOU 4731  CB  HIS D 486    12114  10101  13056  -1185  -2022   -471       C
ATOM   4732  CG  HIS D 486      14.603 -61.221  19.635  1.00103.67           C
ANISOU 4732  CG  HIS D 486    13522  11499  14367  -1128  -2082   -543       C
ATOM   4733  ND1 HIS D 486      14.869 -60.192  18.758  1.00110.11           N
ANISOU 4733  ND1 HIS D 486    14454  12265  15120  -1164  -2213   -477       N
ATOM   4734  CD2 HIS D 486      13.388 -61.710  19.277  1.00132.41           C
ANISOU 4734  CD2 HIS D 486    17097  15211  18002  -1037  -2032   -673       C
ATOM   4735  CE1 HIS D 486      13.868 -60.067  17.902  1.00153.37           C
ANISOU 4735  CE1 HIS D 486    19935  17782  20555  -1101  -2238   -563       C
ATOM   4736  NE2 HIS D 486      12.955 -60.978  18.198  1.00159.26           N
ANISOU 4736  NE2 HIS D 486    20575  18601  21335  -1024  -2130   -682       N
ATOM   4737  N   HIS D 487      17.554 -63.451  19.420  1.00153.67           N
ANISOU 4737  N   HIS D 487    19626  17925  20835  -1433  -1741   -296       N
ATOM   4738  CA  HIS D 487      18.249 -63.952  18.238  1.00166.88           C
ANISOU 4738  CA  HIS D 487    21252  19653  22503  -1530  -1658   -222       C
ATOM   4739  C   HIS D 487      18.343 -65.488  18.214  1.00143.41           C
ANISOU 4739  C   HIS D 487    18113  16779  19598  -1558  -1452   -259       C
ATOM   4740  O   HIS D 487      18.257 -66.097  17.151  1.00155.70           O
ANISOU 4740  O   HIS D 487    19610  18406  21143  -1582  -1370   -277       O
ATOM   4741  CB  HIS D 487      19.609 -63.226  18.059  1.00 74.48           C
ANISOU 4741  CB  HIS D 487     9637   7883  10780  -1644  -1734    -43       C
ATOM   4742  CG  HIS D 487      19.450 -61.764  17.742  1.00120.37           C
ANISOU 4742  CG  HIS D 487    15605  13610  16519  -1620  -1937    -11       C
ATOM   4743  ND1 HIS D 487      20.312 -60.792  18.207  1.00130.47           N
ANISOU 4743  ND1 HIS D 487    16996  14792  17784  -1674  -2064    115       N
ATOM   4744  CD2 HIS D 487      18.501 -61.113  17.027  1.00119.64           C
ANISOU 4744  CD2 HIS D 487    15576  13516  16367  -1547  -2037    -89       C
ATOM   4745  CE1 HIS D 487      19.902 -59.608  17.789  1.00136.57           C
ANISOU 4745  CE1 HIS D 487    17893  15505  18491  -1633  -2235    111       C
ATOM   4746  NE2 HIS D 487      18.808 -59.771  17.067  1.00103.43           N
ANISOU 4746  NE2 HIS D 487    13668  11366  14265  -1557  -2220    -12       N
ATOM   4747  N   ALA D 488      18.466 -66.114  19.381  1.00112.27           N
ANISOU 4747  N   ALA D 488    14094  12840  15722  -1550  -1370   -276       N
ATOM   4748  CA  ALA D 488      18.520 -67.574  19.457  1.00115.70           C
ANISOU 4748  CA  ALA D 488    14367  13367  16228  -1573  -1177   -315       C
ATOM   4749  C   ALA D 488      17.204 -68.223  19.006  1.00128.13           C
ANISOU 4749  C   ALA D 488    15865  15019  17801  -1478  -1123   -471       C
ATOM   4750  O   ALA D 488      17.197 -69.264  18.333  1.00116.76           O
ANISOU 4750  O   ALA D 488    14320  13660  16385  -1506   -991   -497       O
ATOM   4751  CB  ALA D 488      18.880 -68.009  20.863  1.00130.87           C
ANISOU 4751  CB  ALA D 488    16228  15274  18223  -1581  -1116   -301       C
ATOM   4752  N   ASN D 489      16.095 -67.603  19.395  1.00113.74           N
ANISOU 4752  N   ASN D 489    14097  13170  15949  -1363  -1228   -570       N
ATOM   4753  CA  ASN D 489      14.782 -67.973  18.892  1.00111.50           C
ANISOU 4753  CA  ASN D 489    13766  12948  15649  -1268  -1211   -706       C
ATOM   4754  C   ASN D 489      14.749 -67.846  17.358  1.00132.33           C
ANISOU 4754  C   ASN D 489    16437  15614  18228  -1304  -1225   -694       C
ATOM   4755  O   ASN D 489      14.712 -68.855  16.638  1.00 87.77           O
ANISOU 4755  O   ASN D 489    10694  10049  12604  -1333  -1101   -722       O
ATOM   4756  CB  ASN D 489      13.704 -67.112  19.587  1.00113.88           C
ANISOU 4756  CB  ASN D 489    14146  13204  15919  -1142  -1343   -791       C
ATOM   4757  CG  ASN D 489      12.334 -67.213  18.935  1.00138.42           C
ANISOU 4757  CG  ASN D 489    17237  16363  18993  -1043  -1359   -915       C
ATOM   4758  OD1 ASN D 489      11.874 -66.264  18.290  1.00158.59           O
ANISOU 4758  OD1 ASN D 489    19898  18881  21476  -1009  -1483   -926       O
ATOM   4759  ND2 ASN D 489      11.664 -68.356  19.117  1.00105.18           N
ANISOU 4759  ND2 ASN D 489    12891  12235  14836   -998  -1238  -1005       N
ATOM   4760  N   GLU D 490      14.820 -66.611  16.862  1.00148.46           N
ANISOU 4760  N   GLU D 490    18617  17593  20199  -1306  -1376   -647       N
ATOM   4761  CA  GLU D 490      14.736 -66.345  15.426  1.00115.55           C
ANISOU 4761  CA  GLU D 490    14487  13446  15969  -1333  -1408   -635       C
ATOM   4762  C   GLU D 490      15.619 -67.282  14.587  1.00105.67           C
ANISOU 4762  C   GLU D 490    13153  12258  14737  -1437  -1270   -569       C
ATOM   4763  O   GLU D 490      15.201 -67.749  13.524  1.00 93.27           O
ANISOU 4763  O   GLU D 490    11544  10751  13144  -1434  -1219   -617       O
ATOM   4764  CB  GLU D 490      15.086 -64.878  15.137  1.00110.96           C
ANISOU 4764  CB  GLU D 490    14062  12778  15320  -1351  -1585   -552       C
ATOM   4765  CG  GLU D 490      14.028 -63.861  15.597  1.00156.68           C
ANISOU 4765  CG  GLU D 490    19949  18512  21071  -1238  -1735   -631       C
ATOM   4766  CD  GLU D 490      14.390 -62.418  15.223  1.00181.74           C
ANISOU 4766  CD  GLU D 490    23276  21600  24178  -1261  -1913   -548       C
ATOM   4767  OE1 GLU D 490      13.521 -61.518  15.346  1.00177.68           O
ANISOU 4767  OE1 GLU D 490    22850  21042  23620  -1173  -2043   -609       O
ATOM   4768  OE2 GLU D 490      15.548 -62.184  14.806  1.00181.75           O
ANISOU 4768  OE2 GLU D 490    23308  21578  24171  -1366  -1925   -417       O
ATOM   4769  N   TYR D 491      16.833 -67.560  15.054  1.00102.08           N
ANISOU 4769  N   TYR D 491    12674  11787  14325  -1527  -1208   -457       N
ATOM   4770  CA  TYR D 491      17.699 -68.493  14.336  1.00107.72           C
ANISOU 4770  CA  TYR D 491    13306  12562  15060  -1621  -1068   -390       C
ATOM   4771  C   TYR D 491      17.113 -69.885  14.322  1.00103.78           C
ANISOU 4771  C   TYR D 491    12664  12152  14613  -1590   -909   -497       C
ATOM   4772  O   TYR D 491      17.050 -70.526  13.261  1.00 71.40           O
ANISOU 4772  O   TYR D 491     8515   8116  10497  -1611   -831   -518       O
ATOM   4773  CB  TYR D 491      19.123 -68.527  14.915  1.00106.33           C
ANISOU 4773  CB  TYR D 491    13128  12350  14921  -1724  -1030   -241       C
ATOM   4774  CG  TYR D 491      19.967 -69.730  14.491  1.00 86.43           C
ANISOU 4774  CG  TYR D 491    10497   9901  12443  -1809   -853   -184       C
ATOM   4775  CD1 TYR D 491      19.792 -70.966  15.094  1.00 94.52           C
ANISOU 4775  CD1 TYR D 491    11388  10982  13543  -1798   -702   -250       C
ATOM   4776  CD2 TYR D 491      20.952 -69.624  13.506  1.00 89.77           C
