CNRS Nantes University UFIP UFIP
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***  MEMBRANE PROTEIN 02-MAR-18 6CM4  ***

elNémo ID: 191213222746135159

Job options:

ID        	=	 191213222746135159
JOBID     	=	 MEMBRANE PROTEIN 02-MAR-18 6CM4
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    MEMBRANE PROTEIN                        02-MAR-18   6CM4              
TITLE     STRUCTURE OF THE D2 DOPAMINE RECEPTOR BOUND TO THE ATYPICAL           
TITLE    2 ANTIPSYCHOTIC DRUG RISPERIDONE                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D(2) DOPAMINE RECEPTOR, ENDOLYSIN CHIMERA;                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: DOPAMINE D2 RECEPTOR, LYSIS PROTEIN, LYSOZYME, MURAMIDASE,  
COMPND   5 DOPAMINE D2 RECEPTOR;                                                
COMPND   6 EC: 3.2.1.17;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4;          
SOURCE   3 ORGANISM_COMMON: HUMAN, BACTERIOPHAGE T4;                            
SOURCE   4 ORGANISM_TAXID: 9606, 10665;                                         
SOURCE   5 GENE: DRD2, E, T4TP126;                                              
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1-HM                              
KEYWDS    GPCR, D2, DOPAMINE RECEPTOR, ANTIPSYCHOTIC, RISPERIDONE, MEMBRANE     
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.WANG,T.CHE,A.LEVIT,B.K.SHOICHET,D.WACKER,B.L.ROTH                   
REVDAT   5   27-NOV-19 6CM4    1       REMARK                                   
REVDAT   4   20-FEB-19 6CM4    1       REMARK                                   
REVDAT   3   11-APR-18 6CM4    1       DBREF                                    
REVDAT   2   21-MAR-18 6CM4    1       JRNL                                     
REVDAT   1   14-MAR-18 6CM4    0                                                
SPRSDE     14-MAR-18 6CM4      6C38                                             
JRNL        AUTH   S.WANG,T.CHE,A.LEVIT,B.K.SHOICHET,D.WACKER,B.L.ROTH          
JRNL        TITL   STRUCTURE OF THE D2 DOPAMINE RECEPTOR BOUND TO THE ATYPICAL  
JRNL        TITL 2 ANTIPSYCHOTIC DRUG RISPERIDONE.                              
JRNL        REF    NATURE                        V. 555   269 2018              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   29466326                                                     
JRNL        DOI    10.1038/NATURE25758                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.87 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.12_2829: ???)                              
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) : 2.87                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.55                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 12814                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.227                           
REMARK   3   R VALUE            (WORKING SET) : 0.226                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.850                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 622                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.5504 -  4.5475    0.98     3287   157  0.2103 0.2188        
REMARK   3     2  4.5475 -  3.6116    0.99     3151   170  0.2090 0.2511        
REMARK   3     3  3.6116 -  3.1556    0.99     3111   162  0.2730 0.3034        
REMARK   3     4  3.1556 -  2.8674    0.84     2643   133  0.3166 0.3214        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.640           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           3283                                  
REMARK   3   ANGLE     :  0.516           4483                                  
REMARK   3   CHIRALITY :  0.037            544                                  
REMARK   3   PLANARITY :  0.003            549                                  
REMARK   3   DIHEDRAL  : 10.862           1928                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 36 THROUGH 222 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   7.6595   9.9883   1.8227              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3906 T22:   0.3948                                     
REMARK   3      T33:   0.4097 T12:  -0.0409                                     
REMARK   3      T13:   0.0298 T23:   0.0323                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8704 L22:   2.9655                                     
REMARK   3      L33:   4.7317 L12:   0.7811                                     
REMARK   3      L13:   2.8181 L23:   1.4507                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0593 S12:  -0.1051 S13:   0.0093                       
REMARK   3      S21:   0.1418 S22:  -0.1464 S23:   0.1356                       
REMARK   3      S31:   0.4299 S32:  -0.3974 S33:  -0.0137                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1002 THROUGH 1161 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  32.7700  -7.7446  36.3658              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6968 T22:   0.5198                                     
REMARK   3      T33:   0.5000 T12:   0.0363                                     
REMARK   3      T13:   0.0872 T23:   0.1084                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6697 L22:   6.8821                                     
REMARK   3      L33:   6.4568 L12:   1.6541                                     
REMARK   3      L13:   1.9941 L23:   1.4205                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2551 S12:   0.1211 S13:  -0.2547                       
REMARK   3      S21:  -0.3908 S22:  -0.0566 S23:  -0.4642                       
REMARK   3      S31:   0.4711 S32:   0.2364 S33:   0.3147                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 384 THROUGH 460 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   9.8885  -1.6530  -1.3224              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6392 T22:   0.3770                                     
REMARK   3      T33:   0.5276 T12:   0.0087                                     
REMARK   3      T13:  -0.0908 T23:   0.0140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0244 L22:   5.3813                                     
REMARK   3      L33:   6.7255 L12:   0.3578                                     
REMARK   3      L13:   1.1698 L23:   0.5209                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0948 S12:   0.3307 S13:   0.0832                       
REMARK   3      S21:  -0.4022 S22:   0.2772 S23:  -0.0581                       
REMARK   3      S31:   1.2902 S32:  -0.0417 S33:  -0.2847                       
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 6CM4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000232947.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-AUG-17                          
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               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL CRYO-COOLED         
REMARK 200                                   SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12826                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.867                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : 0.13400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 15.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.99                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.73800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 5WIU & 2RH1                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL, PH 7.8, 230 MM          
REMARK 280  LITHIUM NITRATE, 25% PEG400, 4% 1,3-BUTANEDIOL, LIPIDIC CUBIC       
REMARK 280  PHASE, TEMPERATURE 293K                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       25.48950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.65350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.26150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       75.65350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.48950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.26150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 12.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   140                                                      
REMARK 465     LEU A   141                                                      
REMARK 465     TYR A   142                                                      
REMARK 465     ASN A   143                                                      
REMARK 465     LYS A   362                                                      
REMARK 465     LEU A   363                                                      
REMARK 465     CYS A   443                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASN A  35    CG   OD1  ND2                                       
REMARK 470     TYR A  36    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A  43    CG   CD1  CD2                                       
REMARK 470     GLU A  62    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  63    CG   CD   CE   NZ                                   
REMARK 470     VAL A  96    CG1  CG2                                            
REMARK 470     GLU A  99    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 101    CG   CD   CE   NZ                                   
REMARK 470     THR A 144    OG1  CG2                                            
REMARK 470     ARG A 145    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 147    OG                                                  
REMARK 470     LYS A 149    CG   CD   CE   NZ                                   
REMARK 470     ARG A 150    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 176    CG   OD1  ND2                                       
REMARK 470     ASP A 178    CG   OD1  OD2                                       
REMARK 470     GLN A 179    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 180    CG   OD1  ND2                                       
REMARK 470     LYS A 211    CE   NZ                                             
REMARK 470     ARG A 217    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 218    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 221    CG   CD   CE   NZ                                   
REMARK 470     ARG A 222    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1016    CG   CD   CE   NZ                                   
REMARK 470     LYS A1019    CG   CD   CE   NZ                                   
REMARK 470     GLU A1022    CG   CD   OE1  OE2                                  
REMARK 470     LEU A1032    CG   CD1  CD2                                       
REMARK 470     LEU A1033    CG   CD1  CD2                                       
REMARK 470     LYS A1035    CG   CD   CE   NZ                                   
REMARK 470     SER A1036    OG                                                  
REMARK 470     SER A1038    OG                                                  
REMARK 470     ASN A1040    CG   OD1  ND2                                       
REMARK 470     SER A1044    OG                                                  
REMARK 470     GLU A1045    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1048    CG   CD   CE   NZ                                   
REMARK 470     ILE A1050    CG1  CG2  CD1                                       
REMARK 470     ASN A1053    CG   OD1  ND2                                       
REMARK 470     THR A1054    OG1  CG2                                            
REMARK 470     ASN A1055    CG   OD1  ND2                                       
REMARK 470     VAL A1057    CG1  CG2                                            
REMARK 470     LYS A1060    CG   CD   CE   NZ                                   
REMARK 470     LYS A1065    CG   CD   CE   NZ                                   
REMARK 470     ARG A1080    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1083    CG   CD   CE   NZ                                   
REMARK 470     LYS A1085    CG   CD   CE   NZ                                   
REMARK 470     ASN A1116    CG   OD1  ND2                                       
REMARK 470     ASP A1127    CG   OD1  OD2                                       
REMARK 470     VAL A1131    CG1  CG2                                            
REMARK 470     LYS A1135    CG   CD   CE   NZ                                   
REMARK 470     ARG A1137    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A1141    CG   CD   OE1  NE2                                  
REMARK 470     LYS A1147    CG   CD   CE   NZ                                   
REMARK 470     THR A1157    OG1  CG2                                            
REMARK 470     SER A 364    OG                                                  
REMARK 470     GLN A 365    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 366    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 367    CG   CD   CE   NZ                                   
REMARK 470     LYS A 369    CG   CD   CE   NZ                                   
REMARK 470     LYS A 370    CG   CD   CE   NZ                                   
REMARK 470     ILE A 394    CG1  CG2  CD1                                       
REMARK 470     HIS A 398    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP A 400    CG   OD1  OD2                                       
REMARK 470     VAL A 406    CG1  CG2                                            
REMARK 470     LEU A 407    CG   CD1  CD2                                       
REMARK 470     ILE A 431    CG1  CG2  CD1                                       
REMARK 470     GLU A 432    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 434    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 435    CG   CD   CE   NZ                                   
REMARK 470     LEU A 438    CG   CD1  CD2                                       
REMARK 470     LYS A 439    CG   CD   CE   NZ                                   
REMARK 470     HIS A 442    CG   ND1  CD2  CE1  NE2                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A  66       70.23   -104.22                                   
REMARK 500    VAL A  87      -52.46   -121.67                                   
REMARK 500    PHE A 198      -60.72   -124.56                                   
REMARK 500    ASN A1055       17.81     58.75                                   
REMARK 500    PHE A1114       49.44    -89.78                                   
REMARK 500    ASP A 400       11.47     57.92                                   
REMARK 500    LEU A 441       33.98    -88.55                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OLA A 2005                                                       
REMARK 610     OLA A 2006                                                       
DBREF  6CM4 A   35   222  UNP    P14416   DRD2_HUMAN      35    222             
DBREF  6CM4 A 1002  1161  UNP    D9IEF7   D9IEF7_BPT4      2    161             
DBREF  6CM4 A  362   443  UNP    P14416   DRD2_HUMAN     362    443             
SEQADV 6CM4 ALA A  122  UNP  P14416    ILE   122 CONFLICT                       
SEQADV 6CM4 THR A 1054  UNP  D9IEF7    CYS    54 CONFLICT                       
SEQADV 6CM4 ALA A 1097  UNP  D9IEF7    CYS    97 CONFLICT                       
SEQADV 6CM4 ALA A  375  UNP  P14416    LEU   375 CONFLICT                       
SEQADV 6CM4 ALA A  379  UNP  P14416    LEU   379 CONFLICT                       
SEQRES   1 A  430  ASN TYR TYR ALA THR LEU LEU THR LEU LEU ILE ALA VAL          
SEQRES   2 A  430  ILE VAL PHE GLY ASN VAL LEU VAL CYS MET ALA VAL SER          
SEQRES   3 A  430  ARG GLU LYS ALA LEU GLN THR THR THR ASN TYR LEU ILE          
SEQRES   4 A  430  VAL SER LEU ALA VAL ALA ASP LEU LEU VAL ALA THR LEU          
SEQRES   5 A  430  VAL MET PRO TRP VAL VAL TYR LEU GLU VAL VAL GLY GLU          
SEQRES   6 A  430  TRP LYS PHE SER ARG ILE HIS CYS ASP ILE PHE VAL THR          
SEQRES   7 A  430  LEU ASP VAL MET MET CYS THR ALA SER ALA LEU ASN LEU          
SEQRES   8 A  430  CYS ALA ILE SER ILE ASP ARG TYR THR ALA VAL ALA MET          
SEQRES   9 A  430  PRO MET LEU TYR ASN THR ARG TYR SER SER LYS ARG ARG          
SEQRES  10 A  430  VAL THR VAL MET ILE SER ILE VAL TRP VAL LEU SER PHE          
SEQRES  11 A  430  THR ILE SER CYS PRO LEU LEU PHE GLY LEU ASN ASN ALA          
SEQRES  12 A  430  ASP GLN ASN GLU CYS ILE ILE ALA ASN PRO ALA PHE VAL          
SEQRES  13 A  430  VAL TYR SER SER ILE VAL SER PHE TYR VAL PRO PHE ILE          
SEQRES  14 A  430  VAL THR LEU LEU VAL TYR ILE LYS ILE TYR ILE VAL LEU          
SEQRES  15 A  430  ARG ARG ARG ARG LYS ARG ASN ILE PHE GLU MET LEU ARG          
SEQRES  16 A  430  ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP THR          
SEQRES  17 A  430  GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU THR          
SEQRES  18 A  430  LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU ASP          
SEQRES  19 A  430  LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR LYS          
SEQRES  20 A  430  ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP ALA          
SEQRES  21 A  430  ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS PRO          
SEQRES  22 A  430  VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA LEU          
SEQRES  23 A  430  ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL ALA          
SEQRES  24 A  430  GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS ARG          
SEQRES  25 A  430  TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG TRP          
SEQRES  26 A  430  TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE THR          
SEQRES  27 A  430  THR PHE ARG THR GLY THR TRP ASP ALA TYR LYS LEU SER          
SEQRES  28 A  430  GLN GLN LYS GLU LYS LYS ALA THR GLN MET ALA ALA ILE          
SEQRES  29 A  430  VAL ALA GLY VAL PHE ILE ILE CYS TRP LEU PRO PHE PHE          
SEQRES  30 A  430  ILE THR HIS ILE LEU ASN ILE HIS CYS ASP CYS ASN ILE          
SEQRES  31 A  430  PRO PRO VAL LEU TYR SER ALA PHE THR TRP LEU GLY TYR          
SEQRES  32 A  430  VAL ASN SER ALA VAL ASN PRO ILE ILE TYR THR THR PHE          
SEQRES  33 A  430  ASN ILE GLU PHE ARG LYS ALA PHE LEU LYS ILE LEU HIS          
SEQRES  34 A  430  CYS                                                          
HET    8NU  A2001      30                                                       
HET    PEG  A2002       7                                                       
HET    PEG  A2003       7                                                       
HET    PEG  A2004       7                                                       
HET    OLA  A2005      13                                                       
HET    OLA  A2006      12                                                       
HET    OLA  A2007      20                                                       
HETNAM     8NU 3-[2-[4-(6-FLUORANYL-1,2-BENZOXAZOL-3-YL)PIPERIDIN-1-            
HETNAM   2 8NU  YL]ETHYL]-2-METHYL-6,7,8,9-TETRAHYDROPYRIDO[1,2-                
HETNAM   3 8NU  A]PYRIMIDIN-4-ONE                                               
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     OLA OLEIC ACID                                                       
FORMUL   2  8NU    C23 H27 F N4 O2                                              
FORMUL   3  PEG    3(C4 H10 O3)                                                 
FORMUL   6  OLA    3(C18 H34 O2)                                                
FORMUL   9  HOH   *16(H2 O)                                                     
HELIX    1 AA1 ASN A   35  GLU A   62  1                                  28    
HELIX    2 AA2 LYS A   63  GLN A   66  5                                   4    
HELIX    3 AA3 THR A   67  VAL A   87  1                                  21    
HELIX    4 AA4 VAL A   87  GLY A   98  1                                  12    
HELIX    5 AA5 SER A  103  MET A  138  1                                  36    
HELIX    6 AA6 TYR A  146  CYS A  168  1                                  23    
HELIX    7 AA7 PRO A  169  ASN A  176  5                                   8    
HELIX    8 AA8 CYS A  182  ASN A  186  5                                   5    
HELIX    9 AA9 ALA A  188  VAL A  196  1                                   9    
HELIX   10 AB1 PHE A  198  GLU A 1011  1                                  35    
HELIX   11 AB2 SER A 1038  GLY A 1051  1                                  14    
HELIX   12 AB3 THR A 1059  ASN A 1081  1                                  23    
HELIX   13 AB4 LEU A 1084  LEU A 1091  1                                   8    
HELIX   14 AB5 ASP A 1092  ALA A 1112  1                                  21    
HELIX   15 AB6 PHE A 1114  GLN A 1123  1                                  10    
HELIX   16 AB7 ARG A 1125  ALA A 1134  1                                  10    
HELIX   17 AB8 SER A 1136  THR A 1142  1                                   7    
HELIX   18 AB9 THR A 1142  GLY A 1156  1                                  15    
HELIX   19 AC1 GLU A  368  CYS A  399  1                                  32    
HELIX   20 AC2 PRO A  404  ASN A  418  1                                  15    
HELIX   21 AC3 VAL A  421  ASN A  430  1                                  10    
HELIX   22 AC4 ASN A  430  LEU A  441  1                                  12    
SHEET    1 AA1 3 ARG A1014  LYS A1019  0                                        
SHEET    2 AA1 3 TYR A1025  GLY A1028 -1  O  THR A1026   N  TYR A1018           
SHEET    3 AA1 3 HIS A1031  THR A1034 -1  O  LEU A1033   N  TYR A1025           
SSBOND   1 CYS A  107    CYS A  182                          1555   1555  2.03  
SSBOND   2 CYS A  399    CYS A  401                          1555   1555  2.04  
CRYST1   50.979   72.523  151.307  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019616  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013789  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006609        0.00000                         
ATOM      1  N   ASN A  35      -5.317  -8.666 -16.658  1.00108.95           N  
ATOM      2  CA  ASN A  35      -3.999  -9.279 -16.550  1.00112.41           C  
ATOM      3  C   ASN A  35      -3.770  -9.829 -15.148  1.00103.98           C  
ATOM      4  O   ASN A  35      -4.596  -9.642 -14.253  1.00111.14           O  
ATOM      5  CB  ASN A  35      -2.903  -8.271 -16.904  1.00115.88           C  
ATOM      6  N   TYR A  36      -2.640 -10.512 -14.962  1.00122.79           N  
ANISOU    6  N   TYR A  36    17290  13079  16284  -1997  -3163  -3043       N  
ATOM      7  CA  TYR A  36      -2.284 -11.046 -13.653  1.00105.49           C  
ANISOU    7  CA  TYR A  36    15314  10451  14315  -2168  -3210  -2776       C  
ATOM      8  C   TYR A  36      -1.522 -10.036 -12.804  1.00100.38           C  
ANISOU    8  C   TYR A  36    14564  10022  13555  -2013  -2870  -2480       C  
ATOM      9  O   TYR A  36      -1.767  -9.933 -11.597  1.00 95.60           O  
ANISOU    9  O   TYR A  36    13979   9308  13038  -2297  -2774  -2120       O  
ATOM     10  CB  TYR A  36      -1.455 -12.323 -13.811  1.00 98.01           C  
ANISOU   10  CB  TYR A  36    14721   8957  13564  -1967  -3571  -3071       C  
ATOM     11  N   TYR A  37      -0.606  -9.280 -13.416  1.00105.86           N  
ANISOU   11  N   TYR A  37    15140  11047  14036  -1589  -2687  -2627       N  
ATOM     12  CA  TYR A  37       0.202  -8.334 -12.652  1.00101.50           C  
ANISOU   12  CA  TYR A  37    14496  10678  13392  -1434  -2394  -2372       C  
ATOM     13  C   TYR A  37      -0.596  -7.105 -12.233  1.00 97.18           C  
ANISOU   13  C   TYR A  37    13669  10521  12732  -1638  -2109  -2055       C  
ATOM     14  O   TYR A  37      -0.269  -6.474 -11.221  1.00 92.55           O  
ANISOU   14  O   TYR A  37    13035   9983  12145  -1663  -1908  -1774       O  
ATOM     15  CB  TYR A  37       1.435  -7.931 -13.459  1.00105.43           C  
ANISOU   15  CB  TYR A  37    14938  11423  13698   -962  -2294  -2627       C  
ATOM     16  CG  TYR A  37       2.442  -9.052 -13.603  1.00112.39           C  
ANISOU   16  CG  TYR A  37    16060  11928  14715   -688  -2547  -2949       C  
ATOM     17  CD1 TYR A  37       2.745  -9.880 -12.528  1.00116.25           C  
ANISOU   17  CD1 TYR A  37    16804  11893  15472   -778  -2740  -2820       C  
ATOM     18  CD2 TYR A  37       3.084  -9.291 -14.814  1.00112.70           C  
ANISOU   18  CD2 TYR A  37    16070  12145  14606   -332  -2615  -3395       C  
ATOM     19  CE1 TYR A  37       3.662 -10.907 -12.650  1.00117.63           C  
ANISOU   19  CE1 TYR A  37    17203  11682  15808   -489  -3027  -3136       C  
ATOM     20  CE2 TYR A  37       4.002 -10.320 -14.944  1.00114.52           C  
ANISOU   20  CE2 TYR A  37    16488  12042  14980    -35  -2866  -3754       C  
ATOM     21  CZ  TYR A  37       4.287 -11.123 -13.860  1.00116.82           C  
ANISOU   21  CZ  TYR A  37    17037  11766  15584    -99  -3089  -3627       C  
ATOM     22  OH  TYR A  37       5.200 -12.147 -13.987  1.00116.76           O  
ANISOU   22  OH  TYR A  37    17222  11387  15756    236  -3393  -4004       O  
ATOM     23  N   ALA A  38      -1.639  -6.750 -12.985  1.00 96.22           N  
ANISOU   23  N   ALA A  38    13359  10676  12525  -1764  -2113  -2120       N  
ATOM     24  CA  ALA A  38      -2.506  -5.655 -12.566  1.00 90.24           C  
ANISOU   24  CA  ALA A  38    12324  10255  11709  -1946  -1899  -1864       C  
ATOM     25  C   ALA A  38      -3.348  -6.039 -11.356  1.00 93.14           C  
ANISOU   25  C   ALA A  38    12686  10447  12255  -2375  -1898  -1620       C  
ATOM     26  O   ALA A  38      -3.625  -5.191 -10.500  1.00 89.27           O  
ANISOU   26  O   ALA A  38    12015  10164  11737  -2476  -1673  -1375       O  
ATOM     27  CB  ALA A  38      -3.409  -5.222 -13.721  1.00 92.04           C  
ANISOU   27  CB  ALA A  38    12349  10812  11811  -1948  -1956  -2018       C  
ATOM     28  N   THR A  39      -3.759  -7.307 -11.265  1.00101.53           N  
ANISOU   28  N   THR A  39    13946  11141  13491  -2646  -2152  -1687       N  
ATOM     29  CA  THR A  39      -4.521  -7.761 -10.105  1.00 98.62           C  
ANISOU   29  CA  THR A  39    13594  10616  13261  -3121  -2155  -1423       C  
ATOM     30  C   THR A  39      -3.673  -7.706  -8.839  1.00 94.46           C  
ANISOU   30  C   THR A  39    13228   9915  12749  -3111  -2033  -1154       C  
ATOM     31  O   THR A  39      -4.127  -7.220  -7.795  1.00 90.19           O  
ANISOU   31  O   THR A  39    12545   9551  12174  -3363  -1831   -884       O  
ATOM     32  CB  THR A  39      -5.041  -9.178 -10.345  1.00 96.91           C  
ANISOU   32  CB  THR A  39    13602   9983  13235  -3430  -2502  -1538       C  
ATOM     33  OG1 THR A  39      -5.673  -9.242 -11.631  1.00 99.65           O  
ANISOU   33  OG1 THR A  39    13821  10489  13554  -3372  -2644  -1841       O  
ATOM     34  CG2 THR A  39      -6.044  -9.566  -9.272  1.00 85.14           C  
ANISOU   34  CG2 THR A  39    12068   8436  11847  -4016  -2487  -1245       C  
ATOM     35  N   LEU A  40      -2.434  -8.202  -8.915  1.00 91.92           N  
ANISOU   35  N   LEU A  40    13187   9271  12469  -2807  -2162  -1251       N  
ATOM     36  CA  LEU A  40      -1.537  -8.138  -7.766  1.00 89.55           C  
ANISOU   36  CA  LEU A  40    13043   8803  12179  -2751  -2081  -1015       C  
ATOM     37  C   LEU A  40      -1.335  -6.702  -7.304  1.00 83.76           C  
ANISOU   37  C   LEU A  40    12038   8512  11276  -2605  -1722   -856       C  
ATOM     38  O   LEU A  40      -1.301  -6.429  -6.098  1.00 87.36           O  
ANISOU   38  O   LEU A  40    12497   8987  11709  -2775  -1584   -580       O  
ATOM     39  CB  LEU A  40      -0.191  -8.777  -8.104  1.00 87.94           C  
ANISOU   39  CB  LEU A  40    13114   8249  12051  -2357  -2285  -1222       C  
ATOM     40  CG  LEU A  40      -0.166 -10.273  -8.417  1.00 86.57           C  
ANISOU   40  CG  LEU A  40    13274   7524  12094  -2433  -2707  -1405       C  
ATOM     41  CD1 LEU A  40       1.260 -10.798  -8.334  1.00 81.27           C  
ANISOU   41  CD1 LEU A  40    12855   6507  11518  -2029  -2890  -1557       C  
ATOM     42  CD2 LEU A  40      -1.085 -11.041  -7.480  1.00 87.43           C  
ANISOU   42  CD2 LEU A  40    13549   7331  12340  -3007  -2857  -1101       C  
ATOM     43  N   LEU A  41      -1.202  -5.770  -8.248  1.00 77.53           N  
ANISOU   43  N   LEU A  41    11027   8075  10356  -2302  -1588  -1023       N  
ATOM     44  CA  LEU A  41      -1.025  -4.372  -7.871  1.00 83.20           C  
ANISOU   44  CA  LEU A  41    11504   9166  10941  -2162  -1296   -879       C  
ATOM     45  C   LEU A  41      -2.242  -3.847  -7.120  1.00 91.88           C  
ANISOU   45  C   LEU A  41    12365  10511  12032  -2501  -1145   -694       C  
ATOM     46  O   LEU A  41      -2.101  -3.145  -6.111  1.00 94.79           O  
ANISOU   46  O   LEU A  41    12646  11017  12354  -2528   -951   -503       O  
ATOM     47  CB  LEU A  41      -0.739  -3.520  -9.108  1.00 84.35           C  
ANISOU   47  CB  LEU A  41    11487   9616  10946  -1830  -1231  -1064       C  
ATOM     48  CG  LEU A  41       0.684  -3.615  -9.668  1.00 84.82           C  
ANISOU   48  CG  LEU A  41    11682   9604  10941  -1449  -1257  -1222       C  
ATOM     49  CD1 LEU A  41       0.863  -2.686 -10.856  1.00 82.66           C  
ANISOU   49  CD1 LEU A  41    11233   9703  10473  -1206  -1167  -1345       C  
ATOM     50  CD2 LEU A  41       1.708  -3.304  -8.588  1.00 84.95           C  
ANISOU   50  CD2 LEU A  41    11768   9527  10981  -1340  -1134  -1042       C  
ATOM     51  N   THR A  42      -3.447  -4.187  -7.587  1.00 91.95           N  
ANISOU   51  N   THR A  42    12247  10603  12085  -2760  -1237   -778       N  
ATOM     52  CA  THR A  42      -4.651  -3.758  -6.883  1.00 87.42           C  
ANISOU   52  CA  THR A  42    11395  10312  11509  -3092  -1095   -650       C  
ATOM     53  C   THR A  42      -4.741  -4.405  -5.507  1.00 89.21           C  
ANISOU   53  C   THR A  42    11759  10370  11767  -3467  -1059   -402       C  
ATOM     54  O   THR A  42      -5.141  -3.757  -4.533  1.00 90.48           O  
ANISOU   54  O   THR A  42    11720  10805  11853  -3617   -841   -252       O  
ATOM     55  CB  THR A  42      -5.894  -4.085  -7.708  1.00 81.63           C  
ANISOU   55  CB  THR A  42    10483   9703  10829  -3302  -1229   -812       C  
ATOM     56  OG1 THR A  42      -5.719  -3.600  -9.045  1.00 80.89           O  
ANISOU   56  OG1 THR A  42    10326   9737  10673  -2956  -1306  -1030       O  
ATOM     57  CG2 THR A  42      -7.122  -3.427  -7.095  1.00 73.78           C  
ANISOU   57  CG2 THR A  42     9102   9107   9822  -3566  -1057   -743       C  
ATOM     58  N   LEU A  43      -4.372  -5.685  -5.408  1.00 89.32           N  
ANISOU   58  N   LEU A  43    12123   9933  11882  -3624  -1291   -363       N  
ATOM     59  CA  LEU A  43      -4.291  -6.324  -4.100  1.00 89.41           C  
ANISOU   59  CA  LEU A  43    12339   9733  11900  -3975  -1300    -78       C  
ATOM     60  C   LEU A  43      -3.297  -5.599  -3.203  1.00 85.76           C  
ANISOU   60  C   LEU A  43    11923   9332  11330  -3737  -1117     75       C  
ATOM     61  O   LEU A  43      -3.540  -5.429  -2.003  1.00 86.73           O  
ANISOU   61  O   LEU A  43    12007   9591  11355  -4009   -965    311       O  
ATOM     62  CB  LEU A  43      -3.907  -7.795  -4.254  1.00 92.73           C  
ANISOU   62  CB  LEU A  43    13182   9571  12480  -4106  -1657    -74       C  
ATOM     63  N   LEU A  44      -2.173  -5.155  -3.773  1.00 83.60           N  
ANISOU   63  N   LEU A  44    11715   8995  11055  -3246  -1124    -66       N  
ATOM     64  CA  LEU A  44      -1.214  -4.375  -3.000  1.00 85.11           C  
ANISOU   64  CA  LEU A  44    11914   9267  11155  -3006   -957     53       C  
ATOM     65  C   LEU A  44      -1.839  -3.078  -2.502  1.00 85.13           C  
ANISOU   65  C   LEU A  44    11557   9754  11035  -3039   -660    109       C  
ATOM     66  O   LEU A  44      -1.633  -2.688  -1.347  1.00 86.93           O  
ANISOU   66  O   LEU A  44    11776  10082  11172  -3118   -515    286       O  
ATOM     67  CB  LEU A  44       0.031  -4.082  -3.838  1.00 87.56           C  
ANISOU   67  CB  LEU A  44    12295   9491  11483  -2502  -1005   -135       C  
ATOM     68  CG  LEU A  44       1.048  -3.125  -3.207  1.00 86.61           C  
ANISOU   68  CG  LEU A  44    12129   9496  11281  -2230   -831    -46       C  
ATOM     69  CD1 LEU A  44       1.618  -3.719  -1.930  1.00 87.91           C  
ANISOU   69  CD1 LEU A  44    12554   9391  11458  -2363   -905    175       C  
ATOM     70  CD2 LEU A  44       2.164  -2.764  -4.177  1.00 83.34           C  
ANISOU   70  CD2 LEU A  44    11712   9091  10864  -1783   -849   -246       C  
ATOM     71  N   ILE A  45      -2.611  -2.400  -3.356  1.00 82.86           N  
ANISOU   71  N   ILE A  45    10974   9766  10745  -2965   -594    -59       N  
ATOM     72  CA  ILE A  45      -3.287  -1.172  -2.940  1.00 83.78           C  
ANISOU   72  CA  ILE A  45    10732  10317  10784  -2961   -364    -56       C  
ATOM     73  C   ILE A  45      -4.154  -1.429  -1.715  1.00 85.75           C  
ANISOU   73  C   ILE A  45    10876  10734  10969  -3402   -243     98       C  
ATOM     74  O   ILE A  45      -4.169  -0.633  -0.767  1.00 85.46           O  
ANISOU   74  O   ILE A  45    10685  10954  10832  -3395    -44    165       O  
ATOM     75  CB  ILE A  45      -4.118  -0.594  -4.101  1.00 80.09           C  
ANISOU   75  CB  ILE A  45     9986  10096  10350  -2847   -391   -260       C  
ATOM     76  CG1 ILE A  45      -3.232  -0.296  -5.309  1.00 82.72           C  
ANISOU   76  CG1 ILE A  45    10426  10322  10681  -2446   -492   -386       C  
ATOM     77  CG2 ILE A  45      -4.845   0.666  -3.657  1.00 71.03           C  
ANISOU   77  CG2 ILE A  45     8464   9363   9163  -2807   -205   -292       C  
ATOM     78  CD1 ILE A  45      -3.998   0.221  -6.511  1.00 85.25           C  
ANISOU   78  CD1 ILE A  45    10525  10865  11002  -2340   -563   -559       C  
ATOM     79  N   ALA A  46      -4.887  -2.544  -1.711  1.00 89.24           N  
ANISOU   79  N   ALA A  46    11398  11053  11455  -3812   -363    150       N  
ATOM     80  CA  ALA A  46      -5.719  -2.875  -0.560  1.00 84.99           C  
ANISOU   80  CA  ALA A  46    10762  10712  10819  -4309   -240    325       C  
ATOM     81  C   ALA A  46      -4.868  -3.120   0.678  1.00 86.02           C  
ANISOU   81  C   ALA A  46    11172  10680  10833  -4395   -199    583       C  
ATOM     82  O   ALA A  46      -5.201  -2.653   1.773  1.00 82.61           O  
ANISOU   82  O   ALA A  46    10575  10580  10232  -4584     19    688       O  
ATOM     83  CB  ALA A  46      -6.581  -4.096  -0.869  1.00 77.37           C  
ANISOU   83  CB  ALA A  46     9868   9590   9938  -4771   -418    360       C  
ATOM     84  N   VAL A  47      -3.758  -3.841   0.522  1.00 84.11           N  
ANISOU   84  N   VAL A  47    11343   9946  10669  -4238   -419    662       N  
ATOM     85  CA  VAL A  47      -2.894  -4.117   1.664  1.00 83.65           C  
ANISOU   85  CA  VAL A  47    11575   9696  10512  -4292   -436    908       C  
ATOM     86  C   VAL A  47      -2.272  -2.829   2.191  1.00 82.63           C  
ANISOU   86  C   VAL A  47    11279   9847  10269  -3948   -212    871       C  
ATOM     87  O   VAL A  47      -2.139  -2.644   3.406  1.00 89.41           O  
ANISOU   87  O   VAL A  47    12171  10845  10957  -4107    -91   1051       O  
ATOM     88  CB  VAL A  47      -1.826  -5.156   1.281  1.00 85.45           C  
ANISOU   88  CB  VAL A  47    12252   9322  10892  -4129   -768    941       C  
ATOM     89  CG1 VAL A  47      -0.873  -5.397   2.438  1.00 84.04           C  
ANISOU   89  CG1 VAL A  47    12375   8931  10627  -4135   -829   1190       C  
ATOM     90  CG2 VAL A  47      -2.490  -6.457   0.863  1.00 89.97           C  
ANISOU   90  CG2 VAL A  47    13015   9574  11594  -4506  -1029    979       C  
ATOM     91  N   ILE A  48      -1.893  -1.915   1.294  1.00 78.76           N  
ANISOU   91  N   ILE A  48    10618   9450   9859  -3495   -165    645       N  
ATOM     92  CA  ILE A  48      -1.320  -0.643   1.730  1.00 77.79           C  
ANISOU   92  CA  ILE A  48    10338   9559   9659  -3180     16    603       C  
ATOM     93  C   ILE A  48      -2.344   0.158   2.522  1.00 82.81           C  
ANISOU   93  C   ILE A  48    10623  10681  10158  -3375    261    582       C  
ATOM     94  O   ILE A  48      -2.025   0.749   3.560  1.00 85.46           O  
ANISOU   94  O   ILE A  48    10924  11187  10359  -3347    400    647       O  
ATOM     95  CB  ILE A  48      -0.797   0.158   0.525  1.00 76.69           C  
ANISOU   95  CB  ILE A  48    10090   9420   9628  -2722     -7    395       C  
ATOM     96  CG1 ILE A  48       0.350  -0.582  -0.162  1.00 81.09           C  
ANISOU   96  CG1 ILE A  48    10957   9571  10283  -2498   -216    373       C  
ATOM     97  CG2 ILE A  48      -0.339   1.535   0.969  1.00 73.83           C  
ANISOU   97  CG2 ILE A  48     9552   9290   9212  -2449    157    360       C  
ATOM     98  CD1 ILE A  48       0.859   0.105  -1.411  1.00 83.26           C  
ANISOU   98  CD1 ILE A  48    11128   9896  10613  -2110   -227    183       C  
ATOM     99  N   VAL A  49      -3.590   0.189   2.047  1.00 85.62           N  
ANISOU   99  N   VAL A  49    10696  11290  10545  -3560    309    458       N  
ATOM    100  CA  VAL A  49      -4.628   0.950   2.736  1.00 86.41           C  
ANISOU  100  CA  VAL A  49    10399  11901  10530  -3713    539    369       C  
ATOM    101  C   VAL A  49      -5.028   0.256   4.033  1.00 86.76           C  
ANISOU  101  C   VAL A  49    10505  12094  10367  -4215    646    582       C  
ATOM    102  O   VAL A  49      -5.154   0.896   5.083  1.00 84.97           O  
ANISOU  102  O   VAL A  49    10110  12216   9958  -4262    848    578       O  
ATOM    103  CB  VAL A  49      -5.837   1.166   1.811  1.00 85.12           C  
ANISOU  103  CB  VAL A  49     9887  11980  10477  -3747    531    151       C  
ATOM    104  CG1 VAL A  49      -7.004   1.745   2.592  1.00 88.42           C  
ANISOU  104  CG1 VAL A  49     9863  12953  10781  -3956    756     30       C  
ATOM    105  CG2 VAL A  49      -5.456   2.084   0.662  1.00 80.88           C  
ANISOU  105  CG2 VAL A  49     9274  11370  10087  -3251    439    -34       C  
ATOM    106  N   PHE A  50      -5.229  -1.063   3.980  1.00 87.95           N  
ANISOU  106  N   PHE A  50    10908  11980  10529  -4611    497    773       N  
ATOM    107  CA  PHE A  50      -5.635  -1.794   5.177  1.00 89.88           C  
ANISOU  107  CA  PHE A  50    11255  12333  10561  -5041    554   1009       C  
ATOM    108  C   PHE A  50      -4.604  -1.654   6.289  1.00 92.06           C  
ANISOU  108  C   PHE A  50    11792  12524  10663  -4962    580   1197       C  
ATOM    109  O   PHE A  50      -4.957  -1.394   7.445  1.00 93.62           O  
ANISOU  109  O   PHE A  50    11871  13085  10613  -5087    752   1242       O  
ATOM    110  CB  PHE A  50      -5.857  -3.269   4.846  1.00 88.37           C  
ANISOU  110  CB  PHE A  50    11370  11743  10463  -5313    300   1176       C  
ATOM    111  CG  PHE A  50      -6.166  -4.119   6.048  1.00 91.54           C  
ANISOU  111  CG  PHE A  50    11945  12184  10651  -5658    293   1438       C  
ATOM    112  CD1 PHE A  50      -7.465  -4.232   6.518  1.00 92.88           C  
ANISOU  112  CD1 PHE A  50    11823  12793  10672  -5976    452   1419       C  
ATOM    113  CD2 PHE A  50      -5.157  -4.805   6.708  1.00 90.81           C  
ANISOU  113  CD2 PHE A  50    12302  11702  10500  -5665    108   1698       C  
ATOM    114  CE1 PHE A  50      -7.752  -5.011   7.623  1.00 96.10           C  
ANISOU  114  CE1 PHE A  50    12394  13265  10853  -6335    441   1672       C  
ATOM    115  CE2 PHE A  50      -5.439  -5.583   7.816  1.00 94.85           C  
ANISOU  115  CE2 PHE A  50    12982  12260  10797  -6003     73   1952       C  
ATOM    116  CZ  PHE A  50      -6.737  -5.688   8.272  1.00 98.38           C  
ANISOU  116  CZ  PHE A  50    13146  13159  11074  -6358    245   1949       C  
ATOM    117  N   GLY A  51      -3.324  -1.822   5.959  1.00 89.17           N  
ANISOU  117  N   GLY A  51    11775  11692  10415  -4731    395   1283       N  
ATOM    118  CA  GLY A  51      -2.301  -1.796   6.988  1.00 84.51           C  
ANISOU  118  CA  GLY A  51    11458  10976   9676  -4664    370   1475       C  
ATOM    119  C   GLY A  51      -2.075  -0.415   7.573  1.00 79.23           C  
ANISOU  119  C   GLY A  51    10517  10705   8881  -4366    607   1313       C  
ATOM    120  O   GLY A  51      -1.800  -0.278   8.767  1.00 79.21           O  
ANISOU  120  O   GLY A  51    10593  10866   8639  -4497    694   1454       O  
ATOM    121  N   ASN A  52      -2.183   0.626   6.746  1.00 74.87           N  
ANISOU  121  N   ASN A  52     9661  10300   8487  -3969    686   1017       N  
ATOM    122  CA  ASN A  52      -1.869   1.971   7.213  1.00 72.04           C  
ANISOU  122  CA  ASN A  52     9081  10223   8066  -3641    847    847       C  
ATOM    123  C   ASN A  52      -3.057   2.680   7.841  1.00 76.56           C  
ANISOU  123  C   ASN A  52     9223  11393   8475  -3813   1107    674       C  
ATOM    124  O   ASN A  52      -2.860   3.566   8.681  1.00 76.05           O  
ANISOU  124  O   ASN A  52     9026  11599   8272  -3672   1243    574       O  
ATOM    125  CB  ASN A  52      -1.305   2.809   6.069  1.00 68.61           C  
ANISOU  125  CB  ASN A  52     8565   9624   7879  -3132    768    642       C  
ATOM    126  CG  ASN A  52       0.113   2.416   5.715  1.00 79.96           C  
ANISOU  126  CG  ASN A  52    10362  10592   9427  -2882    569    754       C  
ATOM    127  OD1 ASN A  52       1.065   2.835   6.370  1.00 77.35           O  
ANISOU  127  OD1 ASN A  52    10144  10206   9041  -2704    566    802       O  
ATOM    128  ND2 ASN A  52       0.261   1.600   4.681  1.00 80.13           N  
ANISOU  128  ND2 ASN A  52    10547  10294   9604  -2861    393    767       N  
ATOM    129  N   VAL A  53      -4.286   2.318   7.468  1.00 82.38           N  
ANISOU  129  N   VAL A  53     9715  12360   9224  -4106   1170    606       N  
ATOM    130  CA  VAL A  53      -5.441   2.817   8.209  1.00 86.81           C  
ANISOU  130  CA  VAL A  53     9853  13535   9597  -4309   1419    435       C  
ATOM    131  C   VAL A  53      -5.398   2.300   9.643  1.00 91.28           C  
ANISOU  131  C   VAL A  53    10607  14230   9845  -4566   1474    633       C  
ATOM    132  O   VAL A  53      -5.768   3.009  10.588  1.00 98.44           O  
ANISOU  132  O   VAL A  53    11273  15582  10548  -4528   1653    471       O  
ATOM    133  CB  VAL A  53      -6.751   2.433   7.494  1.00 83.17           C  
ANISOU  133  CB  VAL A  53     9126  13231   9243  -4473   1406    307       C  
ATOM    134  CG1 VAL A  53      -7.949   2.691   8.387  1.00 78.74           C  
ANISOU  134  CG1 VAL A  53     8217  13227   8475  -4616   1596    143       C  
ATOM    135  CG2 VAL A  53      -6.893   3.217   6.198  1.00 79.84           C  
ANISOU  135  CG2 VAL A  53     8453  12777   9107  -4129   1341     45       C  
ATOM    136  N   LEU A  54      -4.923   1.065   9.827  1.00 86.53           N  
ANISOU  136  N   LEU A  54    10442  13233   9201  -4813   1292    968       N  
ATOM    137  CA  LEU A  54      -4.726   0.529  11.172  1.00 88.26           C  
ANISOU  137  CA  LEU A  54    10891  13520   9123  -5054   1288   1196       C  
ATOM    138  C   LEU A  54      -3.747   1.383  11.968  1.00 86.94           C  
ANISOU  138  C   LEU A  54    10787  13428   8817  -4810   1356   1171       C  
ATOM    139  O   LEU A  54      -4.002   1.722  13.130  1.00 94.33           O  
ANISOU  139  O   LEU A  54    11611  14759   9469  -4901   1496   1127       O  
ATOM    140  CB  LEU A  54      -4.224  -0.914  11.097  1.00 90.28           C  
ANISOU  140  CB  LEU A  54    11637  13240   9427  -5281   1006   1548       C  
ATOM    141  CG  LEU A  54      -5.198  -2.030  10.729  1.00 92.89           C  
ANISOU  141  CG  LEU A  54    11990  13500   9806  -5638    909   1650       C  
ATOM    142  CD1 LEU A  54      -4.459  -3.354  10.614  1.00 97.20           C  
ANISOU  142  CD1 LEU A  54    13055  13428  10449  -5757    575   1961       C  
ATOM    143  CD2 LEU A  54      -6.301  -2.128  11.763  1.00 96.43           C  
ANISOU  143  CD2 LEU A  54    12213  14478   9948  -5990   1090   1654       C  
ATOM    144  N   VAL A  55      -2.613   1.737  11.356  1.00 84.36           N  
ANISOU  144  N   VAL A  55    10638  12737   8678  -4508   1252   1188       N  
ATOM    145  CA  VAL A  55      -1.593   2.518  12.053  1.00 89.47           C  
ANISOU  145  CA  VAL A  55    11371  13417   9208  -4276   1291   1178       C  
ATOM    146  C   VAL A  55      -2.164   3.838  12.551  1.00 92.31           C  
ANISOU  146  C   VAL A  55    11279  14347   9446  -4112   1550    831       C  
ATOM    147  O   VAL A  55      -1.801   4.314  13.634  1.00 95.44           O  
ANISOU  147  O   VAL A  55    11689  14966   9606  -4066   1624    802       O  
ATOM    148  CB  VAL A  55      -0.374   2.741  11.133  1.00 85.96           C  
ANISOU  148  CB  VAL A  55    11134  12447   9082  -3803   1074   1151       C  
ATOM    149  CG1 VAL A  55       0.679   3.587  11.829  1.00 76.85           C  
ANISOU  149  CG1 VAL A  55    10045  11292   7864  -3476   1063   1092       C  
ATOM    150  CG2 VAL A  55       0.217   1.408  10.697  1.00 86.37           C  
ANISOU  150  CG2 VAL A  55    11619  11948   9251  -3934    799   1439       C  
ATOM    151  N   CYS A  56      -3.075   4.442  11.786  1.00 85.56           N  
ANISOU  151  N   CYS A  56    10018  13731   8759  -3998   1660    538       N  
ATOM    152  CA  CYS A  56      -3.627   5.737  12.175  1.00 80.56           C  
ANISOU  152  CA  CYS A  56     8941  13592   8075  -3762   1850    148       C  
ATOM    153  C   CYS A  56      -4.603   5.598  13.334  1.00 86.48           C  
ANISOU  153  C   CYS A  56     9514  14821   8522  -4005   1984     66       C  
ATOM    154  O   CYS A  56      -4.495   6.313  14.337  1.00 84.77           O  
ANISOU  154  O   CYS A  56     9186  14923   8102  -3899   2089   -102       O  
ATOM    155  CB  CYS A  56      -4.301   6.398  10.975  1.00 67.26           C  
ANISOU  155  CB  CYS A  56     6920  11917   6720  -3468   1818   -150       C  
ATOM    156  SG  CYS A  56      -3.139   6.859   9.688  1.00 71.11           S  
ANISOU  156  SG  CYS A  56     7652  11761   7605  -2939   1540   -134       S  
ATOM    157  N   MET A  57      -5.565   4.680  13.217  1.00 89.30           N  
ANISOU  157  N   MET A  57     9839  15250   8838  -4343   1978    170       N  
ATOM    158  CA  MET A  57      -6.547   4.508  14.283  1.00 99.11           C  
ANISOU  158  CA  MET A  57    10893  16987   9777  -4621   2115     99       C  
ATOM    159  C   MET A  57      -5.891   4.028  15.570  1.00100.31           C  
ANISOU  159  C   MET A  57    11370  17145   9601  -4843   2094    365       C  
ATOM    160  O   MET A  57      -6.282   4.448  16.665  1.00109.98           O  
ANISOU  160  O   MET A  57    12410  18838  10541  -4909   2235    210       O  
ATOM    161  CB  MET A  57      -7.633   3.529  13.845  1.00106.16           C  
ANISOU  161  CB  MET A  57    11719  17920  10695  -4975   2095    198       C  
ATOM    162  CG  MET A  57      -8.458   4.012  12.672  1.00104.93           C  
ANISOU  162  CG  MET A  57    11195  17843  10830  -4777   2113    -94       C  
ATOM    163  SD  MET A  57      -9.729   2.811  12.239  1.00106.23           S  
ANISOU  163  SD  MET A  57    11291  18073  11000  -5226   2085     28       S  
ATOM    164  CE  MET A  57      -8.718   1.360  11.965  1.00104.77           C  
ANISOU  164  CE  MET A  57    11736  17203  10870  -5491   1838    545       C  
ATOM    165  N   ALA A  58      -4.891   3.151  15.458  1.00 91.70           N  
ANISOU  165  N   ALA A  58    10761  15535   8547  -4945   1896    749       N  
ATOM    166  CA  ALA A  58      -4.253   2.590  16.647  1.00 94.86           C  
ANISOU  166  CA  ALA A  58    11502  15887   8653  -5159   1819   1033       C  
ATOM    167  C   ALA A  58      -3.578   3.673  17.478  1.00 93.98           C  
ANISOU  167  C   ALA A  58    11323  16005   8380  -4887   1912    851       C  
ATOM    168  O   ALA A  58      -3.795   3.769  18.691  1.00 97.13           O  
ANISOU  168  O   ALA A  58    11671  16787   8447  -5049   2002    828       O  
ATOM    169  CB  ALA A  58      -3.240   1.521  16.244  1.00 92.30           C  
ANISOU  169  CB  ALA A  58    11700  14899   8471  -5223   1532   1429       C  
ATOM    170  N   VAL A  59      -2.740   4.492  16.841  1.00 96.30           N  
ANISOU  170  N   VAL A  59    11619  16077   8895  -4483   1883    717       N  
ATOM    171  CA  VAL A  59      -2.102   5.595  17.551  1.00 91.92           C  
ANISOU  171  CA  VAL A  59    10983  15733   8211  -4197   1959    504       C  
ATOM    172  C   VAL A  59      -3.144   6.585  18.045  1.00 91.74           C  
ANISOU  172  C   VAL A  59    10460  16322   8077  -4097   2177     56       C  
ATOM    173  O   VAL A  59      -2.990   7.184  19.117  1.00 99.07           O  
ANISOU  173  O   VAL A  59    11313  17573   8756  -4030   2251   -105       O  
ATOM    174  CB  VAL A  59      -1.062   6.271  16.638  1.00 84.96           C  
ANISOU  174  CB  VAL A  59    10179  14491   7608  -3805   1881    441       C  
ATOM    175  CG1 VAL A  59      -0.446   7.484  17.318  1.00 88.37           C  
ANISOU  175  CG1 VAL A  59    10505  15150   7923  -3491   1949    173       C  
ATOM    176  CG2 VAL A  59       0.009   5.267  16.235  1.00 77.23           C  
ANISOU  176  CG2 VAL A  59     9704  12913   6729  -3889   1637    864       C  
ATOM    177  N   SER A  60      -4.229   6.759  17.291  1.00 95.26           N  
ANISOU  177  N   SER A  60    10557  16933   8706  -4072   2257   -169       N  
ATOM    178  CA  SER A  60      -5.247   7.733  17.658  1.00 98.05           C  
ANISOU  178  CA  SER A  60    10416  17831   9007  -3917   2417   -638       C  
ATOM    179  C   SER A  60      -6.057   7.307  18.875  1.00104.36           C  
ANISOU  179  C   SER A  60    11113  19121   9420  -4286   2535   -633       C  
ATOM    180  O   SER A  60      -6.732   8.148  19.479  1.00107.43           O  
ANISOU  180  O   SER A  60    11125  20003   9691  -4157   2661  -1033       O  
ATOM    181  CB  SER A  60      -6.183   7.974  16.473  1.00 97.14           C  
ANISOU  181  CB  SER A  60     9973  17730   9205  -3784   2427   -864       C  
ATOM    182  OG  SER A  60      -7.148   8.967  16.770  1.00 99.99           O  
ANISOU  182  OG  SER A  60     9859  18573   9559  -3574   2531  -1349       O  
ATOM    183  N   ARG A  61      -6.003   6.030  19.255  1.00 98.78           N  
ANISOU  183  N   ARG A  61    10729  18286   8518  -4738   2478   -202       N  
ATOM    184  CA  ARG A  61      -6.880   5.512  20.291  1.00103.46           C  
ANISOU  184  CA  ARG A  61    11212  19353   8745  -5156   2589   -162       C  
ATOM    185  C   ARG A  61      -6.159   4.772  21.410  1.00107.55           C  
ANISOU  185  C   ARG A  61    12131  19803   8928  -5464   2513    219       C  
ATOM    186  O   ARG A  61      -6.808   4.395  22.392  1.00117.52           O  
ANISOU  186  O   ARG A  61    13311  21498   9842  -5828   2609    262       O  
ATOM    187  CB  ARG A  61      -7.937   4.590  19.664  1.00104.53           C  
ANISOU  187  CB  ARG A  61    11265  19502   8951  -5497   2593    -37       C  
ATOM    188  CG  ARG A  61      -8.730   5.267  18.557  1.00 96.67           C  
ANISOU  188  CG  ARG A  61     9865  18588   8277  -5209   2647   -407       C  
ATOM    189  CD  ARG A  61     -10.016   4.534  18.248  1.00108.57           C  
ANISOU  189  CD  ARG A  61    11174  20320   9758  -5564   2702   -387       C  
ATOM    190  NE  ARG A  61      -9.801   3.362  17.409  1.00109.71           N  
ANISOU  190  NE  ARG A  61    11662  19943  10079  -5797   2536     11       N  
ATOM    191  CZ  ARG A  61     -10.778   2.566  16.987  1.00115.93           C  
ANISOU  191  CZ  ARG A  61    12357  20800  10890  -6123   2537     93       C  
ATOM    192  NH1 ARG A  61     -12.034   2.820  17.330  1.00116.46           N  
ANISOU  192  NH1 ARG A  61    11988  21459  10801  -6264   2710   -185       N  
ATOM    193  NH2 ARG A  61     -10.501   1.519  16.223  1.00119.11           N  
ANISOU  193  NH2 ARG A  61    13096  20686  11475  -6303   2354    434       N  
ATOM    194  N   GLU A  62      -4.853   4.558  21.301  1.00 96.97           N  
ANISOU  194  N   GLU A  62    11215  17953   7675  -5333   2333    491       N  
ATOM    195  CA  GLU A  62      -4.083   3.859  22.320  1.00101.43           C  
ANISOU  195  CA  GLU A  62    12192  18393   7956  -5580   2207    858       C  
ATOM    196  C   GLU A  62      -3.184   4.851  23.046  1.00102.22           C  
ANISOU  196  C   GLU A  62    12307  18603   7928  -5257   2227    678       C  
ATOM    197  O   GLU A  62      -2.426   5.591  22.409  1.00 92.57           O  
ANISOU  197  O   GLU A  62    11100  17116   6955  -4842   2178    531       O  
ATOM    198  CB  GLU A  62      -3.246   2.737  21.703  1.00100.84           C  
ANISOU  198  CB  GLU A  62    12621  17618   8074  -5678   1928   1315       C  
ATOM    199  N   LYS A  63      -3.269   4.854  24.378  1.00108.00           N  
ANISOU  199  N   LYS A  63    13040  19738   8259  -5463   2293    691       N  
ATOM    200  CA  LYS A  63      -2.467   5.770  25.183  1.00106.16           C  
ANISOU  200  CA  LYS A  63    12820  19652   7864  -5180   2305    504       C  
ATOM    201  C   LYS A  63      -0.976   5.535  24.970  1.00 98.83           C  
ANISOU  201  C   LYS A  63    12367  18125   7059  -4996   2054    800       C  
ATOM    202  O   LYS A  63      -0.243   6.439  24.552  1.00 90.24           O  
ANISOU  202  O   LYS A  63    11250  16879   6157  -4571   2024    584       O  
ATOM    203  CB  LYS A  63      -2.833   5.616  26.660  1.00114.28           C  
ANISOU  203  CB  LYS A  63    13807  21206   8408  -5502   2401    526       C  
ATOM    204  N   ALA A  64      -0.510   4.312  25.239  1.00108.15           N  
ANISOU  204  N   ALA A  64    13988  18956   8148  -5308   1844   1286       N  
ATOM    205  CA  ALA A  64       0.917   4.011  25.200  1.00103.75           C  
ANISOU  205  CA  ALA A  64    13892  17853   7678  -5142   1563   1569       C  
ATOM    206  C   ALA A  64       1.513   4.169  23.805  1.00 99.33           C  
ANISOU  206  C   ALA A  64    13405  16779   7558  -4812   1452   1552       C  
ATOM    207  O   ALA A  64       2.735   4.041  23.649  1.00 84.58           O  
ANISOU  207  O   ALA A  64    11875  14464   5799  -4615   1215   1732       O  
ATOM    208  CB  ALA A  64       1.164   2.590  25.719  1.00103.60           C  
ANISOU  208  CB  ALA A  64    14310  17538   7516  -5540   1320   2073       C  
ATOM    209  N   LEU A  65       0.685   4.450  22.798  1.00 91.85           N  
ANISOU  209  N   LEU A  65    12140  15902   6858  -4745   1606   1334       N  
ATOM    210  CA  LEU A  65       1.126   4.676  21.429  1.00 92.45           C  
ANISOU  210  CA  LEU A  65    12233  15560   7334  -4450   1535   1288       C  
ATOM    211  C   LEU A  65       1.071   6.143  21.021  1.00 91.55           C  
ANISOU  211  C   LEU A  65    11741  15700   7344  -4047   1715    824       C  
ATOM    212  O   LEU A  65       1.216   6.447  19.835  1.00 98.95           O  
ANISOU  212  O   LEU A  65    12606  16387   8603  -3825   1705    736       O  
ATOM    213  CB  LEU A  65       0.282   3.842  20.465  1.00 91.67           C  
ANISOU  213  CB  LEU A  65    12087  15284   7459  -4662   1529   1402       C  
ATOM    214  CG  LEU A  65       0.533   2.337  20.472  1.00 96.52           C  
ANISOU  214  CG  LEU A  65    13133  15448   8091  -4973   1266   1854       C  
ATOM    215  CD1 LEU A  65      -0.389   1.627  19.490  1.00101.66           C  
ANISOU  215  CD1 LEU A  65    13694  15972   8962  -5162   1269   1895       C  
ATOM    216  CD2 LEU A  65       1.987   2.059  20.143  1.00 88.49           C  
ANISOU  216  CD2 LEU A  65    12531  13837   7256  -4733    974   2071       C  
ATOM    217  N   GLN A  66       0.870   7.056  21.966  1.00 97.64           N  
ANISOU  217  N   GLN A  66    12271  16951   7878  -3940   1858    509       N  
ATOM    218  CA  GLN A  66       0.729   8.476  21.643  1.00 91.59           C  
ANISOU  218  CA  GLN A  66    11125  16421   7256  -3531   1991      9       C  
ATOM    219  C   GLN A  66       2.014   9.220  22.003  1.00 88.27           C  
ANISOU  219  C   GLN A  66    10883  15873   6783  -3219   1872    -76       C  
ATOM    220  O   GLN A  66       2.081  10.015  22.940  1.00 95.43           O  
ANISOU  220  O   GLN A  66    11654  17116   7488  -3077   1921   -364       O  
ATOM    221  CB  GLN A  66      -0.488   9.060  22.354  1.00 94.21           C  
ANISOU  221  CB  GLN A  66    11011  17366   7418  -3569   2200   -377       C  
ATOM    222  CG  GLN A  66      -1.806   8.615  21.747  1.00 90.38           C  
ANISOU  222  CG  GLN A  66    10255  17032   7053  -3778   2313   -412       C  
ATOM    223  CD  GLN A  66      -3.010   9.067  22.544  1.00 98.45           C  
ANISOU  223  CD  GLN A  66    10853  18690   7865  -3861   2497   -767       C  
ATOM    224  OE1 GLN A  66      -2.887   9.506  23.689  1.00102.35           O  
ANISOU  224  OE1 GLN A  66    11295  19524   8070  -3847   2548   -921       O  
ATOM    225  NE2 GLN A  66      -4.187   8.960  21.941  1.00101.41           N  
ANISOU  225  NE2 GLN A  66    10914  19243   8376  -3945   2588   -913       N  
ATOM    226  N   THR A  67       3.049   8.942  21.221  1.00 81.40           N  
ANISOU  226  N   THR A  67    10313  14420   6193  -3058   1648    159       N  
ATOM    227  CA  THR A  67       4.366   9.523  21.416  1.00 80.16           C  
ANISOU  227  CA  THR A  67    10341  13928   6189  -2690   1412    112       C  
ATOM    228  C   THR A  67       4.724  10.396  20.219  1.00 81.81           C  
ANISOU  228  C   THR A  67    10385  13739   6959  -2223   1303   -122       C  
ATOM    229  O   THR A  67       4.047  10.388  19.187  1.00 83.11           O  
ANISOU  229  O   THR A  67    10366  13821   7392  -2189   1372   -182       O  
ATOM    230  CB  THR A  67       5.424   8.430  21.618  1.00 74.28           C  
ANISOU  230  CB  THR A  67    10089  12752   5384  -2838   1150    588       C  
ATOM    231  OG1 THR A  67       5.732   7.823  20.359  1.00 77.15           O  
ANISOU  231  OG1 THR A  67    10579  12565   6169  -2749   1000    784       O  
ATOM    232  CG2 THR A  67       4.909   7.358  22.566  1.00 76.90           C  
ANISOU  232  CG2 THR A  67    10631  13398   5190  -3391   1228    928       C  
ATOM    233  N   THR A  68       5.803  11.165  20.370  1.00 86.60           N  
ANISOU  233  N   THR A  68    11062  14111   7731  -1884   1119   -244       N  
ATOM    234  CA  THR A  68       6.274  11.984  19.259  1.00 81.90           C  
ANISOU  234  CA  THR A  68    10353  13120   7646  -1492    990   -405       C  
ATOM    235  C   THR A  68       6.614  11.116  18.055  1.00 76.38           C  
ANISOU  235  C   THR A  68     9828  11956   7236  -1519    883    -94       C  
ATOM    236  O   THR A  68       6.157  11.379  16.939  1.00 74.99           O  
ANISOU  236  O   THR A  68     9479  11652   7360  -1401    915   -182       O  
ATOM    237  CB  THR A  68       7.490  12.816  19.681  1.00 80.77           C  
ANISOU  237  CB  THR A  68    10291  12786   7611  -1198    788   -526       C  
ATOM    238  OG1 THR A  68       8.582  11.948  20.014  1.00 75.97           O  
ANISOU  238  OG1 THR A  68    10037  11917   6911  -1290    604   -182       O  
ATOM    239  CG2 THR A  68       7.155  13.692  20.878  1.00 83.25           C  
ANISOU  239  CG2 THR A  68    10436  13561   7636  -1147    872   -884       C  
ATOM    240  N   THR A  69       7.412  10.066  18.270  1.00 78.37           N  
ANISOU  240  N   THR A  69    10426  11955   7395  -1662    733    255       N  
ATOM    241  CA  THR A  69       7.811   9.195  17.168  1.00 78.88           C  
ANISOU  241  CA  THR A  69    10662  11578   7732  -1656    605    503       C  
ATOM    242  C   THR A  69       6.596   8.584  16.482  1.00 78.27           C  
ANISOU  242  C   THR A  69    10482  11594   7664  -1890    759    558       C  
ATOM    243  O   THR A  69       6.522   8.550  15.247  1.00 73.15           O  
ANISOU  243  O   THR A  69     9763  10702   7330  -1761    732    539       O  
ATOM    244  CB  THR A  69       8.748   8.097  17.676  1.00 76.37           C  
ANISOU  244  CB  THR A  69    10733  11000   7285  -1777    388    839       C  
ATOM    245  OG1 THR A  69       9.982   8.680  18.112  1.00 72.19           O  
ANISOU  245  OG1 THR A  69    10268  10338   6821  -1513    212    771       O  
ATOM    246  CG2 THR A  69       9.035   7.083  16.582  1.00 74.02           C  
ANISOU  246  CG2 THR A  69    10604  10273   7247  -1776    252   1050       C  
ATOM    247  N   ASN A  70       5.625   8.114  17.269  1.00 82.86           N  
ANISOU  247  N   ASN A  70    11039  12561   7884  -2256    925    618       N  
ATOM    248  CA  ASN A  70       4.436   7.496  16.698  1.00 81.91           C  
ANISOU  248  CA  ASN A  70    10800  12565   7757  -2530   1069    672       C  
ATOM    249  C   ASN A  70       3.562   8.494  15.947  1.00 81.00           C  
ANISOU  249  C   ASN A  70    10269  12649   7860  -2327   1221    314       C  
ATOM    250  O   ASN A  70       2.805   8.084  15.063  1.00 74.10           O  
ANISOU  250  O   ASN A  70     9290  11736   7128  -2431   1271    335       O  
ATOM    251  CB  ASN A  70       3.629   6.801  17.798  1.00 79.20           C  
ANISOU  251  CB  ASN A  70    10505  12647   6942  -3020   1221    832       C  
ATOM    252  CG  ASN A  70       4.333   5.581  18.348  1.00 78.28           C  
ANISOU  252  CG  ASN A  70    10856  12250   6638  -3286   1014   1268       C  
ATOM    253  OD1 ASN A  70       5.224   5.030  17.706  1.00 74.09           O  
ANISOU  253  OD1 ASN A  70    10588  11183   6379  -3127    762   1443       O  
ATOM    254  ND2 ASN A  70       3.941   5.152  19.542  1.00 73.15           N  
ANISOU  254  ND2 ASN A  70    10308  11972   5512  -3692   1103   1439       N  
ATOM    255  N   TYR A  71       3.640   9.786  16.274  1.00 84.07           N  
ANISOU  255  N   TYR A  71    10427  13227   8291  -2033   1261    -20       N  
ATOM    256  CA  TYR A  71       2.933  10.782  15.475  1.00 77.80           C  
ANISOU  256  CA  TYR A  71     9275  12516   7768  -1780   1321   -352       C  
ATOM    257  C   TYR A  71       3.632  11.001  14.143  1.00 70.85           C  
ANISOU  257  C   TYR A  71     8477  11134   7310  -1497   1135   -290       C  
ATOM    258  O   TYR A  71       2.978  11.216  13.117  1.00 65.56           O  
ANISOU  258  O   TYR A  71     7626  10422   6864  -1416   1148   -386       O  
ATOM    259  CB  TYR A  71       2.809  12.094  16.246  1.00 74.68           C  
ANISOU  259  CB  TYR A  71     8632  12431   7314  -1540   1370   -746       C  
ATOM    260  CG  TYR A  71       1.783  12.035  17.350  1.00 80.29           C  
ANISOU  260  CG  TYR A  71     9123  13772   7611  -1796   1612   -924       C  
ATOM    261  CD1 TYR A  71       0.690  11.189  17.253  1.00 82.22           C  
ANISOU  261  CD1 TYR A  71     9248  14311   7681  -2164   1796   -825       C  
ATOM    262  CD2 TYR A  71       1.912  12.814  18.492  1.00 84.10           C  
ANISOU  262  CD2 TYR A  71     9504  14589   7861  -1688   1658  -1202       C  
ATOM    263  CE1 TYR A  71      -0.250  11.123  18.258  1.00 91.89           C  
ANISOU  263  CE1 TYR A  71    10236  16183   8495  -2441   2045   -986       C  
ATOM    264  CE2 TYR A  71       0.976  12.756  19.503  1.00 85.39           C  
ANISOU  264  CE2 TYR A  71     9439  15406   7599  -1932   1905  -1392       C  
ATOM    265  CZ  TYR A  71      -0.103  11.907  19.381  1.00 94.33           C  
ANISOU  265  CZ  TYR A  71    10434  16859   8548  -2320   2110  -1275       C  
ATOM    266  OH  TYR A  71      -1.045  11.839  20.381  1.00 99.85           O  
ANISOU  266  OH  TYR A  71    10911  18103   8926  -2541   2275  -1429       O  
ATOM    267  N   LEU A  72       4.963  10.950  14.139  1.00 66.28           N  
ANISOU  267  N   LEU A  72     8155  10205   6825  -1355    960   -134       N  
ATOM    268  CA  LEU A  72       5.688  10.938  12.880  1.00 65.47           C  
ANISOU  268  CA  LEU A  72     8142   9678   7057  -1158    810    -34       C  
ATOM    269  C   LEU A  72       5.520   9.612  12.156  1.00 66.26           C  
ANISOU  269  C   LEU A  72     8411   9590   7173  -1363    790    218       C  
ATOM    270  O   LEU A  72       5.755   9.545  10.947  1.00 70.26           O  
ANISOU  270  O   LEU A  72     8925   9843   7928  -1232    713    248       O  
ATOM    271  CB  LEU A  72       7.166  11.237  13.129  1.00 68.98           C  
ANISOU  271  CB  LEU A  72     8763   9860   7585   -964    640     32       C  
ATOM    272  CG  LEU A  72       7.464  12.668  13.586  1.00 71.02           C  
ANISOU  272  CG  LEU A  72     8861  10200   7924   -721    600   -231       C  
ATOM    273  CD1 LEU A  72       8.795  12.745  14.308  1.00 68.45           C  
ANISOU  273  CD1 LEU A  72     8719   9732   7557   -638    454   -157       C  
ATOM    274  CD2 LEU A  72       7.449  13.618  12.399  1.00 69.98           C  
ANISOU  274  CD2 LEU A  72     8565   9884   8138   -488    531   -351       C  
ATOM    275  N   ILE A  73       5.112   8.562  12.866  1.00 69.01           N  
ANISOU  275  N   ILE A  73     8906  10062   7254  -1697    844    397       N  
ATOM    276  CA  ILE A  73       4.844   7.288  12.214  1.00 67.68           C  
ANISOU  276  CA  ILE A  73     8907   9691   7118  -1917    795    618       C  
ATOM    277  C   ILE A  73       3.522   7.340  11.460  1.00 71.94           C  
ANISOU  277  C   ILE A  73     9183  10422   7728  -2023    929    489       C  
ATOM    278  O   ILE A  73       3.411   6.809  10.350  1.00 75.02           O  
ANISOU  278  O   ILE A  73     9617  10582   8307  -2015    856    546       O  
ATOM    279  CB  ILE A  73       4.880   6.148  13.249  1.00 69.17           C  
