CNRS Nantes University UFIP UFIP
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***  MEMBRANE PROTEIN 08-JAN-19 6NLE  ***

elNémo ID: 211108153723141854

Job options:

ID        	=	 211108153723141854
JOBID     	=	 MEMBRANE PROTEIN 08-JAN-19 6NLE
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                        08-JAN-19   6NLE              
TITLE     X-RAY STRUCTURE OF LEUT WITH V269 DELETION                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NA(+):NEUROTRANSMITTER SYMPORTER (SNF FAMILY);             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 4-508;                                            
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS (STRAIN VF5);                  
SOURCE   3 ORGANISM_TAXID: 224324;                                              
SOURCE   4 STRAIN: VF5;                                                         
SOURCE   5 GENE: SNF, AQ_2077;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    LEUT, MEMBRANE PROTEIN                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.NAVRATNA,D.YANG,E.GOUAUX                                            
REVDAT   3   29-JUL-20 6NLE    1       COMPND REMARK HETNAM SITE                
REVDAT   2   11-MAR-20 6NLE    1       JRNL                                     
REVDAT   1   15-JAN-20 6NLE    0                                                
JRNL        AUTH   N.G.CAMPBELL,A.SHEKAR,J.I.AGUILAR,D.PENG,V.NAVRATNA,D.YANG,  
JRNL        AUTH 2 A.N.MORLEY,A.M.DURAN,G.GALLI,B.O'GRADY,R.RAMACHANDRAN,       
JRNL        AUTH 3 J.S.SUTCLIFFE,H.H.SITTE,K.ERREGER,J.MEILER,T.STOCKNER,       
JRNL        AUTH 4 L.M.BELLAN,H.J.G.MATTHIES,E.GOUAUX,H.S.MCHAOURAB,A.GALLI     
JRNL        TITL   STRUCTURAL, FUNCTIONAL, AND BEHAVIORAL INSIGHTS OF DOPAMINE  
JRNL        TITL 2 DYSFUNCTION REVEALED BY A DELETION INSLC6A3.                 
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 116  3853 2019              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   30755521                                                     
JRNL        DOI    10.1073/PNAS.1816247116                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.62 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX DEV_2597                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.62                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 76.26                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.430                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 51787                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.226                           
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2588                            
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 76.2886 -  6.8520    0.97     2951   158  0.1829 0.1974        
REMARK   3     2  6.8520 -  5.4391    0.98     2937   154  0.2079 0.2720        
REMARK   3     3  5.4391 -  4.7517    0.98     2983   158  0.1704 0.1675        
REMARK   3     4  4.7517 -  4.3173    0.96     2903   154  0.1634 0.2522        
REMARK   3     5  4.3173 -  4.0079    0.98     3041   154  0.1848 0.2290        
REMARK   3     6  4.0079 -  3.7716    0.96     2872   151  0.2023 0.2206        
REMARK   3     7  3.7716 -  3.5827    0.83     2513   131  0.2918 0.3079        
REMARK   3     8  3.5827 -  3.4267    0.88     2701   145  0.2371 0.2827        
REMARK   3     9  3.4267 -  3.2948    0.92     2744   142  0.2303 0.2778        
REMARK   3    10  3.2948 -  3.1811    0.92     2787   145  0.2608 0.3155        
REMARK   3    11  3.1811 -  3.0816    0.90     2722   150  0.3115 0.3347        
REMARK   3    12  3.0816 -  2.9936    0.90     2755   148  0.3033 0.3849        
REMARK   3    13  2.9936 -  2.9147    0.88     2669   139  0.3042 0.3155        
REMARK   3    14  2.9147 -  2.8436    0.85     2607   146  0.3139 0.3434        
REMARK   3    15  2.8436 -  2.7790    0.83     2502   129  0.3036 0.2852        
REMARK   3    16  2.7790 -  2.7198    0.84     2544   134  0.3020 0.3260        
REMARK   3    17  2.7198 -  2.6654    0.83     2563   135  0.3035 0.3533        
REMARK   3    18  2.6654 -  2.6151    0.81     2405   115  0.2989 0.3273        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.370            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.770           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 49.66                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.20                          