ANISOU 4776  CD2 TYR D 491    10946  10334  12829  -1899   -839    -60       C
ATOM   4777  CE1 TYR D 491      20.562 -72.069  14.722  1.00100.20           C
ANISOU 4777  CE1 TYR D 491    12007  11763  14301  -1874   -540   -200       C
ATOM   4778  CE2 TYR D 491      21.730 -70.725  13.137  1.00109.36           C
ANISOU 4778  CE2 TYR D 491    13328  12879  15345  -1972   -674     -6       C
ATOM   4779  CZ  TYR D 491      21.532 -71.944  13.754  1.00 98.24           C
ANISOU 4779  CZ  TYR D 491    11791  11522  14012  -1959   -525    -78       C
ATOM   4780  OH  TYR D 491      22.296 -73.046  13.427  1.00 75.20           O
ANISOU 4780  OH  TYR D 491     8775   8665  11132  -2029   -361    -27       O
ATOM   4781  N   ARG D 492      16.705 -70.357  15.500  1.00113.41           N
ANISOU 4781  N   ARG D 492    13817  13376  15897  -1539   -864   -562       N
ATOM   4782  CA  ARG D 492      16.168 -71.711  15.615  1.00127.60           C
ANISOU 4782  CA  ARG D 492    15471  15257  17756  -1510   -715   -660       C
ATOM   4783  C   ARG D 492      14.871 -71.877  14.801  1.00108.87           C
ANISOU 4783  C   ARG D 492    13086  12933  15345  -1427   -733   -787       C
ATOM   4784  O   ARG D 492      14.658 -72.911  14.143  1.00 75.42           O
ANISOU 4784  O   ARG D 492     8758   8770  11127  -1437   -619   -837       O
ATOM   4785  CB  ARG D 492      15.963 -72.087  17.076  1.00114.82           C
ANISOU 4785  CB  ARG D 492    13784  13632  16211  -1468   -677   -699       C
ATOM   4786  CG  ARG D 492      15.971 -73.580  17.305  1.00117.66           C
ANISOU 4786  CG  ARG D 492    13981  14072  16651  -1483   -501   -744       C
ATOM   4787  CD  ARG D 492      17.295 -74.031  17.863  1.00112.70           C
ANISOU 4787  CD  ARG D 492    13305  13436  16081  -1586   -405   -629       C
ATOM   4788  NE  ARG D 492      17.468 -73.620  19.252  1.00119.64           N
ANISOU 4788  NE  ARG D 492    14198  14262  16999  -1569   -449   -605       N
ATOM   4789  CZ  ARG D 492      18.334 -74.188  20.087  1.00137.38           C
ANISOU 4789  CZ  ARG D 492    16370  16511  19317  -1635   -353   -537       C
ATOM   4790  NH1 ARG D 492      19.105 -75.187  19.660  1.00132.34           N
ANISOU 4790  NH1 ARG D 492    15639  15925  18719  -1720   -207   -485       N
ATOM   4791  NH2 ARG D 492      18.431 -73.758  21.344  1.00 96.84           N
ANISOU 4791  NH2 ARG D 492    11255  11326  14213  -1614   -403   -520       N
ATOM   4792  N   GLN D 493      14.026 -70.845  14.837  1.00 78.36           N
ANISOU 4792  N   GLN D 493     9320   9025  11429  -1347   -879   -836       N
ATOM   4793  CA  GLN D 493      12.862 -70.780  13.962  1.00109.19           C
ANISOU 4793  CA  GLN D 493    13237  12965  15286  -1277   -918   -937       C
ATOM   4794  C   GLN D 493      13.306 -70.855  12.504  1.00109.38           C
ANISOU 4794  C   GLN D 493    13282  13018  15260  -1348   -896   -891       C
ATOM   4795  O   GLN D 493      12.847 -71.717  11.742  1.00109.19           O
ANISOU 4795  O   GLN D 493    13186  13064  15238  -1341   -810   -956       O
ATOM   4796  CB  GLN D 493      12.037 -69.508  14.226  1.00101.22           C
ANISOU 4796  CB  GLN D 493    12344  11894  14222  -1190  -1088   -974       C
ATOM   4797  CG  GLN D 493      10.889 -69.722  15.219  1.00129.43           C
ANISOU 4797  CG  GLN D 493    15870  15480  17829  -1074  -1095  -1085       C
ATOM   4798  CD  GLN D 493       9.987 -68.508  15.361  1.00138.16           C
ANISOU 4798  CD  GLN D 493    17090  16531  18874   -979  -1257  -1128       C
ATOM   4799  OE1 GLN D 493       9.902 -67.678  14.457  1.00147.68           O
ANISOU 4799  OE1 GLN D 493    18392  17709  20010   -989  -1353  -1107       O
ATOM   4800  NE2 GLN D 493       9.312 -68.397  16.502  1.00123.65           N
ANISOU 4800  NE2 GLN D 493    15241  14679  17063   -885  -1287  -1187       N
ATOM   4801  N   TYR D 494      14.217 -69.963  12.126  1.00 95.21           N
ANISOU 4801  N   TYR D 494    11585  11171  13419  -1415   -975   -775       N
ATOM   4802  CA  TYR D 494      14.708 -69.918  10.760  1.00105.83           C
ANISOU 4802  CA  TYR D 494    12956  12541  14711  -1481   -965   -717       C
ATOM   4803  C   TYR D 494      15.202 -71.279  10.287  1.00102.52           C
ANISOU 4803  C   TYR D 494    12422  12200  14332  -1538   -790   -712       C
ATOM   4804  O   TYR D 494      14.819 -71.755   9.216  1.00 88.18           O
ANISOU 4804  O   TYR D 494    10579  10440  12487  -1536   -745   -761       O
ATOM   4805  CB  TYR D 494      15.827 -68.891  10.626  1.00 97.02           C
ANISOU 4805  CB  TYR D 494    11944  11361  13559  -1556  -1059   -570       C
ATOM   4806  CG  TYR D 494      16.406 -68.853   9.242  1.00 99.06           C
ANISOU 4806  CG  TYR D 494    12224  11652  13764  -1624  -1047   -499       C
ATOM   4807  CD1 TYR D 494      17.577 -69.528   8.944  1.00 74.76           C
ANISOU 4807  CD1 TYR D 494     9093   8605  10707  -1717   -932   -398       C
ATOM   4808  CD2 TYR D 494      15.762 -68.161   8.220  1.00113.19           C
ANISOU 4808  CD2 TYR D 494    14083  13444  15482  -1594  -1146   -533       C
ATOM   4809  CE1 TYR D 494      18.103 -69.508   7.657  1.00135.03           C
ANISOU 4809  CE1 TYR D 494    16744  16274  18288  -1773   -918   -331       C
ATOM   4810  CE2 TYR D 494      16.281 -68.129   6.929  1.00 83.00           C
ANISOU 4810  CE2 TYR D 494    10275   9654  11607  -1653  -1134   -468       C
ATOM   4811  CZ  TYR D 494      17.449 -68.808   6.657  1.00130.80           C
ANISOU 4811  CZ  TYR D 494    16276  15741  17680  -1741  -1020   -368       C
ATOM   4812  OH  TYR D 494      17.971 -68.783   5.391  1.00118.17           O
ANISOU 4812  OH  TYR D 494    14691  14180  16028  -1794  -1007   -300       O
ATOM   4813  N   LEU D 495      16.065 -71.899  11.082  1.00 75.26           N
ANISOU 4813  N   LEU D 495     8904   8748  10945  -1591   -692   -652       N
ATOM   4814  CA  LEU D 495      16.679 -73.154  10.667  1.00104.73           C
ANISOU 4814  CA  LEU D 495    12531  12548  14715  -1653   -524   -632       C
ATOM   4815  C   LEU D 495      15.625 -74.182  10.242  1.00108.78           C
ANISOU 4815  C   LEU D 495    12954  13134  15245  -1594   -440   -771       C
ATOM   4816  O   LEU D 495      15.829 -74.944   9.289  1.00 94.66           O
ANISOU 4816  O   LEU D 495    11119  11402  13444  -1630   -346   -774       O
ATOM   4817  CB  LEU D 495      17.621 -73.709  11.752  1.00105.18           C
ANISOU 4817  CB  LEU D 495    12520  12595  14850  -1708   -429   -559       C
ATOM   4818  CG  LEU D 495      18.130 -75.141  11.508  1.00104.40           C
ANISOU 4818  CG  LEU D 495    12295  12569  14804  -1760   -243   -556       C
ATOM   4819  CD1 LEU D 495      18.491 -75.399  10.054  1.00 86.86           C
ANISOU 4819  CD1 LEU D 495    10085  10391  12526  -1805   -200   -522       C
ATOM   4820  CD2 LEU D 495      19.299 -75.479  12.398  1.00 74.98           C
ANISOU 4820  CD2 LEU D 495     8522   8825  11141  -1836   -162   -448       C
ATOM   4821  N   ASP D 496      14.493 -74.192  10.937  1.00114.40           N
ANISOU 4821  N   ASP D 496    13641  13844  15981  -1502   -477   -882       N