ANISOU  279  CB  ILE A  73     9379   9898   7006  -2275    759    894       C  
ATOM    280  CG1 ILE A  73       6.327   5.743  13.542  1.00 66.13           C  
ANISOU  280  CG1 ILE A  73     9319   9150   6659  -2128    522   1069       C  
ATOM    281  CG2 ILE A  73       4.072   4.944  12.777  1.00 68.47           C  
ANISOU  281  CG2 ILE A  73     9386   9730   6900  -2615    755   1076       C  
ATOM    282  CD1 ILE A  73       6.453   4.548  14.461  1.00 67.07           C  
ANISOU  282  CD1 ILE A  73     9782   9188   6514  -2462    402   1387       C  
ATOM    283  N   VAL A  74       2.507   7.996  12.029  1.00 70.79           N  
ANISOU  283  N   VAL A  74     8739  10720   7436  -2102   1115    280       N  
ATOM    284  CA  VAL A  74       1.244   8.128  11.308  1.00 74.58           C  
ANISOU  284  CA  VAL A  74     8921  11407   8009  -2166   1221    118       C  
ATOM    285  C   VAL A  74       1.392   9.116  10.161  1.00 73.54           C  
ANISOU  285  C   VAL A  74     8633  11099   8211  -1776   1127    -73       C  
ATOM    286  O   VAL A  74       0.708   8.995   9.137  1.00 75.63           O  
ANISOU  286  O   VAL A  74     8769  11334   8631  -1776   1112   -121       O  
ATOM    287  CB  VAL A  74       0.095   8.527  12.256  1.00 73.62           C  
ANISOU  287  CB  VAL A  74     8477  11862   7633  -2350   1446    -95       C  
ATOM    288  CG1 VAL A  74       0.133   7.692  13.523  1.00 69.23           C  
ANISOU  288  CG1 VAL A  74     8110  11512   6684  -2747   1535    127       C  
ATOM    289  CG2 VAL A  74       0.126  10.011  12.581  1.00 69.08           C  
ANISOU  289  CG2 VAL A  74     7641  11478   7130  -1988   1471   -451       C  
ATOM    290  N   SER A  75       2.276  10.106  10.306  1.00 69.43           N  
ANISOU  290  N   SER A  75     8129  10455   7797  -1464   1043   -169       N  
ATOM    291  CA  SER A  75       2.644  10.933   9.164  1.00 66.75           C  
ANISOU  291  CA  SER A  75     7729   9871   7764  -1146    912   -253       C  
ATOM    292  C   SER A  75       3.278  10.082   8.075  1.00 68.29           C  
ANISOU  292  C   SER A  75     8151   9714   8082  -1158    801    -30       C  
ATOM    293  O   SER A  75       3.025  10.291   6.882  1.00 67.91           O  
ANISOU  293  O   SER A  75     8025   9564   8214  -1048    739    -65       O  
ATOM    294  CB  SER A  75       3.595  12.044   9.605  1.00 65.59           C  
ANISOU  294  CB  SER A  75     7599   9627   7697   -876    823   -350       C  
ATOM    295  OG  SER A  75       4.148  12.722   8.492  1.00 65.64           O  
ANISOU  295  OG  SER A  75     7609   9355   7975   -636    678   -344       O  
ATOM    296  N   LEU A  76       4.099   9.107   8.470  1.00 69.61           N  
ANISOU  296  N   LEU A  76     8600   9702   8145  -1281    755    185       N  
ATOM    297  CA  LEU A  76       4.653   8.169   7.503  1.00 70.39           C  
ANISOU  297  CA  LEU A  76     8904   9490   8352  -1284    641    344       C  
ATOM    298  C   LEU A  76       3.555   7.304   6.898  1.00 71.56           C  
ANISOU  298  C   LEU A  76     9015   9685   8488  -1514    675    369       C  
ATOM    299  O   LEU A  76       3.587   6.994   5.700  1.00 67.72           O  
ANISOU  299  O   LEU A  76     8556   9030   8146  -1442    597    372       O  
ATOM    300  CB  LEU A  76       5.725   7.307   8.170  1.00 71.65           C  
ANISOU  300  CB  LEU A  76     9365   9437   8421  -1339    541    534       C  
ATOM    301  CG  LEU A  76       6.488   6.311   7.296  1.00 73.93           C  
ANISOU  301  CG  LEU A  76     9872   9386   8833  -1283    387    648       C  
ATOM    302  CD1 LEU A  76       7.050   6.993   6.057  1.00 66.82           C  
ANISOU  302  CD1 LEU A  76     8859   8395   8135  -1003    352    542       C  
ATOM    303  CD2 LEU A  76       7.598   5.643   8.104  1.00 66.32           C  
ANISOU  303  CD2 LEU A  76     9178   8218   7804  -1274    247    796       C  
ATOM    304  N   ALA A  77       2.567   6.918   7.708  1.00 76.17           N  
ANISOU  304  N   ALA A  77     9525  10531   8886  -1810    794    379       N  
ATOM    305  CA  ALA A  77       1.468   6.103   7.203  1.00 75.85           C  
ANISOU  305  CA  ALA A  77     9422  10562   8836  -2078    825    401       C  
ATOM    306  C   ALA A  77       0.603   6.875   6.217  1.00 76.40           C  
ANISOU  306  C   ALA A  77     9182  10781   9066  -1929    853    183       C  
ATOM    307  O   ALA A  77       0.034   6.277   5.295  1.00 74.94           O  
ANISOU  307  O   ALA A  77     8980  10529   8965  -2027    802    189       O  
ATOM    308  CB  ALA A  77       0.618   5.589   8.364  1.00 77.54           C  
ANISOU  308  CB  ALA A  77     9590  11086   8784  -2476    967    470       C  
ATOM    309  N   VAL A  78       0.484   8.192   6.395  1.00 72.57           N  
ANISOU  309  N   VAL A  78     8462  10479   8634  -1687    898    -17       N  
ATOM    310  CA  VAL A  78      -0.263   9.001   5.438  1.00 73.72           C  
ANISOU  310  CA  VAL A  78     8340  10714   8956  -1502    861   -213       C  
ATOM    311  C   VAL A  78       0.492   9.092   4.118  1.00 73.77           C  
ANISOU  311  C   VAL A  78     8495  10392   9143  -1286    699   -137       C  
ATOM    312  O   VAL A  78      -0.108   9.025   3.037  1.00 75.36           O  
ANISOU  312  O   VAL A  78     8606  10583   9444  -1265    631   -185       O  
ATOM    313  CB  VAL A  78      -0.556  10.391   6.030  1.00 69.67           C  
ANISOU  313  CB  VAL A  78     7563  10433   8477  -1281    899   -460       C  
ATOM    314  CG1 VAL A  78      -1.042  11.346   4.951  1.00 67.83           C  
ANISOU  314  CG1 VAL A  78     7129  10169   8475  -1016    769   -625       C  
ATOM    315  CG2 VAL A  78      -1.591  10.281   7.138  1.00 54.88           C  
ANISOU  315  CG2 VAL A  78     5447   9002   6402  -1505   1086   -609       C  
ATOM    316  N   ALA A  79       1.819   9.239   4.180  1.00 71.40           N  
ANISOU  316  N   ALA A  79     8408   9854   8865  -1136    637    -25       N  
ATOM    317  CA  ALA A  79       2.617   9.243   2.959  1.00 72.25           C  
ANISOU  317  CA  ALA A  79     8642   9715   9095   -969    515     48       C  
ATOM    318  C   ALA A  79       2.382   7.976   2.148  1.00 78.12           C  
ANISOU  318  C   ALA A  79     9512  10348   9824  -1122    472    118       C  
ATOM    319  O   ALA A  79       2.254   8.030   0.919  1.00 82.23           O  
ANISOU  319  O   ALA A  79    10005  10818  10420  -1035    394     87       O  
ATOM    320  CB  ALA A  79       4.097   9.398   3.301  1.00 67.24           C  
ANISOU  320  CB  ALA A  79     8191   8894   8464   -836    476    149       C  
ATOM    321  N   ASP A  80       2.306   6.826   2.820  1.00 70.96           N  
ANISOU  321  N   ASP A  80     8756   9392   8812  -1362    499    214       N  
ATOM    322  CA  ASP A  80       2.041   5.580   2.113  1.00 74.85           C  
ANISOU  322  CA  ASP A  80     9387   9736   9318  -1522    420    263       C  
ATOM    323  C   ASP A  80       0.578   5.468   1.707  1.00 70.40           C  
ANISOU  323  C   ASP A  80     8610   9377   8763  -1703    452    165       C  
ATOM    324  O   ASP A  80       0.275   4.919   0.641  1.00 75.04           O  
ANISOU  324  O   ASP A  80     9225   9874   9413  -1725    358    129       O  
ATOM    325  CB  ASP A  80       2.453   4.386   2.975  1.00 85.13           C  
ANISOU  325  CB  ASP A  80    10957  10859  10529  -1735    379    424       C  
ATOM    326  CG  ASP A  80       3.955   4.316   3.193  1.00 91.73           C  
ANISOU  326  CG  ASP A  80    12008  11459  11389  -1526    293    497       C  
ATOM    327  OD1 ASP A  80       4.707   4.814   2.326  1.00 90.12           O  
ANISOU  327  OD1 ASP A  80    11774  11187  11279  -1257    253    424       O  
ATOM    328  OD2 ASP A  80       4.383   3.762   4.231  1.00 93.76           O  
ANISOU  328  OD2 ASP A  80    12452  11616  11555  -1644    259    631       O  
ATOM    329  N   LEU A  81      -0.340   5.974   2.535  1.00 74.65           N  
ANISOU  329  N   LEU A  81     8912  10218   9233  -1827    580     91       N  
ATOM    330  CA  LEU A  81      -1.751   5.961   2.159  1.00 71.55           C  
ANISOU  330  CA  LEU A  81     8249  10074   8865  -1978    612    -40       C  
ATOM    331  C   LEU A  81      -2.001   6.765   0.893  1.00 74.65           C  
ANISOU  331  C   LEU A  81     8488  10471   9406  -1709    505   -178       C  
ATOM    332  O   LEU A  81      -2.886   6.418   0.105  1.00 69.21           O  
ANISOU  332  O   LEU A  81     7680   9851   8766  -1803    444   -254       O  
ATOM    333  CB  LEU A  81      -2.611   6.504   3.297  1.00 69.87           C  
ANISOU  333  CB  LEU A  81     7752  10250   8545  -2106    782   -153       C  
ATOM    334  CG  LEU A  81      -3.075   5.485   4.331  1.00 74.99           C  
ANISOU  334  CG  LEU A  81     8452  11043   8999  -2544    901    -27       C  
ATOM    335  CD1 LEU A  81      -3.852   6.179   5.437  1.00 74.69           C  
ANISOU  335  CD1 LEU A  81     8087  11477   8814  -2632   1099   -186       C  
ATOM    336  CD2 LEU A  81      -3.924   4.409   3.669  1.00 73.03           C  
ANISOU  336  CD2 LEU A  81     8197  10767   8785  -2854    842     14       C  
ATOM    337  N   LEU A  82      -1.237   7.838   0.678  1.00 69.87           N  
ANISOU  337  N   LEU A  82     7892   9789   8867  -1397    460   -196       N  
ATOM    338  CA  LEU A  82      -1.409   8.637  -0.529  1.00 65.99           C  
ANISOU  338  CA  LEU A  82     7299   9280   8492  -1167    327   -272       C  
ATOM    339  C   LEU A  82      -0.757   7.982  -1.740  1.00 70.21           C  
ANISOU  339  C   LEU A  82     8057   9596   9025  -1131    218   -180       C  
ATOM    340  O   LEU A  82      -1.178   8.231  -2.875  1.00 71.57           O  
ANISOU  340  O   LEU A  82     8160   9794   9239  -1047    101   -233       O  
ATOM    341  CB  LEU A  82      -0.848  10.040  -0.313  1.00 59.37           C  
ANISOU  341  CB  LEU A  82     6407   8421   7728   -892    291   -300       C  
ATOM    342  CG  LEU A  82      -1.644  10.851   0.706  1.00 62.33           C  
ANISOU  342  CG  LEU A  82     6510   9044   8130   -856    360   -482       C  
ATOM    343  CD1 LEU A  82      -1.091  12.261   0.855  1.00 55.10           C  
ANISOU  343  CD1 LEU A  82     5564   8044   7327   -570    267   -530       C  
ATOM    344  CD2 LEU A  82      -3.114  10.883   0.314  1.00 64.42           C  
ANISOU  344  CD2 LEU A  82     6475   9550   8451   -907    325   -667       C  
ATOM    345  N   VAL A  83       0.261   7.147  -1.524  1.00 71.76           N  
ANISOU  345  N   VAL A  83     8510   9592   9162  -1179    238    -64       N  
ATOM    346  CA  VAL A  83       0.813   6.355  -2.620  1.00 69.53           C  
ANISOU  346  CA  VAL A  83     8414   9139   8867  -1147    140    -43       C  
ATOM    347  C   VAL A  83      -0.238   5.394  -3.158  1.00 73.89           C  
ANISOU  347  C   VAL A  83     8937   9715   9422  -1353     76   -116       C  
ATOM    348  O   VAL A  83      -0.404   5.247  -4.375  1.00 79.13           O  
ANISOU  348  O   VAL A  83     9606  10373  10087  -1289    -32   -185       O  
ATOM    349  CB  VAL A  83       2.078   5.608  -2.159  1.00 61.51           C  
ANISOU  349  CB  VAL A  83     7653   7900   7818  -1130    147     49       C  
ATOM    350  CG1 VAL A  83       2.537   4.623  -3.222  1.00 56.33           C  
ANISOU  350  CG1 VAL A  83     7164   7084   7153  -1094     37      1       C  
ATOM    351  CG2 VAL A  83       3.187   6.592  -1.827  1.00 55.01           C  
ANISOU  351  CG2 VAL A  83     6836   7065   7001   -921    189    106       C  
ATOM    352  N   ALA A  84      -0.973   4.732  -2.264  1.00 63.07           N  
ANISOU  352  N   ALA A  84     7532   8393   8036  -1628    136   -100       N  
ATOM    353  CA  ALA A  84      -1.979   3.777  -2.713  1.00 68.51           C  
ANISOU  353  CA  ALA A  84     8190   9097   8744  -1877     65   -159       C  
ATOM    354  C   ALA A  84      -3.109   4.458  -3.475  1.00 67.78           C  
ANISOU  354  C   ALA A  84     7803   9251   8701  -1831     21   -306       C  
ATOM    355  O   ALA A  84      -3.668   3.871  -4.408  1.00 63.21           O  
ANISOU  355  O   ALA A  84     7217   8653   8146  -1911   -101   -386       O  
ATOM    356  CB  ALA A  84      -2.540   3.003  -1.520  1.00 70.03           C  
ANISOU  356  CB  ALA A  84     8393   9327   8888  -2241    149    -72       C  
ATOM    357  N   THR A  85      -3.449   5.692  -3.108  1.00 59.88           N  
ANISOU  357  N   THR A  85     6561   8463   7726  -1685     85   -362       N  
ATOM    358  CA  THR A  85      -4.630   6.368  -3.632  1.00 70.05           C  
ANISOU  358  CA  THR A  85     7536   9994   9087  -1632     16   -521       C  
ATOM    359  C   THR A  85      -4.329   7.352  -4.758  1.00 73.23           C  
ANISOU  359  C   THR A  85     7938  10354   9531  -1316   -140   -540       C  
ATOM    360  O   THR A  85      -5.144   7.493  -5.674  1.00 73.60           O  
ANISOU  360  O   THR A  85     7844  10501   9619  -1283   -285   -640       O  
ATOM    361  CB  THR A  85      -5.355   7.103  -2.501  1.00 66.86           C  
ANISOU  361  CB  THR A  85     6829   9873   8704  -1660    148   -625       C  
ATOM    362  OG1 THR A  85      -4.432   7.958  -1.812  1.00 68.22           O  
ANISOU  362  OG1 THR A  85     7080   9977   8864  -1454    215   -567       O  
ATOM    363  CG2 THR A  85      -5.948   6.109  -1.519  1.00 61.69           C  
ANISOU  363  CG2 THR A  85     6117   9358   7964  -2054    299   -604       C  
ATOM    364  N   LEU A  86      -3.186   8.043  -4.718  1.00 62.95           N  
ANISOU  364  N   LEU A  86     6792   8914   8211  -1106   -129   -431       N  
ATOM    365  CA  LEU A  86      -2.875   9.074  -5.699  1.00 69.96           C  
ANISOU  365  CA  LEU A  86     7691   9770   9119   -857   -279   -398       C  
ATOM    366  C   LEU A  86      -1.823   8.663  -6.718  1.00 73.74           C  
ANISOU  366  C   LEU A  86     8430  10102   9484   -805   -327   -290       C  
ATOM    367  O   LEU A  86      -1.627   9.386  -7.700  1.00 78.44           O  
ANISOU  367  O   LEU A  86     9050  10709  10044   -662   -458   -237       O  
ATOM    368  CB  LEU A  86      -2.400  10.356  -5.000  1.00 71.90           C  
ANISOU  368  CB  LEU A  86     7888   9995   9438   -669   -260   -361       C  
ATOM    369  CG  LEU A  86      -3.358  11.015  -4.012  1.00 70.39           C  
ANISOU  369  CG  LEU A  86     7407   9983   9357   -640   -226   -527       C  
ATOM    370  CD1 LEU A  86      -2.805  12.358  -3.572  1.00 66.08           C  
ANISOU  370  CD1 LEU A  86     6851   9355   8902   -408   -280   -511       C  
ATOM    371  CD2 LEU A  86      -4.735  11.169  -4.633  1.00 73.10           C  
ANISOU  371  CD2 LEU A  86     7488  10505   9781   -625   -371   -694       C  
ATOM    372  N   VAL A  87      -1.137   7.538  -6.512  1.00 71.08           N  
ANISOU  372  N   VAL A  87     8285   9640   9081   -916   -240   -262       N  
ATOM    373  CA  VAL A  87      -0.068   7.087  -7.395  1.00 73.29           C  
ANISOU  373  CA  VAL A  87     8777   9820   9251   -840   -268   -222       C  
ATOM    374  C   VAL A  87      -0.364   5.702  -7.963  1.00 77.64           C  
ANISOU  374  C   VAL A  87     9430  10309   9760   -973   -330   -334       C  
ATOM    375  O   VAL A  87      -0.313   5.497  -9.179  1.00 73.98           O  
ANISOU  375  O   VAL A  87     9018   9892   9199   -916   -433   -399       O  
ATOM    376  CB  VAL A  87       1.295   7.094  -6.673  1.00 71.74           C  
ANISOU  376  CB  VAL A  87     8723   9494   9039   -769   -152   -126       C  
ATOM    377  CG1 VAL A  87       2.408   6.688  -7.635  1.00 74.66           C  
ANISOU  377  CG1 VAL A  87     9249   9829   9290   -667   -171   -133       C  
ATOM    378  CG2 VAL A  87       1.561   8.458  -6.054  1.00 66.12           C  
ANISOU  378  CG2 VAL A  87     7914   8818   8388   -656   -114    -33       C  
ATOM    379  N   MET A  88      -0.666   4.743  -7.091  1.00 80.11           N  
ANISOU  379  N   MET A  88     9788  10515  10136  -1166   -284   -354       N  
ATOM    380  CA  MET A  88      -0.910   3.374  -7.543  1.00 77.27           C  
ANISOU  380  CA  MET A  88     9560  10025   9773  -1313   -382   -456       C  
ATOM    381  C   MET A  88      -2.014   3.257  -8.587  1.00 74.77           C  
ANISOU  381  C   MET A  88     9120   9842   9447  -1377   -521   -585       C  
ATOM    382  O   MET A  88      -1.856   2.434  -9.508  1.00 75.54           O  
ANISOU  382  O   MET A  88     9351   9858   9492  -1370   -641   -704       O  
ATOM    383  CB  MET A  88      -1.213   2.478  -6.335  1.00 80.86           C  
ANISOU  383  CB  MET A  88    10082  10339  10303  -1575   -337   -400       C  
ATOM    384  CG  MET A  88      -0.060   2.322  -5.349  1.00 81.25           C  
ANISOU  384  CG  MET A  88    10311  10211  10350  -1521   -256   -278       C  
ATOM    385  SD  MET A  88       1.427   1.569  -6.040  1.00 83.45           S  
ANISOU  385  SD  MET A  88    10860  10245  10603  -1297   -355   -350       S  
ATOM    386  CE  MET A  88       0.780   0.002  -6.622  1.00 86.55           C  
ANISOU  386  CE  MET A  88    11408  10421  11056  -1493   -560   -493       C  
ATOM    387  N   PRO A  89      -3.134   3.998  -8.521  1.00 73.85           N  
ANISOU  387  N   PRO A  89     8745   9932   9382  -1424   -534   -603       N  
ATOM    388  CA  PRO A  89      -4.103   3.930  -9.629  1.00 74.48           C  
ANISOU  388  CA  PRO A  89     8707  10146   9448  -1448   -704   -735       C  
ATOM    389  C   PRO A  89      -3.480   4.213 -10.985  1.00 73.67           C  
ANISOU  389  C   PRO A  89     8725  10074   9192  -1237   -816   -758       C  
ATOM    390  O   PRO A  89      -3.834   3.559 -11.972  1.00 74.04           O  
ANISOU  390  O   PRO A  89     8817  10141   9174  -1277   -962   -893       O  
ATOM    391  CB  PRO A  89      -5.142   4.990  -9.248  1.00 73.14           C  
ANISOU  391  CB  PRO A  89     8221  10200   9368  -1431   -703   -747       C  
ATOM    392  CG  PRO A  89      -5.085   5.041  -7.779  1.00 71.74           C  
ANISOU  392  CG  PRO A  89     7982  10016   9258  -1543   -514   -680       C  
ATOM    393  CD  PRO A  89      -3.645   4.834  -7.418  1.00 67.98           C  
ANISOU  393  CD  PRO A  89     7787   9325   8719  -1455   -417   -550       C  
ATOM    394  N   TRP A  90      -2.552   5.170 -11.056  1.00 69.93           N  
ANISOU  394  N   TRP A  90     8302   9624   8643  -1037   -753   -630       N  
ATOM    395  CA  TRP A  90      -1.831   5.402 -12.301  1.00 70.06           C  
ANISOU  395  CA  TRP A  90     8440   9716   8463   -885   -824   -623       C  
ATOM    396  C   TRP A  90      -0.927   4.229 -12.652  1.00 73.43           C  
ANISOU  396  C   TRP A  90     9074  10033   8794   -879   -795   -740       C  
ATOM    397  O   TRP A  90      -0.713   3.948 -13.836  1.00 80.52           O  
ANISOU  397  O   TRP A  90    10046  11036   9511   -815   -885   -849       O  
ATOM    398  CB  TRP A  90      -0.996   6.677 -12.206  1.00 72.68           C  
ANISOU  398  CB  TRP A  90     8778  10094   8744   -730   -758   -431       C  
ATOM    399  CG  TRP A  90      -1.743   7.924 -11.827  1.00 78.23           C  
ANISOU  399  CG  TRP A  90     9301  10853   9571   -681   -825   -337       C  
ATOM    400  CD1 TRP A  90      -2.061   8.338 -10.567  1.00 78.70           C  
ANISOU  400  CD1 TRP A  90     9229  10858   9814   -696   -738   -319       C  
ATOM    401  CD2 TRP A  90      -2.229   8.939 -12.716  1.00 88.37           C  
ANISOU  401  CD2 TRP A  90    10523  12253  10801   -588  -1022   -264       C  
ATOM    402  NE1 TRP A  90      -2.729   9.539 -10.616  1.00 79.87           N  
ANISOU  402  NE1 TRP A  90     9218  11075  10052   -589   -872   -284       N  
ATOM    403  CE2 TRP A  90      -2.844   9.929 -11.925  1.00 85.91           C  
ANISOU  403  CE2 TRP A  90    10036  11918  10690   -521  -1067   -232       C  
ATOM    404  CE3 TRP A  90      -2.213   9.101 -14.106  1.00 93.09           C  
ANISOU  404  CE3 TRP A  90    11205  12978  11187   -553  -1185   -228       C  
ATOM    405  CZ2 TRP A  90      -3.436  11.064 -12.476  1.00 91.05           C  
ANISOU  405  CZ2 TRP A  90    10603  12614  11379   -398  -1303   -166       C  
ATOM    406  CZ3 TRP A  90      -2.801  10.229 -14.651  1.00 88.71           C  
ANISOU  406  CZ3 TRP A  90    10584  12483  10637   -467  -1412   -117       C  
ATOM    407  CH2 TRP A  90      -3.404  11.195 -13.838  1.00 91.05           C  
ANISOU  407  CH2 TRP A  90    10716  12700  11179   -380  -1486    -87       C  
ATOM    408  N   VAL A  91      -0.382   3.540 -11.646  1.00 69.25           N  
ANISOU  408  N   VAL A  91     8640   9297   8374   -930   -690   -736       N  
ATOM    409  CA  VAL A  91       0.555   2.453 -11.912  1.00 71.26           C  
ANISOU  409  CA  VAL A  91     9090   9406   8578   -872   -701   -873       C  
ATOM    410  C   VAL A  91      -0.181   1.188 -12.341  1.00 81.86           C  
ANISOU  410  C   VAL A  91    10506  10626   9969  -1010   -867  -1076       C  
ATOM    411  O   VAL A  91       0.272   0.468 -13.239  1.00 84.97           O  
ANISOU  411  O   VAL A  91    11020  11005  10261   -913   -961  -1279       O  
ATOM    412  CB  VAL A  91       1.447   2.203 -10.683  1.00 66.23           C  
ANISOU  412  CB  VAL A  91     8549   8562   8051   -856   -583   -782       C  
ATOM    413  CG1 VAL A  91       2.331   0.984 -10.905  1.00 66.75           C  
ANISOU  413  CG1 VAL A  91     8812   8434   8116   -769   -652   -961       C  
ATOM    414  CG2 VAL A  91       2.295   3.427 -10.395  1.00 71.66           C  
ANISOU  414  CG2 VAL A  91     9171   9373   8685   -712   -442   -614       C  
ATOM    415  N   VAL A  92      -1.320   0.890 -11.713  1.00 76.99           N  
ANISOU  415  N   VAL A  92     9808   9938   9507  -1247   -911  -1047       N  
ATOM    416  CA  VAL A  92      -2.100  -0.267 -12.139  1.00 83.11           C  
ANISOU  416  CA  VAL A  92    10641  10591  10346  -1426  -1092  -1225       C  
ATOM    417  C   VAL A  92      -2.714  -0.014 -13.513  1.00 85.39           C  
ANISOU  417  C   VAL A  92    10837  11112  10496  -1365  -1232  -1373       C  
ATOM    418  O   VAL A  92      -2.760  -0.914 -14.362  1.00 87.20           O  
ANISOU  418  O   VAL A  92    11179  11274  10677  -1366  -1396  -1596       O  
ATOM    419  CB  VAL A  92      -3.160  -0.626 -11.077  1.00 86.97           C  
ANISOU  419  CB  VAL A  92    11035  10994  11015  -1752  -1083  -1133       C  
ATOM    420  CG1 VAL A  92      -4.059   0.557 -10.774  1.00 88.40           C  
ANISOU  420  CG1 VAL A  92    10916  11464  11208  -1788   -990  -1030       C  
ATOM    421  CG2 VAL A  92      -3.984  -1.823 -11.526  1.00 90.14           C  
ANISOU  421  CG2 VAL A  92    11495  11253  11500  -1988  -1291  -1301       C  
ATOM    422  N   TYR A  93      -3.173   1.217 -13.762  1.00 86.77           N  
ANISOU  422  N   TYR A  93    10817  11548  10602  -1298  -1201  -1261       N  
ATOM    423  CA  TYR A  93      -3.600   1.598 -15.106  1.00 83.84           C  
ANISOU  423  CA  TYR A  93    10389  11409  10056  -1209  -1354  -1357       C  
ATOM    424  C   TYR A  93      -2.477   1.379 -16.111  1.00 80.40           C  
ANISOU  424  C   TYR A  93    10133  11042   9375  -1017  -1359  -1466       C  
ATOM    425  O   TYR A  93      -2.706   0.878 -17.219  1.00 74.40           O  
ANISOU  425  O   TYR A  93     9423  10381   8465   -997  -1517  -1669       O  
ATOM    426  CB  TYR A  93      -4.062   3.059 -15.102  1.00 86.78           C  
ANISOU  426  CB  TYR A  93    10567  11993  10412  -1130  -1345  -1178       C  
ATOM    427  CG  TYR A  93      -4.289   3.683 -16.465  1.00 96.56           C  
ANISOU  427  CG  TYR A  93    11788  13469  11430  -1012  -1516  -1193       C  
ATOM    428  CD1 TYR A  93      -5.528   3.603 -17.096  1.00 94.66           C  
ANISOU  428  CD1 TYR A  93    11412  13349  11207  -1088  -1737  -1310       C  
ATOM    429  CD2 TYR A  93      -3.274   4.383 -17.106  1.00 98.40           C  
ANISOU  429  CD2 TYR A  93    12135  13829  11423   -849  -1468  -1073       C  
ATOM    430  CE1 TYR A  93      -5.739   4.185 -18.334  1.00 95.59           C  
ANISOU  430  CE1 TYR A  93    11537  13682  11100   -983  -1926  -1302       C  
ATOM    431  CE2 TYR A  93      -3.475   4.965 -18.343  1.00 97.04           C  
ANISOU  431  CE2 TYR A  93    11974  13889  11007   -780  -1636  -1042       C  
ATOM    432  CZ  TYR A  93      -4.707   4.864 -18.952  1.00 96.39           C  
ANISOU  432  CZ  TYR A  93    11785  13900  10937   -837  -1876  -1153       C  
ATOM    433  OH  TYR A  93      -4.903   5.446 -20.182  1.00 95.53           O  
ANISOU  433  OH  TYR A  93    11712  14022  10562   -771  -2074  -1102       O  
ATOM    434  N   LEU A  94      -1.250   1.724 -15.722  1.00 88.56           N  
ANISOU  434  N   LEU A  94    11244  12051  10355   -879  -1185  -1358       N  
ATOM    435  CA  LEU A  94      -0.090   1.590 -16.592  1.00 90.25           C  
ANISOU  435  CA  LEU A  94    11571  12398  10320   -698  -1144  -1470       C  
ATOM    436  C   LEU A  94       0.187   0.143 -16.984  1.00 86.74           C  
ANISOU  436  C   LEU A  94    11276  11802   9879   -668  -1251  -1798       C  
ATOM    437  O   LEU A  94       0.806  -0.096 -18.027  1.00 79.60           O  
ANISOU  437  O   LEU A  94    10426  11091   8726   -524  -1274  -1999       O  
ATOM    438  CB  LEU A  94       1.131   2.192 -15.893  1.00 91.19           C  
ANISOU  438  CB  LEU A  94    11704  12504  10440   -587   -935  -1297       C  
ATOM    439  CG  LEU A  94       2.362   2.481 -16.745  1.00 96.59           C  
ANISOU  439  CG  LEU A  94    12420  13445  10836   -422   -839  -1342       C  
ATOM    440  CD1 LEU A  94       1.952   3.241 -17.987  1.00 95.48           C  
ANISOU  440  CD1 LEU A  94    12233  13639  10407   -435   -921  -1281       C  
ATOM    441  CD2 LEU A  94       3.366   3.277 -15.931  1.00 94.01           C  
ANISOU  441  CD2 LEU A  94    12057  13105  10556   -364   -648  -1120       C  
ATOM    442  N   GLU A  95      -0.244  -0.827 -16.175  1.00 91.64           N  
ANISOU  442  N   GLU A  95    11967  12086  10767   -809  -1328  -1863       N  
ATOM    443  CA  GLU A  95      -0.007  -2.228 -16.505  1.00 89.73           C  
ANISOU  443  CA  GLU A  95    11897  11617  10578   -779  -1491  -2179       C  
ATOM    444  C   GLU A  95      -1.104  -2.803 -17.392  1.00 87.68           C  
ANISOU  444  C   GLU A  95    11631  11388  10293   -904  -1724  -2391       C  
ATOM    445  O   GLU A  95      -0.812  -3.568 -18.317  1.00 89.77           O  
ANISOU  445  O   GLU A  95    12002  11667  10441   -784  -1865  -2717       O  
ATOM    446  CB  GLU A  95       0.121  -3.065 -15.229  1.00 87.59           C  
ANISOU  446  CB  GLU A  95    11758  10917  10607   -899  -1515  -2120       C  
ATOM    447  CG  GLU A  95       0.439  -4.539 -15.480  1.00 93.67           C  
ANISOU  447  CG  GLU A  95    12747  11357  11487   -851  -1741  -2438       C  
ATOM    448  CD  GLU A  95       1.851  -4.758 -16.002  1.00102.62           C  
ANISOU  448  CD  GLU A  95    13952  12557  12482   -504  -1707  -2681       C  
ATOM    449  OE1 GLU A  95       2.722  -3.902 -15.740  1.00104.20           O  
ANISOU  449  OE1 GLU A  95    14062  12957  12571   -357  -1484  -2527       O  
ATOM    450  OE2 GLU A  95       2.093  -5.788 -16.670  1.00107.64           O  
ANISOU  450  OE2 GLU A  95    14717  13056  13125   -376  -1910  -3051       O  
ATOM    451  N   VAL A  96      -2.362  -2.449 -17.129  1.00 78.94           N  
ANISOU  451  N   VAL A  96    10382  10316   9297  -1131  -1774  -2245       N  
ATOM    452  CA  VAL A  96      -3.462  -2.952 -17.947  1.00 80.52           C  
ANISOU  452  CA  VAL A  96    10543  10563   9488  -1267  -2011  -2444       C  
ATOM    453  C   VAL A  96      -3.331  -2.439 -19.375  1.00 85.05           C  
ANISOU  453  C   VAL A  96    11087  11511   9717  -1081  -2072  -2578       C  
ATOM    454  O   VAL A  96      -3.404  -3.209 -20.340  1.00 82.90           O  
ANISOU  454  O   VAL A  96    10906  11266   9327  -1037  -2258  -2893       O  
ATOM    455  CB  VAL A  96      -4.816  -2.561 -17.328  1.00 77.18           C  
ANISOU  455  CB  VAL A  96     9907  10166   9251  -1538  -2032  -2265       C  
ATOM    456  N   VAL A  97      -3.117  -1.130 -19.528  1.00 87.40           N  
ANISOU  456  N   VAL A  97    11271  12099   9836   -979  -1932  -2336       N  
ATOM    457  CA  VAL A  97      -2.995  -0.529 -20.854  1.00 88.86           C  
ANISOU  457  CA  VAL A  97    11446  12664   9653   -847  -1994  -2384       C  
ATOM    458  C   VAL A  97      -1.719  -0.983 -21.554  1.00 90.16           C  
ANISOU  458  C   VAL A  97    11752  12956   9548   -647  -1919  -2608       C  
ATOM    459  O   VAL A  97      -1.694  -1.122 -22.783  1.00 92.93           O  
ANISOU  459  O   VAL A  97    12140  13588   9583   -572  -2028  -2817       O  
ATOM    460  CB  VAL A  97      -3.061   1.005 -20.740  1.00 86.80           C  
ANISOU  460  CB  VAL A  97    11060  12617   9305   -817  -1897  -2025       C  
ATOM    461  CG1 VAL A  97      -2.893   1.659 -22.106  1.00 88.76           C  
ANISOU  461  CG1 VAL A  97    11335  13252   9139   -721  -1981  -2009       C  
ATOM    462  CG2 VAL A  97      -4.372   1.434 -20.086  1.00 86.16           C  
ANISOU  462  CG2 VAL A  97    10792  12448   9495   -970  -1990  -1884       C  
ATOM    463  N   GLY A  98      -0.650  -1.230 -20.800  1.00 88.15           N  
ANISOU  463  N   GLY A  98    11562  12531   9400   -550  -1740  -2596       N  
ATOM    464  CA  GLY A  98       0.613  -1.604 -21.402  1.00 89.34           C  
ANISOU  464  CA  GLY A  98    11789  12846   9310   -334  -1652  -2837       C  
ATOM    465  C   GLY A  98       1.360  -0.469 -22.059  1.00 91.48           C  
ANISOU  465  C   GLY A  98    11987  13570   9202   -247  -1473  -2660       C  
ATOM    466  O   GLY A  98       2.307  -0.717 -22.810  1.00 93.59           O  
ANISOU  466  O   GLY A  98    12270  14114   9177    -92  -1395  -2892       O  
ATOM    467  N   GLU A  99       0.962   0.772 -21.797  1.00 93.52           N  
ANISOU  467  N   GLU A  99    12159  13918   9455   -352  -1418  -2264       N  
ATOM    468  CA  GLU A  99       1.609   1.938 -22.378  1.00 95.54           C  
ANISOU  468  CA  GLU A  99    12373  14557   9372   -328  -1286  -2022       C  
ATOM    469  C   GLU A  99       1.259   3.151 -21.529  1.00 92.97           C  
ANISOU  469  C   GLU A  99    11976  14105   9244   -422  -1241  -1593       C  
ATOM    470  O   GLU A  99       0.253   3.163 -20.815  1.00 85.82           O  
ANISOU  470  O   GLU A  99    11021  12937   8648   -506  -1345  -1519       O  
ATOM    471  CB  GLU A  99       1.181   2.153 -23.835  1.00 94.86           C  
ANISOU  471  CB  GLU A  99    12308  14866   8868   -355  -1437  -2092       C  
ATOM    472  N   TRP A 100       2.110   4.174 -21.614  1.00 89.68           N  
ANISOU  472  N   TRP A 100    11539  13894   8642   -414  -1089  -1330       N  
ATOM    473  CA  TRP A 100       1.871   5.446 -20.932  1.00 88.27           C  
ANISOU  473  CA  TRP A 100    11308  13606   8625   -483  -1080   -935       C  
ATOM    474  C   TRP A 100       0.892   6.302 -21.742  1.00 91.37           C  
ANISOU  474  C   TRP A 100    11702  14149   8867   -556  -1315   -744       C  
ATOM    475  O   TRP A 100       1.217   7.382 -22.236  1.00 95.09           O  
ANISOU  475  O   TRP A 100    12204  14809   9115   -605  -1334   -453       O  
ATOM    476  CB  TRP A 100       3.188   6.177 -20.702  1.00 86.77           C  
ANISOU  476  CB  TRP A 100    11107  13540   8322   -471   -861   -729       C  
ATOM    477  CG  TRP A 100       4.148   5.471 -19.784  1.00 92.86           C  
ANISOU  477  CG  TRP A 100    11859  14140   9283   -376   -663   -888       C  
ATOM    478  CD1 TRP A 100       4.731   4.252 -19.983  1.00 99.53           C  
ANISOU  478  CD1 TRP A 100    12726  15011  10078   -261   -605  -1253       C  
ATOM    479  CD2 TRP A 100       4.655   5.958 -18.534  1.00 93.04           C  
ANISOU  479  CD2 TRP A 100    11841  13932   9577   -369   -533   -700       C  
ATOM    480  NE1 TRP A 100       5.558   3.944 -18.928  1.00 99.78           N  
ANISOU  480  NE1 TRP A 100    12740  14828  10345   -179   -465  -1286       N  
ATOM    481  CE2 TRP A 100       5.530   4.975 -18.027  1.00 94.10           C  
ANISOU  481  CE2 TRP A 100    11981  13965   9809   -254   -408   -944       C  
ATOM    482  CE3 TRP A 100       4.449   7.125 -17.792  1.00 92.42           C  
ANISOU  482  CE3 TRP A 100    11726  13714   9675   -431   -538   -373       C  
ATOM    483  CZ2 TRP A 100       6.198   5.125 -16.811  1.00 92.35           C  
ANISOU  483  CZ2 TRP A 100    11733  13525   9830   -217   -285   -845       C  
ATOM    484  CZ3 TRP A 100       5.114   7.273 -16.583  1.00 87.83           C  
ANISOU  484  CZ3 TRP A 100    11114  12928   9330   -397   -398   -300       C  
ATOM    485  CH2 TRP A 100       5.977   6.279 -16.107  1.00 90.94           C  
ANISOU  485  CH2 TRP A 100    11517  13244   9792   -299   -271   -522       C  
ATOM    486  N   LYS A 101      -0.329   5.791 -21.877  1.00 95.15           N  
ANISOU  486  N   LYS A 101    12148  14527   9477   -577  -1521   -906       N  
ATOM    487  CA  LYS A 101      -1.365   6.446 -22.678  1.00 96.45           C  
ANISOU  487  CA  LYS A 101    12300  14824   9522   -619  -1798   -787       C  
ATOM    488  C   LYS A 101      -2.121   7.498 -21.869  1.00 98.53           C  
ANISOU  488  C   LYS A 101    12457  14876  10104   -621  -1907   -529       C  
ATOM    489  O   LYS A 101      -3.351   7.502 -21.813  1.00100.15           O  
ANISOU  489  O   LYS A 101    12553  15004  10495   -628  -2120   -595       O  
ATOM    490  CB  LYS A 101      -2.319   5.405 -23.251  1.00 91.01           C  
ANISOU  490  CB  LYS A 101    11597  14158   8826   -638  -1991  -1116       C  
ATOM    491  N   PHE A 102      -1.377   8.397 -21.223  1.00 92.76           N  
ANISOU  491  N   PHE A 102    11736  14060   9449   -605  -1768   -264       N  
ATOM    492  CA  PHE A 102      -1.943   9.593 -20.620  1.00 93.22           C  
ANISOU  492  CA  PHE A 102    11716  13947   9756   -575  -1904    -18       C  
ATOM    493  C   PHE A 102      -1.857  10.735 -21.628  1.00 91.71           C  
ANISOU  493  C   PHE A 102    11641  13918   9287   -599  -2119    289       C  
ATOM    494  O   PHE A 102      -1.422  10.558 -22.768  1.00103.07           O  
ANISOU  494  O   PHE A 102    13204  15642  10313   -665  -2138    313       O  
ATOM    495  CB  PHE A 102      -1.202   9.983 -19.340  1.00 94.22           C  
ANISOU  495  CB  PHE A 102    11808  13862  10129   -551  -1677     95       C  
ATOM    496  CG  PHE A 102      -0.815   8.827 -18.469  1.00 91.97           C  
ANISOU  496  CG  PHE A 102    11490  13455  10000   -556  -1432   -141       C  
ATOM    497  CD1 PHE A 102      -1.737   8.243 -17.618  1.00 88.34           C  
ANISOU  497  CD1 PHE A 102    10903  12822   9841   -574  -1444   -314       C  
ATOM    498  CD2 PHE A 102       0.483   8.344 -18.477  1.00 88.17           C  
ANISOU  498  CD2 PHE A 102    11097  13037   9364   -553  -1204   -181       C  
ATOM    499  CE1 PHE A 102      -1.375   7.184 -16.805  1.00 84.23           C  
ANISOU  499  CE1 PHE A 102    10394  12156   9452   -611  -1257   -481       C  
ATOM    500  CE2 PHE A 102       0.849   7.286 -17.667  1.00 83.36           C  
ANISOU  500  CE2 PHE A 102    10485  12270   8917   -538  -1037   -386       C  
ATOM    501  CZ  PHE A 102      -0.082   6.706 -16.830  1.00 81.83           C  
ANISOU  501  CZ  PHE A 102    10213  11865   9014   -578  -1075   -513       C  
ATOM    502  N   SER A 103      -2.265  11.924 -21.210  1.00 88.70           N  
ANISOU  502  N   SER A 103    11226  13356   9120   -550  -2299    526       N  
ATOM    503  CA  SER A 103      -1.855  13.135 -21.896  1.00 82.43           C  
ANISOU  503  CA  SER A 103    10589  12620   8110   -603  -2476    904       C  
ATOM    504  C   SER A 103      -0.586  13.661 -21.237  1.00 83.13           C  
ANISOU  504  C   SER A 103    10732  12623   8230   -660  -2230   1106       C  
ATOM    505  O   SER A 103      -0.135  13.148 -20.210  1.00 83.31           O  
ANISOU  505  O   SER A 103    10661  12526   8466   -622  -1957    945       O  
ATOM    506  CB  SER A 103      -2.969  14.182 -21.869  1.00 79.20           C  
ANISOU  506  CB  SER A 103    10137  12018   7939   -498  -2879   1043       C  
ATOM    507  OG  SER A 103      -3.335  14.521 -20.542  1.00 76.16           O  
ANISOU  507  OG  SER A 103     9579  11344   8016   -372  -2840    955       O  
ATOM    508  N   ARG A 104       0.009  14.689 -21.845  1.00 84.27           N  
ANISOU  508  N   ARG A 104    11037  12833   8148   -776  -2344   1478       N  
ATOM    509  CA  ARG A 104       1.252  15.212 -21.290  1.00 80.60           C  
ANISOU  509  CA  ARG A 104    10612  12312   7701   -868  -2123   1679       C  
ATOM    510  C   ARG A 104       1.025  15.830 -19.921  1.00 77.44           C  
ANISOU  510  C   ARG A 104    10113  11518   7794   -740  -2150   1682       C  
ATOM    511  O   ARG A 104       1.913  15.783 -19.064  1.00 78.86           O  
ANISOU  511  O   ARG A 104    10250  11620   8096   -755  -1890   1666       O  
ATOM    512  CB  ARG A 104       1.881  16.231 -22.235  1.00 80.66           C  
ANISOU  512  CB  ARG A 104    10815  12469   7362  -1078  -2266   2114       C  
ATOM    513  CG  ARG A 104       3.382  16.383 -22.031  1.00 90.20           C  
ANISOU  513  CG  ARG A 104    12038  13815   8417  -1248  -1948   2260       C  
ATOM    514  CD  ARG A 104       3.766  17.736 -21.446  1.00101.17           C  
ANISOU  514  CD  ARG A 104    13504  14894  10041  -1329  -2089   2624       C  
ATOM    515  NE  ARG A 104       3.451  18.831 -22.359  1.00106.68           N  
ANISOU  515  NE  ARG A 104    14414  15562  10556  -1484  -2476   3046       N  
ATOM    516  CZ  ARG A 104       2.650  19.849 -22.059  1.00108.76           C  
ANISOU  516  CZ  ARG A 104    14758  15416  11150  -1381  -2885   3220       C  
ATOM    517  NH1 ARG A 104       2.092  19.927 -20.857  1.00104.63           N  
ANISOU  517  NH1 ARG A 104    14088  14533  11136  -1126  -2918   2984       N  
ATOM    518  NH2 ARG A 104       2.417  20.795 -22.961  1.00112.28           N  
ANISOU  518  NH2 ARG A 104    15433  15822  11408  -1532  -3275   3626       N  
ATOM    519  N   ILE A 105      -0.160  16.392 -19.688  1.00 79.98           N  
ANISOU  519  N   ILE A 105    10379  11613   8397   -597  -2469   1666       N  
ATOM    520  CA  ILE A 105      -0.435  17.000 -18.394  1.00 78.38           C  
ANISOU  520  CA  ILE A 105    10057  11079   8646   -452  -2502   1613       C  
ATOM    521  C   ILE A 105      -0.797  15.939 -17.359  1.00 74.85           C  
ANISOU  521  C   ILE A 105     9401  10617   8423   -355  -2239   1232       C  
ATOM    522  O   ILE A 105      -0.422  16.063 -16.189  1.00 73.96           O  
ANISOU  522  O   ILE A 105     9211  10343   8549   -307  -2066   1171       O  
ATOM    523  CB  ILE A 105      -1.528  18.076 -18.534  1.00 77.26           C  
ANISOU  523  CB  ILE A 105     9910  10715   8730   -308  -2966   1710       C  
ATOM    524  CG1 ILE A 105      -1.691  18.858 -17.227  1.00 76.93           C  
ANISOU  524  CG1 ILE A 105     9750  10345   9133   -142  -3017   1643       C  
ATOM    525  CG2 ILE A 105      -2.847  17.465 -18.989  1.00 71.80           C  
ANISOU  525  CG2 ILE A 105     9083  10142   8055   -199  -3143   1458       C  
ATOM    526  CD1 ILE A 105      -0.522  19.761 -16.903  1.00 63.79           C  
ANISOU  526  CD1 ILE A 105     8244   8504   7489   -248  -2982   1938       C  
ATOM    527  N   HIS A 106      -1.425  14.862 -17.789  1.00 78.10           N  
ANISOU  527  N   HIS A 106     9732  11194   8747   -350  -2214    984       N  
ATOM    528  CA  HIS A 106      -1.751  13.780 -16.889  1.00 72.04           C  
ANISOU  528  CA  HIS A 106     8805  10412   8157   -326  -1967    668       C  
ATOM    529  C   HIS A 106      -0.480  13.081 -16.470  1.00 75.28           C  
ANISOU  529  C   HIS A 106     9289  10863   8451   -409  -1617    644       C  
ATOM    530  O   HIS A 106      -0.345  12.663 -15.351  1.00 70.37           O  
ANISOU  530  O   HIS A 106     8580  10125   8032   -389  -1418    503       O  
ATOM    531  CB  HIS A 106      -2.690  12.806 -17.558  1.00 69.03           C  
ANISOU  531  CB  HIS A 106     8344  10182   7701   -344  -2050    426       C  
ATOM    532  CG  HIS A 106      -4.109  13.257 -17.558  1.00 86.66           C  
ANISOU  532  CG  HIS A 106    10420  12382  10122   -239  -2375    359       C  
ATOM    533  ND1 HIS A 106      -4.497  14.469 -17.043  1.00 93.53           N  
ANISOU  533  ND1 HIS A 106    11265  13098  11175   -109  -2634    518       N  
ATOM    534  CD2 HIS A 106      -5.234  12.662 -18.003  1.00 92.54           C  
ANISOU  534  CD2 HIS A 106    11011  13228  10921   -235  -2507    125       C  
ATOM    535  CE1 HIS A 106      -5.801  14.602 -17.170  1.00 95.16           C  
ANISOU  535  CE1 HIS A 106    11292  13325  11539     -1  -2912    369       C  
ATOM    536  NE2 HIS A 106      -6.273  13.520 -17.751  1.00 94.46           N  
ANISOU  536  NE2 HIS A 106    11111  13409  11371    -89  -2829    134       N  
ATOM    537  N   CYS A 107       0.459  12.953 -17.384  1.00 74.40           N  
ANISOU  537  N   CYS A 107     9326  10942   8001   -501  -1547    768       N  
ATOM    538  CA  CYS A 107       1.750  12.355 -17.073  1.00 74.41           C  
ANISOU  538  CA  CYS A 107     9366  11008   7898   -548  -1239    725       C  
ATOM    539  C   CYS A 107       2.520  13.220 -16.082  1.00 69.26           C  
ANISOU  539  C   CYS A 107     8705  10174   7436   -541  -1146    902       C  
ATOM    540  O   CYS A 107       3.036  12.718 -15.076  1.00 62.15           O  
ANISOU  540  O   CYS A 107     7754   9173   6688   -508   -936    780       O  
ATOM    541  CB  CYS A 107       2.542  12.149 -18.368  1.00 77.98           C  
ANISOU  541  CB  CYS A 107     9930  11782   7918   -646  -1190    790       C  
ATOM    542  SG  CYS A 107       4.200  11.445 -18.193  1.00 79.49           S  
ANISOU  542  SG  CYS A 107    10119  12137   7945   -673   -832    689       S  
ATOM    543  N   ASP A 108       2.590  14.530 -16.341  1.00 68.64           N  
ANISOU  543  N   ASP A 108     8692  10029   7359   -576  -1335   1195       N  
ATOM    544  CA  ASP A 108       3.289  15.433 -15.430  1.00 67.61           C  
ANISOU  544  CA  ASP A 108     8561   9699   7427   -578  -1293   1358       C  
ATOM    545  C   ASP A 108       2.673  15.405 -14.037  1.00 65.65           C  
ANISOU  545  C   ASP A 108     8180   9208   7557   -435  -1270   1167       C  
ATOM    546  O   ASP A 108       3.393  15.362 -13.033  1.00 66.27           O  
ANISOU  546  O   ASP A 108     8226   9190   7765   -423  -1086   1133       O  
ATOM    547  CB  ASP A 108       3.280  16.856 -15.990  1.00 70.02           C  
ANISOU  547  CB  ASP A 108     8985   9912   7707   -648  -1582   1705       C  
ATOM    548  CG  ASP A 108       4.274  17.047 -17.124  1.00 81.41           C  
ANISOU  548  CG  ASP A 108    10562  11623   8747   -867  -1532   1967       C  
ATOM    549  OD1 ASP A 108       5.293  16.329 -17.150  1.00 84.41           O  
ANISOU  549  OD1 ASP A 108    10904  12225   8943   -940  -1226   1879       O  
ATOM    550  OD2 ASP A 108       4.043  17.922 -17.986  1.00 86.93           O  
ANISOU  550  OD2 ASP A 108    11397  12326   9305   -971  -1808   2260       O  
ATOM    551  N   ILE A 109       1.341  15.424 -13.956  1.00 63.48           N  
ANISOU  551  N   ILE A 109     7808   8870   7442   -332  -1455   1030       N  
ATOM    552  CA  ILE A 109       0.665  15.365 -12.662  1.00 61.96           C  
ANISOU  552  CA  ILE A 109     7449   8532   7562   -218  -1412    821       C  
ATOM    553  C   ILE A 109       1.015  14.072 -11.937  1.00 63.72           C  
ANISOU  553  C   ILE A 109     7629   8811   7771   -268  -1106    623       C  
ATOM    554  O   ILE A 109       1.341  14.076 -10.743  1.00 59.23           O  
ANISOU  554  O   ILE A 109     7010   8137   7359   -241   -960    564       O  
ATOM    555  CB  ILE A 109      -0.856  15.511 -12.845  1.00 58.03           C  
ANISOU  555  CB  ILE A 109     6805   8039   7204   -115  -1656    674       C  
ATOM    556  CG1 ILE A 109      -1.212  16.937 -13.262  1.00 58.42           C  
ANISOU  556  CG1 ILE A 109     6896   7940   7362    -12  -2018    855       C  
ATOM    557  CG2 ILE A 109      -1.588  15.133 -11.573  1.00 56.04           C  
ANISOU  557  CG2 ILE A 109     6336   7761   7197    -50  -1535    405       C  
ATOM    558  CD1 ILE A 109      -2.681  17.131 -13.524  1.00 59.89           C  
ANISOU  558  CD1 ILE A 109     6917   8142   7695    126  -2302    693       C  
ATOM    559  N   PHE A 110       0.949  12.945 -12.648  1.00 61.78           N  
ANISOU  559  N   PHE A 110     7422   8717   7335   -338  -1034    516       N  
ATOM    560  CA  PHE A 110       1.250  11.658 -12.031  1.00 58.79           C  
ANISOU  560  CA  PHE A 110     7039   8336   6961   -385   -808    335       C  
ATOM    561  C   PHE A 110       2.679  11.622 -11.510  1.00 63.91           C  
ANISOU  561  C   PHE A 110     7771   8939   7574   -390   -613    414       C  
ATOM    562  O   PHE A 110       2.921  11.236 -10.361  1.00 59.44           O  
ANISOU  562  O   PHE A 110     7180   8260   7146   -384   -476    340       O  
ATOM    563  CB  PHE A 110       0.997  10.530 -13.034  1.00 61.38           C  
ANISOU  563  CB  PHE A 110     7419   8803   7098   -442   -823    194       C  
ATOM    564  CG  PHE A 110       1.692   9.234 -12.700  1.00 68.94           C  
ANISOU  564  CG  PHE A 110     8447   9728   8016   -477   -636     42       C  
ATOM    565  CD1 PHE A 110       1.579   8.662 -11.444  1.00 75.18           C  
ANISOU  565  CD1 PHE A 110     9204  10361   8999   -508   -525    -42       C  
ATOM    566  CD2 PHE A 110       2.437   8.573 -13.660  1.00 71.59           C  
ANISOU  566  CD2 PHE A 110     8887  10201   8115   -474   -595    -28       C  
ATOM    567  CE1 PHE A 110       2.216   7.472 -11.150  1.00 77.40           C  
ANISOU  567  CE1 PHE A 110     9585  10560   9264   -531   -416   -161       C  
ATOM    568  CE2 PHE A 110       3.070   7.383 -13.372  1.00 74.90           C  
ANISOU  568  CE2 PHE A 110     9372  10553   8534   -462   -477   -203       C  
ATOM    569  CZ  PHE A 110       2.960   6.833 -12.116  1.00 77.70           C  
ANISOU  569  CZ  PHE A 110     9724  10690   9110   -489   -407   -255       C  
ATOM    570  N   VAL A 111       3.641  12.034 -12.340  1.00 65.60           N  
ANISOU  570  N   VAL A 111     8072   9264   7587   -416   -603    568       N  
ATOM    571  CA  VAL A 111       5.043  11.987 -11.930  1.00 66.54           C  
ANISOU  571  CA  VAL A 111     8228   9388   7667   -424   -420    620       C  
ATOM    572  C   VAL A 111       5.288  12.924 -10.757  1.00 60.65           C  
ANISOU  572  C   VAL A 111     7442   8452   7150   -393   -417    727       C  
ATOM    573  O   VAL A 111       6.026  12.590  -9.822  1.00 56.21           O  
ANISOU  573  O   VAL A 111     6872   7814   6670   -370   -270    674       O  
ATOM    574  CB  VAL A 111       5.960  12.317 -13.119  1.00 69.81           C  
ANISOU  574  CB  VAL A 111     8700  10035   7791   -499   -401    765       C  
ATOM    575  CG1 VAL A 111       7.405  12.336 -12.671  1.00 60.98           C  
ANISOU  575  CG1 VAL A 111     7563   8955   6651   -512   -214    801       C  
ATOM    576  CG2 VAL A 111       5.758  11.308 -14.235  1.00 72.95           C  
ANISOU  576  CG2 VAL A 111     9130  10652   7937   -508   -394    597       C  
ATOM    577  N   THR A 112       4.669  14.106 -10.784  1.00 59.23           N  
ANISOU  577  N   THR A 112     7242   8180   7083   -374   -610    861       N  
ATOM    578  CA  THR A 112       4.789  15.036  -9.664  1.00 65.31           C  
ANISOU  578  CA  THR A 112     7970   8754   8090   -319   -646    910       C  
ATOM    579  C   THR A 112       4.286  14.407  -8.371  1.00 66.52           C  
ANISOU  579  C   THR A 112     8031   8833   8410   -256   -532    693       C  
ATOM    580  O   THR A 112       4.970  14.440  -7.343  1.00 76.31           O  
ANISOU  580  O   THR A 112     9268   9991   9734   -241   -417    676       O  
ATOM    581  CB  THR A 112       4.019  16.321  -9.963  1.00 64.71           C  
ANISOU  581  CB  THR A 112     7889   8561   8139   -269   -933   1031       C  
ATOM    582  OG1 THR A 112       4.645  17.010 -11.052  1.00 63.73           O  
ANISOU  582  OG1 THR A 112     7888   8484   7843   -379  -1048   1304       O  
ATOM    583  CG2 THR A 112       3.995  17.223  -8.744  1.00 62.38           C  
ANISOU  583  CG2 THR A 112     7534   8052   8116   -171   -994    998       C  
ATOM    584  N   LEU A 113       3.086  13.825  -8.407  1.00 61.29           N  
ANISOU  584  N   LEU A 113     7289   8219   7778   -245   -569    534       N  
ATOM    585  CA  LEU A 113       2.533  13.195  -7.214  1.00 68.29           C  
ANISOU  585  CA  LEU A 113     8081   9085   8780   -248   -453    353       C  
ATOM    586  C   LEU A 113       3.348  11.975  -6.799  1.00 67.53           C  
ANISOU  586  C   LEU A 113     8081   8983   8595   -321   -257    312       C  
ATOM    587  O   LEU A 113       3.573  11.752  -5.604  1.00 68.67           O  
ANISOU  587  O   LEU A 113     8216   9064   8811   -332   -149    267       O  
ATOM    588  CB  LEU A 113       1.075  12.808  -7.454  1.00 70.65           C  
ANISOU  588  CB  LEU A 113     8249   9477   9119   -266   -536    201       C  
ATOM    589  CG  LEU A 113       0.073  13.960  -7.517  1.00 65.91           C  
ANISOU  589  CG  LEU A 113     7497   8872   8673   -146   -751    162       C  
ATOM    590  CD1 LEU A 113      -1.287  13.451  -7.958  1.00 61.41           C  
ANISOU  590  CD1 LEU A 113     6776   8439   8118   -174   -840      2       C  
ATOM    591  CD2 LEU A 113      -0.016  14.648  -6.165  1.00 61.76           C  
ANISOU  591  CD2 LEU A 113     6853   8287   8324    -59   -710     69       C  
ATOM    592  N   ASP A 114       3.794  11.174  -7.768  1.00 63.91           N  
ANISOU  592  N   ASP A 114     7718   8590   7975   -359   -233    311       N  
ATOM    593  CA  ASP A 114       4.598   9.999  -7.445  1.00 66.05           C  
ANISOU  593  CA  ASP A 114     8086   8820   8191   -384   -102    240       C  
ATOM    594  C   ASP A 114       5.885  10.392  -6.734  1.00 66.08           C  
ANISOU  594  C   ASP A 114     8124   8760   8225   -333    -12    324       C  
ATOM    595  O   ASP A 114       6.262   9.778  -5.730  1.00 69.96           O  
ANISOU  595  O   ASP A 114     8658   9151   8773   -337     64    278       O  
ATOM    596  CB  ASP A 114       4.901   9.208  -8.720  1.00 75.01           C  
ANISOU  596  CB  ASP A 114     9296  10059   9148   -388   -118    174       C  
ATOM    597  CG  ASP A 114       5.951   8.133  -8.509  1.00 75.49           C  
ANISOU  597  CG  ASP A 114     9451  10063   9168   -352    -25     76       C  
ATOM    598  OD1 ASP A 114       5.746   7.255  -7.648  1.00 74.37           O  
ANISOU  598  OD1 ASP A 114     9364   9766   9125   -388     -9     -2       O  
ATOM    599  OD2 ASP A 114       6.981   8.161  -9.214  1.00 76.15           O  
ANISOU  599  OD2 ASP A 114     9549  10268   9116   -291     20     74       O  
ATOM    600  N   VAL A 115       6.568  11.421  -7.235  1.00 71.45           N  
ANISOU  600  N   VAL A 115     8790   9494   8864   -306    -41    464       N  
ATOM    601  CA  VAL A 115       7.809  11.865  -6.610  1.00 70.24           C  
ANISOU  601  CA  VAL A 115     8641   9297   8749   -279     30    542       C  
ATOM    602  C   VAL A 115       7.535  12.461  -5.234  1.00 69.24           C  
ANISOU  602  C   VAL A 115     8477   9030   8802   -253     19    542       C  
ATOM    603  O   VAL A 115       8.282  12.220  -4.279  1.00 70.91           O  
ANISOU  603  O   VAL A 115     8710   9175   9059   -230     93    521       O  
ATOM    604  CB  VAL A 115       8.536  12.862  -7.531  1.00 65.07           C  
ANISOU  604  CB  VAL A 115     7975   8750   7999   -319     -9    719       C  
ATOM    605  CG1 VAL A 115       9.683  13.529  -6.804  1.00 60.52           C  
ANISOU  605  CG1 VAL A 115     7374   8118   7505   -321     36    809       C  
ATOM    606  CG2 VAL A 115       9.043  12.156  -8.778  1.00 62.56           C  
ANISOU  606  CG2 VAL A 115     7676   8649   7446   -346     53    680       C  
ATOM    607  N   MET A 116       6.454  13.232  -5.103  1.00 72.12           N  
ANISOU  607  N   MET A 116     8773   9364   9266   -239    -88    539       N  
ATOM    608  CA  MET A 116       6.164  13.889  -3.832  1.00 68.31           C  
ANISOU  608  CA  MET A 116     8226   8792   8936   -191   -103    487       C  
ATOM    609  C   MET A 116       5.814  12.877  -2.746  1.00 67.37           C  
ANISOU  609  C   MET A 116     8106   8685   8808   -232     19    357       C  
ATOM    610  O   MET A 116       6.435  12.860  -1.677  1.00 67.14           O  
ANISOU  610  O   MET A 116     8105   8604   8802   -221     83    349       O  
ATOM    611  CB  MET A 116       5.031  14.896  -4.005  1.00 66.63           C  
ANISOU  611  CB  MET A 116     7912   8564   8843   -129   -269    455       C  
ATOM    612  CG  MET A 116       4.669  15.602  -2.718  1.00 65.54           C  
ANISOU  612  CG  MET A 116     7676   8370   8856    -46   -291    332       C  
ATOM    613  SD  MET A 116       3.209  16.636  -2.880  1.00 73.08           S  
ANISOU  613  SD  MET A 116     8464   9323   9980     85   -509    199       S  
ATOM    614  CE  MET A 116       3.000  17.178  -1.184  1.00 75.15           C  
ANISOU  614  CE  MET A 116     8597   9592  10365    186   -462    -23       C  
ATOM    615  N   MET A 117       4.820  12.023  -3.000  1.00 57.68           N  
ANISOU  615  N   MET A 117     6854   7527   7535   -303     36    271       N  
ATOM    616  CA  MET A 117       4.373  11.084  -1.977  1.00 63.01           C  
ANISOU  616  CA  MET A 117     7536   8218   8187   -406    135    188       C  
ATOM    617  C   MET A 117       5.457  10.093  -1.578  1.00 71.53           C  
ANISOU  617  C   MET A 117     8783   9196   9201   -439    202    236       C  
ATOM    618  O   MET A 117       5.388   9.526  -0.482  1.00 77.20           O  
ANISOU  618  O   MET A 117     9549   9888   9894   -524    260    225       O  
ATOM    619  CB  MET A 117       3.132  10.337  -2.457  1.00 61.50           C  
ANISOU  619  CB  MET A 117     7283   8115   7968   -518    120    103       C  
ATOM    620  CG  MET A 117       1.975  11.258  -2.770  1.00 64.85           C  
ANISOU  620  CG  MET A 117     7509   8654   8476   -463     28     19       C  
ATOM    621  SD  MET A 117       1.790  12.509  -1.489  1.00 62.59           S  
ANISOU  621  SD  MET A 117     7071   8409   8301   -354     37    -66       S  
ATOM    622  CE  MET A 117       0.518  13.548  -2.206  1.00 56.74           C  
ANISOU  622  CE  MET A 117     6109   7754   7697   -221   -153   -189       C  
ATOM    623  N   CYS A 118       6.449   9.867  -2.434  1.00 70.60           N  
ANISOU  623  N   CYS A 118     8747   9036   9042   -373    183    282       N  
ATOM    624  CA  CYS A 118       7.576   9.023  -2.062  1.00 70.67           C  
ANISOU  624  CA  CYS A 118     8885   8946   9021   -346    211    289       C  
ATOM    625  C   CYS A 118       8.689   9.813  -1.387  1.00 68.27           C  
ANISOU  625  C   CYS A 118     8564   8615   8761   -260    228    351       C  
ATOM    626  O   CYS A 118       9.435   9.249  -0.578  1.00 62.32           O  
ANISOU  626  O   CYS A 118     7898   7774   8009   -239    233    351       O  
ATOM    627  CB  CYS A 118       8.121   8.295  -3.295  1.00 71.86           C  
ANISOU  627  CB  CYS A 118     9091   9112   9101   -295    188    239       C  
ATOM    628  SG  CYS A 118       6.974   7.093  -4.021  1.00 68.74           S  
ANISOU  628  SG  CYS A 118     8755   8698   8664   -398    132    131       S  
ATOM    629  N   THR A 119       8.819  11.105  -1.703  1.00 71.90           N  
ANISOU  629  N   THR A 119     8925   9128   9267   -218    203    409       N  
ATOM    630  CA  THR A 119       9.769  11.947  -0.985  1.00 68.93           C  
ANISOU  630  CA  THR A 119     8523   8711   8956   -165    196    461       C  
ATOM    631  C   THR A 119       9.300  12.212   0.440  1.00 62.52           C  
ANISOU  631  C   THR A 119     7704   7861   8191   -175    201    411       C  
ATOM    632  O   THR A 119      10.125  12.295   1.357  1.00 61.89           O  
ANISOU  632  O   THR A 119     7656   7732   8127   -144    202    417       O  
ATOM    633  CB  THR A 119       9.981  13.271  -1.728  1.00 67.89           C  
ANISOU  633  CB  THR A 119     8314   8606   8874   -156    129    558       C  
ATOM    634  OG1 THR A 119      10.268  13.009  -3.105  1.00 63.88           O  
ANISOU  634  OG1 THR A 119     7808   8202   8260   -182    139    610       O  
ATOM    635  CG2 THR A 119      11.148  14.045  -1.129  1.00 64.40           C  
ANISOU  635  CG2 THR A 119     7848   8113   8507   -132    108    616       C  
ATOM    636  N   ALA A 120       7.987  12.343   0.642  1.00 61.79           N  
ANISOU  636  N   ALA A 120     7547   7824   8105   -218    203    341       N  
ATOM    637  CA  ALA A 120       7.457  12.486   1.992  1.00 59.49           C  
ANISOU  637  CA  ALA A 120     7220   7579   7805   -246    240    258       C  
ATOM    638  C   ALA A 120       7.815  11.283   2.852  1.00 61.28           C  
ANISOU  638  C   ALA A 120     7585   7779   7919   -337    300    286       C  
ATOM    639  O   ALA A 120       8.114  11.433   4.041  1.00 62.06           O  
ANISOU  639  O   ALA A 120     7711   7891   7976   -343    316    271       O  
ATOM    640  CB  ALA A 120       5.943  12.676   1.947  1.00 60.06           C  
ANISOU  640  CB  ALA A 120     7153   7780   7886   -287    251    145       C  
ATOM    641  N   SER A 121       7.784  10.080   2.268  1.00 59.91           N  
ANISOU  641  N   SER A 121     7518   7552   7694   -409    305    325       N  
ATOM    642  CA  SER A 121       8.208   8.889   2.998  1.00 65.17           C  
ANISOU  642  CA  SER A 121     8361   8120   8282   -489    296    378       C  
ATOM    643  C   SER A 121       9.662   9.003   3.431  1.00 68.85           C  
ANISOU  643  C   SER A 121     8900   8486   8775   -361    241    416       C  
ATOM    644  O   SER A 121      10.014   8.643   4.561  1.00 69.48           O  
ANISOU  644  O   SER A 121     9088   8521   8792   -399    214    457       O  
ATOM    645  CB  SER A 121       8.013   7.640   2.137  1.00 61.09           C  
ANISOU  645  CB  SER A 121     7954   7505   7753   -550    254    383       C  
ATOM    646  OG  SER A 121       6.661   7.485   1.747  1.00 71.73           O  
ANISOU  646  OG  SER A 121     9221   8952   9081   -688    290    343       O  
ATOM    647  N   ALA A 122      10.522   9.500   2.544  1.00 66.20           N  
ANISOU  647  N   ALA A 122     8498   8140   8516   -228    219    409       N  
ATOM    648  CA  ALA A 122      11.932   9.632   2.882  1.00 64.09           C  
ANISOU  648  CA  ALA A 122     8247   7817   8288   -115    169    424       C  
ATOM    649  C   ALA A 122      12.144  10.731   3.911  1.00 67.35           C  
ANISOU  649  C   ALA A 122     8599   8264   8729    -99    162    428       C  
ATOM    650  O   ALA A 122      12.870  10.544   4.893  1.00 67.60           O  
ANISOU  650  O   ALA A 122     8699   8245   8739    -68    109    438       O  
ATOM    651  CB  ALA A 122      12.746   9.905   1.621  1.00 62.95           C  
ANISOU  651  CB  ALA A 122     8005   7723   8189    -24    175    411       C  
ATOM    652  N   LEU A 123      11.511  11.886   3.707  1.00 62.65           N  
ANISOU  652  N   LEU A 123     7879   7737   8186   -107    182    403       N  
ATOM    653  CA  LEU A 123      11.661  12.982   4.654  1.00 64.73           C  
ANISOU  653  CA  LEU A 123     8084   8013   8499    -71    145    360       C  
ATOM    654  C   LEU A 123      11.002  12.677   5.993  1.00 68.58           C  
ANISOU  654  C   LEU A 123     8623   8569   8865   -134    179    297       C  
ATOM    655  O   LEU A 123      11.397  13.259   7.008  1.00 65.26           O  
ANISOU  655  O   LEU A 123     8197   8165   8435    -96    140    244       O  
ATOM    656  CB  LEU A 123      11.095  14.271   4.056  1.00 60.03           C  
ANISOU  656  CB  LEU A 123     7361   7429   8020    -42    106    331       C  
ATOM    657  CG  LEU A 123      12.060  15.137   3.236  1.00 62.40           C  
ANISOU  657  CG  LEU A 123     7610   7663   8437    -13     31    421       C  
ATOM    658  CD1 LEU A 123      12.857  14.325   2.223  1.00 59.85           C  
ANISOU  658  CD1 LEU A 123     7308   7374   8057    -33     81    508       C  
ATOM    659  CD2 LEU A 123      11.293  16.248   2.540  1.00 58.42           C  
ANISOU  659  CD2 LEU A 123     7032   7125   8039     -7    -54    431       C  
ATOM    660  N   ASN A 124      10.015  11.778   6.022  1.00 64.20           N  
ANISOU  660  N   ASN A 124     8115   8078   8200   -253    250    303       N  
ATOM    661  CA  ASN A 124       9.452  11.343   7.295  1.00 68.55           C  
ANISOU  661  CA  ASN A 124     8724   8742   8580   -376    301    282       C  
ATOM    662  C   ASN A 124      10.430  10.450   8.047  1.00 72.49           C  
ANISOU  662  C   ASN A 124     9424   9133   8985   -402    229    393       C  
ATOM    663  O   ASN A 124      10.617  10.600   9.260  1.00 78.80           O  
ANISOU  663  O   ASN A 124    10273  10006   9661   -433    215    382       O  
ATOM    664  CB  ASN A 124       8.129  10.616   7.067  1.00 63.03           C  
ANISOU  664  CB  ASN A 124     8004   8152   7791   -549    391    281       C  
ATOM    665  CG  ASN A 124       6.940  11.540   7.141  1.00 59.12           C  
ANISOU  665  CG  ASN A 124     7283   7866   7312   -543    463    113       C  
ATOM    666  OD1 ASN A 124       6.864  12.399   8.016  1.00 58.74           O  
ANISOU  666  OD1 ASN A 124     7141   7941   7236   -481    474    -16       O  
ATOM    667  ND2 ASN A 124       6.000  11.373   6.218  1.00 59.97           N  
ANISOU  667  ND2 ASN A 124     7292   8020   7473   -588    490     83       N  
ATOM    668  N   LEU A 125      11.062   9.508   7.343  1.00 66.29           N  
ANISOU  668  N   LEU A 125     8756   8179   8253   -373    162    480       N  
ATOM    669  CA  LEU A 125      12.084   8.682   7.972  1.00 65.46           C  
ANISOU  669  CA  LEU A 125     8836   7929   8106   -343     35    565       C  
ATOM    670  C   LEU A 125      13.243   9.524   8.477  1.00 65.97           C  
ANISOU  670  C   LEU A 125     8840   7991   8234   -191    -37    522       C  
ATOM    671  O   LEU A 125      13.922   9.139   9.436  1.00 61.15           O  
ANISOU  671  O   LEU A 125     8360   7325   7547   -177   -149    572       O  
ATOM    672  CB  LEU A 125      12.583   7.629   6.988  1.00 62.70           C  
ANISOU  672  CB  LEU A 125     8578   7397   7847   -276    -48    593       C  
ATOM    673  CG  LEU A 125      11.555   6.553   6.663  1.00 64.43           C  
ANISOU  673  CG  LEU A 125     8919   7557   8006   -451    -38    646       C  
ATOM    674  CD1 LEU A 125      12.089   5.633   5.597  1.00 62.96           C  
ANISOU  674  CD1 LEU A 125     8802   7188   7932   -337   -140    608       C  
ATOM    675  CD2 LEU A 125      11.214   5.779   7.920  1.00 61.82           C  
ANISOU  675  CD2 LEU A 125     8799   7183   7505   -650   -100    783       C  
ATOM    676  N   CYS A 126      13.482  10.673   7.849  1.00 67.22           N  
ANISOU  676  N   CYS A 126     8812   8199   8530    -94      0    444       N  
ATOM    677  CA  CYS A 126      14.522  11.568   8.333  1.00 68.85           C  
ANISOU  677  CA  CYS A 126     8945   8402   8814     11    -78    401       C  
ATOM    678  C   CYS A 126      14.084  12.257   9.617  1.00 71.84           C  
ANISOU  678  C   CYS A 126     9323   8885   9086    -30    -78    330       C  
ATOM    679  O   CYS A 126      14.848  12.331  10.588  1.00 74.42           O  
ANISOU  679  O   CYS A 126     9709   9205   9362      8   -177    320       O  
ATOM    680  CB  CYS A 126      14.866  12.592   7.257  1.00 64.79           C  
ANISOU  680  CB  CYS A 126     8252   7891   8474     72    -60    375       C  
ATOM    681  SG  CYS A 126      16.409  13.441   7.561  1.00 69.06           S  
ANISOU  681  SG  CYS A 126     8693   8402   9146    160   -175    353       S  
ATOM    682  N   ALA A 127      12.849  12.762   9.642  1.00 60.58           N  
ANISOU  682  N   ALA A 127     7817   7582   7618    -95     24    250       N  
ATOM    683  CA  ALA A 127      12.322  13.375  10.854  1.00 61.10           C  
ANISOU  683  CA  ALA A 127     7852   7809   7555   -121     44    122       C  
ATOM    684  C   ALA A 127      12.220  12.369  11.990  1.00 65.12           C  
ANISOU  684  C   ALA A 127     8538   8411   7794   -256     52    201       C  
ATOM    685  O   ALA A 127      12.407  12.729  13.158  1.00 65.71           O  
ANISOU  685  O   ALA A 127     8640   8603   7724   -258     16    127       O  
ATOM    686  CB  ALA A 127      10.957  13.996  10.570  1.00 60.25           C  
ANISOU  686  CB  ALA A 127     7585   7843   7462   -141    147    -17       C  
ATOM    687  N   ILE A 128      11.925  11.108  11.673  1.00 64.09           N  
ANISOU  687  N   ILE A 128     8546   8221   7582   -384     77    357       N  
ATOM    688  CA  ILE A 128      11.829  10.083  12.705  1.00 61.38           C  
ANISOU  688  CA  ILE A 128     8417   7924   6982   -558     46    492       C  
ATOM    689  C   ILE A 128      13.184   9.868  13.370  1.00 64.99           C  
ANISOU  689  C   ILE A 128     9025   8241   7426   -455   -148    563       C  
ATOM    690  O   ILE A 128      13.286   9.807  14.600  1.00 69.74           O  
ANISOU  690  O   ILE A 128     9740   8959   7800   -534   -198    591       O  
ATOM    691  CB  ILE A 128      11.271   8.779  12.108  1.00 62.32           C  
ANISOU  691  CB  ILE A 128     8673   7934   7072   -722     61    653       C  
ATOM    692  CG1 ILE A 128       9.772   8.923  11.836  1.00 63.83           C  