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      :  0.002           4029                                  
REMARK   3   ANGLE     :  0.457           5475                                  
REMARK   3   CHIRALITY :  0.036            624                                  
REMARK   3   PLANARITY :  0.005            655                                  
REMARK   3   DIHEDRAL  :  8.290           2245                                  
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 4 THROUGH 190 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -18.9448 -13.7481  16.1893              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3690 T22:   0.3206                                     
REMARK   3      T33:   0.2897 T12:  -0.0496                                     
REMARK   3      T13:  -0.0457 T23:   0.0291                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1614 L22:   1.3053                                     
REMARK   3      L33:   2.1138 L12:  -0.7114                                     
REMARK   3      L13:  -0.1071 L23:   0.1514                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0208 S12:   0.0127 S13:  -0.0765                       
REMARK   3      S21:  -0.0885 S22:   0.0991 S23:   0.0969                       
REMARK   3      S31:   0.0412 S32:  -0.1864 S33:  -0.0841                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 191 THROUGH 437 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -22.5419 -14.6663  11.8135              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3870 T22:   0.4044                                     
REMARK   3      T33:   0.3479 T12:  -0.0111                                     
REMARK   3      T13:  -0.0572 T23:   0.0441                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9812 L22:   1.3638                                     
REMARK   3      L33:   1.5220 L12:  -0.2052                                     
REMARK   3      L13:  -0.2755 L23:   0.1728                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0526 S12:   0.0946 S13:  -0.0420                       
REMARK   3      S21:  -0.0553 S22:   0.0755 S23:   0.1511                       
REMARK   3      S31:  -0.0705 S32:  -0.2121 S33:  -0.0184                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 438 THROUGH 508 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -31.7514  -8.1419  25.6643              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3641 T22:   0.4209                                     
REMARK   3      T33:   0.3454 T12:   0.0388                                     
REMARK   3      T13:   0.0820 T23:   0.0060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4166 L22:   1.9082                                     
REMARK   3      L33:   4.2857 L12:  -0.9366                                     
REMARK   3      L13:   2.4843 L23:  -1.1033                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0878 S12:  -0.2068 S13:  -0.1173                       
REMARK   3      S21:   0.1804 S22:   0.0884 S23:   0.3331                       
REMARK   3      S31:  -0.0393 S32:  -0.4358 S33:  -0.1717                       
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 6NLE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000238800.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-APR-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000010                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51787                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 76.256                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 3.011                              
REMARK 200  R MERGE                    (I) : 0.10500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.62                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.68                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.54                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.890                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.7.17                                         
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 3000, 100 MM SODIUM CACODYLATE   
REMARK 280  TRIHYDRATE, PH 6.5, AND 200 MM MAGNESIUM CHLORIDE HEXAHYDRATE,      
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       74.77000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.07000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       74.77000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       43.07000            