ATOM   4822  CA  ASP D 496      13.420 -75.119  10.597  1.00125.17           C
ANISOU 4822  CA  ASP D 496    14922  15275  17364  -1442   -411  -1010       C
ATOM   4823  C   ASP D 496      12.857 -74.819   9.223  1.00121.64           C
ANISOU 4823  C   ASP D 496    14532  14848  16837  -1428   -464  -1047       C
ATOM   4824  O   ASP D 496      12.721 -75.713   8.387  1.00115.64           O
ANISOU 4824  O   ASP D 496    13714  14149  16076  -1443   -373  -1087       O
ATOM   4825  CB  ASP D 496      12.303 -75.055  11.631  1.00118.84           C
ANISOU 4825  CB  ASP D 496    14092  14466  16598  -1341   -457  -1109       C
ATOM   4826  CG  ASP D 496      12.484 -76.071  12.730  1.00133.57           C
ANISOU 4826  CG  ASP D 496    15833  16359  18560  -1342   -340  -1127       C
ATOM   4827  OD1 ASP D 496      13.096 -77.130  12.459  1.00138.88           O
ANISOU 4827  OD1 ASP D 496    16416  17078  19273  -1404   -204  -1106       O
ATOM   4828  OD2 ASP D 496      12.015 -75.811  13.860  1.00139.08           O
ANISOU 4828  OD2 ASP D 496    16520  17033  19292  -1279   -384  -1161       O
ATOM   4829  N   ALA D 497      12.528 -73.551   8.999  1.00107.69           N
ANISOU 4829  N   ALA D 497    12881  13030  15006  -1398   -614  -1033       N
ATOM   4830  CA  ALA D 497      12.003 -73.118   7.715  1.00108.81           C
ANISOU 4830  CA  ALA D 497    13085  13188  15070  -1386   -679  -1061       C
ATOM   4831  C   ALA D 497      12.957 -73.526   6.610  1.00121.74           C
ANISOU 4831  C   ALA D 497    14717  14861  16680  -1475   -603   -986       C
ATOM   4832  O   ALA D 497      12.536 -74.054   5.580  1.00118.40           O
ANISOU 4832  O   ALA D 497    14270  14491  16228  -1472   -559  -1040       O
ATOM   4833  CB  ALA D 497      11.803 -71.614   7.707  1.00121.94           C
ANISOU 4833  CB  ALA D 497    14877  14782  16672  -1360   -851  -1028       C
ATOM   4834  N   TYR D 498      14.245 -73.272   6.831  1.00126.83           N
ANISOU 4834  N   TYR D 498    15383  15475  17330  -1553   -588   -858       N
ATOM   4835  CA  TYR D 498      15.263 -73.585   5.840  1.00123.50           C
ANISOU 4835  CA  TYR D 498    14960  15085  16879  -1637   -519   -768       C
ATOM   4836  C   TYR D 498      15.252 -75.080   5.584  1.00108.10           C
ANISOU 4836  C   TYR D 498    12892  13208  14972  -1648   -351   -824       C
ATOM   4837  O   TYR D 498      15.016 -75.521   4.459  1.00108.73           O
ANISOU 4837  O   TYR D 498    12962  13337  15012  -1652   -311   -860       O
ATOM   4838  CB  TYR D 498      16.646 -73.114   6.316  1.00140.95           C
ANISOU 4838  CB  TYR D 498    17205  17251  19101  -1716   -527   -614       C
ATOM   4839  CG  TYR D 498      17.821 -73.586   5.468  1.00121.90           C
ANISOU 4839  CG  TYR D 498    14772  14876  16669  -1803   -433   -506       C
ATOM   4840  CD1 TYR D 498      18.448 -74.799   5.732  1.00107.77           C
ANISOU 4840  CD1 TYR D 498    12880  13129  14938  -1845   -270   -488       C
ATOM   4841  CD2 TYR D 498      18.314 -72.812   4.425  1.00 78.87           C
ANISOU 4841  CD2 TYR D 498     9403   9421  11143  -1843   -507   -417       C
ATOM   4842  CE1 TYR D 498      19.523 -75.239   4.976  1.00115.99           C
ANISOU 4842  CE1 TYR D 498    13904  14206  15960  -1920   -179   -386       C
ATOM   4843  CE2 TYR D 498      19.389 -73.248   3.656  1.00130.59           C
ANISOU 4843  CE2 TYR D 498    15933  16011  17673  -1917   -419   -313       C
ATOM   4844  CZ  TYR D 498      19.994 -74.465   3.938  1.00128.42           C
ANISOU 4844  CZ  TYR D 498    15561  15778  17456  -1954   -253   -297       C
ATOM   4845  OH  TYR D 498      21.071 -74.916   3.187  1.00101.97           O
ANISOU 4845  OH  TYR D 498    12191  12469  14084  -2022   -161   -190       O
ATOM   4846  N   ASN D 499      15.460 -75.850   6.646  1.00 96.84           N
ANISOU 4846  N   ASN D 499    11378  11787  13628  -1651   -258   -835       N
ATOM   4847  CA  ASN D 499      15.498 -77.302   6.559  1.00113.17           C
ANISOU 4847  CA  ASN D 499    13329  13920  15750  -1663    -97   -885       C
ATOM   4848  C   ASN D 499      14.292 -77.920   5.848  1.00127.49           C
ANISOU 4848  C   ASN D 499    15107  15785  17549  -1602    -79  -1020       C
ATOM   4849  O   ASN D 499      14.393 -79.000   5.261  1.00127.16           O
ANISOU 4849  O   ASN D 499    14996  15799  17520  -1622     38  -1051       O
ATOM   4850  CB  ASN D 499      15.616 -77.896   7.957  1.00116.63           C
ANISOU 4850  CB  ASN D 499    13678  14351  16283  -1656    -27   -897       C
ATOM   4851  CG  ASN D 499      16.961 -78.481   8.211  1.00125.70           C
ANISOU 4851  CG  ASN D 499    14776  15509  17475  -1744     91   -788       C
ATOM   4852  OD1 ASN D 499      17.659 -78.078   9.145  1.00137.46           O
ANISOU 4852  OD1 ASN D 499    16277  16955  18998  -1777     75   -704       O
ATOM   4853  ND2 ASN D 499      17.351 -79.447   7.377  1.00142.10           N
ANISOU 4853  ND2 ASN D 499    16799  17643  19549  -1783    212   -784       N
ATOM   4854  N   MET D 500      13.145 -77.255   5.927  1.00115.77           N
ANISOU 4854  N   MET D 500    13668  14280  16038  -1526   -195  -1100       N
ATOM   4855  CA  MET D 500      11.969 -77.724   5.219  1.00116.77           C
ANISOU 4855  CA  MET D 500    13772  14452  16144  -1469   -193  -1219       C
ATOM   4856  C   MET D 500      12.126 -77.536   3.706  1.00136.84           C
ANISOU 4856  C   MET D 500    16373  17017  18602  -1503   -208  -1198       C
ATOM   4857  O   MET D 500      11.945 -78.487   2.942  1.00143.66           O
ANISOU 4857  O   MET D 500    17186  17935  19463  -1510   -120  -1249       O
ATOM   4858  CB  MET D 500      10.702 -77.045   5.743  1.00120.55           C
ANISOU 4858  CB  MET D 500    14282  14903  16617  -1377   -312  -1301       C
ATOM   4859  CG  MET D 500       9.490 -77.238   4.840  1.00149.17           C
ANISOU 4859  CG  MET D 500    17911  18566  20202  -1323   -341  -1405       C
ATOM   4860  SD  MET D 500       7.908 -77.282   5.709  1.00160.07           S
ANISOU 4860  SD  MET D 500    19250  19948  21620  -1208   -397  -1525       S
ATOM   4861  CE  MET D 500       8.164 -76.029   6.983  1.00146.13           C
ANISOU 4861  CE  MET D 500    17554  18106  19863  -1180   -509  -1466       C
ATOM   4862  N   MET D 501      12.470 -76.320   3.276  1.00142.40           N
ANISOU 4862  N   MET D 501    17184  17681  19240  -1523   -321  -1123       N
ATOM   4863  CA  MET D 501      12.729 -76.051   1.858  1.00134.92           C
ANISOU 4863  CA  MET D 501    16294  16756  18212  -1559   -341  -1088       C
ATOM   4864  C   MET D 501      13.843 -76.939   1.299  1.00118.49           C
ANISOU 4864  C   MET D 501    14166  14719  16135  -1632   -205  -1020       C
ATOM   4865  O   MET D 501      13.908 -77.204   0.103  1.00119.12           O
ANISOU 4865  O   MET D 501    14259  14840  16161  -1652   -175  -1023       O
ATOM   4866  CB  MET D 501      13.094 -74.585   1.639  1.00113.27           C
ANISOU 4866  CB  MET D 501    13667  13962  15409  -1577   -483   -998       C