ANISOU  692  CG1 ILE A 128     8711   8345   7195   -888    252    582       C  
ATOM    693  CG2 ILE A 128      11.548   7.604  13.028  1.00 64.88           C  
ANISOU  693  CG2 ILE A 128     9290   8172   7190   -886    -69    860       C  
ATOM    694  CD1 ILE A 128       9.120   7.668  11.294  1.00 68.59           C  
ANISOU  694  CD1 ILE A 128     9440   8852   7770  -1092    259    730       C  
ATOM    695  N   SER A 129      14.244   9.756  12.565  1.00 66.20           N  
ANISOU  695  N   SER A 129     9164   8178   7810   -278   -262    578       N  
ATOM    696  CA  SER A 129      15.586   9.611  13.121  1.00 63.02           C  
ANISOU  696  CA  SER A 129     8848   7658   7438   -147   -463    607       C  
ATOM    697  C   SER A 129      15.949  10.799  13.998  1.00 65.47           C  
ANISOU  697  C   SER A 129     9055   8109   7713    -86   -487    474       C  
ATOM    698  O   SER A 129      16.527  10.629  15.078  1.00 65.88           O  
ANISOU  698  O   SER A 129     9234   8177   7619    -82   -631    506       O  
ATOM    699  CB  SER A 129      16.603   9.467  11.995  1.00 65.36           C  
ANISOU  699  CB  SER A 129     9050   7784   7998     39   -538    582       C  
ATOM    700  OG  SER A 129      16.749  10.693  11.302  1.00 65.87           O  
ANISOU  700  OG  SER A 129     8871   7922   8235    114   -445    460       O  
ATOM    701  N   ILE A 130      15.624  12.011  13.546  1.00 64.82           N  
ANISOU  701  N   ILE A 130     8755   8106   7766    -35   -383    319       N  
ATOM    702  CA  ILE A 130      15.959  13.208  14.313  1.00 68.76           C  
ANISOU  702  CA  ILE A 130     9156   8695   8276     36   -439    156       C  
ATOM    703  C   ILE A 130      15.205  13.216  15.636  1.00 70.22           C  
ANISOU  703  C   ILE A 130     9425   9110   8144    -76   -395     92       C  
ATOM    704  O   ILE A 130      15.775  13.502  16.695  1.00 76.17           O  
ANISOU  704  O   ILE A 130    10235   9933   8773    -45   -514     30       O  
ATOM    705  CB  ILE A 130      15.668  14.473  13.488  1.00 69.26           C  
ANISOU  705  CB  ILE A 130     9002   8739   8574    105   -379     19       C  
ATOM    706  CG1 ILE A 130      16.553  14.504  12.241  1.00 65.51           C  
ANISOU  706  CG1 ILE A 130     8440   8094   8355    174   -420    103       C  
ATOM    707  CG2 ILE A 130      15.878  15.716  14.329  1.00 65.28           C  
ANISOU  707  CG2 ILE A 130     8415   8293   8097    175   -469   -180       C  
ATOM    708  CD1 ILE A 130      16.380  15.745  11.402  1.00 62.56           C  
ANISOU  708  CD1 ILE A 130     7895   7673   8203    202   -405     32       C  
ATOM    709  N   ASP A 131      13.909  12.904  15.595  1.00 70.28           N  
ANISOU  709  N   ASP A 131     9426   9280   7998   -221   -219     94       N  
ATOM    710  CA  ASP A 131      13.155  12.749  16.833  1.00 71.28           C  
ANISOU  710  CA  ASP A 131     9617   9702   7763   -378   -141     50       C  
ATOM    711  C   ASP A 131      13.708  11.611  17.677  1.00 75.20           C  
ANISOU  711  C   ASP A 131    10397  10170   8008   -506   -269    283       C  
ATOM    712  O   ASP A 131      13.639  11.660  18.910  1.00 73.14           O  
ANISOU  712  O   ASP A 131    10222  10134   7432   -599   -289    255       O  
ATOM    713  CB  ASP A 131      11.678  12.515  16.525  1.00 70.71           C  
ANISOU  713  CB  ASP A 131     9449   9834   7586   -540     79     22       C  
ATOM    714  CG  ASP A 131      10.820  12.477  17.775  1.00 76.68           C  
ANISOU  714  CG  ASP A 131    10201  10991   7942   -727    206    -66       C  
ATOM    715  OD1 ASP A 131      10.819  13.472  18.528  1.00 78.05           O  
ANISOU  715  OD1 ASP A 131    10254  11363   8039   -619    204   -327       O  
ATOM    716  OD2 ASP A 131      10.140  11.455  18.001  1.00 79.31           O  
ANISOU  716  OD2 ASP A 131    10647  11456   8030   -996    304    118       O  
ATOM    717  N   ARG A 132      14.264  10.581  17.036  1.00 72.55           N  
ANISOU  717  N   ARG A 132    10215   9556   7796   -504   -380    502       N  
ATOM    718  CA  ARG A 132      14.921   9.521  17.791  1.00 74.39           C  
ANISOU  718  CA  ARG A 132    10739   9679   7847   -579   -584    726       C  
ATOM    719  C   ARG A 132      16.221  10.003  18.417  1.00 74.84           C  
ANISOU  719  C   ARG A 132    10811   9673   7954   -388   -804    656       C  
ATOM    720  O   ARG A 132      16.614   9.507  19.479  1.00 74.70           O  
ANISOU  720  O   ARG A 132    11012   9686   7686   -458   -973    778       O  
ATOM    721  CB  ARG A 132      15.175   8.307  16.894  1.00 71.71           C  
ANISOU  721  CB  ARG A 132    10547   9024   7674   -578   -687    923       C  
ATOM    722  CG  ARG A 132      13.976   7.378  16.715  1.00 69.10           C  
ANISOU  722  CG  ARG A 132    10338   8727   7188   -858   -567   1086       C  
ATOM    723  CD  ARG A 132      13.493   6.832  18.055  1.00 75.91           C  
ANISOU  723  CD  ARG A 132    11433   9782   7627  -1155   -591   1269       C  
ATOM    724  NE  ARG A 132      12.518   7.717  18.686  1.00 77.94           N  
ANISOU  724  NE  ARG A 132    11497  10480   7636  -1291   -337   1099       N  
ATOM    725  CZ  ARG A 132      12.271   7.756  19.990  1.00 77.58           C  
ANISOU  725  CZ  ARG A 132    11552  10740   7186  -1484   -317   1141       C  
ATOM    726  NH1 ARG A 132      12.931   6.960  20.822  1.00 76.41           N  
ANISOU  726  NH1 ARG A 132    11728  10477   6827  -1585   -559   1394       N  
ATOM    727  NH2 ARG A 132      11.366   8.602  20.464  1.00 79.78           N  
ANISOU  727  NH2 ARG A 132    11599  11452   7261  -1565    -71    912       N  
ATOM    728  N   TYR A 133      16.902  10.960  17.786  1.00 73.32           N  
ANISOU  728  N   TYR A 133    10393   9395   8070   -171   -822    476       N  
ATOM    729  CA  TYR A 133      18.124  11.492  18.379  1.00 72.55           C  
ANISOU  729  CA  TYR A 133    10271   9257   8037    -13  -1032    389       C  
ATOM    730  C   TYR A 133      17.813  12.311  19.624  1.00 76.41           C  
ANISOU  730  C   TYR A 133    10753  10016   8263    -65  -1020    228       C  
ATOM    731  O   TYR A 133      18.475  12.161  20.658  1.00 82.66           O  
ANISOU  731  O   TYR A 133    11685  10852   8869    -54  -1214    255       O  
ATOM    732  CB  TYR A 133      18.894  12.340  17.365  1.00 65.57           C  
ANISOU  732  CB  TYR A 133     9133   8238   7542    169  -1045    254       C  
ATOM    733  CG  TYR A 133      20.160  12.957  17.931  1.00 69.03           C  
ANISOU  733  CG  TYR A 133     9504   8648   8079    305  -1262    149       C  
ATOM    734  CD1 TYR A 133      21.367  12.268  17.901  1.00 73.59           C  
ANISOU  734  CD1 TYR A 133    10124   9075   8760    424  -1482    232       C  
ATOM    735  CD2 TYR A 133      20.148  14.224  18.502  1.00 67.30           C  
ANISOU  735  CD2 TYR A 133     9162   8546   7862    326  -1271    -61       C  
ATOM    736  CE1 TYR A 133      22.526  12.825  18.419  1.00 73.44           C  
ANISOU  736  CE1 TYR A 133    10011   9052   8839    539  -1690    123       C  
ATOM    737  CE2 TYR A 133      21.303  14.789  19.022  1.00 69.25           C  
ANISOU  737  CE2 TYR A 133     9341   8760   8209    429  -1488   -164       C  
ATOM    738  CZ  TYR A 133      22.488  14.084  18.977  1.00 74.54           C  
ANISOU  738  CZ  TYR A 133    10039   9309   8975    524  -1689    -64       C  
ATOM    739  OH  TYR A 133      23.637  14.640  19.490  1.00 78.51           O  
ANISOU  739  OH  TYR A 133    10443   9800   9586    618  -1914   -178       O  
ATOM    740  N   THR A 134      16.813  13.190  19.544  1.00 70.79           N  
ANISOU  740  N   THR A 134     9871   9496   7530   -102   -814     34       N  
ATOM    741  CA  THR A 134      16.526  14.064  20.674  1.00 74.84           C  
ANISOU  741  CA  THR A 134    10337  10284   7814   -106   -805   -201       C  
ATOM    742  C   THR A 134      16.021  13.276  21.876  1.00 73.81           C  
ANISOU  742  C   THR A 134    10425  10433   7188   -319   -780    -82       C  
ATOM    743  O   THR A 134      16.266  13.672  23.021  1.00 83.45           O  
ANISOU  743  O   THR A 134    11696  11863   8150   -318   -870   -208       O  
ATOM    744  CB  THR A 134      15.517  15.137  20.270  1.00 81.04           C  
ANISOU  744  CB  THR A 134    10877  11199   8715    -61   -617   -471       C  
ATOM    745  OG1 THR A 134      14.231  14.541  20.084  1.00 85.24           O  
ANISOU  745  OG1 THR A 134    11407  11920   9060   -236   -387   -405       O  
ATOM    746  CG2 THR A 134      15.945  15.803  18.969  1.00 80.96           C  
ANISOU  746  CG2 THR A 134    10697  10893   9169     91   -653   -505       C  
ATOM    747  N   ALA A 135      15.341  12.151  21.642  1.00 74.49           N  
ANISOU  747  N   ALA A 135    10655  10530   7120   -527   -674    172       N  
ATOM    748  CA  ALA A 135      14.858  11.340  22.756  1.00 76.81           C  
ANISOU  748  CA  ALA A 135    11182  11087   6918   -800   -658    350       C  
ATOM    749  C   ALA A 135      16.008  10.654  23.480  1.00 76.81           C  
ANISOU  749  C   ALA A 135    11471  10921   6791   -787   -978    571       C  
ATOM    750  O   ALA A 135      15.979  10.505  24.707  1.00 82.26           O  
ANISOU  750  O   ALA A 135    12330  11871   7053   -935  -1044    623       O  
ATOM    751  CB  ALA A 135      13.849  10.307  22.259  1.00 69.76           C  
ANISOU  751  CB  ALA A 135    10373  10203   5930  -1063   -492    588       C  
ATOM    752  N   VAL A 136      17.029  10.233  22.739  1.00 76.95           N  
ANISOU  752  N   VAL A 136    11539  10534   7164   -603  -1189    688       N  
ATOM    753  CA  VAL A 136      18.154   9.535  23.350  1.00 82.31           C  
ANISOU  753  CA  VAL A 136    12472  11024   7777   -545  -1537    878       C  
ATOM    754  C   VAL A 136      19.136  10.524  23.967  1.00 82.04           C  
ANISOU  754  C   VAL A 136    12325  11053   7795   -336  -1708    644       C  
ATOM    755  O   VAL A 136      19.554  10.367  25.120  1.00 81.48           O  
ANISOU  755  O   VAL A 136    12446  11103   7411   -382  -1911    704       O  
ATOM    756  CB  VAL A 136      18.839   8.630  22.309  1.00 77.31           C  
ANISOU  756  CB  VAL A 136    11904   9961   7508   -406  -1706   1045       C  
ATOM    757  CG1 VAL A 136      20.246   8.278  22.755  1.00 77.43           C  
ANISOU  757  CG1 VAL A 136    12049   9764   7606   -210  -2095   1106       C  
ATOM    758  CG2 VAL A 136      18.017   7.366  22.083  1.00 72.64           C  
ANISOU  758  CG2 VAL A 136    11557   9266   6777   -655  -1667   1340       C  
ATOM    759  N   ALA A 137      19.501  11.568  23.224  1.00 77.79           N  
ANISOU  759  N   ALA A 137    11484  10437   7637   -128  -1644    384       N  
ATOM    760  CA  ALA A 137      20.609  12.434  23.603  1.00 80.22           C  
ANISOU  760  CA  ALA A 137    11669  10715   8097     69  -1852    182       C  
ATOM    761  C   ALA A 137      20.209  13.605  24.491  1.00 87.12           C  
ANISOU  761  C   ALA A 137    12440  11898   8765     54  -1780   -115       C  
ATOM    762  O   ALA A 137      21.094  14.243  25.073  1.00 87.55           O  
ANISOU  762  O   ALA A 137    12447  11955   8861    179  -1994   -277       O  
ATOM    763  CB  ALA A 137      21.304  12.975  22.349  1.00 74.40           C  
ANISOU  763  CB  ALA A 137    10663   9730   7877    260  -1849     74       C  
ATOM    764  N   MET A 138      18.922  13.910  24.616  1.00 85.65           N  
ANISOU  764  N   MET A 138    12198  11978   8368    -81  -1504   -224       N  
ATOM    765  CA  MET A 138      18.517  15.099  25.348  1.00 91.36           C  
ANISOU  765  CA  MET A 138    12776  12989   8948    -40  -1439   -587       C  
ATOM    766  C   MET A 138      17.450  14.760  26.377  1.00 93.65           C  
ANISOU  766  C   MET A 138    13184  13730   8670   -264  -1268   -595       C  
ATOM    767  O   MET A 138      16.648  13.844  26.169  1.00 90.32           O  
ANISOU  767  O   MET A 138    12865  13389   8064   -478  -1095   -353       O  
ATOM    768  CB  MET A 138      18.001  16.181  24.387  1.00 94.18           C  
ANISOU  768  CB  MET A 138    12839  13259   9687     83  -1276   -847       C  
ATOM    769  CG  MET A 138      19.095  16.769  23.500  1.00 98.65           C  
ANISOU  769  CG  MET A 138    13264  13452  10767    263  -1446   -874       C  
ATOM    770  SD  MET A 138      18.521  18.077  22.402  1.00105.80           S  
ANISOU  770  SD  MET A 138    13881  14215  12101    371  -1319  -1121       S  
ATOM    771  CE  MET A 138      20.031  18.481  21.533  1.00105.56           C  
ANISOU  771  CE  MET A 138    13744  13805  12559    477  -1542  -1039       C  
ATOM    772  N   PRO A 139      17.425  15.482  27.515  1.00104.46           N  
ANISOU  772  N   PRO A 139    14532  15425   9735   -241  -1315   -880       N  
ATOM    773  CA  PRO A 139      16.509  15.224  28.635  1.00105.59           C  
ANISOU  773  CA  PRO A 139    14765  16095   9259   -469  -1152   -923       C  
ATOM    774  C   PRO A 139      15.042  15.103  28.221  1.00104.65           C  
ANISOU  774  C   PRO A 139    14492  16238   9033   -630   -782   -969       C  
ATOM    775  O   PRO A 139      14.317  16.097  28.261  1.00106.02           O  
ANISOU  775  O   PRO A 139    14394  16653   9234   -519   -617  -1385       O  
ATOM    776  CB  PRO A 139      16.714  16.446  29.535  1.00103.32           C  
ANISOU  776  CB  PRO A 139    14347  16058   8852   -301  -1242  -1390       C  
ATOM    777  CG  PRO A 139      18.112  16.868  29.263  1.00100.62           C  
ANISOU  777  CG  PRO A 139    14009  15289   8934    -72  -1575  -1406       C  
ATOM    778  CD  PRO A 139      18.340  16.603  27.805  1.00 97.12           C  
ANISOU  778  CD  PRO A 139    13483  14389   9030     -4  -1545  -1193       C  
ATOM    779  N   THR A 144       8.716  17.350  27.929  1.00103.31           N  
ANISOU  779  N   THR A 144    12885  17966   8400   -718    631  -2535       N  
ATOM    780  CA  THR A 144       7.590  18.233  28.208  1.00111.55           C  
ANISOU  780  CA  THR A 144    13533  19499   9351   -578    832  -3111       C  
ATOM    781  C   THR A 144       6.396  17.895  27.318  1.00111.78           C  
ANISOU  781  C   THR A 144    13322  19627   9521   -685   1084  -3075       C  
ATOM    782  O   THR A 144       6.556  17.666  26.122  1.00115.16           O  
ANISOU  782  O   THR A 144    13802  19541  10411   -631   1006  -2812       O  
ATOM    783  CB  THR A 144       7.971  19.712  28.006  1.00112.47           C  
ANISOU  783  CB  THR A 144    13477  19327   9931   -104    597  -3618       C  
ATOM    784  N   ARG A 145       5.198  17.868  27.907  1.00112.87           N  
ANISOU  784  N   ARG A 145    13181  20279   9425   -824   1334  -3251       N  
ATOM    785  CA  ARG A 145       4.002  17.509  27.151  1.00114.09           C  
ANISOU  785  CA  ARG A 145    13078  20551   9719   -950   1551  -3212       C  
ATOM    786  C   ARG A 145       3.581  18.596  26.170  1.00118.73           C  
ANISOU  786  C   ARG A 145    13352  20930  10830   -531   1477  -3651       C  
ATOM    787  O   ARG A 145       2.846  18.305  25.221  1.00119.01           O  
ANISOU  787  O   ARG A 145    13234  20913  11072   -582   1585  -3578       O  
ATOM    788  CB  ARG A 145       2.846  17.198  28.104  1.00118.50           C  
ANISOU  788  CB  ARG A 145    13396  21689   9937  -1221   1786  -3270       C  
ATOM    789  N   TYR A 146       4.024  19.834  26.375  1.00121.59           N  
ANISOU  789  N   TYR A 146    13630  21133  11434   -123   1259  -4089       N  
ATOM    790  CA  TYR A 146       3.700  20.948  25.491  1.00117.64           C  
ANISOU  790  CA  TYR A 146    12880  20335  11482    295   1102  -4485       C  
ATOM    791  C   TYR A 146       4.829  21.280  24.526  1.00108.31           C  
ANISOU  791  C   TYR A 146    11951  18428  10772    498    805  -4303       C  
ATOM    792  O   TYR A 146       4.573  21.530  23.344  1.00100.71           O  
ANISOU  792  O   TYR A 146    10911  17078  10275    638    718  -4241       O  
ATOM    793  CB  TYR A 146       3.345  22.185  26.325  1.00124.08           C  
ANISOU  793  CB  TYR A 146    13429  21323  12394    606    974  -5030       C  
ATOM    794  CG  TYR A 146       3.156  23.462  25.533  1.00125.41           C  
ANISOU  794  CG  TYR A 146    13400  21084  13165   1062    702  -5422       C  
ATOM    795  CD1 TYR A 146       1.920  23.794  24.993  1.00128.22           C  
ANISOU  795  CD1 TYR A 146    13405  21556  13758   1181    740  -5641       C  
ATOM    796  CD2 TYR A 146       4.211  24.347  25.345  1.00125.84           C  
ANISOU  796  CD2 TYR A 146    13634  20614  13563   1355    362  -5554       C  
ATOM    797  CE1 TYR A 146       1.746  24.966  24.276  1.00131.82           C  
ANISOU  797  CE1 TYR A 146    13721  21595  14769   1588    432  -5955       C  
ATOM    798  CE2 TYR A 146       4.047  25.515  24.631  1.00128.03           C  
ANISOU  798  CE2 TYR A 146    13776  20456  14413   1732     64  -5846       C  
ATOM    799  CZ  TYR A 146       2.815  25.821  24.099  1.00132.64           C  
ANISOU  799  CZ  TYR A 146    14037  21147  15214   1852     92  -6034       C  
ATOM    800  OH  TYR A 146       2.656  26.988  23.388  1.00136.93           O  
ANISOU  800  OH  TYR A 146    14484  21222  16320   2213   -261  -6277       O  
ATOM    801  N   SER A 147       6.076  21.287  25.005  1.00108.97           N  
ANISOU  801  N   SER A 147    12336  18257  10810    490    611  -4125       N  
ATOM    802  CA  SER A 147       7.206  21.602  24.138  1.00104.01           C  
ANISOU  802  CA  SER A 147    11926  16901  10691    633    308  -3860       C  
ATOM    803  C   SER A 147       7.407  20.541  23.065  1.00103.85           C  
ANISOU  803  C   SER A 147    12083  16559  10818    407    370  -3277       C  
ATOM    804  O   SER A 147       7.842  20.861  21.953  1.00 99.45           O  
ANISOU  804  O   SER A 147    11570  15480  10738    539    199  -3123       O  
ATOM    805  CB  SER A 147       8.481  21.758  24.972  1.00101.67           C  
ANISOU  805  CB  SER A 147    11877  16479  10273    647     99  -3814       C  
ATOM    806  N   SER A 148       7.103  19.279  23.375  1.00100.58           N  
ANISOU  806  N   SER A 148    11778  16447   9991     56    598  -2950       N  
ATOM    807  CA  SER A 148       7.325  18.214  22.404  1.00 97.98           C  
ANISOU  807  CA  SER A 148    11636  15794   9798   -147    625  -2427       C  
ATOM    808  C   SER A 148       6.273  18.239  21.303  1.00 88.88           C  
ANISOU  808  C   SER A 148    10254  14611   8905   -117    745  -2472       C  
ATOM    809  O   SER A 148       6.602  18.071  20.125  1.00 80.56           O  
ANISOU  809  O   SER A 148     9283  13109   8218    -74    646  -2217       O  
ATOM    810  CB  SER A 148       7.339  16.858  23.106  1.00103.00           C  
ANISOU  810  CB  SER A 148    12497  16702   9935   -541    771  -2055       C  
ATOM    811  OG  SER A 148       6.089  16.599  23.719  1.00106.17           O  
ANISOU  811  OG  SER A 148    12692  17721   9926   -754   1057  -2228       O  
ATOM    812  N   LYS A 149       5.003  18.446  21.667  1.00 92.05           N  
ANISOU  812  N   LYS A 149    10349  15519   9108   -139    955  -2812       N  
ATOM    813  CA  LYS A 149       3.946  18.506  20.661  1.00 84.26           C  
ANISOU  813  CA  LYS A 149     9110  14536   8369    -93   1046  -2895       C  
ATOM    814  C   LYS A 149       4.192  19.638  19.673  1.00 88.93           C  
ANISOU  814  C   LYS A 149     9627  14634   9529    289    781  -3067       C  
ATOM    815  O   LYS A 149       3.943  19.488  18.470  1.00 93.01           O  
ANISOU  815  O   LYS A 149    10125  14862  10350    308    742  -2887       O  
ATOM    816  CB  LYS A 149       2.585  18.670  21.333  1.00 79.97           C  
ANISOU  816  CB  LYS A 149     8188  14678   7518   -142   1299  -3315       C  
ATOM    817  N   ARG A 150       4.688  20.778  20.160  1.00 87.49           N  
ANISOU  817  N   ARG A 150     9416  14340   9487    578    575  -3405       N  
ATOM    818  CA  ARG A 150       5.060  21.865  19.261  1.00 81.69           C  
ANISOU  818  CA  ARG A 150     8671  13071   9295    893    273  -3505       C  
ATOM    819  C   ARG A 150       6.223  21.474  18.359  1.00 80.21           C  
ANISOU  819  C   ARG A 150     8786  12341   9349    799    130  -2998       C  
ATOM    820  O   ARG A 150       6.317  21.964  17.230  1.00 82.46           O  
ANISOU  820  O   ARG A 150     9071  12222  10039    928    -38  -2909       O  
ATOM    821  CB  ARG A 150       5.411  23.117  20.063  1.00 80.33           C  
ANISOU  821  CB  ARG A 150     8437  12868   9215   1187     52  -3965       C  
ATOM    822  N   ARG A 151       7.111  20.595  18.831  1.00 78.36           N  
ANISOU  822  N   ARG A 151     8802  12110   8862    578    185  -2672       N  
ATOM    823  CA  ARG A 151       8.234  20.166  18.003  1.00 72.71           C  
ANISOU  823  CA  ARG A 151     8328  10937   8361    507     62  -2239       C  
ATOM    824  C   ARG A 151       7.780  19.202  16.916  1.00 79.91           C  
ANISOU  824  C   ARG A 151     9266  11777   9319    342    198  -1915       C  
ATOM    825  O   ARG A 151       8.310  19.226  15.799  1.00 80.42           O  
ANISOU  825  O   ARG A 151     9410  11464   9683    376     87  -1687       O  
ATOM    826  CB  ARG A 151       9.319  19.528  18.870  1.00 74.01           C  
ANISOU  826  CB  ARG A 151     8732  11123   8264    367     34  -2034       C  
ATOM    827  CG  ARG A 151      10.576  19.134  18.110  1.00 82.30           C  
ANISOU  827  CG  ARG A 151     9986  11745   9540    333   -108  -1658       C  
ATOM    828  CD  ARG A 151      11.637  18.577  19.045  1.00 87.06           C  
ANISOU  828  CD  ARG A 151    10798  12374   9905    242   -184  -1509       C  
ATOM    829  NE  ARG A 151      11.097  17.537  19.917  1.00 91.56           N  
ANISOU  829  NE  ARG A 151    11463  13317  10010     18     -7  -1413       N  
ATOM    830  CZ  ARG A 151      11.047  16.249  19.600  1.00 88.57           C  
ANISOU  830  CZ  ARG A 151    11241  12910   9500   -194     83  -1059       C  
ATOM    831  NH1 ARG A 151      10.538  15.370  20.453  1.00 83.32           N  
ANISOU  831  NH1 ARG A 151    10680  12574   8402   -440    216   -953       N  
ATOM    832  NH2 ARG A 151      11.506  15.837  18.428  1.00 87.56           N  
ANISOU  832  NH2 ARG A 151    11174  12429   9667   -175     27   -816       N  
ATOM    833  N   VAL A 152       6.797  18.350  17.218  1.00 81.56           N  
ANISOU  833  N   VAL A 152     9402  12365   9221    140    437  -1897       N  
ATOM    834  CA  VAL A 152       6.288  17.429  16.204  1.00 81.36           C  
ANISOU  834  CA  VAL A 152     9394  12272   9245    -25    549  -1623       C  
ATOM    835  C   VAL A 152       5.564  18.196  15.104  1.00 80.65           C  
ANISOU  835  C   VAL A 152     9093  12045   9504    168    481  -1785       C  
ATOM    836  O   VAL A 152       5.709  17.888  13.915  1.00 78.73           O  
ANISOU  836  O   VAL A 152     8921  11517   9474    149    431  -1543       O  
ATOM    837  CB  VAL A 152       5.377  16.364  16.843  1.00 80.98           C  
ANISOU  837  CB  VAL A 152     9312  12669   8787   -333    803  -1562       C  
ATOM    838  CG1 VAL A 152       5.106  15.241  15.863  1.00 82.24           C  
ANISOU  838  CG1 VAL A 152     9570  12682   8997   -541    871  -1224       C  
ATOM    839  CG2 VAL A 152       6.004  15.810  18.104  1.00 83.35           C  
ANISOU  839  CG2 VAL A 152     9819  13145   8703   -511    831  -1443       C  
ATOM    840  N   THR A 153       4.781  19.211  15.482  1.00 84.22           N  
ANISOU  840  N   THR A 153     9285  12700  10015    371    455  -2213       N  
ATOM    841  CA  THR A 153       4.057  20.004  14.492  1.00 78.54           C  
ANISOU  841  CA  THR A 153     8369  11830   9642    587    332  -2387       C  
ATOM    842  C   THR A 153       5.011  20.696  13.525  1.00 75.61           C  
ANISOU  842  C   THR A 153     8160  10910   9657    737     57  -2208       C  
ATOM    843  O   THR A 153       4.738  20.779  12.322  1.00 76.21           O  
ANISOU  843  O   THR A 153     8221  10766   9967    773    -25  -2073       O  
ATOM    844  CB  THR A 153       3.168  21.031  15.195  1.00 80.46           C  
ANISOU  844  CB  THR A 153     8306  12365   9901    832    300  -2933       C  
ATOM    845  OG1 THR A 153       2.144  20.354  15.937  1.00 82.11           O  
ANISOU  845  OG1 THR A 153     8305  13162   9733    652    595  -3096       O  
ATOM    846  CG2 THR A 153       2.527  21.976  14.186  1.00 77.79           C  
ANISOU  846  CG2 THR A 153     7796  11785   9977   1109     80  -3121       C  
ATOM    847  N   VAL A 154       6.141  21.193  14.030  1.00 73.65           N  
ANISOU  847  N   VAL A 154     8065  10459   9460    799    -90  -2194       N  
ATOM    848  CA  VAL A 154       7.112  21.843  13.156  1.00 71.40           C  
ANISOU  848  CA  VAL A 154     7922   9692   9516    880   -337  -2000       C  
ATOM    849  C   VAL A 154       7.787  20.821  12.246  1.00 67.73           C  
ANISOU  849  C   VAL A 154     7638   9069   9028    675   -255  -1548       C  
ATOM    850  O   VAL A 154       8.007  21.079  11.057  1.00 61.81           O  
ANISOU  850  O   VAL A 154     6927   8041   8515    690   -370  -1361       O  
ATOM    851  CB  VAL A 154       8.137  22.627  13.993  1.00 65.37           C  
ANISOU  851  CB  VAL A 154     7244   8781   8811    974   -518  -2127       C  
ATOM    852  CG1 VAL A 154       9.256  23.154  13.108  1.00 56.93           C  
ANISOU  852  CG1 VAL A 154     6321   7254   8055    968   -742  -1864       C  
ATOM    853  CG2 VAL A 154       7.453  23.767  14.722  1.00 60.75           C  
ANISOU  853  CG2 VAL A 154     6475   8294   8312   1228   -654  -2627       C  
ATOM    854  N   MET A 155       8.122  19.645  12.784  1.00 69.04           N  
ANISOU  854  N   MET A 155     7921   9413   8899    483    -75  -1374       N  
ATOM    855  CA  MET A 155       8.784  18.630  11.972  1.00 68.64           C  
ANISOU  855  CA  MET A 155     8035   9207   8837    329    -24  -1003       C  
ATOM    856  C   MET A 155       7.875  18.134  10.856  1.00 64.55           C  
ANISOU  856  C   MET A 155     7452   8706   8368    269     63   -905       C  
ATOM    857  O   MET A 155       8.316  17.979   9.712  1.00 59.62           O  
ANISOU  857  O   MET A 155     6898   7863   7894    252      8   -690       O  
ATOM    858  CB  MET A 155       9.241  17.467  12.851  1.00 72.37           C  
ANISOU  858  CB  MET A 155     8663   9833   9001    158     94   -859       C  
ATOM    859  CG  MET A 155      10.407  17.803  13.768  1.00 80.64           C  
ANISOU  859  CG  MET A 155     9815  10814  10011    208    -29   -884       C  
ATOM    860  SD  MET A 155      11.031  16.373  14.674  1.00 89.65           S  
ANISOU  860  SD  MET A 155    11184  12069  10810     19     37   -657       S  
ATOM    861  CE  MET A 155      12.405  17.110  15.553  1.00 99.07           C  
ANISOU  861  CE  MET A 155    12443  13153  12047    140   -171   -742       C  
ATOM    862  N   ILE A 156       6.602  17.886  11.166  1.00 67.34           N  
ANISOU  862  N   ILE A 156     7652   9352   8582    227    200  -1075       N  
ATOM    863  CA  ILE A 156       5.685  17.372  10.156  1.00 68.91           C  
ANISOU  863  CA  ILE A 156     7773   9590   8821    157    271  -1001       C  
ATOM    864  C   ILE A 156       5.469  18.403   9.059  1.00 69.08           C  
ANISOU  864  C   ILE A 156     7705   9384   9158    345     81  -1053       C  
ATOM    865  O   ILE A 156       5.484  18.072   7.867  1.00 70.31           O  
ANISOU  865  O   ILE A 156     7916   9392   9407    300     52   -852       O  
ATOM    866  CB  ILE A 156       4.357  16.945  10.806  1.00 70.36           C  
ANISOU  866  CB  ILE A 156     7765  10184   8786     48    458  -1197       C  
ATOM    867  CG1 ILE A 156       4.590  15.773  11.761  1.00 67.02           C  
ANISOU  867  CG1 ILE A 156     7488   9956   8020   -215    628  -1044       C  
ATOM    868  CG2 ILE A 156       3.332  16.571   9.742  1.00 64.85           C  
ANISOU  868  CG2 ILE A 156     6940   9528   8171     -3    496  -1169       C  
ATOM    869  CD1 ILE A 156       3.333  15.249  12.401  1.00 60.59           C  
ANISOU  869  CD1 ILE A 156     6493   9587   6942   -411    838  -1180       C  
ATOM    870  N   SER A 157       5.271  19.668   9.439  1.00 67.59           N  
ANISOU  870  N   SER A 157     7393   9155   9133    558    -76  -1325       N  
ATOM    871  CA  SER A 157       5.081  20.719   8.446  1.00 66.91           C  
ANISOU  871  CA  SER A 157     7261   8799   9364    734   -321  -1352       C  
ATOM    872  C   SER A 157       6.261  20.789   7.488  1.00 65.20           C  
ANISOU  872  C   SER A 157     7252   8247   9275    664   -437  -1006       C  
ATOM    873  O   SER A 157       6.079  20.905   6.271  1.00 70.97           O  
ANISOU  873  O   SER A 157     8005   8831  10130    658   -531   -845       O  
ATOM    874  CB  SER A 157       4.876  22.064   9.138  1.00 53.19           C  
ANISOU  874  CB  SER A 157     5403   7001   7805    983   -525  -1706       C  
ATOM    875  OG  SER A 157       3.770  22.013  10.019  1.00 59.25           O  
ANISOU  875  OG  SER A 157     5930   8154   8428   1059   -395  -2076       O  
ATOM    876  N   ILE A 158       7.481  20.701   8.019  1.00 63.38           N  
ANISOU  876  N   ILE A 158     7159   7930   8993    600   -428   -895       N  
ATOM    877  CA  ILE A 158       8.662  20.757   7.168  1.00 62.29           C  
ANISOU  877  CA  ILE A 158     7167   7544   8955    516   -512   -595       C  
ATOM    878  C   ILE A 158       8.684  19.577   6.207  1.00 66.42           C  
ANISOU  878  C   ILE A 158     7754   8134   9350    369   -356   -352       C  
ATOM    879  O   ILE A 158       9.069  19.717   5.042  1.00 76.92           O  
ANISOU  879  O   ILE A 158     9134   9324  10767    323   -426   -148       O  
ATOM    880  CB  ILE A 158       9.935  20.815   8.030  1.00 62.52           C  
ANISOU  880  CB  ILE A 158     7286   7519   8948    483   -529   -568       C  
ATOM    881  CG1 ILE A 158       9.969  22.114   8.833  1.00 61.54           C  
ANISOU  881  CG1 ILE A 158     7112   7280   8990    635   -734   -823       C  
ATOM    882  CG2 ILE A 158      11.177  20.683   7.165  1.00 56.51           C  
ANISOU  882  CG2 ILE A 158     6625   6594   8253    369   -564   -273       C  
ATOM    883  CD1 ILE A 158      11.102  22.178   9.819  1.00 68.44           C  
ANISOU  883  CD1 ILE A 158     8055   8136   9811    610   -764   -846       C  
ATOM    884  N   VAL A 159       8.260  18.399   6.670  1.00 61.58           N  
ANISOU  884  N   VAL A 159     7145   7737   8515    280   -157   -371       N  
ATOM    885  CA  VAL A 159       8.270  17.217   5.808  1.00 61.95           C  
ANISOU  885  CA  VAL A 159     7267   7816   8456    152    -40   -177       C  
ATOM    886  C   VAL A 159       7.403  17.448   4.578  1.00 58.47           C  
ANISOU  886  C   VAL A 159     6754   7353   8111    173    -97   -152       C  
ATOM    887  O   VAL A 159       7.847  17.270   3.437  1.00 64.62           O  
ANISOU  887  O   VAL A 159     7599   8038   8915    129   -128     32       O  
ATOM    888  CB  VAL A 159       7.811  15.973   6.589  1.00 61.71           C  
ANISOU  888  CB  VAL A 159     7270   7984   8194     28    136   -202       C  
ATOM    889  CG1 VAL A 159       7.571  14.812   5.641  1.00 58.85           C  
ANISOU  889  CG1 VAL A 159     6974   7622   7763    -90    212    -53       C  
ATOM    890  CG2 VAL A 159       8.840  15.593   7.634  1.00 64.69           C  
ANISOU  890  CG2 VAL A 159     7772   8351   8457     -6    154   -157       C  
ATOM    891  N   TRP A 160       6.156  17.865   4.792  1.00 55.67           N  
ANISOU  891  N   TRP A 160     6244   7112   7797    249   -122   -357       N  
ATOM    892  CA  TRP A 160       5.209  17.964   3.688  1.00 61.87           C  
ANISOU  892  CA  TRP A 160     6946   7902   8658    275   -191   -352       C  
ATOM    893  C   TRP A 160       5.414  19.222   2.854  1.00 68.14           C  
ANISOU  893  C   TRP A 160     7758   8458   9675    394   -447   -287       C  
ATOM    894  O   TRP A 160       5.155  19.201   1.645  1.00 72.46           O  
ANISOU  894  O   TRP A 160     8331   8951  10250    369   -527   -148       O  
ATOM    895  CB  TRP A 160       3.778  17.893   4.226  1.00 54.20           C  
ANISOU  895  CB  TRP A 160     5762   7176   7654    313   -130   -618       C  
ATOM    896  CG  TRP A 160       3.447  16.528   4.729  1.00 59.47           C  
ANISOU  896  CG  TRP A 160     6436   8074   8087    111    106   -599       C  
ATOM    897  CD1 TRP A 160       3.428  16.111   6.027  1.00 64.43           C  
ANISOU  897  CD1 TRP A 160     7047   8894   8538     21    258   -694       C  
ATOM    898  CD2 TRP A 160       3.129  15.380   3.933  1.00 65.48           C  
ANISOU  898  CD2 TRP A 160     7253   8873   8755    -53    190   -456       C  
ATOM    899  NE1 TRP A 160       3.105  14.776   6.089  1.00 64.83           N  
ANISOU  899  NE1 TRP A 160     7153   9080   8400   -211    420   -586       N  
ATOM    900  CE2 TRP A 160       2.917  14.305   4.817  1.00 67.13           C  
ANISOU  900  CE2 TRP A 160     7487   9263   8758   -251    374   -455       C  
ATOM    901  CE3 TRP A 160       2.997  15.161   2.558  1.00 66.76           C  
ANISOU  901  CE3 TRP A 160     7455   8935   8975    -62    110   -331       C  
ATOM    902  CZ2 TRP A 160       2.575  13.030   4.371  1.00 70.04           C  
ANISOU  902  CZ2 TRP A 160     7926   9666   9019   -454    457   -337       C  
ATOM    903  CZ3 TRP A 160       2.659  13.895   2.117  1.00 69.12           C  
ANISOU  903  CZ3 TRP A 160     7807   9302   9154   -239    209   -252       C  
ATOM    904  CH2 TRP A 160       2.451  12.846   3.021  1.00 68.25           C  
ANISOU  904  CH2 TRP A 160     7727   9325   8880   -431    370   -257       C  
ATOM    905  N   VAL A 161       5.874  20.317   3.463  1.00 67.95           N  
ANISOU  905  N   VAL A 161     7737   8280   9802    507   -599   -373       N  
ATOM    906  CA  VAL A 161       6.140  21.520   2.680  1.00 69.19           C  
ANISOU  906  CA  VAL A 161     7952   8155  10182    576   -883   -262       C  
ATOM    907  C   VAL A 161       7.379  21.323   1.823  1.00 65.64           C  
ANISOU  907  C   VAL A 161     7665   7597   9678    402   -867     76       C  
ATOM    908  O   VAL A 161       7.447  21.799   0.684  1.00 71.00           O  
ANISOU  908  O   VAL A 161     8411   8144  10420    354  -1023    278       O  
ATOM    909  CB  VAL A 161       6.273  22.747   3.599  1.00 68.92           C  
ANISOU  909  CB  VAL A 161     7883   7953  10351    740  -1087   -473       C  
ATOM    910  CG1 VAL A 161       6.754  23.958   2.810  1.00 55.10           C  
ANISOU  910  CG1 VAL A 161     6251   5845   8841    751  -1414   -291       C  
ATOM    911  CG2 VAL A 161       4.941  23.041   4.271  1.00 68.37           C  
ANISOU  911  CG2 VAL A 161     7604   8033  10340    947  -1123   -858       C  
ATOM    912  N   LEU A 162       8.370  20.607   2.346  1.00 57.34           N  
ANISOU  912  N   LEU A 162     6669   6627   8492    302   -683    137       N  
ATOM    913  CA  LEU A 162       9.567  20.343   1.562  1.00 62.34           C  
ANISOU  913  CA  LEU A 162     7399   7226   9060    152   -640    403       C  
ATOM    914  C   LEU A 162       9.274  19.375   0.424  1.00 64.44           C  
ANISOU  914  C   LEU A 162     7686   7633   9165     68   -521    527       C  
ATOM    915  O   LEU A 162       9.756  19.565  -0.698  1.00 73.70           O  
ANISOU  915  O   LEU A 162     8910   8787  10307    -32   -568    735       O  
ATOM    916  CB  LEU A 162      10.668  19.803   2.467  1.00 66.33           C  
ANISOU  916  CB  LEU A 162     7929   7786   9485    111   -507    389       C  
ATOM    917  CG  LEU A 162      12.083  19.741   1.909  1.00 71.44           C  
ANISOU  917  CG  LEU A 162     8616   8419  10108    -16   -484    596       C  
ATOM    918  CD1 LEU A 162      12.409  21.020   1.165  1.00 63.78           C  
ANISOU  918  CD1 LEU A 162     7665   7275   9293    -96   -691    765       C  
ATOM    919  CD2 LEU A 162      13.044  19.530   3.061  1.00 75.47           C  
ANISOU  919  CD2 LEU A 162     9125   8941  10610      0   -439    519       C  
ATOM    920  N   SER A 163       8.481  18.334   0.691  1.00 62.39           N  
ANISOU  920  N   SER A 163     7390   7531   8786     86   -371    399       N  
ATOM    921  CA  SER A 163       8.099  17.410  -0.371  1.00 64.81           C  
ANISOU  921  CA  SER A 163     7718   7951   8957     15   -289    475       C  
ATOM    922  C   SER A 163       7.384  18.143  -1.499  1.00 65.90           C  
ANISOU  922  C   SER A 163     7840   8039   9160     33   -467    552       C  
ATOM    923  O   SER A 163       7.634  17.874  -2.680  1.00 71.94           O  
ANISOU  923  O   SER A 163     8662   8855   9817    -51   -466    710       O  
ATOM    924  CB  SER A 163       7.213  16.302   0.193  1.00 64.78           C  
ANISOU  924  CB  SER A 163     7674   8087   8852      4   -146    321       C  
ATOM    925  OG  SER A 163       7.785  15.740   1.357  1.00 61.15           O  
ANISOU  925  OG  SER A 163     7254   7650   8329    -18    -31    269       O  
ATOM    926  N   PHE A 164       6.497  19.078  -1.153  1.00 60.59           N  
ANISOU  926  N   PHE A 164     7089   7277   8655    156   -639    427       N  
ATOM    927  CA  PHE A 164       5.825  19.887  -2.164  1.00 61.72           C  
ANISOU  927  CA  PHE A 164     7234   7322   8893    201   -880    505       C  
ATOM    928  C   PHE A 164       6.833  20.691  -2.972  1.00 65.16           C  
ANISOU  928  C   PHE A 164     7806   7601   9350     94  -1027    793       C  
ATOM    929  O   PHE A 164       6.879  20.597  -4.203  1.00 65.92           O  
ANISOU  929  O   PHE A 164     7974   7746   9327    -10  -1074    992       O  
ATOM    930  CB  PHE A 164       4.803  20.813  -1.496  1.00 57.42           C  
ANISOU  930  CB  PHE A 164     6564   6683   8568    400  -1076    267       C  
ATOM    931  CG  PHE A 164       4.135  21.779  -2.443  1.00 61.42           C  
ANISOU  931  CG  PHE A 164     7089   7023   9226    488  -1405    340       C  
ATOM    932  CD1 PHE A 164       3.067  21.374  -3.232  1.00 63.79           C  
ANISOU  932  CD1 PHE A 164     7317   7446   9476    519  -1453    302       C  
ATOM    933  CD2 PHE A 164       4.563  23.097  -2.528  1.00 60.79           C  
ANISOU  933  CD2 PHE A 164     7109   6640   9350    534  -1703    451       C  
ATOM    934  CE1 PHE A 164       2.450  22.259  -4.099  1.00 64.22           C  
ANISOU  934  CE1 PHE A 164     7400   7336   9667    615  -1799    378       C  
ATOM    935  CE2 PHE A 164       3.946  23.988  -3.393  1.00 65.28           C  
ANISOU  935  CE2 PHE A 164     7729   7008  10065    614  -2062    545       C  
ATOM    936  CZ  PHE A 164       2.889  23.566  -4.178  1.00 64.54           C  
ANISOU  936  CZ  PHE A 164     7564   7051   9906    666  -2113    510       C  
ATOM    937  N   THR A 165       7.667  21.477  -2.285  1.00 60.91           N  
ANISOU  937  N   THR A 165     7302   6899   8944     90  -1100    820       N  
ATOM    938  CA  THR A 165       8.590  22.366  -2.984  1.00 68.08           C  
ANISOU  938  CA  THR A 165     8326   7648   9893    -59  -1264   1109       C  
ATOM    939  C   THR A 165       9.585  21.592  -3.836  1.00 67.06           C  
ANISOU  939  C   THR A 165     8237   7731   9511   -266  -1055   1321       C  
ATOM    940  O   THR A 165      10.068  22.114  -4.846  1.00 74.56           O  
ANISOU  940  O   THR A 165     9269   8666  10395   -439  -1158   1596       O  
ATOM    941  CB  THR A 165       9.335  23.256  -1.988  1.00 72.21           C  
ANISOU  941  CB  THR A 165     8862   7963  10613    -43  -1373   1067       C  
ATOM    942  OG1 THR A 165      10.064  22.439  -1.068  1.00 84.36           O  
ANISOU  942  OG1 THR A 165    10343   9656  12055    -52  -1111    946       O  
ATOM    943  CG2 THR A 165       8.362  24.133  -1.215  1.00 69.54           C  
ANISOU  943  CG2 THR A 165     8475   7415  10531    191  -1616    813       C  
ATOM    944  N   ILE A 166       9.898  20.352  -3.455  1.00 69.64           N  
ANISOU  944  N   ILE A 166     8506   8267   9687   -255   -775   1193       N  
ATOM    945  CA  ILE A 166      10.825  19.548  -4.247  1.00 72.15           C  
ANISOU  945  CA  ILE A 166     8831   8805   9778   -397   -585   1317       C  
ATOM    946  C   ILE A 166      10.150  19.043  -5.520  1.00 72.60           C  
ANISOU  946  C   ILE A 166     8918   9016   9653   -435   -578   1379       C  
ATOM    947  O   ILE A 166      10.751  19.045  -6.601  1.00 74.34           O  
ANISOU  947  O   ILE A 166     9167   9388   9690   -588   -548   1564       O  
ATOM    948  CB  ILE A 166      11.383  18.389  -3.402  1.00 64.44           C  
ANISOU  948  CB  ILE A 166     7804   7945   8737   -337   -355   1141       C  
ATOM    949  CG1 ILE A 166      12.401  18.911  -2.386  1.00 65.09           C  
ANISOU  949  CG1 ILE A 166     7859   7927   8946   -345   -368   1133       C  
ATOM    950  CG2 ILE A 166      12.008  17.326  -4.294  1.00 61.90           C  
ANISOU  950  CG2 ILE A 166     7469   7861   8189   -405   -177   1168       C  
ATOM    951  CD1 ILE A 166      12.979  17.825  -1.505  1.00 55.41           C  
ANISOU  951  CD1 ILE A 166     6604   6788   7663   -276   -195    979       C  
ATOM    952  N   SER A 167       8.896  18.605  -5.414  1.00 66.08           N  
ANISOU  952  N   SER A 167     8070   8185   8852   -311   -603   1216       N  
ATOM    953  CA  SER A 167       8.168  18.066  -6.554  1.00 69.77           C  
ANISOU  953  CA  SER A 167     8557   8794   9156   -335   -616   1237       C  
ATOM    954  C   SER A 167       7.500  19.138  -7.404  1.00 70.97           C  
ANISOU  954  C   SER A 167     8769   8841   9355   -354   -900   1407       C  
ATOM    955  O   SER A 167       7.132  18.860  -8.553  1.00 69.63           O  
ANISOU  955  O   SER A 167     8642   8809   9005   -415   -942   1493       O  
ATOM    956  CB  SER A 167       7.104  17.078  -6.070  1.00 67.68           C  
ANISOU  956  CB  SER A 167     8226   8582   8907   -228   -531    989       C  
ATOM    957  OG  SER A 167       6.153  17.737  -5.251  1.00 68.82           O  
ANISOU  957  OG  SER A 167     8295   8591   9261   -104   -663    859       O  
ATOM    958  N   CYS A 168       7.324  20.345  -6.871  1.00 72.75           N  
ANISOU  958  N   CYS A 168     9009   8812   9819   -293  -1126   1446       N  
ATOM    959  CA  CYS A 168       6.648  21.393  -7.631  1.00 73.51           C  
ANISOU  959  CA  CYS A 168     9186   8743  10001   -284  -1466   1607       C  
ATOM    960  C   CYS A 168       7.347  21.747  -8.942  1.00 77.62           C  
ANISOU  960  C   CYS A 168     9848   9341  10301   -524  -1540   1966       C  
ATOM    961  O   CYS A 168       6.638  22.045  -9.918  1.00 81.68           O  
ANISOU  961  O   CYS A 168    10442   9849  10744   -540  -1760   2098       O  
ATOM    962  CB  CYS A 168       6.478  22.640  -6.754  1.00 74.94           C  
ANISOU  962  CB  CYS A 168     9371   8593  10510   -158  -1727   1556       C  
ATOM    963  SG  CYS A 168       5.411  23.906  -7.472  1.00 83.98           S  
ANISOU  963  SG  CYS A 168    10608   9450  11852    -51  -2231   1669       S  
ATOM    964  N   PRO A 169       8.683  21.755  -9.044  1.00 78.38           N  
ANISOU  964  N   PRO A 169     9970   9541  10269   -727  -1380   2136       N  
ATOM    965  CA  PRO A 169       9.296  22.005 -10.360  1.00 83.73           C  
ANISOU  965  CA  PRO A 169    10752  10394  10669   -996  -1410   2471       C  
ATOM    966  C   PRO A 169       8.894  21.001 -11.428  1.00 84.95           C  
ANISOU  966  C   PRO A 169    10900  10878  10501  -1015  -1280   2429       C  
ATOM    967  O   PRO A 169       8.857  21.362 -12.611  1.00 84.19           O  
ANISOU  967  O   PRO A 169    10915  10894  10178  -1189  -1413   2692       O  
ATOM    968  CB  PRO A 169      10.799  21.935 -10.063  1.00 82.55           C  
ANISOU  968  CB  PRO A 169    10540  10383  10443  -1178  -1179   2547       C  
ATOM    969  CG  PRO A 169      10.912  22.332  -8.645  1.00 76.42           C  
ANISOU  969  CG  PRO A 169     9712   9325   9998  -1032  -1220   2380       C  
ATOM    970  CD  PRO A 169       9.698  21.762  -7.973  1.00 74.69           C  
ANISOU  970  CD  PRO A 169     9435   9030   9916   -740  -1219   2057       C  
ATOM    971  N   LEU A 170       8.584  19.755 -11.051  1.00 79.08           N  
ANISOU  971  N   LEU A 170    10044  10281   9723   -856  -1047   2113       N  
ATOM    972  CA  LEU A 170       8.270  18.731 -12.044  1.00 73.43           C  
ANISOU  972  CA  LEU A 170     9322   9863   8714   -871   -932   2033       C  
ATOM    973  C   LEU A 170       7.035  19.090 -12.860  1.00 76.56           C  
ANISOU  973  C   LEU A 170     9801  10208   9081   -835  -1215   2109       C  
ATOM    974  O   LEU A 170       6.917  18.677 -14.020  1.00 77.86           O  
ANISOU  974  O   LEU A 170    10015  10626   8942   -927  -1211   2171       O  
ATOM    975  CB  LEU A 170       8.080  17.380 -11.356  1.00 67.28           C  
ANISOU  975  CB  LEU A 170     8435   9155   7972   -710   -697   1684       C  
ATOM    976  CG  LEU A 170       9.176  16.975 -10.366  1.00 66.79           C  
ANISOU  976  CG  LEU A 170     8297   9091   7988   -692   -470   1577       C  
ATOM    977  CD1 LEU A 170       8.737  15.773  -9.563  1.00 66.74           C  
ANISOU  977  CD1 LEU A 170     8235   9057   8068   -536   -332   1276       C  
ATOM    978  CD2 LEU A 170      10.488  16.689 -11.074  1.00 61.58           C  
ANISOU  978  CD2 LEU A 170     7607   8724   7065   -840   -287   1659       C  
ATOM    979  N   LEU A 171       6.108  19.856 -12.280  1.00 72.91           N  
ANISOU  979  N   LEU A 171     9340   9439   8925   -685  -1477   2076       N  
ATOM    980  CA  LEU A 171       4.945  20.322 -13.024  1.00 75.80           C  
ANISOU  980  CA  LEU A 171     9768   9727   9306   -622  -1806   2146       C  
ATOM    981  C   LEU A 171       5.311  21.339 -14.094  1.00 79.71           C  
ANISOU  981  C   LEU A 171    10460  10190   9637   -830  -2066   2561       C  
ATOM    982  O   LEU A 171       4.541  21.531 -15.041  1.00 84.88           O  
ANISOU  982  O   LEU A 171    11203  10874  10173   -833  -2320   2673       O  
ATOM    983  CB  LEU A 171       3.917  20.942 -12.075  1.00 74.05           C  
ANISOU  983  CB  LEU A 171     9460   9199   9478   -376  -2034   1961       C  
ATOM    984  CG  LEU A 171       2.918  20.015 -11.385  1.00 69.74           C  
ANISOU  984  CG  LEU A 171     8717   8733   9050   -185  -1900   1574       C  
ATOM    985  CD1 LEU A 171       2.056  20.807 -10.416  1.00 68.86           C  
ANISOU  985  CD1 LEU A 171     8486   8373   9305     44  -2112   1385       C  
ATOM    986  CD2 LEU A 171       2.059  19.311 -12.420  1.00 65.45           C  
ANISOU  986  CD2 LEU A 171     8160   8395   8313   -188  -1959   1520       C  
ATOM    987  N   PHE A 172       6.460  21.995 -13.967  1.00 68.04           N  
ANISOU  987  N   PHE A 172     9054   8656   8140  -1028  -2027   2807       N  
ATOM    988  CA  PHE A 172       6.795  23.074 -14.882  1.00 78.77           C  
ANISOU  988  CA  PHE A 172    10620   9942   9366  -1280  -2310   3252       C  
ATOM    989  C   PHE A 172       8.096  22.777 -15.619  1.00 85.91           C  
ANISOU  989  C   PHE A 172    11542  11237   9862  -1615  -2028   3473       C  
ATOM    990  O   PHE A 172       9.011  23.607 -15.641  1.00 88.20           O  
ANISOU  990  O   PHE A 172    11911  11460  10141  -1873  -2078   3779       O  
ATOM    991  CB  PHE A 172       6.876  24.399 -14.118  1.00 84.73           C  
ANISOU  991  CB  PHE A 172    11461  10224  10509  -1254  -2621   3391       C  
ATOM    992  CG  PHE A 172       5.617  24.738 -13.360  1.00 85.93           C  
ANISOU  992  CG  PHE A 172    11551  10035  11063   -893  -2895   3113       C  
ATOM    993  CD1 PHE A 172       4.602  25.461 -13.964  1.00 86.94           C  
ANISOU  993  CD1 PHE A 172    11803   9937  11293   -793  -3356   3232       C  
ATOM    994  CD2 PHE A 172       5.447  24.323 -12.046  1.00 83.56           C  
ANISOU  994  CD2 PHE A 172    11054   9673  11022   -654  -2699   2721       C  
ATOM    995  CE1 PHE A 172       3.443  25.769 -13.275  1.00 83.30           C  
ANISOU  995  CE1 PHE A 172    11232   9212  11208   -436  -3605   2923       C  
ATOM    996  CE2 PHE A 172       4.288  24.629 -11.350  1.00 82.96           C  
ANISOU  996  CE2 PHE A 172    10876   9366  11280   -334  -2919   2431       C  
ATOM    997  CZ  PHE A 172       3.286  25.353 -11.967  1.00 83.10           C  
ANISOU  997  CZ  PHE A 172    10978   9179  11417   -212  -3367   2511       C  
ATOM    998  N   GLY A 173       8.179  21.592 -16.224  1.00 92.00           N  
ANISOU  998  N   GLY A 173    12224  12431  10302  -1618  -1741   3296       N  
ATOM    999  CA  GLY A 173       9.333  21.223 -17.023  1.00 99.29           C  
ANISOU  999  CA  GLY A 173    13120  13810  10797  -1900  -1463   3431       C  
ATOM   1000  C   GLY A 173      10.629  21.114 -16.255  1.00105.40           C  
ANISOU 1000  C   GLY A 173    13746  14661  11642  -1983  -1167   3370       C  
ATOM   1001  O   GLY A 173      11.703  21.225 -16.853  1.00109.34           O  
ANISOU 1001  O   GLY A 173    14209  15498  11836  -2275   -998   3563       O  
ATOM   1002  N   LEU A 174      10.558  20.899 -14.940  1.00100.46           N  
ANISOU 1002  N   LEU A 174    13015  13761  11393  -1742  -1102   3100       N  
ATOM   1003  CA  LEU A 174      11.734  20.873 -14.068  1.00103.35           C  
ANISOU 1003  CA  LEU A 174    13246  14141  11880  -1788   -879   3034       C  
ATOM   1004  C   LEU A 174      12.539  22.163 -14.183  1.00110.64           C  
ANISOU 1004  C   LEU A 174    14250  14960  12828  -2107  -1028   3434       C  
ATOM   1005  O   LEU A 174      13.746  22.179 -13.930  1.00113.38           O  
ANISOU 1005  O   LEU A 174    14470  15481  13128  -2273   -823   3467       O  
ATOM   1006  CB  LEU A 174      12.615  19.654 -14.361  1.00 97.67           C  
ANISOU 1006  CB  LEU A 174    12350  13885  10875  -1796   -492   2806       C  
ATOM   1007  CG  LEU A 174      13.534  19.118 -13.264  1.00 92.37           C  
ANISOU 1007  CG  LEU A 174    11502  13215  10381  -1682   -254   2560       C  
ATOM   1008  CD1 LEU A 174      12.928  19.339 -11.890  1.00 88.80           C  
ANISOU 1008  CD1 LEU A 174    11078  12307  10354  -1450   -387   2419       C  
ATOM   1009  CD2 LEU A 174      13.792  17.638 -13.505  1.00 90.06           C  
ANISOU 1009  CD2 LEU A 174    11076  13252   9891  -1525     22   2210       C  
ATOM   1010  N   ASN A 175      11.863  23.254 -14.556  1.00127.08           N  
ANISOU 1010  N   ASN A 175    16542  16739  15004  -2196  -1417   3738       N  
ATOM   1011  CA  ASN A 175      12.511  24.539 -14.814  1.00131.09           C  
ANISOU 1011  CA  ASN A 175    17185  17092  15530  -2547  -1637   4178       C  
ATOM   1012  C   ASN A 175      13.737  24.358 -15.706  1.00135.52           C  
ANISOU 1012  C   ASN A 175    17627  18169  15696  -2875  -1339   4267       C  
ATOM   1013  O   ASN A 175      14.777  24.991 -15.516  1.00141.49           O  
ANISOU 1013  O   ASN A 175    18317  18930  16514  -3096  -1295   4368       O  
ATOM   1014  CB  ASN A 175      12.876  25.244 -13.504  1.00127.19           C  
ANISOU 1014  CB  ASN A 175    16665  16177  15484  -2475  -1748   4122       C  
ATOM   1015  CG  ASN A 175      11.656  25.790 -12.774  1.00121.37           C  
ANISOU 1015  CG  ASN A 175    16035  14913  15169  -2144  -2109   3974       C  
ATOM   1016  OD1 ASN A 175      10.689  26.228 -13.400  1.00120.30           O  
ANISOU 1016  OD1 ASN A 175    16064  14605  15041  -2092  -2430   4105       O  
ATOM   1017  ND2 ASN A 175      11.697  25.764 -11.445  1.00115.08           N  
ANISOU 1017  ND2 ASN A 175    15127  13886  14713  -1906  -2061   3672       N  
ATOM   1018  N   ASN A 176      13.611  23.469 -16.686  1.00138.51           N  
ANISOU 1018  N   ASN A 176    17960  19005  15662  -2893  -1141   4194       N  
ATOM   1019  CA  ASN A 176      14.702  23.139 -17.593  1.00128.90           C  
ANISOU 1019  CA  ASN A 176    16590  18346  14041  -3148   -837   4194       C  
ATOM   1020  C   ASN A 176      14.143  23.135 -19.012  1.00130.29           C  
ANISOU 1020  C   ASN A 176    16893  18756  13854  -3256   -934   4312       C  
ATOM   1021  O   ASN A 176      13.054  23.656 -19.280  1.00128.25           O  
ANISOU 1021  O   ASN A 176    16856  18174  13701  -3186  -1280   4456       O  
ATOM   1022  CB  ASN A 176      15.347  21.804 -17.188  1.00114.40           C  
ANISOU 1022  CB  ASN A 176    14490  16909  12066  -3004   -416   3849       C  
ATOM   1023  N   ALA A 177      14.888  22.541 -19.940  1.00131.35           N  
ANISOU 1023  N   ALA A 177    16876  19466  13564  -3410   -639   4223       N  
ATOM   1024  CA  ALA A 177      14.518  22.512 -21.354  1.00133.06           C  
ANISOU 1024  CA  ALA A 177    17193  19978  13388  -3547   -695   4324       C  
ATOM   1025  C   ALA A 177      13.850  21.175 -21.665  1.00139.43           C  
ANISOU 1025  C   ALA A 177    17953  21060  13966  -3279   -543   3999       C  
ATOM   1026  O   ALA A 177      14.499  20.218 -22.087  1.00134.42           O  
ANISOU 1026  O   ALA A 177    17113  20932  13028  -3260   -210   3722       O  
ATOM   1027  CB  ALA A 177      15.744  22.740 -22.230  1.00132.82           C  
ANISOU 1027  CB  ALA A 177    17018  20431  13018  -3895   -487   4415       C  
ATOM   1028  N   ASP A 178      12.535  21.113 -21.456  1.00139.56           N  
ANISOU 1028  N   ASP A 178    18147  20737  14141  -3057   -814   4002       N  
ATOM   1029  CA  ASP A 178      11.738  19.985 -21.927  1.00140.00           C  
ANISOU 1029  CA  ASP A 178    18203  21034  13957  -2843   -761   3735       C  
ATOM   1030  C   ASP A 178      10.328  20.465 -22.235  1.00139.46           C  
ANISOU 1030  C   ASP A 178    18375  20618  13994  -2746  -1185   3897       C  
ATOM   1031  O   ASP A 178       9.372  20.082 -21.554  1.00142.64           O  
ANISOU 1031  O   ASP A 178    18808  20766  14622  -2479  -1336   3761       O  
ATOM   1032  CB  ASP A 178      11.711  18.857 -20.894  1.00137.06           C  
ANISOU 1032  CB  ASP A 178    17675  20675  13728  -2556   -547   3368       C  
ATOM   1033  N   GLN A 179      10.191  21.295 -23.270  1.00143.02           N  
ANISOU 1033  N   GLN A 179    18983  21074  14284  -2960  -1392   4178       N  
ATOM   1034  CA  GLN A 179       8.987  22.105 -23.424  1.00133.33           C  
ANISOU 1034  CA  GLN A 179    17987  19403  13269  -2879  -1859   4383       C  
ATOM   1035  C   GLN A 179       7.753  21.243 -23.675  1.00128.51           C  
ANISOU 1035  C   GLN A 179    17406  18844  12578  -2605  -1987   4153       C  
ATOM   1036  O   GLN A 179       6.787  21.279 -22.902  1.00124.40           O  
ANISOU 1036  O   GLN A 179    16911  17946  12410  -2345  -2237   4071       O  
ATOM   1037  CB  GLN A 179       9.188  23.117 -24.553  1.00132.56           C  
ANISOU 1037  CB  GLN A 179    18056  19342  12970  -3191  -2041   4737       C  
ATOM   1038  N   ASN A 180       7.766  20.455 -24.749  1.00126.77           N  
ANISOU 1038  N   ASN A 180    17160  19104  11903  -2656  -1831   4014       N  
ATOM   1039  CA  ASN A 180       6.565  19.780 -25.230  1.00115.92           C  
ANISOU 1039  CA  ASN A 180    15839  17790  10414  -2448  -2017   3825       C  
ATOM   1040  C   ASN A 180       6.535  18.292 -24.886  1.00111.57           C  
ANISOU 1040  C   ASN A 180    15109  17542   9741  -2253  -1745   3379       C  
ATOM   1041  O   ASN A 180       5.949  17.498 -25.625  1.00103.18           O  
ANISOU 1041  O   ASN A 180    14050  16740   8415  -2166  -1771   3154       O  
ATOM   1042  CB  ASN A 180       6.419  19.972 -26.739  1.00115.56           C  
ANISOU 1042  CB  ASN A 180    15926  18028   9952  -2620  -2110   3964       C  
ATOM   1043  N   GLU A 181       7.135  17.896 -23.764  1.00104.62           N  
ANISOU 1043  N   GLU A 181    14065  16578   9107  -2156  -1490   3195       N  
ATOM   1044  CA  GLU A 181       7.136  16.494 -23.369  1.00106.80           C  
ANISOU 1044  CA  GLU A 181    14149  16965   9465  -1902  -1204   2656       C  
ATOM   1045  C   GLU A 181       6.948  16.366 -21.867  1.00100.72           C  
ANISOU 1045  C   GLU A 181    13266  15721   9281  -1661  -1157   2456       C  
ATOM   1046  O   GLU A 181       7.211  17.295 -21.099  1.00102.83           O  
ANISOU 1046  O   GLU A 181    13557  15677   9838  -1708  -1233   2688       O  
ATOM   1047  CB  GLU A 181       8.426  15.780 -23.782  1.00111.20           C  
ANISOU 1047  CB  GLU A 181    14562  18052   9639  -2014   -799   2478       C  
ATOM   1048  CG  GLU A 181       8.455  15.363 -25.237  1.00118.18           C  
ANISOU 1048  CG  GLU A 181    15491  19499   9912  -2150   -768   2439       C  
ATOM   1049  CD  GLU A 181       9.558  14.373 -25.529  1.00125.80           C  
ANISOU 1049  CD  GLU A 181    16244  20936  10620  -2119   -359   2054       C  
ATOM   1050  OE1 GLU A 181       9.649  13.356 -24.809  1.00127.00           O  
ANISOU 1050  OE1 GLU A 181    16258  20997  10999  -1858   -200   1630       O  
ATOM   1051  OE2 GLU A 181      10.339  14.618 -26.473  1.00132.18           O  
ANISOU 1051  OE2 GLU A 181    16999  22090  11133  -2311   -210   2123       O  
ATOM   1052  N   CYS A 182       6.490  15.185 -21.461  1.00 85.77           N  
ANISOU 1052  N   CYS A 182    11262  13784   7544  -1421  -1042   2020       N  
ATOM   1053  CA  CYS A 182       6.326  14.886 -20.051  1.00 85.01           C  
ANISOU 1053  CA  CYS A 182    11057  13309   7934  -1219   -963   1809       C  
ATOM   1054  C   CYS A 182       7.659  15.034 -19.325  1.00 85.25           C  
ANISOU 1054  C   CYS A 182    10998  13354   8038  -1280   -699   1848       C  
ATOM   1055  O   CYS A 182       8.737  14.991 -19.927  1.00 87.66           O  
ANISOU 1055  O   CYS A 182    11266  14030   8011  -1441   -506   1910       O  
ATOM   1056  CB  CYS A 182       5.770  13.473 -19.864  1.00 85.07           C  
ANISOU 1056  CB  CYS A 182    10980  13320   8021  -1022   -869   1364       C  
ATOM   1057  SG  CYS A 182       5.430  13.056 -18.147  1.00 88.55           S  
ANISOU 1057  SG  CYS A 182    11313  13325   9006   -826   -793   1143       S  
ATOM   1058  N   ILE A 183       7.575  15.222 -18.009  1.00 86.69           N  
ANISOU 1058  N   ILE A 183    11127  13162   8650  -1153   -694   1796       N  
ATOM   1059  CA  ILE A 183       8.782  15.505 -17.243  1.00 88.06           C  
ANISOU 1059  CA  ILE A 183    11221  13307   8931  -1209   -498   1856       C  
ATOM   1060  C   ILE A 183       9.631  14.253 -17.070  1.00 90.76           C  
ANISOU 1060  C   ILE A 183    11430  13873   9183  -1113   -193   1518       C  
ATOM   1061  O   ILE A 183      10.856  14.349 -16.944  1.00 89.70           O  
ANISOU 1061  O   ILE A 183    11199  13916   8966  -1199     -1   1550       O  
ATOM   1062  CB  ILE A 183       8.428  16.141 -15.888  1.00 82.65           C  
ANISOU 1062  CB  ILE A 183    10529  12169   8706  -1098   -610   1893       C  
ATOM   1063  CG1 ILE A 183       9.689  16.703 -15.236  1.00 81.90           C  
ANISOU 1063  CG1 ILE A 183    10377  12044   8696  -1203   -475   2026       C  
ATOM   1064  CG2 ILE A 183       7.755  15.134 -14.972  1.00 80.02           C  
ANISOU 1064  CG2 ILE A 183    10121  11657   8626   -869   -543   1542       C  
ATOM   1065  CD1 ILE A 183      10.562  17.486 -16.201  1.00 77.13           C  
ANISOU 1065  CD1 ILE A 183     9815  11711   7778  -1501   -472   2363       C  
ATOM   1066  N   ILE A 184       9.020  13.066 -17.078  1.00 86.05           N  
ANISOU 1066  N   ILE A 184    10817  13266   8612   -938   -167   1182       N  
ATOM   1067  CA  ILE A 184       9.808  11.848 -16.945  1.00 81.50           C  
ANISOU 1067  CA  ILE A 184    10141  12849   7978   -818     61    843       C  
ATOM   1068  C   ILE A 184      10.649  11.603 -18.187  1.00 77.44           C  
ANISOU 1068  C   ILE A 184     9566  12848   7010   -918    205    786       C  
ATOM   1069  O   ILE A 184      11.589  10.802 -18.148  1.00 77.18           O  
ANISOU 1069  O   ILE A 184     9408  13014   6904   -822    403    514       O  
ATOM   1070  CB  ILE A 184       8.907  10.636 -16.645  1.00 80.64           C  
ANISOU 1070  CB  ILE A 184    10060  12549   8030   -635      7    515       C  
ATOM   1071  CG1 ILE A 184       9.694   9.574 -15.876  1.00 78.25           C  
ANISOU 1071  CG1 ILE A 184     9688  12171   7873   -478    168    222       C  
ATOM   1072  CG2 ILE A 184       8.346  10.052 -17.932  1.00 83.92           C  
ANISOU 1072  CG2 ILE A 184    10523  13226   8137   -643    -67    367       C  
ATOM   1073  CD1 ILE A 184       8.861   8.383 -15.456  1.00 80.33           C  
ANISOU 1073  CD1 ILE A 184    10011  12185   8326   -346     90    -54       C  
ATOM   1074  N   ALA A 185      10.335  12.279 -19.291  1.00 80.23           N  
ANISOU 1074  N   ALA A 185     9999  13442   7044  -1105     98   1028       N  
ATOM   1075  CA  ALA A 185      11.162  12.234 -20.487  1.00 83.51           C  
ANISOU 1075  CA  ALA A 185    10349  14420   6960  -1262    251   1031       C  
ATOM   1076  C   ALA A 185      12.352  13.177 -20.411  1.00 83.75           C  
ANISOU 1076  C   ALA A 185    10288  14647   6887  -1499    393   1327       C  
ATOM   1077  O   ALA A 185      13.207  13.143 -21.301  1.00 89.61           O  
ANISOU 1077  O   ALA A 185    10921  15924   7202  -1661    576   1320       O  
ATOM   1078  CB  ALA A 185      10.320  12.565 -21.723  1.00 73.89           C  
ANISOU 1078  CB  ALA A 185     9279  13403   5395  -1401     57   1201       C  
ATOM   1079  N   ASN A 186      12.425  14.011 -19.384  1.00 87.95           N  
ANISOU 1079  N   ASN A 186    10846  14788   7782  -1536    315   1567       N  
ATOM   1080  CA  ASN A 186      13.545  14.931 -19.235  1.00 90.37           C  
ANISOU 1080  CA  ASN A 186    11066  15232   8039  -1784    421   1852       C  
ATOM   1081  C   ASN A 186      14.781  14.156 -18.795  1.00 93.04           C  
ANISOU 1081  C   ASN A 186    11153  15806   8392  -1671    718   1526       C  
ATOM   1082  O   ASN A 186      14.734  13.472 -17.765  1.00 90.82           O  
ANISOU 1082  O   ASN A 186    10830  15214   8462  -1399    737   1252       O  
ATOM   1083  CB  ASN A 186      13.200  16.017 -18.220  1.00 86.22           C  
ANISOU 1083  CB  ASN A 186    10651  14175   7934  -1820    209   2150       C  
ATOM   1084  CG  ASN A 186      14.162  17.185 -18.259  1.00 89.29           C  
ANISOU 1084  CG  ASN A 186    11013  14659   8255  -2152    225   2537       C  
ATOM   1085  OD1 ASN A 186      15.380  17.008 -18.241  1.00 95.97           O  
ANISOU 1085  OD1 ASN A 186    11655  15837   8971  -2255    479   2464       O  
ATOM   1086  ND2 ASN A 186      13.616  18.393 -18.314  1.00 87.60           N  
ANISOU 1086  ND2 ASN A 186    10997  14142   8145  -2325    -71   2943       N  
ATOM   1087  N   PRO A 187      15.895  14.232 -19.527  1.00 95.07           N  
ANISOU 1087  N   PRO A 187    11229  16621   8273  -1873    941   1541       N  
ATOM   1088  CA  PRO A 187      17.095  13.486 -19.110  1.00 94.27           C  
ANISOU 1088  CA  PRO A 187    10845  16765   8209  -1726   1203   1183       C  
ATOM   1089  C   PRO A 187      17.587  13.857 -17.721  1.00 93.98           C  
ANISOU 1089  C   PRO A 187    10749  16330   8627  -1662   1185   1242       C  
ATOM   1090  O   PRO A 187      18.317  13.067 -17.109  1.00 94.56           O  
ANISOU 1090  O   PRO A 187    10638  16436   8855  -1433   1319    896       O  
ATOM   1091  CB  PRO A 187      18.127  13.845 -20.190  1.00 87.30           C  
ANISOU 1091  CB  PRO A 187     9769  16534   6867  -2026   1406   1271       C  
ATOM   1092  CG  PRO A 187      17.630  15.128 -20.784  1.00 81.91           C  
ANISOU 1092  CG  PRO A 187     9311  15710   6102  -2368   1189   1793       C  
ATOM   1093  CD  PRO A 187      16.135  15.035 -20.737  1.00 89.48           C  
ANISOU 1093  CD  PRO A 187    10552  16349   7098  -2256    952   1890       C  
ATOM   1094  N   ALA A 188      17.198  15.020 -17.198  1.00 89.90           N  
ANISOU 1094  N   ALA A 188    10393  15427   8337  -1837    994   1648       N  
ATOM   1095  CA  ALA A 188      17.621  15.462 -15.877  1.00 87.20           C  
ANISOU 1095  CA  ALA A 188    10012  14708   8411  -1788    952   1704       C  
ATOM   1096  C   ALA A 188      16.681  15.017 -14.764  1.00 83.84           C  
ANISOU 1096  C   ALA A 188     9732  13727   8396  -1473    795   1536       C  
ATOM   1097  O   ALA A 188      16.983  15.253 -13.591  1.00 75.80           O  
ANISOU 1097  O   ALA A 188     8687  12406   7707  -1395    761   1530       O  
ATOM   1098  CB  ALA A 188      17.750  16.987 -15.848  1.00 80.85           C  
ANISOU 1098  CB  ALA A 188     9302  13764   7654  -2142    804   2201       C  
ATOM   1099  N   PHE A 189      15.554  14.386 -15.094  1.00 80.92           N  
ANISOU 1099  N   PHE A 189     9504  13244   7997  -1314    698   1400       N  
ATOM   1100  CA  PHE A 189      14.640  13.936 -14.051  1.00 78.27           C  
ANISOU 1100  CA  PHE A 189     9281  12440   8018  -1065    570   1248       C  
ATOM   1101  C   PHE A 189      15.276  12.851 -13.193  1.00 80.35           C  
ANISOU 1101  C   PHE A 189     9430  12648   8450   -824    697    901       C  
ATOM   1102  O   PHE A 189      15.128  12.856 -11.964  1.00 75.11           O  
ANISOU 1102  O   PHE A 189     8806  11626   8105   -710    633    876       O  
ATOM   1103  CB  PHE A 189      13.335  13.437 -14.671  1.00 80.58           C  
ANISOU 1103  CB  PHE A 189     9715  12675   8225   -983    445   1165       C  
ATOM   1104  CG  PHE A 189      12.426  12.754 -13.693  1.00 85.91           C  
ANISOU 1104  CG  PHE A 189    10465  12965   9214   -760    358    965       C  