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 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     PRO A   132                                                      
REMARK 465     ASN A   133                                                      
REMARK 465     ALA A   134                                                      
REMARK 465     GLU A   470                                                      
REMARK 465     TYR A   471                                                      
REMARK 465     ILE A   472                                                      
REMARK 465     PRO A   473                                                      
REMARK 465     LYS A   474                                                      
REMARK 465     ILE A   475                                                      
REMARK 465     MET A   476                                                      
REMARK 465     GLU A   477                                                      
REMARK 465     GLU A   478                                                      
REMARK 465     THR A   479                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A   4    CG   CD   CE   NZ                                   
REMARK 470     ARG A  86    CZ   NH1  NH2                                       
REMARK 470     ARG A  88    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE A  89    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     GLU A 129    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 136    CG   OD1  OD2                                       
REMARK 470     ILE A 140    CG1  CG2  CD1                                       
REMARK 470     LYS A 156    CG   CD   CE   NZ                                   
REMARK 470     GLU A 159    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 163    CD   CE   NZ                                        
REMARK 470     LYS A 189    CE   NZ                                             
REMARK 470     GLU A 217    CD   OE1  OE2                                       
REMARK 470     GLU A 236    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 239    CD   CE   NZ                                        
REMARK 470     LYS A 271    CG   CD   CE   NZ                                   
REMARK 470     LYS A 398    CD   CE   NZ                                        
REMARK 470     LYS A 431    CE   NZ                                             
REMARK 470     GLU A 434    OE1  OE2                                            
REMARK 470     ARG A 469    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 507    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 508    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG1  THR A   218     O    ALA A   304              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A  54      -51.57   -126.43                                   
REMARK 500    ARG A  86       66.45    -69.81                                   
REMARK 500    LEU A 126       65.98   -104.94                                   
REMARK 500    ILE A 325      -56.51   -123.60                                   
REMARK 500    TYR A 454      -50.20   -128.76                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 778        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH A 779        DISTANCE =  6.47 ANGSTROMS                       
REMARK 525    HOH A 780        DISTANCE =  6.49 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 602  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A  20   O                                                      
REMARK 620 2 VAL A  23   O    80.4                                              
REMARK 620 3 ALA A 351   O   161.7  84.6                                        
REMARK 620 4 THR A 354   OG1 107.9 119.0  88.5                                  
REMARK 620 5 SER A 355   OG   79.4  82.1  88.3 158.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 603  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A  22   O                                                      
REMARK 620 2 ASN A  27   OD1  94.4                                              
REMARK 620 3 THR A 254   O    74.5 164.8                                        
REMARK 620 4 THR A 254   OG1 135.5 111.6  72.0                                  
REMARK 620 5 ASN A 286   OD1  75.0  93.6  73.7  68.2                            