ATOM   4867  CG  MET D 501      14.153 -74.400   0.572  1.00120.69           C
ANISOU 4867  CG  MET D 501    14645  14920  16291  -1652   -466   -888       C
ATOM   4868  SD  MET D 501      15.028 -72.821   0.673  1.00160.01           S
ANISOU 4868  SD  MET D 501    19738  19832  21228  -1695   -611   -740       S
ATOM   4869  CE  MET D 501      13.649 -71.695   0.288  1.00 62.30           C
ANISOU 4869  CE  MET D 501     7447   7428   8795  -1620   -782   -827       C
ATOM   4870  N   ILE D 502      14.733 -77.381   2.172  1.00123.11           N
ANISOU 4870  N   ILE D 502    14699  15295  16784  -1672   -122   -955       N
ATOM   4871  CA  ILE D 502      15.794 -78.292   1.777  1.00133.75           C
ANISOU 4871  CA  ILE D 502    15993  16683  18143  -1738     18   -889       C
ATOM   4872  C   ILE D 502      15.184 -79.661   1.540  1.00133.63           C
ANISOU 4872  C   ILE D 502    15884  16725  18163  -1711    136  -1003       C
ATOM   4873  O   ILE D 502      15.492 -80.325   0.545  1.00146.83           O
ANISOU 4873  O   ILE D 502    17541  18445  19804  -1737    217  -1001       O
ATOM   4874  CB  ILE D 502      16.917 -78.353   2.848  1.00135.76           C
ANISOU 4874  CB  ILE D 502    16215  16908  18459  -1792     72   -782       C
ATOM   4875  CG1 ILE D 502      17.984 -77.301   2.540  1.00118.36           C
ANISOU 4875  CG1 ILE D 502    14101  14669  16203  -1852     -1   -629       C
ATOM   4876  CG2 ILE D 502      17.543 -79.751   2.918  1.00110.55           C
ANISOU 4876  CG2 ILE D 502    12918  13764  15321  -1830    249   -775       C
ATOM   4877  CD1 ILE D 502      17.413 -75.971   2.037  1.00104.70           C
ANISOU 4877  CD1 ILE D 502    12480  12903  14400  -1821   -172   -632       C
ATOM   4878  N   SER D 503      14.296 -80.063   2.446  1.00130.71           N
ANISOU 4878  N   SER D 503    15453  16352  17858  -1655    140  -1101       N
ATOM   4879  CA  SER D 503      13.621 -81.349   2.336  1.00105.50           C
ANISOU 4879  CA  SER D 503    12167  13211  14709  -1624    239  -1212       C
ATOM   4880  C   SER D 503      12.584 -81.323   1.211  1.00117.48           C
ANISOU 4880  C   SER D 503    13721  14754  16161  -1582    187  -1303       C
ATOM   4881  O   SER D 503      12.251 -82.360   0.644  1.00120.47           O
ANISOU 4881  O   SER D 503    14047  15180  16547  -1575    270  -1373       O
ATOM   4882  CB  SER D 503      12.982 -81.734   3.662  1.00105.97           C
ANISOU 4882  CB  SER D 503    12147  13261  14857  -1576    250  -1279       C
ATOM   4883  OG  SER D 503      12.350 -82.995   3.564  1.00159.04           O
ANISOU 4883  OG  SER D 503    18772  20031  21624  -1549    343  -1380       O
ATOM   4884  N   ALA D 504      12.083 -80.131   0.895  1.00118.43           N
ANISOU 4884  N   ALA D 504    13936  14842  16219  -1555     47  -1300       N
ATOM   4885  CA  ALA D 504      11.207 -79.926  -0.259  1.00 93.92           C
ANISOU 4885  CA  ALA D 504    10881  11760  13044  -1524    -14  -1368       C
ATOM   4886  C   ALA D 504      11.973 -79.976  -1.569  1.00121.93           C
ANISOU 4886  C   ALA D 504    14470  15337  16520  -1580     22  -1307       C
ATOM   4887  O   ALA D 504      11.384 -79.809  -2.631  1.00152.49           O
ANISOU 4887  O   ALA D 504    18385  19229  20326  -1565    -22  -1352       O
ATOM   4888  CB  ALA D 504      10.459 -78.615  -0.150  1.00103.78           C
ANISOU 4888  CB  ALA D 504    12214  12965  14252  -1479   -174  -1379       C
ATOM   4889  N   GLY D 505      13.293 -80.129  -1.488  1.00147.33           N
ANISOU 4889  N   GLY D 505    17679  18555  19746  -1644     96  -1198       N
ATOM   4890  CA  GLY D 505      14.107 -80.381  -2.665  1.00168.57           C
ANISOU 4890  CA  GLY D 505    20391  21283  22375  -1694    156  -1135       C
ATOM   4891  C   GLY D 505      14.781 -79.192  -3.335  1.00167.17           C
ANISOU 4891  C   GLY D 505    20310  21088  22120  -1731     64  -1022       C
ATOM   4892  O   GLY D 505      15.470 -79.364  -4.345  1.00173.34           O
ANISOU 4892  O   GLY D 505    21109  21904  22846  -1770    111   -963       O
ATOM   4893  N   PHE D 506      14.590 -77.989  -2.801  1.00141.90           N
ANISOU 4893  N   PHE D 506    17170  17834  18913  -1718    -68   -989       N
ATOM   4894  CA  PHE D 506      15.283 -76.821  -3.345  1.00144.06           C
ANISOU 4894  CA  PHE D 506    17532  18086  19120  -1756   -163   -871       C
ATOM   4895  C   PHE D 506      16.738 -76.760  -2.859  1.00151.55           C
ANISOU 4895  C   PHE D 506    18472  19018  20092  -1823   -112   -723       C
ATOM   4896  O   PHE D 506      17.064 -77.243  -1.767  1.00125.90           O
ANISOU 4896  O   PHE D 506    15165  15751  16918  -1831    -46   -713       O
ATOM   4897  CB  PHE D 506      14.581 -75.521  -2.959  1.00118.59           C
ANISOU 4897  CB  PHE D 506    14378  14803  15877  -1719   -329   -884       C
ATOM   4898  CG  PHE D 506      13.172 -75.406  -3.457  1.00122.86           C
ANISOU 4898  CG  PHE D 506    14937  15356  16388  -1656   -395  -1012       C
ATOM   4899  CD1 PHE D 506      12.211 -76.327  -3.080  1.00121.95           C
ANISOU 4899  CD1 PHE D 506    14754  15261  16321  -1605   -336  -1138       C
ATOM   4900  CD2 PHE D 506      12.792 -74.338  -4.264  1.00138.97           C
ANISOU 4900  CD2 PHE D 506    17061  17386  18355  -1648   -522  -1000       C
ATOM   4901  CE1 PHE D 506      10.908 -76.201  -3.519  1.00134.45           C
ANISOU 4901  CE1 PHE D 506    16353  16854  17877  -1548   -399  -1246       C
ATOM   4902  CE2 PHE D 506      11.474 -74.208  -4.710  1.00108.59           C
ANISOU 4902  CE2 PHE D 506    13230  13549  14482  -1592   -583  -1112       C
ATOM   4903  CZ  PHE D 506      10.541 -75.136  -4.338  1.00104.08           C
ANISOU 4903  CZ  PHE D 506    12593  12997  13957  -1543   -522  -1233       C
ATOM   4904  N   SER D 507      17.599 -76.141  -3.667  1.00155.97           N
ANISOU 4904  N   SER D 507    19088  19587  20588  -1870   -146   -604       N
ATOM   4905  CA  SER D 507      19.006 -75.958  -3.319  1.00147.93           C
ANISOU 4905  CA  SER D 507    18071  18553  19582  -1936   -113   -445       C
ATOM   4906  C   SER D 507      19.445 -74.526  -3.630  1.00132.24           C
ANISOU 4906  C   SER D 507    16179  16530  17539  -1962   -260   -328       C
ATOM   4907  O   SER D 507      18.808 -73.840  -4.445  1.00108.90           O
ANISOU 4907  O   SER D 507    13279  13578  14520  -1937   -362   -364       O
ATOM   4908  CB  SER D 507      19.867 -76.955  -4.090  1.00138.10           C
ANISOU 4908  CB  SER D 507    16780  17373  18320  -1976     34   -393       C
ATOM   4909  OG  SER D 507      19.056 -77.785  -4.908  1.00144.61           O
ANISOU 4909  OG  SER D 507    17576  18250  19121  -1937     94   -520       O
ATOM   4910  N   LEU D 508      20.522 -74.070  -2.989  1.00 98.77           N
ANISOU 4910  N   LEU D 508    11954  12253  13321  -2015   -276   -187       N
ATOM   4911  CA  LEU D 508      21.012 -72.716  -3.251  1.00109.34           C
ANISOU 4911  CA  LEU D 508    13381  13554  14610  -2044   -421    -64       C