ATOM   1105  CD1 PHE A 189      11.690  13.490 -12.780  1.00 86.83           C  
ANISOU 1105  CD1 PHE A 189    10658  12708   9625   -749    203   1115       C  
ATOM   1106  CD2 PHE A 189      12.306  11.375 -13.683  1.00 84.50           C  
ANISOU 1106  CD2 PHE A 189    10274  12804   9028   -575    421    619       C  
ATOM   1107  CE1 PHE A 189      10.853  12.861 -11.873  1.00 82.22           C  
ANISOU 1107  CE1 PHE A 189    10115  11841   9283   -588    152    936       C  
ATOM   1108  CE2 PHE A 189      11.471  10.742 -12.779  1.00 79.97           C  
ANISOU 1108  CE2 PHE A 189     9777  11887   8720   -435    339    479       C  
ATOM   1109  CZ  PHE A 189      10.745  11.486 -11.874  1.00 75.49           C  
ANISOU 1109  CZ  PHE A 189     9262  11015   8404   -457    224    645       C  
ATOM   1110  N   VAL A 190      15.990  11.913 -13.820  1.00 82.64           N  
ANISOU 1110  N   VAL A 190     9581  13296   8524   -736    857    620       N  
ATOM   1111  CA  VAL A 190      16.608  10.825 -13.066  1.00 79.80           C  
ANISOU 1111  CA  VAL A 190     9129  12855   8338   -476    921    274       C  
ATOM   1112  C   VAL A 190      17.619  11.375 -12.070  1.00 73.96           C  
ANISOU 1112  C   VAL A 190     8263  12038   7801   -501    965    362       C  
ATOM   1113  O   VAL A 190      17.647  10.963 -10.905  1.00 69.81           O  
ANISOU 1113  O   VAL A 190     7780  11184   7561   -328    899    257       O  
ATOM   1114  CB  VAL A 190      17.246   9.799 -14.024  1.00 76.29           C  
ANISOU 1114  CB  VAL A 190     8531  12834   7621   -350   1058    -85       C  
ATOM   1115  CG1 VAL A 190      18.329   8.997 -13.321  1.00 73.98           C  
ANISOU 1115  CG1 VAL A 190     8071  12543   7496   -111   1121   -401       C  
ATOM   1116  CG2 VAL A 190      16.181   8.863 -14.570  1.00 70.22           C  
ANISOU 1116  CG2 VAL A 190     7922  11973   6787   -219    957   -292       C  
ATOM   1117  N   VAL A 191      18.449  12.327 -12.502  1.00 74.89           N  
ANISOU 1117  N   VAL A 191     8232  12459   7764   -745   1062    574       N  
ATOM   1118  CA  VAL A 191      19.440  12.910 -11.603  1.00 69.99           C  
ANISOU 1118  CA  VAL A 191     7472  11783   7337   -800   1089    659       C  
ATOM   1119  C   VAL A 191      18.756  13.666 -10.472  1.00 71.73           C  
ANISOU 1119  C   VAL A 191     7882  11494   7879   -818    904    880       C  
ATOM   1120  O   VAL A 191      19.167  13.580  -9.308  1.00 74.22           O  
ANISOU 1120  O   VAL A 191     8168  11584   8449   -696    866    802       O  
ATOM   1121  CB  VAL A 191      20.401  13.820 -12.387  1.00 69.86           C  
ANISOU 1121  CB  VAL A 191     7256  12216   7071  -1128   1224    873       C  
ATOM   1122  CG1 VAL A 191      21.588  14.210 -11.518  1.00 61.69           C  
ANISOU 1122  CG1 VAL A 191     6014  11194   6229  -1167   1269    875       C  
ATOM   1123  CG2 VAL A 191      20.860  13.135 -13.669  1.00 71.25           C  
ANISOU 1123  CG2 VAL A 191     7250  12975   6848  -1136   1419    651       C  
ATOM   1124  N   TYR A 192      17.698  14.409 -10.792  1.00 73.30           N  
ANISOU 1124  N   TYR A 192     8269  11519   8064   -952    769   1133       N  
ATOM   1125  CA  TYR A 192      17.008  15.209  -9.786  1.00 69.49           C  
ANISOU 1125  CA  TYR A 192     7937  10591   7877   -952    585   1300       C  
ATOM   1126  C   TYR A 192      16.386  14.323  -8.714  1.00 69.05           C  
ANISOU 1126  C   TYR A 192     7966  10230   8040   -683    540   1063       C  
ATOM   1127  O   TYR A 192      16.743  14.407  -7.534  1.00 70.50           O  
ANISOU 1127  O   TYR A 192     8135  10210   8443   -602    510   1018       O  
ATOM   1128  CB  TYR A 192      15.946  16.079 -10.460  1.00 70.53           C  
ANISOU 1128  CB  TYR A 192     8235  10616   7948  -1102    419   1566       C  
ATOM   1129  CG  TYR A 192      15.223  17.022  -9.524  1.00 71.79           C  
ANISOU 1129  CG  TYR A 192     8522  10343   8412  -1083    204   1704       C  
ATOM   1130  CD1 TYR A 192      15.814  18.212  -9.114  1.00 72.52           C  
ANISOU 1130  CD1 TYR A 192     8604  10305   8647  -1251    105   1926       C  
ATOM   1131  CD2 TYR A 192      13.943  16.733  -9.066  1.00 75.40           C  
ANISOU 1131  CD2 TYR A 192     9093  10543   9014   -904     92   1589       C  
ATOM   1132  CE1 TYR A 192      15.157  19.082  -8.265  1.00 72.60           C  
ANISOU 1132  CE1 TYR A 192     8724   9917   8942  -1200   -114   1996       C  
ATOM   1133  CE2 TYR A 192      13.275  17.600  -8.217  1.00 78.40           C  
ANISOU 1133  CE2 TYR A 192     9549  10580   9658   -860    -96   1656       C  
ATOM   1134  CZ  TYR A 192      13.887  18.772  -7.820  1.00 72.16           C  
ANISOU 1134  CZ  TYR A 192     8758   9648   9013   -988   -206   1843       C  
ATOM   1135  OH  TYR A 192      13.226  19.632  -6.973  1.00 63.34           O  
ANISOU 1135  OH  TYR A 192     7711   8188   8168   -909   -415   1853       O  
ATOM   1136  N   SER A 193      15.457  13.449  -9.114  1.00 72.61           N  
ANISOU 1136  N   SER A 193     8511  10659   8417   -566    526    916       N  
ATOM   1137  CA  SER A 193      14.715  12.654  -8.139  1.00 77.34           C  
ANISOU 1137  CA  SER A 193     9213  10968   9205   -382    469    746       C  
ATOM   1138  C   SER A 193      15.615  11.681  -7.386  1.00 75.22           C  
ANISOU 1138  C   SER A 193     8884  10678   9019   -217    535    524       C  
ATOM   1139  O   SER A 193      15.294  11.286  -6.260  1.00 76.80           O  
ANISOU 1139  O   SER A 193     9170  10614   9397   -116    473    460       O  
ATOM   1140  CB  SER A 193      13.580  11.897  -8.830  1.00 79.11           C  
ANISOU 1140  CB  SER A 193     9536  11195   9327   -336    430    640       C  
ATOM   1141  OG  SER A 193      14.075  10.934  -9.741  1.00 69.99           O  
ANISOU 1141  OG  SER A 193     8324  10300   7968   -274    524    442       O  
ATOM   1142  N   SER A 194      16.739  11.283  -7.980  1.00 71.25           N  
ANISOU 1142  N   SER A 194     8226  10467   8381   -186    646    398       N  
ATOM   1143  CA  SER A 194      17.664  10.407  -7.271  1.00 72.26           C  
ANISOU 1143  CA  SER A 194     8279  10561   8614      6    663    171       C  
ATOM   1144  C   SER A 194      18.401  11.166  -6.177  1.00 76.18           C  
ANISOU 1144  C   SER A 194     8709  10947   9290    -29    635    286       C  
ATOM   1145  O   SER A 194      18.423  10.741  -5.014  1.00 72.02           O  
ANISOU 1145  O   SER A 194     8263  10164   8939     99    550    218       O  
ATOM   1146  CB  SER A 194      18.661   9.784  -8.246  1.00 72.31           C  
ANISOU 1146  CB  SER A 194     8087  10955   8432     84    784    -57       C  
ATOM   1147  OG  SER A 194      17.998   9.092  -9.286  1.00 80.43           O  
ANISOU 1147  OG  SER A 194     9180  12101   9277    122    797   -194       O  
ATOM   1148  N   ILE A 195      19.005  12.300  -6.530  1.00 77.08           N  
ANISOU 1148  N   ILE A 195     8687  11249   9349   -226    688    474       N  
ATOM   1149  CA  ILE A 195      19.847  13.021  -5.580  1.00 70.51           C  
ANISOU 1149  CA  ILE A 195     7763  10342   8685   -272    652    555       C  
ATOM   1150  C   ILE A 195      18.988  13.748  -4.552  1.00 66.52           C  
ANISOU 1150  C   ILE A 195     7438   9466   8370   -304    511    708       C  
ATOM   1151  O   ILE A 195      19.129  13.541  -3.341  1.00 74.63           O  
ANISOU 1151  O   ILE A 195     8511  10286   9557   -186    438    633       O  
ATOM   1152  CB  ILE A 195      20.787  13.987  -6.321  1.00 68.49           C  
ANISOU 1152  CB  ILE A 195     7299  10412   8313   -520    744    715       C  
ATOM   1153  CG1 ILE A 195      21.784  13.200  -7.177  1.00 66.22           C  
ANISOU 1153  CG1 ILE A 195     6764  10568   7828   -459    911    488       C  
ATOM   1154  CG2 ILE A 195      21.510  14.892  -5.337  1.00 63.89           C  
ANISOU 1154  CG2 ILE A 195     6643   9700   7932   -613    668    829       C  
ATOM   1155  CD1 ILE A 195      22.738  14.064  -7.971  1.00 56.97           C  
ANISOU 1155  CD1 ILE A 195     5348   9813   6484   -752   1041    642       C  
ATOM   1156  N   VAL A 196      18.073  14.597  -5.019  1.00 62.66           N  
ANISOU 1156  N   VAL A 196     7052   8902   7854   -450    454    905       N  
ATOM   1157  CA  VAL A 196      17.332  15.463  -4.105  1.00 67.97           C  
ANISOU 1157  CA  VAL A 196     7847   9264   8715   -469    309   1012       C  
ATOM   1158  C   VAL A 196      16.343  14.656  -3.269  1.00 67.07           C  
ANISOU 1158  C   VAL A 196     7868   8944   8670   -296    275    861       C  
ATOM   1159  O   VAL A 196      16.268  14.814  -2.046  1.00 61.49           O  
ANISOU 1159  O   VAL A 196     7206   8054   8102   -231    210    818       O  
ATOM   1160  CB  VAL A 196      16.626  16.582  -4.888  1.00 64.23           C  
ANISOU 1160  CB  VAL A 196     7440   8750   8216   -643    212   1244       C  
ATOM   1161  CG1 VAL A 196      15.849  17.474  -3.945  1.00 52.97           C  
ANISOU 1161  CG1 VAL A 196     6116   7001   7009   -610     37   1287       C  
ATOM   1162  CG2 VAL A 196      17.638  17.392  -5.674  1.00 71.96           C  
ANISOU 1162  CG2 VAL A 196     8304   9935   9102   -883    238   1445       C  
ATOM   1163  N   SER A 197      15.571  13.778  -3.911  1.00 68.31           N  
ANISOU 1163  N   SER A 197     8091   9151   8712   -244    315    780       N  
ATOM   1164  CA  SER A 197      14.505  13.073  -3.211  1.00 64.29           C  
ANISOU 1164  CA  SER A 197     7706   8466   8256   -150    280    676       C  
ATOM   1165  C   SER A 197      14.986  11.839  -2.460  1.00 64.86           C  
ANISOU 1165  C   SER A 197     7819   8478   8346    -22    301    516       C  
ATOM   1166  O   SER A 197      14.304  11.401  -1.528  1.00 71.84           O  
ANISOU 1166  O   SER A 197     8812   9202   9284      7    262    476       O  
ATOM   1167  CB  SER A 197      13.401  12.668  -4.191  1.00 64.34           C  
ANISOU 1167  CB  SER A 197     7768   8525   8155   -175    281    661       C  
ATOM   1168  OG  SER A 197      12.416  13.677  -4.297  1.00 65.40           O  
ANISOU 1168  OG  SER A 197     7921   8583   8345   -241    188    775       O  
ATOM   1169  N   PHE A 198      16.134  11.265  -2.824  1.00 56.65           N  
ANISOU 1169  N   PHE A 198     6693   7571   7259     50    348    422       N  
ATOM   1170  CA  PHE A 198      16.563  10.006  -2.225  1.00 61.84           C  
ANISOU 1170  CA  PHE A 198     7413   8131   7953    205    308    258       C  
ATOM   1171  C   PHE A 198      17.951  10.080  -1.597  1.00 66.94           C  
ANISOU 1171  C   PHE A 198     7945   8814   8677    293    283    207       C  
ATOM   1172  O   PHE A 198      18.076   9.853  -0.391  1.00 63.30           O  
ANISOU 1172  O   PHE A 198     7574   8170   8306    352    191    202       O  
ATOM   1173  CB  PHE A 198      16.518   8.887  -3.269  1.00 62.27           C  
ANISOU 1173  CB  PHE A 198     7477   8279   7904    290    331     91       C  
ATOM   1174  CG  PHE A 198      16.836   7.525  -2.714  1.00 71.87           C  
ANISOU 1174  CG  PHE A 198     8800   9318   9188    461    226    -82       C  
ATOM   1175  CD1 PHE A 198      15.889   6.822  -1.986  1.00 73.26           C  
ANISOU 1175  CD1 PHE A 198     9194   9229   9414    432    130    -54       C  
ATOM   1176  CD2 PHE A 198      18.074   6.944  -2.927  1.00 66.14           C  
ANISOU 1176  CD2 PHE A 198     7955   8695   8481    641    204   -273       C  
ATOM   1177  CE1 PHE A 198      16.173   5.566  -1.481  1.00 70.07           C  
ANISOU 1177  CE1 PHE A 198     8932   8611   9079    560    -15   -171       C  
ATOM   1178  CE2 PHE A 198      18.365   5.687  -2.423  1.00 70.55           C  
ANISOU 1178  CE2 PHE A 198     8637   9036   9134    826     45   -436       C  
ATOM   1179  CZ  PHE A 198      17.412   4.997  -1.700  1.00 69.64           C  
ANISOU 1179  CZ  PHE A 198     8787   8602   9070    775    -79   -363       C  
ATOM   1180  N   TYR A 199      18.996  10.380  -2.373  1.00 67.17           N  
ANISOU 1180  N   TYR A 199     7766   9103   8654    290    360    166       N  
ATOM   1181  CA  TYR A 199      20.356  10.230  -1.861  1.00 67.05           C  
ANISOU 1181  CA  TYR A 199     7598   9159   8719    402    329     58       C  
ATOM   1182  C   TYR A 199      20.656  11.224  -0.746  1.00 67.17           C  
ANISOU 1182  C   TYR A 199     7604   9058   8859    323    261    193       C  
ATOM   1183  O   TYR A 199      21.379  10.897   0.202  1.00 60.26           O  
ANISOU 1183  O   TYR A 199     6716   8098   8082    445    161    112       O  
ATOM   1184  CB  TYR A 199      21.367  10.375  -2.997  1.00 71.88           C  
ANISOU 1184  CB  TYR A 199     7935  10155   9221    380    457    -32       C  
ATOM   1185  CG  TYR A 199      21.372   9.197  -3.942  1.00 81.30           C  
ANISOU 1185  CG  TYR A 199     9102  11489  10299    540    498   -275       C  
ATOM   1186  CD1 TYR A 199      21.185   7.907  -3.469  1.00 86.13           C  
ANISOU 1186  CD1 TYR A 199     9871  11856  10998    769    359   -463       C  
ATOM   1187  CD2 TYR A 199      21.545   9.374  -5.307  1.00 83.10           C  
ANISOU 1187  CD2 TYR A 199     9165  12088  10320    449    652   -315       C  
ATOM   1188  CE1 TYR A 199      21.177   6.825  -4.325  1.00 85.63           C  
ANISOU 1188  CE1 TYR A 199     9799  11878  10859    933    355   -719       C  
ATOM   1189  CE2 TYR A 199      21.538   8.297  -6.171  1.00 80.51           C  
ANISOU 1189  CE2 TYR A 199     8809  11905   9875    615    680   -585       C  
ATOM   1190  CZ  TYR A 199      21.352   7.026  -5.674  1.00 76.43           C  
ANISOU 1190  CZ  TYR A 199     8448  11104   9487    871    522   -803       C  
ATOM   1191  OH  TYR A 199      21.344   5.950  -6.531  1.00 69.70           O  
ANISOU 1191  OH  TYR A 199     7579  10355   8547   1053    510  -1106       O  
ATOM   1192  N   VAL A 200      20.116  12.435  -0.831  1.00 65.74           N  
ANISOU 1192  N   VAL A 200     7439   8856   8685    133    281    383       N  
ATOM   1193  CA  VAL A 200      20.375  13.434   0.206  1.00 71.58           C  
ANISOU 1193  CA  VAL A 200     8173   9468   9555     66    193    476       C  
ATOM   1194  C   VAL A 200      19.616  13.076   1.483  1.00 70.25           C  
ANISOU 1194  C   VAL A 200     8210   9046   9435    156     95    445       C  
ATOM   1195  O   VAL A 200      20.203  13.156   2.571  1.00 66.48           O  
ANISOU 1195  O   VAL A 200     7736   8490   9035    213      0    407       O  
ATOM   1196  CB  VAL A 200      20.038  14.854  -0.281  1.00 71.46           C  
ANISOU 1196  CB  VAL A 200     8129   9461   9562   -148    192    671       C  
ATOM   1197  CG1 VAL A 200      20.109  15.848   0.873  1.00 70.31           C  
ANISOU 1197  CG1 VAL A 200     8017   9123   9575   -187     60    720       C  
ATOM   1198  CG2 VAL A 200      20.992  15.264  -1.393  1.00 67.72           C  
ANISOU 1198  CG2 VAL A 200     7444   9277   9011   -300    285    742       C  
ATOM   1199  N   PRO A 201      18.333  12.691   1.432  1.00 68.63           N  
ANISOU 1199  N   PRO A 201     8167   8739   9171    150    111    459       N  
ATOM   1200  CA  PRO A 201      17.717  12.147   2.655  1.00 67.01           C  
ANISOU 1200  CA  PRO A 201     8135   8363   8962    204     43    424       C  
ATOM   1201  C   PRO A 201      18.416  10.898   3.166  1.00 63.12           C  
ANISOU 1201  C   PRO A 201     7712   7811   8461    342    -32    331       C  
ATOM   1202  O   PRO A 201      18.541  10.711   4.383  1.00 64.72           O  
ANISOU 1202  O   PRO A 201     8019   7903   8669    376   -131    332       O  
ATOM   1203  CB  PRO A 201      16.275  11.860   2.217  1.00 66.92           C  
ANISOU 1203  CB  PRO A 201     8227   8319   8879    142     97    446       C  
ATOM   1204  CG  PRO A 201      16.022  12.833   1.137  1.00 66.63           C  
ANISOU 1204  CG  PRO A 201     8086   8379   8852     55    144    523       C  
ATOM   1205  CD  PRO A 201      17.319  12.916   0.383  1.00 66.70           C  
ANISOU 1205  CD  PRO A 201     7946   8542   8857     61    178    525       C  
ATOM   1206  N   PHE A 202      18.884  10.041   2.258  1.00 56.10           N  
ANISOU 1206  N   PHE A 202     6771   6992   7551    435    -11    238       N  
ATOM   1207  CA  PHE A 202      19.593   8.829   2.655  1.00 63.87           C  
ANISOU 1207  CA  PHE A 202     7821   7882   8566    610   -137    119       C  
ATOM   1208  C   PHE A 202      20.816   9.156   3.509  1.00 70.36           C  
ANISOU 1208  C   PHE A 202     8539   8718   9475    697   -242     86       C  
ATOM   1209  O   PHE A 202      20.977   8.621   4.613  1.00 72.54           O  
ANISOU 1209  O   PHE A 202     8969   8826   9768    771   -400     91       O  
ATOM   1210  CB  PHE A 202      19.992   8.047   1.402  1.00 62.85           C  
ANISOU 1210  CB  PHE A 202     7591   7872   8416    726    -97    -41       C  
ATOM   1211  CG  PHE A 202      20.499   6.659   1.671  1.00 70.17           C  
ANISOU 1211  CG  PHE A 202     8620   8639   9403    941   -273   -200       C  
ATOM   1212  CD1 PHE A 202      20.468   6.114   2.942  1.00 73.47           C  
ANISOU 1212  CD1 PHE A 202     9254   8795   9864    982   -462   -139       C  
ATOM   1213  CD2 PHE A 202      21.014   5.899   0.638  1.00 76.10           C  
ANISOU 1213  CD2 PHE A 202     9257   9501  10156   1108   -271   -423       C  
ATOM   1214  CE1 PHE A 202      20.939   4.847   3.177  1.00 78.88           C  
ANISOU 1214  CE1 PHE A 202    10067   9279  10625   1182   -682   -264       C  
ATOM   1215  CE2 PHE A 202      21.485   4.628   0.866  1.00 75.62           C  
ANISOU 1215  CE2 PHE A 202     9296   9248  10187   1343   -483   -603       C  
ATOM   1216  CZ  PHE A 202      21.447   4.100   2.137  1.00 79.28           C  
ANISOU 1216  CZ  PHE A 202    10003   9395  10724   1380   -707   -507       C  
ATOM   1217  N   ILE A 203      21.692  10.031   3.011  1.00 69.89           N  
ANISOU 1217  N   ILE A 203     8223   8871   9462    667   -169     66       N  
ATOM   1218  CA  ILE A 203      22.931  10.333   3.726  1.00 70.07           C  
ANISOU 1218  CA  ILE A 203     8101   8940   9583    743   -275      9       C  
ATOM   1219  C   ILE A 203      22.628  10.977   5.074  1.00 68.51           C  
ANISOU 1219  C   ILE A 203     8043   8585   9403    671   -375    114       C  
ATOM   1220  O   ILE A 203      23.185  10.584   6.106  1.00 61.96           O  
ANISOU 1220  O   ILE A 203     7279   7659   8605    783   -545     72       O  
ATOM   1221  CB  ILE A 203      23.843  11.227   2.870  1.00 67.00           C  
ANISOU 1221  CB  ILE A 203     7390   8840   9226    648   -158     -7       C  
ATOM   1222  CG1 ILE A 203      24.189  10.534   1.555  1.00 68.52           C  
ANISOU 1222  CG1 ILE A 203     7420   9264   9349    728    -43   -152       C  
ATOM   1223  CG2 ILE A 203      25.111  11.566   3.623  1.00 62.39           C  
ANISOU 1223  CG2 ILE A 203     6625   8319   8761    704   -276    -75       C  
ATOM   1224  CD1 ILE A 203      24.882  11.438   0.566  1.00 75.16           C  
ANISOU 1224  CD1 ILE A 203     7956  10453  10148    555    118   -121       C  
ATOM   1225  N   VAL A 204      21.738  11.974   5.082  1.00 68.09           N  
ANISOU 1225  N   VAL A 204     8035   8512   9324    499   -292    232       N  
ATOM   1226  CA  VAL A 204      21.439  12.706   6.313  1.00 64.98           C  
ANISOU 1226  CA  VAL A 204     7739   8013   8938    443   -378    276       C  
ATOM   1227  C   VAL A 204      20.881  11.767   7.375  1.00 65.55           C  
ANISOU 1227  C   VAL A 204     8061   7945   8902    504   -469    277       C  
ATOM   1228  O   VAL A 204      21.332  11.764   8.527  1.00 66.60           O  
ANISOU 1228  O   VAL A 204     8259   8027   9017    550   -610    260       O  
ATOM   1229  CB  VAL A 204      20.471  13.865   6.027  1.00 56.49           C  
ANISOU 1229  CB  VAL A 204     6664   6928   7872    291   -296    354       C  
ATOM   1230  CG1 VAL A 204      19.900  14.399   7.325  1.00 59.98           C  
ANISOU 1230  CG1 VAL A 204     7227   7276   8289    274   -375    333       C  
ATOM   1231  CG2 VAL A 204      21.185  14.972   5.267  1.00 55.27           C  
ANISOU 1231  CG2 VAL A 204     6299   6869   7831    182   -275    403       C  
ATOM   1232  N   THR A 205      19.886  10.960   7.005  1.00 66.29           N  
ANISOU 1232  N   THR A 205     8302   7982   8903    478   -403    312       N  
ATOM   1233  CA  THR A 205      19.340   9.991   7.947  1.00 66.07           C  
ANISOU 1233  CA  THR A 205     8524   7824   8753    475   -492    356       C  
ATOM   1234  C   THR A 205      20.407   9.003   8.395  1.00 73.22           C  
ANISOU 1234  C   THR A 205     9501   8627   9694    637   -693    319       C  
ATOM   1235  O   THR A 205      20.450   8.611   9.567  1.00 73.97           O  
ANISOU 1235  O   THR A 205     9780   8626   9698    635   -843    376       O  
ATOM   1236  CB  THR A 205      18.162   9.258   7.313  1.00 64.13           C  
ANISOU 1236  CB  THR A 205     8398   7536   8434    391   -397    399       C  
ATOM   1237  OG1 THR A 205      17.159  10.210   6.937  1.00 70.05           O  
ANISOU 1237  OG1 THR A 205     9065   8385   9167    268   -244    415       O  
ATOM   1238  CG2 THR A 205      17.567   8.265   8.291  1.00 59.18           C  
ANISOU 1238  CG2 THR A 205     8038   6780   7668    317   -492    485       C  
ATOM   1239  N   LEU A 206      21.282   8.594   7.476  1.00 71.22           N  
ANISOU 1239  N   LEU A 206     9095   8407   9557    784   -714    211       N  
ATOM   1240  CA  LEU A 206      22.343   7.663   7.839  1.00 69.37           C  
ANISOU 1240  CA  LEU A 206     8891   8070   9395    992   -940    126       C  
ATOM   1241  C   LEU A 206      23.325   8.302   8.810  1.00 67.69           C  
ANISOU 1241  C   LEU A 206     8584   7907   9228   1046  -1074    104       C  
ATOM   1242  O   LEU A 206      23.847   7.629   9.705  1.00 63.83           O  
ANISOU 1242  O   LEU A 206     8237   7281   8736   1166  -1318    106       O  
ATOM   1243  CB  LEU A 206      23.069   7.177   6.586  1.00 68.74           C  
ANISOU 1243  CB  LEU A 206     8603   8086   9429   1162   -911    -54       C  
ATOM   1244  CG  LEU A 206      24.254   6.253   6.864  1.00 66.60           C  
ANISOU 1244  CG  LEU A 206     8300   7728   9276   1438  -1170   -212       C  
ATOM   1245  CD1 LEU A 206      23.779   4.999   7.577  1.00 68.61           C  
ANISOU 1245  CD1 LEU A 206     8929   7645   9495   1492  -1416   -131       C  
ATOM   1246  CD2 LEU A 206      24.981   5.908   5.578  1.00 65.91           C  
ANISOU 1246  CD2 LEU A 206     7933   7826   9284   1614  -1102   -453       C  
ATOM   1247  N   LEU A 207      23.592   9.597   8.647  1.00 71.05           N  
ANISOU 1247  N   LEU A 207     8784   8507   9703    951   -950     91       N  
ATOM   1248  CA  LEU A 207      24.489  10.279   9.572  1.00 68.27           C  
ANISOU 1248  CA  LEU A 207     8336   8199   9405    979  -1088     58       C  
ATOM   1249  C   LEU A 207      23.856  10.418  10.949  1.00 68.21           C  
ANISOU 1249  C   LEU A 207     8586   8088   9244    897  -1186    154       C  
ATOM   1250  O   LEU A 207      24.552  10.352  11.967  1.00 66.32           O  
ANISOU 1250  O   LEU A 207     8392   7815   8989    976  -1395    132       O  
ATOM   1251  CB  LEU A 207      24.875  11.645   9.012  1.00 63.44           C  
ANISOU 1251  CB  LEU A 207     7441   7765   8897    855   -953     35       C  
ATOM   1252  CG  LEU A 207      25.757  11.605   7.765  1.00 58.28           C  
ANISOU 1252  CG  LEU A 207     6481   7306   8356    900   -859    -62       C  
ATOM   1253  CD1 LEU A 207      25.869  12.987   7.135  1.00 58.28           C  
ANISOU 1253  CD1 LEU A 207     6266   7458   8418    685   -713     -2       C  
ATOM   1254  CD2 LEU A 207      27.133  11.057   8.115  1.00 60.06           C  
ANISOU 1254  CD2 LEU A 207     6537   7593   8688   1106  -1049   -219       C  
ATOM   1255  N   VAL A 208      22.536  10.604  11.000  1.00 65.76           N  
ANISOU 1255  N   VAL A 208     8427   7760   8800    740  -1039    244       N  
ATOM   1256  CA  VAL A 208      21.850  10.728  12.283  1.00 70.01           C  
ANISOU 1256  CA  VAL A 208     9179   8279   9143    643  -1090    309       C  
ATOM   1257  C   VAL A 208      21.897   9.408  13.042  1.00 72.90           C  
ANISOU 1257  C   VAL A 208     9821   8505   9370    686  -1284    405       C  
ATOM   1258  O   VAL A 208      22.211   9.371  14.237  1.00 72.29           O  
ANISOU 1258  O   VAL A 208     9878   8422   9167    690  -1459    437       O  
ATOM   1259  CB  VAL A 208      20.403  11.205  12.072  1.00 62.31           C  
ANISOU 1259  CB  VAL A 208     8243   7366   8066    475   -875    344       C  
ATOM   1260  CG1 VAL A 208      19.616  11.100  13.361  1.00 57.35           C  
ANISOU 1260  CG1 VAL A 208     7821   6784   7185    363   -898    391       C  
ATOM   1261  CG2 VAL A 208      20.388  12.634  11.560  1.00 55.34           C  
ANISOU 1261  CG2 VAL A 208     7134   6567   7324    438   -769    263       C  
ATOM   1262  N   TYR A 209      21.584   8.304  12.360  1.00 67.17           N  
ANISOU 1262  N   TYR A 209     9206   7651   8663    711  -1285    458       N  
ATOM   1263  CA  TYR A 209      21.578   7.010  13.032  1.00 62.85           C  
ANISOU 1263  CA  TYR A 209     8966   6907   8008    728  -1515    581       C  
ATOM   1264  C   TYR A 209      22.975   6.598  13.468  1.00 67.38           C  
ANISOU 1264  C   TYR A 209     9528   7379   8695    962  -1822    518       C  
ATOM   1265  O   TYR A 209      23.130   5.942  14.504  1.00 76.08           O  
ANISOU 1265  O   TYR A 209    10894   8346   9666    963  -2077    640       O  
ATOM   1266  CB  TYR A 209      20.960   5.946  12.126  1.00 60.49           C  
ANISOU 1266  CB  TYR A 209     8784   6452   7749    710  -1483    623       C  
ATOM   1267  CG  TYR A 209      19.452   5.927  12.179  1.00 66.56           C  
ANISOU 1267  CG  TYR A 209     9685   7270   8334    437  -1286    750       C  
ATOM   1268  CD1 TYR A 209      18.788   5.544  13.335  1.00 66.30           C  
ANISOU 1268  CD1 TYR A 209     9921   7223   8047    229  -1351    931       C  
ATOM   1269  CD2 TYR A 209      18.693   6.292  11.078  1.00 67.85           C  
ANISOU 1269  CD2 TYR A 209     9692   7530   8559    372  -1040    687       C  
ATOM   1270  CE1 TYR A 209      17.408   5.526  13.397  1.00 71.51           C  
ANISOU 1270  CE1 TYR A 209    10651   7990   8531    -39  -1153   1024       C  
ATOM   1271  CE2 TYR A 209      17.312   6.271  11.129  1.00 67.87           C  
ANISOU 1271  CE2 TYR A 209     9776   7601   8410    135   -874    776       C  
ATOM   1272  CZ  TYR A 209      16.675   5.892  12.292  1.00 73.98           C  
ANISOU 1272  CZ  TYR A 209    10778   8387   8944    -71   -920    933       C  
ATOM   1273  OH  TYR A 209      15.301   5.875  12.350  1.00 78.65           O  
ANISOU 1273  OH  TYR A 209    11400   9107   9378   -325   -736    998       O  
ATOM   1274  N   ILE A 210      24.002   6.972  12.702  1.00 65.59           N  
ANISOU 1274  N   ILE A 210     8989   7235   8698   1151  -1815    332       N  
ATOM   1275  CA  ILE A 210      25.373   6.731  13.144  1.00 66.53           C  
ANISOU 1275  CA  ILE A 210     9020   7316   8943   1384  -2102    228       C  
ATOM   1276  C   ILE A 210      25.669   7.536  14.402  1.00 68.90           C  
ANISOU 1276  C   ILE A 210     9347   7706   9128   1318  -2205    265       C  
ATOM   1277  O   ILE A 210      26.296   7.036  15.343  1.00 66.82           O  
ANISOU 1277  O   ILE A 210     9234   7337   8820   1429  -2518    299       O  
ATOM   1278  CB  ILE A 210      26.368   7.053  12.015  1.00 68.77           C  
ANISOU 1278  CB  ILE A 210     8898   7760   9473   1556  -2020      2       C  
ATOM   1279  CG1 ILE A 210      26.237   6.043  10.879  1.00 66.91           C  
ANISOU 1279  CG1 ILE A 210     8656   7435   9331   1685  -1991    -87       C  
ATOM   1280  CG2 ILE A 210      27.792   7.062  12.545  1.00 69.56           C  
ANISOU 1280  CG2 ILE A 210     8822   7898   9711   1774  -2291   -139       C  
ATOM   1281  CD1 ILE A 210      27.237   6.254   9.771  1.00 66.26           C  
ANISOU 1281  CD1 ILE A 210     8158   7579   9440   1852  -1900   -335       C  
ATOM   1282  N   LYS A 211      25.221   8.797  14.439  1.00 68.09           N  
ANISOU 1282  N   LYS A 211     9108   7786   8977   1147  -1974    247       N  
ATOM   1283  CA  LYS A 211      25.368   9.607  15.645  1.00 72.77           C  
ANISOU 1283  CA  LYS A 211     9739   8468   9442   1077  -2066    245       C  
ATOM   1284  C   LYS A 211      24.551   9.044  16.798  1.00 75.75           C  
ANISOU 1284  C   LYS A 211    10492   8790   9501    949  -2158    418       C  
ATOM   1285  O   LYS A 211      24.918   9.225  17.965  1.00 75.16           O  
ANISOU 1285  O   LYS A 211    10526   8758   9275    949  -2353    430       O  
ATOM   1286  CB  LYS A 211      24.956  11.053  15.367  1.00 72.52           C  
ANISOU 1286  CB  LYS A 211     9503   8598   9455    934  -1825    165       C  
ATOM   1287  CG  LYS A 211      26.059  11.921  14.784  1.00 76.74           C  
ANISOU 1287  CG  LYS A 211     9682   9223  10251    997  -1830     21       C  
ATOM   1288  CD  LYS A 211      27.081  12.304  15.845  1.00 80.50           C  
ANISOU 1288  CD  LYS A 211    10106   9734  10746   1072  -2092    -66       C  
ATOM   1289  N   ILE A 212      23.444   8.363  16.492  1.00 76.82           N  
ANISOU 1289  N   ILE A 212    10821   8858   9510    813  -2022    555       N  
ATOM   1290  CA  ILE A 212      22.634   7.738  17.534  1.00 75.49           C  
ANISOU 1290  CA  ILE A 212    11004   8670   9009    629  -2092    753       C  
ATOM   1291  C   ILE A 212      23.351   6.523  18.110  1.00 78.85           C  
ANISOU 1291  C   ILE A 212    11697   8862   9401    741  -2475    889       C  
ATOM   1292  O   ILE A 212      23.426   6.348  19.332  1.00 81.23           O  
ANISOU 1292  O   ILE A 212    12234   9186   9445    664  -2673   1015       O  
ATOM   1293  CB  ILE A 212      21.244   7.368  16.983  1.00 72.94           C  
ANISOU 1293  CB  ILE A 212    10775   8353   8584    420  -1838    858       C  
ATOM   1294  CG1 ILE A 212      20.367   8.618  16.858  1.00 72.24           C  
ANISOU 1294  CG1 ILE A 212    10488   8519   8442    291  -1522    738       C  
ATOM   1295  CG2 ILE A 212      20.575   6.319  17.861  1.00 71.22           C  
ANISOU 1295  CG2 ILE A 212    10941   8062   8058    211  -1961   1112       C  
ATOM   1296  CD1 ILE A 212      18.962   8.339  16.351  1.00 65.08           C  
ANISOU 1296  CD1 ILE A 212     9627   7664   7437     90  -1276    811       C  
ATOM   1297  N   TYR A 213      23.890   5.666  17.237  1.00 80.40           N  
ANISOU 1297  N   TYR A 213    11866   8833   9849    936  -2607    855       N  
ATOM   1298  CA  TYR A 213      24.609   4.484  17.706  1.00 74.91           C  
ANISOU 1298  CA  TYR A 213    11423   7857   9182   1095  -3032    956       C  
ATOM   1299  C   TYR A 213      25.796   4.871  18.580  1.00 76.60           C  
ANISOU 1299  C   TYR A 213    11566   8127   9414   1272  -3314    873       C  
ATOM   1300  O   TYR A 213      26.091   4.197  19.574  1.00 75.58           O  
ANISOU 1300  O   TYR A 213    11741   7846   9129   1288  -3670   1037       O  
ATOM   1301  CB  TYR A 213      25.070   3.642  16.515  1.00 69.47           C  
ANISOU 1301  CB  TYR A 213    10637   6949   8811   1339  -3122    828       C  
ATOM   1302  CG  TYR A 213      25.850   2.401  16.899  1.00 82.87           C  
ANISOU 1302  CG  TYR A 213    12578   8305  10605   1567  -3612    881       C  
ATOM   1303  CD1 TYR A 213      25.198   1.248  17.317  1.00 88.00           C  
ANISOU 1303  CD1 TYR A 213    13681   8643  11110   1422  -3838   1153       C  
ATOM   1304  CD2 TYR A 213      27.237   2.376  16.828  1.00 83.04           C  
ANISOU 1304  CD2 TYR A 213    12370   8305  10877   1924  -3876    656       C  
ATOM   1305  CE1 TYR A 213      25.906   0.107  17.664  1.00 88.45           C  
ANISOU 1305  CE1 TYR A 213    13945   8382  11281   1597  -4262   1171       C  
ATOM   1306  CE2 TYR A 213      27.955   1.241  17.174  1.00 84.14           C  
ANISOU 1306  CE2 TYR A 213    12701   8139  11130   2144  -4318    655       C  
ATOM   1307  CZ  TYR A 213      27.286   0.109  17.589  1.00 88.74           C  
ANISOU 1307  CZ  TYR A 213    13713   8432  11572   1950  -4461    892       C  
ATOM   1308  OH  TYR A 213      27.998  -1.023  17.933  1.00 93.97           O  
ANISOU 1308  OH  TYR A 213    14524   8828  12351   2091  -4813    843       O  
ATOM   1309  N   ILE A 214      26.491   5.955  18.226  1.00 79.22           N  
ANISOU 1309  N   ILE A 214    11503   8668   9929   1388  -3184    634       N  
ATOM   1310  CA  ILE A 214      27.667   6.368  18.988  1.00 79.71           C  
ANISOU 1310  CA  ILE A 214    11448   8796  10043   1553  -3456    525       C  
ATOM   1311  C   ILE A 214      27.278   6.769  20.407  1.00 82.99           C  
ANISOU 1311  C   ILE A 214    12112   9325  10094   1359  -3536    663       C  
ATOM   1312  O   ILE A 214      27.993   6.468  21.373  1.00 77.18           O  
ANISOU 1312  O   ILE A 214    11526   8534   9267   1459  -3903    709       O  
ATOM   1313  CB  ILE A 214      28.405   7.505  18.256  1.00 74.49           C  
ANISOU 1313  CB  ILE A 214    10301   8350   9651   1642  -3272    259       C  
ATOM   1314  CG1 ILE A 214      28.993   6.995  16.944  1.00 73.37           C  
ANISOU 1314  CG1 ILE A 214     9897   8156   9825   1855  -3239    102       C  
ATOM   1315  CG2 ILE A 214      29.508   8.085  19.125  1.00 79.54           C  
ANISOU 1315  CG2 ILE A 214    10802   9091  10328   1753  -3532    141       C  
ATOM   1316  CD1 ILE A 214      29.840   8.022  16.221  1.00 79.87           C  
ANISOU 1316  CD1 ILE A 214    10233   9224  10891   1906  -3079   -130       C  
ATOM   1317  N   VAL A 215      26.138   7.447  20.558  1.00 80.48           N  
ANISOU 1317  N   VAL A 215    11834   9193   9553   1092  -3207    710       N  
ATOM   1318  CA  VAL A 215      25.693   7.866  21.883  1.00 80.01           C  
ANISOU 1318  CA  VAL A 215    11978   9313   9108    905  -3241    790       C  
ATOM   1319  C   VAL A 215      25.303   6.658  22.722  1.00 86.31           C  
ANISOU 1319  C   VAL A 215    13235   9978   9582    774  -3480   1098       C  
ATOM   1320  O   VAL A 215      25.668   6.557  23.900  1.00 89.76           O  
ANISOU 1320  O   VAL A 215    13882  10466   9758    750  -3755   1189       O  
ATOM   1321  CB  VAL A 215      24.532   8.868  21.764  1.00 69.82           C  
ANISOU 1321  CB  VAL A 215    10575   8272   7681    685  -2829    710       C  
ATOM   1322  CG1 VAL A 215      23.873   9.073  23.115  1.00 70.46           C  
ANISOU 1322  CG1 VAL A 215    10891   8582   7299    474  -2833    787       C  
ATOM   1323  CG2 VAL A 215      25.035  10.188  21.201  1.00 70.96           C  
ANISOU 1323  CG2 VAL A 215    10323   8520   8117    791  -2692    435       C  
ATOM   1324  N   LEU A 216      24.556   5.722  22.131  1.00 88.27           N  
ANISOU 1324  N   LEU A 216    13660  10047   9830    664  -3400   1278       N  
ATOM   1325  CA  LEU A 216      24.129   4.539  22.870  1.00 81.42           C  
ANISOU 1325  CA  LEU A 216    13257   9014   8666    480  -3641   1616       C  
ATOM   1326  C   LEU A 216      25.314   3.682  23.294  1.00 84.21           C  
ANISOU 1326  C   LEU A 216    13802   9063   9129    728  -4180   1700       C  
ATOM   1327  O   LEU A 216      25.268   3.046  24.353  1.00 81.69           O  
ANISOU 1327  O   LEU A 216    13836   8687   8514    577  -4427   1947       O  
ATOM   1328  CB  LEU A 216      23.148   3.725  22.025  1.00 83.40           C  
ANISOU 1328  CB  LEU A 216    13629   9094   8967    318  -3470   1765       C  
ATOM   1329  CG  LEU A 216      21.846   4.440  21.657  1.00 89.34           C  
ANISOU 1329  CG  LEU A 216    14218  10142   9584     56  -2973   1707       C  
ATOM   1330  CD1 LEU A 216      21.017   3.625  20.676  1.00 88.79           C  
ANISOU 1330  CD1 LEU A 216    14221   9881   9633    -62  -2839   1814       C  
ATOM   1331  CD2 LEU A 216      21.046   4.736  22.911  1.00 97.88           C  
ANISOU 1331  CD2 LEU A 216    15482  11550  10159   -274  -2870   1850       C  
ATOM   1332  N   ARG A 217      26.382   3.651  22.492  1.00 81.94           N  
ANISOU 1332  N   ARG A 217    13237   8618   9279   1094  -4322   1464       N  
ATOM   1333  CA  ARG A 217      27.561   2.877  22.871  1.00 83.41           C  
ANISOU 1333  CA  ARG A 217    13486   8566   9641   1348  -4750   1435       C  
ATOM   1334  C   ARG A 217      28.345   3.556  23.985  1.00 85.61           C  
ANISOU 1334  C   ARG A 217    13711   9042   9775   1403  -4934   1364       C  
ATOM   1335  O   ARG A 217      28.952   2.873  24.816  1.00 80.30           O  
ANISOU 1335  O   ARG A 217    13221   8234   9057   1442  -5229   1443       O  
ATOM   1336  CB  ARG A 217      28.460   2.641  21.658  1.00 74.00           C  
ANISOU 1336  CB  ARG A 217    11946   7228   8942   1710  -4789   1141       C  
ATOM   1337  N   ARG A 218      28.347   4.891  24.021  1.00 77.47           N  
ANISOU 1337  N   ARG A 218    12427   8320   8687   1399  -4771   1198       N  
ATOM   1338  CA  ARG A 218      28.948   5.589  25.152  1.00 79.95           C  
ANISOU 1338  CA  ARG A 218    12725   8839   8812   1411  -4955   1127       C  
ATOM   1339  C   ARG A 218      28.170   5.328  26.435  1.00 82.04           C  
ANISOU 1339  C   ARG A 218    13403   9226   8543   1087  -4970   1402       C  
ATOM   1340  O   ARG A 218      28.765   5.243  27.517  1.00 84.60           O  
ANISOU 1340  O   ARG A 218    13838   9600   8707   1097  -5207   1432       O  
ATOM   1341  CB  ARG A 218      29.022   7.089  24.868  1.00 75.14           C  
ANISOU 1341  CB  ARG A 218    11692   8536   8320   1397  -4623    823       C  
ATOM   1342  N   ARG A 219      26.847   5.179  26.326  1.00 85.99           N  
ANISOU 1342  N   ARG A 219    14111   9803   8758    785  -4704   1599       N  
ATOM   1343  CA  ARG A 219      26.016   4.885  27.490  1.00 84.46           C  
ANISOU 1343  CA  ARG A 219    14260   9795   8035    425  -4645   1858       C  
ATOM   1344  C   ARG A 219      26.340   3.511  28.066  1.00 86.08           C  
ANISOU 1344  C   ARG A 219    14765   9710   8230    380  -4920   2118       C  
ATOM   1345  O   ARG A 219      26.501   3.361  29.283  1.00 90.06           O  
ANISOU 1345  O   ARG A 219    15467  10337   8414    256  -5076   2247       O  
ATOM   1346  CB  ARG A 219      24.539   4.978  27.102  1.00 85.75           C  
ANISOU 1346  CB  ARG A 219    14494  10127   7961    100  -4243   1970       C  
ATOM   1347  CG  ARG A 219      23.566   4.985  28.270  1.00 97.90           C  
ANISOU 1347  CG  ARG A 219    16277  12019   8900   -302  -4086   2160       C  
ATOM   1348  CD  ARG A 219      22.137   5.191  27.780  1.00103.51           C  
ANISOU 1348  CD  ARG A 219    16923  12951   9455   -597  -3619   2177       C  
ATOM   1349  NE  ARG A 219      22.015   6.380  26.940  1.00103.98           N  
ANISOU 1349  NE  ARG A 219    16513  13152   9842   -422  -3259   1780       N  
ATOM   1350  CZ  ARG A 219      21.746   7.599  27.400  1.00102.81           C  
ANISOU 1350  CZ  ARG A 219    16138  13388   9536   -439  -3032   1497       C  
ATOM   1351  NH1 ARG A 219      21.567   7.793  28.700  1.00112.25           N  
ANISOU 1351  NH1 ARG A 219    17509  14920  10223   -616  -3093   1534       N  
ATOM   1352  NH2 ARG A 219      21.656   8.624  26.563  1.00 90.07           N  
ANISOU 1352  NH2 ARG A 219    14137  11821   8266   -282  -2765   1173       N  
ATOM   1353  N   ARG A 220      26.443   2.493  27.205  1.00 85.93           N  
ANISOU 1353  N   ARG A 220    14788   9305   8558    483  -5002   2177       N  
ATOM   1354  CA  ARG A 220      26.753   1.145  27.680  1.00 92.53           C  
ANISOU 1354  CA  ARG A 220    15922   9808   9426    451  -5313   2391       C  
ATOM   1355  C   ARG A 220      28.118   1.092  28.355  1.00 98.18           C  
ANISOU 1355  C   ARG A 220    16600  10438  10265    730  -5700   2278       C  
ATOM   1356  O   ARG A 220      28.296   0.384  29.353  1.00 99.06           O  
ANISOU 1356  O   ARG A 220    17008  10452  10178    616  -5960   2492       O  
ATOM   1357  CB  ARG A 220      26.686   0.149  26.522  1.00 94.83           C  
ANISOU 1357  CB  ARG A 220    16221   9701  10109    561  -5350   2378       C  
ATOM   1358  CG  ARG A 220      25.281  -0.055  25.969  1.00100.75           C  
ANISOU 1358  CG  ARG A 220    17071  10487  10720    234  -5015   2543       C  
ATOM   1359  CD  ARG A 220      25.299  -0.715  24.596  1.00102.73           C  
ANISOU 1359  CD  ARG A 220    17220  10409  11403    417  -5011   2417       C  
ATOM   1360  NE  ARG A 220      23.971  -0.712  23.986  1.00105.76           N  
ANISOU 1360  NE  ARG A 220    17640  10872  11673    124  -4663   2533       N  
ATOM   1361  CZ  ARG A 220      23.743  -0.876  22.687  1.00111.13           C  
ANISOU 1361  CZ  ARG A 220    18166  11401  12658    249  -4533   2393       C  
ATOM   1362  NH1 ARG A 220      24.756  -1.052  21.850  1.00115.91           N  
ANISOU 1362  NH1 ARG A 220    18552  11801  13687    664  -4699   2115       N  
ATOM   1363  NH2 ARG A 220      22.500  -0.857  22.220  1.00109.07           N  
ANISOU 1363  NH2 ARG A 220    17943  11230  12267    -44  -4223   2509       N  
ATOM   1364  N   LYS A 221      29.096   1.832  27.826  1.00 87.90           N  
ANISOU 1364  N   LYS A 221    14922   9183   9293   1081  -5746   1943       N  
ATOM   1365  CA  LYS A 221      30.396   1.903  28.485  1.00 91.01           C  
ANISOU 1365  CA  LYS A 221    15227   9552   9800   1332  -6088   1803       C  
ATOM   1366  C   LYS A 221      30.311   2.643  29.815  1.00 92.81           C  
ANISOU 1366  C   LYS A 221    15563  10123   9576   1152  -6111   1881       C  
ATOM   1367  O   LYS A 221      31.080   2.348  30.738  1.00 97.14           O  
ANISOU 1367  O   LYS A 221    16229  10626  10054   1227  -6434   1922       O  
ATOM   1368  CB  LYS A 221      31.420   2.575  27.569  1.00 88.24           C  
ANISOU 1368  CB  LYS A 221    14391   9229   9907   1702  -6082   1409       C  
ATOM   1369  N   ARG A 222      29.386   3.599  29.935  1.00 89.90           N  
ANISOU 1369  N   ARG A 222    15156  10111   8890    923  -5782   1877       N  
ATOM   1370  CA  ARG A 222      29.220   4.328  31.190  1.00 91.86           C  
ANISOU 1370  CA  ARG A 222    15494  10740   8669    746  -5774   1897       C  
ATOM   1371  C   ARG A 222      28.375   3.544  32.190  1.00 96.10           C  
ANISOU 1371  C   ARG A 222    16450  11352   8712    379  -5763   2271       C  
ATOM   1372  O   ARG A 222      28.677   3.536  33.390  1.00100.34           O  
ANISOU 1372  O   ARG A 222    17145  12050   8928    306  -5948   2359       O  
ATOM   1373  CB  ARG A 222      28.596   5.698  30.923  1.00 87.62           C  
ANISOU 1373  CB  ARG A 222    14726  10572   7995    668  -5443   1670       C  
ATOM   1374  N   ASN A1002      27.322   2.874  31.712  1.00 85.72           N  
ANISOU 1374  N   ASN A1002    12716   9421  10431    154  -1889   1403       N  
ATOM   1375  CA  ASN A1002      26.456   2.104  32.601  1.00 78.54           C  
ANISOU 1375  CA  ASN A1002    11488   8720   9636    336  -1772   1042       C  
ATOM   1376  C   ASN A1002      27.206   0.951  33.259  1.00 74.17           C  
ANISOU 1376  C   ASN A1002    10829   8409   8943    253  -1283    980       C  
ATOM   1377  O   ASN A1002      26.974   0.646  34.435  1.00 77.99           O  
ANISOU 1377  O   ASN A1002    11066   9013   9552    361  -1151    748       O  
ATOM   1378  CB  ASN A1002      25.242   1.584  31.828  1.00 72.27           C  
ANISOU 1378  CB  ASN A1002    10694   8018   8747    370  -1959    956       C  
ATOM   1379  CG  ASN A1002      24.296   2.693  31.414  1.00 85.39           C  
ANISOU 1379  CG  ASN A1002    12363   9440  10641    548  -2522    954       C  
ATOM   1380  OD1 ASN A1002      24.569   3.871  31.643  1.00 91.93           O  
ANISOU 1380  OD1 ASN A1002    13249   9977  11701    641  -2774   1033       O  
ATOM   1381  ND2 ASN A1002      23.179   2.324  30.796  1.00 95.12           N  
ANISOU 1381  ND2 ASN A1002    13533  10764  11844    599  -2763    857       N  
ATOM   1382  N   ILE A1003      28.104   0.295  32.520  1.00 69.88           N  
ANISOU 1382  N   ILE A1003    10476   7942   8134     67  -1017   1180       N  
ATOM   1383  CA  ILE A1003      28.844  -0.824  33.094  1.00 75.25           C  
ANISOU 1383  CA  ILE A1003    11058   8796   8739     40   -607   1126       C  
ATOM   1384  C   ILE A1003      29.846  -0.336  34.137  1.00 79.70           C  
ANISOU 1384  C   ILE A1003    11473   9334   9474     69   -527   1154       C  
ATOM   1385  O   ILE A1003      30.117  -1.035  35.121  1.00 81.90           O  
ANISOU 1385  O   ILE A1003    11597   9734   9788    131   -334   1048       O  
ATOM   1386  CB  ILE A1003      29.526  -1.644  31.981  1.00 76.66           C  
ANISOU 1386  CB  ILE A1003    11445   9056   8624   -116   -342   1259       C  
ATOM   1387  CG1 ILE A1003      30.131  -2.927  32.553  1.00 83.23           C  
ANISOU 1387  CG1 ILE A1003    12171  10007   9446    -76     25   1164       C  
ATOM   1388  CG2 ILE A1003      30.599  -0.830  31.276  1.00 75.86           C  
ANISOU 1388  CG2 ILE A1003    11492   8897   8434   -279   -312   1524       C  
ATOM   1389  CD1 ILE A1003      30.765  -3.812  31.509  1.00 89.05           C  
ANISOU 1389  CD1 ILE A1003    13083  10813   9939   -170    311   1194       C  
ATOM   1390  N   PHE A1004      30.403   0.862  33.954  1.00 72.73           N  
ANISOU 1390  N   PHE A1004    10657   8281   8697      0   -708   1309       N  
ATOM   1391  CA  PHE A1004      31.300   1.419  34.961  1.00 72.86           C  
ANISOU 1391  CA  PHE A1004    10523   8260   8901      1   -698   1302       C  
ATOM   1392  C   PHE A1004      30.561   1.658  36.271  1.00 75.78           C  
ANISOU 1392  C   PHE A1004    10709   8641   9442    194   -837   1009       C  
ATOM   1393  O   PHE A1004      31.045   1.293  37.349  1.00 75.51           O  
ANISOU 1393  O   PHE A1004    10525   8740   9424    231   -703    911       O  
ATOM   1394  CB  PHE A1004      31.920   2.718  34.446  1.00 74.85           C  
ANISOU 1394  CB  PHE A1004    10908   8273   9256   -164   -904   1525       C  
ATOM   1395  CG  PHE A1004      32.831   3.387  35.431  1.00 80.49           C  
ANISOU 1395  CG  PHE A1004    11471   8921  10192   -205   -951   1497       C  
ATOM   1396  CD1 PHE A1004      34.093   2.876  35.685  1.00 79.31           C  
ANISOU 1396  CD1 PHE A1004    11166   8951  10018   -317   -675   1584       C  
ATOM   1397  CD2 PHE A1004      32.429   4.533  36.100  1.00 83.97           C  
ANISOU 1397  CD2 PHE A1004    11907   9110  10888   -118  -1297   1351       C  
ATOM   1398  CE1 PHE A1004      34.938   3.492  36.589  1.00 82.95           C  
ANISOU 1398  CE1 PHE A1004    11465   9368  10684   -377   -769   1550       C  
ATOM   1399  CE2 PHE A1004      33.269   5.154  37.007  1.00 85.07           C  
ANISOU 1399  CE2 PHE A1004    11928   9181  11215   -183  -1370   1289       C  
ATOM   1400  CZ  PHE A1004      34.525   4.633  37.251  1.00 84.25           C  
ANISOU 1400  CZ  PHE A1004    11666   9282  11062   -331  -1119   1402       C  
ATOM   1401  N   GLU A1005      29.376   2.270  36.194  1.00 75.34           N  
ANISOU 1401  N   GLU A1005    10654   8467   9503    325  -1114    852       N  
ATOM   1402  CA  GLU A1005      28.576   2.488  37.395  1.00 80.23           C  
ANISOU 1402  CA  GLU A1005    11062   9155  10266    516  -1188    504       C  
ATOM   1403  C   GLU A1005      28.115   1.169  38.000  1.00 86.02           C  
ANISOU 1403  C   GLU A1005    11656  10202  10825    527   -889    366       C  
ATOM   1404  O   GLU A1005      28.046   1.030  39.227  1.00 90.45           O  
ANISOU 1404  O   GLU A1005    12070  10923  11372    580   -788    167       O  
ATOM   1405  CB  GLU A1005      27.375   3.375  37.076  1.00 77.92           C  
ANISOU 1405  CB  GLU A1005    10741   8676  10189    694  -1544    334       C  
ATOM   1406  CG  GLU A1005      27.742   4.831  36.890  1.00 84.80           C  
ANISOU 1406  CG  GLU A1005    11751   9159  11311    720  -1903    409       C  
ATOM   1407  CD  GLU A1005      28.491   5.393  38.081  1.00 89.89           C  
ANISOU 1407  CD  GLU A1005    12315   9761  12076    724  -1883    248       C  
ATOM   1408  OE1 GLU A1005      27.991   5.262  39.219  1.00 89.61           O  
ANISOU 1408  OE1 GLU A1005    12069   9916  12064    880  -1796   -120       O  
ATOM   1409  OE2 GLU A1005      29.591   5.949  37.880  1.00 88.50           O  
ANISOU 1409  OE2 GLU A1005    12285   9394  11947    539  -1944    483       O  
ATOM   1410  N   MET A1006      27.798   0.187  37.153  1.00 78.13           N  
ANISOU 1410  N   MET A1006    10736   9284   9667    448   -755    474       N  
ATOM   1411  CA  MET A1006      27.337  -1.104  37.657  1.00 72.09           C  
ANISOU 1411  CA  MET A1006     9881   8748   8762    410   -494    376       C  
ATOM   1412  C   MET A1006      28.381  -1.755  38.553  1.00 75.65           C  
ANISOU 1412  C   MET A1006    10336   9295   9114    362   -262    468       C  
ATOM   1413  O   MET A1006      28.038  -2.402  39.549  1.00 76.42           O  
ANISOU 1413  O   MET A1006    10345   9565   9126    348   -119    363       O  
ATOM   1414  CB  MET A1006      26.994  -2.033  36.497  1.00 63.48           C  
ANISOU 1414  CB  MET A1006     8926   7661   7531    307   -419    476       C  
ATOM   1415  CG  MET A1006      26.279  -3.292  36.913  1.00 70.23           C  
ANISOU 1415  CG  MET A1006     9703   8684   8298    231   -215    360       C  
ATOM   1416  SD  MET A1006      26.609  -4.663  35.798  1.00 70.93           S  
ANISOU 1416  SD  MET A1006    10037   8714   8198     86    -29    502       S  
ATOM   1417  CE  MET A1006      25.235  -5.747  36.183  1.00 79.60           C  
ANISOU 1417  CE  MET A1006    11010   9948   9288    -46     55    311       C  
ATOM   1418  N   LEU A1007      29.660  -1.591  38.223  1.00 74.32           N  
ANISOU 1418  N   LEU A1007    10257   9030   8951    321   -234    678       N  
ATOM   1419  CA  LEU A1007      30.716  -2.231  38.992  1.00 72.19           C  
ANISOU 1419  CA  LEU A1007     9955   8841   8633    310    -74    777       C  
ATOM   1420  C   LEU A1007      31.310  -1.346  40.078  1.00 77.91           C  
ANISOU 1420  C   LEU A1007    10574   9585   9442    343   -217    715       C  
ATOM   1421  O   LEU A1007      31.846  -1.881  41.054  1.00 81.18           O  
ANISOU 1421  O   LEU A1007    10944  10120   9781    352   -154    740       O  
ATOM   1422  CB  LEU A1007      31.835  -2.718  38.066  1.00 71.02           C  
ANISOU 1422  CB  LEU A1007     9882   8633   8470    261     76    992       C  
ATOM   1423  CG  LEU A1007      31.556  -4.102  37.475  1.00 67.80           C  
ANISOU 1423  CG  LEU A1007     9585   8237   7941    251    288   1010       C  
ATOM   1424  CD1 LEU A1007      30.727  -4.015  36.198  1.00 65.13           C  
ANISOU 1424  CD1 LEU A1007     9386   7844   7514    183    249    974       C  
ATOM   1425  CD2 LEU A1007      32.848  -4.848  37.236  1.00 68.79           C  
ANISOU 1425  CD2 LEU A1007     9698   8348   8090    287    481   1140       C  
ATOM   1426  N   ARG A1008      31.232  -0.018  39.954  1.00 81.15           N  
ANISOU 1426  N   ARG A1008    10972   9855  10007    355   -447    635       N  
ATOM   1427  CA  ARG A1008      31.610   0.793  41.106  1.00 79.83           C  
ANISOU 1427  CA  ARG A1008    10721   9701   9912    383   -602    485       C  
ATOM   1428  C   ARG A1008      30.583   0.693  42.224  1.00 79.95           C  
ANISOU 1428  C   ARG A1008    10660   9903   9815    473   -581    181       C  
ATOM   1429  O   ARG A1008      30.878   1.089  43.357  1.00 82.62           O  
ANISOU 1429  O   ARG A1008    10953  10337  10104    486   -655     22       O  
ATOM   1430  CB  ARG A1008      31.814   2.257  40.711  1.00 75.25           C  
ANISOU 1430  CB  ARG A1008    10178   8848   9565    361   -878    461       C  
ATOM   1431  CG  ARG A1008      30.548   3.009  40.384  1.00 84.73           C  
ANISOU 1431  CG  ARG A1008    11405   9893  10893    488  -1070    258       C  
ATOM   1432  CD  ARG A1008      30.759   4.502  40.562  1.00 91.79           C  
ANISOU 1432  CD  ARG A1008    12342  10481  12053    509  -1399    147       C  
ATOM   1433  NE  ARG A1008      30.802   4.870  41.973  1.00 97.78           N  
ANISOU 1433  NE  ARG A1008    12996  11338  12815    587  -1451   -187       N  
ATOM   1434  CZ  ARG A1008      29.731   5.209  42.684  1.00100.58           C  
ANISOU 1434  CZ  ARG A1008    13254  11756  13206    785  -1504   -595       C  
ATOM   1435  NH1 ARG A1008      28.534   5.231  42.111  1.00 94.43           N  
ANISOU 1435  NH1 ARG A1008    12420  10935  12522    941  -1541   -707       N  
ATOM   1436  NH2 ARG A1008      29.857   5.526  43.966  1.00105.64           N  
ANISOU 1436  NH2 ARG A1008    13834  12529  13777    825  -1520   -917       N  
ATOM   1437  N   ILE A1009      29.394   0.171  41.926  1.00 74.25           N  
ANISOU 1437  N   ILE A1009     9910   9267   9034    507   -473     81       N  
ATOM   1438  CA  ILE A1009      28.416  -0.151  42.956  1.00 75.30           C  
ANISOU 1438  CA  ILE A1009     9929   9661   9019    531   -350   -186       C  
ATOM   1439  C   ILE A1009      28.680  -1.535  43.536  1.00 78.79           C  
ANISOU 1439  C   ILE A1009    10438  10305   9194    403   -107     -8       C  
ATOM   1440  O   ILE A1009      28.534  -1.752  44.743  1.00 85.17           O  
ANISOU 1440  O   ILE A1009    11227  11348   9787    355    -20   -120       O  
ATOM   1441  CB  ILE A1009      26.996  -0.039  42.373  1.00 72.07           C  
ANISOU 1441  CB  ILE A1009     9394   9267   8722    603   -364   -387       C  
ATOM   1442  CG1 ILE A1009      26.670   1.415  42.030  1.00 73.75           C  
ANISOU 1442  CG1 ILE A1009     9547   9243   9230    783   -675   -591       C  
ATOM   1443  CG2 ILE A1009      25.968  -0.620  43.332  1.00 70.49           C  
ANISOU 1443  CG2 ILE A1009     9027   9408   8349    556   -136   -634       C  
ATOM   1444  CD1 ILE A1009      25.423   1.572  41.190  1.00 76.17           C  
ANISOU 1444  CD1 ILE A1009     9730   9499   9713    890   -796   -718       C  
ATOM   1445  N   ASP A1010      29.079  -2.490  42.694  1.00 72.06           N  
ANISOU 1445  N   ASP A1010     9694   9350   8336    343     -7    269       N  
ATOM   1446  CA  ASP A1010      29.286  -3.870  43.127  1.00 72.56           C  
ANISOU 1446  CA  ASP A1010     9858   9501   8210    243    179    457       C  
ATOM   1447  C   ASP A1010      30.708  -4.106  43.629  1.00 75.95           C  
ANISOU 1447  C   ASP A1010    10352   9894   8612    272    117    675       C  
ATOM   1448  O   ASP A1010      30.908  -4.550  44.763  1.00 79.91           O  
ANISOU 1448  O   ASP A1010    10905  10541   8916    226    124    730       O  
ATOM   1449  CB  ASP A1010      28.966  -4.834  41.979  1.00 68.87           C  
ANISOU 1449  CB  ASP A1010     9481   8902   7784    190    300    582       C  
ATOM   1450  CG  ASP A1010      27.482  -4.951  41.709  1.00 73.05           C  
ANISOU 1450  CG  ASP A1010     9921   9528   8308    113    358    385       C  
ATOM   1451  OD1 ASP A1010      26.693  -4.307  42.432  1.00 67.48           O  
ANISOU 1451  OD1 ASP A1010     9046   9009   7582    124    341    140       O  
ATOM   1452  OD2 ASP A1010      27.105  -5.691  40.773  1.00 78.54           O1+
ANISOU 1452  OD2 ASP A1010    10691  10123   9026     43    418    440       O1+
ATOM   1453  N   GLU A1011      31.702  -3.824  42.788  1.00 76.16           N  
ANISOU 1453  N   GLU A1011    10363   9749   8825    334     50    808       N  
ATOM   1454  CA  GLU A1011      33.088  -4.089  43.149  1.00 80.16           C  
ANISOU 1454  CA  GLU A1011    10842  10236   9377    379    -14    997       C  
ATOM   1455  C   GLU A1011      33.663  -2.965  44.003  1.00 86.62           C  
ANISOU 1455  C   GLU A1011    11560  11131  10222    377   -238    897       C  
ATOM   1456  O   GLU A1011      34.212  -3.213  45.081  1.00 98.58           O  
ANISOU 1456  O   GLU A1011    13076  12768  11614    380   -345    952       O  
ATOM   1457  CB  GLU A1011      33.926  -4.284  41.885  1.00 82.54           C  
ANISOU 1457  CB  GLU A1011    11111  10383   9867    418     68   1140       C  
ATOM   1458  CG  GLU A1011      35.344  -4.765  42.134  1.00 89.74           C  
ANISOU 1458  CG  GLU A1011    11913  11291  10894    502     40   1313       C  
ATOM   1459  CD  GLU A1011      35.393  -6.223  42.539  1.00 95.34           C  
ANISOU 1459  CD  GLU A1011    12731  11959  11534    586    111   1445       C  
ATOM   1460  OE1 GLU A1011      35.895  -6.518  43.646  1.00 99.56           O  
ANISOU 1460  OE1 GLU A1011    13255  12559  12013    632    -51   1549       O  
ATOM   1461  OE2 GLU A1011      34.920  -7.072  41.751  1.00 94.59           O  
ANISOU 1461  OE2 GLU A1011    12763  11742  11436    596    295   1450       O  
ATOM   1462  N   GLY A1012      33.549  -1.725  43.534  1.00 83.15           N  
ANISOU 1462  N   GLY A1012    11062  10592   9938    362   -351    758       N  
ATOM   1463  CA  GLY A1012      34.064  -0.590  44.272  1.00 80.42           C  
ANISOU 1463  CA  GLY A1012    10644  10253   9660    339   -589    621       C  
ATOM   1464  C   GLY A1012      35.145   0.176  43.536  1.00 76.41           C  
ANISOU 1464  C   GLY A1012    10041   9573   9418    270   -701    745       C  
ATOM   1465  O   GLY A1012      36.026  -0.422  42.909  1.00 75.35           O  
ANISOU 1465  O   GLY A1012     9829   9430   9369    254   -588    972       O  
ATOM   1466  N   LEU A1013      35.090   1.505  43.610  1.00 72.47           N  
ANISOU 1466  N   LEU A1013     9539   8928   9066    216   -914    581       N  
ATOM   1467  CA  LEU A1013      36.059   2.381  42.960  1.00 75.06           C  
ANISOU 1467  CA  LEU A1013     9799   9069   9653     69  -1037    711       C  
ATOM   1468  C   LEU A1013      37.076   2.842  43.998  1.00 85.43           C  
ANISOU 1468  C   LEU A1013    10980  10447  11031    -12  -1266    645       C  
ATOM   1469  O   LEU A1013      36.730   3.569  44.935  1.00 92.30           O  
ANISOU 1469  O   LEU A1013    11906  11301  11864      3  -1478    364       O  
ATOM   1470  CB  LEU A1013      35.362   3.575  42.309  1.00 76.93           C  
ANISOU 1470  CB  LEU A1013    10164   9014  10053     35  -1188    614       C  
ATOM   1471  CG  LEU A1013      36.264   4.677  41.743  1.00 81.85           C  
ANISOU 1471  CG  LEU A1013    10778   9382  10939   -188  -1361    759       C  
ATOM   1472  CD1 LEU A1013      37.119   4.145  40.607  1.00 83.65           C  
ANISOU 1472  CD1 LEU A1013    10936   9672  11176   -345  -1119   1104       C  
ATOM   1473  CD2 LEU A1013      35.444   5.879  41.290  1.00 79.42           C  
ANISOU 1473  CD2 LEU A1013    10661   8711  10803   -183  -1600    657       C  
ATOM   1474  N   ARG A1014      38.324   2.416  43.830  1.00 82.30           N  
ANISOU 1474  N   ARG A1014    10388  10143  10740    -92  -1229    865       N  
ATOM   1475  CA  ARG A1014      39.431   2.846  44.673  1.00 87.70           C  
ANISOU 1475  CA  ARG A1014    10885  10900  11537   -200  -1487    834       C  
ATOM   1476  C   ARG A1014      40.374   3.720  43.858  1.00 91.11           C  
ANISOU 1476  C   ARG A1014    11154  11170  12293   -454  -1533    970       C  
ATOM   1477  O   ARG A1014      40.854   3.301  42.800  1.00 93.58           O  
ANISOU 1477  O   ARG A1014    11348  11510  12699   -513  -1278   1201       O  
ATOM   1478  CB  ARG A1014      40.189   1.647  45.242  1.00 89.70           C  
ANISOU 1478  CB  ARG A1014    10969  11409  11702    -83  -1465    977       C  
ATOM   1479  CG  ARG A1014      39.445   0.867  46.311  1.00 95.14           C  
ANISOU 1479  CG  ARG A1014    11845  12266  12037     80  -1493    888       C  
ATOM   1480  CD  ARG A1014      40.338   0.658  47.527  1.00103.70           C  
ANISOU 1480  CD  ARG A1014    12817  13547  13039     82  -1799    903       C  
ATOM   1481  NE  ARG A1014      39.801  -0.327  48.462  1.00107.67           N  
ANISOU 1481  NE  ARG A1014    13522  14230  13160    204  -1802    939       N  
ATOM   1482  CZ  ARG A1014      40.399  -0.677  49.597  1.00111.85           C  
ANISOU 1482  CZ  ARG A1014    14048  14948  13504    219  -2094    997       C  
ATOM   1483  NH1 ARG A1014      41.553  -0.119  49.939  1.00113.46           N  
ANISOU 1483  NH1 ARG A1014    14008  15196  13905    140  -2424    984       N  
ATOM   1484  NH2 ARG A1014      39.844  -1.584  50.391  1.00112.62           N  
ANISOU 1484  NH2 ARG A1014    14392  15192  13208    282  -2078   1085       N  
ATOM   1485  N   LEU A1015      40.648   4.926  44.357  1.00 92.65           N  
ANISOU 1485  N   LEU A1015    11353  11202  12646   -633  -1845    811       N  
ATOM   1486  CA  LEU A1015      41.453   5.897  43.627  1.00 98.42           C  
ANISOU 1486  CA  LEU A1015    11974  11728  13694   -955  -1914    952       C  
ATOM   1487  C   LEU A1015      42.928   5.886  44.013  1.00100.85           C  
ANISOU 1487  C   LEU A1015    11893  12218  14209  -1148  -2036   1034       C  
ATOM   1488  O   LEU A1015      43.750   6.434  43.268  1.00 98.40           O  
ANISOU 1488  O   LEU A1015    11399  11829  14161  -1460  -1984   1214       O  
ATOM   1489  CB  LEU A1015      40.885   7.309  43.827  1.00 99.65           C  
ANISOU 1489  CB  LEU A1015    12381  11497  13985  -1071  -2220    736       C  
ATOM   1490  CG  LEU A1015      39.471   7.567  43.292  1.00 99.54           C  
ANISOU 1490  CG  LEU A1015    12694  11242  13885   -893  -2166    655       C  
ATOM   1491  CD1 LEU A1015      39.000   8.964  43.667  1.00 99.18           C  
ANISOU 1491  CD1 LEU A1015    12859  10780  14044   -939  -2532    377       C  
ATOM   1492  CD2 LEU A1015      39.410   7.369  41.782  1.00 97.70           C  
ANISOU 1492  CD2 LEU A1015    12526  10927  13670   -996  -1904   1008       C  
ATOM   1493  N   LYS A1016      43.285   5.285  45.145  1.00105.59           N  
ANISOU 1493  N   LYS A1016    12353  13074  14693   -995  -2209    921       N  
ATOM   1494  CA  LYS A1016      44.673   5.127  45.549  1.00101.07           C  
ANISOU 1494  CA  LYS A1016    11354  12717  14330  -1119  -2373    997       C  
ATOM   1495  C   LYS A1016      45.057   3.654  45.506  1.00 97.42           C  
ANISOU 1495  C   LYS A1016    10673  12549  13792   -837  -2171   1168       C  
ATOM   1496  O   LYS A1016      44.204   2.765  45.581  1.00 93.98           O  
ANISOU 1496  O   LYS A1016    10480  12152  13076   -558  -2006   1179       O  
ATOM   1497  CB  LYS A1016      44.913   5.693  46.953  1.00 96.36           C  
ANISOU 1497  CB  LYS A1016    10775  12159  13680  -1180  -2856    730       C  
ATOM   1498  N   ILE A1017      46.361   3.401  45.382  1.00 93.92           N  
ANISOU 1498  N   ILE A1017     9745  12296  13643   -915  -2196   1291       N  
ATOM   1499  CA  ILE A1017      46.835   2.030  45.257  1.00 95.27           C  
ANISOU 1499  CA  ILE A1017     9663  12692  13845   -609  -2025   1434       C  
ATOM   1500  C   ILE A1017      46.498   1.247  46.517  1.00 93.58           C  
ANISOU 1500  C   ILE A1017     9634  12578  13344   -317  -2322   1390       C  
ATOM   1501  O   ILE A1017      46.630   1.745  47.643  1.00 98.49           O  
ANISOU 1501  O   ILE A1017    10306  13255  13861   -400  -2751   1258       O  
ATOM   1502  CB  ILE A1017      48.346   2.013  44.968  1.00 99.88           C  
ANISOU 1502  CB  ILE A1017     9604  13484  14862   -733  -2035   1517       C  
ATOM   1503  CG1 ILE A1017      48.641   2.776  43.677  1.00 99.15           C  
ANISOU 1503  CG1 ILE A1017     9368  13325  14980  -1097  -1674   1598       C  
ATOM   1504  CG2 ILE A1017      48.859   0.586  44.863  1.00102.32           C  
ANISOU 1504  CG2 ILE A1017     9624  13983  15272   -342  -1894   1617       C  
ATOM   1505  CD1 ILE A1017      50.072   2.657  43.214  1.00100.19           C  
ANISOU 1505  CD1 ILE A1017     8808  13728  15530  -1237  -1535   1668       C  
ATOM   1506  N   TYR A1018      46.040   0.013  46.328  1.00 96.96           N  
ANISOU 1506  N   TYR A1018    10204  13021  13613     -4  -2100   1503       N  
ATOM   1507  CA  TYR A1018      45.693  -0.867  47.432  1.00100.96           C  
ANISOU 1507  CA  TYR A1018    10937  13603  13821    241  -2341   1544       C  
ATOM   1508  C   TYR A1018      45.961  -2.303  47.006  1.00113.96           C  
ANISOU 1508  C   TYR A1018    12472  15250  15576    569  -2149   1734       C  
ATOM   1509  O   TYR A1018      46.224  -2.587  45.835  1.00121.07           O  
ANISOU 1509  O   TYR A1018    13172  16106  16722    616  -1774   1767       O  
ATOM   1510  CB  TYR A1018      44.232  -0.693  47.850  1.00 93.06           C  
ANISOU 1510  CB  TYR A1018    10474  12514  12372    220  -2278   1421       C  
ATOM   1511  CG  TYR A1018      43.253  -1.208  46.822  1.00 94.64           C  
ANISOU 1511  CG  TYR A1018    10901  12566  12493    308  -1824   1465       C  
ATOM   1512  CD1 TYR A1018      43.069  -0.541  45.617  1.00 98.44           C  
ANISOU 1512  CD1 TYR A1018    11346  12911  13146    160  -1544   1428       C  
ATOM   1513  CD2 TYR A1018      42.513  -2.358  47.053  1.00 92.36           C  
ANISOU 1513  CD2 TYR A1018    10884  12266  11944    505  -1704   1563       C  
ATOM   1514  CE1 TYR A1018      42.179  -1.007  44.669  1.00 97.08           C  
ANISOU 1514  CE1 TYR A1018    11389  12624  12873    230  -1183   1460       C  
ATOM   1515  CE2 TYR A1018      41.614  -2.831  46.111  1.00 95.41           C  
ANISOU 1515  CE2 TYR A1018    11463  12519  12271    556  -1325   1577       C  
ATOM   1516  CZ  TYR A1018      41.450  -2.147  44.923  1.00 96.24           C  
ANISOU 1516  CZ  TYR A1018    11515  12518  12534    430  -1079   1511       C  
ATOM   1517  OH  TYR A1018      40.562  -2.611  43.980  1.00 94.30           O  