REMARK 620 6 LEU A 601   O    84.1  82.0 106.6 133.2 158.3                      
REMARK 620 N                    1     2     3     4     5                       
DBREF  6NLE A    4   501  UNP    O67854   O67854_AQUAE     4    508             
SEQADV 6NLE     A       UNP  O67854    VAL   269 DELETION                       
SEQRES   1 A  504  LYS ARG GLU HIS TRP ALA THR ARG LEU GLY LEU ILE LEU          
SEQRES   2 A  504  ALA MET ALA GLY ASN ALA VAL GLY LEU GLY ASN PHE LEU          
SEQRES   3 A  504  ARG PHE PRO VAL GLN ALA ALA GLU ASN GLY GLY GLY ALA          
SEQRES   4 A  504  PHE MET ILE PRO TYR ILE ILE ALA PHE LEU LEU VAL GLY          
SEQRES   5 A  504  ILE PRO LEU MET TRP ILE GLU TRP ALA MET GLY ARG TYR          
SEQRES   6 A  504  GLY GLY ALA GLN GLY HIS GLY THR THR PRO ALA ILE PHE          
SEQRES   7 A  504  TYR LEU LEU TRP ARG ASN ARG PHE ALA LYS ILE LEU GLY          
SEQRES   8 A  504  VAL PHE GLY LEU TRP ILE PRO LEU VAL VAL ALA ILE TYR          
SEQRES   9 A  504  TYR VAL TYR ILE GLU SER TRP THR LEU GLY PHE ALA ILE          
SEQRES  10 A  504  LYS PHE LEU VAL GLY LEU VAL PRO GLU PRO PRO PRO ASN          
SEQRES  11 A  504  ALA THR ASP PRO ASP SER ILE LEU ARG PRO PHE LYS GLU          
SEQRES  12 A  504  PHE LEU TYR SER TYR ILE GLY VAL PRO LYS GLY ASP GLU          
SEQRES  13 A  504  PRO ILE LEU LYS PRO SER LEU PHE ALA TYR ILE VAL PHE          
SEQRES  14 A  504  LEU ILE THR MET PHE ILE ASN VAL SER ILE LEU ILE ARG          
SEQRES  15 A  504  GLY ILE SER LYS GLY ILE GLU ARG PHE ALA LYS ILE ALA          
SEQRES  16 A  504  MET PRO THR LEU PHE ILE LEU ALA VAL PHE LEU VAL ILE          
SEQRES  17 A  504  ARG VAL PHE LEU LEU GLU THR PRO ASN GLY THR ALA ALA          
SEQRES  18 A  504  ASP GLY LEU ASN PHE LEU TRP THR PRO ASP PHE GLU LYS          
SEQRES  19 A  504  LEU LYS ASP PRO GLY VAL TRP ILE ALA ALA VAL GLY GLN          
SEQRES  20 A  504  ILE PHE PHE THR LEU SER LEU GLY PHE GLY ALA ILE ILE          
SEQRES  21 A  504  THR TYR ALA SER TYR ARG LYS ASP GLN ASP ILE VAL LEU          
SEQRES  22 A  504  SER GLY LEU THR ALA ALA THR LEU ASN GLU LYS ALA GLU          
SEQRES  23 A  504  VAL ILE LEU GLY GLY SER ILE SER ILE PRO ALA ALA VAL          
SEQRES  24 A  504  ALA PHE PHE GLY VAL ALA ASN ALA VAL ALA ILE ALA LYS          
SEQRES  25 A  504  ALA GLY ALA PHE ASN LEU GLY PHE ILE THR LEU PRO ALA          
SEQRES  26 A  504  ILE PHE SER GLN THR ALA GLY GLY THR PHE LEU GLY PHE          
SEQRES  27 A  504  LEU TRP PHE PHE LEU LEU PHE PHE ALA GLY LEU THR SER          
SEQRES  28 A  504  SER ILE ALA ILE MET GLN PRO MET ILE ALA PHE LEU GLU          
SEQRES  29 A  504  ASP GLU LEU LYS LEU SER ARG LYS HIS ALA VAL LEU TRP          
SEQRES  30 A  504  THR ALA ALA ILE VAL PHE PHE SER ALA HIS LEU VAL MET          
SEQRES  31 A  504  PHE LEU ASN LYS SER LEU ASP GLU MET ASP PHE TRP ALA          
SEQRES  32 A  504  GLY THR ILE GLY VAL VAL PHE PHE GLY LEU THR GLU LEU          
SEQRES  33 A  504  ILE ILE PHE PHE TRP ILE PHE GLY ALA ASP LYS ALA TRP          
SEQRES  34 A  504  GLU GLU ILE ASN ARG GLY GLY ILE ILE LYS VAL PRO ARG          
SEQRES  35 A  504  ILE TYR TYR TYR VAL MET ARG TYR ILE THR PRO ALA PHE          
SEQRES  36 A  504  LEU ALA VAL LEU LEU VAL VAL TRP ALA ARG GLU TYR ILE          
SEQRES  37 A  504  PRO LYS ILE MET GLU GLU THR HIS TRP THR VAL TRP ILE          
SEQRES  38 A  504  THR ARG PHE TYR ILE ILE GLY LEU PHE LEU PHE LEU THR          
SEQRES  39 A  504  PHE LEU VAL PHE LEU ALA GLU ARG ARG ARG                      
HET    LEU  A 601       9                                                       
HET     NA  A 602       1                                                       
HET     NA  A 603       1                                                       
HET    GOL  A 604       6                                                       
HET    GOL  A 605       6                                                       
HET    PEG  A 606       7                                                       
HET    PEG  A 607       7                                                       
HET    PEG  A 608       7                                                       
HET    TRS  A 609       8                                                       
HET    TRS  A 610       8                                                       
HET    BOG  A 611      20                                                       
HET    OCT  A 612       8                                                       
HET    OCT  A 613       8                                                       