ATOM   4912  C   LEU D 508      22.354 -72.655  -3.996  1.00148.84           C
ANISOU 4912  C   LEU D 508    18392  18591  19570  -2112   -382    105       C
ATOM   4913  O   LEU D 508      23.328 -73.342  -3.638  1.00127.86           O
ANISOU 4913  O   LEU D 508    15684  15949  16948  -2157   -265    190       O
ATOM   4914  CB  LEU D 508      21.123 -71.895  -1.964  1.00141.22           C
ANISOU 4914  CB  LEU D 508    17455  17508  18695  -2048   -519    -21       C
ATOM   4915  CG  LEU D 508      19.938 -71.612  -1.038  1.00153.88           C
ANISOU 4915  CG  LEU D 508    19068  19061  20337  -1981   -593   -153       C
ATOM   4916  CD1 LEU D 508      18.644 -71.134  -1.798  1.00 61.91           C
ANISOU 4916  CD1 LEU D 508     7464   7422   8637  -1918   -690   -273       C
ATOM   4917  CD2 LEU D 508      19.689 -72.843  -0.178  1.00142.83           C
ANISOU 4917  CD2 LEU D 508    17574  17678  19017  -1961   -453   -241       C
ATOM   4918  N   TRP D 509      22.386 -71.821  -5.035  1.00161.87           N
ANISOU 4918  N   TRP D 509    20104  20257  21144  -2118   -482    157       N
ATOM   4919  CA  TRP D 509      23.619 -71.515  -5.758  1.00155.74           C
ANISOU 4919  CA  TRP D 509    19346  19510  20320  -2177   -480    332       C
ATOM   4920  C   TRP D 509      23.826 -70.004  -5.788  1.00144.57           C
ANISOU 4920  C   TRP D 509    18016  18042  18871  -2197   -665    436       C
ATOM   4921  O   TRP D 509      22.882 -69.231  -6.070  1.00 86.60           O
ANISOU 4921  O   TRP D 509    10727  10679  11500  -2157   -791    357       O
ATOM   4922  CB  TRP D 509      23.592 -72.092  -7.179  1.00137.72           C
ANISOU 4922  CB  TRP D 509    17044  17313  17970  -2169   -405    310       C
ATOM   4923  CG  TRP D 509      23.402 -73.576  -7.201  1.00153.98           C
ANISOU 4923  CG  TRP D 509    19024  19422  20059  -2149   -228    209       C
ATOM   4924  CD1 TRP D 509      22.218 -74.253  -7.308  1.00161.36           C
ANISOU 4924  CD1 TRP D 509    19931  20374  21006  -2093   -189     28       C
ATOM   4925  CD2 TRP D 509      24.426 -74.575  -7.093  1.00163.21           C
ANISOU 4925  CD2 TRP D 509    20131  20628  21252  -2187    -69    287       C
ATOM   4926  NE1 TRP D 509      22.446 -75.611  -7.275  1.00170.42           N
ANISOU 4926  NE1 TRP D 509    21003  21565  22184  -2094    -19    -14       N
ATOM   4927  CE2 TRP D 509      23.789 -75.833  -7.146  1.00181.46           C
ANISOU 4927  CE2 TRP D 509    22380  22977  23590  -2150     60    141       C
ATOM   4928  CE3 TRP D 509      25.812 -74.527  -6.959  1.00136.65           C
ANISOU 4928  CE3 TRP D 509    16759  17270  17890  -2248    -24    470       C
ATOM   4929  CZ2 TRP D 509      24.501 -77.031  -7.071  1.00169.54           C
ANISOU 4929  CZ2 TRP D 509    20800  21507  22109  -2171    231    168       C
ATOM   4930  CZ3 TRP D 509      26.511 -75.716  -6.887  1.00126.21           C
ANISOU 4930  CZ3 TRP D 509    15367  15990  16595  -2269    150    499       C
ATOM   4931  CH2 TRP D 509      25.858 -76.950  -6.945  1.00127.36           C
ANISOU 4931  CH2 TRP D 509    15453  16171  16768  -2230    276    347       C
ATOM   4932  N   ILE D 510      25.053 -69.590  -5.470  1.00126.99           N
ANISOU 4932  N   ILE D 510    15805  15793  16652  -2259   -684    616       N
ATOM   4933  CA  ILE D 510      25.384 -68.176  -5.355  1.00106.44           C
ANISOU 4933  CA  ILE D 510    13283  13133  14028  -2285   -862    732       C
ATOM   4934  C   ILE D 510      26.804 -67.934  -5.840  1.00117.34           C
ANISOU 4934  C   ILE D 510    14667  14539  15377  -2355   -855    945       C
ATOM   4935  O   ILE D 510      27.582 -68.884  -5.976  1.00111.18           O
ANISOU 4935  O   ILE D 510    13826  13810  14605  -2384   -704   1006       O
ATOM   4936  CB  ILE D 510      25.291 -67.728  -3.900  1.00119.59           C
ANISOU 4936  CB  ILE D 510    14974  14705  15759  -2285   -929    728       C
ATOM   4937  CG1 ILE D 510      25.257 -66.201  -3.797  1.00115.73           C
ANISOU 4937  CG1 ILE D 510    14580  14147  15245  -2293  -1136    799       C
ATOM   4938  CG2 ILE D 510      26.446 -68.310  -3.101  1.00 91.98           C
ANISOU 4938  CG2 ILE D 510    11433  11200  12316  -2343   -822    847       C
ATOM   4939  CD1 ILE D 510      24.969 -65.699  -2.392  1.00 87.15           C
ANISOU 4939  CD1 ILE D 510    10999  10433  11684  -2278  -1217    769       C
ATOM   4940  N   TYR D 511      27.140 -66.665  -6.070  1.00130.81           N
ANISOU 4940  N   TYR D 511    16443  16210  17048  -2380  -1019   1063       N
ATOM   4941  CA  TYR D 511      28.456 -66.288  -6.587  1.00153.15           C
ANISOU 4941  CA  TYR D 511    19281  19066  19844  -2445  -1037   1279       C
ATOM   4942  C   TYR D 511      29.608 -66.688  -5.673  1.00144.92           C
ANISOU 4942  C   TYR D 511    18209  17999  18854  -2504   -957   1416       C
ATOM   4943  O   TYR D 511      29.440 -66.744  -4.455  1.00144.53           O
ANISOU 4943  O   TYR D 511    18163  17882  18871  -2504   -958   1374       O
ATOM   4944  CB  TYR D 511      28.513 -64.792  -6.884  1.00153.36           C
ANISOU 4944  CB  TYR D 511    19390  19049  19832  -2460  -1246   1373       C
ATOM   4945  CG  TYR D 511      28.102 -63.902  -5.734  1.00117.87           C
ANISOU 4945  CG  TYR D 511    14959  14446  15382  -2453  -1387   1346       C
ATOM   4946  CD1 TYR D 511      28.921 -63.743  -4.633  1.00118.96           C
ANISOU 4946  CD1 TYR D 511    15108  14519  15571  -2501  -1399   1460       C
ATOM   4947  CD2 TYR D 511      26.905 -63.190  -5.769  1.00111.51           C
ANISOU 4947  CD2 TYR D 511    14204  13601  14562  -2398  -1512   1211       C
ATOM   4948  CE1 TYR D 511      28.558 -62.913  -3.585  1.00144.60           C
ANISOU 4948  CE1 TYR D 511    18420  17665  18855  -2491  -1531   1435       C
ATOM   4949  CE2 TYR D 511      26.538 -62.358  -4.732  1.00125.77           C
ANISOU 4949  CE2 TYR D 511    16074  15309  16404  -2386  -1643   1187       C
ATOM   4950  CZ  TYR D 511      27.367 -62.228  -3.637  1.00143.07           C
ANISOU 4950  CZ  TYR D 511    18278  17436  18645  -2431  -1652   1297       C
ATOM   4951  OH  TYR D 511      27.014 -61.410  -2.584  1.00128.61           O
ANISOU 4951  OH  TYR D 511    16516  15505  16847  -2416  -1782   1273       O
ATOM   4952  N   LYS D 512      30.774 -66.953  -6.269  1.00141.51           N
ANISOU 4952  N   LYS D 512    17750  17625  18395  -2553   -887   1585       N
ATOM   4953  CA  LYS D 512      31.899 -67.534  -5.532  1.00147.97           C
ANISOU 4953  CA  LYS D 512    18526  18436  19260  -2610   -778   1717       C
ATOM   4954  C   LYS D 512      32.517 -66.526  -4.565  1.00148.90           C
ANISOU 4954  C   LYS D 512    18701  18462  19413  -2662   -914   1859       C
ATOM   4955  O   LYS D 512      33.254 -66.897  -3.627  1.00108.22           O
ANISOU 4955  O   LYS D 512    13524  13279  14317  -2708   -845   1943       O
ATOM   4956  CB  LYS D 512      32.942 -68.085  -6.498  1.00143.69           C
ANISOU 4956  CB  LYS D 512    17939  17985  18671  -2642   -667   1862       C