ANISOU 1517  OH  TYR A1018    11469  12159  12201    471   -755   1517       O  
ATOM   1518  N   LYS A1019      45.882  -3.212  47.972  1.00112.29           N  
ANISOU 1518  N   LYS A1019    12428  15075  15161    787  -2416   1854       N  
ATOM   1519  CA  LYS A1019      46.124  -4.629  47.736  1.00114.49           C  
ANISOU 1519  CA  LYS A1019    12662  15272  15567   1129  -2330   2040       C  
ATOM   1520  C   LYS A1019      44.796  -5.365  47.616  1.00112.47           C  
ANISOU 1520  C   LYS A1019    12933  14846  14954   1191  -2067   2094       C  
ATOM   1521  O   LYS A1019      43.893  -5.162  48.435  1.00114.99           O  
ANISOU 1521  O   LYS A1019    13645  15200  14846   1061  -2176   2073       O  
ATOM   1522  CB  LYS A1019      46.964  -5.233  48.863  1.00116.93           C  
ANISOU 1522  CB  LYS A1019    12829  15675  15923   1330  -2866   2206       C  
ATOM   1523  N   ASP A1020      44.677  -6.212  46.597  1.00112.39           N  
ANISOU 1523  N   ASP A1020    12914  14672  15118   1369  -1707   2129       N  
ATOM   1524  CA  ASP A1020      43.491  -7.038  46.453  1.00108.38           C  
ANISOU 1524  CA  ASP A1020    12868  13981  14329   1415  -1485   2186       C  
ATOM   1525  C   ASP A1020      43.556  -8.206  47.436  1.00111.34           C  
ANISOU 1525  C   ASP A1020    13459  14255  14590   1619  -1796   2432       C  
ATOM   1526  O   ASP A1020      44.475  -8.316  48.253  1.00111.64           O  
ANISOU 1526  O   ASP A1020    13307  14376  14734   1741  -2219   2559       O  
ATOM   1527  CB  ASP A1020      43.344  -7.520  45.010  1.00103.84           C  
ANISOU 1527  CB  ASP A1020    12244  13254  13957   1507  -1026   2105       C  
ATOM   1528  CG  ASP A1020      44.444  -8.477  44.594  1.00108.01           C  
ANISOU 1528  CG  ASP A1020    12440  13694  14903   1844  -1010   2150       C  
ATOM   1529  OD1 ASP A1020      45.525  -8.453  45.217  1.00113.64           O  
ANISOU 1529  OD1 ASP A1020    12802  14515  15861   1981  -1346   2220       O  
ATOM   1530  OD2 ASP A1020      44.228  -9.253  43.639  1.00105.75           O1+
ANISOU 1530  OD2 ASP A1020    12227  13235  14718   1987   -677   2082       O1+
ATOM   1531  N   THR A1021      42.571  -9.101  47.357  1.00111.86           N  
ANISOU 1531  N   THR A1021    13936  14124  14441   1634  -1618   2524       N  
ATOM   1532  CA  THR A1021      42.498 -10.201  48.311  1.00111.37           C  
ANISOU 1532  CA  THR A1021    14180  13918  14216   1754  -1913   2816       C  
ATOM   1533  C   THR A1021      43.592 -11.242  48.108  1.00113.87           C  
ANISOU 1533  C   THR A1021    14272  14000  14994   2154  -2104   2966       C  
ATOM   1534  O   THR A1021      43.713 -12.150  48.936  1.00122.97           O  
ANISOU 1534  O   THR A1021    15669  14982  16073   2291  -2453   3261       O  
ATOM   1535  CB  THR A1021      41.130 -10.879  48.236  1.00106.11           C  
ANISOU 1535  CB  THR A1021    14000  13085  13230   1600  -1650   2877       C  
ATOM   1536  OG1 THR A1021      40.997 -11.555  46.980  1.00101.52           O  
ANISOU 1536  OG1 THR A1021    13390  12234  12949   1746  -1308   2783       O  
ATOM   1537  CG2 THR A1021      40.020  -9.844  48.372  1.00105.59           C  
ANISOU 1537  CG2 THR A1021    14074  13265  12778   1259  -1443   2671       C  
ATOM   1538  N   GLU A1022      44.388 -11.136  47.045  1.00109.65           N  
ANISOU 1538  N   GLU A1022    13282  13452  14927   2346  -1889   2772       N  
ATOM   1539  CA  GLU A1022      45.477 -12.070  46.790  1.00109.91           C  
ANISOU 1539  CA  GLU A1022    13002  13289  15472   2780  -2033   2824       C  
ATOM   1540  C   GLU A1022      46.850 -11.447  47.014  1.00110.30           C  
ANISOU 1540  C   GLU A1022    12423  13602  15882   2906  -2315   2766       C  
ATOM   1541  O   GLU A1022      47.866 -12.107  46.769  1.00114.91           O  
ANISOU 1541  O   GLU A1022    12609  14084  16969   3299  -2431   2752       O  
ATOM   1542  CB  GLU A1022      45.376 -12.625  45.367  1.00110.94           C  
ANISOU 1542  CB  GLU A1022    13056  13217  15878   2939  -1526   2594       C  
ATOM   1543  N   GLY A1023      46.907 -10.195  47.471  1.00108.89           N  
ANISOU 1543  N   GLY A1023    12123  13753  15498   2586  -2436   2704       N  
ATOM   1544  CA  GLY A1023      48.156  -9.536  47.793  1.00110.44           C  
ANISOU 1544  CA  GLY A1023    11736  14212  16013   2619  -2755   2653       C  
ATOM   1545  C   GLY A1023      48.709  -8.632  46.710  1.00113.05           C  
ANISOU 1545  C   GLY A1023    11548  14751  16654   2465  -2360   2382       C  
ATOM   1546  O   GLY A1023      49.639  -7.862  46.986  1.00112.39           O  
ANISOU 1546  O   GLY A1023    10982  14921  16798   2361  -2597   2323       O  
ATOM   1547  N   TYR A1024      48.174  -8.700  45.495  1.00108.30           N  
ANISOU 1547  N   TYR A1024    11043  14058  16046   2411  -1784   2230       N  
ATOM   1548  CA  TYR A1024      48.663  -7.880  44.398  1.00113.34           C  
ANISOU 1548  CA  TYR A1024    11259  14900  16907   2217  -1372   2019       C  
ATOM   1549  C   TYR A1024      48.186  -6.439  44.545  1.00111.52           C  
ANISOU 1549  C   TYR A1024    11170  14816  16386   1738  -1381   1979       C  
ATOM   1550  O   TYR A1024      47.084  -6.173  45.033  1.00110.91           O  
ANISOU 1550  O   TYR A1024    11615  14645  15882   1574  -1459   2021       O  
ATOM   1551  CB  TYR A1024      48.188  -8.447  43.060  1.00116.94           C  
ANISOU 1551  CB  TYR A1024    11856  15216  17360   2297   -787   1879       C  
ATOM   1552  CG  TYR A1024      48.578  -9.890  42.820  1.00122.30           C  
ANISOU 1552  CG  TYR A1024    12446  15674  18349   2790   -744   1850       C  
ATOM   1553  CD1 TYR A1024      49.830 -10.364  43.189  1.00128.61           C  
ANISOU 1553  CD1 TYR A1024    12689  16530  19645   3150  -1024   1848       C  
ATOM   1554  CD2 TYR A1024      47.689 -10.779  42.227  1.00118.01           C  
ANISOU 1554  CD2 TYR A1024    12364  14836  17638   2906   -460   1804       C  
ATOM   1555  CE1 TYR A1024      50.188 -11.681  42.970  1.00131.77           C  
ANISOU 1555  CE1 TYR A1024    13011  16664  20391   3655  -1019   1793       C  
ATOM   1556  CE2 TYR A1024      48.037 -12.096  42.004  1.00120.38           C  
ANISOU 1556  CE2 TYR A1024    12621  14859  18257   3363   -444   1744       C  
ATOM   1557  CZ  TYR A1024      49.287 -12.542  42.377  1.00129.11           C  
ANISOU 1557  CZ  TYR A1024    13187  15991  19879   3758   -723   1736       C  
ATOM   1558  OH  TYR A1024      49.639 -13.855  42.158  1.00133.04           O  
ANISOU 1558  OH  TYR A1024    13642  16152  20756   4269   -742   1651       O  
ATOM   1559  N   TYR A1025      49.029  -5.504  44.113  1.00117.71           N  
ANISOU 1559  N   TYR A1025    11469  15821  17433   1507  -1294   1881       N  
ATOM   1560  CA  TYR A1025      48.682  -4.087  44.152  1.00110.35           C  
ANISOU 1560  CA  TYR A1025    10659  14955  16314   1049  -1319   1834       C  
ATOM   1561  C   TYR A1025      47.758  -3.760  42.985  1.00104.43           C  
ANISOU 1561  C   TYR A1025    10246  14092  15339    855   -821   1781       C  
ATOM   1562  O   TYR A1025      48.115  -3.979  41.822  1.00101.17           O  
ANISOU 1562  O   TYR A1025     9617  13740  15082    859   -384   1729       O  
ATOM   1563  CB  TYR A1025      49.939  -3.221  44.101  1.00111.84           C  
ANISOU 1563  CB  TYR A1025    10220  15385  16890    814  -1427   1782       C  
ATOM   1564  CG  TYR A1025      50.892  -3.432  45.257  1.00115.51           C  
ANISOU 1564  CG  TYR A1025    10303  15992  17595    978  -1998   1822       C  
ATOM   1565  CD1 TYR A1025      50.776  -2.688  46.423  1.00114.38           C  
ANISOU 1565  CD1 TYR A1025    10332  15875  17252    775  -2517   1825       C  
ATOM   1566  CD2 TYR A1025      51.915  -4.369  45.177  1.00120.42           C  
ANISOU 1566  CD2 TYR A1025    10384  16722  18646   1352  -2046   1830       C  
ATOM   1567  CE1 TYR A1025      51.647  -2.875  47.481  1.00116.89           C  
ANISOU 1567  CE1 TYR A1025    10328  16345  17742    906  -3095   1869       C  
ATOM   1568  CE2 TYR A1025      52.791  -4.563  46.228  1.00124.27           C  
ANISOU 1568  CE2 TYR A1025    10509  17338  19372   1522  -2643   1887       C  
ATOM   1569  CZ  TYR A1025      52.653  -3.813  47.377  1.00124.31           C  
ANISOU 1569  CZ  TYR A1025    10724  17386  19121   1279  -3180   1923       C  
ATOM   1570  OH  TYR A1025      53.523  -4.004  48.428  1.00131.17           O  
ANISOU 1570  OH  TYR A1025    11258  18402  20177   1430  -3829   1986       O  
ATOM   1571  N   THR A1026      46.569  -3.247  43.288  1.00104.70           N  
ANISOU 1571  N   THR A1026    10799  13985  14997    692   -893   1776       N  
ATOM   1572  CA  THR A1026      45.596  -2.892  42.268  1.00105.81           C  
ANISOU 1572  CA  THR A1026    11282  14002  14919    524   -528   1739       C  
ATOM   1573  C   THR A1026      45.108  -1.467  42.499  1.00102.55           C  
ANISOU 1573  C   THR A1026    11058  13525  14382    179   -701   1694       C  
ATOM   1574  O   THR A1026      45.449  -0.819  43.493  1.00 98.86           O  
ANISOU 1574  O   THR A1026    10500  13102  13962     75  -1083   1653       O  
ATOM   1575  CB  THR A1026      44.400  -3.858  42.255  1.00102.47           C  
ANISOU 1575  CB  THR A1026    11323  13413  14198    735   -413   1745       C  
ATOM   1576  OG1 THR A1026      43.497  -3.517  43.312  1.00 98.43           O  
ANISOU 1576  OG1 THR A1026    11152  12846  13400    677   -704   1728       O  
ATOM   1577  CG2 THR A1026      44.861  -5.301  42.437  1.00103.30           C  
ANISOU 1577  CG2 THR A1026    11315  13487  14447   1108   -410   1798       C  
ATOM   1578  N   ILE A1027      44.296  -0.982  41.560  1.00 99.57           N  
ANISOU 1578  N   ILE A1027    10963  13018  13850     15   -450   1686       N  
ATOM   1579  CA  ILE A1027      43.734   0.361  41.638  1.00 94.27           C  
ANISOU 1579  CA  ILE A1027    10513  12198  13107   -265   -621   1637       C  
ATOM   1580  C   ILE A1027      42.483   0.419  40.770  1.00 89.78           C  
ANISOU 1580  C   ILE A1027    10350  11463  12301   -276   -407   1635       C  
ATOM   1581  O   ILE A1027      42.233  -0.483  39.962  1.00 86.52           O  
ANISOU 1581  O   ILE A1027    10008  11080  11787   -145    -97   1677       O  
ATOM   1582  CB  ILE A1027      44.771   1.417  41.213  1.00 89.65           C  
ANISOU 1582  CB  ILE A1027     9615  11643  12803   -620   -639   1700       C  
ATOM   1583  CG1 ILE A1027      44.397   2.796  41.761  1.00 84.69           C  
ANISOU 1583  CG1 ILE A1027     9187  10803  12189   -869   -988   1614       C  
ATOM   1584  CG2 ILE A1027      44.914   1.453  39.698  1.00 80.58           C  
ANISOU 1584  CG2 ILE A1027     8450  10512  11654   -794   -204   1829       C  
ATOM   1585  CD1 ILE A1027      45.403   3.866  41.434  1.00 82.74           C  
ANISOU 1585  CD1 ILE A1027     8667  10528  12241  -1282  -1056   1694       C  
ATOM   1586  N   GLY A1028      41.681   1.469  40.938  1.00 90.15           N  
ANISOU 1586  N   GLY A1028    10659  11318  12274   -414   -605   1560       N  
ATOM   1587  CA  GLY A1028      40.491   1.617  40.118  1.00 84.64           C  
ANISOU 1587  CA  GLY A1028    10306  10458  11396   -412   -482   1559       C  
ATOM   1588  C   GLY A1028      39.429   0.607  40.504  1.00 83.32           C  
ANISOU 1588  C   GLY A1028    10333  10329  10994   -142   -422   1455       C  
ATOM   1589  O   GLY A1028      39.140   0.390  41.685  1.00 81.04           O  
ANISOU 1589  O   GLY A1028    10066  10102  10624    -17   -599   1333       O  
ATOM   1590  N   ILE A1029      38.832  -0.021  39.494  1.00 90.61           N  
ANISOU 1590  N   ILE A1029    11415  11232  11782    -90   -168   1506       N  
ATOM   1591  CA  ILE A1029      37.857  -1.077  39.728  1.00 88.98           C  
ANISOU 1591  CA  ILE A1029    11375  11052  11381    109    -82   1426       C  
ATOM   1592  C   ILE A1029      38.467  -2.405  39.306  1.00 96.86           C  
ANISOU 1592  C   ILE A1029    12278  12138  12386    239    180   1504       C  
ATOM   1593  O   ILE A1029      38.305  -2.841  38.160  1.00 98.47           O  
ANISOU 1593  O   ILE A1029    12577  12322  12515    224    426   1527       O  
ATOM   1594  CB  ILE A1029      36.538  -0.812  38.980  1.00 75.33           C  
ANISOU 1594  CB  ILE A1029     9908   9202   9511     82    -63   1368       C  
ATOM   1595  CG1 ILE A1029      35.978   0.560  39.350  1.00 71.56           C  
ANISOU 1595  CG1 ILE A1029     9501   8581   9108     11   -352   1261       C  
ATOM   1596  CG2 ILE A1029      35.522  -1.900  39.298  1.00 63.88           C  
ANISOU 1596  CG2 ILE A1029     8583   7799   7889    229     23   1272       C  
ATOM   1597  CD1 ILE A1029      34.589   0.806  38.813  1.00 68.30           C  
ANISOU 1597  CD1 ILE A1029     9287   8054   8610     55   -413   1168       C  
ATOM   1598  N   GLY A1030      39.179  -3.050  40.226  1.00 99.15           N  
ANISOU 1598  N   GLY A1030    12396  12511  12765    380    101   1529       N  
ATOM   1599  CA  GLY A1030      39.787  -4.335  39.947  1.00 98.18           C  
ANISOU 1599  CA  GLY A1030    12171  12410  12722    571    291   1577       C  
ATOM   1600  C   GLY A1030      40.760  -4.288  38.789  1.00 94.57           C  
ANISOU 1600  C   GLY A1030    11485  12025  12421    523    562   1598       C  
ATOM   1601  O   GLY A1030      40.506  -4.869  37.728  1.00 95.69           O  
ANISOU 1601  O   GLY A1030    11749  12138  12469    550    849   1553       O  
ATOM   1602  N   HIS A1031      41.878  -3.592  38.977  1.00 87.03           N  
ANISOU 1602  N   HIS A1031    10189  11192  11687    421    486   1644       N  
ATOM   1603  CA  HIS A1031      42.893  -3.436  37.938  1.00 89.86           C  
ANISOU 1603  CA  HIS A1031    10256  11692  12196    312    785   1660       C  
ATOM   1604  C   HIS A1031      44.259  -3.687  38.565  1.00 92.16           C  
ANISOU 1604  C   HIS A1031    10046  12138  12831    439    693   1664       C  
ATOM   1605  O   HIS A1031      44.848  -2.781  39.162  1.00 95.75           O  
ANISOU 1605  O   HIS A1031    10270  12666  13443    260    450   1711       O  
ATOM   1606  CB  HIS A1031      42.821  -2.053  37.308  1.00 89.34           C  
ANISOU 1606  CB  HIS A1031    10256  11621  12066    -69    797   1742       C  
ATOM   1607  CG  HIS A1031      43.762  -1.865  36.161  1.00 92.70           C  
ANISOU 1607  CG  HIS A1031    10434  12232  12556   -271   1167   1789       C  
ATOM   1608  ND1 HIS A1031      43.332  -1.784  34.855  1.00 93.45           N  
ANISOU 1608  ND1 HIS A1031    10789  12339  12379   -440   1471   1824       N  
ATOM   1609  CD2 HIS A1031      45.109  -1.748  36.123  1.00 96.67           C  
ANISOU 1609  CD2 HIS A1031    10434  12956  13341   -356   1297   1798       C  
ATOM   1610  CE1 HIS A1031      44.375  -1.621  34.061  1.00 97.80           C  
ANISOU 1610  CE1 HIS A1031    11037  13125  12996   -641   1814   1858       C  
ATOM   1611  NE2 HIS A1031      45.465  -1.597  34.805  1.00100.11           N  
ANISOU 1611  NE2 HIS A1031    10830  13554  13654   -592   1731   1833       N  
ATOM   1612  N   LEU A1032      44.761  -4.912  38.422  1.00 91.24           N  
ANISOU 1612  N   LEU A1032     9754  12051  12863    756    853   1596       N  
ATOM   1613  CA  LEU A1032      46.058  -5.267  38.982  1.00 95.11           C  
ANISOU 1613  CA  LEU A1032     9720  12682  13737    952    730   1587       C  
ATOM   1614  C   LEU A1032      47.161  -4.499  38.265  1.00 99.71           C  
ANISOU 1614  C   LEU A1032     9815  13531  14540    697    975   1562       C  
ATOM   1615  O   LEU A1032      47.347  -4.649  37.054  1.00 96.96           O  
ANISOU 1615  O   LEU A1032     9403  13297  14140    624   1442   1479       O  
ATOM   1616  CB  LEU A1032      46.290  -6.772  38.868  1.00 93.50           C  
ANISOU 1616  CB  LEU A1032     9457  12381  13686   1392    849   1495       C  
ATOM   1617  N   LEU A1033      47.887  -3.667  39.013  1.00 97.35           N  
ANISOU 1617  N   LEU A1033     9181  13349  14459    521    666   1628       N  
ATOM   1618  CA  LEU A1033      49.025  -2.964  38.434  1.00104.31           C  
ANISOU 1618  CA  LEU A1033     9528  14502  15604    230    883   1619       C  
ATOM   1619  C   LEU A1033      50.158  -3.934  38.121  1.00112.65           C  
ANISOU 1619  C   LEU A1033     9983  15786  17034    550   1131   1473       C  
ATOM   1620  O   LEU A1033      50.737  -3.897  37.029  1.00115.99           O  
ANISOU 1620  O   LEU A1033    10102  16446  17521    410   1635   1381       O  
ATOM   1621  CB  LEU A1033      49.494  -1.861  39.381  1.00103.46           C  
ANISOU 1621  CB  LEU A1033     9213  14430  15668    -55    434   1699       C  
ATOM   1622  N   THR A1034      50.477  -4.818  39.064  1.00114.71           N  
ANISOU 1622  N   THR A1034    10071  15980  17534    990    782   1443       N  
ATOM   1623  CA  THR A1034      51.514  -5.822  38.866  1.00119.05           C  
ANISOU 1623  CA  THR A1034    10043  16677  18514   1403    933   1278       C  
ATOM   1624  C   THR A1034      51.333  -6.919  39.904  1.00116.13           C  
ANISOU 1624  C   THR A1034     9831  16045  18250   1915    470   1326       C  
ATOM   1625  O   THR A1034      50.615  -6.756  40.893  1.00112.94           O  
ANISOU 1625  O   THR A1034     9869  15449  17593   1873     24   1499       O  
ATOM   1626  CB  THR A1034      52.919  -5.218  38.968  1.00123.11           C  
ANISOU 1626  CB  THR A1034     9729  17558  19489   1237    901   1232       C  
ATOM   1627  OG1 THR A1034      53.898  -6.241  38.746  1.00127.31           O  
ANISOU 1627  OG1 THR A1034     9644  18240  20490   1707   1059   1022       O  
ATOM   1628  CG2 THR A1034      53.135  -4.617  40.344  1.00124.58           C  
ANISOU 1628  CG2 THR A1034     9836  17714  19783   1140    210   1384       C  
ATOM   1629  N   LYS A1035      51.998  -8.046  39.660  1.00124.24           N  
ANISOU 1629  N   LYS A1035    10499  17061  19647   2398    588   1165       N  
ATOM   1630  CA  LYS A1035      52.071  -9.132  40.624  1.00115.60           C  
ANISOU 1630  CA  LYS A1035     9471  15694  18757   2910    100   1245       C  
ATOM   1631  C   LYS A1035      53.350  -9.089  41.448  1.00124.45           C  
ANISOU 1631  C   LYS A1035     9878  17011  20395   3112   -361   1270       C  
ATOM   1632  O   LYS A1035      53.591 -10.004  42.241  1.00126.86           O  
ANISOU 1632  O   LYS A1035    10167  17100  20932   3572   -826   1360       O  
ATOM   1633  CB  LYS A1035      51.953 -10.483  39.911  1.00108.04           C  
ANISOU 1633  CB  LYS A1035     8621  14489  17940   3381    417   1046       C  
ATOM   1634  N   SER A1036      54.169  -8.044  41.282  1.00124.75           N  
ANISOU 1634  N   SER A1036     9333  17441  20626   2756   -279   1212       N  
ATOM   1635  CA  SER A1036      55.429  -7.892  41.994  1.00130.16           C  
ANISOU 1635  CA  SER A1036     9248  18374  21834   2880   -717   1205       C  
ATOM   1636  C   SER A1036      55.191  -7.369  43.411  1.00127.51           C  
ANISOU 1636  C   SER A1036     9199  17961  21290   2719  -1470   1465       C  
ATOM   1637  O   SER A1036      54.249  -6.611  43.652  1.00124.62           O  
ANISOU 1637  O   SER A1036     9437  17497  20415   2316  -1507   1585       O  
ATOM   1638  CB  SER A1036      56.351  -6.937  41.243  1.00133.68           C  
ANISOU 1638  CB  SER A1036     8966  19280  22547   2465   -307   1043       C  
ATOM   1639  N   PRO A1037      56.041  -7.758  44.369  1.00132.59           N  
ANISOU 1639  N   PRO A1037     9408  18656  22314   3043  -2094   1531       N  
ATOM   1640  CA  PRO A1037      55.818  -7.332  45.758  1.00131.46           C  
ANISOU 1640  CA  PRO A1037     9590  18465  21895   2895  -2836   1763       C  
ATOM   1641  C   PRO A1037      56.251  -5.907  46.050  1.00131.07           C  
ANISOU 1641  C   PRO A1037     9233  18724  21845   2324  -3004   1723       C  
ATOM   1642  O   PRO A1037      55.767  -5.327  47.031  1.00128.15           O  
ANISOU 1642  O   PRO A1037     9314  18300  21079   2075  -3470   1849       O  
ATOM   1643  CB  PRO A1037      56.658  -8.330  46.564  1.00137.89           C  
ANISOU 1643  CB  PRO A1037    10022  19225  23144   3474  -3467   1855       C  
ATOM   1644  CG  PRO A1037      57.788  -8.659  45.647  1.00141.32           C  
ANISOU 1644  CG  PRO A1037     9525  19887  24282   3748  -3098   1581       C  
ATOM   1645  CD  PRO A1037      57.205  -8.654  44.250  1.00138.32           C  
ANISOU 1645  CD  PRO A1037     9352  19476  23728   3597  -2186   1384       C  
ATOM   1646  N   SER A1038      57.142  -5.329  45.249  1.00134.97           N  
ANISOU 1646  N   SER A1038     8987  19535  22758   2087  -2636   1539       N  
ATOM   1647  CA  SER A1038      57.615  -3.977  45.512  1.00138.82           C  
ANISOU 1647  CA  SER A1038     9165  20272  23307   1497  -2818   1510       C  
ATOM   1648  C   SER A1038      56.508  -2.965  45.234  1.00142.03           C  
ANISOU 1648  C   SER A1038    10304  20506  23157    966  -2548   1556       C  
ATOM   1649  O   SER A1038      55.905  -2.966  44.156  1.00142.81           O  
ANISOU 1649  O   SER A1038    10685  20515  23061    864  -1905   1526       O  
ATOM   1650  CB  SER A1038      58.845  -3.669  44.659  1.00137.97           C  
ANISOU 1650  CB  SER A1038     8060  20560  23801   1331  -2429   1322       C  
ATOM   1651  N   LEU A1039      56.235  -2.105  46.219  1.00148.93           N  
ANISOU 1651  N   LEU A1039    11491  21326  23772    647  -3071   1607       N  
ATOM   1652  CA  LEU A1039      55.237  -1.059  46.027  1.00137.41           C  
ANISOU 1652  CA  LEU A1039    10670  19674  21866    176  -2887   1609       C  
ATOM   1653  C   LEU A1039      55.728  -0.005  45.042  1.00134.86           C  
ANISOU 1653  C   LEU A1039     9968  19484  21790   -372  -2464   1547       C  
ATOM   1654  O   LEU A1039      54.942   0.522  44.246  1.00128.51           O  
ANISOU 1654  O   LEU A1039     9617  18504  20707   -648  -2029   1577       O  
ATOM   1655  CB  LEU A1039      54.882  -0.422  47.371  1.00133.76           C  
ANISOU 1655  CB  LEU A1039    10606  19126  21088      8  -3557   1606       C  
ATOM   1656  CG  LEU A1039      53.969   0.807  47.351  1.00123.44           C  
ANISOU 1656  CG  LEU A1039     9880  17606  19417   -461  -3487   1537       C  
ATOM   1657  CD1 LEU A1039      52.634   0.486  46.697  1.00115.73           C  
ANISOU 1657  CD1 LEU A1039     9575  16373  18024   -334  -3002   1586       C  
ATOM   1658  CD2 LEU A1039      53.766   1.349  48.759  1.00121.51           C  
ANISOU 1658  CD2 LEU A1039     9948  17332  18887   -575  -4163   1451       C  
ATOM   1659  N   ASN A1040      57.027   0.309  45.078  1.00140.78           N  
ANISOU 1659  N   ASN A1040     9881  20545  23065   -557  -2602   1481       N  
ATOM   1660  CA  ASN A1040      57.584   1.273  44.135  1.00137.59           C  
ANISOU 1660  CA  ASN A1040     9069  20297  22910  -1145  -2171   1458       C  
ATOM   1661  C   ASN A1040      57.424   0.803  42.695  1.00142.78           C  
ANISOU 1661  C   ASN A1040     9696  21027  23528  -1086  -1335   1468       C  
ATOM   1662  O   ASN A1040      57.214   1.623  41.793  1.00129.49           O  
ANISOU 1662  O   ASN A1040     8176  19309  21715  -1595   -895   1536       O  
ATOM   1663  CB  ASN A1040      59.058   1.528  44.452  1.00137.97           C  
ANISOU 1663  CB  ASN A1040     8117  20728  23578  -1326  -2453   1368       C  
ATOM   1664  N   ALA A1041      57.513  -0.508  42.459  1.00141.43           N  
ANISOU 1664  N   ALA A1041     9359  20933  23447   -478  -1132   1401       N  
ATOM   1665  CA  ALA A1041      57.326  -1.032  41.111  1.00146.42           C  
ANISOU 1665  CA  ALA A1041    10009  21635  23988   -388   -344   1347       C  
ATOM   1666  C   ALA A1041      55.865  -0.980  40.683  1.00137.93           C  
ANISOU 1666  C   ALA A1041     9919  20195  22294   -425   -117   1454       C  
ATOM   1667  O   ALA A1041      55.576  -0.783  39.497  1.00137.36           O  
ANISOU 1667  O   ALA A1041    10016  20159  22015   -671    490   1467       O  
ATOM   1668  CB  ALA A1041      57.852  -2.465  41.023  1.00155.04           C  
ANISOU 1668  CB  ALA A1041    10644  22857  25406    310   -239   1186       C  
ATOM   1669  N   ALA A1042      54.935  -1.157  41.626  1.00140.82           N  
ANISOU 1669  N   ALA A1042    10925  20238  22341   -200   -595   1527       N  
ATOM   1670  CA  ALA A1042      53.519  -1.060  41.288  1.00132.90           C  
ANISOU 1670  CA  ALA A1042    10790  18913  20795   -244   -420   1604       C  
ATOM   1671  C   ALA A1042      53.142   0.352  40.863  1.00133.14           C  
ANISOU 1671  C   ALA A1042    11109  18838  20640   -869   -326   1693       C  
ATOM   1672  O   ALA A1042      52.205   0.531  40.075  1.00130.01           O  
ANISOU 1672  O   ALA A1042    11253  18260  19885   -986      1   1755       O  
ATOM   1673  CB  ALA A1042      52.662  -1.505  42.472  1.00126.18           C  
ANISOU 1673  CB  ALA A1042    10481  17801  19659     81   -937   1646       C  
ATOM   1674  N   LYS A1043      53.853   1.361  41.370  1.00137.98           N  
ANISOU 1674  N   LYS A1043    11384  19531  21510  -1275   -652   1703       N  
ATOM   1675  CA  LYS A1043      53.613   2.736  40.950  1.00131.35           C  
ANISOU 1675  CA  LYS A1043    10799  18530  20579  -1894   -598   1802       C  
ATOM   1676  C   LYS A1043      54.204   3.022  39.577  1.00133.43           C  
ANISOU 1676  C   LYS A1043    10730  19015  20952  -2291     34   1891       C  
ATOM   1677  O   LYS A1043      53.705   3.899  38.864  1.00133.13           O  
ANISOU 1677  O   LYS A1043    11108  18782  20694  -2733    227   2044       O  
ATOM   1678  CB  LYS A1043      54.192   3.713  41.976  1.00128.92           C  
ANISOU 1678  CB  LYS A1043    10263  18193  20526  -2230  -1186   1758       C  
ATOM   1679  CG  LYS A1043      53.569   3.618  43.359  1.00124.36           C  
ANISOU 1679  CG  LYS A1043    10090  17422  19739  -1936  -1811   1654       C  
ATOM   1680  CD  LYS A1043      54.054   4.744  44.258  1.00124.45           C  
ANISOU 1680  CD  LYS A1043     9973  17371  19941  -2345  -2374   1565       C  
ATOM   1681  CE  LYS A1043      53.301   4.761  45.577  1.00122.13           C  
ANISOU 1681  CE  LYS A1043    10189  16897  19319  -2105  -2935   1426       C  
ATOM   1682  NZ  LYS A1043      53.698   5.919  46.425  1.00124.65           N  
ANISOU 1682  NZ  LYS A1043    10461  17121  19779  -2520  -3485   1275       N  
ATOM   1683  N   SER A1044      55.263   2.305  39.194  1.00130.51           N  
ANISOU 1683  N   SER A1044     9619  19057  20914  -2142    357   1795       N  
ATOM   1684  CA  SER A1044      55.858   2.511  37.879  1.00137.15           C  
ANISOU 1684  CA  SER A1044    10108  20197  21806  -2533   1041   1845       C  
ATOM   1685  C   SER A1044      54.904   2.086  36.770  1.00136.57           C  
ANISOU 1685  C   SER A1044    10643  20016  21232  -2427   1563   1899       C  
ATOM   1686  O   SER A1044      54.789   2.771  35.747  1.00141.22           O  
ANISOU 1686  O   SER A1044    11441  20628  21589  -2937   1967   2067       O  
ATOM   1687  CB  SER A1044      57.179   1.749  37.775  1.00143.25           C  
ANISOU 1687  CB  SER A1044     9888  21468  23072  -2311   1285   1648       C  
ATOM   1688  N   GLU A1045      54.211   0.960  36.954  1.00136.81           N  
ANISOU 1688  N   GLU A1045    10988  19917  21076  -1800   1534   1777       N  
ATOM   1689  CA  GLU A1045      53.243   0.521  35.955  1.00129.18           C  
ANISOU 1689  CA  GLU A1045    10619  18832  19631  -1695   1960   1797       C  
ATOM   1690  C   GLU A1045      52.010   1.415  35.939  1.00128.34           C  
ANISOU 1690  C   GLU A1045    11333  18313  19118  -1974   1718   2002       C  
ATOM   1691  O   GLU A1045      51.383   1.582  34.887  1.00126.75           O  
ANISOU 1691  O   GLU A1045    11575  18053  18531  -2171   2069   2109       O  
ATOM   1692  CB  GLU A1045      52.847  -0.934  36.210  1.00121.20           C  
ANISOU 1692  CB  GLU A1045     9714  17751  18586   -982   1950   1604       C  
ATOM   1693  N   LEU A1046      51.650   1.998  37.088  1.00131.91           N  
ANISOU 1693  N   LEU A1046    11988  18485  19645  -1980   1106   2037       N  
ATOM   1694  CA  LEU A1046      50.490   2.885  37.146  1.00126.43           C  
ANISOU 1694  CA  LEU A1046    12012  17383  18643  -2189    846   2169       C  
ATOM   1695  C   LEU A1046      50.730   4.156  36.342  1.00134.52           C  
ANISOU 1695  C   LEU A1046    13116  18345  19652  -2860    993   2395       C  
ATOM   1696  O   LEU A1046      49.873   4.579  35.558  1.00138.35           O  
ANISOU 1696  O   LEU A1046    14165  18604  19797  -3036   1114   2555       O  
ATOM   1697  CB  LEU A1046      50.156   3.227  38.600  1.00114.87           C  
ANISOU 1697  CB  LEU A1046    10689  15684  17273  -2043    195   2081       C  
ATOM   1698  CG  LEU A1046      49.189   4.395  38.827  1.00103.62           C  
ANISOU 1698  CG  LEU A1046     9857  13838  15674  -2297   -138   2146       C  
ATOM   1699  CD1 LEU A1046      47.828   4.107  38.217  1.00 96.31           C  
ANISOU 1699  CD1 LEU A1046     9556  12698  14341  -2097     22   2183       C  
ATOM   1700  CD2 LEU A1046      49.056   4.722  40.308  1.00 99.47           C  
ANISOU 1700  CD2 LEU A1046     9379  13170  15245  -2171   -734   1980       C  
ATOM   1701  N   ASP A1047      51.893   4.784  36.529  1.00127.49           N  
ANISOU 1701  N   ASP A1047    11667  17635  19137  -3262    951   2433       N  
ATOM   1702  CA  ASP A1047      52.188   6.012  35.801  1.00131.96           C  
ANISOU 1702  CA  ASP A1047    12311  18112  19714  -3978   1078   2692       C  
ATOM   1703  C   ASP A1047      52.444   5.742  34.324  1.00130.92           C  
ANISOU 1703  C   ASP A1047    12130  18291  19323  -4228   1792   2837       C  
ATOM   1704  O   ASP A1047      52.172   6.607  33.483  1.00133.98           O  
ANISOU 1704  O   ASP A1047    12921  18510  19475  -4745   1927   3128       O  
ATOM   1705  CB  ASP A1047      53.382   6.723  36.435  1.00141.47           C  
ANISOU 1705  CB  ASP A1047    12895  19442  21416  -4390    835   2678       C  
ATOM   1706  CG  ASP A1047      53.050   7.320  37.791  1.00139.91           C  
ANISOU 1706  CG  ASP A1047    12900  18874  21385  -4305     95   2555       C  
ATOM   1707  OD1 ASP A1047      51.910   7.125  38.263  1.00133.93           O  
ANISOU 1707  OD1 ASP A1047    12719  17809  20359  -3898   -178   2466       O  
ATOM   1708  OD2 ASP A1047      53.925   7.988  38.382  1.00142.42           O  
ANISOU 1708  OD2 ASP A1047    12791  19231  22093  -4666   -203   2522       O  
ATOM   1709  N   LYS A1048      52.958   4.557  33.986  1.00136.15           N  
ANISOU 1709  N   LYS A1048    12332  19393  20008  -3866   2239   2634       N  
ATOM   1710  CA  LYS A1048      53.156   4.211  32.584  1.00137.23           C  
ANISOU 1710  CA  LYS A1048    12447  19868  19828  -4059   2961   2691       C  
ATOM   1711  C   LYS A1048      51.836   3.990  31.855  1.00136.24           C  
ANISOU 1711  C   LYS A1048    13159  19483  19123  -3907   3045   2785       C  
ATOM   1712  O   LYS A1048      51.813   4.012  30.619  1.00135.03           O  
ANISOU 1712  O   LYS A1048    13198  19529  18579  -4209   3556   2913       O  
ATOM   1713  CB  LYS A1048      54.036   2.964  32.467  1.00137.25           C  
ANISOU 1713  CB  LYS A1048    11720  20374  20055  -3634   3395   2361       C  
ATOM   1714  N   ALA A1049      50.743   3.782  32.587  1.00134.09           N  
ANISOU 1714  N   ALA A1049    13374  18806  18767  -3471   2557   2719       N  
ATOM   1715  CA  ALA A1049      49.423   3.607  31.993  1.00136.97           C  
ANISOU 1715  CA  ALA A1049    14488  18911  18642  -3319   2551   2790       C  
ATOM   1716  C   ALA A1049      48.555   4.853  32.093  1.00139.86           C  
ANISOU 1716  C   ALA A1049    15461  18785  18895  -3629   2088   3059       C  
ATOM   1717  O   ALA A1049      47.775   5.130  31.178  1.00144.34           O  
ANISOU 1717  O   ALA A1049    16587  19202  19054  -3792   2166   3254       O  
ATOM   1718  CB  ALA A1049      48.697   2.429  32.649  1.00134.83           C  
ANISOU 1718  CB  ALA A1049    14339  18543  18349  -2619   2376   2514       C  
ATOM   1719  N   ILE A1050      48.667   5.615  33.186  1.00147.00           N  
ANISOU 1719  N   ILE A1050    16279  19419  20157  -3696   1573   3052       N  
ATOM   1720  CA  ILE A1050      47.884   6.843  33.320  1.00137.76           C  
ANISOU 1720  CA  ILE A1050    15661  17727  18955  -3954   1109   3250       C  
ATOM   1721  C   ILE A1050      48.527   8.029  32.621  1.00135.31           C  
ANISOU 1721  C   ILE A1050    15376  17334  18700  -4696   1193   3602       C  
ATOM   1722  O   ILE A1050      47.861   9.054  32.425  1.00132.09           O  
ANISOU 1722  O   ILE A1050    15513  16449  18227  -4950    855   3834       O  
ATOM   1723  CB  ILE A1050      47.649   7.192  34.802  1.00112.75           C  
ANISOU 1723  CB  ILE A1050    12459  14272  16111  -3710    512   3036       C  
ATOM   1724  N   GLY A1051      49.800   7.923  32.236  1.00128.26           N  
ANISOU 1724  N   GLY A1051    13902  16884  17947  -5058   1630   3652       N  
ATOM   1725  CA  GLY A1051      50.479   8.964  31.501  1.00126.01           C  
ANISOU 1725  CA  GLY A1051    13606  16592  17681  -5844   1802   4017       C  
ATOM   1726  C   GLY A1051      51.114  10.046  32.350  1.00125.68           C  
ANISOU 1726  C   GLY A1051    13328  16279  18144  -6255   1362   4067       C  
ATOM   1727  O   GLY A1051      52.053  10.703  31.888  1.00131.62           O  
ANISOU 1727  O   GLY A1051    13814  17166  19028  -6906   1590   4283       O  
ATOM   1728  N   ARG A1052      50.638  10.250  33.572  1.00125.39           N  
ANISOU 1728  N   ARG A1052    13398  15875  18368  -5892    754   3830       N  
ATOM   1729  CA  ARG A1052      51.137  11.295  34.452  1.00130.48           C  
ANISOU 1729  CA  ARG A1052    13895  16207  19473  -6249    261   3810       C  
ATOM   1730  C   ARG A1052      51.879  10.681  35.633  1.00133.64           C  
ANISOU 1730  C   ARG A1052    13610  16936  20230  -5922     98   3432       C  
ATOM   1731  O   ARG A1052      51.880   9.465  35.836  1.00139.15           O  
ANISOU 1731  O   ARG A1052    14025  18014  20831  -5363    306   3204       O  
ATOM   1732  CB  ARG A1052      49.986  12.174  34.954  1.00127.22           C  
ANISOU 1732  CB  ARG A1052    14202  15072  19066  -6123   -369   3798       C  
ATOM   1733  CG  ARG A1052      49.063  11.466  35.933  1.00118.27           C  
ANISOU 1733  CG  ARG A1052    13210  13879  17849  -5343   -664   3404       C  
ATOM   1734  CD  ARG A1052      47.922  12.363  36.372  1.00115.96           C  
ANISOU 1734  CD  ARG A1052    13565  12916  17579  -5212  -1224   3339       C  
ATOM   1735  NE  ARG A1052      47.116  11.751  37.424  1.00114.03           N  
ANISOU 1735  NE  ARG A1052    13390  12676  17262  -4541  -1477   2931       N  
ATOM   1736  CZ  ARG A1052      47.303  11.960  38.723  1.00115.93           C  
ANISOU 1736  CZ  ARG A1052    13460  12852  17737  -4403  -1881   2594       C  
ATOM   1737  NH1 ARG A1052      48.271  12.768  39.132  1.00119.81           N  
ANISOU 1737  NH1 ARG A1052    13686  13244  18594  -4875  -2117   2592       N  
ATOM   1738  NH2 ARG A1052      46.523  11.364  39.613  1.00113.10           N  
ANISOU 1738  NH2 ARG A1052    13205  12544  17222  -3834  -2048   2259       N  
ATOM   1739  N   ASN A1053      52.517  11.551  36.419  1.00125.16           N  
ANISOU 1739  N   ASN A1053    12297  15678  19580  -6291   -324   3375       N  
ATOM   1740  CA  ASN A1053      53.118  11.156  37.692  1.00123.03           C  
ANISOU 1740  CA  ASN A1053    11481  15629  19636  -6002   -663   3022       C  
ATOM   1741  C   ASN A1053      52.002  11.117  38.731  1.00122.77           C  
ANISOU 1741  C   ASN A1053    11968  15217  19462  -5447  -1194   2750       C  
ATOM   1742  O   ASN A1053      51.786  12.056  39.502  1.00122.02           O  
ANISOU 1742  O   ASN A1053    12131  14690  19541  -5602  -1734   2626       O  
ATOM   1743  CB  ASN A1053      54.234  12.115  38.089  1.00126.67           C  
ANISOU 1743  CB  ASN A1053    11485  16063  20583  -6663   -923   3047       C  
ATOM   1744  N   THR A1054      51.272   9.995  38.739  1.00124.33           N  
ANISOU 1744  N   THR A1054    12319  15587  19333  -4804  -1013   2632       N  
ATOM   1745  CA  THR A1054      50.060   9.901  39.547  1.00119.55           C  
ANISOU 1745  CA  THR A1054    12244  14668  18513  -4306  -1394   2406       C  
ATOM   1746  C   THR A1054      50.366   9.947  41.037  1.00119.71           C  
ANISOU 1746  C   THR A1054    12048  14716  18720  -4133  -1918   2083       C  
ATOM   1747  O   THR A1054      49.504  10.334  41.835  1.00120.96           O  
ANISOU 1747  O   THR A1054    12645  14548  18764  -3922  -2315   1863       O  
ATOM   1748  CB  THR A1054      49.295   8.620  39.212  1.00115.03           C  
ANISOU 1748  CB  THR A1054    11827  14310  17568  -3728  -1059   2370       C  
ATOM   1749  N   ASN A1055      51.577   9.556  41.433  1.00118.97           N  
ANISOU 1749  N   ASN A1055    11271  15030  18901  -4213  -1934   2029       N  
ATOM   1750  CA  ASN A1055      52.004   9.557  42.830  1.00116.22           C  
ANISOU 1750  CA  ASN A1055    10681  14771  18707  -4084  -2473   1748       C  
ATOM   1751  C   ASN A1055      51.115   8.687  43.711  1.00119.38           C  
ANISOU 1751  C   ASN A1055    11395  15214  18750  -3437  -2650   1539       C  
ATOM   1752  O   ASN A1055      51.131   8.822  44.935  1.00121.96           O  
ANISOU 1752  O   ASN A1055    11754  15533  19052  -3324  -3143   1293       O  
ATOM   1753  CB  ASN A1055      52.071  10.984  43.391  1.00109.11           C  
ANISOU 1753  CB  ASN A1055     9992  13444  18023  -4552  -2980   1627       C  
ATOM   1754  N   GLY A1056      50.340   7.783  43.111  1.00115.78           N  
ANISOU 1754  N   GLY A1056    11183  14819  17987  -3045  -2253   1632       N  
ATOM   1755  CA  GLY A1056      49.518   6.838  43.832  1.00115.99           C  
ANISOU 1755  CA  GLY A1056    11480  14915  17677  -2485  -2341   1489       C  
ATOM   1756  C   GLY A1056      48.027   7.076  43.671  1.00112.88           C  
ANISOU 1756  C   GLY A1056    11762  14182  16944  -2317  -2293   1431       C  
ATOM   1757  O   GLY A1056      47.247   6.120  43.742  1.00109.86           O  
ANISOU 1757  O   GLY A1056    11592  13885  16264  -1902  -2132   1408       O  
ATOM   1758  N   VAL A1057      47.618   8.323  43.454  1.00113.85           N  
ANISOU 1758  N   VAL A1057    12208  13906  17145  -2632  -2448   1405       N  
ATOM   1759  CA  VAL A1057      46.211   8.699  43.361  1.00103.36           C  
ANISOU 1759  CA  VAL A1057    11467  12226  15579  -2456  -2483   1304       C  
ATOM   1760  C   VAL A1057      45.881   9.003  41.907  1.00105.21           C  
ANISOU 1760  C   VAL A1057    11904  12256  15814  -2653  -2149   1598       C  
ATOM   1761  O   VAL A1057      46.708   9.560  41.176  1.00111.08           O  
ANISOU 1761  O   VAL A1057    12459  12960  16785  -3103  -2041   1831       O  
ATOM   1762  CB  VAL A1057      45.900   9.912  44.260  1.00 96.42           C  
ANISOU 1762  CB  VAL A1057    10853  10979  14804  -2591  -2980   1005       C  
ATOM   1763  N   ILE A1058      44.667   8.639  41.488  1.00104.59           N  
ANISOU 1763  N   ILE A1058    12209  12071  15459  -2350  -1994   1597       N  
ATOM   1764  CA  ILE A1058      44.203   8.889  40.131  1.00100.91           C  
ANISOU 1764  CA  ILE A1058    12012  11414  14916  -2498  -1744   1872       C  
ATOM   1765  C   ILE A1058      42.794   9.466  40.170  1.00 98.60           C  
ANISOU 1765  C   ILE A1058    12224  10714  14524  -2295  -1978   1737       C  
ATOM   1766  O   ILE A1058      42.091   9.405  41.182  1.00 92.24           O  
ANISOU 1766  O   ILE A1058    11523   9875  13648  -1976  -2199   1403       O  
ATOM   1767  CB  ILE A1058      44.229   7.619  39.253  1.00 94.08           C  
ANISOU 1767  CB  ILE A1058    11024  10914  13808  -2321  -1243   2041       C  
ATOM   1768  CG1 ILE A1058      43.313   6.543  39.831  1.00 82.54           C  
ANISOU 1768  CG1 ILE A1058     9675   9599  12089  -1804  -1208   1830       C  
ATOM   1769  CG2 ILE A1058      45.650   7.101  39.083  1.00 91.55           C  
ANISOU 1769  CG2 ILE A1058    10149  10986  13649  -2498   -980   2147       C  
ATOM   1770  CD1 ILE A1058      43.175   5.325  38.950  1.00 80.94           C  
ANISOU 1770  CD1 ILE A1058     9440   9653  11661  -1618   -764   1951       C  
ATOM   1771  N   THR A1059      42.391  10.038  39.038  1.00100.27           N  
ANISOU 1771  N   THR A1059    12740  10636  14723  -2488  -1928   2000       N  
ATOM   1772  CA  THR A1059      41.046  10.571  38.887  1.00100.12           C  
ANISOU 1772  CA  THR A1059    13164  10218  14658  -2267  -2166   1907       C  
ATOM   1773  C   THR A1059      40.043   9.431  38.714  1.00 93.93           C  
ANISOU 1773  C   THR A1059    12445   9697  13549  -1832  -1928   1816       C  
ATOM   1774  O   THR A1059      40.390   8.322  38.302  1.00 93.12           O  
ANISOU 1774  O   THR A1059    12152   9988  13239  -1781  -1546   1935       O  
ATOM   1775  CB  THR A1059      40.982  11.515  37.681  1.00103.74           C  
ANISOU 1775  CB  THR A1059    13952  10269  15193  -2630  -2248   2286       C  
ATOM   1776  OG1 THR A1059      42.175  12.306  37.630  1.00105.14           O  
ANISOU 1776  OG1 THR A1059    13991  10320  15636  -3159  -2321   2476       O  
ATOM   1777  CG2 THR A1059      39.778  12.440  37.771  1.00108.32           C  
ANISOU 1777  CG2 THR A1059    14955  10292  15912  -2422  -2687   2144       C  
ATOM   1778  N   LYS A1060      38.780   9.709  39.047  1.00 98.18           N  
ANISOU 1778  N   LYS A1060    13229  10001  14072  -1515  -2161   1570       N  
ATOM   1779  CA  LYS A1060      37.721   8.768  38.697  1.00 98.24           C  
ANISOU 1779  CA  LYS A1060    13319  10201  13806  -1182  -1964   1522       C  
ATOM   1780  C   LYS A1060      37.594   8.635  37.188  1.00 99.60           C  
ANISOU 1780  C   LYS A1060    13688  10335  13819  -1346  -1790   1903       C  
ATOM   1781  O   LYS A1060      37.139   7.599  36.688  1.00 95.67           O  
ANISOU 1781  O   LYS A1060    13192  10106  13053  -1183  -1519   1935       O  
ATOM   1782  CB  LYS A1060      36.389   9.207  39.307  1.00 93.38           C  
ANISOU 1782  CB  LYS A1060    12863   9359  13257   -838  -2249   1162       C  
ATOM   1783  N   ASP A1061      37.997   9.671  36.449  1.00103.09           N  
ANISOU 1783  N   ASP A1061    14329  10441  14400  -1703  -1952   2200       N  
ATOM   1784  CA  ASP A1061      38.006   9.603  34.993  1.00101.97           C  
ANISOU 1784  CA  ASP A1061    14414  10301  14028  -1942  -1780   2607       C  
ATOM   1785  C   ASP A1061      39.176   8.768  34.485  1.00100.34           C  
ANISOU 1785  C   ASP A1061    13939  10555  13629  -2196  -1275   2797       C  
ATOM   1786  O   ASP A1061      39.012   7.961  33.563  1.00 99.43           O  
ANISOU 1786  O   ASP A1061    13894  10699  13185  -2180   -958   2926       O  
ATOM   1787  CB  ASP A1061      38.055  11.015  34.413  1.00102.76           C  
ANISOU 1787  CB  ASP A1061    14862   9863  14320  -2281  -2142   2907       C  
ATOM   1788  CG  ASP A1061      37.962  11.029  32.903  1.00102.52           C  
ANISOU 1788  CG  ASP A1061    15156   9822  13974  -2555  -2021   3367       C  
ATOM   1789  OD1 ASP A1061      36.881  10.700  32.371  1.00 98.49           O  
ANISOU 1789  OD1 ASP A1061    14872   9291  13258  -2289  -2114   3362       O  
ATOM   1790  OD2 ASP A1061      38.970  11.374  32.248  1.00105.90           O1+
ANISOU 1790  OD2 ASP A1061    15607  10290  14339  -3064  -1832   3728       O1+
ATOM   1791  N   GLU A1062      40.362   8.948  35.075  1.00102.50           N  
ANISOU 1791  N   GLU A1062    13880  10945  14119  -2420  -1205   2776       N  
ATOM   1792  CA  GLU A1062      41.504   8.118  34.707  1.00 96.62           C  
ANISOU 1792  CA  GLU A1062    12770  10671  13271  -2592   -725   2880       C  
ATOM   1793  C   GLU A1062      41.237   6.651  35.014  1.00 88.82           C  
ANISOU 1793  C   GLU A1062    11588  10061  12098  -2156   -455   2641       C  
ATOM   1794  O   GLU A1062      41.657   5.764  34.262  1.00 83.40           O  
ANISOU 1794  O   GLU A1062    10776   9705  11208  -2174    -28   2718       O  
ATOM   1795  CB  GLU A1062      42.761   8.595  35.435  1.00 87.02           C  
ANISOU 1795  CB  GLU A1062    11163   9509  12392  -2870   -785   2852       C  
ATOM   1796  CG  GLU A1062      43.240   9.972  35.025  1.00 95.42           C  
ANISOU 1796  CG  GLU A1062    12385  10212  13658  -3416   -988   3136       C  
ATOM   1797  CD  GLU A1062      44.494  10.395  35.768  1.00 99.73           C  
ANISOU 1797  CD  GLU A1062    12491  10838  14563  -3723  -1061   3077       C  
ATOM   1798  OE1 GLU A1062      44.628  10.042  36.959  1.00 95.17           O  
ANISOU 1798  OE1 GLU A1062    11645  10382  14135  -3431  -1231   2743       O  
ATOM   1799  OE2 GLU A1062      45.347  11.075  35.159  1.00104.48           O1+
ANISOU 1799  OE2 GLU A1062    13018  11399  15279  -4288   -958   3375       O1+
ATOM   1800  N   ALA A1063      40.542   6.377  36.121  1.00 85.45           N  
ANISOU 1800  N   ALA A1063    11151   9581  11735  -1777   -689   2337       N  
ATOM   1801  CA  ALA A1063      40.186   5.003  36.456  1.00 86.64           C  
ANISOU 1801  CA  ALA A1063    11186  10021  11712  -1400   -477   2151       C  
ATOM   1802  C   ALA A1063      39.112   4.459  35.526  1.00 88.99           C  
ANISOU 1802  C   ALA A1063    11790  10309  11715  -1259   -345   2190       C  
ATOM   1803  O   ALA A1063      39.030   3.242  35.325  1.00 88.77           O  
ANISOU 1803  O   ALA A1063    11692  10524  11512  -1068    -60   2120       O  
ATOM   1804  CB  ALA A1063      39.719   4.914  37.909  1.00 84.46           C  
ANISOU 1804  CB  ALA A1063    10850   9716  11524  -1112   -751   1850       C  
ATOM   1805  N   GLU A1064      38.283   5.337  34.957  1.00 91.39           N  
ANISOU 1805  N   GLU A1064    12438  10307  11980  -1346   -590   2294       N  
ATOM   1806  CA  GLU A1064      37.273   4.882  34.009  1.00 91.30           C  
ANISOU 1806  CA  GLU A1064    12709  10296  11686  -1243   -529   2345       C  
ATOM   1807  C   GLU A1064      37.898   4.478  32.678  1.00 95.38           C  
ANISOU 1807  C   GLU A1064    13297  11022  11922  -1504   -156   2596       C  
ATOM   1808  O   GLU A1064      37.402   3.560  32.016  1.00 93.85           O  
ANISOU 1808  O   GLU A1064    13219  10996  11445  -1384     47   2550       O  
ATOM   1809  CB  GLU A1064      36.216   5.969  33.805  1.00 88.36           C  
ANISOU 1809  CB  GLU A1064    12660   9522  11391  -1222   -972   2387       C  
ATOM   1810  CG  GLU A1064      34.995   5.506  33.022  1.00 85.95           C  
ANISOU 1810  CG  GLU A1064    12598   9220  10839  -1054  -1023   2379       C  
ATOM   1811  CD  GLU A1064      33.877   6.532  33.012  1.00 92.64           C  
ANISOU 1811  CD  GLU A1064    13676   9668  11857   -926  -1527   2353       C  
ATOM   1812  OE1 GLU A1064      32.798   6.224  32.460  1.00 92.14           O  
ANISOU 1812  OE1 GLU A1064    13758   9602  11649   -763  -1648   2318       O  
ATOM   1813  OE2 GLU A1064      34.072   7.641  33.555  1.00 96.90           O  
ANISOU 1813  OE2 GLU A1064    14234   9879  12704   -975  -1826   2343       O  
ATOM   1814  N   LYS A1065      38.982   5.144  32.270  1.00 96.04           N  
ANISOU 1814  N   LYS A1065    13309  11119  12064  -1890    -43   2837       N  
ATOM   1815  CA  LYS A1065      39.706   4.695  31.086  1.00 95.76           C  
ANISOU 1815  CA  LYS A1065    13269  11382  11732  -2158    412   3024       C  
ATOM   1816  C   LYS A1065      40.338   3.328  31.321  1.00 92.50           C  
ANISOU 1816  C   LYS A1065    12480  11360  11306  -1927    838   2784       C  
ATOM   1817  O   LYS A1065      40.296   2.460  30.442  1.00 93.15           O  
ANISOU 1817  O   LYS A1065    12640  11673  11077  -1892   1185   2745       O  
ATOM   1818  CB  LYS A1065      40.767   5.724  30.695  1.00 97.00           C  
ANISOU 1818  CB  LYS A1065    13372  11502  11982  -2673    474   3332       C  
ATOM   1819  N   LEU A1066      40.918   3.114  32.505  1.00 86.38           N  
ANISOU 1819  N   LEU A1066    11317  10638  10865  -1755    781   2609       N  
ATOM   1820  CA  LEU A1066      41.504   1.814  32.815  1.00 89.95           C  
ANISOU 1820  CA  LEU A1066    11422  11389  11367  -1482   1095   2400       C  
ATOM   1821  C   LEU A1066      40.439   0.729  32.871  1.00 88.33           C  
ANISOU 1821  C   LEU A1066    11426  11159  10977  -1113   1097   2208       C  
ATOM   1822  O   LEU A1066      40.672  -0.401  32.428  1.00 91.55           O  
ANISOU 1822  O   LEU A1066    11755  11759  11269   -957   1433   2085       O  
ATOM   1823  CB  LEU A1066      42.265   1.875  34.139  1.00 96.43           C  
ANISOU 1823  CB  LEU A1066    11833  12240  12567  -1373    917   2292       C  
ATOM   1824  CG  LEU A1066      43.442   2.845  34.220  1.00110.23           C  
ANISOU 1824  CG  LEU A1066    13274  14038  14572  -1754    899   2439       C  
ATOM   1825  CD1 LEU A1066      44.173   2.679  35.543  1.00109.37           C  
ANISOU 1825  CD1 LEU A1066    12741  14009  14807  -1592    693   2287       C  
ATOM   1826  CD2 LEU A1066      44.392   2.653  33.043  1.00117.21           C  
ANISOU 1826  CD2 LEU A1066    13951  15231  15353  -2035   1407   2560       C  
ATOM   1827  N   PHE A1067      39.266   1.055  33.417  1.00 88.20           N  
ANISOU 1827  N   PHE A1067    11656  10901  10956   -977    731   2152       N  
ATOM   1828  CA  PHE A1067      38.202   0.064  33.527  1.00 86.10           C  
ANISOU 1828  CA  PHE A1067    11554  10620  10539   -687    725   1975       C  
ATOM   1829  C   PHE A1067      37.743  -0.409  32.155  1.00 85.87           C  
ANISOU 1829  C   PHE A1067    11803  10657  10168   -762    941   2008       C  
ATOM   1830  O   PHE A1067      37.513  -1.606  31.949  1.00 84.89           O  
ANISOU 1830  O   PHE A1067    11703  10627   9925   -580   1146   1847       O  
ATOM   1831  CB  PHE A1067      37.028   0.640  34.316  1.00 89.23           C  
ANISOU 1831  CB  PHE A1067    12101  10796  11006   -569    323   1888       C  
ATOM   1832  CG  PHE A1067      35.849  -0.282  34.400  1.00 87.05           C  
ANISOU 1832  CG  PHE A1067    11964  10525  10586   -347    317   1719       C  
ATOM   1833  CD1 PHE A1067      35.865  -1.372  35.252  1.00 83.17           C  
ANISOU 1833  CD1 PHE A1067    11332  10130  10137   -136    418   1574       C  
ATOM   1834  CD2 PHE A1067      34.724  -0.058  33.627  1.00 86.11           C  
ANISOU 1834  CD2 PHE A1067    12115  10304  10299   -373    179   1726       C  
ATOM   1835  CE1 PHE A1067      34.781  -2.221  35.329  1.00 78.20           C  
ANISOU 1835  CE1 PHE A1067    10832   9493   9387     -3    424   1440       C  
ATOM   1836  CE2 PHE A1067      33.638  -0.903  33.702  1.00 81.95           C  
ANISOU 1836  CE2 PHE A1067    11664   9800   9671   -214    168   1558       C  
ATOM   1837  CZ  PHE A1067      33.666  -1.985  34.553  1.00 78.15           C  
ANISOU 1837  CZ  PHE A1067    11043   9414   9235    -52    312   1415       C  
ATOM   1838  N   ASN A1068      37.604   0.516  31.201  1.00 90.24           N  
ANISOU 1838  N   ASN A1068    12604  11140  10543  -1046    869   2222       N  
ATOM   1839  CA  ASN A1068      37.203   0.127  29.853  1.00 83.46           C  
ANISOU 1839  CA  ASN A1068    12053  10378   9278  -1159   1045   2269       C  
ATOM   1840  C   ASN A1068      38.222  -0.816  29.228  1.00 82.78           C  
ANISOU 1840  C   ASN A1068    11803  10602   9046  -1191   1575   2173       C  
ATOM   1841  O   ASN A1068      37.856  -1.728  28.479  1.00 84.94           O  
ANISOU 1841  O   ASN A1068    12255  10985   9033  -1118   1777   2024       O  
ATOM   1842  CB  ASN A1068      37.008   1.367  28.984  1.00 87.76           C  
ANISOU 1842  CB  ASN A1068    12920  10786   9638  -1498    837   2587       C  
ATOM   1843  CG  ASN A1068      35.631   1.982  29.145  1.00 95.27           C  
ANISOU 1843  CG  ASN A1068    14135  11430  10632  -1379    315   2609       C  
ATOM   1844  OD1 ASN A1068      34.845   2.027  28.198  1.00102.99           O  
ANISOU 1844  OD1 ASN A1068    15454  12372  11305  -1446    169   2702       O  
ATOM   1845  ND2 ASN A1068      35.327   2.448  30.350  1.00 94.72           N  
ANISOU 1845  ND2 ASN A1068    13890  11159  10939  -1190     20   2495       N  
ATOM   1846  N   GLN A1069      39.507  -0.618  29.532  1.00 82.90           N  
ANISOU 1846  N   GLN A1069    11450  10766   9281  -1289   1799   2217       N  
ATOM   1847  CA  GLN A1069      40.533  -1.532  29.041  1.00 93.96           C  
ANISOU 1847  CA  GLN A1069    12588  12479  10633  -1250   2317   2059       C  
ATOM   1848  C   GLN A1069      40.355  -2.926  29.631  1.00 96.67           C  
ANISOU 1848  C   GLN A1069    12801  12800  11129   -811   2383   1749       C  
ATOM   1849  O   GLN A1069      40.472  -3.931  28.918  1.00 96.30           O  
ANISOU 1849  O   GLN A1069    12800  12887  10901   -697   2721   1539       O  
ATOM   1850  CB  GLN A1069      41.922  -0.978  29.364  1.00104.31           C  
ANISOU 1850  CB  GLN A1069    13439  13961  12234  -1436   2488   2158       C  
ATOM   1851  CG  GLN A1069      42.191   0.399  28.770  1.00112.15           C  
ANISOU 1851  CG  GLN A1069    14573  14942  13096  -1947   2442   2503       C  
ATOM   1852  CD  GLN A1069      43.505   1.002  29.237  1.00116.78           C  
ANISOU 1852  CD  GLN A1069    14664  15667  14039  -2175   2548   2595       C  
ATOM   1853  OE1 GLN A1069      44.350   0.314  29.812  1.00124.86           O  
ANISOU 1853  OE1 GLN A1069    15191  16882  15370  -1946   2730   2385       O  
ATOM   1854  NE2 GLN A1069      43.681   2.297  28.993  1.00109.98           N  
ANISOU 1854  NE2 GLN A1069    13937  14684  13167  -2636   2395   2919       N  
ATOM   1855  N   ASP A1070      40.068  -3.007  30.934  1.00 93.20           N  
ANISOU 1855  N   ASP A1070    12231  12176  11004   -577   2056   1715       N  
ATOM   1856  CA  ASP A1070      39.831  -4.304  31.560  1.00 92.78           C  
ANISOU 1856  CA  ASP A1070    12121  12049  11083   -206   2064   1494       C  
ATOM   1857  C   ASP A1070      38.580  -4.968  31.000  1.00 84.10           C  
ANISOU 1857  C   ASP A1070    11427  10832   9697   -148   2030   1376       C  
ATOM   1858  O   ASP A1070      38.532  -6.195  30.858  1.00 74.28           O  
ANISOU 1858  O   ASP A1070    10218   9558   8448     64   2204   1167       O  
ATOM   1859  CB  ASP A1070      39.714  -4.145  33.076  1.00 97.16           C  
ANISOU 1859  CB  ASP A1070    12517  12464  11936    -46   1705   1529       C  
ATOM   1860  CG  ASP A1070      40.993  -3.637  33.711  1.00101.50           C  
ANISOU 1860  CG  ASP A1070    12635  13134  12794    -83   1688   1606       C  
ATOM   1861  OD1 ASP A1070      42.082  -3.940  33.181  1.00105.37           O  
ANISOU 1861  OD1 ASP A1070    12832  13826  13379    -89   2015   1558       O  
ATOM   1862  OD2 ASP A1070      40.905  -2.936  34.743  1.00 98.07           O1+
ANISOU 1862  OD2 ASP A1070    12136  12614  12514   -110   1349   1680       O1+
ATOM   1863  N   VAL A1071      37.557  -4.174  30.679  1.00 85.78           N  
ANISOU 1863  N   VAL A1071    11939  10950   9704   -328   1771   1495       N  
ATOM   1864  CA  VAL A1071      36.322  -4.733  30.136  1.00 82.23           C  
ANISOU 1864  CA  VAL A1071    11829  10413   9002   -301   1681   1379       C  
ATOM   1865  C   VAL A1071      36.565  -5.310  28.749  1.00 86.97           C  
ANISOU 1865  C   VAL A1071    12623  11169   9251   -401   2023   1266       C  
ATOM   1866  O   VAL A1071      36.169  -6.443  28.455  1.00 91.66           O  
ANISOU 1866  O   VAL A1071    13352  11723   9752   -267   2137   1029       O  
ATOM   1867  CB  VAL A1071      35.214  -3.667  30.113  1.00 77.64           C  
ANISOU 1867  CB  VAL A1071    11459   9702   8338   -435   1276   1525       C  
ATOM   1868  CG1 VAL A1071      34.018  -4.169  29.323  1.00 68.20           C  
ANISOU 1868  CG1 VAL A1071    10579   8473   6862   -455   1173   1415       C  
ATOM   1869  CG2 VAL A1071      34.807  -3.308  31.524  1.00 79.71           C  
ANISOU 1869  CG2 VAL A1071    11544   9829   8913   -289    982   1517       C  
ATOM   1870  N   ASP A1072      37.208  -4.533  27.872  1.00 86.89           N  
ANISOU 1870  N   ASP A1072    12656  11340   9019   -672   2197   1425       N  
ATOM   1871  CA  ASP A1072      37.548  -5.045  26.549  1.00 93.69           C  
ANISOU 1871  CA  ASP A1072    13699  12426   9474   -799   2587   1294       C  
ATOM   1872  C   ASP A1072      38.419  -6.289  26.649  1.00 93.29           C  
ANISOU 1872  C   ASP A1072    13380  12470   9598   -530   3002    969       C  
ATOM   1873  O   ASP A1072      38.186  -7.273  25.940  1.00100.45           O  
ANISOU 1873  O   ASP A1072    14485  13404  10277   -445   3208    683       O  
ATOM   1874  CB  ASP A1072      38.246  -3.964  25.724  1.00101.72           C  
ANISOU 1874  CB  ASP A1072    14764  13660  10224  -1186   2755   1563       C  
ATOM   1875  CG  ASP A1072      37.274  -2.951  25.152  1.00105.64           C  
ANISOU 1875  CG  ASP A1072    15691  14039  10407  -1457   2355   1858       C  
ATOM   1876  OD1 ASP A1072      36.104  -3.321  24.911  1.00105.43           O1+
ANISOU 1876  OD1 ASP A1072    15959  13888  10212  -1367   2080   1761       O1+
ATOM   1877  OD2 ASP A1072      37.677  -1.787  24.942  1.00108.66           O  
ANISOU 1877  OD2 ASP A1072    16112  14434  10740  -1764   2286   2192       O  
ATOM   1878  N   ALA A1073      39.417  -6.269  27.537  1.00 84.98           N  
ANISOU 1878  N   ALA A1073    11874  11440   8973   -376   3089    988       N  
ATOM   1879  CA  ALA A1073      40.250  -7.451  27.738  1.00 87.42           C  
ANISOU 1879  CA  ALA A1073    11887  11783   9546    -46   3401    685       C  
ATOM   1880  C   ALA A1073      39.418  -8.640  28.199  1.00 88.42           C  
ANISOU 1880  C   ALA A1073    12207  11603   9787    254   3220    480       C  
ATOM   1881  O   ALA A1073      39.645  -9.774  27.760  1.00 91.45           O  
ANISOU 1881  O   ALA A1073    12623  11947  10175    465   3482    159       O  
ATOM   1882  CB  ALA A1073      41.357  -7.149  28.747  1.00 88.38           C  
ANISOU 1882  CB  ALA A1073    11477  11958  10146     77   3385    785       C  
ATOM   1883  N   ALA A1074      38.441  -8.397  29.079  1.00 83.01           N  
ANISOU 1883  N   ALA A1074    11651  10689   9199    259   2785    645       N  
ATOM   1884  CA  ALA A1074      37.590  -9.476  29.567  1.00 85.44           C  
ANISOU 1884  CA  ALA A1074    12143  10714   9605    456   2615    500       C  
ATOM   1885  C   ALA A1074      36.749 -10.084  28.454  1.00 93.89           C  
ANISOU 1885  C   ALA A1074    13614  11749  10313    356   2695    279       C  
ATOM   1886  O   ALA A1074      36.388 -11.263  28.528  1.00 97.64           O  
ANISOU 1886  O   ALA A1074    14228  11998  10874    520   2705     57       O  
ATOM   1887  CB  ALA A1074      36.686  -8.968  30.689  1.00 78.28           C  
ANISOU 1887  CB  ALA A1074    11263   9662   8819    417   2191    709       C  
ATOM   1888  N   VAL A1075      36.430  -9.305  27.419  1.00 95.22           N  
ANISOU 1888  N   VAL A1075    13998  12114  10069     70   2718    348       N  
ATOM   1889  CA  VAL A1075      35.614  -9.821  26.325  1.00 92.66           C  
ANISOU 1889  CA  VAL A1075    14075  11790   9341    -54   2737    139       C  
ATOM   1890  C   VAL A1075      36.457 -10.646  25.357  1.00100.97           C  
ANISOU 1890  C   VAL A1075    15170  12983  10213     22   3217   -207       C  
ATOM   1891  O   VAL A1075      35.987 -11.658  24.824  1.00101.40           O  
ANISOU 1891  O   VAL A1075    15489  12912  10125     79   3272   -531       O  
ATOM   1892  CB  VAL A1075      34.888  -8.661  25.617  1.00 82.73           C  
ANISOU 1892  CB  VAL A1075    13071  10672   7689   -380   2491    377       C  
ATOM   1893  CG1 VAL A1075      34.069  -9.171  24.446  1.00 75.94           C  
ANISOU 1893  CG1 VAL A1075    12635   9852   6368   -528   2457    166       C  
ATOM   1894  CG2 VAL A1075      33.993  -7.930  26.604  1.00 76.88           C  
ANISOU 1894  CG2 VAL A1075    12256   9765   7192   -384   2023    620       C  
ATOM   1895  N   ARG A1076      37.712 -10.240  25.115  1.00100.09           N  
ANISOU 1895  N   ARG A1076    14776  13139  10116     17   3583   -182       N  
ATOM   1896  CA  ARG A1076      38.592 -11.049  24.273  1.00106.02           C  
ANISOU 1896  CA  ARG A1076    15475  14062  10744    139   4103   -579       C  
ATOM   1897  C   ARG A1076      38.740 -12.458  24.828  1.00110.21           C  
ANISOU 1897  C   ARG A1076    15911  14258  11706    564   4141   -922       C  
ATOM   1898  O   ARG A1076      38.867 -13.421  24.062  1.00118.72           O  
ANISOU 1898  O   ARG A1076    17153  15310  12647    690   4425  -1359       O  
ATOM   1899  CB  ARG A1076      39.980 -10.411  24.143  1.00109.75           C  
ANISOU 1899  CB  ARG A1076    15519  14893  11289     84   4503   -500       C  
ATOM   1900  CG  ARG A1076      40.027  -8.904  24.227  1.00109.02           C  
ANISOU 1900  CG  ARG A1076    15378  14979  11066   -286   4338    -22       C  
ATOM   1901  CD  ARG A1076      39.706  -8.229  22.910  1.00113.54           C  
ANISOU 1901  CD  ARG A1076    16360  15831  10947   -724   4457     91       C  
ATOM   1902  NE  ARG A1076      39.657  -6.778  23.063  1.00113.48           N  
ANISOU 1902  NE  ARG A1076    16365  15872  10879  -1069   4203    591       N  
ATOM   1903  CZ  ARG A1076      39.507  -5.923  22.058  1.00114.12           C  
ANISOU 1903  CZ  ARG A1076    16787  16166  10409  -1503   4233    842       C  
ATOM   1904  NH1 ARG A1076      39.395  -6.367  20.812  1.00118.70           N1+
ANISOU 1904  NH1 ARG A1076    17722  16997  10383  -1663   4528    629       N1+
ATOM   1905  NH2 ARG A1076      39.471  -4.619  22.301  1.00110.17           N  
ANISOU 1905  NH2 ARG A1076    16305  15605   9949  -1786   3945   1307       N  
ATOM   1906  N   GLY A1077      38.727 -12.597  26.152  1.00104.33           N  
ANISOU 1906  N   GLY A1077    14938  13235  11468    780   3843   -732       N  
ATOM   1907  CA  GLY A1077      38.862 -13.893  26.781  1.00103.24           C  
ANISOU 1907  CA  GLY A1077    14749  12715  11761   1164   3801   -960       C  
ATOM   1908  C   GLY A1077      37.555 -14.652  26.832  1.00100.52           C  
ANISOU 1908  C   GLY A1077    14844  12012  11338   1106   3509  -1046       C  
ATOM   1909  O   GLY A1077      37.538 -15.875  26.663  1.00104.59           O  
ANISOU 1909  O   GLY A1077    15516  12220  12003   1321   3586  -1382       O  
ATOM   1910  N   ILE A1078      36.453 -13.936  27.070  1.00 99.32           N  
ANISOU 1910  N   ILE A1078    14869  11880  10988    814   3165   -762       N  
ATOM   1911  CA  ILE A1078      35.138 -14.573  27.087  1.00 95.36           C  
ANISOU 1911  CA  ILE A1078    14721  11103  10410    692   2887   -841       C  
ATOM   1912  C   ILE A1078      34.872 -15.266  25.758  1.00 94.23           C  
ANISOU 1912  C   ILE A1078    14931  10962   9909    611   3076  -1259       C  
ATOM   1913  O   ILE A1078      34.461 -16.432  25.713  1.00 91.07           O  
ANISOU 1913  O   ILE A1078    14757  10213   9633    693   3032  -1537       O  
ATOM   1914  CB  ILE A1078      34.042 -13.542  27.412  1.00 93.90           C  
ANISOU 1914  CB  ILE A1078    14585  11030  10063    404   2522   -518       C  
ATOM   1915  CG1 ILE A1078      33.993 -13.263  28.917  1.00 93.60           C  
ANISOU 1915  CG1 ILE A1078    14291  10873  10400    497   2289   -213       C  
ATOM   1916  CG2 ILE A1078      32.692 -14.024  26.911  1.00 91.88           C  
ANISOU 1916  CG2 ILE A1078    14674  10646   9590    192   2300   -673       C  
ATOM   1917  CD1 ILE A1078      33.002 -12.183  29.313  1.00 86.14           C  
ANISOU 1917  CD1 ILE A1078    13326  10053   9351    273   1966     41       C  
ATOM   1918  N   LEU A1079      35.121 -14.560  24.654  1.00 96.21           N  
ANISOU 1918  N   LEU A1079    15266  11598   9690    421   3283  -1311       N  
ATOM   1919  CA  LEU A1079      34.910 -15.148  23.339  1.00 99.06           C  
ANISOU 1919  CA  LEU A1079    15997  12035   9608    315   3475  -1730       C  
ATOM   1920  C   LEU A1079      35.911 -16.261  23.058  1.00104.43           C  
ANISOU 1920  C   LEU A1079    16609  12586  10483    653   3898  -2204       C  
ATOM   1921  O   LEU A1079      35.576 -17.237  22.375  1.00107.18           O  
ANISOU 1921  O   LEU A1079    17287  12752  10686    675   3966  -2650       O  
ATOM   1922  CB  LEU A1079      34.990 -14.061  22.271  1.00 97.08           C  
ANISOU 1922  CB  LEU A1079    15879  12261   8747     -2   3592  -1606       C  
ATOM   1923  CG  LEU A1079      34.022 -12.896  22.494  1.00 92.62           C  
ANISOU 1923  CG  LEU A1079    15381  11775   8035   -286   3126  -1146       C  
ATOM   1924  CD1 LEU A1079      34.208 -11.832  21.427  1.00 87.85           C  
ANISOU 1924  CD1 LEU A1079    14956  11583   6838   -599   3216   -967       C  
ATOM   1925  CD2 LEU A1079      32.586 -13.395  22.521  1.00 89.61           C  
ANISOU 1925  CD2 LEU A1079    15271  11148   7628   -399   2691  -1233       C  
ATOM   1926  N   ARG A1080      37.134 -16.141  23.574  1.00102.78           N  
ANISOU 1926  N   ARG A1080    15961  12455  10635    932   4161  -2150       N  
ATOM   1927  CA  ARG A1080      38.113 -17.215  23.463  1.00106.42           C  
ANISOU 1927  CA  ARG A1080    16265  12749  11422   1346   4516  -2607       C  
ATOM   1928  C   ARG A1080      37.864 -18.345  24.454  1.00114.00           C  
ANISOU 1928  C   ARG A1080    17260  13084  12971   1658   4225  -2653       C  
ATOM   1929  O   ARG A1080      38.585 -19.348  24.417  1.00121.35           O  
ANISOU 1929  O   ARG A1080    18104  13749  14255   2055   4430  -3041       O  
ATOM   1930  CB  ARG A1080      39.528 -16.662  23.652  1.00 95.46           C  