HETNAM     LEU LEUCINE                                                          
HETNAM      NA SODIUM ION                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETNAM     BOG OCTYL BETA-D-GLUCOPYRANOSIDE                                     
HETNAM     OCT N-OCTANE                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   2  LEU    C6 H13 N O2                                                  
FORMUL   3   NA    2(NA 1+)                                                     
FORMUL   5  GOL    2(C3 H8 O3)                                                  
FORMUL   7  PEG    3(C4 H10 O3)                                                 
FORMUL  10  TRS    2(C4 H12 N O3 1+)                                            
FORMUL  12  BOG    C14 H28 O6                                                   
FORMUL  13  OCT    2(C8 H18)                                                    
FORMUL  15  HOH   *80(H2 O)                                                     
HELIX    1 AA1 THR A   10  VAL A   23  1                                  14    
HELIX    2 AA2 GLY A   24  LEU A   29  1                                   6    
HELIX    3 AA3 LEU A   29  ASN A   38  1                                  10    
HELIX    4 AA4 GLY A   40  VAL A   54  1                                  15    
HELIX    5 AA5 VAL A   54  ALA A   71  1                                  18    
HELIX    6 AA6 THR A   76  TRP A   85  1                                  10    
HELIX    7 AA7 ASN A   87  VAL A   95  1                                   9    
HELIX    8 AA8 VAL A   95  GLY A  125  1                                  31    
HELIX    9 AA9 ASP A  136  GLY A  153  1                                  18    
HELIX   10 AB1 SER A  165  ILE A  184  1                                  20    
HELIX   11 AB2 GLY A  190  LEU A  215  1                                  26    
HELIX   12 AB3 ALA A  223  THR A  232  1                                  10    
HELIX   13 AB4 ASP A  234  LYS A  239  5                                   6    
HELIX   14 AB5 ASP A  240  LEU A  255  1                                  16    
HELIX   15 AB6 GLY A  260  SER A  267  1                                   8    
HELIX   16 AB7 ASP A  274  ILE A  292  1                                  19    
HELIX   17 AB8 LEU A  293  SER A  296  5                                   4    
HELIX   18 AB9 ILE A  297  GLY A  307  1                                  11    
HELIX   19 AC1 GLY A  307  GLY A  318  1                                  12    
HELIX   20 AC2 ILE A  325  GLN A  333  1                                   9    
HELIX   21 AC3 GLY A  336  GLU A  370  1                                  35    
HELIX   22 AC4 SER A  374  LEU A  396  1                                  23    
HELIX   23 AC5 LYS A  398  ALA A  407  1                                  10    
HELIX   24 AC6 THR A  409  TRP A  425  1                                  17    
HELIX   25 AC7 GLY A  428  ARG A  438  1                                  11    
HELIX   26 AC8 ARG A  446  TYR A  454  1                                   9    
HELIX   27 AC9 TYR A  454  VAL A  466  1                                  13    
HELIX   28 AD1 TRP A  481  ARG A  508  1                                  28    
SHEET    1 AA1 2 GLU A 217  THR A 218  0                                        
SHEET    2 AA1 2 GLY A 221  THR A 222 -1  O  GLY A 221   N  THR A 218           
LINK         O   GLY A  20                NA    NA A 602     1555   1555  2.30  
LINK         O   ALA A  22                NA    NA A 603     1555   1555  2.39  
LINK         O   VAL A  23                NA    NA A 602     1555   1555  2.47  
LINK         OD1 ASN A  27                NA    NA A 603     1555   1555  2.37  
LINK         O   THR A 254                NA    NA A 603     1555   1555  2.52  
LINK         OG1 THR A 254                NA    NA A 603     1555   1555  2.42  
LINK         OD1 ASN A 286                NA    NA A 603     1555   1555  2.77  
LINK         O   ALA A 351                NA    NA A 602     1555   1555  2.32  
LINK         OG1 THR A 354                NA    NA A 602     1555   1555  2.38  
LINK         OG  SER A 355                NA    NA A 602     1555   1555  2.49  
LINK         O   LEU A 601                NA    NA A 603     1555   1555  2.89  
CRYST1  149.540   86.140   81.530  90.00 110.72  90.00 C 1 2 1       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      0.006687  0.000000  0.002530        0.00000                         