ATOM   4957  CG  LYS D 512      32.336 -68.717  -7.745  1.00127.77           C
ANISOU 4957  CG  LYS D 512    15893  16058  16595  -2588   -588   1744       C
ATOM   4958  CD  LYS D 512      32.782 -70.160  -7.907  1.00142.49           C
ANISOU 4958  CD  LYS D 512    17678  17992  18471  -2588   -370   1732       C
ATOM   4959  CE  LYS D 512      32.858 -70.530  -9.384  1.00138.38           C
ANISOU 4959  CE  LYS D 512    17140  17572  17867  -2562   -310   1738       C
ATOM   4960  NZ  LYS D 512      33.181 -71.969  -9.614  1.00141.89           N
ANISOU 4960  NZ  LYS D 512    17511  18084  18316  -2552    -98   1705       N
ATOM   4961  N   GLN D 513      32.176 -65.258  -4.799  1.00158.82           N
ANISOU 4961  N   GLN D 513    20034  19674  20637  -2655  -1107   1879       N
ATOM   4962  CA  GLN D 513      32.618 -64.134  -3.977  1.00178.16           C
ANISOU 4962  CA  GLN D 513    22554  22028  23110  -2697  -1269   2000       C
ATOM   4963  C   GLN D 513      32.070 -64.196  -2.545  1.00155.07           C
ANISOU 4963  C   GLN D 513    19644  19016  20258  -2680  -1279   1889       C
ATOM   4964  O   GLN D 513      32.791 -63.958  -1.574  1.00134.78           O
ANISOU 4964  O   GLN D 513    17094  16384  17734  -2730  -1305   2002       O
ATOM   4965  CB  GLN D 513      32.162 -62.819  -4.621  1.00164.40           C
ANISOU 4965  CB  GLN D 513    20889  20261  21315  -2680  -1473   2011       C
ATOM   4966  CG  GLN D 513      32.285 -62.767  -6.142  1.00133.45           C
ANISOU 4966  CG  GLN D 513    16951  16435  17318  -2674  -1470   2057       C
ATOM   4967  CD  GLN D 513      31.615 -61.531  -6.726  1.00146.98           C
ANISOU 4967  CD  GLN D 513    18733  18123  18987  -2648  -1666   2029       C
ATOM   4968  OE1 GLN D 513      31.564 -60.475  -6.085  1.00120.01           O
ANISOU 4968  OE1 GLN D 513    15389  14618  15589  -2662  -1832   2070       O
ATOM   4969  NE2 GLN D 513      31.087 -61.659  -7.943  1.00151.35           N
ANISOU 4969  NE2 GLN D 513    19268  18756  19482  -2612  -1649   1958       N
ATOM   4970  N   PHE D 514      30.792 -64.539  -2.433  1.00145.69           N
ANISOU 4970  N   PHE D 514    18447  17828  19081  -2607  -1255   1670       N
ATOM   4971  CA  PHE D 514      30.049 -64.417  -1.188  1.00124.77           C
ANISOU 4971  CA  PHE D 514    15820  15097  16488  -2572  -1294   1546       C
ATOM   4972  C   PHE D 514      30.739 -65.130  -0.032  1.00134.42           C
ANISOU 4972  C   PHE D 514    16997  16294  17784  -2614  -1180   1597       C
ATOM   4973  O   PHE D 514      31.013 -66.336  -0.088  1.00 91.72           O
ANISOU 4973  O   PHE D 514    11503  10948  12399  -2622   -997   1577       O
ATOM   4974  CB  PHE D 514      28.639 -64.972  -1.389  1.00123.37           C
ANISOU 4974  CB  PHE D 514    15615  14950  16311  -2488  -1242   1310       C
ATOM   4975  CG  PHE D 514      27.786 -64.925  -0.166  1.00138.13           C
ANISOU 4975  CG  PHE D 514    17499  16748  18235  -2441  -1272   1173       C
ATOM   4976  CD1 PHE D 514      27.899 -65.915   0.807  1.00123.20           C
ANISOU 4976  CD1 PHE D 514    15542  14855  16413  -2444  -1133   1127       C
ATOM   4977  CD2 PHE D 514      26.861 -63.899   0.012  1.00126.93           C
ANISOU 4977  CD2 PHE D 514    16159  15268  16800  -2391  -1438   1089       C
ATOM   4978  CE1 PHE D 514      27.121 -65.887   1.936  1.00 82.90           C
ANISOU 4978  CE1 PHE D 514    10447   9692  11360  -2398  -1159   1005       C
ATOM   4979  CE2 PHE D 514      26.060 -63.856   1.156  1.00 93.41           C
ANISOU 4979  CE2 PHE D 514    11928  10960  12603  -2340  -1465    964       C
ATOM   4980  CZ  PHE D 514      26.196 -64.853   2.116  1.00102.50           C
ANISOU 4980  CZ  PHE D 514    13010  12114  13822  -2343  -1325    923       C
ATOM   4981  N   ASP D 515      30.988 -64.361   1.023  1.00158.82           N
ANISOU 4981  N   ASP D 515    20146  19290  20909  -2638  -1294   1661       N
ATOM   4982  CA  ASP D 515      31.640 -64.845   2.229  1.00161.79           C
ANISOU 4982  CA  ASP D 515    20490  19626  21354  -2682  -1214   1719       C
ATOM   4983  C   ASP D 515      30.886 -64.240   3.402  1.00155.97           C
ANISOU 4983  C   ASP D 515    19812  18794  20657  -2642  -1325   1617       C
ATOM   4984  O   ASP D 515      30.600 -63.038   3.399  1.00129.40           O
ANISOU 4984  O   ASP D 515    16540  15364  17260  -2628  -1511   1633       O
ATOM   4985  CB  ASP D 515      33.107 -64.408   2.250  1.00172.19           C
ANISOU 4985  CB  ASP D 515    21830  20926  22667  -2776  -1250   1972       C
ATOM   4986  CG  ASP D 515      33.893 -65.057   3.370  1.00187.08           C
ANISOU 4986  CG  ASP D 515    23670  22787  24625  -2831  -1141   2048       C
ATOM   4987  OD1 ASP D 515      33.402 -66.070   3.922  1.00167.27           O
ANISOU 4987  OD1 ASP D 515    21090  20299  22166  -2799  -1000   1910       O
ATOM   4988  OD2 ASP D 515      35.001 -64.561   3.689  1.00199.28           O
ANISOU 4988  OD2 ASP D 515    25248  24293  26178  -2908  -1196   2250       O
ATOM   4989  N   THR D 516      30.553 -65.073   4.387  1.00153.15           N
ANISOU 4989  N   THR D 516    19397  18429  20364  -2621  -1213   1512       N
ATOM   4990  CA  THR D 516      29.699 -64.672   5.507  1.00130.98           C
ANISOU 4990  CA  THR D 516    16631  15543  17593  -2567  -1295   1389       C
ATOM   4991  C   THR D 516      30.373 -63.662   6.429  1.00133.61           C
ANISOU 4991  C   THR D 516    17049  15773  17943  -2615  -1436   1524       C
ATOM   4992  O   THR D 516      29.702 -62.978   7.222  1.00109.29           O
ANISOU 4992  O   THR D 516    14035  12615  14873  -2568  -1555   1444       O
ATOM   4993  CB  THR D 516      29.328 -65.882   6.352  1.00124.53           C
ANISOU 4993  CB  THR D 516    15719  14750  16845  -2540  -1129   1266       C
ATOM   4994  OG1 THR D 516      30.336 -66.890   6.190  1.00155.59           O
ANISOU 4994  OG1 THR D 516    19567  18745  20805  -2607   -959   1369       O
ATOM   4995  CG2 THR D 516      27.979 -66.429   5.932  1.00 88.78           C
ANISOU 4995  CG2 THR D 516    11151  10274  12308  -2449  -1078   1052       C
ATOM   4996  N   TYR D 517      31.701 -63.597   6.336  1.00127.42           N
ANISOU 4996  N   TYR D 517    16264  14990  17161  -2707  -1422   1732       N
ATOM   4997  CA  TYR D 517      32.497 -62.697   7.165  1.00 97.59           C
ANISOU 4997  CA  TYR D 517    12564  11116  13399  -2767  -1550   1886       C
ATOM   4998  C   TYR D 517      32.257 -61.240   6.803  1.00 90.67           C
ANISOU 4998  C   TYR D 517    11807  10174  12468  -2752  -1779   1925       C
ATOM   4999  O   TYR D 517      32.581 -60.342   7.571  1.00141.62           O
ANISOU 4999  O   TYR D 517    18346  16532  18933  -2778  -1920   2006       O
ATOM   5000  CB  TYR D 517      33.978 -63.010   7.046  1.00 65.35           C
ANISOU 5000  CB  TYR D 517     8446   7057   9328  -2871  -1476   2110       C
ATOM   5001  CG  TYR D 517      34.455 -64.244   7.790  1.00 83.35           C
ANISOU 5001  CG  TYR D 517    10625   9368  11676  -2906  -1278   2115       C
ATOM   5002  CD1 TYR D 517      34.797 -64.184   9.129  1.00 91.14           C