ANISOU 1930  CB  ARG A1080    14320  11699  10249   1534   4874  -2535       C  
ATOM   1931  N   ASN A1081      36.877 -18.203  25.339  1.00113.30           N  
ANISOU 1931  N   ASN A1081    17292  12754  13003   1487   3760  -2268       N  
ATOM   1932  CA  ASN A1081      36.488 -19.263  26.264  1.00110.82           C  
ANISOU 1932  CA  ASN A1081    17098  11850  13160   1666   3466  -2242       C  
ATOM   1933  C   ASN A1081      35.348 -20.052  25.630  1.00107.85           C  
ANISOU 1933  C   ASN A1081    17225  11189  12565   1437   3324  -2533       C  
ATOM   1934  O   ASN A1081      34.255 -19.516  25.418  1.00 96.74           O  
ANISOU 1934  O   ASN A1081    16004   9943  10809   1044   3098  -2372       O  
ATOM   1935  CB  ASN A1081      36.075 -18.682  27.614  1.00104.89           C  
ANISOU 1935  CB  ASN A1081    16179  11052  12621   1564   3094  -1681       C  
ATOM   1936  CG  ASN A1081      35.935 -19.745  28.696  1.00100.82           C  
ANISOU 1936  CG  ASN A1081    15751   9964  12593   1757   2830  -1573       C  
ATOM   1937  OD1 ASN A1081      35.536 -20.881  28.430  1.00 96.54           O  
ANISOU 1937  OD1 ASN A1081    15540   8975  12166   1793   2783  -1851       O  
ATOM   1938  ND2 ASN A1081      36.265 -19.375  29.927  1.00 99.41           N  
ANISOU 1938  ND2 ASN A1081    15308   9782  12683   1855   2634  -1158       N  
ATOM   1939  N   ALA A1082      35.603 -21.330  25.335  1.00104.72           N  
ANISOU 1939  N   ALA A1082    17030  10346  12412   1693   3425  -2982       N  
ATOM   1940  CA  ALA A1082      34.620 -22.148  24.633  1.00104.56           C  
ANISOU 1940  CA  ALA A1082    17500  10033  12195   1466   3305  -3342       C  
ATOM   1941  C   ALA A1082      33.348 -22.360  25.442  1.00101.54           C  
ANISOU 1941  C   ALA A1082    17302   9334  11945   1142   2845  -3001       C  
ATOM   1942  O   ALA A1082      32.300 -22.654  24.856  1.00101.98           O  
ANISOU 1942  O   ALA A1082    17693   9314  11739    801   2679  -3190       O  
ATOM   1943  CB  ALA A1082      35.231 -23.499  24.264  1.00107.82           C  
ANISOU 1943  CB  ALA A1082    18086   9944  12935   1850   3489  -3914       C  
ATOM   1944  N   LYS A1083      33.409 -22.219  26.764  1.00105.02           N  
ANISOU 1944  N   LYS A1083    17519   9623  12760   1215   2642  -2520       N  
ATOM   1945  CA  LYS A1083      32.243 -22.435  27.607  1.00 99.72           C  
ANISOU 1945  CA  LYS A1083    16986   8701  12202    885   2273  -2194       C  
ATOM   1946  C   LYS A1083      31.446 -21.163  27.871  1.00 97.98           C  
ANISOU 1946  C   LYS A1083    16574   8985  11668    541   2119  -1821       C  
ATOM   1947  O   LYS A1083      30.317 -21.253  28.366  1.00 96.09           O  
ANISOU 1947  O   LYS A1083    16414   8652  11442    209   1857  -1636       O  
ATOM   1948  CB  LYS A1083      32.666 -23.061  28.941  1.00 98.15           C  
ANISOU 1948  CB  LYS A1083    16717   8046  12528   1114   2120  -1873       C  
ATOM   1949  N   LEU A1084      31.992 -19.986  27.551  1.00 99.46           N  
ANISOU 1949  N   LEU A1084    16502   9689  11600    605   2275  -1719       N  
ATOM   1950  CA  LEU A1084      31.288 -18.729  27.771  1.00 97.55           C  
ANISOU 1950  CA  LEU A1084    16090   9867  11109    333   2100  -1390       C  
ATOM   1951  C   LEU A1084      30.919 -17.993  26.491  1.00101.44           C  
ANISOU 1951  C   LEU A1084    16699  10753  11090    121   2131  -1554       C  
ATOM   1952  O   LEU A1084      30.009 -17.161  26.521  1.00102.09           O  
ANISOU 1952  O   LEU A1084    16730  11072  10987   -136   1884  -1351       O  
ATOM   1953  CB  LEU A1084      32.124 -17.790  28.654  1.00 93.67           C  
ANISOU 1953  CB  LEU A1084    15216   9609  10766    522   2147  -1024       C  
ATOM   1954  CG  LEU A1084      32.376 -18.250  30.092  1.00 99.39           C  
ANISOU 1954  CG  LEU A1084    15814  10040  11911    678   2020   -744       C  
ATOM   1955  CD1 LEU A1084      33.068 -17.160  30.896  1.00100.96           C  
ANISOU 1955  CD1 LEU A1084    15645  10540  12174    797   2010   -411       C  
ATOM   1956  CD2 LEU A1084      31.075 -18.668  30.757  1.00 98.30           C  
ANISOU 1956  CD2 LEU A1084    15830   9700  11820    371   1756   -602       C  
ATOM   1957  N   LYS A1085      31.598 -18.269  25.378  1.00102.45           N  
ANISOU 1957  N   LYS A1085    16983  10965  10978    227   2417  -1917       N  
ATOM   1958  CA  LYS A1085      31.262 -17.597  24.126  1.00 99.55           C  
ANISOU 1958  CA  LYS A1085    16799  10990  10037    -13   2431  -2041       C  
ATOM   1959  C   LYS A1085      29.850 -17.899  23.627  1.00 99.81           C  
ANISOU 1959  C   LYS A1085    17128  10950   9847   -354   2083  -2182       C  
ATOM   1960  O   LYS A1085      29.193 -16.966  23.138  1.00 92.79           O  
ANISOU 1960  O   LYS A1085    16268  10388   8598   -594   1861  -2023       O  
ATOM   1961  CB  LYS A1085      32.301 -17.947  23.053  1.00 96.22           C  
ANISOU 1961  CB  LYS A1085    16501  10703   9355    149   2870  -2453       C  
ATOM   1962  N   PRO A1086      29.335 -19.137  23.693  1.00105.32           N  
ANISOU 1962  N   PRO A1086    18044  11220  10751   -402   1987  -2468       N  
ATOM   1963  CA  PRO A1086      27.961 -19.366  23.201  1.00106.72           C  
ANISOU 1963  CA  PRO A1086    18449  11373  10729   -778   1625  -2606       C  
ATOM   1964  C   PRO A1086      26.904 -18.527  23.902  1.00101.72           C  
ANISOU 1964  C   PRO A1086    17551  10915  10184  -1000   1260  -2201       C  
ATOM   1965  O   PRO A1086      26.130 -17.830  23.232  1.00 97.88           O  
ANISOU 1965  O   PRO A1086    17104  10733   9353  -1226    992  -2175       O  
ATOM   1966  CB  PRO A1086      27.759 -20.868  23.445  1.00108.18           C  
ANISOU 1966  CB  PRO A1086    18857  10979  11267   -780   1611  -2917       C  
ATOM   1967  CG  PRO A1086      29.125 -21.438  23.364  1.00108.60           C  
ANISOU 1967  CG  PRO A1086    18951  10834  11479   -369   2012  -3150       C  
ATOM   1968  CD  PRO A1086      30.018 -20.411  23.991  1.00103.81           C  
ANISOU 1968  CD  PRO A1086    17951  10542  10950   -127   2192  -2744       C  
ATOM   1969  N   VAL A1087      26.844 -18.575  25.235  1.00 98.45           N  
ANISOU 1969  N   VAL A1087    16867  10324  10214   -932   1231  -1899       N  
ATOM   1970  CA  VAL A1087      25.825 -17.817  25.956  1.00 96.16           C  
ANISOU 1970  CA  VAL A1087    16290  10223  10024  -1125    937  -1588       C  
ATOM   1971  C   VAL A1087      26.024 -16.321  25.749  1.00 94.05           C  
ANISOU 1971  C   VAL A1087    15830  10386   9517  -1049    881  -1337       C  
ATOM   1972  O   VAL A1087      25.055 -15.564  25.617  1.00 93.16           O  
ANISOU 1972  O   VAL A1087    15592  10501   9302  -1221    565  -1236       O  
ATOM   1973  CB  VAL A1087      25.834 -18.196  27.449  1.00 97.74           C  
ANISOU 1973  CB  VAL A1087    16281  10182  10673  -1078    978  -1328       C  
ATOM   1974  CG1 VAL A1087      27.238 -18.088  28.024  1.00102.40           C  
ANISOU 1974  CG1 VAL A1087    16780  10706  11420   -706   1259  -1166       C  
ATOM   1975  CG2 VAL A1087      24.863 -17.323  28.230  1.00 89.97           C  
ANISOU 1975  CG2 VAL A1087    14954   9465   9765  -1245    754  -1058       C  
ATOM   1976  N   TYR A1088      27.284 -15.876  25.692  1.00 89.69           N  
ANISOU 1976  N   TYR A1088    15242   9934   8902   -793   1168  -1242       N  
ATOM   1977  CA  TYR A1088      27.580 -14.457  25.515  1.00 90.57           C  
ANISOU 1977  CA  TYR A1088    15204  10393   8813   -755   1125   -975       C  
ATOM   1978  C   TYR A1088      26.959 -13.916  24.234  1.00 95.61           C  
ANISOU 1978  C   TYR A1088    16073  11277   8976   -968    892  -1053       C  
ATOM   1979  O   TYR A1088      26.470 -12.781  24.202  1.00 93.98           O  
ANISOU 1979  O   TYR A1088    15753  11275   8682  -1035    611   -805       O  
ATOM   1980  CB  TYR A1088      29.095 -14.250  25.512  1.00 93.94           C  
ANISOU 1980  CB  TYR A1088    15566  10885   9242   -509   1510   -919       C  
ATOM   1981  CG  TYR A1088      29.544 -12.810  25.574  1.00 98.44           C  
ANISOU 1981  CG  TYR A1088    15953  11742   9710   -493   1488   -591       C  
ATOM   1982  CD1 TYR A1088      29.740 -12.178  26.794  1.00 98.86           C  
ANISOU 1982  CD1 TYR A1088    15682  11781  10099   -378   1424   -304       C  
ATOM   1983  CD2 TYR A1088      29.792 -12.088  24.415  1.00103.73           C  
ANISOU 1983  CD2 TYR A1088    16808  12681   9923   -622   1523   -565       C  
ATOM   1984  CE1 TYR A1088      30.162 -10.863  26.860  1.00 99.84           C  
ANISOU 1984  CE1 TYR A1088    15661  12107  10167   -380   1378    -29       C  
ATOM   1985  CE2 TYR A1088      30.213 -10.771  24.470  1.00106.12           C  
ANISOU 1985  CE2 TYR A1088    16981  13181  10158   -650   1482   -232       C  
ATOM   1986  CZ  TYR A1088      30.395 -10.164  25.696  1.00103.83           C  
ANISOU 1986  CZ  TYR A1088    16357  12826  10268   -522   1402     20       C  
ATOM   1987  OH  TYR A1088      30.810  -8.854  25.759  1.00103.35           O  
ANISOU 1987  OH  TYR A1088    16189  12904  10176   -568   1333    326       O  
ATOM   1988  N   ASP A1089      26.969 -14.714  23.164  1.00102.12           N  
ANISOU 1988  N   ASP A1089    17248  12069   9485  -1067    973  -1406       N  
ATOM   1989  CA  ASP A1089      26.320 -14.293  21.927  1.00102.51           C  
ANISOU 1989  CA  ASP A1089    17573  12361   9018  -1301    696  -1486       C  
ATOM   1990  C   ASP A1089      24.810 -14.185  22.110  1.00 97.68           C  
ANISOU 1990  C   ASP A1089    16847  11734   8531  -1503    175  -1453       C  
ATOM   1991  O   ASP A1089      24.193 -13.208  21.669  1.00 94.27           O  
ANISOU 1991  O   ASP A1089    16405  11528   7886  -1603   -198  -1266       O  
ATOM   1992  CB  ASP A1089      26.658 -15.270  20.798  1.00107.75           C  
ANISOU 1992  CB  ASP A1089    18652  12996   9292  -1371    911  -1943       C  
ATOM   1993  CG  ASP A1089      28.153 -15.360  20.522  1.00109.36           C  
ANISOU 1993  CG  ASP A1089    18906  13282   9365  -1158   1468  -2039       C  
ATOM   1994  OD1 ASP A1089      28.859 -14.349  20.724  1.00107.83           O  
ANISOU 1994  OD1 ASP A1089    18522  13306   9142  -1077   1610  -1702       O  
ATOM   1995  OD2 ASP A1089      28.623 -16.442  20.104  1.00108.54           O1+
ANISOU 1995  OD2 ASP A1089    19006  13016   9217  -1074   1762  -2478       O1+
ATOM   1996  N   SER A1090      24.200 -15.124  22.768  1.00 95.52           N  
ANISOU 1996  N   SER A1090    16469  11190   8635  -1571    131  -1622       N  
ATOM   1997  CA  SER A1090      22.775 -15.087  22.914  1.00100.79           C  
ANISOU 1997  CA  SER A1090    16964  11869   9463  -1805   -311  -1652       C  
ATOM   1998  C   SER A1090      22.220 -13.982  23.739  1.00102.57           C  
ANISOU 1998  C   SER A1090    16755  12269   9949  -1733   -541  -1311       C  
ATOM   1999  O   SER A1090      21.034 -13.763  23.747  1.00106.04           O  
ANISOU 1999  O   SER A1090    16983  12810  10497  -1894   -938  -1340       O  
ATOM   2000  CB  SER A1090      22.377 -16.406  23.588  1.00 99.01           C  
ANISOU 2000  CB  SER A1090    16709  11296   9615  -1937   -227  -1860       C  
ATOM   2001  OG  SER A1090      21.208 -16.357  24.395  1.00 95.53           O  
ANISOU 2001  OG  SER A1090    15874  10901   9522  -2092   -478  -1730       O  
ATOM   2002  N   LEU A1091      23.062 -13.325  24.481  1.00 99.87           N  
ANISOU 2002  N   LEU A1091    16250  11965   9730  -1492   -315  -1031       N  
ATOM   2003  CA  LEU A1091      22.607 -12.416  25.517  1.00 95.87           C  
ANISOU 2003  CA  LEU A1091    15324  11551   9550  -1398   -463   -783       C  
ATOM   2004  C   LEU A1091      22.327 -11.026  24.968  1.00 97.76           C  
ANISOU 2004  C   LEU A1091    15525  12007   9612  -1342   -816   -587       C  
ATOM   2005  O   LEU A1091      23.032 -10.535  24.083  1.00 95.64           O  
ANISOU 2005  O   LEU A1091    15549  11818   8971  -1317   -786   -485       O  
ATOM   2006  CB  LEU A1091      23.641 -12.333  26.638  1.00 87.84           C  
ANISOU 2006  CB  LEU A1091    14159  10436   8780  -1181    -92   -597       C  
ATOM   2007  CG  LEU A1091      23.680 -13.560  27.542  1.00 82.06           C  
ANISOU 2007  CG  LEU A1091    13386   9458   8336  -1224    143   -690       C  
ATOM   2008  CD1 LEU A1091      24.786 -13.425  28.573  1.00 80.82           C  
ANISOU 2008  CD1 LEU A1091    13114   9224   8371   -989    440   -482       C  
ATOM   2009  CD2 LEU A1091      22.327 -13.769  28.206  1.00 80.36           C  
ANISOU 2009  CD2 LEU A1091    12890   9277   8367  -1435    -70   -736       C  
ATOM   2010  N   ASP A1092      21.376 -10.343  25.562  1.00 96.05           N  
ANISOU 2010  N   ASP A1092    14944  11880   9672  -1329  -1151   -538       N  
ATOM   2011  CA  ASP A1092      21.052  -8.988  25.248  1.00 94.58           C  
ANISOU 2011  CA  ASP A1092    14656  11809   9469  -1194  -1512   -321       C  
ATOM   2012  C   ASP A1092      22.222  -8.197  25.771  1.00 90.97           C  
ANISOU 2012  C   ASP A1092    14182  11304   9080   -989  -1249    -61       C  
ATOM   2013  O   ASP A1092      22.961  -8.670  26.567  1.00 94.84           O  
ANISOU 2013  O   ASP A1092    14566  11715   9754   -916   -857    -59       O  
ATOM   2014  CB  ASP A1092      19.780  -8.669  26.007  1.00101.30           C  
ANISOU 2014  CB  ASP A1092    15029  12751  10711  -1166  -1868   -406       C  
ATOM   2015  CG  ASP A1092      19.607  -7.210  26.318  1.00111.33           C  
ANISOU 2015  CG  ASP A1092    16080  14045  12176   -914  -2131   -205       C  
ATOM   2016  OD1 ASP A1092      20.277  -6.361  25.708  1.00117.45           O  
ANISOU 2016  OD1 ASP A1092    17125  14798  12702   -861  -2417     -1       O  
ATOM   2017  OD2 ASP A1092      18.756  -6.904  27.171  1.00112.11           O  
ANISOU 2017  OD2 ASP A1092    15757  14174  12666   -784  -2057   -258       O  
ATOM   2018  N   ALA A1093      22.381  -6.966  25.331  1.00 96.88           N  
ANISOU 2018  N   ALA A1093    15054  12081   9674   -916  -1505    178       N  
ATOM   2019  CA  ALA A1093      23.488  -6.122  25.778  1.00 91.46           C  
ANISOU 2019  CA  ALA A1093    14374  11336   9042   -782  -1292    431       C  
ATOM   2020  C   ALA A1093      23.421  -5.832  27.272  1.00 93.10           C  
ANISOU 2020  C   ALA A1093    14165  11492   9718   -603  -1188    414       C  
ATOM   2021  O   ALA A1093      24.464  -5.712  27.927  1.00 87.73           O  
ANISOU 2021  O   ALA A1093    13451  10765   9118   -524   -866    519       O  
ATOM   2022  CB  ALA A1093      23.503  -4.814  24.988  1.00 88.70           C  
ANISOU 2022  CB  ALA A1093    14227  10970   8505   -779  -1676    717       C  
ATOM   2023  N   VAL A1094      22.214  -5.720  27.829  1.00 97.94           N  
ANISOU 2023  N   VAL A1094    14439  12147  10627   -546  -1450    262       N  
ATOM   2024  CA  VAL A1094      22.076  -5.445  29.257  1.00 93.00           C  
ANISOU 2024  CA  VAL A1094    13427  11531  10378   -399  -1324    200       C  
ATOM   2025  C   VAL A1094      22.441  -6.680  30.072  1.00 88.59           C  
ANISOU 2025  C   VAL A1094    12819  10982   9860   -491   -879     98       C  
ATOM   2026  O   VAL A1094      23.204  -6.601  31.041  1.00 83.02           O  
ANISOU 2026  O   VAL A1094    12036  10247   9261   -400   -616    175       O  
ATOM   2027  CB  VAL A1094      20.652  -4.956  29.576  1.00 91.34           C  
ANISOU 2027  CB  VAL A1094    12822  11413  10469   -310  -1694     21       C  
ATOM   2028  CG1 VAL A1094      20.546  -4.549  31.038  1.00 87.18           C  
ANISOU 2028  CG1 VAL A1094    11914  10940  10271   -155  -1529    -81       C  
ATOM   2029  CG2 VAL A1094      20.261  -3.802  28.656  1.00 92.19           C  
ANISOU 2029  CG2 VAL A1094    13027  11445  10557   -192  -2230    148       C  
ATOM   2030  N   ARG A1095      21.898  -7.840  29.694  1.00 90.63           N  
ANISOU 2030  N   ARG A1095    13144  11253  10038   -685   -833    -66       N  
ATOM   2031  CA  ARG A1095      22.284  -9.087  30.344  1.00 90.96           C  
ANISOU 2031  CA  ARG A1095    13231  11214  10116   -790   -456   -122       C  
ATOM   2032  C   ARG A1095      23.746  -9.427  30.091  1.00 87.34           C  
ANISOU 2032  C   ARG A1095    13078  10619   9487   -715   -154      0       C  
ATOM   2033  O   ARG A1095      24.354 -10.144  30.893  1.00 79.42           O  
ANISOU 2033  O   ARG A1095    12074   9515   8587   -689    132     31       O  
ATOM   2034  CB  ARG A1095      21.389 -10.229  29.864  1.00 87.99           C  
ANISOU 2034  CB  ARG A1095    12907  10817   9709  -1046   -517   -333       C  
ATOM   2035  CG  ARG A1095      19.913  -9.890  29.887  1.00 88.08           C  
ANISOU 2035  CG  ARG A1095    12562  11010   9896  -1139   -853   -486       C  
ATOM   2036  CD  ARG A1095      19.099 -10.979  29.236  1.00 93.06           C  
ANISOU 2036  CD  ARG A1095    13265  11616  10479  -1439   -963   -697       C  
ATOM   2037  NE  ARG A1095      17.793 -10.502  28.791  1.00103.22           N  
ANISOU 2037  NE  ARG A1095    14244  13099  11877  -1501  -1404   -846       N  
ATOM   2038  CZ  ARG A1095      16.679 -10.583  29.511  1.00102.98           C  
ANISOU 2038  CZ  ARG A1095    13724  13246  12157  -1620  -1455   -997       C  
ATOM   2039  NH1 ARG A1095      16.705 -11.126  30.720  1.00101.20           N1+
ANISOU 2039  NH1 ARG A1095    13324  13034  12095  -1735  -1072   -988       N1+
ATOM   2040  NH2 ARG A1095      15.535 -10.122  29.020  1.00102.93           N  
ANISOU 2040  NH2 ARG A1095    13394  13427  12289  -1634  -1897  -1154       N  
ATOM   2041  N   ARG A1096      24.321  -8.920  29.001  1.00 90.45           N  
ANISOU 2041  N   ARG A1096    13718  11024   9623   -685   -218     78       N  
ATOM   2042  CA  ARG A1096      25.730  -9.168  28.728  1.00 86.04           C  
ANISOU 2042  CA  ARG A1096    13368  10402   8921   -614    110    159       C  
ATOM   2043  C   ARG A1096      26.623  -8.481  29.750  1.00 81.52           C  
ANISOU 2043  C   ARG A1096    12598   9829   8548   -445    250    350       C  
ATOM   2044  O   ARG A1096      27.697  -8.997  30.076  1.00 76.37           O  
ANISOU 2044  O   ARG A1096    11967   9110   7940   -359    548    380       O  
ATOM   2045  CB  ARG A1096      26.072  -8.706  27.313  1.00 85.80           C  
ANISOU 2045  CB  ARG A1096    13637  10453   8510   -686     38    205       C  
ATOM   2046  CG  ARG A1096      26.974  -9.657  26.568  1.00 82.89           C  
ANISOU 2046  CG  ARG A1096    13541  10054   7898   -716    389     63       C  
ATOM   2047  CD  ARG A1096      27.247  -9.180  25.159  1.00 85.44           C  
ANISOU 2047  CD  ARG A1096    14183  10531   7750   -844    350    102       C  
ATOM   2048  NE  ARG A1096      26.098  -9.355  24.282  1.00 94.36           N  
ANISOU 2048  NE  ARG A1096    15514  11710   8629  -1018     -6    -32       N  
ATOM   2049  CZ  ARG A1096      26.167  -9.297  22.957  1.00 97.59           C  
ANISOU 2049  CZ  ARG A1096    16291  12257   8531  -1179    -60    -72       C  
ATOM   2050  NH1 ARG A1096      27.333  -9.075  22.369  1.00 93.17           N  
ANISOU 2050  NH1 ARG A1096    15919  11820   7663  -1201    286      6       N  
ATOM   2051  NH2 ARG A1096      25.078  -9.465  22.222  1.00102.27           N  
ANISOU 2051  NH2 ARG A1096    17053  12899   8906  -1338   -456   -197       N  
ATOM   2052  N   ALA A1097      26.196  -7.325  30.270  1.00 83.15           N  
ANISOU 2052  N   ALA A1097    12599  10095   8899   -381     10    450       N  
ATOM   2053  CA  ALA A1097      26.963  -6.656  31.316  1.00 74.83           C  
ANISOU 2053  CA  ALA A1097    11361   9035   8036   -245    100    585       C  
ATOM   2054  C   ALA A1097      26.946  -7.446  32.617  1.00 73.67           C  
ANISOU 2054  C   ALA A1097    11047   8874   8072   -207    277    525       C  
ATOM   2055  O   ALA A1097      27.942  -7.452  33.348  1.00 74.45           O  
ANISOU 2055  O   ALA A1097    11087   8949   8253   -111    442    628       O  
ATOM   2056  CB  ALA A1097      26.423  -5.246  31.550  1.00 63.51           C  
ANISOU 2056  CB  ALA A1097     9778   7621   6732   -175   -226    643       C  
ATOM   2057  N   ALA A1098      25.832  -8.117  32.923  1.00 71.99           N  
ANISOU 2057  N   ALA A1098    10755   8685   7912   -311    230    379       N  
ATOM   2058  CA  ALA A1098      25.774  -8.940  34.125  1.00 74.69           C  
ANISOU 2058  CA  ALA A1098    11001   9011   8365   -346    407    373       C  
ATOM   2059  C   ALA A1098      26.760 -10.098  34.047  1.00 83.58           C  
ANISOU 2059  C   ALA A1098    12344   9949   9462   -326    646    434       C  
ATOM   2060  O   ALA A1098      27.358 -10.485  35.059  1.00 82.43           O  
ANISOU 2060  O   ALA A1098    12168   9750   9403   -262    768    547       O  
ATOM   2061  CB  ALA A1098      24.351  -9.450  34.338  1.00 76.99           C  
ANISOU 2061  CB  ALA A1098    11160   9381   8710   -537    335    213       C  
ATOM   2062  N   LEU A1099      26.946 -10.665  32.852  1.00 86.05           N  
ANISOU 2062  N   LEU A1099    12886  10156   9651   -363    693    343       N  
ATOM   2063  CA  LEU A1099      27.950 -11.710  32.691  1.00 84.37           C  
ANISOU 2063  CA  LEU A1099    12858   9742   9457   -276    922    336       C  
ATOM   2064  C   LEU A1099      29.360 -11.153  32.838  1.00 75.62           C  
ANISOU 2064  C   LEU A1099    11669   8675   8388    -65   1050    473       C  
ATOM   2065  O   LEU A1099      30.242 -11.829  33.380  1.00 59.72           O  
ANISOU 2065  O   LEU A1099     9651   6525   6517     79   1192    528       O  
ATOM   2066  CB  LEU A1099      27.785 -12.397  31.335  1.00 88.81           C  
ANISOU 2066  CB  LEU A1099    13687  10211   9847   -362    961    126       C  
ATOM   2067  CG  LEU A1099      28.635 -13.647  31.091  1.00 89.13           C  
ANISOU 2067  CG  LEU A1099    13929   9988   9947   -253   1195     11       C  
ATOM   2068  CD1 LEU A1099      28.246 -14.750  32.060  1.00 88.78           C  
ANISOU 2068  CD1 LEU A1099    13929   9678  10126   -318   1188     43       C  
ATOM   2069  CD2 LEU A1099      28.496 -14.118  29.655  1.00 91.08           C  
ANISOU 2069  CD2 LEU A1099    14451  10201   9955   -337   1240   -262       C  
ATOM   2070  N   ILE A1100      29.591  -9.928  32.363  1.00 70.27           N  
ANISOU 2070  N   ILE A1100    10921   8168   7612    -56    974    541       N  
ATOM   2071  CA  ILE A1100      30.888  -9.294  32.557  1.00 70.30           C  
ANISOU 2071  CA  ILE A1100    10796   8234   7680     77   1083    680       C  
ATOM   2072  C   ILE A1100      31.120  -9.006  34.034  1.00 76.98           C  
ANISOU 2072  C   ILE A1100    11428   9092   8729    165   1006    808       C  
ATOM   2073  O   ILE A1100      32.244  -9.120  34.537  1.00 80.54           O  
ANISOU 2073  O   ILE A1100    11764   9529   9310    301   1104    897       O  
ATOM   2074  CB  ILE A1100      30.983  -8.022  31.697  1.00 68.88           C  
ANISOU 2074  CB  ILE A1100    10638   8193   7340    -10    989    761       C  
ATOM   2075  CG1 ILE A1100      30.869  -8.386  30.212  1.00 75.73           C  
ANISOU 2075  CG1 ILE A1100    11771   9090   7912   -120   1082    646       C  
ATOM   2076  CG2 ILE A1100      32.279  -7.281  31.978  1.00 63.94           C  
ANISOU 2076  CG2 ILE A1100     9841   7638   6817     56   1090    917       C  
ATOM   2077  CD1 ILE A1100      30.869  -7.196  29.275  1.00 65.67           C  
ANISOU 2077  CD1 ILE A1100    10607   7938   6405   -260    954    784       C  
ATOM   2078  N   ASN A1101      30.057  -8.645  34.757  1.00 76.26           N  
ANISOU 2078  N   ASN A1101    11262   9055   8656     88    828    795       N  
ATOM   2079  CA  ASN A1101      30.161  -8.449  36.200  1.00 71.74           C  
ANISOU 2079  CA  ASN A1101    10532   8535   8191    138    773    876       C  
ATOM   2080  C   ASN A1101      30.619  -9.725  36.896  1.00 69.64           C  
ANISOU 2080  C   ASN A1101    10339   8134   7987    190    891    949       C  
ATOM   2081  O   ASN A1101      31.439  -9.679  37.821  1.00 64.42           O  
ANISOU 2081  O   ASN A1101     9588   7486   7403    297    869   1078       O  
ATOM   2082  CB  ASN A1101      28.811  -7.981  36.750  1.00 72.99           C  
ANISOU 2082  CB  ASN A1101    10589   8814   8330     34    629    774       C  
ATOM   2083  CG  ASN A1101      28.882  -7.542  38.204  1.00 79.76           C  
ANISOU 2083  CG  ASN A1101    11293   9793   9219     68    586    807       C  
ATOM   2084  OD1 ASN A1101      29.385  -8.264  39.065  1.00 88.11           O  
ANISOU 2084  OD1 ASN A1101    12391  10824  10262     80    664    919       O  
ATOM   2085  ND2 ASN A1101      28.363  -6.353  38.484  1.00 77.04           N  
ANISOU 2085  ND2 ASN A1101    10794   9569   8909     92    434    696       N  
ATOM   2086  N   MET A1102      30.111 -10.877  36.452  1.00 67.47           N  
ANISOU 2086  N   MET A1102    10246   7696   7691    110    973    875       N  
ATOM   2087  CA  MET A1102      30.457 -12.137  37.100  1.00 68.00           C  
ANISOU 2087  CA  MET A1102    10442   7546   7851    150   1035    971       C  
ATOM   2088  C   MET A1102      31.900 -12.539  36.815  1.00 75.21           C  
ANISOU 2088  C   MET A1102    11354   8314   8910    407   1126   1011       C  
ATOM   2089  O   MET A1102      32.611 -12.984  37.723  1.00 77.63           O  
ANISOU 2089  O   MET A1102    11635   8519   9341    543   1075   1172       O  
ATOM   2090  CB  MET A1102      29.492 -13.233  36.655  1.00 70.40           C  
ANISOU 2090  CB  MET A1102    10958   7659   8132    -38   1075    861       C  
ATOM   2091  CG  MET A1102      28.072 -13.024  37.150  1.00 76.57           C  
ANISOU 2091  CG  MET A1102    11663   8605   8824   -310   1005    826       C  
ATOM   2092  SD  MET A1102      27.010 -14.445  36.822  1.00 81.97           S  
ANISOU 2092  SD  MET A1102    12572   9042   9532   -608   1039    733       S  
ATOM   2093  CE  MET A1102      27.916 -15.743  37.652  1.00 80.68           C  
ANISOU 2093  CE  MET A1102    12664   8490   9502   -523   1086    972       C  
ATOM   2094  N   VAL A1103      32.352 -12.395  35.565  1.00 79.58           N  
ANISOU 2094  N   VAL A1103    11918   8879   9439    475   1257    861       N  
ATOM   2095  CA  VAL A1103      33.743 -12.721  35.251  1.00 82.54           C  
ANISOU 2095  CA  VAL A1103    12205   9184   9974    728   1400    840       C  
ATOM   2096  C   VAL A1103      34.689 -11.726  35.912  1.00 80.24           C  
ANISOU 2096  C   VAL A1103    11618   9095   9774    826   1331   1000       C  
ATOM   2097  O   VAL A1103      35.848 -12.053  36.198  1.00 82.23           O  
ANISOU 2097  O   VAL A1103    11705   9299  10238   1051   1366   1045       O  
ATOM   2098  CB  VAL A1103      33.969 -12.782  33.727  1.00 84.75           C  
ANISOU 2098  CB  VAL A1103    12570   9500  10133    729   1619    609       C  
ATOM   2099  CG1 VAL A1103      32.942 -13.689  33.066  1.00 85.19           C  
ANISOU 2099  CG1 VAL A1103    12933   9364  10070    590   1631    415       C  
ATOM   2100  CG2 VAL A1103      33.931 -11.394  33.115  1.00 83.71           C  
ANISOU 2100  CG2 VAL A1103    12339   9665   9801    582   1615    646       C  
ATOM   2101  N   PHE A1104      34.222 -10.502  36.163  1.00 72.46           N  
ANISOU 2101  N   PHE A1104    10543   8321   8669    670   1206   1064       N  
ATOM   2102  CA  PHE A1104      35.025  -9.556  36.927  1.00 74.27           C  
ANISOU 2102  CA  PHE A1104    10521   8703   8994    721   1090   1196       C  
ATOM   2103  C   PHE A1104      35.203 -10.013  38.369  1.00 79.15           C  
ANISOU 2103  C   PHE A1104    11108   9268   9696    808    920   1340       C  
ATOM   2104  O   PHE A1104      36.258  -9.779  38.969  1.00 81.90           O  
ANISOU 2104  O   PHE A1104    11250   9676  10191    937    827   1439       O  
ATOM   2105  CB  PHE A1104      34.382  -8.171  36.883  1.00 67.54           C  
ANISOU 2105  CB  PHE A1104     9633   8010   8019    545    959   1195       C  
ATOM   2106  CG  PHE A1104      35.032  -7.234  35.911  1.00 71.68           C  
ANISOU 2106  CG  PHE A1104    10068   8632   8534    483   1036   1205       C  
ATOM   2107  CD1 PHE A1104      34.785  -7.340  34.554  1.00 74.18           C  
ANISOU 2107  CD1 PHE A1104    10546   8950   8690    396   1191   1126       C  
ATOM   2108  CD2 PHE A1104      35.892  -6.243  36.356  1.00 80.86           C  
ANISOU 2108  CD2 PHE A1104    11011   9893   9821    465    944   1303       C  
ATOM   2109  CE1 PHE A1104      35.384  -6.477  33.659  1.00 78.16           C  
ANISOU 2109  CE1 PHE A1104    11011   9565   9121    278   1280   1183       C  
ATOM   2110  CE2 PHE A1104      36.492  -5.376  35.467  1.00 85.63           C  
ANISOU 2110  CE2 PHE A1104    11550  10576  10412    335   1028   1354       C  
ATOM   2111  CZ  PHE A1104      36.238  -5.493  34.115  1.00 81.25           C  
ANISOU 2111  CZ  PHE A1104    11176  10035   9661    234   1209   1314       C  
ATOM   2112  N   GLN A1105      34.192 -10.669  38.935  1.00 80.45           N  
ANISOU 2112  N   GLN A1105    11475   9341   9754    708    866   1365       N  
ATOM   2113  CA  GLN A1105      34.237 -11.118  40.319  1.00 76.17           C  
ANISOU 2113  CA  GLN A1105    10978   8769   9193    723    706   1544       C  
ATOM   2114  C   GLN A1105      34.839 -12.508  40.465  1.00 79.87           C  
ANISOU 2114  C   GLN A1105    11579   8938   9829    899    695   1660       C  
ATOM   2115  O   GLN A1105      35.670 -12.731  41.352  1.00 77.78           O  
ANISOU 2115  O   GLN A1105    11252   8640   9660   1051    517   1841       O  
ATOM   2116  CB  GLN A1105      32.830 -11.107  40.918  1.00 71.88           C  
ANISOU 2116  CB  GLN A1105    10574   8313   8426    472    687   1531       C  
ATOM   2117  CG  GLN A1105      32.752 -11.692  42.313  1.00 71.95           C  
ANISOU 2117  CG  GLN A1105    10707   8315   8315    408    569   1741       C  
ATOM   2118  CD  GLN A1105      31.379 -11.534  42.928  1.00 72.70           C  
ANISOU 2118  CD  GLN A1105    10864   8598   8159    121    622   1689       C  
ATOM   2119  OE1 GLN A1105      30.414 -11.193  42.241  1.00 76.06           O  
ANISOU 2119  OE1 GLN A1105    11232   9099   8567     -1    727   1488       O  
ATOM   2120  NE2 GLN A1105      31.282 -11.777  44.230  1.00 68.30           N  
ANISOU 2120  NE2 GLN A1105    10410   8146   7396      7    545   1865       N  
ATOM   2121  N   MET A1106      34.433 -13.446  39.607  1.00 80.28           N  
ANISOU 2121  N   MET A1106    11826   8743   9934    892    842   1548       N  
ATOM   2122  CA  MET A1106      34.803 -14.847  39.734  1.00 82.95           C  
ANISOU 2122  CA  MET A1106    12358   8697  10463   1051    807   1630       C  
ATOM   2123  C   MET A1106      35.843 -15.311  38.725  1.00 89.43           C  
ANISOU 2123  C   MET A1106    13075   9350  11554   1362    949   1444       C  
ATOM   2124  O   MET A1106      36.305 -16.452  38.830  1.00 92.75           O  
ANISOU 2124  O   MET A1106    13623   9404  12215   1580    890   1476       O  
ATOM   2125  CB  MET A1106      33.551 -15.727  39.604  1.00 79.57           C  
ANISOU 2125  CB  MET A1106    12259   8043   9930    793    855   1607       C  
ATOM   2126  CG  MET A1106      32.706 -15.755  40.856  1.00 84.73           C  
ANISOU 2126  CG  MET A1106    13038   8785  10370    512    733   1843       C  
ATOM   2127  SD  MET A1106      30.984 -16.135  40.503  1.00 86.03           S  
ANISOU 2127  SD  MET A1106    13388   8937  10364     82    862   1721       S  
ATOM   2128  CE  MET A1106      30.421 -14.540  39.929  1.00 88.27           C  
ANISOU 2128  CE  MET A1106    13356   9694  10490     13    937   1471       C  
ATOM   2129  N   GLY A1107      36.219 -14.477  37.763  1.00 83.47           N  
ANISOU 2129  N   GLY A1107    12104   8844  10768   1383   1136   1249       N  
ATOM   2130  CA  GLY A1107      37.045 -14.923  36.668  1.00 86.98           C  
ANISOU 2130  CA  GLY A1107    12460   9202  11389   1617   1365   1006       C  
ATOM   2131  C   GLY A1107      36.292 -15.824  35.707  1.00 88.79           C  
ANISOU 2131  C   GLY A1107    13014   9179  11544   1543   1521    764       C  
ATOM   2132  O   GLY A1107      35.264 -16.426  36.027  1.00 86.13           O  
ANISOU 2132  O   GLY A1107    12973   8625  11128   1354   1409    824       O  
ATOM   2133  N   GLU A1108      36.843 -15.917  34.497  1.00 89.49           N  
ANISOU 2133  N   GLU A1108    13038   9319  11644   1667   1796    468       N  
ATOM   2134  CA  GLU A1108      36.262 -16.761  33.464  1.00 87.52           C  
ANISOU 2134  CA  GLU A1108    13103   8850  11300   1613   1951    163       C  
ATOM   2135  C   GLU A1108      36.230 -18.231  33.861  1.00 85.64           C  
ANISOU 2135  C   GLU A1108    13113   8070  11356   1798   1837    124       C  
ATOM   2136  O   GLU A1108      35.365 -18.973  33.377  1.00 84.49           O  
ANISOU 2136  O   GLU A1108    13313   7661  11130   1634   1842    -46       O  
ATOM   2137  CB  GLU A1108      37.029 -16.590  32.160  1.00 95.88           C  
ANISOU 2137  CB  GLU A1108    14037  10114  12279   1733   2303   -169       C  
ATOM   2138  CG  GLU A1108      36.931 -15.181  31.598  1.00102.62           C  
ANISOU 2138  CG  GLU A1108    14756  11443  12792   1470   2402   -100       C  
ATOM   2139  CD  GLU A1108      37.375 -15.104  30.157  1.00109.37           C  
ANISOU 2139  CD  GLU A1108    15629  12514  13413   1456   2771   -421       C  
ATOM   2140  OE1 GLU A1108      37.716 -16.168  29.591  1.00113.53           O  
ANISOU 2140  OE1 GLU A1108    16260  12832  14044   1672   2970   -764       O  
ATOM   2141  OE2 GLU A1108      37.380 -13.985  29.593  1.00105.41           O1+
ANISOU 2141  OE2 GLU A1108    15063  12377  12612   1221   2859   -335       O1+
ATOM   2142  N   THR A1109      37.155 -18.669  34.719  1.00 90.70           N  
ANISOU 2142  N   THR A1109    13597   8510  12353   2124   1695    286       N  
ATOM   2143  CA  THR A1109      37.120 -20.042  35.207  1.00 95.84           C  
ANISOU 2143  CA  THR A1109    14532   8571  13311   2298   1506    331       C  
ATOM   2144  C   THR A1109      35.855 -20.297  36.012  1.00 92.70           C  
ANISOU 2144  C   THR A1109    14477   8003  12741   1906   1273    629       C  
ATOM   2145  O   THR A1109      35.133 -21.269  35.766  1.00 95.09           O  
ANISOU 2145  O   THR A1109    15151   7895  13084   1765   1241    533       O  
ATOM   2146  CB  THR A1109      38.349 -20.335  36.066  1.00 97.86           C  
ANISOU 2146  CB  THR A1109    14535   8674  13974   2728   1309    517       C  
ATOM   2147  OG1 THR A1109      39.538 -19.920  35.381  1.00102.45           O  
ANISOU 2147  OG1 THR A1109    14672   9535  14718   3048   1561    242       O  
ATOM   2148  CG2 THR A1109      38.427 -21.828  36.376  1.00 97.85           C  
ANISOU 2148  CG2 THR A1109    14861   7969  14349   2976   1099    531       C  
ATOM   2149  N   GLY A1110      35.567 -19.420  36.975  1.00 95.75           N  
ANISOU 2149  N   GLY A1110    14731   8720  12931   1701   1128    965       N  
ATOM   2150  CA  GLY A1110      34.456 -19.660  37.880  1.00 94.88           C  
ANISOU 2150  CA  GLY A1110    14887   8513  12649   1331    949   1253       C  
ATOM   2151  C   GLY A1110      33.103 -19.552  37.204  1.00 88.67           C  
ANISOU 2151  C   GLY A1110    14261   7826  11602    922   1075   1072       C  
ATOM   2152  O   GLY A1110      32.191 -20.329  37.497  1.00 82.42           O  
ANISOU 2152  O   GLY A1110    13765   6760  10793    635    997   1160       O  
ATOM   2153  N   VAL A1111      32.952 -18.588  36.296  1.00 85.36           N  
ANISOU 2153  N   VAL A1111    13649   7799  10986    866   1244    836       N  
ATOM   2154  CA  VAL A1111      31.676 -18.422  35.606  1.00 83.59           C  
ANISOU 2154  CA  VAL A1111    13541   7694  10525    508   1297    660       C  
ATOM   2155  C   VAL A1111      31.371 -19.646  34.751  1.00 86.94           C  
ANISOU 2155  C   VAL A1111    14292   7686  11055    469   1346    385       C  
ATOM   2156  O   VAL A1111      30.217 -20.080  34.649  1.00 84.62           O  
ANISOU 2156  O   VAL A1111    14188   7281  10681    116   1284    338       O  
ATOM   2157  CB  VAL A1111      31.689 -17.125  34.776  1.00 78.72           C  
ANISOU 2157  CB  VAL A1111    12692   7539   9679    492   1403    508       C  
ATOM   2158  CG1 VAL A1111      30.403 -16.979  33.994  1.00 82.94           C  
ANISOU 2158  CG1 VAL A1111    13340   8183   9992    166   1385    324       C  
ATOM   2159  CG2 VAL A1111      31.894 -15.925  35.684  1.00 68.67           C  
ANISOU 2159  CG2 VAL A1111    11133   6621   8339    498   1317    755       C  
ATOM   2160  N   ALA A1112      32.402 -20.242  34.147  1.00 83.83           N  
ANISOU 2160  N   ALA A1112    13946   7039  10867    828   1457    166       N  
ATOM   2161  CA  ALA A1112      32.208 -21.434  33.331  1.00 86.95           C  
ANISOU 2161  CA  ALA A1112    14676   6976  11386    838   1502   -166       C  
ATOM   2162  C   ALA A1112      31.727 -22.636  34.137  1.00 97.68           C  
ANISOU 2162  C   ALA A1112    16361   7762  12989    696   1293     31       C  
ATOM   2163  O   ALA A1112      31.408 -23.672  33.541  1.00107.07           O  
ANISOU 2163  O   ALA A1112    17878   8495  14308    634   1283   -236       O  
ATOM   2164  CB  ALA A1112      33.504 -21.784  32.597  1.00 82.87           C  
ANISOU 2164  CB  ALA A1112    14088   6331  11068   1312   1699   -487       C  
ATOM   2165  N   GLY A1113      31.670 -22.528  35.467  1.00 94.08           N  
ANISOU 2165  N   GLY A1113    15859   7311  12576    613   1121    490       N  
ATOM   2166  CA  GLY A1113      31.127 -23.580  36.301  1.00 91.96           C  
ANISOU 2166  CA  GLY A1113    15934   6547  12461    374    924    767       C  
ATOM   2167  C   GLY A1113      29.632 -23.536  36.499  1.00 88.01           C  
ANISOU 2167  C   GLY A1113    15526   6189  11726   -228    907    854       C  
ATOM   2168  O   GLY A1113      29.067 -24.463  37.088  1.00 90.55           O  
ANISOU 2168  O   GLY A1113    16155   6098  12153   -532    780   1074       O  
ATOM   2169  N   PHE A1114      28.975 -22.477  36.030  1.00 89.32           N  
ANISOU 2169  N   PHE A1114    15419   6923  11597   -417   1020    697       N  
ATOM   2170  CA  PHE A1114      27.518 -22.347  36.101  1.00 93.06           C  
ANISOU 2170  CA  PHE A1114    15868   7604  11887   -955   1007    701       C  
ATOM   2171  C   PHE A1114      26.844 -22.935  34.867  1.00 97.68           C  
ANISOU 2171  C   PHE A1114    16640   7982  12490  -1154   1008    293       C  
ATOM   2172  O   PHE A1114      25.996 -22.294  34.250  1.00100.46           O  
ANISOU 2172  O   PHE A1114    16812   8720  12638  -1379   1016     94       O  
ATOM   2173  CB  PHE A1114      27.127 -20.883  36.266  1.00 94.49           C  
ANISOU 2173  CB  PHE A1114    15638   8468  11794  -1010   1062    728       C  
ATOM   2174  CG  PHE A1114      27.602 -20.258  37.542  1.00 95.33           C  
ANISOU 2174  CG  PHE A1114    15570   8818  11834   -900   1044   1086       C  
ATOM   2175  CD1 PHE A1114      26.863 -20.382  38.706  1.00 96.26           C  
ANISOU 2175  CD1 PHE A1114    15694   9032  11847  -1255   1023   1375       C  
ATOM   2176  CD2 PHE A1114      28.773 -19.521  37.572  1.00 93.76           C  
ANISOU 2176  CD2 PHE A1114    15190   8788  11647   -478   1057   1113       C  
ATOM   2177  CE1 PHE A1114      27.293 -19.799  39.881  1.00 93.49           C  
ANISOU 2177  CE1 PHE A1114    15219   8937  11366  -1170    999   1669       C  
ATOM   2178  CE2 PHE A1114      29.209 -18.933  38.743  1.00 90.99           C  
ANISOU 2178  CE2 PHE A1114    14688   8664  11219   -396    999   1410       C  
ATOM   2179  CZ  PHE A1114      28.468 -19.072  39.900  1.00 89.90           C  
ANISOU 2179  CZ  PHE A1114    14603   8619  10937   -731    961   1678       C  
ATOM   2180  N   THR A1115      27.213 -24.163  34.496  1.00 93.63           N  
ANISOU 2180  N   THR A1115    16502   6840  12234  -1062    963    146       N  
ATOM   2181  CA  THR A1115      26.755 -24.715  33.225  1.00 97.80           C  
ANISOU 2181  CA  THR A1115    17241   7160  12760  -1192    960   -325       C  
ATOM   2182  C   THR A1115      25.237 -24.821  33.175  1.00101.53           C  
ANISOU 2182  C   THR A1115    17699   7752  13126  -1809    862   -353       C  
ATOM   2183  O   THR A1115      24.618 -24.467  32.164  1.00100.69           O  
ANISOU 2183  O   THR A1115    17515   7914  12829  -1958    838   -694       O  
ATOM   2184  CB  THR A1115      27.395 -26.081  32.984  1.00104.56           C  
ANISOU 2184  CB  THR A1115    18523   7240  13966   -980    909   -494       C  
ATOM   2185  OG1 THR A1115      26.936 -27.010  33.974  1.00111.74           O  
ANISOU 2185  OG1 THR A1115    19700   7650  15106  -1304    745   -134       O  
ATOM   2186  CG2 THR A1115      28.912 -25.975  33.059  1.00103.25           C  
ANISOU 2186  CG2 THR A1115    18273   6991  13964   -334   1002   -493       C  
ATOM   2187  N   ASN A1116      24.617 -25.292  34.259  1.00109.01           N  
ANISOU 2187  N   ASN A1116    18703   8536  14180  -2193    797     12       N  
ATOM   2188  CA  ASN A1116      23.168 -25.450  34.256  1.00114.25           C  
ANISOU 2188  CA  ASN A1116    19286   9335  14790  -2821    734    -24       C  
ATOM   2189  C   ASN A1116      22.464 -24.103  34.180  1.00108.33           C  
ANISOU 2189  C   ASN A1116    18027   9368  13766  -2910    776    -69       C  
ATOM   2190  O   ASN A1116      21.401 -23.993  33.560  1.00112.39           O  
ANISOU 2190  O   ASN A1116    18389  10096  14219  -3257    688   -317       O  
ATOM   2191  CB  ASN A1116      22.716 -26.227  35.496  1.00119.12           C  
ANISOU 2191  CB  ASN A1116    20066   9646  15546  -3254    712    417       C  
ATOM   2192  N   SER A1117      23.040 -23.071  34.794  1.00107.10           N  
ANISOU 2192  N   SER A1117    17599   9621  13474  -2592    871    149       N  
ATOM   2193  CA  SER A1117      22.434 -21.748  34.719  1.00102.31           C  
ANISOU 2193  CA  SER A1117    16531   9686  12658  -2613    880     85       C  
ATOM   2194  C   SER A1117      22.674 -21.101  33.361  1.00102.29           C  
ANISOU 2194  C   SER A1117    16484   9870  12513  -2343    814   -265       C  
ATOM   2195  O   SER A1117      21.756 -20.507  32.785  1.00100.23           O  
ANISOU 2195  O   SER A1117    15984   9960  12139  -2521    696   -453       O  
ATOM   2196  CB  SER A1117      22.981 -20.857  35.835  1.00 98.47           C  
ANISOU 2196  CB  SER A1117    15811   9527  12076  -2381    982    404       C  
ATOM   2197  OG  SER A1117      22.892 -21.504  37.092  1.00 97.73           O  
ANISOU 2197  OG  SER A1117    15842   9258  12035  -2624   1039    761       O  
ATOM   2198  N   LEU A1118      23.897 -21.215  32.836  1.00104.26           N  
ANISOU 2198  N   LEU A1118    16951   9904  12761  -1923    883   -351       N  
ATOM   2199  CA  LEU A1118      24.243 -20.548  31.585  1.00100.23           C  
ANISOU 2199  CA  LEU A1118    16425   9622  12038  -1690    875   -637       C  
ATOM   2200  C   LEU A1118      23.389 -21.046  30.427  1.00107.73           C  
ANISOU 2200  C   LEU A1118    17547  10492  12892  -1976    724  -1011       C  
ATOM   2201  O   LEU A1118      23.041 -20.274  29.525  1.00110.02           O  
ANISOU 2201  O   LEU A1118    17736  11135  12931  -1982    613  -1185       O  
ATOM   2202  CB  LEU A1118      25.722 -20.757  31.279  1.00 92.05           C  
ANISOU 2202  CB  LEU A1118    15569   8366  11040  -1233   1041   -692       C  
ATOM   2203  CG  LEU A1118      26.695 -19.998  32.171  1.00 86.98           C  
ANISOU 2203  CG  LEU A1118    14695   7910  10443   -907   1144   -375       C  
ATOM   2204  CD1 LEU A1118      28.100 -20.549  32.003  1.00 86.56           C  
ANISOU 2204  CD1 LEU A1118    14792   7548  10551   -488   1291   -444       C  
ATOM   2205  CD2 LEU A1118      26.654 -18.516  31.846  1.00 86.67           C  
ANISOU 2205  CD2 LEU A1118    14359   8413  10159   -835   1133   -349       C  
ATOM   2206  N   ARG A1119      23.046 -22.333  30.429  1.00104.44           N  
ANISOU 2206  N   ARG A1119    17422   9590  12668  -2232    680  -1129       N  
ATOM   2207  CA  ARG A1119      22.191 -22.858  29.372  1.00103.70           C  
ANISOU 2207  CA  ARG A1119    17500   9406  12496  -2554    498  -1514       C  
ATOM   2208  C   ARG A1119      20.795 -22.250  29.433  1.00102.63           C  
ANISOU 2208  C   ARG A1119    16991   9707  12297  -2952    292  -1490       C  
ATOM   2209  O   ARG A1119      20.133 -22.113  28.398  1.00102.11           O  
ANISOU 2209  O   ARG A1119    16930   9811  12055  -3119     75  -1792       O  
ATOM   2210  CB  ARG A1119      22.123 -24.383  29.466  1.00105.66           C  
ANISOU 2210  CB  ARG A1119    18150   8971  13026  -2774    474  -1635       C  
ATOM   2211  CG  ARG A1119      21.461 -25.066  28.282  1.00110.68           C  
ANISOU 2211  CG  ARG A1119    19053   9414  13586  -3068    283  -2116       C  
ATOM   2212  CD  ARG A1119      21.400 -26.576  28.478  1.00119.37           C  
ANISOU 2212  CD  ARG A1119    20574   9750  15030  -3303    239  -2220       C  
ATOM   2213  NE  ARG A1119      20.881 -26.936  29.795  1.00121.59           N  
ANISOU 2213  NE  ARG A1119    20741   9865  15590  -3652    240  -1772       N  
ATOM   2214  CZ  ARG A1119      21.609 -27.484  30.763  1.00120.23           C  
ANISOU 2214  CZ  ARG A1119    20757   9256  15669  -3483    350  -1432       C  
ATOM   2215  NH1 ARG A1119      22.893 -27.748  30.561  1.00119.50           N1+
ANISOU 2215  NH1 ARG A1119    20917   8831  15658  -2927    455  -1524       N1+
ATOM   2216  NH2 ARG A1119      21.053 -27.772  31.933  1.00120.62           N  
ANISOU 2216  NH2 ARG A1119    20732   9219  15878  -3878    351  -1000       N  
ATOM   2217  N   MET A1120      20.338 -21.863  30.627  1.00100.48           N  
ANISOU 2217  N   MET A1120    16375   9649  12155  -3093    347  -1158       N  
ATOM   2218  CA  MET A1120      19.012 -21.263  30.756  1.00103.10           C  
ANISOU 2218  CA  MET A1120    16260  10430  12486  -3427    184  -1176       C  
ATOM   2219  C   MET A1120      19.000 -19.818  30.272  1.00100.31           C  
ANISOU 2219  C   MET A1120    15604  10594  11915  -3129     66  -1209       C  
ATOM   2220  O   MET A1120      18.009 -19.365  29.686  1.00100.24           O  
ANISOU 2220  O   MET A1120    15342  10888  11857  -3303   -198  -1388       O  
ATOM   2221  CB  MET A1120      18.535 -21.349  32.203  1.00106.18           C  
ANISOU 2221  CB  MET A1120    16380  10910  13054  -3686    341   -856       C  
ATOM   2222  CG  MET A1120      18.420 -22.776  32.714  1.00117.71           C  
ANISOU 2222  CG  MET A1120    18166  11832  14725  -4073    415   -750       C  
ATOM   2223  SD  MET A1120      17.789 -22.885  34.401  1.00123.98           S  
ANISOU 2223  SD  MET A1120    18683  12804  15620  -4485    629   -335       S  
ATOM   2224  CE  MET A1120      17.761 -24.663  34.625  1.00131.09           C  
ANISOU 2224  CE  MET A1120    20134  12916  16760  -4951    624   -214       C  
ATOM   2225  N   LEU A1121      20.082 -19.075  30.519  1.00100.35           N  
ANISOU 2225  N   LEU A1121    15626  10687  11815  -2692    222  -1026       N  
ATOM   2226  CA  LEU A1121      20.236 -17.769  29.884  1.00100.41           C  
ANISOU 2226  CA  LEU A1121    15473  11071  11608  -2415     91  -1049       C  
ATOM   2227  C   LEU A1121      20.299 -17.911  28.369  1.00105.95           C  
ANISOU 2227  C   LEU A1121    16480  11732  12045  -2411    -85  -1340       C  
ATOM   2228  O   LEU A1121      19.794 -17.057  27.629  1.00108.90           O  
ANISOU 2228  O   LEU A1121    16728  12416  12235  -2399   -355  -1411       O  
ATOM   2229  CB  LEU A1121      21.498 -17.077  30.396  1.00 89.96           C  
ANISOU 2229  CB  LEU A1121    14156   9787  10238  -2005    306   -807       C  
ATOM   2230  CG  LEU A1121      21.578 -16.711  31.874  1.00 82.79           C  
ANISOU 2230  CG  LEU A1121    12972   8988   9494  -1956    454   -522       C  
ATOM   2231  CD1 LEU A1121      22.975 -16.220  32.204  1.00 72.92           C  
ANISOU 2231  CD1 LEU A1121    11799   7708   8200  -1566    625   -331       C  
ATOM   2232  CD2 LEU A1121      20.549 -15.649  32.207  1.00 85.66           C  
ANISOU 2232  CD2 LEU A1121    12882   9776   9890  -2027    296   -524       C  
ATOM   2233  N   GLN A1122      20.920 -18.991  27.892  1.00 98.13           N  
ANISOU 2233  N   GLN A1122    15913  10351  11023  -2411     46  -1520       N  
ATOM   2234  CA  GLN A1122      21.020 -19.232  26.459  1.00 98.26           C  
ANISOU 2234  CA  GLN A1122    16271  10336  10727  -2427    -75  -1857       C  
ATOM   2235  C   GLN A1122      19.667 -19.584  25.852  1.00 96.39           C  
ANISOU 2235  C   GLN A1122    15998  10161  10466  -2846   -440  -2111       C  
ATOM   2236  O   GLN A1122      19.425 -19.301  24.674  1.00 98.68           O  
ANISOU 2236  O   GLN A1122    16445  10634  10417  -2889   -682  -2330       O  
ATOM   2237  CB  GLN A1122      22.036 -20.346  26.201  1.00103.05           C  
ANISOU 2237  CB  GLN A1122    17309  10483  11362  -2283    189  -2053       C  
ATOM   2238  CG  GLN A1122      22.347 -20.616  24.747  1.00107.55           C  
ANISOU 2238  CG  GLN A1122    18269  11042  11552  -2252    165  -2458       C  
ATOM   2239  CD  GLN A1122      23.447 -21.645  24.581  1.00111.75           C  
ANISOU 2239  CD  GLN A1122    19160  11128  12172  -2017    475  -2696       C  
ATOM   2240  OE1 GLN A1122      24.039 -22.100  25.559  1.00115.12           O  
ANISOU 2240  OE1 GLN A1122    19540  11237  12962  -1840    666  -2506       O  
ATOM   2241  NE2 GLN A1122      23.726 -22.017  23.338  1.00113.25           N  
ANISOU 2241  NE2 GLN A1122    19714  11294  12023  -1998    511  -3131       N  
ATOM   2242  N   GLN A1123      18.773 -20.184  26.639  1.00102.08           N  
ANISOU 2242  N   GLN A1123    16506  10761  11521  -3189   -495  -2073       N  
ATOM   2243  CA  GLN A1123      17.459 -20.603  26.168  1.00103.74           C  
ANISOU 2243  CA  GLN A1123    16604  11025  11786  -3643   -839  -2321       C  
ATOM   2244  C   GLN A1123      16.362 -19.590  26.496  1.00108.72           C  
ANISOU 2244  C   GLN A1123    16638  12153  12517  -3742  -1093  -2203       C  
ATOM   2245  O   GLN A1123      15.179 -19.947  26.486  1.00110.87           O  
ANISOU 2245  O   GLN A1123    16643  12510  12973  -4152  -1332  -2352       O  
ATOM   2246  CB  GLN A1123      17.101 -21.971  26.754  1.00101.84           C  
ANISOU 2246  CB  GLN A1123    16492  10326  11878  -4039   -744  -2378       C  
ATOM   2247  CG  GLN A1123      17.964 -23.119  26.251  1.00 99.00           C  
ANISOU 2247  CG  GLN A1123    16739   9389  11487  -3971   -604  -2613       C  
ATOM   2248  CD  GLN A1123      17.609 -24.442  26.905  1.00109.60           C  
ANISOU 2248  CD  GLN A1123    18244  10191  13208  -4372   -553  -2607       C  
ATOM   2249  OE1 GLN A1123      17.694 -24.589  28.124  1.00109.83           O  
ANISOU 2249  OE1 GLN A1123    18131  10108  13491  -4423   -352  -2243       O  
ATOM   2250  NE2 GLN A1123      17.200 -25.410  26.095  1.00111.61           N  
ANISOU 2250  NE2 GLN A1123    18833  10095  13478  -4692   -754  -3005       N  
ATOM   2251  N   LYS A1124      16.728 -18.344  26.794  1.00101.10           N  
ANISOU 2251  N   LYS A1124    15436  11503  11475  -3376  -1053  -1965       N  
ATOM   2252  CA  LYS A1124      15.801 -17.264  27.128  1.00102.00           C  
ANISOU 2252  CA  LYS A1124    14979  12055  11722  -3354  -1290  -1880       C  
ATOM   2253  C   LYS A1124      14.956 -17.560  28.362  1.00106.14           C  
ANISOU 2253  C   LYS A1124    15026  12671  12629  -3642  -1145  -1813       C  
ATOM   2254  O   LYS A1124      13.969 -16.858  28.613  1.00108.27           O  
ANISOU 2254  O   LYS A1124    14746  13316  13075  -3688  -1344  -1851       O  
ATOM   2255  CB  LYS A1124      14.875 -16.927  25.950  1.00104.85           C  
ANISOU 2255  CB  LYS A1124    15253  12649  11937  -3482  -1823  -2115       C  
ATOM   2256  CG  LYS A1124      15.585 -16.569  24.655  1.00106.34           C  
ANISOU 2256  CG  LYS A1124    15931  12827  11648  -3267  -1994  -2170       C  
ATOM   2257  CD  LYS A1124      16.318 -15.246  24.762  1.00102.53           C  
ANISOU 2257  CD  LYS A1124    15411  12521  11026  -2834  -1939  -1876       C  
ATOM   2258  CE  LYS A1124      16.710 -14.725  23.392  1.00104.63           C  
ANISOU 2258  CE  LYS A1124    16088  12882  10786  -2721  -2205  -1897       C  
ATOM   2259  NZ  LYS A1124      15.510 -14.429  22.560  1.00109.17           N  
ANISOU 2259  NZ  LYS A1124    16517  13684  11279  -2897  -2828  -2043       N  
ATOM   2260  N   ARG A1125      15.311 -18.583  29.142  1.00109.81           N  
ANISOU 2260  N   ARG A1125    15685  12809  13228  -3839   -806  -1713       N  
ATOM   2261  CA  ARG A1125      14.563 -18.937  30.349  1.00105.46           C  
ANISOU 2261  CA  ARG A1125    14749  12354  12966  -4188   -611  -1603       C  
ATOM   2262  C   ARG A1125      15.011 -18.038  31.502  1.00105.15           C  
ANISOU 2262  C   ARG A1125    14454  12555  12943  -3878   -338  -1327       C  
ATOM   2263  O   ARG A1125      15.645 -18.469  32.467  1.00102.11           O  
ANISOU 2263  O   ARG A1125    14245  11977  12576  -3884    -12  -1083       O  
ATOM   2264  CB  ARG A1125      14.757 -20.408  30.687  1.00100.56           C  
ANISOU 2264  CB  ARG A1125    14519  11232  12456  -4562   -413  -1558       C  
ATOM   2265  CG  ARG A1125      14.118 -21.370  29.702  1.00104.76           C  
ANISOU 2265  CG  ARG A1125    15255  11516  13034  -4972   -689  -1879       C  
ATOM   2266  CD  ARG A1125      14.117 -22.790  30.251  1.00109.68           C  
ANISOU 2266  CD  ARG A1125    16197  11614  13861  -5418   -505  -1800       C  
ATOM   2267  NE  ARG A1125      15.435 -23.419  30.187  1.00111.71           N  
ANISOU 2267  NE  ARG A1125    17086  11317  14042  -5114   -333  -1714       N  
ATOM   2268  CZ  ARG A1125      15.756 -24.551  30.807  1.00114.79           C  
ANISOU 2268  CZ  ARG A1125    17840  11156  14619  -5338   -166  -1549       C  
ATOM   2269  NH1 ARG A1125      14.859 -25.182  31.553  1.00117.33           N1+
ANISOU 2269  NH1 ARG A1125    17995  11419  15168  -5934   -115  -1411       N1+
ATOM   2270  NH2 ARG A1125      16.978 -25.051  30.689  1.00114.27           N  
ANISOU 2270  NH2 ARG A1125    18294  10594  14529  -4971    -54  -1512       N  
ATOM   2271  N   TRP A1126      14.657 -16.753  31.387  1.00102.43           N  
ANISOU 2271  N   TRP A1126    13702  12620  12595  -3599   -520  -1377       N  
ATOM   2272  CA  TRP A1126      15.103 -15.775  32.375  1.00 99.11           C  
ANISOU 2272  CA  TRP A1126    13061  12418  12179  -3267   -310  -1183       C  
ATOM   2273  C   TRP A1126      14.567 -16.088  33.763  1.00100.00           C  
ANISOU 2273  C   TRP A1126    12842  12708  12447  -3564     17  -1092       C  
ATOM   2274  O   TRP A1126      15.235 -15.807  34.763  1.00 95.88           O  
ANISOU 2274  O   TRP A1126    12367  12211  11852  -3395    296   -877       O  
ATOM   2275  CB  TRP A1126      14.683 -14.363  31.959  1.00 98.18           C  
ANISOU 2275  CB  TRP A1126    12566  12644  12092  -2934   -622  -1293       C  
ATOM   2276  CG  TRP A1126      15.001 -14.027  30.537  1.00 99.97           C  
ANISOU 2276  CG  TRP A1126    13108  12760  12116  -2737   -990  -1360       C  
ATOM   2277  CD1 TRP A1126      14.127 -13.586  29.588  1.00102.49           C  
ANISOU 2277  CD1 TRP A1126    13224  13259  12460  -2750  -1458  -1549       C  
ATOM   2278  CD2 TRP A1126      16.280 -14.113  29.895  1.00100.88           C  
ANISOU 2278  CD2 TRP A1126    13796  12592  11940  -2519   -920  -1236       C  
ATOM   2279  NE1 TRP A1126      14.782 -13.387  28.397  1.00102.69           N  
ANISOU 2279  NE1 TRP A1126    13720  13132  12164  -2582  -1684  -1520       N  
ATOM   2280  CE2 TRP A1126      16.105 -13.705  28.559  1.00102.48           C  
ANISOU 2280  CE2 TRP A1126    14155  12841  11942  -2447  -1322  -1348       C  
ATOM   2281  CE3 TRP A1126      17.558 -14.494  30.321  1.00101.84           C  
ANISOU 2281  CE3 TRP A1126    14288  12451  11954  -2377   -563  -1048       C  
ATOM   2282  CZ2 TRP A1126      17.157 -13.666  27.646  1.00107.44           C  
ANISOU 2282  CZ2 TRP A1126    15302  13297  12222  -2277  -1308  -1288       C  
ATOM   2283  CZ3 TRP A1126      18.601 -14.457  29.411  1.00101.67           C  
ANISOU 2283  CZ3 TRP A1126    14713  12253  11664  -2171   -560  -1020       C  
ATOM   2284  CH2 TRP A1126      18.393 -14.051  28.088  1.00104.96           C  
ANISOU 2284  CH2 TRP A1126    15284  12756  11842  -2142   -895  -1146       C  
ATOM   2285  N   ASP A1127      13.370 -16.667  33.848  1.00105.05           N  
ANISOU 2285  N   ASP A1127    13142  13500  13273  -4040    -10  -1251       N  
ATOM   2286  CA  ASP A1127      12.801 -16.985  35.152  1.00105.65           C  
ANISOU 2286  CA  ASP A1127    12891  13805  13446  -4403    350  -1159       C  
ATOM   2287  C   ASP A1127      13.638 -18.034  35.873  1.00102.58           C  
ANISOU 2287  C   ASP A1127    13044  13002  12929  -4604    661   -828       C  
ATOM   2288  O   ASP A1127      14.085 -17.819  37.005  1.00 97.10           O  
ANISOU 2288  O   ASP A1127    12362  12413  12117  -4531    958   -598       O  
ATOM   2289  CB  ASP A1127      11.355 -17.458  34.988  1.00113.14           C  
ANISOU 2289  CB  ASP A1127    13346  15002  14642  -4937    260  -1403       C  
ATOM   2290  N   GLU A1128      13.877 -19.175  35.221  1.00105.05           N  
ANISOU 2290  N   GLU A1128    13834  12818  13263  -4840    560   -812       N  
ATOM   2291  CA  GLU A1128      14.589 -20.266  35.881  1.00101.37           C  
ANISOU 2291  CA  GLU A1128    13890  11878  12749  -5036    788   -497       C  
ATOM   2292  C   GLU A1128      16.064 -19.940  36.072  1.00 98.59           C  
ANISOU 2292  C   GLU A1128    13939  11292  12227  -4482    856   -278       C  
ATOM   2293  O   GLU A1128      16.652 -20.294  37.101  1.00 98.75           O  
ANISOU 2293  O   GLU A1128    14183  11164  12175  -4507   1075     48       O  
ATOM   2294  CB  GLU A1128      14.433 -21.557  35.083  1.00102.72           C  
ANISOU 2294  CB  GLU A1128    14465  11516  13047  -5400    625   -601       C  
ATOM   2295  CG  GLU A1128      13.004 -22.014  34.909  1.00109.16           C  
ANISOU 2295  CG  GLU A1128    14894  12518  14063  -6031    538   -807       C  
ATOM   2296  CD  GLU A1128      12.920 -23.465  34.496  1.00117.05           C  
ANISOU 2296  CD  GLU A1128    16374  12895  15205  -6501    444   -827       C  
ATOM   2297  OE1 GLU A1128      13.445 -24.324  35.236  1.00119.18           O  
ANISOU 2297  OE1 GLU A1128    17078  12716  15487  -6681    639   -499       O  
ATOM   2298  OE2 GLU A1128      12.343 -23.744  33.426  1.00122.20           O  
ANISOU 2298  OE2 GLU A1128    16997  13477  15956  -6685    137  -1171       O  
ATOM   2299  N   ALA A1129      16.686 -19.280  35.090  1.00106.39           N  
ANISOU 2299  N   ALA A1129    15026  12259  13140  -4007    658   -438       N  
ATOM   2300  CA  ALA A1129      18.089 -18.904  35.232  1.00 98.44           C  
ANISOU 2300  CA  ALA A1129    14315  11087  12002  -3503    734   -256       C  
ATOM   2301  C   ALA A1129      18.313 -18.065  36.481  1.00 99.96           C  
ANISOU 2301  C   ALA A1129    14247  11624  12110  -3345    925    -40       C  
ATOM   2302  O   ALA A1129      19.394 -18.111  37.080  1.00 91.71           O  
ANISOU 2302  O   ALA A1129    13458  10403  10986  -3100   1037    208       O  
ATOM   2303  CB  ALA A1129      18.562 -18.146  33.991  1.00 90.27           C  
ANISOU 2303  CB  ALA A1129    13335  10100  10864  -3097    524   -462       C  
ATOM   2304  N   ALA A1130      17.300 -17.301  36.894  1.00101.90           N  
ANISOU 2304  N   ALA A1130    13969  12366  12382  -3472    950   -165       N  
ATOM   2305  CA  ALA A1130      17.396 -16.557  38.143  1.00100.47           C  
ANISOU 2305  CA  ALA A1130    13541  12535  12097  -3370   1159    -30       C  
ATOM   2306  C   ALA A1130      17.236 -17.478  39.344  1.00 96.24           C  
ANISOU 2306  C   ALA A1130    13135  11951  11481  -3804   1437    243       C  
ATOM   2307  O   ALA A1130      17.958 -17.340  40.339  1.00 91.99           O  
ANISOU 2307  O   ALA A1130    12752  11434  10767  -3682   1586    498       O  
ATOM   2308  CB  ALA A1130      16.348 -15.446  38.172  1.00102.74           C  
ANISOU 2308  CB  ALA A1130    13205  13359  12471  -3324   1106   -319       C  
ATOM   2309  N   VAL A1131      16.303 -18.428  39.267  1.00 92.07           N  
ANISOU 2309  N   VAL A1131    12568  11350  11062  -4347   1484    213       N  
ATOM   2310  CA  VAL A1131      16.030 -19.294  40.409  1.00 92.71           C  
ANISOU 2310  CA  VAL A1131    12779  11404  11044  -4858   1755    513       C  
ATOM   2311  C   VAL A1131      17.210 -20.220  40.681  1.00 93.11           C  
ANISOU 2311  C   VAL A1131    13506  10845  11028  -4781   1726    899       C  
ATOM   2312  O   VAL A1131      17.533 -20.509  41.839  1.00 94.49           O  
ANISOU 2312  O   VAL A1131    13879  11018  11005  -4935   1900   1255       O  
ATOM   2313  CB  VAL A1131      14.728 -20.083  40.179  1.00 91.93           C  
ANISOU 2313  CB  VAL A1131    12455  11353  11120  -5514   1797    386       C  
ATOM   2314  N   ASN A1132      17.877 -20.696  39.626  1.00 98.73           N  
ANISOU 2314  N   ASN A1132    14580  11039  11893  -4528   1494    823       N  
ATOM   2315  CA  ASN A1132      19.028 -21.572  39.827  1.00 99.57           C  
ANISOU 2315  CA  ASN A1132    15279  10537  12016  -4371   1439   1132       C  
ATOM   2316  C   ASN A1132      20.208 -20.804  40.407  1.00 98.88           C  
ANISOU 2316  C   ASN A1132    15239  10564  11768  -3840   1452   1311       C  
ATOM   2317  O   ASN A1132      20.866 -21.282  41.338  1.00106.13           O  
ANISOU 2317  O   ASN A1132    16469  11262  12593  -3844   1482   1689       O  
ATOM   2318  CB  ASN A1132      19.417 -22.244  38.508  1.00100.70           C  
ANISOU 2318  CB  ASN A1132    15748  10141  12372  -4206   1226    906       C  
ATOM   2319  CG  ASN A1132      20.355 -23.432  38.702  1.00102.63           C  
ANISOU 2319  CG  ASN A1132    16592   9660  12743  -4136   1159   1173       C  
ATOM   2320  OD1 ASN A1132      21.259 -23.402  39.538  1.00 99.29           O  
ANISOU 2320  OD1 ASN A1132    16345   9141  12242  -3883   1185   1501       O  
ATOM   2321  ND2 ASN A1132      20.136 -24.489  37.929  1.00107.31           N  
ANISOU 2321  ND2 ASN A1132    17502   9719  13554  -4348   1034   1014       N  
ATOM   2322  N   LEU A1133      20.483 -19.606  39.881  1.00 85.10           N  
ANISOU 2322  N   LEU A1133    13195   9149   9988  -3405   1394   1062       N  
ATOM   2323  CA  LEU A1133      21.652 -18.849  40.317  1.00 79.83           C  
ANISOU 2323  CA  LEU A1133    12558   8566   9209  -2920   1377   1196       C  
ATOM   2324  C   LEU A1133      21.591 -18.470  41.792  1.00 85.06           C  
ANISOU 2324  C   LEU A1133    13112   9576   9629  -3048   1529   1445       C  
ATOM   2325  O   LEU A1133      22.638 -18.221  42.399  1.00 82.43           O  
ANISOU 2325  O   LEU A1133    12927   9198   9193  -2748   1484   1656       O  
ATOM   2326  CB  LEU A1133      21.813 -17.596  39.454  1.00 84.72           C  
ANISOU 2326  CB  LEU A1133    12879   9469   9842  -2527   1283    893       C  
ATOM   2327  CG  LEU A1133      22.459 -17.798  38.079  1.00 88.21           C  
ANISOU 2327  CG  LEU A1133    13529   9583  10405  -2245   1143    716       C  
ATOM   2328  CD1 LEU A1133      22.334 -16.537  37.242  1.00 90.94           C  
ANISOU 2328  CD1 LEU A1133    13587  10258  10710  -1997   1039    463       C  
ATOM   2329  CD2 LEU A1133      23.920 -18.203  38.219  1.00 83.43           C  
ANISOU 2329  CD2 LEU A1133    13242   8615   9844  -1895   1135    911       C  
ATOM   2330  N   ALA A1134      20.399 -18.433  42.386  1.00 84.49           N  
ANISOU 2330  N   ALA A1134    12774   9880   9449  -3501   1713   1404       N  
ATOM   2331  CA  ALA A1134      20.263 -18.129  43.804  1.00 83.30           C  
ANISOU 2331  CA  ALA A1134    12544  10115   8992  -3684   1912   1604       C  
ATOM   2332  C   ALA A1134      20.570 -19.322  44.697  1.00 95.28           C  
ANISOU 2332  C   ALA A1134    14547  11297  10359  -4027   1952   2087       C  
ATOM   2333  O   ALA A1134      20.536 -19.181  45.925  1.00100.46           O  
ANISOU 2333  O   ALA A1134    15234  12260  10675  -4222   2106   2315       O  
ATOM   2334  CB  ALA A1134      18.855 -17.614  44.103  1.00 88.70           C  
ANISOU 2334  CB  ALA A1134    12701  11389   9612  -4038   2147   1331       C  
ATOM   2335  N   LYS A1135      20.860 -20.486  44.116  1.00 88.10           N  
ANISOU 2335  N   LYS A1135    14044   9751   9678  -4109   1800   2243       N  
ATOM   2336  CA  LYS A1135      21.205 -21.680  44.871  1.00 87.20           C  
ANISOU 2336  CA  LYS A1135    14461   9179   9491  -4398   1755   2737       C  
ATOM   2337  C   LYS A1135      22.701 -21.967  44.852  1.00 86.32           C  
ANISOU 2337  C   LYS A1135    14744   8566   9488  -3866   1479   2966       C  
ATOM   2338  O   LYS A1135      23.109 -23.103  45.109  1.00102.38           O  
ANISOU 2338  O   LYS A1135    17270  10011  11619  -3979   1327   3328       O  
ATOM   2339  CB  LYS A1135      20.432 -22.884  44.332  1.00 91.82           C  
ANISOU 2339  CB  LYS A1135    15253   9320  10313  -4902   1752   2756       C  
ATOM   2340  N   SER A1136      23.523 -20.968  44.553  1.00 82.36           N  
ANISOU 2340  N   SER A1136    14022   8267   9005  -3296   1395   2765       N  
ATOM   2341  CA  SER A1136      24.959 -21.160  44.431  1.00 83.52           C  
ANISOU 2341  CA  SER A1136    14419   8004   9312  -2765   1149   2911       C  
ATOM   2342  C   SER A1136      25.684 -20.619  45.656  1.00 88.67           C  
ANISOU 2342  C   SER A1136    15092   8930   9667  -2607   1075   3205       C  