ANISOU 5002  CD1 TYR D 517    11626  10281  12724  -2939  -1289   2153       C
ATOM   5003  CD2 TYR D 517      34.616 -65.456   7.133  1.00140.40           C
ANISOU 5003  CD2 TYR D 517    17744  16696  18905  -2909  -1084   2091       C
ATOM   5004  CE1 TYR D 517      35.258 -65.305   9.807  1.00116.73           C
ANISOU 5004  CE1 TYR D 517    14769  13552  16030  -2976  -1108   2164       C
ATOM   5005  CE2 TYR D 517      35.077 -66.574   7.795  1.00138.56           C
ANISOU 5005  CE2 TYR D 517    17418  16492  18737  -2943   -905   2101       C
ATOM   5006  CZ  TYR D 517      35.398 -66.496   9.132  1.00119.16           C
ANISOU 5006  CZ  TYR D 517    14969  13963  16342  -2978   -916   2139       C
ATOM   5007  OH  TYR D 517      35.855 -67.619   9.800  1.00125.03           O
ANISOU 5007  OH  TYR D 517    15614  14737  17154  -3015   -735   2150       O
ATOM   5008  N   ASN D 518      31.720 -61.001   5.620  1.00 75.72           N
ANISOU 5008  N   ASN D 518     9921   8332  10516  -2714  -1817   1871       N
ATOM   5009  CA  ASN D 518      31.355 -59.648   5.243  1.00133.54           C
ANISOU 5009  CA  ASN D 518    17351  15598  17789  -2692  -2031   1886       C
ATOM   5010  C   ASN D 518      30.169 -59.175   6.073  1.00126.09           C
ANISOU 5010  C   ASN D 518    16466  14582  16860  -2608  -2124   1711       C
ATOM   5011  O   ASN D 518      29.976 -57.970   6.265  1.00113.17           O
ANISOU 5011  O   ASN D 518    14935  12864  15200  -2596  -2316   1735       O
ATOM   5012  CB  ASN D 518      31.053 -59.568   3.745  1.00158.60           C
ANISOU 5012  CB  ASN D 518    20509  18853  20898  -2671  -2038   1869       C
ATOM   5013  CG  ASN D 518      32.297 -59.321   2.917  1.00166.79           C
ANISOU 5013  CG  ASN D 518    21543  19928  21903  -2754  -2056   2093       C
ATOM   5014  OD1 ASN D 518      33.158 -60.198   2.781  1.00139.87           O
ANISOU 5014  OD1 ASN D 518    18057  16577  18509  -2806  -1906   2190       O
ATOM   5015  ND2 ASN D 518      32.405 -58.117   2.363  1.00177.59           N
ANISOU 5015  ND2 ASN D 518    22991  21262  23225  -2766  -2243   2182       N
ATOM   5016  N   LEU D 519      29.391 -60.142   6.566  1.00117.63           N
ANISOU 5016  N   LEU D 519    15325  13543  15826  -2550  -1987   1539       N
ATOM   5017  CA  LEU D 519      28.205 -59.872   7.373  1.00108.81           C
ANISOU 5017  CA  LEU D 519    14246  12371  14724  -2461  -2048   1362       C
ATOM   5018  C   LEU D 519      28.622 -59.444   8.766  1.00116.05           C
ANISOU 5018  C   LEU D 519    15220  13189  15687  -2483  -2116   1420       C
ATOM   5019  O   LEU D 519      28.104 -58.460   9.314  1.00107.69           O
ANISOU 5019  O   LEU D 519    14258  12044  14616  -2439  -2277   1377       O
ATOM   5020  CB  LEU D 519      27.319 -61.117   7.472  1.00120.00           C
ANISOU 5020  CB  LEU D 519    15561  13860  16172  -2397  -1872   1177       C
ATOM   5021  CG  LEU D 519      26.344 -61.441   6.337  1.00119.70           C
ANISOU 5021  CG  LEU D 519    15487  13902  16092  -2335  -1833   1042       C
ATOM   5022  CD1 LEU D 519      25.765 -60.150   5.753  1.00 93.33           C
ANISOU 5022  CD1 LEU D 519    12250  10519  12691  -2298  -2028   1027       C
ATOM   5023  CD2 LEU D 519      27.020 -62.288   5.265  1.00120.91           C
ANISOU 5023  CD2 LEU D 519    15558  14154  16229  -2388  -1693   1115       C
ATOM   5024  N   TRP D 520      29.558 -60.206   9.331  1.00109.81           N
ANISOU 5024  N   TRP D 520    14365  12411  14946  -2551  -1991   1515       N
ATOM   5025  CA  TRP D 520      30.132 -59.899  10.634  1.00 96.43           C
ANISOU 5025  CA  TRP D 520    12714  10628  13297  -2589  -2039   1594       C
ATOM   5026  C   TRP D 520      30.559 -58.435  10.704  1.00124.88           C
ANISOU 5026  C   TRP D 520    16453  14132  16865  -2620  -2265   1722       C
ATOM   5027  O   TRP D 520      30.433 -57.784  11.742  1.00143.95           O
ANISOU 5027  O   TRP D 520    18948  16451  19297  -2603  -2377   1713       O
ATOM   5028  CB  TRP D 520      31.340 -60.788  10.896  1.00 94.72           C
ANISOU 5028  CB  TRP D 520    12415  10447  13127  -2683  -1886   1734       C
ATOM   5029  CG  TRP D 520      30.999 -62.205  11.192  1.00118.58           C
ANISOU 5029  CG  TRP D 520    15309  13544  16200  -2658  -1673   1614       C
ATOM   5030  CD1 TRP D 520      31.450 -63.319  10.543  1.00135.14           C
ANISOU 5030  CD1 TRP D 520    17299  15740  18310  -2694  -1490   1643       C
ATOM   5031  CD2 TRP D 520      30.134 -62.667  12.238  1.00130.40           C
ANISOU 5031  CD2 TRP D 520    16774  15026  17746  -2588  -1621   1447       C
ATOM   5032  NE1 TRP D 520      30.919 -64.447  11.124  1.00144.44           N
ANISOU 5032  NE1 TRP D 520    18377  16960  19542  -2655  -1331   1504       N
ATOM   5033  CE2 TRP D 520      30.120 -64.076  12.151  1.00145.40           C
ANISOU 5033  CE2 TRP D 520    18540  17017  19689  -2591  -1407   1386       C
ATOM   5034  CE3 TRP D 520      29.383 -62.025  13.215  1.00112.76           C
ANISOU 5034  CE3 TRP D 520    14610  12711  15521  -2522  -1735   1349       C
ATOM   5035  CZ2 TRP D 520      29.358 -64.844  13.034  1.00147.34           C
ANISOU 5035  CZ2 TRP D 520    18717  17277  19991  -2531  -1310   1229       C
ATOM   5036  CZ3 TRP D 520      28.641 -62.795  14.081  1.00121.23           C
ANISOU 5036  CZ3 TRP D 520    15615  13802  16647  -2460  -1634   1196       C
ATOM   5037  CH2 TRP D 520      28.632 -64.190  13.985  1.00142.27           C
ANISOU 5037  CH2 TRP D 520    18141  16559  19357  -2466  -1425   1139       C
ATOM   5038  N   ASN D 521      31.078 -57.925   9.593  1.00120.77           N
ANISOU 5038  N   ASN D 521    15957  13635  16294  -2665  -2334   1846       N
ATOM   5039  CA  ASN D 521      31.517 -56.539   9.523  1.00119.03           C
ANISOU 5039  CA  ASN D 521    15859  13328  16039  -2699  -2554   1980       C
ATOM   5040  C   ASN D 521      30.392 -55.494   9.635  1.00136.42           C
ANISOU 5040  C   ASN D 521    18164  15461  18207  -2610  -2731   1848       C
ATOM   5041  O   ASN D 521      30.669 -54.301   9.661  1.00166.55           O
ANISOU 5041  O   ASN D 521    22088  19196  21997  -2631  -2924   1945       O
ATOM   5042  CB  ASN D 521      32.426 -56.296   8.304  1.00131.61           C
ANISOU 5042  CB  ASN D 521    17443  14972  17591  -2773  -2578   2160       C
ATOM   5043  CG  ASN D 521      33.864 -56.796   8.527  1.00157.78           C
ANISOU 5043  CG  ASN D 521    20710  18302  20938  -2881  -2487   2367       C
ATOM   5044  OD1 ASN D 521      34.348 -57.679   7.820  1.00153.47           O
ANISOU 5044  OD1 ASN D 521    20069  17853  20391  -2915  -2333   2419       O
ATOM   5045  ND2 ASN D 521      34.546 -56.223   9.513  1.00173.16           N
ANISOU 5045  ND2 ASN D 521    22727  20152  22914  -2935  -2585   2488       N
ATOM   5046  N   THR D 522      29.133 -55.933   9.687  1.00123.96           N
ANISOU 5046  N   THR D 522    16552  13917  16630  -2511  -2668   1635       N
ATOM   5047  CA  THR D 522      27.999 -55.004   9.828  1.00125.77           C