ATOM   2343  O   SER A1136      25.148 -19.816  46.424  1.00 92.03           O  
ANISOU 2343  O   SER A1136    15281   9935   9752  -2806   1240   3175       O  
ATOM   2344  CB  SER A1136      25.494 -20.477  43.171  1.00 79.24           C  
ANISOU 2344  CB  SER A1136    13626   7476   9007  -2270   1101   2495       C  
ATOM   2345  OG  SER A1136      25.423 -19.068  43.285  1.00 73.97           O  
ANISOU 2345  OG  SER A1136    12540   7401   8165  -2108   1183   2288       O  
ATOM   2346  N   ARG A1137      26.926 -21.078  45.832  1.00 91.39           N  
ANISOU 2346  N   ARG A1137    15712   8855  10158  -2229    806   3459       N  
ATOM   2347  CA  ARG A1137      27.767 -20.540  46.894  1.00 91.41           C  
ANISOU 2347  CA  ARG A1137    15721   9100   9909  -2019    652   3712       C  
ATOM   2348  C   ARG A1137      28.177 -19.101  46.613  1.00 85.85           C  
ANISOU 2348  C   ARG A1137    14558   8882   9179  -1656    695   3357       C  
ATOM   2349  O   ARG A1137      28.655 -18.413  47.521  1.00 85.58           O  
ANISOU 2349  O   ARG A1137    14453   9182   8883  -1561    604   3470       O  
ATOM   2350  CB  ARG A1137      29.009 -21.414  47.089  1.00 94.63           C  
ANISOU 2350  CB  ARG A1137    16484   8915  10557  -1666    293   4057       C  
ATOM   2351  N   TRP A1138      28.013 -18.639  45.372  1.00 85.61           N  
ANISOU 2351  N   TRP A1138    14253   8876   9400  -1476    803   2943       N  
ATOM   2352  CA  TRP A1138      28.240 -17.235  45.053  1.00 83.05           C  
ANISOU 2352  CA  TRP A1138    13523   8984   9049  -1214    846   2628       C  
ATOM   2353  C   TRP A1138      27.118 -16.360  45.596  1.00 83.65           C  
ANISOU 2353  C   TRP A1138    13343   9618   8821  -1522   1044   2460       C  
ATOM   2354  O   TRP A1138      27.378 -15.303  46.181  1.00 74.31           O  
ANISOU 2354  O   TRP A1138    11960   8813   7461  -1395   1022   2377       O  
ATOM   2355  CB  TRP A1138      28.387 -17.069  43.541  1.00 81.72           C  
ANISOU 2355  CB  TRP A1138    13205   8653   9191   -970    885   2291       C  
ATOM   2356  CG  TRP A1138      28.200 -15.675  43.038  1.00 80.37           C  
ANISOU 2356  CG  TRP A1138    12659   8893   8984   -845    952   1971       C  
ATOM   2357  CD1 TRP A1138      29.008 -14.601  43.270  1.00 79.75           C  
ANISOU 2357  CD1 TRP A1138    12375   9046   8880   -571    866   1931       C  
ATOM   2358  CD2 TRP A1138      27.151 -15.209  42.179  1.00 79.40           C  
ANISOU 2358  CD2 TRP A1138    12339   8950   8882   -990   1065   1659       C  
ATOM   2359  NE1 TRP A1138      28.520 -13.492  42.620  1.00 74.10           N  
ANISOU 2359  NE1 TRP A1138    11385   8600   8171   -543    925   1634       N  
ATOM   2360  CE2 TRP A1138      27.381 -13.840  41.944  1.00 77.74           C  
ANISOU 2360  CE2 TRP A1138    11841   9040   8657   -775   1031   1470       C  
ATOM   2361  CE3 TRP A1138      26.036 -15.814  41.592  1.00 70.14           C  
ANISOU 2361  CE3 TRP A1138    11201   7697   7754  -1292   1152   1527       C  
ATOM   2362  CZ2 TRP A1138      26.539 -13.069  41.149  1.00 75.61           C  
ANISOU 2362  CZ2 TRP A1138    11345   8968   8416   -815   1054   1185       C  
ATOM   2363  CZ3 TRP A1138      25.201 -15.044  40.801  1.00 72.99           C  
ANISOU 2363  CZ3 TRP A1138    11290   8307   8136  -1332   1174   1217       C  
ATOM   2364  CH2 TRP A1138      25.457 -13.689  40.588  1.00 72.54           C  
ANISOU 2364  CH2 TRP A1138    10974   8524   8064  -1078   1113   1063       C  
ATOM   2365  N   TYR A1139      25.867 -16.790  45.424  1.00 82.65           N  
ANISOU 2365  N   TYR A1139    13198   9549   8658  -1927   1233   2375       N  
ATOM   2366  CA  TYR A1139      24.743 -16.053  45.987  1.00 86.12           C  
ANISOU 2366  CA  TYR A1139    13337  10541   8845  -2219   1452   2182       C  
ATOM   2367  C   TYR A1139      24.771 -16.040  47.509  1.00 83.42           C  
ANISOU 2367  C   TYR A1139    13129  10492   8073  -2444   1516   2445       C  
ATOM   2368  O   TYR A1139      24.214 -15.122  48.120  1.00 85.20           O  
ANISOU 2368  O   TYR A1139    13075  11244   8055  -2528   1680   2223       O  
ATOM   2369  CB  TYR A1139      23.424 -16.647  45.483  1.00 93.06           C  
ANISOU 2369  CB  TYR A1139    14126  11418   9815  -2639   1632   2048       C  
ATOM   2370  CG  TYR A1139      22.187 -15.947  45.998  1.00 97.27           C  
ANISOU 2370  CG  TYR A1139    14256  12545  10156  -2931   1887   1793       C  
ATOM   2371  CD1 TYR A1139      21.714 -14.791  45.393  1.00 97.09           C  
ANISOU 2371  CD1 TYR A1139    13784  12829  10275  -2703   1891   1360       C  
ATOM   2372  CD2 TYR A1139      21.487 -16.449  47.086  1.00101.31           C  
ANISOU 2372  CD2 TYR A1139    14831  13310  10352  -3435   2125   1984       C  
ATOM   2373  CE1 TYR A1139      20.582 -14.152  45.862  1.00 98.45           C  
ANISOU 2373  CE1 TYR A1139    13534  13534  10340  -2906   2113   1072       C  
ATOM   2374  CE2 TYR A1139      20.357 -15.817  47.560  1.00102.23           C  
ANISOU 2374  CE2 TYR A1139    14515  14020  10307  -3689   2412   1691       C  
ATOM   2375  CZ  TYR A1139      19.909 -14.671  46.946  1.00 98.03           C  
ANISOU 2375  CZ  TYR A1139    13492  13774   9981  -3392   2400   1210       C  
ATOM   2376  OH  TYR A1139      18.781 -14.044  47.424  1.00 96.25           O  
ANISOU 2376  OH  TYR A1139    12784  14130   9656  -3586   2677    868       O  
ATOM   2377  N   ASN A1140      25.410 -17.028  48.134  1.00 84.98           N  
ANISOU 2377  N   ASN A1140    13766  10358   8165  -2531   1372   2902       N  
ATOM   2378  CA  ASN A1140      25.511 -17.069  49.585  1.00 81.09           C  
ANISOU 2378  CA  ASN A1140    13485  10139   7189  -2767   1384   3212       C  
ATOM   2379  C   ASN A1140      26.720 -16.316  50.123  1.00 81.14           C  
ANISOU 2379  C   ASN A1140    13495  10255   7081  -2354   1121   3259       C  
ATOM   2380  O   ASN A1140      26.732 -15.963  51.308  1.00 91.34           O  
ANISOU 2380  O   ASN A1140    14868  11933   7905  -2514   1139   3371       O  
ATOM   2381  CB  ASN A1140      25.564 -18.521  50.073  1.00 83.93           C  
ANISOU 2381  CB  ASN A1140    14351  10066   7474  -3090   1289   3738       C  
ATOM   2382  CG  ASN A1140      24.263 -19.268  49.834  1.00 88.69           C  
ANISOU 2382  CG  ASN A1140    14898  10646   8154  -3583   1553   3682       C  
ATOM   2383  OD1 ASN A1140      23.328 -19.182  50.631  1.00 94.13           O  
ANISOU 2383  OD1 ASN A1140    15427  11795   8542  -3964   1814   3633       O  
ATOM   2384  ND2 ASN A1140      24.203 -20.015  48.739  1.00 88.26           N  
ANISOU 2384  ND2 ASN A1140    14971  10056   8508  -3583   1485   3663       N  
ATOM   2385  N   GLN A1141      27.731 -16.058  49.292  1.00 79.05           N  
ANISOU 2385  N   GLN A1141    13135   9692   7209  -1861    889   3159       N  
ATOM   2386  CA  GLN A1141      28.944 -15.389  49.751  1.00 83.34           C  
ANISOU 2386  CA  GLN A1141    13640  10316   7710  -1493    612   3207       C  
ATOM   2387  C   GLN A1141      28.857 -13.872  49.622  1.00 86.83           C  
ANISOU 2387  C   GLN A1141    13669  11193   8130  -1321    691   2761       C  
ATOM   2388  O   GLN A1141      29.270 -13.148  50.534  1.00 90.33           O  
ANISOU 2388  O   GLN A1141    14085  11948   8290  -1274    578   2742       O  
ATOM   2389  CB  GLN A1141      30.158 -15.908  48.974  1.00 81.76           C  
ANISOU 2389  CB  GLN A1141    13505   9595   7966  -1066    339   3330       C  
ATOM   2390  N   THR A1142      28.341 -13.378  48.497  1.00 81.15           N  
ANISOU 2390  N   THR A1142    12660  10468   7708  -1228    841   2404       N  
ATOM   2391  CA  THR A1142      28.099 -11.952  48.276  1.00 75.62           C  
ANISOU 2391  CA  THR A1142    11594  10099   7040  -1081    896   1987       C  
ATOM   2392  C   THR A1142      26.654 -11.815  47.825  1.00 80.15           C  
ANISOU 2392  C   THR A1142    11953  10861   7638  -1313   1170   1698       C  
ATOM   2393  O   THR A1142      26.373 -11.645  46.629  1.00 76.21           O  
ANISOU 2393  O   THR A1142    11292  10208   7456  -1195   1180   1504       O  
ATOM   2394  CB  THR A1142      29.064 -11.368  47.245  1.00 71.01           C  
ANISOU 2394  CB  THR A1142    10854   9291   6836   -689    721   1873       C  
ATOM   2395  OG1 THR A1142      28.852 -12.004  45.979  1.00 61.90           O  
ANISOU 2395  OG1 THR A1142     9720   7819   5981   -656    792   1847       O  
ATOM   2396  CG2 THR A1142      30.507 -11.581  47.678  1.00 64.20           C  
ANISOU 2396  CG2 THR A1142    10120   8261   6011   -463    447   2144       C  
ATOM   2397  N   PRO A1143      25.702 -11.890  48.760  1.00 78.66           N  
ANISOU 2397  N   PRO A1143    11743  11039   7106  -1659   1396   1658       N  
ATOM   2398  CA  PRO A1143      24.288 -11.947  48.355  1.00 77.44           C  
ANISOU 2398  CA  PRO A1143    11332  11073   7019  -1917   1663   1400       C  
ATOM   2399  C   PRO A1143      23.754 -10.645  47.786  1.00 81.38           C  
ANISOU 2399  C   PRO A1143    11396  11793   7731  -1681   1672    913       C  
ATOM   2400  O   PRO A1143      22.964 -10.679  46.836  1.00 67.23           O  
ANISOU 2400  O   PRO A1143     9390   9947   6208  -1709   1715    723       O  
ATOM   2401  CB  PRO A1143      23.575 -12.337  49.655  1.00 74.02           C  
ANISOU 2401  CB  PRO A1143    10976  11033   6115  -2363   1931   1502       C  
ATOM   2402  CG  PRO A1143      24.484 -11.856  50.733  1.00 74.95           C  
ANISOU 2402  CG  PRO A1143    11275  11318   5883  -2235   1792   1614       C  
ATOM   2403  CD  PRO A1143      25.873 -12.037  50.213  1.00 80.85           C  
ANISOU 2403  CD  PRO A1143    12236  11590   6893  -1870   1423   1866       C  
ATOM   2404  N   ASN A1144      24.148  -9.498  48.346  1.00 79.84           N  
ANISOU 2404  N   ASN A1144    11080  11820   7435  -1453   1593    702       N  
ATOM   2405  CA  ASN A1144      23.656  -8.219  47.839  1.00 82.18           C  
ANISOU 2405  CA  ASN A1144    11000  12248   7977  -1203   1550    249       C  
ATOM   2406  C   ASN A1144      24.024  -8.031  46.372  1.00 83.32           C  
ANISOU 2406  C   ASN A1144    11122  12002   8536   -947   1323    262       C  
ATOM   2407  O   ASN A1144      23.168  -7.712  45.538  1.00 77.89           O  
ANISOU 2407  O   ASN A1144    10184  11322   8089   -907   1317     25       O  
ATOM   2408  CB  ASN A1144      24.209  -7.072  48.683  1.00 86.17           C  
ANISOU 2408  CB  ASN A1144    11466  12947   8328   -999   1448     44       C  
ATOM   2409  CG  ASN A1144      23.399  -6.831  49.942  1.00 91.58           C  
ANISOU 2409  CG  ASN A1144    12020  14149   8626  -1210   1730   -220       C  
ATOM   2410  OD1 ASN A1144      22.445  -6.054  49.938  1.00 89.43           O  
ANISOU 2410  OD1 ASN A1144    11378  14135   8467  -1137   1861   -680       O  
ATOM   2411  ND2 ASN A1144      23.778  -7.496  51.028  1.00 95.06           N  
ANISOU 2411  ND2 ASN A1144    12763  14756   8600  -1466   1818     62       N  
ATOM   2412  N   ARG A1145      25.302  -8.228  46.040  1.00 83.54           N  
ANISOU 2412  N   ARG A1145    11397  11711   8633   -780   1132    536       N  
ATOM   2413  CA  ARG A1145      25.740  -8.103  44.655  1.00 77.75           C  
ANISOU 2413  CA  ARG A1145    10673  10652   8215   -579    973    561       C  
ATOM   2414  C   ARG A1145      25.101  -9.167  43.774  1.00 76.82           C  
ANISOU 2414  C   ARG A1145    10624  10365   8200   -753   1062    630       C  
ATOM   2415  O   ARG A1145      24.721  -8.887  42.631  1.00 82.58           O  
ANISOU 2415  O   ARG A1145    11252  10993   9130   -675    981    488       O  
ATOM   2416  CB  ARG A1145      27.264  -8.189  44.587  1.00 73.67           C  
ANISOU 2416  CB  ARG A1145    10353   9896   7744   -393    814    816       C  
ATOM   2417  CG  ARG A1145      27.829  -8.227  43.179  1.00 69.75           C  
ANISOU 2417  CG  ARG A1145     9893   9104   7505   -234    729    865       C  
ATOM   2418  CD  ARG A1145      29.352  -8.232  43.189  1.00 73.59           C  
ANISOU 2418  CD  ARG A1145    10468   9428   8064    -50    612   1067       C  
ATOM   2419  NE  ARG A1145      29.897  -8.135  41.837  1.00 80.75           N  
ANISOU 2419  NE  ARG A1145    11375  10131   9175     79    594   1070       N  
ATOM   2420  CZ  ARG A1145      31.175  -7.901  41.556  1.00 82.83           C  
ANISOU 2420  CZ  ARG A1145    11612  10298   9561    237    528   1175       C  
ATOM   2421  NH1 ARG A1145      32.054  -7.734  42.535  1.00 82.57           N  
ANISOU 2421  NH1 ARG A1145    11535  10328   9508    307    415   1287       N  
ATOM   2422  NH2 ARG A1145      31.574  -7.829  40.293  1.00 85.74           N  
ANISOU 2422  NH2 ARG A1145    11982  10541  10053    302    578   1158       N  
ATOM   2423  N   ALA A1146      24.974 -10.393  44.287  1.00 78.38           N  
ANISOU 2423  N   ALA A1146    11025  10507   8249  -1011   1196    857       N  
ATOM   2424  CA  ALA A1146      24.412 -11.480  43.491  1.00 77.28           C  
ANISOU 2424  CA  ALA A1146    10992  10148   8224  -1212   1259    913       C  
ATOM   2425  C   ALA A1146      22.965 -11.191  43.114  1.00 83.69           C  
ANISOU 2425  C   ALA A1146    11482  11202   9113  -1389   1341    610       C  
ATOM   2426  O   ALA A1146      22.575 -11.340  41.951  1.00 81.20           O  
ANISOU 2426  O   ALA A1146    11127  10738   8988  -1380   1252    495       O  
ATOM   2427  CB  ALA A1146      24.519 -12.800  44.253  1.00 75.31           C  
ANISOU 2427  CB  ALA A1146    11049   9751   7813  -1491   1359   1239       C  
ATOM   2428  N   LYS A1147      22.154 -10.771  44.090  1.00 81.29           N  
ANISOU 2428  N   LYS A1147    10927  11303   8657  -1547   1506    451       N  
ATOM   2429  CA  LYS A1147      20.760 -10.442  43.804  1.00 80.52           C  
ANISOU 2429  CA  LYS A1147    10420  11486   8686  -1680   1585    116       C  
ATOM   2430  C   LYS A1147      20.649  -9.302  42.799  1.00 83.83           C  
ANISOU 2430  C   LYS A1147    10611  11866   9377  -1325   1329   -152       C  
ATOM   2431  O   LYS A1147      19.710  -9.273  41.995  1.00 68.30           O  
ANISOU 2431  O   LYS A1147     8403   9940   7609  -1375   1246   -350       O  
ATOM   2432  CB  LYS A1147      20.023 -10.088  45.098  1.00 67.35           C  
ANISOU 2432  CB  LYS A1147     8483  10311   6797  -1863   1853    -63       C  
ATOM   2433  N   ARG A1148      21.599  -8.365  42.815  1.00 85.54           N  
ANISOU 2433  N   ARG A1148    10910  11984   9606   -988   1167   -140       N  
ATOM   2434  CA  ARG A1148      21.574  -7.277  41.842  1.00 79.68           C  
ANISOU 2434  CA  ARG A1148    10031  11139   9107   -685    892   -317       C  
ATOM   2435  C   ARG A1148      21.891  -7.783  40.437  1.00 82.33           C  
ANISOU 2435  C   ARG A1148    10589  11152   9539   -673    733   -165       C  
ATOM   2436  O   ARG A1148      21.289  -7.330  39.457  1.00 90.33           O  
ANISOU 2436  O   ARG A1148    11469  12136  10717   -591    526   -312       O  
ATOM   2437  CB  ARG A1148      22.555  -6.182  42.261  1.00 70.66           C  
ANISOU 2437  CB  ARG A1148     8952   9944   7952   -403    768   -316       C  
ATOM   2438  CG  ARG A1148      21.892  -4.860  42.620  1.00 71.12           C  
ANISOU 2438  CG  ARG A1148     8676  10192   8155   -198    669   -688       C  
ATOM   2439  CD  ARG A1148      22.475  -4.260  43.892  1.00 73.19           C  
ANISOU 2439  CD  ARG A1148     8962  10601   8247   -122    743   -769       C  
ATOM   2440  NE  ARG A1148      23.934  -4.303  43.899  1.00 73.07           N  
ANISOU 2440  NE  ARG A1148     9271  10346   8145    -63    641   -461       N  
ATOM   2441  CZ  ARG A1148      24.686  -4.003  44.953  1.00 72.04           C  
ANISOU 2441  CZ  ARG A1148     9236  10306   7829    -40    656   -444       C  
ATOM   2442  NH1 ARG A1148      24.121  -3.632  46.093  1.00 77.77           N  
ANISOU 2442  NH1 ARG A1148     9809  11363   8378    -79    795   -729       N  
ATOM   2443  NH2 ARG A1148      26.005  -4.075  44.867  1.00 70.75           N  
ANISOU 2443  NH2 ARG A1148     9301   9933   7647     15    532   -167       N  
ATOM   2444  N   VAL A1149      22.824  -8.727  40.321  1.00 86.59           N  
ANISOU 2444  N   VAL A1149    11473  11454   9974   -742    812    112       N  
ATOM   2445  CA  VAL A1149      23.201  -9.252  39.011  1.00 82.53           C  
ANISOU 2445  CA  VAL A1149    11189  10655   9513   -723    713    200       C  
ATOM   2446  C   VAL A1149      22.160 -10.240  38.500  1.00 89.46           C  
ANISOU 2446  C   VAL A1149    12052  11515  10424  -1007    747    112       C  
ATOM   2447  O   VAL A1149      21.841 -10.260  37.304  1.00 88.71           O  
ANISOU 2447  O   VAL A1149    11995  11326  10387  -1003    583     17       O  
ATOM   2448  CB  VAL A1149      24.603  -9.881  39.089  1.00 69.15           C  
ANISOU 2448  CB  VAL A1149     9812   8710   7751   -638    790    459       C  
ATOM   2449  CG1 VAL A1149      24.961 -10.583  37.793  1.00 62.41           C  
ANISOU 2449  CG1 VAL A1149     9197   7590   6927   -632    765    483       C  
ATOM   2450  CG2 VAL A1149      25.636  -8.812  39.423  1.00 65.57           C  
ANISOU 2450  CG2 VAL A1149     9323   8286   7303   -385    710    522       C  
ATOM   2451  N   ILE A1150      21.606 -11.063  39.394  1.00 84.73           N  
ANISOU 2451  N   ILE A1150    11413  11014   9767  -1295    945    151       N  
ATOM   2452  CA  ILE A1150      20.566 -12.008  38.997  1.00 83.24           C  
ANISOU 2452  CA  ILE A1150    11179  10809   9639  -1639    980     64       C  
ATOM   2453  C   ILE A1150      19.315 -11.263  38.545  1.00 84.16           C  
ANISOU 2453  C   ILE A1150    10861  11211   9905  -1651    831   -246       C  
ATOM   2454  O   ILE A1150      18.622 -11.692  37.612  1.00 93.69           O  
ANISOU 2454  O   ILE A1150    12028  12360  11209  -1807    688   -369       O  
ATOM   2455  CB  ILE A1150      20.272 -12.986  40.152  1.00 84.83           C  
ANISOU 2455  CB  ILE A1150    11442  11060   9730  -2003   1240    225       C  
ATOM   2456  CG1 ILE A1150      21.486 -13.878  40.414  1.00 82.12           C  
ANISOU 2456  CG1 ILE A1150    11568  10333   9299  -1964   1285    553       C  
ATOM   2457  CG2 ILE A1150      19.059 -13.839  39.844  1.00 86.81           C  
ANISOU 2457  CG2 ILE A1150    11564  11344  10076  -2432   1287    113       C  
ATOM   2458  CD1 ILE A1150      21.367 -14.717  41.663  1.00 70.60           C  
ANISOU 2458  CD1 ILE A1150    10253   8891   7682  -2294   1484    806       C  
ATOM   2459  N   THR A1151      19.009 -10.131  39.188  1.00 79.62           N  
ANISOU 2459  N   THR A1151     9946  10934   9371  -1467    829   -404       N  
ATOM   2460  CA  THR A1151      17.920  -9.283  38.713  1.00 85.27           C  
ANISOU 2460  CA  THR A1151    10223  11875  10301  -1363    618   -716       C  
ATOM   2461  C   THR A1151      18.194  -8.785  37.302  1.00 88.73           C  
ANISOU 2461  C   THR A1151    10820  12078  10815  -1128    245   -709       C  
ATOM   2462  O   THR A1151      17.290  -8.744  36.460  1.00 89.80           O  
ANISOU 2462  O   THR A1151    10761  12268  11090  -1177     -2   -876       O  
ATOM   2463  CB  THR A1151      17.713  -8.098  39.655  1.00 85.11           C  
ANISOU 2463  CB  THR A1151     9861  12141  10338  -1127    668   -919       C  
ATOM   2464  OG1 THR A1151      17.364  -8.577  40.957  1.00 90.34           O  
ANISOU 2464  OG1 THR A1151    10377  13098  10849  -1398   1046   -947       O  
ATOM   2465  CG2 THR A1151      16.602  -7.194  39.144  1.00 80.06           C  
ANISOU 2465  CG2 THR A1151     8743  11680   9998   -942    398  -1262       C  
ATOM   2466  N   THR A1152      19.440  -8.402  37.023  1.00 89.05           N  
ANISOU 2466  N   THR A1152    11208  11880  10745   -898    191   -508       N  
ATOM   2467  CA  THR A1152      19.772  -7.948  35.679  1.00 88.03           C  
ANISOU 2467  CA  THR A1152    11283  11556  10607   -736   -114   -459       C  
ATOM   2468  C   THR A1152      19.666  -9.080  34.665  1.00 84.57           C  
ANISOU 2468  C   THR A1152    11105  10963  10066   -967   -143   -432       C  
ATOM   2469  O   THR A1152      19.276  -8.846  33.516  1.00 88.93           O  
ANISOU 2469  O   THR A1152    11704  11483  10603   -948   -442   -501       O  
ATOM   2470  CB  THR A1152      21.170  -7.335  35.670  1.00 84.93           C  
ANISOU 2470  CB  THR A1152    11169  10986  10115   -508    -96   -248       C  
ATOM   2471  OG1 THR A1152      21.238  -6.314  36.674  1.00 87.26           O  
ANISOU 2471  OG1 THR A1152    11240  11404  10511   -322    -88   -315       O  
ATOM   2472  CG2 THR A1152      21.473  -6.721  34.321  1.00 75.79           C  
ANISOU 2472  CG2 THR A1152    10215   9677   8903   -385   -386   -175       C  
ATOM   2473  N   PHE A1153      19.988 -10.311  35.069  1.00 80.31           N  
ANISOU 2473  N   PHE A1153    10763  10305   9447  -1189    130   -341       N  
ATOM   2474  CA  PHE A1153      19.838 -11.445  34.163  1.00 86.85           C  
ANISOU 2474  CA  PHE A1153    11850  10938  10209  -1417    102   -378       C  
ATOM   2475  C   PHE A1153      18.375 -11.753  33.876  1.00 94.28           C  
ANISOU 2475  C   PHE A1153    12493  12048  11280  -1692    -61   -605       C  
ATOM   2476  O   PHE A1153      18.051 -12.271  32.802  1.00 97.03           O  
ANISOU 2476  O   PHE A1153    13001  12289  11578  -1834   -250   -712       O  
ATOM   2477  CB  PHE A1153      20.524 -12.681  34.744  1.00 85.98           C  
ANISOU 2477  CB  PHE A1153    12033  10584  10052  -1564    394   -224       C  
ATOM   2478  CG  PHE A1153      21.973 -12.790  34.388  1.00 82.81           C  
ANISOU 2478  CG  PHE A1153    11993   9932   9541  -1323    479    -73       C  
ATOM   2479  CD1 PHE A1153      22.400 -12.549  33.096  1.00 87.89           C  
ANISOU 2479  CD1 PHE A1153    12840  10494  10062  -1196    348   -140       C  
ATOM   2480  CD2 PHE A1153      22.908 -13.132  35.345  1.00 77.41           C  
ANISOU 2480  CD2 PHE A1153    11425   9126   8862  -1234    685    132       C  
ATOM   2481  CE1 PHE A1153      23.735 -12.650  32.764  1.00 85.44           C  
ANISOU 2481  CE1 PHE A1153    12792  10012   9660   -991    485    -39       C  
ATOM   2482  CE2 PHE A1153      24.244 -13.233  35.021  1.00 77.07           C  
ANISOU 2482  CE2 PHE A1153    11625   8883   8776   -993    759    238       C  
ATOM   2483  CZ  PHE A1153      24.658 -12.992  33.729  1.00 80.39           C  
ANISOU 2483  CZ  PHE A1153    12194   9251   9099   -874    690    135       C  
ATOM   2484  N   ARG A1154      17.484 -11.446  34.817  1.00 88.53           N  
ANISOU 2484  N   ARG A1154    11311  11612  10713  -1783     15   -710       N  
ATOM   2485  CA  ARG A1154      16.070 -11.771  34.679  1.00 90.56           C  
ANISOU 2485  CA  ARG A1154    11175  12087  11146  -2076    -96   -944       C  
ATOM   2486  C   ARG A1154      15.287 -10.657  33.990  1.00 94.08           C  
ANISOU 2486  C   ARG A1154    11255  12736  11753  -1845   -507  -1151       C  
ATOM   2487  O   ARG A1154      14.589 -10.908  33.004  1.00 98.43           O  
ANISOU 2487  O   ARG A1154    11752  13292  12353  -1977   -823  -1290       O  
ATOM   2488  CB  ARG A1154      15.471 -12.072  36.056  1.00 91.66           C  
ANISOU 2488  CB  ARG A1154    10967  12492  11368  -2333    250   -973       C  
ATOM   2489  CG  ARG A1154      13.953 -12.110  36.087  1.00 98.75           C  
ANISOU 2489  CG  ARG A1154    11273  13741  12505  -2600    179  -1261       C  
ATOM   2490  CD  ARG A1154      13.450 -12.527  37.460  1.00 98.15           C  
ANISOU 2490  CD  ARG A1154    10903  13957  12432  -2937    616  -1264       C  
ATOM   2491  NE  ARG A1154      14.141 -11.809  38.526  1.00 96.23           N  
ANISOU 2491  NE  ARG A1154    10691  13830  12042  -2666    855  -1169       N  
ATOM   2492  CZ  ARG A1154      13.729 -10.656  39.043  1.00 99.35           C  
ANISOU 2492  CZ  ARG A1154    10627  14571  12550  -2384    862  -1413       C  
ATOM   2493  NH1 ARG A1154      12.618 -10.085  38.594  1.00102.81           N1+
ANISOU 2493  NH1 ARG A1154    10503  15271  13290  -2299    634  -1752       N1+
ATOM   2494  NH2 ARG A1154      14.426 -10.074  40.011  1.00 97.58           N  
ANISOU 2494  NH2 ARG A1154    10500  14418  12157  -2171   1067  -1343       N  
ATOM   2495  N   THR A1155      15.394  -9.425  34.492  1.00 91.70           N  
ANISOU 2495  N   THR A1155    10720  12575  11545  -1493   -553  -1180       N  
ATOM   2496  CA  THR A1155      14.626  -8.327  33.913  1.00 95.66           C  
ANISOU 2496  CA  THR A1155    10869  13211  12265  -1227   -991  -1368       C  
ATOM   2497  C   THR A1155      15.189  -7.887  32.570  1.00 97.84           C  
ANISOU 2497  C   THR A1155    11567  13229  12380  -1038  -1391  -1215       C  
ATOM   2498  O   THR A1155      14.426  -7.500  31.678  1.00103.63           O  
ANISOU 2498  O   THR A1155    12148  14011  13216   -975  -1852  -1325       O  
ATOM   2499  CB  THR A1155      14.590  -7.135  34.871  1.00 96.53           C  
ANISOU 2499  CB  THR A1155    10639  13482  12554   -890   -932  -1480       C  
ATOM   2500  OG1 THR A1155      15.865  -6.481  34.875  1.00 89.26           O  
ANISOU 2500  OG1 THR A1155    10139  12306  11469   -624   -926  -1243       O  
ATOM   2501  CG2 THR A1155      14.254  -7.597  36.282  1.00102.13           C  
ANISOU 2501  CG2 THR A1155    11038  14480  13285  -1108   -443  -1599       C  
ATOM   2502  N   GLY A1156      16.506  -7.938  32.402  1.00 98.59           N  
ANISOU 2502  N   GLY A1156    12176  13074  12209   -961  -1232   -958       N  
ATOM   2503  CA  GLY A1156      17.109  -7.426  31.192  1.00 97.17           C  
ANISOU 2503  CA  GLY A1156    12393  12702  11824   -813  -1538   -796       C  
ATOM   2504  C   GLY A1156      17.208  -5.922  31.139  1.00 94.99           C  
ANISOU 2504  C   GLY A1156    12028  12391  11674   -459  -1843   -727       C  
ATOM   2505  O   GLY A1156      17.414  -5.364  30.057  1.00 94.83           O  
ANISOU 2505  O   GLY A1156    12287  12241  11502   -370  -2199   -582       O  
ATOM   2506  N   THR A1157      17.055  -5.243  32.275  1.00 98.59           N  
ANISOU 2506  N   THR A1157    12130  12944  12386   -269  -1724   -831       N  
ATOM   2507  CA  THR A1157      17.188  -3.793  32.334  1.00 99.99           C  
ANISOU 2507  CA  THR A1157    12241  13012  12740     83  -2014   -798       C  
ATOM   2508  C   THR A1157      18.117  -3.396  33.475  1.00 95.58           C  
ANISOU 2508  C   THR A1157    11722  12408  12187    197  -1666   -741       C  
ATOM   2509  O   THR A1157      18.739  -4.258  34.103  1.00 99.83           O  
ANISOU 2509  O   THR A1157    12385  12993  12552     13  -1238   -673       O  
ATOM   2510  CB  THR A1157      15.819  -3.130  32.503  1.00100.53           C  
ANISOU 2510  CB  THR A1157    11744  13243  13210    283  -2359  -1106       C  
ATOM   2511  N   TRP A1158      18.225  -2.094  33.747  1.00 93.22           N  
ANISOU 2511  N   TRP A1158    11337  11987  12095    500  -1890   -770       N  
ATOM   2512  CA  TRP A1158      19.077  -1.577  34.810  1.00 93.29           C  
ANISOU 2512  CA  TRP A1158    11380  11944  12121    611  -1638   -757       C  
ATOM   2513  C   TRP A1158      18.284  -1.180  36.050  1.00100.83           C  
ANISOU 2513  C   TRP A1158    11839  13130  13343    767  -1520  -1143       C  
ATOM   2514  O   TRP A1158      18.687  -0.262  36.773  1.00104.41           O  
ANISOU 2514  O   TRP A1158    12262  13494  13913    976  -1523  -1234       O  
ATOM   2515  CB  TRP A1158      19.888  -0.380  34.315  1.00 93.24           C  
ANISOU 2515  CB  TRP A1158    11675  11603  12148    796  -1939   -534       C  
ATOM   2516  CG  TRP A1158      20.831  -0.689  33.202  1.00 90.86           C  
ANISOU 2516  CG  TRP A1158    11861  11134  11527    615  -1955   -159       C  
ATOM   2517  CD1 TRP A1158      20.661  -0.401  31.878  1.00 92.31           C  
ANISOU 2517  CD1 TRP A1158    12294  11175  11605    591  -2335     30       C  
ATOM   2518  CD2 TRP A1158      22.100  -1.341  33.312  1.00 84.64           C  
ANISOU 2518  CD2 TRP A1158    11359  10335  10467    435  -1569     52       C  
ATOM   2519  NE1 TRP A1158      21.746  -0.835  31.158  1.00 87.61           N  
ANISOU 2519  NE1 TRP A1158    12125  10516  10649    382  -2146    322       N  
ATOM   2520  CE2 TRP A1158      22.643  -1.417  32.015  1.00 81.33           C  
ANISOU 2520  CE2 TRP A1158    11324   9793   9787    307  -1675    322       C  
ATOM   2521  CE3 TRP A1158      22.829  -1.871  34.381  1.00 79.01           C  
ANISOU 2521  CE3 TRP A1158    10605   9715   9699    377  -1161     35       C  
ATOM   2522  CZ2 TRP A1158      23.881  -2.001  31.759  1.00 77.25           C  
ANISOU 2522  CZ2 TRP A1158    11088   9260   9004    149  -1343    521       C  
ATOM   2523  CZ3 TRP A1158      24.059  -2.452  34.124  1.00 69.87           C  
ANISOU 2523  CZ3 TRP A1158     9733   8502   8314    244   -903    268       C  
ATOM   2524  CH2 TRP A1158      24.572  -2.511  32.824  1.00 69.73           C  
ANISOU 2524  CH2 TRP A1158    10033   8375   8085    144   -972    482       C  
ATOM   2525  N   ASP A1159      17.156  -1.850  36.306  1.00 98.45           N  
ANISOU 2525  N   ASP A1159    11135  13138  13133    646  -1402  -1399       N  
ATOM   2526  CA  ASP A1159      16.331  -1.497  37.457  1.00 97.23           C  
ANISOU 2526  CA  ASP A1159    10456  13283  13205    769  -1227  -1814       C  
ATOM   2527  C   ASP A1159      17.098  -1.638  38.765  1.00 90.66           C  
ANISOU 2527  C   ASP A1159     9725  12569  12151    685   -774  -1819       C  
ATOM   2528  O   ASP A1159      16.820  -0.916  39.727  1.00 92.33           O  
ANISOU 2528  O   ASP A1159     9651  12933  12497    879   -679  -2146       O  
ATOM   2529  CB  ASP A1159      15.076  -2.368  37.498  1.00105.69           C  
ANISOU 2529  CB  ASP A1159    11073  14718  14366    540  -1095  -2046       C  
ATOM   2530  CG  ASP A1159      14.329  -2.379  36.182  1.00109.35           C  
ANISOU 2530  CG  ASP A1159    11447  15092  15007    573  -1581  -2031       C  
ATOM   2531  OD1 ASP A1159      14.839  -2.991  35.220  1.00106.95           O1+
ANISOU 2531  OD1 ASP A1159    11588  14593  14457    378  -1693  -1714       O1+
ATOM   2532  OD2 ASP A1159      13.231  -1.786  36.115  1.00113.68           O  
ANISOU 2532  OD2 ASP A1159    11472  15783  15940    804  -1860  -2361       O  
ATOM   2533  N   ALA A1160      18.061  -2.558  38.822  1.00 90.75           N  
ANISOU 2533  N   ALA A1160    10142  12514  11824    416   -516  -1483       N  
ATOM   2534  CA  ALA A1160      18.793  -2.777  40.062  1.00 83.07           C  
ANISOU 2534  CA  ALA A1160     9285  11661  10616    322   -147  -1445       C  
ATOM   2535  C   ALA A1160      19.805  -1.671  40.330  1.00 83.07           C  
ANISOU 2535  C   ALA A1160     9492  11427  10644    577   -301  -1398       C  
ATOM   2536  O   ALA A1160      20.159  -1.427  41.488  1.00 80.26           O  
ANISOU 2536  O   ALA A1160     9111  11213  10170    595    -98  -1520       O  
ATOM   2537  CB  ALA A1160      19.490  -4.133  40.023  1.00 69.19           C  
ANISOU 2537  CB  ALA A1160     7878   9858   8554     -5    110  -1098       C  
ATOM   2538  N   TYR A1161      20.270  -0.989  39.289  1.00 85.89           N  
ANISOU 2538  N   TYR A1161    10067  11436  11131    737   -663  -1221       N  
ATOM   2539  CA  TYR A1161      21.312   0.021  39.439  1.00 81.29           C  
ANISOU 2539  CA  TYR A1161     9712  10587  10590    902   -820  -1122       C  
ATOM   2540  C   TYR A1161      20.830   1.413  39.031  1.00 86.56           C  
ANISOU 2540  C   TYR A1161    10259  11009  11620   1221  -1257  -1309       C  
ATOM   2541  O   TYR A1161      19.780   1.882  39.473  1.00 90.75           O  
ANISOU 2541  O   TYR A1161    10405  11678  12398   1423  -1325  -1710       O  
ATOM   2542  CB  TYR A1161      22.541  -0.357  38.608  1.00 78.82           C  
ANISOU 2542  CB  TYR A1161     9822  10037  10089    757   -833   -681       C  
ATOM   2543  CG  TYR A1161      23.144  -1.708  38.932  1.00 79.07           C  
ANISOU 2543  CG  TYR A1161    10004  10209   9831    508   -467   -486       C  
ATOM   2544  CD1 TYR A1161      22.612  -2.876  38.400  1.00 78.87           C  
ANISOU 2544  CD1 TYR A1161     9993  10274   9701    320   -342   -427       C  
ATOM   2545  CD2 TYR A1161      24.263  -1.813  39.748  1.00 75.01           C  
ANISOU 2545  CD2 TYR A1161     9629   9697   9174    468   -297   -359       C  
ATOM   2546  CE1 TYR A1161      23.166  -4.110  38.683  1.00 74.50           C  
ANISOU 2546  CE1 TYR A1161     9613   9760   8934    118    -53   -248       C  
ATOM   2547  CE2 TYR A1161      24.824  -3.042  40.039  1.00 67.83           C  
ANISOU 2547  CE2 TYR A1161     8865   8860   8048    288    -30   -162       C  
ATOM   2548  CZ  TYR A1161      24.272  -4.189  39.504  1.00 71.43           C  
ANISOU 2548  CZ  TYR A1161     9359   9354   8428    123     94   -104       C  
ATOM   2549  OH  TYR A1161      24.829  -5.416  39.787  1.00 69.66           O  
ANISOU 2549  OH  TYR A1161     9313   9118   8037    -32    319     91       O  
ATOM   2550  N   SER A 364      17.508   3.047  36.367  1.00104.00           N  
ATOM   2551  CA  SER A 364      18.568   3.670  35.585  1.00104.92           C  
ATOM   2552  C   SER A 364      18.623   3.097  34.167  1.00111.72           C  
ATOM   2553  O   SER A 364      19.675   3.111  33.526  1.00111.66           O  
ATOM   2554  CB  SER A 364      19.919   3.488  36.282  1.00 97.65           C  
ATOM   2555  N   GLN A 365      17.486   2.600  33.682  1.00122.15           N  
ATOM   2556  CA  GLN A 365      17.397   1.937  32.386  1.00115.38           C  
ATOM   2557  C   GLN A 365      16.553   2.767  31.428  1.00110.61           C  
ATOM   2558  O   GLN A 365      15.419   3.137  31.753  1.00 98.43           O  
ATOM   2559  CB  GLN A 365      16.796   0.536  32.527  1.00106.22           C  
ATOM   2560  N   GLN A 366      17.101   3.039  30.246  1.00120.06           N  
ATOM   2561  CA  GLN A 366      16.385   3.791  29.223  1.00115.06           C  
ATOM   2562  C   GLN A 366      15.363   2.887  28.544  1.00110.82           C  
ATOM   2563  O   GLN A 366      15.719   1.836  27.999  1.00106.83           O  
ATOM   2564  CB  GLN A 366      17.364   4.363  28.199  1.00114.61           C  
ATOM   2565  N   LYS A 367      14.097   3.295  28.574  1.00106.95           N  
ATOM   2566  CA  LYS A 367      13.014   2.529  27.974  1.00112.85           C  
ATOM   2567  C   LYS A 367      12.771   2.895  26.516  1.00109.20           C  
ATOM   2568  O   LYS A 367      11.803   2.410  25.921  1.00103.35           O  
ATOM   2569  CB  LYS A 367      11.727   2.721  28.781  1.00115.42           C  
ATOM   2570  N   GLU A 368      13.626   3.733  25.930  1.00114.20           N  
ATOM   2571  CA  GLU A 368      13.436   4.206  24.566  1.00 99.97           C  
ATOM   2572  C   GLU A 368      14.152   3.361  23.525  1.00100.67           C  
ATOM   2573  O   GLU A 368      13.805   3.444  22.342  1.00 97.34           O  
ATOM   2574  CB  GLU A 368      13.920   5.655  24.437  1.00 81.44           C  
ATOM   2575  CG  GLU A 368      13.087   6.681  25.188  1.00 79.48           C  
ATOM   2576  CD  GLU A 368      11.923   7.216  24.368  1.00 87.69           C  
ATOM   2577  OE1 GLU A 368      11.484   6.529  23.419  1.00 87.57           O  
ATOM   2578  OE2 GLU A 368      11.451   8.332  24.674  1.00 90.78           O  
ATOM   2579  N   LYS A 369      15.139   2.557  23.932  1.00101.97           N  
ATOM   2580  CA  LYS A 369      15.965   1.842  22.963  1.00 93.96           C  
ATOM   2581  C   LYS A 369      15.123   0.959  22.051  1.00 87.89           C  
ATOM   2582  O   LYS A 369      15.377   0.886  20.844  1.00 84.82           O  
ATOM   2583  CB  LYS A 369      17.025   1.012  23.689  1.00 94.15           C  
ATOM   2584  N   LYS A 370      14.107   0.291  22.605  1.00 95.07           N  
ATOM   2585  CA  LYS A 370      13.254  -0.567  21.787  1.00 92.51           C  
ATOM   2586  C   LYS A 370      12.587   0.220  20.665  1.00 85.60           C  
ATOM   2587  O   LYS A 370      12.454  -0.280  19.541  1.00 77.93           O  
ATOM   2588  CB  LYS A 370      12.203  -1.254  22.662  1.00 85.65           C  
ATOM   2589  N   ALA A 371      12.167   1.454  20.944  1.00 85.70           N  
ATOM   2590  CA  ALA A 371      11.556   2.271  19.901  1.00 78.85           C  
ATOM   2591  C   ALA A 371      12.589   2.776  18.902  1.00 73.40           C  
ATOM   2592  O   ALA A 371      12.274   2.940  17.718  1.00 67.94           O  
ATOM   2593  CB  ALA A 371      10.805   3.440  20.520  1.00 20.00           C  
ATOM   2594  N   THR A 372      13.820   3.030  19.357  1.00 75.36           N  
ATOM   2595  CA  THR A 372      14.875   3.470  18.451  1.00 64.07           C  
ATOM   2596  C   THR A 372      15.326   2.343  17.535  1.00 71.79           C  
ATOM   2597  O   THR A 372      15.714   2.593  16.389  1.00 80.74           O  
ATOM   2598  CB  THR A 372      16.066   4.010  19.246  1.00 69.33           C  
ATOM   2599  OG1 THR A 372      15.634   5.071  20.104  1.00 74.68           O  
ATOM   2600  CG2 THR A 372      17.138   4.544  18.316  1.00 68.04           C  
ATOM   2601  N   GLN A 373      15.283   1.100  18.019  1.00 68.72           N  
ATOM   2602  CA  GLN A 373      15.663  -0.031  17.180  1.00 79.96           C  
ATOM   2603  C   GLN A 373      14.624  -0.283  16.095  1.00 79.40           C  
ATOM   2604  O   GLN A 373      14.972  -0.633  14.961  1.00 75.09           O  
ATOM   2605  CB  GLN A 373      15.857  -1.276  18.043  1.00 95.27           C  
ATOM   2606  CG  GLN A 373      17.006  -1.162  19.028  1.00107.01           C  
ATOM   2607  CD  GLN A 373      16.835  -2.074  20.228  1.00113.19           C  
ATOM   2608  OE1 GLN A 373      15.768  -2.652  20.438  1.00109.22           O  
ATOM   2609  NE2 GLN A 373      17.889  -2.204  21.025  1.00117.08           N  
ATOM   2610  N   MET A 374      13.345  -0.105  16.421  1.00 79.17           N  
ATOM   2611  CA  MET A 374      12.307  -0.277  15.413  1.00 76.40           C  
ATOM   2612  C   MET A 374      12.384   0.814  14.350  1.00 70.69           C  
ATOM   2613  O   MET A 374      12.182   0.543  13.160  1.00 68.25           O  
ATOM   2614  CB  MET A 374      10.934  -0.292  16.079  1.00 77.49           C  
ATOM   2615  CG  MET A 374       9.801  -0.689  15.153  1.00 81.14           C  
ATOM   2616  SD  MET A 374       8.219  -0.741  16.009  1.00 84.97           S  
ATOM   2617  CE  MET A 374       8.086   0.958  16.565  1.00103.28           C  
ATOM   2618  N   ALA A 375      12.684   2.052  14.756  1.00 72.85           N  
ATOM   2619  CA  ALA A 375      12.789   3.144  13.793  1.00 69.01           C  
ATOM   2620  C   ALA A 375      13.899   2.887  12.783  1.00 71.99           C  
ATOM   2621  O   ALA A 375      13.756   3.203  11.596  1.00 68.65           O  
ATOM   2622  CB  ALA A 375      13.021   4.464  14.513  1.00 20.00           C  
ATOM   2623  N   ALA A 376      15.014   2.312  13.234  1.00 72.30           N  
ATOM   2624  CA  ALA A 376      16.110   2.018  12.320  1.00 74.21           C  
ATOM   2625  C   ALA A 376      15.790   0.830  11.427  1.00 77.19           C  
ATOM   2626  O   ALA A 376      16.261   0.771  10.285  1.00 87.02           O  
ATOM   2627  CB  ALA A 376      17.398   1.765  13.104  1.00 74.32           C  
ATOM   2628  N   ILE A 377      15.001  -0.125  11.921  1.00 87.67           N  
ATOM   2629  CA  ILE A 377      14.633  -1.265  11.089  1.00 95.90           C  
ATOM   2630  C   ILE A 377      13.706  -0.839   9.957  1.00101.03           C  
ATOM   2631  O   ILE A 377      13.826  -1.331   8.830  1.00 92.85           O  
ATOM   2632  CB  ILE A 377      13.963  -2.361  11.939  1.00 20.00           C  
ATOM   2633  CG1 ILE A 377      14.964  -2.954  12.932  1.00 20.00           C  
ATOM   2634  CG2 ILE A 377      13.385  -3.448  11.046  1.00 20.00           C  
ATOM   2635  CD1 ILE A 377      14.332  -3.844  13.978  1.00 20.00           C  
ATOM   2636  N   VAL A 378      12.786   0.088  10.234  1.00 89.06           N  
ATOM   2637  CA  VAL A 378      11.896   0.596   9.192  1.00 75.68           C  
ATOM   2638  C   VAL A 378      12.683   1.387   8.156  1.00 75.18           C  
ATOM   2639  O   VAL A 378      12.445   1.268   6.948  1.00 76.19           O  
ATOM   2640  CB  VAL A 378      10.775   1.445   9.820  1.00 64.00           C  
ATOM   2641  CG1 VAL A 378       9.960   2.132   8.740  1.00 62.64           C  
ATOM   2642  CG2 VAL A 378       9.887   0.580  10.701  1.00 69.48           C  
ATOM   2643  N   ALA A 379      13.629   2.210   8.612  1.00 84.87           N  
ATOM   2644  CA  ALA A 379      14.470   2.963   7.688  1.00 87.10           C  
ATOM   2645  C   ALA A 379      15.330   2.035   6.842  1.00 88.96           C  
ATOM   2646  O   ALA A 379      15.578   2.310   5.662  1.00 81.40           O  
ATOM   2647  CB  ALA A 379      15.348   3.945   8.463  1.00 44.79           C  
ATOM   2648  N   GLY A 380      15.802   0.935   7.428  1.00 77.23           N  
ATOM   2649  CA  GLY A 380      16.620   0.001   6.670  1.00 80.45           C  
ATOM   2650  C   GLY A 380      15.818  -0.749   5.624  1.00 77.59           C  
ATOM   2651  O   GLY A 380      16.246  -0.884   4.475  1.00 69.34           O  
ATOM   2652  N   VAL A 381      14.642  -1.252   6.012  1.00 81.99           N  
ATOM   2653  CA  VAL A 381      13.758  -1.918   5.057  1.00 83.38           C  
ATOM   2654  C   VAL A 381      13.412  -0.978   3.910  1.00 77.79           C  
ATOM   2655  O   VAL A 381      13.311  -1.397   2.751  1.00 66.26           O  
ATOM   2656  CB  VAL A 381      12.494  -2.434   5.772  1.00 76.89           C  
ATOM   2657  CG1 VAL A 381      11.472  -2.937   4.769  1.00 69.18           C  
ATOM   2658  CG2 VAL A 381      12.858  -3.534   6.752  1.00 75.31           C  
ATOM   2659  N   PHE A 382      13.231   0.308   4.214  1.00 79.75           N  
ATOM   2660  CA  PHE A 382      13.014   1.298   3.166  1.00 68.40           C  
ATOM   2661  C   PHE A 382      14.165   1.294   2.171  1.00 73.80           C  
ATOM   2662  O   PHE A 382      13.953   1.186   0.958  1.00 78.38           O  
ATOM   2663  CB  PHE A 382      12.844   2.679   3.796  1.00 62.89           C  
ATOM   2664  CG  PHE A 382      12.514   3.767   2.815  1.00 69.81           C  
ATOM   2665  CD1 PHE A 382      11.203   4.013   2.452  1.00 78.17           C  
ATOM   2666  CD2 PHE A 382      13.513   4.560   2.276  1.00 67.00           C  
ATOM   2667  CE1 PHE A 382      10.895   5.021   1.557  1.00 75.89           C  
ATOM   2668  CE2 PHE A 382      13.211   5.566   1.380  1.00 62.38           C  
ATOM   2669  CZ  PHE A 382      11.900   5.797   1.021  1.00 65.04           C  
ATOM   2670  N   ILE A 383      15.399   1.395   2.672  1.00 79.94           N  
ATOM   2671  CA  ILE A 383      16.564   1.405   1.792  1.00 76.66           C  
ATOM   2672  C   ILE A 383      16.668   0.093   1.027  1.00 74.25           C  
ATOM   2673  O   ILE A 383      17.053   0.072  -0.148  1.00 81.52           O  
ATOM   2674  CB  ILE A 383      17.840   1.702   2.601  1.00 71.78           C  
ATOM   2675  CG1 ILE A 383      17.851   3.163   3.035  1.00 63.66           C  
ATOM   2676  CG2 ILE A 383      19.084   1.400   1.789  1.00 79.30           C  
ATOM   2677  CD1 ILE A 383      17.701   4.126   1.880  1.00 64.10           C  
ATOM   2678  N   ILE A 384      16.309  -1.019   1.668  1.00 77.47           N  
ANISOU 2678  N   ILE A 384    10269   8636  10532   1676   -785   -446       N  
ATOM   2679  CA  ILE A 384      16.346  -2.312   0.990  1.00 77.09           C  
ANISOU 2679  CA  ILE A 384    10626   8415  10249   1786   -743   -487       C  
ATOM   2680  C   ILE A 384      15.395  -2.323  -0.203  1.00 79.25           C  
ANISOU 2680  C   ILE A 384    11068   8660  10381   1476   -652   -397       C  
ATOM   2681  O   ILE A 384      15.699  -2.905  -1.252  1.00 79.85           O  
ANISOU 2681  O   ILE A 384    11325   8712  10302   1540   -544   -477       O  
ATOM   2682  CB  ILE A 384      16.026  -3.439   1.989  1.00 74.75           C  
ANISOU 2682  CB  ILE A 384    10740   7870   9793   1895   -906   -471       C  
ATOM   2683  CG1 ILE A 384      17.200  -3.648   2.941  1.00 77.41           C  
ANISOU 2683  CG1 ILE A 384    10961   8240  10210   2294  -1026   -570       C  
ATOM   2684  CG2 ILE A 384      15.704  -4.737   1.267  1.00 71.60           C  
ANISOU 2684  CG2 ILE A 384    10844   7191   9169   1898   -891   -497       C  
ATOM   2685  CD1 ILE A 384      18.443  -4.186   2.256  1.00 79.90           C  
ANISOU 2685  CD1 ILE A 384    11224   8571  10564   2673   -951   -738       C  
ATOM   2686  N   CYS A 385      14.245  -1.657  -0.076  1.00 75.66           N  
ANISOU 2686  N   CYS A 385    10540   8236   9971   1156   -704   -252       N  
ATOM   2687  CA  CYS A 385      13.214  -1.744  -1.106  1.00 79.40           C  
ANISOU 2687  CA  CYS A 385    11178   8693  10298    856   -690   -152       C  
ATOM   2688  C   CYS A 385      13.483  -0.807  -2.281  1.00 77.99           C  
ANISOU 2688  C   CYS A 385    10754   8710  10168    769   -575    -84       C  
ATOM   2689  O   CYS A 385      13.199  -1.160  -3.432  1.00 80.47           O  
ANISOU 2689  O   CYS A 385    11270   9043  10261    646   -531    -66       O  
ATOM   2690  CB  CYS A 385      11.842  -1.449  -0.500  1.00 80.67           C  
ANISOU 2690  CB  CYS A 385    11312   8841  10500    576   -801    -23       C  
ATOM   2691  SG  CYS A 385      11.235  -2.722   0.645  1.00 83.19           S  
ANISOU 2691  SG  CYS A 385    12017   8939  10653    532   -901    -25       S  
ATOM   2692  N   TRP A 386      14.018   0.384  -2.024  1.00 68.60           N  
ANISOU 2692  N   TRP A 386     9160   7658   9246    804   -535    -37       N  
ATOM   2693  CA  TRP A 386      14.213   1.350  -3.095  1.00 71.32           C  
ANISOU 2693  CA  TRP A 386     9293   8158   9646    667   -432     98       C  
ATOM   2694  C   TRP A 386      15.618   1.346  -3.677  1.00 73.91           C  
ANISOU 2694  C   TRP A 386     9483   8642   9959    842   -227     12       C  
ATOM   2695  O   TRP A 386      15.812   1.874  -4.776  1.00 77.41           O  
ANISOU 2695  O   TRP A 386     9849   9237  10328    705    -92    139       O  
ATOM   2696  CB  TRP A 386      13.885   2.767  -2.612  1.00 68.85           C  
ANISOU 2696  CB  TRP A 386     8631   7857   9670    543   -510    230       C  
ATOM   2697  CG  TRP A 386      12.415   3.071  -2.565  1.00 72.68           C  
ANISOU 2697  CG  TRP A 386     9161   8279  10174    338   -661    365       C  
ATOM   2698  CD1 TRP A 386      11.648   3.236  -1.448  1.00 67.00           C  
ANISOU 2698  CD1 TRP A 386     8370   7494   9594    332   -777    320       C  
ATOM   2699  CD2 TRP A 386      11.534   3.244  -3.684  1.00 78.89           C  
ANISOU 2699  CD2 TRP A 386    10042   9108  10823    121   -715    558       C  
ATOM   2700  NE1 TRP A 386      10.348   3.502  -1.801  1.00 70.95           N  
ANISOU 2700  NE1 TRP A 386     8865   8000  10093    139   -882    461       N  
ATOM   2701  CE2 TRP A 386      10.251   3.512  -3.168  1.00 76.55           C  
ANISOU 2701  CE2 TRP A 386     9677   8767  10641      9   -876    617       C  
ATOM   2702  CE3 TRP A 386      11.706   3.200  -5.072  1.00 78.88           C  
ANISOU 2702  CE3 TRP A 386    10168   9215  10586     17   -646    682       C  
ATOM   2703  CZ2 TRP A 386       9.146   3.736  -3.988  1.00 75.36           C  
ANISOU 2703  CZ2 TRP A 386     9547   8666  10419   -188  -1008    800       C  
ATOM   2704  CZ3 TRP A 386      10.606   3.421  -5.885  1.00 78.84           C  
ANISOU 2704  CZ3 TRP A 386    10240   9252  10462   -196   -791    875       C  
ATOM   2705  CH2 TRP A 386       9.343   3.684  -5.340  1.00 78.30           C  
ANISOU 2705  CH2 TRP A 386    10069   9128  10555   -289   -989    935       C  
ATOM   2706  N   LEU A 387      16.599   0.779  -2.986  1.00 71.16           N  
ANISOU 2706  N   LEU A 387     9082   8289   9666   1138   -199   -185       N  
ATOM   2707  CA  LEU A 387      17.963   0.908  -3.486  1.00 77.39           C  
ANISOU 2707  CA  LEU A 387     9613   9290  10501   1307     10   -275       C  
ATOM   2708  C   LEU A 387      18.178   0.130  -4.783  1.00 81.59           C  
ANISOU 2708  C   LEU A 387    10394   9919  10687   1358    212   -346       C  
ATOM   2709  O   LEU A 387      18.816   0.661  -5.701  1.00 86.35           O  
ANISOU 2709  O   LEU A 387    10786  10774  11250   1288    442   -288       O  
ATOM   2710  CB  LEU A 387      18.985   0.473  -2.436  1.00 76.08           C  
ANISOU 2710  CB  LEU A 387     9284   9129  10492   1656    -47   -481       C  
ATOM   2711  CG  LEU A 387      20.393   0.933  -2.792  1.00 73.95           C  
ANISOU 2711  CG  LEU A 387     8566   9145  10385   1779    152   -557       C  
ATOM   2712  CD1 LEU A 387      20.380   2.425  -3.067  1.00 70.62           C  
ANISOU 2712  CD1 LEU A 387     7792   8838  10202   1432    210   -352       C  
ATOM   2713  CD2 LEU A 387      21.363   0.599  -1.677  1.00 74.27           C  
ANISOU 2713  CD2 LEU A 387     8384   9220  10617   2125     25   -752       C  
ATOM   2714  N   PRO A 388      17.692  -1.112  -4.913  1.00 79.42           N  
ANISOU 2714  N   PRO A 388    10576   9454  10144   1463    148   -479       N  
ATOM   2715  CA  PRO A 388      17.785  -1.780  -6.223  1.00 83.37           C  
ANISOU 2715  CA  PRO A 388    11355  10040  10283   1481    328   -585       C  
ATOM   2716  C   PRO A 388      17.190  -0.967  -7.356  1.00 88.60           C  
ANISOU 2716  C   PRO A 388    12005  10889  10771   1117    400   -357       C  
ATOM   2717  O   PRO A 388      17.670  -1.054  -8.493  1.00 89.35           O  
ANISOU 2717  O   PRO A 388    12143  11216  10591   1123    637   -407       O  
ATOM   2718  CB  PRO A 388      17.015  -3.085  -5.998  1.00 78.09           C  
ANISOU 2718  CB  PRO A 388    11219   9031   9418   1534    148   -722       C  
ATOM   2719  CG  PRO A 388      17.214  -3.371  -4.563  1.00 73.10           C  
ANISOU 2719  CG  PRO A 388    10537   8200   9037   1742    -22   -758       C  
ATOM   2720  CD  PRO A 388      17.196  -2.039  -3.878  1.00 74.29           C  
ANISOU 2720  CD  PRO A 388    10229   8503   9495   1588    -73   -564       C  
ATOM   2721  N   PHE A 389      16.157  -0.168  -7.077  1.00 87.86           N  
ANISOU 2721  N   PHE A 389    11851  10717  10815    821    202   -105       N  
ATOM   2722  CA  PHE A 389      15.588   0.699  -8.103  1.00 88.83           C  
ANISOU 2722  CA  PHE A 389    11946  10997  10808    504    215    164       C  
ATOM   2723  C   PHE A 389      16.581   1.776  -8.524  1.00 87.11           C  
ANISOU 2723  C   PHE A 389    11342  11030  10726    460    445    317       C  
ATOM   2724  O   PHE A 389      16.791   2.009  -9.719  1.00 91.58           O  
ANISOU 2724  O   PHE A 389    11960  11831  11005    327    627    435       O  
ATOM   2725  CB  PHE A 389      14.287   1.323  -7.592  1.00 81.78           C  
ANISOU 2725  CB  PHE A 389    11019   9946  10106    271    -69    378       C  
ATOM   2726  CG  PHE A 389      13.670   2.319  -8.536  1.00 78.75           C  
ANISOU 2726  CG  PHE A 389    10580   9686   9656    -11   -125    698       C  
ATOM   2727  CD1 PHE A 389      12.947   1.897  -9.638  1.00 72.20           C  
ANISOU 2727  CD1 PHE A 389    10065   8946   8421   -182   -197    758       C  
ATOM   2728  CD2 PHE A 389      13.795   3.677  -8.309  1.00 74.32           C  
ANISOU 2728  CD2 PHE A 389     9675   9124   9438   -104   -142    940       C  
ATOM   2729  CE1 PHE A 389      12.374   2.812 -10.501  1.00 66.21           C  
ANISOU 2729  CE1 PHE A 389     9270   8308   7580   -418   -296   1089       C  
ATOM   2730  CE2 PHE A 389      13.221   4.593  -9.169  1.00 73.66           C  
ANISOU 2730  CE2 PHE A 389     9576   9102   9309   -336   -229   1275       C  
ATOM   2731  CZ  PHE A 389      12.508   4.160 -10.263  1.00 67.96           C  
ANISOU 2731  CZ  PHE A 389     9160   8501   8161   -483   -313   1367       C  
ATOM   2732  N   PHE A 390      17.211   2.438  -7.553  1.00 78.28           N  
ANISOU 2732  N   PHE A 390     9842   9876  10022    542    440    319       N  
ATOM   2733  CA  PHE A 390      18.154   3.503  -7.865  1.00 77.80           C  
ANISOU 2733  CA  PHE A 390     9387  10020  10154    435    640    473       C  
ATOM   2734  C   PHE A 390      19.520   2.977  -8.285  1.00 85.50           C  
ANISOU 2734  C   PHE A 390    10201  11281  11003    650    968    266       C  
ATOM   2735  O   PHE A 390      20.266   3.699  -8.955  1.00 80.65           O  
ANISOU 2735  O   PHE A 390     9313  10928  10401    495   1220    418       O  
ATOM   2736  CB  PHE A 390      18.290   4.441  -6.666  1.00 72.78           C  
ANISOU 2736  CB  PHE A 390     8403   9227  10023    409    479    515       C  
ATOM   2737  CG  PHE A 390      17.046   5.229  -6.384  1.00 71.97           C  
ANISOU 2737  CG  PHE A 390     8367   8891  10086    201    217    731       C  
ATOM   2738  CD1 PHE A 390      16.770   6.384  -7.095  1.00 73.92           C  
ANISOU 2738  CD1 PHE A 390     8531   9132  10422    -77    215   1066       C  
ATOM   2739  CD2 PHE A 390      16.146   4.810  -5.423  1.00 69.40           C  
ANISOU 2739  CD2 PHE A 390     8185   8358   9824    295    -21    611       C  
ATOM   2740  CE1 PHE A 390      15.624   7.110  -6.848  1.00 69.85           C  
ANISOU 2740  CE1 PHE A 390     8056   8392  10093   -202    -42   1247       C  
ATOM   2741  CE2 PHE A 390      14.995   5.533  -5.171  1.00 69.17           C  
ANISOU 2741  CE2 PHE A 390     8161   8162   9960    142   -234    777       C  
ATOM   2742  CZ  PHE A 390      14.735   6.685  -5.884  1.00 63.89           C  
ANISOU 2742  CZ  PHE A 390     7389   7471   9415    -78   -256   1080       C  
ATOM   2743  N   ILE A 391      19.865   1.744  -7.905  1.00 83.05           N  
ANISOU 2743  N   ILE A 391    10043  10926  10586   1005    976    -67       N  
ATOM   2744  CA  ILE A 391      21.044   1.100  -8.477  1.00 88.93           C  
ANISOU 2744  CA  ILE A 391    10677  11954  11158   1273   1299   -305       C  
ATOM   2745  C   ILE A 391      20.854   0.907  -9.975  1.00 91.28           C  
ANISOU 2745  C   ILE A 391    11243  12480  10960   1127   1541   -254       C  
ATOM   2746  O   ILE A 391      21.789   1.084 -10.766  1.00 94.74           O  
ANISOU 2746  O   ILE A 391    11451  13294  11253   1139   1904   -276       O  
ATOM   2747  CB  ILE A 391      21.321  -0.238  -7.761  1.00 85.00           C  
ANISOU 2747  CB  ILE A 391    10370  11271  10655   1728   1197   -664       C  
ATOM   2748  CG1 ILE A 391      21.803   0.004  -6.329  1.00 81.99           C  
ANISOU 2748  CG1 ILE A 391     9657  10782  10715   1901    995   -715       C  
ATOM   2749  CG2 ILE A 391      22.336  -1.068  -8.534  1.00 85.18           C  
ANISOU 2749  CG2 ILE A 391    10376  11551  10438   2063   1525   -960       C  
ATOM   2750  CD1 ILE A 391      22.006  -1.268  -5.531  1.00 79.71           C  
ANISOU 2750  CD1 ILE A 391     9598  10266  10423   2344    833   -991       C  
ATOM   2751  N   THR A 392      19.633   0.564 -10.388  1.00 91.03           N  
ANISOU 2751  N   THR A 392    11682  12262  10642    965   1345   -183       N  
ATOM   2752  CA  THR A 392      19.347   0.341 -11.801  1.00 92.03           C  
ANISOU 2752  CA  THR A 392    12124  12607  10236    813   1511   -151       C  
ATOM   2753  C   THR A 392      19.510   1.622 -12.611  1.00 96.64           C  
ANISOU 2753  C   THR A 392    12473  13487  10758    456   1684    247       C  
ATOM   2754  O   THR A 392      19.972   1.585 -13.759  1.00 99.51           O  
ANISOU 2754  O   THR A 392    12896  14212  10701    394   2002    256       O  
ATOM   2755  CB  THR A 392      17.934  -0.222 -11.949  1.00 85.65           C  
ANISOU 2755  CB  THR A 392    11821  11527   9195    670   1183   -144       C  
ATOM   2756  OG1 THR A 392      17.843  -1.462 -11.238  1.00 86.36           O  
ANISOU 2756  OG1 THR A 392    12169  11313   9330    965   1047   -489       O  
ATOM   2757  CG2 THR A 392      17.589  -0.458 -13.404  1.00 82.50           C  
ANISOU 2757  CG2 THR A 392    11776  11367   8203    498   1292   -131       C  
ATOM   2758  N   HIS A 393      19.187   2.742 -12.031  1.00 88.71           N  
ANISOU 2758  N   HIS A 393    11226  12324  10155    219   1485    579       N  
ATOM   2759  CA  HIS A 393      19.363   3.957 -12.738  1.00 88.98           C  
ANISOU 2759  CA  HIS A 393    11056  12550  10202   -130   1618   1001       C  
ATOM   2760  C   HIS A 393      20.809   4.181 -13.033  1.00 88.31           C  
ANISOU 2760  C   HIS A 393    10554  12829  10172   -105   2051    965       C  
ATOM   2761  O   HIS A 393      21.145   4.651 -14.071  1.00 90.40           O  
ANISOU 2761  O   HIS A 393    10759  13392  10197   -381   2313   1255       O  
ATOM   2762  CB  HIS A 393      18.863   5.074 -11.893  1.00 92.81           C  
ANISOU 2762  CB  HIS A 393    11357  12712  11192   -324   1304   1294       C  
ATOM   2763  CG  HIS A 393      17.412   5.334 -12.064  1.00 96.38           C  
ANISOU 2763  CG  HIS A 393    12141  12922  11557   -443    932   1454       C  
ATOM   2764  ND1 HIS A 393      16.815   5.355 -13.296  1.00101.35           N  
ANISOU 2764  ND1 HIS A 393    12985  13642  11882   -712    860   1815       N  
ATOM   2765  CD2 HIS A 393      16.440   5.591 -11.168  1.00 93.09           C  
ANISOU 2765  CD2 HIS A 393    11851  12212  11307   -333    611   1312       C  
ATOM   2766  CE1 HIS A 393      15.536   5.622 -13.155  1.00 98.51           C  
ANISOU 2766  CE1 HIS A 393    12830  13059  11540   -744    489   1868       C  
ATOM   2767  NE2 HIS A 393      15.282   5.762 -11.872  1.00 93.35           N  
ANISOU 2767  NE2 HIS A 393    12117  12180  11171   -533    357   1563       N  
ATOM   2768  N   ILE A 394      21.675   3.869 -12.094  1.00 95.53           N  
ANISOU 2768  N   ILE A 394    11157  13746  11395    209   2124    635       N  
ATOM   2769  CA  ILE A 394      23.103   4.065 -12.304  1.00100.46           C  
ANISOU 2769  CA  ILE A 394    11300  14765  12104    258   2532    556       C  
ATOM   2770  C   ILE A 394      23.590   3.234 -13.480  1.00110.00           C  
ANISOU 2770  C   ILE A 394    12669  16389  12736    410   2939    349       C  
ATOM   2771  O   ILE A 394      24.530   3.628 -14.181  1.00116.65           O  
ANISOU 2771  O   ILE A 394    13187  17679  13455    283   3367    434       O  
ATOM   2772  CB  ILE A 394      23.876   3.735 -11.014  1.00 95.87           C  
ANISOU 2772  CB  ILE A 394    10335  14092  12001    599   2436    239       C  
ATOM   2773  N   LEU A 395      22.959   2.084 -13.726  1.00109.05           N  
ANISOU 2773  N   LEU A 395    13051  16136  12246    661   2828     65       N  
ATOM   2774  CA  LEU A 395      23.384   1.213 -14.816  1.00115.80           C  
ANISOU 2774  CA  LEU A 395    14119  17349  12533    853   3195   -221       C  
ATOM   2775  C   LEU A 395      22.911   1.731 -16.169  1.00123.98           C  
ANISOU 2775  C   LEU A 395    15434  18666  13007    451   3352    106       C  
ATOM   2776  O   LEU A 395      23.622   1.591 -17.170  1.00132.70           O  
ANISOU 2776  O   LEU A 395    16488  20259  13673    459   3812     22       O  
ATOM   2777  CB  LEU A 395      22.873  -0.208 -14.578  1.00113.04           C  
ANISOU 2777  CB  LEU A 395    14254  16684  12011   1243   2983   -662       C  
ATOM   2778  CG  LEU A 395      23.285  -0.827 -13.242  1.00107.58           C  
ANISOU 2778  CG  LEU A 395    13379  15684  11813   1666   2788   -952       C  
ATOM   2779  CD1 LEU A 395      22.874  -2.287 -13.174  1.00109.94           C  
ANISOU 2779  CD1 LEU A 395    14213  15663  11896   2035   2631  -1369       C  
ATOM   2780  CD2 LEU A 395      24.782  -0.681 -13.009  1.00102.89           C  
ANISOU 2780  CD2 LEU A 395    12151  15454  11490   1927   3132  -1110       C  
ATOM   2781  N   ASN A 396      21.713   2.324 -16.219  1.00120.69           N  
ANISOU 2781  N   ASN A 396    15306  17974  12576    116   2975    478       N  
ATOM   2782  CA  ASN A 396      21.242   2.943 -17.454  1.00120.58           C  
ANISOU 2782  CA  ASN A 396    15547  18214  12053   -278   3052    871       C  
ATOM   2783  C   ASN A 396      22.194   4.031 -17.930  1.00122.42           C  
ANISOU 2783  C   ASN A 396    15355  18837  12322   -573   3455   1241       C  
ATOM   2784  O   ASN A 396      22.387   4.205 -19.139  1.00125.81           O  
ANISOU 2784  O   ASN A 396    15933  19697  12171   -784   3770   1420       O  
ATOM   2785  CB  ASN A 396      19.841   3.523 -17.251  1.00116.75           C  
ANISOU 2785  CB  ASN A 396    15328  17340  11693   -546   2527   1239       C  
ATOM   2786  CG  ASN A 396      18.760   2.676 -17.888  1.00117.94           C  
ANISOU 2786  CG  ASN A 396    16062  17433  11316   -534   2274   1087       C  
ATOM   2787  OD1 ASN A 396      18.987   1.516 -18.228  1.00121.59           O  
ANISOU 2787  OD1 ASN A 396    16780  18007  11413   -276   2424    626       O  
ATOM   2788  ND2 ASN A 396      17.576   3.253 -18.057  1.00116.24           N  
ANISOU 2788  ND2 ASN A 396    16052  17032  11079   -807   1870   1457       N  
ATOM   2789  N   ILE A 397      22.806   4.760 -16.997  1.00128.30           N  
ANISOU 2789  N   ILE A 397    15581  19448  13721   -619   3450   1356       N  
ATOM   2790  CA  ILE A 397      23.706   5.849 -17.357  1.00131.63           C  
ANISOU 2790  CA  ILE A 397    15568  20182  14265   -972   3805   1730       C  
ATOM   2791  C   ILE A 397      25.103   5.322 -17.667  1.00137.13           C  
ANISOU 2791  C   ILE A 397    15858  21427  14818   -764   4380   1392       C  
ATOM   2792  O   ILE A 397      25.789   5.839 -18.556  1.00140.52           O  
ANISOU 2792  O   ILE A 397    16093  22338  14959  -1056   4838   1642       O  
ATOM   2793  CB  ILE A 397      23.731   6.896 -16.228  1.00123.72           C  
ANISOU 2793  CB  ILE A 397    14191  18774  14042  -1149   3517   1971       C  
ATOM   2794  CG1 ILE A 397      22.331   7.473 -16.007  1.00113.56           C  
ANISOU 2794  CG1 ILE A 397    13280  16985  12883  -1327   2987   2301       C  
ATOM   2795  CG2 ILE A 397      24.735   8.002 -16.530  1.00125.40           C  
ANISOU 2795  CG2 ILE A 397    13930  19262  14453  -1557   3873   2337       C  
ATOM   2796  CD1 ILE A 397      22.251   8.459 -14.860  1.00102.21           C  
ANISOU 2796  CD1 ILE A 397    11537  15104  12195  -1449   2680   2462       C  
ATOM   2797  N   HIS A 398      25.537   4.278 -16.959  1.00136.75           N  
ANISOU 2797  N   HIS A 398    15674  21329  14958   -248   4372    832       N  
ATOM   2798  CA  HIS A 398      26.930   3.846 -17.033  1.00140.25           C  
ANISOU 2798  CA  HIS A 398    15599  22260  15431     23   4867    485       C  
ATOM   2799  C   HIS A 398      27.250   3.199 -18.376  1.00154.68           C  
ANISOU 2799  C   HIS A 398    17644  24638  16490    117   5371    293       C  
ATOM   2800  O   HIS A 398      28.121   3.674 -19.114  1.00162.37           O  
ANISOU 2800  O   HIS A 398    18256  26184  17254   -111   5901    448       O  
ATOM   2801  CB  HIS A 398      27.240   2.881 -15.886  1.00132.50           C  
ANISOU 2801  CB  HIS A 398    14462  21019  14861    602   4649    -39       C  
ATOM   2802  N   CYS A 399      26.570   2.103 -18.707  1.00157.99           N  
ANISOU 2802  N   CYS A 399    18652  24908  16468    436   5229    -65       N  
ATOM   2803  CA  CYS A 399      26.929   1.309 -19.875  1.00171.19           C  
ANISOU 2803  CA  CYS A 399    20554  27077  17414    635   5693   -403       C  
ATOM   2804  C   CYS A 399      25.915   1.388 -21.006  1.00172.38           C  
ANISOU 2804  C   CYS A 399    21379  27292  16826    306   5614   -163       C  
ATOM   2805  O   CYS A 399      26.152   0.799 -22.069  1.00171.94           O  
ANISOU 2805  O   CYS A 399    21574  27683  16070    417   5999   -433       O  
ATOM   2806  CB  CYS A 399      27.145  -0.157 -19.472  1.00177.68           C  
ANISOU 2806  CB  CYS A 399    21527  27720  18264   1324   5648  -1118       C  
ATOM   2807  SG  CYS A 399      25.689  -1.129 -18.956  1.00177.65           S  
ANISOU 2807  SG  CYS A 399    22318  26935  18245   1520   4957  -1341       S  
ATOM   2808  N   ASP A 400      24.802   2.093 -20.815  1.00169.42           N  
ANISOU 2808  N   ASP A 400    21292  26506  16572    -73   5118    313       N  
ATOM   2809  CA  ASP A 400      23.708   2.176 -21.779  1.00172.19           C  
ANISOU 2809  CA  ASP A 400    22278  26866  16282   -369   4909    565       C  
ATOM   2810  C   ASP A 400      23.130   0.810 -22.126  1.00178.49           C  
ANISOU 2810  C   ASP A 400    23661  27552  16606    -24   4760      1       C  
ATOM   2811  O   ASP A 400      22.354   0.694 -23.084  1.00180.90           O  
ANISOU 2811  O   ASP A 400    24500  27979  16254   -230   4642     91       O  
ATOM   2812  CB  ASP A 400      24.139   2.903 -23.061  1.00174.58           C  
ANISOU 2812  CB  ASP A 400    22570  27804  15958   -772   5382    965       C  
ATOM   2813  N   CYS A 401      23.494  -0.229 -21.377  1.00180.63           N  
ANISOU 2813  N   CYS A 401    23862  27575  17194    489   4738   -576       N  
ATOM   2814  CA  CYS A 401      22.923  -1.551 -21.583  1.00179.00           C  
ANISOU 2814  CA  CYS A 401    24242  27130  16641    806   4543  -1120       C  
ATOM   2815  C   CYS A 401      21.440  -1.519 -21.252  1.00170.63           C  
ANISOU 2815  C   CYS A 401    23622  25538  15671    556   3881   -897       C  
ATOM   2816  O   CYS A 401      21.063  -1.243 -20.109  1.00166.40           O  
ANISOU 2816  O   CYS A 401    22893  24541  15789    548   3513   -729       O  
ATOM   2817  CB  CYS A 401      23.624  -2.583 -20.701  1.00179.14           C  
ANISOU 2817  CB  CYS A 401    24079  26891  17096   1410   4598  -1700       C  
ATOM   2818  SG  CYS A 401      25.421  -2.457 -20.478  1.00183.37           S  
ANISOU 2818  SG  CYS A 401    23801  27930  17940   1774   5237  -1908       S  
ATOM   2819  N   ASN A 402      20.597  -1.793 -22.244  1.00163.09           N  
ANISOU 2819  N   ASN A 402    23235  24683  14049    348   3727   -908       N  
ATOM   2820  CA  ASN A 402      19.171  -1.877 -21.964  1.00152.09           C  
ANISOU 2820  CA  ASN A 402    22222  22828  12736    126   3092   -755       C  
ATOM   2821  C   ASN A 402      18.914  -3.031 -21.004  1.00144.87           C  
ANISOU 2821  C   ASN A 402    21476  21352  12215    479   2819  -1242       C  
ATOM   2822  O   ASN A 402      19.334  -4.167 -21.242  1.00148.09           O  
ANISOU 2822  O   ASN A 402    22151  21737  12380    836   2997  -1823       O  
ATOM   2823  CB  ASN A 402      18.364  -2.039 -23.255  1.00153.00           C  
ANISOU 2823  CB  ASN A 402    22907  23202  12025   -153   2955   -727       C  
ATOM   2824  CG  ASN A 402      18.644  -3.344 -23.970  1.00154.48           C  
ANISOU 2824  CG  ASN A 402    23550  23525  11619    142   3169  -1424       C  
ATOM   2825  OD1 ASN A 402      18.048  -4.376 -23.657  1.00152.23           O  
ANISOU 2825  OD1 ASN A 402    23645  22801  11394    294   2842  -1846       O  
ATOM   2826  ND2 ASN A 402      19.540  -3.303 -24.949  1.00156.47           N  
ANISOU 2826  ND2 ASN A 402    23784  24383  11285    209   3730  -1554       N  
ATOM   2827  N   ILE A 403      18.259  -2.719 -19.893  1.00137.95           N  
ANISOU 2827  N   ILE A 403    20445  20015  11956    389   2403   -999       N  
ATOM   2828  CA  ILE A 403      18.056  -3.664 -18.801  1.00126.08           C  
ANISOU 2828  CA  ILE A 403    19041  17968  10897    679   2150  -1342       C  
ATOM   2829  C   ILE A 403      16.725  -4.370 -19.025  1.00123.67           C  
ANISOU 2829  C   ILE A 403    19300  17348  10341    476   1691  -1463       C  
ATOM   2830  O   ILE A 403      15.774  -3.737 -19.506  1.00123.23           O  
ANISOU 2830  O   ILE A 403    19345  17396  10082     73   1419  -1099       O  
ATOM   2831  CB  ILE A 403      18.121  -2.936 -17.448  1.00116.57           C  
ANISOU 2831  CB  ILE A 403    17344  16498  10450    680   1990  -1029       C  
ATOM   2832  CG1 ILE A 403      19.571  -2.545 -17.154  1.00117.76           C  
ANISOU 2832  CG1 ILE A 403    16950  16923  10871    944   2430  -1064       C  
ATOM   2833  CG2 ILE A 403      17.524  -3.771 -16.324  1.00111.83           C  
ANISOU 2833  CG2 ILE A 403    16927  15326  10238    834   1619  -1235       C  
ATOM   2834  CD1 ILE A 403      19.744  -1.682 -15.938  1.00115.05           C  
ANISOU 2834  CD1 ILE A 403    16103  16396  11214    903   2293   -760       C  
ATOM   2835  N   PRO A 404      16.628  -5.671 -18.745  1.00118.90           N  
ANISOU 2835  N   PRO A 404    19074  16363   9738    731   1581  -1960       N  
ATOM   2836  CA  PRO A 404      15.360  -6.387 -18.918  1.00118.90           C  
ANISOU 2836  CA  PRO A 404    19598  16036   9542    479   1130  -2089       C  
ATOM   2837  C   PRO A 404      14.199  -5.600 -18.342  1.00114.46           C  
ANISOU 2837  C   PRO A 404    18849  15327   9312     80    700  -1589       C  
ATOM   2838  O   PRO A 404      14.149  -5.345 -17.130  1.00111.06           O  
ANISOU 2838  O   PRO A 404    18106  14611   9479    144    589  -1414       O  
ATOM   2839  CB  PRO A 404      15.590  -7.690 -18.142  1.00118.42           C  
ANISOU 2839  CB  PRO A 404    19799  15435   9759    841   1069  -2563       C  
ATOM   2840  CG  PRO A 404      17.050  -7.938 -18.305  1.00121.83           C  
ANISOU 2840  CG  PRO A 404    20054  16085  10152   1347   1569  -2883       C  
ATOM   2841  CD  PRO A 404      17.718  -6.580 -18.344  1.00119.79           C  
ANISOU 2841  CD  PRO A 404    19169  16331  10014   1271   1867  -2444       C  
ATOM   2842  N   PRO A 405      13.257  -5.175 -19.187  1.00111.48           N  
ANISOU 2842  N   PRO A 405    18639  15168   8549   -316    448  -1354       N  
ATOM   2843  CA  PRO A 405      12.126  -4.381 -18.686  1.00109.02           C  
ANISOU 2843  CA  PRO A 405    18100  14751   8571   -653     36   -886       C  
ATOM   2844  C   PRO A 405      11.320  -5.093 -17.621  1.00107.40           C  
ANISOU 2844  C   PRO A 405    17974  14039   8792   -700   -301  -1012       C  
ATOM   2845  O   PRO A 405      10.656  -4.425 -16.820  1.00106.74           O  
ANISOU 2845  O   PRO A 405    17562  13840   9155   -851   -528   -666       O  
ATOM   2846  CB  PRO A 405      11.292  -4.119 -19.948  1.00110.35           C  
ANISOU 2846  CB  PRO A 405    18539  15248   8141  -1009   -207   -731       C  
ATOM   2847  CG  PRO A 405      11.691  -5.197 -20.899  1.00113.76           C  
ANISOU 2847  CG  PRO A 405    19491  15789   7942   -900    -38  -1264       C  
ATOM   2848  CD  PRO A 405      13.141  -5.456 -20.627  1.00117.16           C  
ANISOU 2848  CD  PRO A 405    19780  16246   8490   -452    496  -1536       C  
ATOM   2849  N   VAL A 406      11.356  -6.428 -17.580  1.00111.87           N  
ANISOU 2849  N   VAL A 406    18978  14290   9236   -579   -329  -1496       N  
ATOM   2850  CA  VAL A 406      10.738  -7.139 -16.469  1.00102.56           C  
ANISOU 2850  CA  VAL A 406    17881  12600   8486   -624   -592  -1581       C  
ATOM   2851  C   VAL A 406      11.508  -6.882 -15.181  1.00104.10           C  
ANISOU 2851  C   VAL A 406    17697  12610   9246   -300   -398  -1479       C  
ATOM   2852  O   VAL A 406      10.926  -6.894 -14.090  1.00102.17           O  
ANISOU 2852  O   VAL A 406    17313  12081   9424   -395   -602  -1324       O  
ATOM   2853  CB  VAL A 406      10.640  -8.644 -16.776  1.00 94.49           C  
ANISOU 2853  CB  VAL A 406    17480  11217   7203   -584   -680  -2114       C  
ATOM   2854  N   LEU A 407      12.818  -6.639 -15.277  1.00103.82           N  
ANISOU 2854  N   LEU A 407    17468  12769   9209     74     -3  -1567       N  
ATOM   2855  CA  LEU A 407      13.592  -6.296 -14.089  1.00100.38           C  
ANISOU 2855  CA  LEU A 407    16623  12220   9296    369    146  -1462       C  
ATOM   2856  C   LEU A 407      13.390  -4.838 -13.698  1.00 94.26           C  
ANISOU 2856  C   LEU A 407    15315  11675   8824    182    114   -975       C  
ATOM   2857  O   LEU A 407      13.200  -4.533 -12.516  1.00 88.29           O  
ANISOU 2857  O   LEU A 407    14299  10718   8529    200     -8   -812       O  
ATOM   2858  CB  LEU A 407      15.077  -6.584 -14.317  1.00101.90           C  
ANISOU 2858  CB  LEU A 407    16737  12562   9418    837    561  -1755       C  
ATOM   2859  N   TYR A 408      13.370  -3.956 -14.650  1.00 94.06           N  
ANISOU 2859  N   TYR A 408    15152  12055   8531      5    218   -738       N  
ATOM   2860  CA  TYR A 408      13.143  -2.599 -14.299  1.00 92.67           C  
ANISOU 2860  CA  TYR A 408    14536  12021   8655   -189    141   -264       C  
ATOM   2861  C   TYR A 408      11.764  -2.493 -13.713  1.00 95.64           C  
ANISOU 2861  C   TYR A 408    14901  12179   9258   -462   -278    -65       C  
ATOM   2862  O   TYR A 408      11.578  -1.795 -12.766  1.00 92.85           O  
ANISOU 2862  O   TYR A 408    14175  11751   9352   -489   -366    194       O  
ATOM   2863  CB  TYR A 408      13.263  -1.746 -15.521  1.00 92.66           C  
ANISOU 2863  CB  TYR A 408    14496  12449   8263   -369    283     -7       C  
ATOM   2864  CG  TYR A 408      13.909  -0.444 -15.274  1.00 92.93           C  
ANISOU 2864  CG  TYR A 408    14043  12651   8617   -377    472    359       C  
ATOM   2865  CD1 TYR A 408      13.694   0.227 -14.129  1.00 88.51           C  
ANISOU 2865  CD1 TYR A 408    13122  11858   8651   -379    316    564       C  
ATOM   2866  CD2 TYR A 408      14.725   0.122 -16.199  1.00 98.66           C  
ANISOU 2866  CD2 TYR A 408    14681  13767   9040   -406    819    487       C  
ATOM   2867  CE1 TYR A 408      14.287   1.434 -13.904  1.00 87.26           C  
ANISOU 2867  CE1 TYR A 408    12549  11797   8809   -413    462    866       C  
ATOM   2868  CE2 TYR A 408      15.323   1.331 -15.973  1.00 98.99           C  
ANISOU 2868  CE2 TYR A 408    14288  13921   9401   -474    985    837       C  
ATOM   2869  CZ  TYR A 408      15.086   1.974 -14.814  1.00 95.40           C  
ANISOU 2869  CZ  TYR A 408    13502  13174   9570   -479    786   1014       C  
ATOM   2870  OH  TYR A 408      15.640   3.178 -14.533  1.00 98.94           O  
ANISOU 2870  OH  TYR A 408    13550  13681  10361   -572    923   1329       O  
ATOM   2871  N   SER A 409      10.781  -3.173 -14.278  1.00105.38           N  
ANISOU 2871  N   SER A 409    16521  13320  10198   -667   -536   -211       N  
ATOM   2872  CA  SER A 409       9.431  -3.119 -13.727  1.00100.18           C  
ANISOU 2872  CA  SER A 409    15802  12496   9765   -940   -916    -53       C  
ATOM   2873  C   SER A 409       9.363  -3.750 -12.341  1.00 91.59           C  
ANISOU 2873  C   SER A 409    14684  11035   9081   -825   -948   -193       C  
ATOM   2874  O   SER A 409       8.543  -3.336 -11.513  1.00 85.61           O  
ANISOU 2874  O   SER A 409    13671  10195   8661   -967  -1137      4       O  
ATOM   2875  CB  SER A 409       8.447  -3.811 -14.672  1.00102.06           C  
ANISOU 2875  CB  SER A 409    16434  12778   9567  -1245  -1202   -175       C  
ATOM   2876  OG  SER A 409       8.493  -3.239 -15.967  1.00105.65           O  
ANISOU 2876  OG  SER A 409    16956  13611   9576  -1354  -1197    -26       O  
ATOM   2877  N   ALA A 410      10.216  -4.740 -12.069  1.00 90.76           N  
ANISOU 2877  N   ALA A 410    14837  10715   8935   -552   -765   -524       N  
ATOM   2878  CA  ALA A 410      10.196  -5.405 -10.769  1.00 84.55           C  
ANISOU 2878  CA  ALA A 410    14089   9558   8478   -436   -813   -622       C  
ATOM   2879  C   ALA A 410      10.716  -4.488  -9.669  1.00 85.46           C  
ANISOU 2879  C   ALA A 410    13726   9716   9028   -244   -702   -420       C  
ATOM   2880  O   ALA A 410      10.097  -4.365  -8.607  1.00 76.26           O  
ANISOU 2880  O   ALA A 410    12411   8410   8155   -337   -841   -294       O  
ATOM   2881  CB  ALA A 410      11.018  -6.693 -10.829  1.00 79.54           C  
ANISOU 2881  CB  ALA A 410    13883   8649   7690   -141   -680  -1016       C  
ATOM   2882  N   PHE A 411      11.858  -3.837  -9.904  1.00 82.88           N  
ANISOU 2882  N   PHE A 411    13149   9606   8736      5   -442   -403       N  
ATOM   2883  CA  PHE A 411      12.446  -2.977  -8.883  1.00 81.51           C  
ANISOU 2883  CA  PHE A 411    12529   9464   8975    175   -355   -259       C  
ATOM   2884  C   PHE A 411      11.593  -1.745  -8.614  1.00 76.95           C  
ANISOU 2884  C   PHE A 411    11608   8991   8637    -75   -511     73       C  
ATOM   2885  O   PHE A 411      11.658  -1.179  -7.516  1.00 76.38           O  
ANISOU 2885  O   PHE A 411    11240   8854   8929      0   -536    155       O  
ATOM   2886  CB  PHE A 411      13.859  -2.567  -9.293  1.00 88.89           C  
ANISOU 2886  CB  PHE A 411    13244  10633   9898    438    -44   -321       C  
ATOM   2887  CG  PHE A 411      14.856  -3.688  -9.233  1.00 94.35           C  
ANISOU 2887  CG  PHE A 411    14147  11212  10488    811    121   -674       C  
ATOM   2888  CD1 PHE A 411      14.562  -4.860  -8.555  1.00 93.62           C  
ANISOU 2888  CD1 PHE A 411    14407  10746  10418    926    -36   -865       C  
ATOM   2889  CD2 PHE A 411      16.092  -3.568  -9.846  1.00 94.90           C  
ANISOU 2889  CD2 PHE A 411    14052  11548  10457   1055    438   -805       C  
ATOM   2890  CE1 PHE A 411      15.480  -5.891  -8.497  1.00 91.66           C  
ANISOU 2890  CE1 PHE A 411    14375  10339  10112   1324     82  -1184       C  
ATOM   2891  CE2 PHE A 411      17.013  -4.595  -9.790  1.00 91.21           C  
ANISOU 2891  CE2 PHE A 411    13738  10988   9931   1464    585  -1156       C  
ATOM   2892  CZ  PHE A 411      16.707  -5.757  -9.115  1.00 90.35           C  
ANISOU 2892  CZ  PHE A 411    14011  10453   9865   1623    389  -1349       C  
ATOM   2893  N   THR A 412      10.799  -1.310  -9.596  1.00 86.37           N  
ANISOU 2893  N   THR A 412    12841  10347   9628   -346   -634    251       N  
ATOM   2894  CA  THR A 412       9.854  -0.225  -9.353  1.00 83.78           C  
ANISOU 2894  CA  THR A 412    12208  10075   9551   -541   -831    553       C  
ATOM   2895  C   THR A 412       8.712  -0.693  -8.459  1.00 78.58           C  
ANISOU 2895  C   THR A 412    11565   9242   9050   -678  -1053    522       C  
ATOM   2896  O   THR A 412       8.335  -0.005  -7.503  1.00 75.36           O  
ANISOU 2896  O   THR A 412    10841   8797   8997   -662  -1111    634       O  
ATOM   2897  CB  THR A 412       9.310   0.315 -10.677  1.00 83.99           C  
ANISOU 2897  CB  THR A 412    12287  10328   9297   -765   -948    775       C  
ATOM   2898  OG1 THR A 412      10.397   0.624 -11.557  1.00 88.79           O  
ANISOU 2898  OG1 THR A 412    12926  11134   9675   -676   -690    805       O  
ATOM   2899  CG2 THR A 412       8.491   1.578 -10.436  1.00 76.49           C  
ANISOU 2899  CG2 THR A 412    10981   9411   8671   -879  -1149   1106       C  
ATOM   2900  N   TRP A 413       8.148  -1.866  -8.758  1.00 79.97           N  
ANISOU 2900  N   TRP A 413    12110   9314   8961   -831  -1168    357       N  
ATOM   2901  CA  TRP A 413       7.078  -2.406  -7.927  1.00 79.43           C  
ANISOU 2901  CA  TRP A 413    12060   9094   9024  -1024  -1347    342       C  
ATOM   2902  C   TRP A 413       7.576  -2.703  -6.520  1.00 73.46           C  
ANISOU 2902  C   TRP A 413    11258   8138   8517   -819  -1224    254       C  
ATOM   2903  O   TRP A 413       6.853  -2.491  -5.539  1.00 70.81           O  
ANISOU 2903  O   TRP A 413    10714   7782   8407   -915  -1295    340       O  
ATOM   2904  CB  TRP A 413       6.498  -3.667  -8.569  1.00 85.80           C  
ANISOU 2904  CB  TRP A 413    13317   9783   9501  -1268  -1494    166       C  
ATOM   2905  CG  TRP A 413       5.728  -3.398  -9.828  1.00 91.51           C  
ANISOU 2905  CG  TRP A 413    14070  10739   9962  -1534  -1703    261       C  
ATOM   2906  CD1 TRP A 413       5.242  -2.195 -10.250  1.00 85.59           C  
ANISOU 2906  CD1 TRP A 413    12966  10256   9299  -1598  -1823    542       C  
ATOM   2907  CD2 TRP A 413       5.358  -4.354 -10.833  1.00 96.72           C  
ANISOU 2907  CD2 TRP A 413    15160  11373  10216  -1760  -1855     72       C  
ATOM   2908  NE1 TRP A 413       4.589  -2.343 -11.449  1.00 88.41           N  
ANISOU 2908  NE1 TRP A 413    13492  10790   9309  -1846  -2056    571       N  
ATOM   2909  CE2 TRP A 413       4.646  -3.658 -11.829  1.00 95.02           C  
ANISOU 2909  CE2 TRP A 413    14808  11468   9826  -1963  -2077    265       C  
ATOM   2910  CE3 TRP A 413       5.558  -5.731 -10.985  1.00100.43           C  
ANISOU 2910  CE3 TRP A 413    16143  11559  10456  -1802  -1850   -252       C  
ATOM   2911  CZ2 TRP A 413       4.135  -4.290 -12.963  1.00 98.69           C  
ANISOU 2911  CZ2 TRP A 413    15618  12022   9858  -2226  -2299    130       C  
ATOM   2912  CZ3 TRP A 413       5.049  -6.356 -12.111  1.00103.40           C  
ANISOU 2912  CZ3 TRP A 413    16876  11980  10432  -2067  -2053   -417       C  
ATOM   2913  CH2 TRP A 413       4.347  -5.636 -13.085  1.00102.66           C  
ANISOU 2913  CH2 TRP A 413    16621  12251  10133  -2286  -2277   -233       C  
ATOM   2914  N   LEU A 414       8.817  -3.184  -6.402  1.00 75.32           N  
ANISOU 2914  N   LEU A 414    11667   8256   8695   -521  -1041     79       N  
ATOM   2915  CA  LEU A 414       9.384  -3.467  -5.087  1.00 69.21           C  
ANISOU 2915  CA  LEU A 414    10863   7310   8123   -291   -967     10       C  
ATOM   2916  C   LEU A 414       9.434  -2.210  -4.226  1.00 77.59           C  
ANISOU 2916  C   LEU A 414    11447   8517   9516   -215   -939    159       C  
ATOM   2917  O   LEU A 414       9.179  -2.265  -3.016  1.00 79.71           O  
ANISOU 2917  O   LEU A 414    11637   8710   9938   -194   -969    169       O  
ATOM   2918  CB  LEU A 414      10.778  -4.078  -5.238  1.00 67.92           C  
ANISOU 2918  CB  LEU A 414    10893   7049   7867     71   -800   -201       C  
ATOM   2919  CG  LEU A 414      11.552  -4.368  -3.947  1.00 71.97           C  
ANISOU 2919  CG  LEU A 414    11370   7408   8567    375   -760   -268       C  
ATOM   2920  CD1 LEU A 414      10.756  -5.279  -3.035  1.00 56.68           C  
ANISOU 2920  CD1 LEU A 414     9726   5197   6611    226   -906   -242       C  
ATOM   2921  CD2 LEU A 414      12.904  -4.980  -4.260  1.00 76.87           C  
ANISOU 2921  CD2 LEU A 414    12133   7966   9108    768   -617   -490       C  
ATOM   2922  N   GLY A 415       9.747  -1.065  -4.832  1.00 76.07           N  
ANISOU 2922  N   GLY A 415    10960   8524   9421   -187   -885    275       N  
ATOM   2923  CA  GLY A 415       9.745   0.179  -4.081  1.00 72.96           C  
ANISOU 2923  CA  GLY A 415    10144   8207   9369   -132   -886    390       C  
ATOM   2924  C   GLY A 415       8.357   0.581  -3.618  1.00 74.19           C  
ANISOU 2924  C   GLY A 415    10131   8394   9665   -339  -1044    507       C  
ATOM   2925  O   GLY A 415       8.180   1.043  -2.488  1.00 75.00           O  
ANISOU 2925  O   GLY A 415    10010   8487   9999   -269  -1044    489       O  
ATOM   2926  N   TYR A 416       7.355   0.423  -4.485  1.00 71.29           N  
ANISOU 2926  N   TYR A 416     9841   8097   9148   -588  -1184    609       N  
ATOM   2927  CA  TYR A 416       5.978   0.695  -4.089  1.00 65.72           C  
ANISOU 2927  CA  TYR A 416     8925   7466   8580   -782  -1337    704       C  
ATOM   2928  C   TYR A 416       5.494  -0.288  -3.030  1.00 74.23           C  
ANISOU 2928  C   TYR A 416    10136   8452   9617   -880  -1320    595       C  
ATOM   2929  O   TYR A 416       4.629   0.058  -2.215  1.00 72.94           O  
ANISOU 2929  O   TYR A 416     9706   8378   9627   -957  -1345    631       O  
ATOM   2930  CB  TYR A 416       5.065   0.646  -5.312  1.00 62.97           C  
ANISOU 2930  CB  TYR A 416     8626   7243   8059  -1034  -1533    831       C  
ATOM   2931  CG  TYR A 416       5.257   1.800  -6.266  1.00 72.57           C  
ANISOU 2931  CG  TYR A 416     9671   8573   9328   -975  -1592   1030       C  
ATOM   2932  CD1 TYR A 416       5.334   3.107  -5.802  1.00 77.77           C  
ANISOU 2932  CD1 TYR A 416     9966   9229  10353   -816  -1582   1149       C  
ATOM   2933  CD2 TYR A 416       5.362   1.584  -7.633  1.00 70.98           C  
ANISOU 2933  CD2 TYR A 416     9709   8467   8795  -1089  -1663   1103       C  
ATOM   2934  CE1 TYR A 416       5.505   4.166  -6.675  1.00 81.18           C  
ANISOU 2934  CE1 TYR A 416    10288   9707  10852   -788  -1652   1381       C  
ATOM   2935  CE2 TYR A 416       5.537   2.637  -8.513  1.00 78.84           C  
ANISOU 2935  CE2 TYR A 416    10587   9572   9796  -1063  -1716   1345       C  
ATOM   2936  CZ  TYR A 416       5.608   3.925  -8.030  1.00 78.01           C  
ANISOU 2936  CZ  TYR A 416    10131   9419  10091   -919  -1715   1507       C  
ATOM   2937  OH  TYR A 416       5.781   4.974  -8.906  1.00 66.59           O  
ANISOU 2937  OH  TYR A 416     8612   8022   8665   -917  -1783   1795       O  
ATOM   2938  N   VAL A 417       6.036  -1.510  -3.031  1.00 75.00           N  
ANISOU 2938  N   VAL A 417    10650   8367   9481   -873  -1268    468       N  
ATOM   2939  CA  VAL A 417       5.682  -2.503  -2.019  1.00 75.22           C  
ANISOU 2939  CA  VAL A 417    10882   8250   9450   -979  -1253    416       C  
ATOM   2940  C   VAL A 417       6.049  -2.017  -0.621  1.00 75.65           C  
ANISOU 2940  C   VAL A 417    10726   8332   9686   -769  -1144    400       C  
ATOM   2941  O   VAL A 417       5.383  -2.367   0.363  1.00 73.28           O  
ANISOU 2941  O   VAL A 417    10419   8044   9381   -909  -1125    429       O  
ATOM   2942  CB  VAL A 417       6.357  -3.847  -2.359  1.00 69.42           C  
ANISOU 2942  CB  VAL A 417    10679   7234   8461   -938  -1241    282       C  
ATOM   2943  CG1 VAL A 417       6.474  -4.740  -1.133  1.00 66.88           C  
ANISOU 2943  CG1 VAL A 417    10605   6693   8112   -911  -1204    262       C  
ATOM   2944  CG2 VAL A 417       5.575  -4.550  -3.446  1.00 68.97           C  
ANISOU 2944  CG2 VAL A 417    10878   7133   8193  -1268  -1387    262       C  
ATOM   2945  N   ASN A 418       7.086  -1.184  -0.510  1.00 69.14           N  
ANISOU 2945  N   ASN A 418     9719   7544   9007   -464  -1071    354       N  
ATOM   2946  CA  ASN A 418       7.506  -0.674   0.790  1.00 59.69           C  
ANISOU 2946  CA  ASN A 418     8331   6385   7962   -263  -1004    296       C  
ATOM   2947  C   ASN A 418       6.365   0.000   1.544  1.00 72.46           C  
ANISOU 2947  C   ASN A 418     9629   8176   9728   -397  -1007    338       C  
ATOM   2948  O   ASN A 418       6.372   0.033   2.780  1.00 78.40           O  
ANISOU 2948  O   ASN A 418    10330   8974  10483   -321   -946    277       O  
ATOM   2949  CB  ASN A 418       8.666   0.302   0.607  1.00 65.48           C  
ANISOU 2949  CB  ASN A 418     8842   7154   8882      6   -958    240       C  
ATOM   2950  CG  ASN A 418       9.105   0.938   1.907  1.00 70.06           C  
ANISOU 2950  CG  ASN A 418     9208   7784   9627    195   -932    141       C  
ATOM   2951  OD1 ASN A 418       9.915   0.373   2.644  1.00 72.31           O  
ANISOU 2951  OD1 ASN A 418     9648   8008   9820    376   -923     50       O  
ATOM   2952  ND2 ASN A 418       8.575   2.123   2.197  1.00 73.88           N  
ANISOU 2952  ND2 ASN A 418     9344   8372  10354    175   -946    143       N  
ATOM   2953  N   SER A 419       5.371   0.528   0.828  1.00 73.71           N  
ANISOU 2953  N   SER A 419     9563   8456   9988   -577  -1081    433       N  
ATOM   2954  CA  SER A 419       4.257   1.208   1.479  1.00 74.87           C  
ANISOU 2954  CA  SER A 419     9342   8795  10311   -653  -1075    444       C  
ATOM   2955  C   SER A 419       3.387   0.269   2.304  1.00 71.13           C  
ANISOU 2955  C   SER A 419     8963   8398   9665   -899  -1010    455       C  
ATOM   2956  O   SER A 419       2.578   0.748   3.105  1.00 79.35           O  
ANISOU 2956  O   SER A 419     9691   9646  10814   -930   -935    423       O  
ATOM   2957  CB  SER A 419       3.402   1.927   0.433  1.00 76.98           C  
ANISOU 2957  CB  SER A 419     9339   9174  10737   -757  -1215    564       C  
ATOM   2958  OG  SER A 419       4.102   3.028  -0.124  1.00 76.00           O  
ANISOU 2958  OG  SER A 419     9078   8985  10813   -542  -1256    597       O  
ATOM   2959  N   ALA A 420       3.532  -1.043   2.146  1.00 64.52           N  
ANISOU 2959  N   ALA A 420     8553   7392   8567  -1076  -1023    494       N  
ATOM   2960  CA  ALA A 420       2.711  -1.998   2.873  1.00 70.62           C  
ANISOU 2960  CA  ALA A 420     9465   8194   9173  -1382   -964    556       C  
ATOM   2961  C   ALA A 420       3.486  -2.802   3.908  1.00 76.87           C  
ANISOU 2961  C   ALA A 420    10638   8808   9762  -1279   -878    546       C  
ATOM   2962  O   ALA A 420       2.886  -3.634   4.598  1.00 79.00           O  
ANISOU 2962  O   ALA A 420    11085   9071   9862  -1550   -815    643       O  
ATOM   2963  CB  ALA A 420       2.026  -2.954   1.892  1.00 69.09           C  
ANISOU 2963  CB  ALA A 420     9496   7901   8853  -1760  -1092    637       C  
ATOM   2964  N   VAL A 421       4.793  -2.590   4.035  1.00 77.91           N  
ANISOU 2964  N   VAL A 421    10893   8806   9904   -910   -888    455       N  
ATOM   2965  CA  VAL A 421       5.579  -3.412   4.946  1.00 79.27           C  
ANISOU 2965  CA  VAL A 421    11443   8799   9879   -770   -869    464       C  
ATOM   2966  C   VAL A 421       5.680  -2.792   6.335  1.00 78.59           C  
ANISOU 2966  C   VAL A 421    11159   8929   9775   -616   -776    415       C  
ATOM   2967  O   VAL A 421       5.844  -3.521   7.319  1.00 80.37           O  
ANISOU 2967  O   VAL A 421    11677   9096   9766   -626   -753    490       O  
ATOM   2968  CB  VAL A 421       6.980  -3.686   4.367  1.00 73.59           C  
ANISOU 2968  CB  VAL A 421    10961   7841   9160   -437   -947    375       C  
ATOM   2969  CG1 VAL A 421       6.871  -4.312   2.991  1.00 71.39           C  
ANISOU 2969  CG1 VAL A 421    10910   7375   8838   -578  -1015    377       C  
ATOM   2970  CG2 VAL A 421       7.810  -2.409   4.324  1.00 65.73           C  
ANISOU 2970  CG2 VAL A 421     9584   7002   8387   -121   -934    246       C  
ATOM   2971  N   ASN A 422       5.581  -1.466   6.440  1.00 74.03           N  
ANISOU 2971  N   ASN A 422    10123   8582   9422   -475   -738    288       N  
ATOM   2972  CA  ASN A 422       5.742  -0.820   7.742  1.00 73.83           C  
ANISOU 2972  CA  ASN A 422     9929   8759   9366   -304   -662    170       C  
ATOM   2973  C   ASN A 422       4.697  -1.265   8.756  1.00 74.68           C  
ANISOU 2973  C   ASN A 422    10063   9076   9236   -564   -510    254       C  
ATOM   2974  O   ASN A 422       5.081  -1.611   9.887  1.00 76.59           O  
ANISOU 2974  O   ASN A 422    10516   9367   9218   -484   -475    261       O  
ATOM   2975  CB  ASN A 422       5.757   0.700   7.560  1.00 72.41           C  
ANISOU 2975  CB  ASN A 422     9279   8717   9517   -120   -663     -7       C  
ATOM   2976  CG  ASN A 422       7.075   1.199   7.026  1.00 70.46           C  
ANISOU 2976  CG  ASN A 422     9018   8305   9448    152   -777    -94       C  
ATOM   2977  OD1 ASN A 422       8.006   0.419   6.829  1.00 69.93           O  
ANISOU 2977  OD1 ASN A 422     9248   8068   9254    251   -842    -54       O  
ATOM   2978  ND2 ASN A 422       7.166   2.500   6.780  1.00 74.23           N  
ANISOU 2978  ND2 ASN A 422     9142   8823  10239    275   -798   -213       N  
ATOM   2979  N   PRO A 423       3.396  -1.299   8.444  1.00 74.98           N  
ANISOU 2979  N   PRO A 423     9889   9275   9326   -884   -418    332       N  
ATOM   2980  CA  PRO A 423       2.439  -1.829   9.431  1.00 79.39           C  
ANISOU 2980  CA  PRO A 423    10466  10068   9629  -1180   -229    435       C  
ATOM   2981  C   PRO A 423       2.722  -3.267   9.832  1.00 83.90           C  
ANISOU 2981  C   PRO A 423    11615  10404   9861  -1378   -249    663       C  
ATOM   2982  O   PRO A 423       2.406  -3.662  10.961  1.00 90.16           O  
ANISOU 2982  O   PRO A 423    12538  11363  10356  -1521    -99    763       O  
ATOM   2983  CB  PRO A 423       1.089  -1.697   8.713  1.00 72.48           C  
ANISOU 2983  CB  PRO A 423     9227   9375   8937  -1503   -180    488       C  
ATOM   2984  CG  PRO A 423       1.299  -0.620   7.719  1.00 68.97           C  
ANISOU 2984  CG  PRO A 423     8463   8890   8854  -1250   -321    353       C  
ATOM   2985  CD  PRO A 423       2.703  -0.792   7.246  1.00 69.67           C  
ANISOU 2985  CD  PRO A 423     8902   8634   8934   -993   -481    335       C  
ATOM   2986  N   ILE A 424       3.313  -4.062   8.939  1.00 83.26           N  
ANISOU 2986  N   ILE A 424    11907   9927   9801  -1380   -427    747       N  
ATOM   2987  CA  ILE A 424       3.682  -5.430   9.285  1.00 83.10           C  
ANISOU 2987  CA  ILE A 424    12489   9580   9504  -1500   -487    952       C  
ATOM   2988  C   ILE A 424       4.819  -5.441  10.300  1.00 81.27           C  
ANISOU 2988  C   ILE A 424    12492   9304   9083  -1119   -542    931       C  
ATOM   2989  O   ILE A 424       4.919  -6.359  11.125  1.00 80.08           O  
ANISOU 2989  O   ILE A 424    12773   9025   8629  -1213   -546   1138       O  
ATOM   2990  CB  ILE A 424       4.040  -6.206   8.002  1.00 78.55           C  
ANISOU 2990  CB  ILE A 424    12237   8582   9027  -1536   -666    971       C  
ATOM   2991  CG1 ILE A 424       2.825  -6.276   7.073  1.00 73.56           C  
ANISOU 2991  CG1 ILE A 424    11398   8028   8524  -1971   -654   1003       C  
ATOM   2992  CG2 ILE A 424       4.560  -7.600   8.325  1.00 80.22           C  
ANISOU 2992  CG2 ILE A 424    13116   8357   9008  -1567   -766   1149       C  
ATOM   2993  CD1 ILE A 424       3.095  -6.975   5.758  1.00 71.89           C  
ANISOU 2993  CD1 ILE A 424    11502   7446   8367  -2028   -834    970       C  
ATOM   2994  N   ILE A 425       5.680  -4.422  10.275  1.00 72.91           N  
ANISOU 2994  N   ILE A 425    11155   8352   8197   -705   -607    699       N  
ATOM   2995  CA  ILE A 425       6.795  -4.363  11.215  1.00 77.19           C  
ANISOU 2995  CA  ILE A 425    11857   8894   8577   -341   -708    646       C  
ATOM   2996  C   ILE A 425       6.320  -3.961  12.608  1.00 86.64           C  
ANISOU 2996  C   ILE A 425    12947  10469   9504   -403   -561    636       C  
ATOM   2997  O   ILE A 425       6.863  -4.432  13.615  1.00 84.58           O  
ANISOU 2997  O   ILE A 425    13008  10207   8921   -280   -633    733       O  
ATOM   2998  CB  ILE A 425       7.877  -3.406  10.689  1.00 71.65           C  
ANISOU 2998  CB  ILE A 425    10863   8188   8172     58   -830    392       C  
ATOM   2999  CG1 ILE A 425       8.343  -3.850   9.303  1.00 71.05           C  
ANISOU 2999  CG1 ILE A 425    10906   7796   8294    111   -926    402       C  
ATOM   3000  CG2 ILE A 425       9.062  -3.360  11.634  1.00 68.37           C  
ANISOU 3000  CG2 ILE A 425    10565   7798   7613    422   -980    318       C  
ATOM   3001  CD1 ILE A 425       9.377  -2.939   8.685  1.00 69.86           C  
ANISOU 3001  CD1 ILE A 425    10448   7667   8427    435  -1000    194       C  
ATOM   3002  N   TYR A 426       5.302  -3.102  12.695  1.00 80.85           N  
ANISOU 3002  N   TYR A 426    11769  10077   8874   -571   -359    514       N  
ATOM   3003  CA  TYR A 426       4.811  -2.668  13.999  1.00 87.40           C  
ANISOU 3003  CA  TYR A 426    12467  11316   9424   -609   -172    444       C  
ATOM   3004  C   TYR A 426       4.159  -3.813  14.767  1.00 95.75           C  
ANISOU 3004  C   TYR A 426    13906  12427  10045   -980    -30    771       C  
ATOM   3005  O   TYR A 426       4.175  -3.815  16.004  1.00 99.16           O  
ANISOU 3005  O   TYR A 426    14463  13130  10085   -961     67    794       O  
ATOM   3006  CB  TYR A 426       3.826  -1.511  13.828  1.00 86.99           C  
ANISOU 3006  CB  TYR A 426    11825  11596   9630   -664     22    214       C  
ATOM   3007  CG  TYR A 426       4.370  -0.345  13.027  1.00 85.70           C  
ANISOU 3007  CG  TYR A 426    11311  11332   9920   -350   -120    -55       C  
ATOM   3008  CD1 TYR A 426       5.706   0.027  13.118  1.00 83.30           C  
ANISOU 3008  CD1 TYR A 426    11097  10869   9684      2   -327   -201       C  
ATOM   3009  CD2 TYR A 426       3.547   0.381  12.176  1.00 83.93           C  
ANISOU 3009  CD2 TYR A 426    10656  11172  10061   -422    -61   -137       C  
ATOM   3010  CE1 TYR A 426       6.206   1.093  12.385  1.00 79.72           C  
ANISOU 3010  CE1 TYR A 426    10330  10311   9648    224   -438   -408       C  
ATOM   3011  CE2 TYR A 426       4.037   1.447  11.441  1.00 82.37           C  
ANISOU 3011  CE2 TYR A 426    10186  10845  10265   -163   -196   -323       C  
ATOM   3012  CZ  TYR A 426       5.368   1.799  11.548  1.00 77.29           C  
ANISOU 3012  CZ  TYR A 426     9656  10030   9679    135   -368   -452       C  
ATOM   3013  OH  TYR A 426       5.859   2.858  10.815  1.00 65.48           O  
ANISOU 3013  OH  TYR A 426     7898   8395   8588    330   -485   -601       O  
ATOM   3014  N   THR A 427       3.583  -4.790  14.059  1.00 94.12           N  
ANISOU 3014  N   THR A 427    13912  11967   9880  -1346    -21   1029       N  
ATOM   3015  CA  THR A 427       2.981  -5.936  14.735  1.00 94.73           C  
ANISOU 3015  CA  THR A 427    14395  12024   9574  -1766    104   1385       C  
ATOM   3016  C   THR A 427       4.036  -6.873  15.301  1.00 93.77           C  
ANISOU 3016  C   THR A 427    14923  11553   9151  -1581   -115   1608       C  
ATOM   3017  O   THR A 427       3.779  -7.565  16.293  1.00107.23           O  
ANISOU 3017  O   THR A 427    16989  13325  10429  -1808    -22   1896       O  
ATOM   3018  CB  THR A 427       2.076  -6.711  13.777  1.00 92.02           C  
ANISOU 3018  CB  THR A 427    14101  11462   9402  -2246    135   1572       C  
ATOM   3019  OG1 THR A 427       2.869  -7.267  12.722  1.00 87.69           O  
ANISOU 3019  OG1 THR A 427    13873  10378   9067  -2083   -148   1577       O  
ATOM   3020  CG2 THR A 427       1.028  -5.801  13.182  1.00 92.49           C  
ANISOU 3020  CG2 THR A 427    13488  11881   9771  -2397    298   1371       C  
ATOM   3021  N   THR A 428       5.216  -6.918  14.687  1.00 86.78           N  
ANISOU 3021  N   THR A 428    14188  10309   8477  -1167   -404   1497       N  
ATOM   3022  CA  THR A 428       6.250  -7.850  15.112  1.00 80.90           C  
ANISOU 3022  CA  THR A 428    14030   9197   7512   -924   -656   1699       C  
ATOM   3023  C   THR A 428       7.087  -7.298  16.260  1.00 88.26           C  
ANISOU 3023  C   THR A 428    14945  10410   8178   -536   -758   1595       C  
ATOM   3024  O   THR A 428       7.228  -7.954  17.297  1.00 98.04           O  
ANISOU 3024  O   THR A 428    16618  11653   8981   -567   -810   1867       O  
ATOM   3025  CB  THR A 428       7.162  -8.200  13.934  1.00 75.14           C  
ANISOU 3025  CB  THR A 428    13433   7992   7124   -626   -905   1599       C  
ATOM   3026  OG1 THR A 428       6.369  -8.438  12.764  1.00 66.95           O  
ANISOU 3026  OG1 THR A 428    12310   6784   6344   -965   -819   1592       O  
ATOM   3027  CG2 THR A 428       7.977  -9.450  14.258  1.00 74.10           C  
ANISOU 3027  CG2 THR A 428    13971   7385   6798   -439  -1156   1861       C  
ATOM   3028  N   PHE A 429       7.642  -6.097  16.092  1.00 82.80           N  
ANISOU 3028  N   PHE A 429    13778   9948   7733   -194   -807   1216       N  
ATOM   3029  CA  PHE A 429       8.628  -5.569  17.024  1.00 85.65           C  
ANISOU 3029  CA  PHE A 429    14115  10520   7909    205   -988   1057       C  
ATOM   3030  C   PHE A 429       8.031  -4.731  18.145  1.00 88.27           C  
ANISOU 3030  C   PHE A 429    14208  11398   7933    109   -780    904       C  
ATOM   3031  O   PHE A 429       8.759  -4.373  19.077  1.00 94.52           O  
ANISOU 3031  O   PHE A 429    15046  12401   8467    386   -940    780       O  
ATOM   3032  CB  PHE A 429       9.666  -4.731  16.274  1.00 81.51           C  
ANISOU 3032  CB  PHE A 429    13220   9923   7826    606  -1176    717       C  
ATOM   3033  CG  PHE A 429      10.610  -5.545  15.451  1.00 86.84           C  
ANISOU 3033  CG  PHE A 429    14151  10141   8702    848  -1415    814       C  
ATOM   3034  CD1 PHE A 429      11.723  -6.132  16.031  1.00 95.71           C  
ANISOU 3034  CD1 PHE A 429    15590  11131   9647   1208  -1714    909       C  
ATOM   3035  CD2 PHE A 429      10.383  -5.736  14.099  1.00 90.50           C  
ANISOU 3035  CD2 PHE A 429    14539  10330   9515    740  -1348    797       C  
ATOM   3036  CE1 PHE A 429      12.597  -6.891  15.275  1.00100.77           C  
ANISOU 3036  CE1 PHE A 429    16434  11359  10493   1488  -1918    962       C  
ATOM   3037  CE2 PHE A 429      11.253  -6.492  13.334  1.00 94.15           C  
ANISOU 3037  CE2 PHE A 429    15239  10395  10137    990  -1533    835       C  
ATOM   3038  CZ  PHE A 429      12.362  -7.070  13.923  1.00 99.97           C  
ANISOU 3038  CZ  PHE A 429    16261  10992  10733   1381  -1805    907       C  
ATOM   3039  N   ASN A 430       6.743  -4.409  18.090  1.00 83.72           N  
ANISOU 3039  N   ASN A 430    13363  11080   7368   -257   -438    882       N  
ATOM   3040  CA  ASN A 430       6.116  -3.571  19.103  1.00 88.98           C  
ANISOU 3040  CA  ASN A 430    13756  12293   7759   -315   -190    673       C  
ATOM   3041  C   ASN A 430       4.910  -4.295  19.678  1.00 94.26           C  
ANISOU 3041  C   ASN A 430    14603  13185   8026   -804    139    994       C  
ATOM   3042  O   ASN A 430       3.949  -4.578  18.954  1.00 90.37           O  
ANISOU 3042  O   ASN A 430    13952  12628   7755  -1162    332   1116       O  
ATOM   3043  CB  ASN A 430       5.708  -2.218  18.523  1.00 82.34           C  
ANISOU 3043  CB  ASN A 430    12274  11632   7378   -219    -60    251       C  
ATOM   3044  CG  ASN A 430       5.177  -1.278  19.577  1.00 86.94           C  
ANISOU 3044  CG  ASN A 430    12575  12746   7711   -183    175    -57       C  
ATOM   3045  OD1 ASN A 430       3.978  -1.247  19.844  1.00 86.57           O  
ANISOU 3045  OD1 ASN A 430    12339  13023   7531   -474    525    -28       O  
ATOM   3046  ND2 ASN A 430       6.069  -0.510  20.193  1.00 93.49           N  
ANISOU 3046  ND2 ASN A 430    13362  13689   8473    174    -14   -380       N  
ATOM   3047  N   ILE A 431       4.963  -4.590  20.979  1.00 96.66           N  
ANISOU 3047  N   ILE A 431    15226  13779   7721   -842    197   1137       N  
ATOM   3048  CA  ILE A 431       3.848  -5.262  21.638  1.00 92.58           C  
ANISOU 3048  CA  ILE A 431    14883  13536   6757  -1346    552   1472       C  
ATOM   3049  C   ILE A 431       2.630  -4.348  21.695  1.00 98.55           C  
ANISOU 3049  C   ILE A 431    15013  14819   7614  -1537    984   1175       C  
ATOM   3050  O   ILE A 431       1.488  -4.806  21.569  1.00 98.81           O  
ANISOU 3050  O   ILE A 431    14936  14997   7611  -2018   1303   1397       O  
ATOM   3051  CB  ILE A 431       4.263  -5.738  23.042  1.00 91.00           C  
ANISOU 3051  CB  ILE A 431    15200  13558   5818  -1318    503   1710       C  
ATOM   3052  N   GLU A 432       2.851  -3.043  21.881  1.00 96.20           N  
ANISOU 3052  N   GLU A 432    14279  14803   7470  -1163    992    657       N  
ATOM   3053  CA  GLU A 432       1.733  -2.109  21.979  1.00 93.30           C  
ANISOU 3053  CA  GLU A 432    13305  14920   7225  -1248   1385    325       C  
ATOM   3054  C   GLU A 432       1.005  -1.971  20.646  1.00 90.82           C  
ANISOU 3054  C   GLU A 432    12560  14400   7549  -1408   1437    316       C  
ATOM   3055  O   GLU A 432      -0.230  -1.927  20.610  1.00 84.30           O  
ANISOU 3055  O   GLU A 432    11363  13912   6757  -1725   1791    333       O  
ATOM   3056  CB  GLU A 432       2.229  -0.750  22.471  1.00 88.42           C  
ANISOU 3056  CB  GLU A 432    12394  14544   6659   -774   1324   -250       C  
ATOM   3057  N   PHE A 433       1.747  -1.901  19.538  1.00 90.26           N  
ANISOU 3057  N   PHE A 433    12509  13817   7970  -1197   1087    288       N  
ATOM   3058  CA  PHE A 433       1.098  -1.850  18.232  1.00 93.03           C  
ANISOU 3058  CA  PHE A 433    12520  13969   8860  -1363   1090    317       C  
ATOM   3059  C   PHE A 433       0.366  -3.155  17.929  1.00 92.59           C  
ANISOU 3059  C   PHE A 433    12717  13789   8674  -1909   1194    776       C  
ATOM   3060  O   PHE A 433      -0.768  -3.136  17.438  1.00 86.48           O  
ANISOU 3060  O   PHE A 433    11554  13195   8111  -2229   1396    805       O  
ATOM   3061  CB  PHE A 433       2.125  -1.540  17.137  1.00 94.23           C  
ANISOU 3061  CB  PHE A 433    12696  13628   9479  -1036    712    208       C  
ATOM   3062  CG  PHE A 433       2.253  -0.070  16.807  1.00 90.02           C  
ANISOU 3062  CG  PHE A 433    11657  13176   9371   -672    669   -233       C  
ATOM   3063  CD1 PHE A 433       1.220   0.604  16.178  1.00 82.18           C  
ANISOU 3063  CD1 PHE A 433    10137  12335   8753   -746    821   -367       C  
ATOM   3064  CD2 PHE A 433       3.413   0.630  17.106  1.00 88.82           C  
ANISOU 3064  CD2 PHE A 433    11559  12920   9269   -265    446   -498       C  
ATOM   3065  CE1 PHE A 433       1.331   1.949  15.867  1.00 78.56           C  
ANISOU 3065  CE1 PHE A 433     9265  11877   8709   -401    756   -738       C  
ATOM   3066  CE2 PHE A 433       3.531   1.976  16.796  1.00 82.75           C  
ANISOU 3066  CE2 PHE A 433    10368  12155   8919     24    394   -882       C  
ATOM   3067  CZ  PHE A 433       2.487   2.635  16.177  1.00 81.74           C  
ANISOU 3067  CZ  PHE A 433     9768  12128   9161    -34    550   -991       C  
ATOM   3068  N   ARG A 434       0.991  -4.296  18.232  1.00 96.08           N  
ANISOU 3068  N   ARG A 434    13805  13913   8786  -2025   1037   1134       N  
ATOM   3069  CA  ARG A 434       0.385  -5.588  17.918  1.00 91.88           C  
ANISOU 3069  CA  ARG A 434    13600  13146   8164  -2562   1089   1576       C  
ATOM   3070  C   ARG A 434      -0.930  -5.778  18.663  1.00 88.38           C  
ANISOU 3070  C   ARG A 434    12942  13229   7411  -3068   1532   1730       C  
ATOM   3071  O   ARG A 434      -1.944  -6.162  18.068  1.00 89.59           O  
ANISOU 3071  O   ARG A 434    12864  13413   7764  -3530   1674   1870       O  
ATOM   3072  CB  ARG A 434       1.360  -6.718  18.249  1.00 91.99           C  
ANISOU 3072  CB  ARG A 434    14390  12689   7871  -2520    823   1923       C  
ATOM   3073  N   LYS A 435      -0.934  -5.515  19.973  1.00 92.30           N  
ANISOU 3073  N   LYS A 435    13491  14183   7397  -3005   1759   1697       N  
ATOM   3074  CA  LYS A 435      -2.157  -5.679  20.753  1.00 95.80           C  
ANISOU 3074  CA  LYS A 435    13709  15207   7485  -3485   2243   1837       C  
ATOM   3075  C   LYS A 435      -3.199  -4.633  20.385  1.00 95.39           C  
ANISOU 3075  C   LYS A 435    12798  15636   7810  -3466   2525   1447       C  
ATOM   3076  O   LYS A 435      -4.399  -4.865  20.566  1.00100.11           O  
ANISOU 3076  O   LYS A 435    13054  16654   8329  -3942   2904   1572       O  
ATOM   3077  CB  LYS A 435      -1.843  -5.617  22.249  1.00100.45           C  
ANISOU 3077  CB  LYS A 435    14594  16206   7366  -3383   2418   1871       C  
ATOM   3078  N   ALA A 436      -2.763  -3.482  19.869  1.00 97.48           N  
ANISOU 3078  N   ALA A 436    12695  15840   8503  -2926   2339    989       N  
ATOM   3079  CA  ALA A 436      -3.711  -2.457  19.446  1.00 99.12           C  
ANISOU 3079  CA  ALA A 436    12109  16422   9131  -2835   2542    627       C  
ATOM   3080  C   ALA A 436      -4.463  -2.884  18.193  1.00 98.71           C  
ANISOU 3080  C   ALA A 436    11791  16164   9549  -3194   2456    809       C  
ATOM   3081  O   ALA A 436      -5.682  -2.702  18.103  1.00 98.79           O  
ANISOU 3081  O   ALA A 436    11222  16613   9701  -3464   2744    764       O  
ATOM   3082  CB  ALA A 436      -2.984  -1.133  19.210  1.00 94.08           C  
ANISOU 3082  CB  ALA A 436    11230  15675   8839  -2179   2321    134       C  
ATOM   3083  N   PHE A 437      -3.753  -3.456  17.217  1.00 90.64           N  
ANISOU 3083  N   PHE A 437    11168  14510   8763  -3193   2056    991       N  
ATOM   3084  CA  PHE A 437      -4.405  -3.888  15.985  1.00 89.75           C  
ANISOU 3084  CA  PHE A 437    10864  14185   9052  -3536   1925   1136       C  
ATOM   3085  C   PHE A 437      -5.403  -5.004  16.256  1.00 98.61           C  
ANISOU 3085  C   PHE A 437    12055  15479   9935  -4263   2173   1518       C  
ATOM   3086  O   PHE A 437      -6.491  -5.031  15.669  1.00 97.68           O  
ANISOU 3086  O   PHE A 437    11436  15585  10092  -4617   2265   1534       O  
ATOM   3087  CB  PHE A 437      -3.365  -4.353  14.965  1.00 85.17           C  
ANISOU 3087  CB  PHE A 437    10775  12904   8681  -3381   1477   1231       C  
ATOM   3088  CG  PHE A 437      -2.480  -3.255  14.437  1.00 86.40           C  
ANISOU 3088  CG  PHE A 437    10779  12886   9165  -2763   1230    890       C  
ATOM   3089  CD1 PHE A 437      -2.661  -1.937  14.822  1.00 90.40           C  
ANISOU 3089  CD1 PHE A 437    10767  13767   9814  -2388   1365    522       C  
ATOM   3090  CD2 PHE A 437      -1.469  -3.548  13.540  1.00 80.59           C  
ANISOU 3090  CD2 PHE A 437    10422  11598   8603  -2569    873    931       C  
ATOM   3091  CE1 PHE A 437      -1.838  -0.938  14.328  1.00 85.90           C  
ANISOU 3091  CE1 PHE A 437    10090  12981   9568  -1879   1127    241       C  
ATOM   3092  CE2 PHE A 437      -0.645  -2.555  13.044  1.00 80.08           C  
ANISOU 3092  CE2 PHE A 437    10206  11388   8833  -2065    672    655       C  
ATOM   3093  CZ  PHE A 437      -0.831  -1.248  13.438  1.00 81.28           C  
ANISOU 3093  CZ  PHE A 437     9867  11875   9140  -1744    789    329       C  
ATOM   3094  N   LEU A 438      -5.047  -5.938  17.144  1.00 97.43           N  
ANISOU 3094  N   LEU A 438    12520  15222   9276  -4511   2262   1848       N  
ATOM   3095  CA  LEU A 438      -5.930  -7.059  17.446  1.00 99.16           C  
ANISOU 3095  CA  LEU A 438    12887  15540   9250  -5265   2497   2270       C  
ATOM   3096  C   LEU A 438      -7.187  -6.605  18.176  1.00104.88           C  
ANISOU 3096  C   LEU A 438    12926  17091   9832  -5548   3020   2189       C  
ATOM   3097  O   LEU A 438      -8.233  -7.257  18.066  1.00112.28           O  
ANISOU 3097  O   LEU A 438    13646  18228  10786  -6211   3228   2440       O  
ATOM   3098  CB  LEU A 438      -5.179  -8.106  18.269  1.00101.79           C  
ANISOU 3098  CB  LEU A 438    14093  15526   9057  -5410   2445   2676       C  
ATOM   3099  N   LYS A 439      -7.108  -5.501  18.923  1.00104.77           N  
ANISOU 3099  N   LYS A 439    12553  17573   9684  -5064   3242   1817       N  
ATOM   3100  CA  LYS A 439      -8.295  -4.960  19.574  1.00111.86           C  
ANISOU 3100  CA  LYS A 439    12728  19296  10480  -5232   3763   1648       C  
ATOM   3101  C   LYS A 439      -9.200  -4.234  18.588  1.00113.57           C  
ANISOU 3101  C   LYS A 439    12089  19730  11334  -5165   3740   1359       C  
ATOM   3102  O   LYS A 439     -10.419  -4.192  18.788  1.00116.22           O  
ANISOU 3102  O   LYS A 439    11788  20658  11710  -5514   4113   1349       O  
ATOM   3103  CB  LYS A 439      -7.894  -4.019  20.711  1.00111.35           C  
ANISOU 3103  CB  LYS A 439    12602  19665  10042  -4703   3997   1288       C  
ATOM   3104  N   ILE A 440      -8.629  -3.664  17.526  1.00111.11           N  
ANISOU 3104  N   ILE A 440    11741  18958  11519  -4713   3295   1139       N  
ATOM   3105  CA  ILE A 440      -9.451  -3.036  16.502  1.00110.51           C  
ANISOU 3105  CA  ILE A 440    10923  19028  12037  -4650   3192    931       C  
ATOM   3106  C   ILE A 440     -10.182  -4.088  15.675  1.00112.85           C  
ANISOU 3106  C   ILE A 440    11191  19185  12503  -5352   3077   1285       C  
ATOM   3107  O   ILE A 440     -11.326  -3.874  15.259  1.00112.91           O  
ANISOU 3107  O   ILE A 440    10465  19613  12823  -5584   3184   1219       O  
ATOM   3108  CB  ILE A 440      -8.581  -2.115  15.629  1.00104.69           C  
ANISOU 3108  CB  ILE A 440    10219  17834  11725  -3988   2753    640       C  
ATOM   3109  CG1 ILE A 440      -7.927  -1.040  16.500  1.00107.61           C  
ANISOU 3109  CG1 ILE A 440    10580  18352  11953  -3351   2868    257       C  
ATOM   3110  CG2 ILE A 440      -9.411  -1.469  14.537  1.00101.39           C  
ANISOU 3110  CG2 ILE A 440     9088  17539  11896  -3905   2594    477       C  
ATOM   3111  CD1 ILE A 440      -7.131  -0.015  15.728  1.00100.57           C  
ANISOU 3111  CD1 ILE A 440     9658  17052  11502  -2734   2483    -35       C  
ATOM   3112  N   LEU A 441      -9.554  -5.245  15.440  1.00112.02           N  
ANISOU 3112  N   LEU A 441    11866  18490  12207  -5698   2844   1648       N  
ATOM   3113  CA  LEU A 441     -10.167  -6.342  14.697  1.00113.38           C  
ANISOU 3113  CA  LEU A 441    12136  18432  12510  -6402   2704   1969       C  
ATOM   3114  C   LEU A 441     -10.959  -7.287  15.593  1.00125.26           C  
ANISOU 3114  C   LEU A 441    13779  20090  13724  -6864   2989   2236       C  
ATOM   3115  O   LEU A 441     -11.000  -8.499  15.335  1.00130.59           O  
ANISOU 3115  O   LEU A 441    14979  20276  14364  -7284   2800   2536       O  
ATOM   3116  CB  LEU A 441      -9.096  -7.115  13.924  1.00105.56           C  
ANISOU 3116  CB  LEU A 441    11981  16582  11546  -6372   2234   2137       C  
ATOM   3117  CG  LEU A 441      -8.272  -6.304  12.915  1.00100.01           C  
ANISOU 3117  CG  LEU A 441    11276  15521  11203  -5710   1825   1833       C  
ATOM   3118  CD1 LEU A 441      -7.049  -7.083  12.435  1.00 92.92           C  
ANISOU 3118  CD1 LEU A 441    11249  13839  10218  -5600   1460   1975       C  
ATOM   3119  CD2 LEU A 441      -9.133  -5.880  11.735  1.00101.27           C  
ANISOU 3119  CD2 LEU A 441    10791  15843  11843  -5803   1635   1687       C  
ATOM   3120  N   HIS A 442     -11.587  -6.766  16.640  1.00118.20           N  
ANISOU 3120  N   HIS A 442    12431  19851  12628  -6779   3439   2114       N  
ATOM   3121  CA  HIS A 442     -12.365  -7.591  17.554  1.00126.48           C  
ANISOU 3121  CA  HIS A 442    13562  21110  13385  -7224   3754   2376       C  
ATOM   3122  C   HIS A 442     -13.375  -6.752  18.337  1.00131.96           C  
ANISOU 3122  C   HIS A 442    13462  22622  14057  -7071   4227   2114       C  
ATOM   3123  O   HIS A 442     -14.028  -5.864  17.785  1.00131.46           O  
ANISOU 3123  O   HIS A 442    12638  22887  14424  -6809   4221   1787       O  
ATOM   3124  CB  HIS A 442     -11.436  -8.335  18.515  1.00127.27           C  
ANISOU 3124  CB  HIS A 442    14545  20900  12913  -7295   3807   2692       C  
TER    3125      HIS A 442                                                      
HETATM 3126  C01 8NU A2001       5.798   4.520 -12.898  1.00 53.67           C  
HETATM 3127  C02 8NU A2001       7.144   4.033 -13.365  1.00 73.44           C  
HETATM 3128  C03 8NU A2001       8.262   4.600 -12.909  1.00 81.52           C  
HETATM 3129  C04 8NU A2001       8.206   5.746 -11.897  1.00 83.19           C  
HETATM 3130  C05 8NU A2001       8.798   5.236 -10.556  1.00 77.95           C  
HETATM 3131  C07 8NU A2001       9.857   7.323  -9.903  1.00 83.90           C  
HETATM 3132  C08 8NU A2001      10.085   8.347  -8.777  1.00 87.68           C  
HETATM 3133  C09 8NU A2001      10.598   7.582  -7.553  1.00 81.18           C  
HETATM 3134  C10 8NU A2001       9.569   6.528  -7.120  1.00 68.50           C  
HETATM 3135  C11 8NU A2001       9.363   5.565  -8.280  1.00 79.77           C  
HETATM 3136  C12 8NU A2001      10.978   8.513  -6.434  1.00 83.67           C  
HETATM 3137  C15 8NU A2001      11.604   9.387  -4.561  1.00 77.42           C  
HETATM 3138  C16 8NU A2001      11.346   8.184  -5.148  1.00 77.32           C  
HETATM 3139  C17 8NU A2001      11.480   6.976  -4.482  1.00 58.28           C  
HETATM 3140  C18 8NU A2001      11.893   7.042  -3.152  1.00 57.84           C  
HETATM 3141  C19 8NU A2001      12.158   8.271  -2.538  1.00 70.59           C  
HETATM 3142  C21 8NU A2001      12.017   9.471  -3.239  1.00 71.68           C  
HETATM 3143  C22 8NU A2001       9.544   4.089 -13.391  1.00 77.92           C  
HETATM 3144  C25 8NU A2001      10.828   2.550 -14.812  1.00 72.98           C  
HETATM 3145  C26 8NU A2001      10.659   1.689 -16.072  1.00 63.09           C  
HETATM 3146  C27 8NU A2001       9.633   0.613 -15.771  1.00 79.48           C  
HETATM 3147  C28 8NU A2001       8.257   1.284 -15.641  1.00 81.12           C  
HETATM 3148  C29 8NU A2001       8.311   2.465 -14.703  1.00 76.00           C  
HETATM 3149  F20 8NU A2001      12.555   8.290  -1.257  1.00 71.11           F  
HETATM 3150  N06 8NU A2001       8.882   6.272  -9.486  1.00 82.54           N  
HETATM 3151  N13 8NU A2001      11.047   9.842  -6.521  1.00 87.02           N  
HETATM 3152  N24 8NU A2001       9.552   3.033 -14.306  1.00 78.56           N  
HETATM 3153  N30 8NU A2001       7.209   2.946 -14.270  1.00 76.66           N  
HETATM 3154  O14 8NU A2001      11.404  10.328  -5.431  1.00 84.77           O  
HETATM 3155  O23 8NU A2001      10.714   4.653 -12.983  1.00 74.60           O  
HETATM 3156  C1  PEG A2002      13.738  19.153  11.296  1.00 72.10           C  
HETATM 3157  O1  PEG A2002      13.425  19.871  12.503  1.00 65.09           O  
HETATM 3158  C2  PEG A2002      12.621  18.262  10.668  1.00 83.14           C  
HETATM 3159  O2  PEG A2002      12.675  18.051   9.395  1.00 87.46           O  
HETATM 3160  C3  PEG A2002      12.767  16.692   8.891  1.00 81.97           C  
HETATM 3161  C4  PEG A2002      12.969  16.518   7.378  1.00 79.46           C  
HETATM 3162  O4  PEG A2002      14.040  17.136   6.817  1.00 81.73           O  
HETATM 3163  C1  PEG A2003      22.198   2.267  14.051  1.00 85.07           C  
HETATM 3164  O1  PEG A2003      22.242   2.005  12.633  1.00 77.13           O  
HETATM 3165  C2  PEG A2003      20.827   2.102  14.782  1.00 84.42           C  
HETATM 3166  O2  PEG A2003      20.817   2.118  16.075  1.00 85.32           O  
HETATM 3167  C3  PEG A2003      19.883   1.249  16.778  1.00 93.34           C  
HETATM 3168  C4  PEG A2003      20.010   1.103  18.306  1.00 94.49           C  
HETATM 3169  O4  PEG A2003      21.115   0.493  18.807  1.00 88.36           O  
HETATM 3170  C1  PEG A2004      -5.266   7.216 -12.595  1.00 78.78           C  
HETATM 3171  O1  PEG A2004      -5.406   6.769 -13.959  1.00 82.42           O  
HETATM 3172  C2  PEG A2004      -6.274   8.287 -12.075  1.00 83.69           C  
HETATM 3173  O2  PEG A2004      -5.917   9.017 -11.072  1.00 95.26           O  
HETATM 3174  C3  PEG A2004      -6.353   8.668  -9.728  1.00 95.45           C  
HETATM 3175  C4  PEG A2004      -6.658   9.830  -8.768  1.00 93.47           C  
HETATM 3176  O4  PEG A2004      -5.847  10.916  -8.828  1.00 94.71           O  
HETATM 3177  C1  OLA A2005      19.754  16.684  15.996  1.00103.47           C  
HETATM 3178  O1  OLA A2005      19.134  17.736  15.945  1.00106.47           O1-
HETATM 3179  O2  OLA A2005      19.858  16.092  17.050  1.00100.57           O  
HETATM 3180  C2  OLA A2005      20.380  16.079  14.781  1.00100.30           C  
HETATM 3181  C3  OLA A2005      21.721  15.459  15.111  1.00 85.16           C  
HETATM 3182  C4  OLA A2005      22.296  14.616  13.989  1.00 75.85           C  
HETATM 3183  C5  OLA A2005      22.315  15.351  12.658  1.00 76.55           C  
HETATM 3184  C6  OLA A2005      23.649  15.221  11.960  1.00 84.25           C  
HETATM 3185  C7  OLA A2005      23.502  15.265  10.460  1.00 79.47           C  
HETATM 3186  C8  OLA A2005      23.089  16.616   9.956  1.00 79.39           C  
HETATM 3187  C9  OLA A2005      23.686  16.861   8.593  1.00 69.85           C  
HETATM 3188  C10 OLA A2005      24.899  17.367   8.461  1.00 53.24           C  
HETATM 3189  C11 OLA A2005      25.483  17.608   7.100  1.00 53.87           C  
HETATM 3190  C1  OLA A2006      20.492   1.698   9.419  1.00 90.11           C  
HETATM 3191  O1  OLA A2006      20.499   0.477   9.482  1.00 88.05           O1-
HETATM 3192  O2  OLA A2006      21.139   2.360  10.195  1.00 99.57           O  
HETATM 3193  C2  OLA A2006      19.685   2.399   8.399  1.00 78.95           C  
HETATM 3194  C3  OLA A2006      20.418   3.603   7.911  1.00 70.44           C  
HETATM 3195  C4  OLA A2006      19.398   4.667   7.677  1.00 69.07           C  
HETATM 3196  C5  OLA A2006      18.568   4.321   6.487  1.00 67.97           C  
HETATM 3197  C6  OLA A2006      18.593   5.497   5.570  1.00 62.32           C  
HETATM 3198  C7  OLA A2006      17.322   6.257   5.694  1.00 57.29           C  
HETATM 3199  C8  OLA A2006      17.070   6.697   4.296  1.00 63.53           C  
HETATM 3200  C9  OLA A2006      15.693   7.225   4.217  1.00 74.02           C  
HETATM 3201  C10 OLA A2006      15.463   8.094   3.273  1.00 81.56           C  
HETATM 3202  C1  OLA A2007      20.946  19.605   5.507  1.00104.81           C  
HETATM 3203  O1  OLA A2007      20.786  19.480   4.293  1.00106.45           O1-
HETATM 3204  O2  OLA A2007      21.833  19.000   6.102  1.00106.45           O  
HETATM 3205  C2  OLA A2007      20.063  20.532   6.282  1.00 99.47           C  
HETATM 3206  C3  OLA A2007      19.930  20.039   7.714  1.00 92.83           C  
HETATM 3207  C4  OLA A2007      19.660  21.205   8.650  1.00 89.51           C  
HETATM 3208  C5  OLA A2007      18.925  20.737   9.890  1.00 90.62           C  
HETATM 3209  C6  OLA A2007      18.698  21.919  10.797  1.00 87.43           C  
HETATM 3210  C7  OLA A2007      19.145  21.568  12.187  1.00 87.56           C  
HETATM 3211  C8  OLA A2007      17.984  21.172  13.062  1.00 92.99           C  
HETATM 3212  C9  OLA A2007      18.045  22.031  14.289  1.00 97.77           C  
HETATM 3213  C10 OLA A2007      17.496  21.625  15.424  1.00104.05           C  
HETATM 3214  C11 OLA A2007      16.783  20.300  15.516  1.00106.41           C  
HETATM 3215  C12 OLA A2007      15.861  20.259  16.733  1.00108.65           C  
HETATM 3216  C13 OLA A2007      16.546  20.802  17.987  1.00108.30           C  
HETATM 3217  C14 OLA A2007      16.078  20.161  19.288  1.00104.26           C  
HETATM 3218  C15 OLA A2007      15.097  21.040  20.036  1.00103.67           C  
HETATM 3219  C16 OLA A2007      14.019  21.544  19.086  1.00108.16           C  
HETATM 3220  C17 OLA A2007      13.012  22.466  19.761  1.00101.56           C  
HETATM 3221  C18 OLA A2007      12.822  23.759  18.999  1.00 93.87           C  
HETATM 3222  O   HOH A2101      15.559  11.273 -16.923  1.00 85.24           O  
HETATM 3223  O   HOH A2102      13.685   6.206  10.425  1.00 56.75           O  
HETATM 3224  O   HOH A2103      11.676   4.647  10.912  1.00 71.92           O  
HETATM 3225  O   HOH A2104      51.603  -6.966  43.388  1.00114.99           O  
HETATM 3226  O   HOH A2105      13.506   9.763 -16.484  1.00 75.43           O  
HETATM 3227  O   HOH A2106       6.801  19.222 -16.747  1.00 81.47           O  
HETATM 3228  O   HOH A2107      50.953   6.133  28.786  1.00111.89           O  
HETATM 3229  O   HOH A2108       0.325  -2.269   5.124  1.00 63.44           O  
HETATM 3230  O   HOH A2109      18.297  11.785  27.570  1.00 76.28           O  
HETATM 3231  O   HOH A2110      25.722 -23.567  29.432  1.00109.39           O  
HETATM 3232  O   HOH A2111      39.760   0.401  36.535  1.00 72.69           O  
HETATM 3233  O   HOH A2112      12.468   7.264 -12.152  1.00 90.82           O  
HETATM 3234  O   HOH A2113      41.115  12.799  34.547  1.00 88.30           O  
HETATM 3235  O   HOH A2114      17.478 -27.491  32.936  1.00101.23           O  
HETATM 3236  O   HOH A2115       6.185  -5.781 -16.925  1.00 97.58           O  
HETATM 3237  O   HOH A2116      -8.638  -1.389  -3.037  1.00 71.84           O  
CONECT  542 1057                                                                
CONECT 1057  542                                                                
CONECT 2807 2818                                                                
CONECT 2818 2807                                                                
CONECT 3126 3127                                                                
CONECT 3127 3126 3128 3153                                                      
CONECT 3128 3127 3129 3143                                                      
CONECT 3129 3128 3130                                                           
CONECT 3130 3129 3150                                                           
CONECT 3131 3132 3150                                                           
CONECT 3132 3131 3133                                                           
CONECT 3133 3132 3134 3136                                                      
CONECT 3134 3133 3135                                                           
CONECT 3135 3134 3150                                                           
CONECT 3136 3133 3138 3151                                                      
CONECT 3137 3138 3142 3154                                                      
CONECT 3138 3136 3137 3139                                                      
CONECT 3139 3138 3140                                                           
CONECT 3140 3139 3141                                                           
CONECT 3141 3140 3142 3149                                                      
CONECT 3142 3137 3141                                                           
CONECT 3143 3128 3152 3155                                                      
CONECT 3144 3145 3152                                                           
CONECT 3145 3144 3146                                                           
CONECT 3146 3145 3147                                                           
CONECT 3147 3146 3148                                                           
CONECT 3148 3147 3152 3153                                                      
CONECT 3149 3141                                                                
CONECT 3150 3130 3131 3135                                                      
CONECT 3151 3136 3154                                                           
CONECT 3152 3143 3144 3148                                                      
CONECT 3153 3127 3148                                                           
CONECT 3154 3137 3151                                                           
CONECT 3155 3143                                                                
CONECT 3156 3157 3158                                                           
CONECT 3157 3156                                                                
CONECT 3158 3156 3159                                                           
CONECT 3159 3158 3160                                                           
CONECT 3160 3159 3161                                                           
CONECT 3161 3160 3162                                                           
CONECT 3162 3161                                                                
CONECT 3163 3164 3165                                                           
CONECT 3164 3163                                                                
CONECT 3165 3163 3166                                                           
CONECT 3166 3165 3167                                                           
CONECT 3167 3166 3168                                                           
CONECT 3168 3167 3169                                                           
CONECT 3169 3168                                                                
CONECT 3170 3171 3172                                                           
CONECT 3171 3170                                                                
CONECT 3172 3170 3173                                                           
CONECT 3173 3172 3174                                                           
CONECT 3174 3173 3175                                                           
CONECT 3175 3174 3176                                                           
CONECT 3176 3175                                                                
CONECT 3177 3178 3179 3180                                                      
CONECT 3178 3177                                                                
CONECT 3179 3177                                                                
CONECT 3180 3177 3181                                                           
CONECT 3181 3180 3182                                                           
CONECT 3182 3181 3183                                                           
CONECT 3183 3182 3184                                                           
CONECT 3184 3183 3185                                                           
CONECT 3185 3184 3186                                                           
CONECT 3186 3185 3187                                                           
CONECT 3187 3186 3188                                                           
CONECT 3188 3187 3189                                                           
CONECT 3189 3188                                                                
CONECT 3190 3191 3192 3193                                                      
CONECT 3191 3190                                                                
CONECT 3192 3190                                                                
CONECT 3193 3190 3194                                                           
CONECT 3194 3193 3195                                                           
CONECT 3195 3194 3196                                                           
CONECT 3196 3195 3197                                                           
CONECT 3197 3196 3198                                                           
CONECT 3198 3197 3199                                                           
CONECT 3199 3198 3200                                                           
CONECT 3200 3199 3201                                                           
CONECT 3201 3200                                                                
CONECT 3202 3203 3204 3205                                                      
CONECT 3203 3202                                                                
CONECT 3204 3202                                                                
CONECT 3205 3202 3206                                                           
CONECT 3206 3205 3207                                                           
CONECT 3207 3206 3208                                                           
CONECT 3208 3207 3209                                                           
CONECT 3209 3208 3210                                                           
CONECT 3210 3209 3211                                                           
CONECT 3211 3210 3212                                                           
CONECT 3212 3211 3213                                                           
CONECT 3213 3212 3214                                                           
CONECT 3214 3213 3215                                                           
CONECT 3215 3214 3216                                                           
CONECT 3216 3215 3217                                                           
CONECT 3217 3216 3218                                                           
CONECT 3218 3217 3219                                                           
CONECT 3219 3218 3220                                                           
CONECT 3220 3219 3221                                                           
CONECT 3221 3220                                                                
MASTER      364    0    7   22    3    0    0    6 3236    1  100   34          
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.