ANISOU 5047  CA  THR D 522    16873  14085  16828  -2419  -2823   1503       C
ATOM   5048  C   THR D 522      27.845 -54.488  11.246  1.00151.87           C
ANISOU 5048  C   THR D 522    20261  17281  20163  -2390  -2916   1474       C
ATOM   5049  O   THR D 522      27.286 -53.412  11.473  1.00168.69           O
ANISOU 5049  O   THR D 522    22501  19331  22264  -2337  -3091   1432       O
ATOM   5050  CB  THR D 522      26.645 -55.663   9.497  1.00115.26           C
ANISOU 5050  CB  THR D 522    15479  12825  15490  -2318  -2724   1283       C
ATOM   5051  OG1 THR D 522      26.851 -56.947   8.897  1.00113.69           O
ANISOU 5051  OG1 THR D 522    15151  12738  15308  -2344  -2519   1268       O
ATOM   5052  CG2 THR D 522      25.803 -54.760   8.587  1.00100.69           C
ANISOU 5052  CG2 THR D 522    13698  10976  13583  -2263  -2863   1218       C
ATOM   5053  N   PHE D 523      28.300 -55.291  12.199  1.00156.51           N
ANISOU 5053  N   PHE D 523    20791  17868  20807  -2418  -2792   1488       N
ATOM   5054  CA  PHE D 523      28.104 -55.010  13.614  1.00184.04           C
ANISOU 5054  CA  PHE D 523    24336  21263  24326  -2384  -2848   1443       C
ATOM   5055  C   PHE D 523      29.094 -53.985  14.125  1.00188.08           C
ANISOU 5055  C   PHE D 523    24961  21665  24834  -2458  -3014   1623       C
ATOM   5056  O   PHE D 523      28.725 -53.031  14.814  1.00173.72           O
ANISOU 5056  O   PHE D 523    23257  19746  23002  -2412  -3176   1592       O
ATOM   5057  CB  PHE D 523      28.236 -56.305  14.407  1.00193.62           C
ANISOU 5057  CB  PHE D 523    25436  22525  25606  -2392  -2645   1395       C
ATOM   5058  CG  PHE D 523      27.313 -57.393  13.933  1.00166.32           C
ANISOU 5058  CG  PHE D 523    21861  19176  22157  -2325  -2477   1226       C
ATOM   5059  CD1 PHE D 523      26.018 -57.095  13.536  1.00143.97           C
ANISOU 5059  CD1 PHE D 523    19055  16359  19290  -2220  -2531   1061       C
ATOM   5060  CD2 PHE D 523      27.746 -58.709  13.869  1.00128.81           C
ANISOU 5060  CD2 PHE D 523    16978  14513  17452  -2369  -2269   1236       C
ATOM   5061  CE1 PHE D 523      25.165 -58.094  13.096  1.00144.03           C
ANISOU 5061  CE1 PHE D 523    18957  16464  19306  -2161  -2383    911       C
ATOM   5062  CE2 PHE D 523      26.911 -59.706  13.435  1.00 76.54           C
ANISOU 5062  CE2 PHE D 523    10253   7986  10840  -2309  -2122   1084       C
ATOM   5063  CZ  PHE D 523      25.611 -59.404  13.047  1.00123.10           C
ANISOU 5063  CZ  PHE D 523    16176  13896  16701  -2206  -2180    922       C
ATOM   5064  N   THR D 524      30.358 -54.198  13.779  1.00205.42           N
ANISOU 5064  N   THR D 524    27125  23883  27043  -2571  -2973   1815       N
ATOM   5065  CA  THR D 524      31.419 -53.279  14.148  1.00211.60           C
ANISOU 5065  CA  THR D 524    28006  24569  27823  -2655  -3126   2013       C
ATOM   5066  C   THR D 524      31.065 -51.857  13.688  1.00222.58           C
ANISOU 5066  C   THR D 524    29527  25886  29156  -2624  -3363   2028       C
ATOM   5067  O   THR D 524      31.225 -50.899  14.445  1.00220.27           O
ANISOU 5067  O   THR D 524    29354  25478  28860  -2627  -3532   2076       O
ATOM   5068  CB  THR D 524      32.783 -53.750  13.586  1.00185.47           C
ANISOU 5068  CB  THR D 524    24630  21314  24527  -2778  -3040   2224       C
ATOM   5069  OG1 THR D 524      32.895 -53.390  12.203  1.00193.40           O
ANISOU 5069  OG1 THR D 524    25632  22372  25480  -2795  -3090   2289       O
ATOM   5070  CG2 THR D 524      32.928 -55.276  13.741  1.00121.66           C
ANISOU 5070  CG2 THR D 524    16400  13330  16495  -2793  -2784   2178       C
ATOM   5071  N   ARG D 525      30.553 -51.729  12.464  1.00223.64           N
ANISOU 5071  N   ARG D 525    29640  26086  29245  -2593  -3374   1980       N
ATOM   5072  CA  ARG D 525      30.137 -50.426  11.934  1.00223.51           C
ANISOU 5072  CA  ARG D 525    29736  26012  29176  -2560  -3589   1982       C
ATOM   5073  C   ARG D 525      29.072 -49.777  12.822  1.00207.75           C
ANISOU 5073  C   ARG D 525    27836  23927  27173  -2456  -3702   1823       C
ATOM   5074  O   ARG D 525      28.347 -48.878  12.391  1.00190.44           O
ANISOU 5074  O   ARG D 525    25721  21701  24937  -2397  -3847   1759       O
ATOM   5075  CB  ARG D 525      29.616 -50.546  10.491  1.00235.97           C
ANISOU 5075  CB  ARG D 525    31258  27690  30712  -2534  -3555   1929       C
ATOM   5076  CG  ARG D 525      30.544 -51.290   9.527  1.00239.23           C
ANISOU 5076  CG  ARG D 525    31566  28205  31124  -2620  -3424   2064       C
ATOM   5077  CD  ARG D 525      30.114 -51.137   8.063  1.00235.93           C
ANISOU 5077  CD  ARG D 525    31118  27870  30655  -2600  -3437   2036       C
ATOM   5078  NE  ARG D 525      30.482 -52.299   7.249  1.00233.21           N
ANISOU 5078  NE  ARG D 525    30644  27650  30314  -2634  -3237   2059       N
ATOM   5079  CZ  ARG D 525      30.792 -52.250   5.954  1.00221.62           C
ANISOU 5079  CZ  ARG D 525    29139  26260  28807  -2667  -3235   2140       C
ATOM   5080  NH1 ARG D 525      30.793 -51.089   5.310  1.00221.86           N
ANISOU 5080  NH1 ARG D 525    29246  26256  28794  -2673  -3423   2210       N
ATOM   5081  NH2 ARG D 525      31.110 -53.366   5.304  1.00200.45           N
ANISOU 5081  NH2 ARG D 525    26344  23690  26129  -2691  -3044   2151       N
TER    5082      ARG D 525
HETATM 5083 ZN   ZN  C 201     -33.533-106.640 -27.893  1.00132.04          Zn
ANISOU 5083 ZN   ZN  C 201    16025  16767  17378  -1518  -2118  -3089      Zn
HETATM 5084 ZN   ZN  C 202     -55.673-105.683 -21.758  1.00184.23          Zn
ANISOU 5084 ZN   ZN  C 202    21549  23813  24636  -1075  -3926   -675      Zn
HETATM 5085 ZN   ZN  D 601     -15.340 -91.295  -1.529  1.00102.99          Zn
ANISOU 5085 ZN   ZN  D 601    11048  13464  14621   -422   -640  -2744      Zn
HETATM 5086 ZN   ZN  D 602       9.648 -87.734 -23.430  1.00183.06          Zn
ANISOU 5086 ZN   ZN  D 602    22710  23800  23046  -1602    520  -1950      Zn
HETATM 5087 ZN   ZN  D 603      21.226 -60.859  19.928  1.00117.24          Zn
ANISOU 5087 ZN   ZN  D 603    15327  13044  16175  -1718  -2050    199      Zn
HETATM 5088 MG   MG  D 604      -3.277 -95.429 -30.577  1.00151.50          Mg
ANISOU 5088 MG   MG  D 604    19031  19707  18825  -1498    106  -3165      Mg
CONECT  532 5083
CONECT  558 5083
CONECT  611 5083
CONECT  663 5083
CONECT  868 5084
CONECT  888 5084
CONECT  949 5084
CONECT  961 5084
CONECT 1688 5088
CONECT 1689 5088
CONECT 2474 5088
CONECT 2604 5085
CONECT 2624 5085
CONECT 2744 5085
CONECT 2773 5085
CONECT 2776 5085
CONECT 3007 5086
CONECT 3040 5086
CONECT 3063 5086
CONECT 3066 5086
CONECT 3170 5086
CONECT 4565 5087
CONECT 4673 5087
CONECT 4715 5087
CONECT 4743 5087
CONECT 5083  532  558  611  663
CONECT 5084  949  868  961  888
CONECT 5085 2744 2776 2773 2604
CONECT 5085 2624
CONECT 5086 3066 3170 3040 3063
CONECT 5086 3007
CONECT 5087 4673 4715 4743 4565
CONECT 5088 1689 2474 1688
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.