SCALE2      0.000000  0.011609  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013114        0.00000                         
ATOM      1  N   LYS A   4     -13.006  14.307  21.343  1.00 72.04           N  
ANISOU    1  N   LYS A   4    10832   5884  10655   -481    -98   -851       N  
ATOM      2  CA  LYS A   4     -14.133  14.114  20.438  1.00 70.16           C  
ANISOU    2  CA  LYS A   4    10656   5692  10310   -320    -54   -618       C  
ATOM      3  C   LYS A   4     -14.329  12.636  20.123  1.00 68.74           C  
ANISOU    3  C   LYS A   4    10341   5843   9935   -299    -68   -513       C  
ATOM      4  O   LYS A   4     -13.359  11.901  19.930  1.00 69.14           O  
ANISOU    4  O   LYS A   4    10286   6010   9976   -457    -60   -513       O  
ATOM      5  CB  LYS A   4     -13.925  14.906  19.145  1.00 69.64           C  
ANISOU    5  CB  LYS A   4    10711   5377  10371   -394     50   -410       C  
ATOM      6  N   ARG A   5     -15.587  12.205  20.077  1.00 66.83           N  
ANISOU    6  N   ARG A   5    10098   5749   9544   -102    -89   -430       N  
ATOM      7  CA  ARG A   5     -15.888  10.818  19.755  1.00 64.80           C  
ANISOU    7  CA  ARG A   5     9723   5784   9114    -80   -104   -331       C  
ATOM      8  C   ARG A   5     -15.475  10.498  18.324  1.00 66.14           C  
ANISOU    8  C   ARG A   5     9898   5950   9281   -183    -35   -124       C  
ATOM      9  O   ARG A   5     -15.413  11.374  17.458  1.00 70.20           O  
ANISOU    9  O   ARG A   5    10524   6258   9889   -203     31      0       O  
ATOM     10  CB  ARG A   5     -17.377  10.529  19.945  1.00 57.17           C  
ANISOU   10  CB  ARG A   5     8752   4960   8010    142   -137   -280       C  
ATOM     11  CG  ARG A   5     -17.769  10.253  21.384  1.00 51.49           C  
ANISOU   11  CG  ARG A   5     7967   4378   7217    240   -204   -467       C  
ATOM     12  CD  ARG A   5     -19.229   9.850  21.495  1.00 51.61           C  
ANISOU   12  CD  ARG A   5     7949   4566   7094    443   -221   -396       C  
ATOM     13  NE  ARG A   5     -19.414   8.402  21.488  1.00 52.20           N  
ANISOU   13  NE  ARG A   5     7890   4918   7027    420   -241   -339       N  
ATOM     14  CZ  ARG A   5     -19.993   7.723  20.502  1.00 53.32           C  
ANISOU   14  CZ  ARG A   5     7996   5173   7091    438   -227   -165       C  
ATOM     15  NH1 ARG A   5     -20.119   6.406  20.590  1.00 48.60           N  
ANISOU   15  NH1 ARG A   5     7281   4803   6382    406   -248   -135       N  
ATOM     16  NH2 ARG A   5     -20.446   8.358  19.429  1.00 56.66           N  
ANISOU   16  NH2 ARG A   5     8503   5479   7548    491   -195    -22       N  
ATOM     17  N   GLU A   6     -15.191   9.222  18.083  1.00 63.78           N  
ANISOU   17  N   GLU A   6     9482   5882   8869   -241    -47    -86       N  
ATOM     18  CA  GLU A   6     -14.730   8.792  16.774  1.00 66.97           C  
ANISOU   18  CA  GLU A   6     9879   6318   9250   -335     15     87       C  
ATOM     19  C   GLU A   6     -15.858   8.902  15.749  1.00 71.53           C  
ANISOU   19  C   GLU A   6    10528   6906   9743   -194     37    281       C  
ATOM     20  O   GLU A   6     -17.020   9.154  16.080  1.00 69.91           O  
ANISOU   20  O   GLU A   6    10356   6717   9491    -23     -2    281       O  
ATOM     21  CB  GLU A   6     -14.186   7.368  16.850  1.00 68.75           C  
ANISOU   21  CB  GLU A   6     9965   6784   9372   -411    -11     57       C  
ATOM     22  CG  GLU A   6     -12.991   7.238  17.781  1.00 71.40           C  
ANISOU   22  CG  GLU A   6    10219   7128   9782   -543    -36   -123       C  
ATOM     23  CD  GLU A   6     -12.515   5.810  17.923  1.00 74.54           C  
ANISOU   23  CD  GLU A   6    10487   7761  10072   -587    -67   -149       C  
ATOM     24  OE1 GLU A   6     -12.504   5.294  19.061  1.00 74.47           O  
ANISOU   24  OE1 GLU A   6    10408   7871  10017   -552   -135   -287       O  
ATOM     25  OE2 GLU A   6     -12.155   5.202  16.895  1.00 76.06           O  
ANISOU   25  OE2 GLU A   6    10655   8022  10224   -646    -22    -30       O  
ATOM     26  N   HIS A   7     -15.501   8.705  14.481  1.00 78.17           N  
ANISOU   26  N   HIS A   7    11388   7756  10557   -259     99    446       N  
ATOM     27  CA  HIS A   7     -16.398   9.040  13.384  1.00 76.74           C  
ANISOU   27  CA  HIS A   7    11295   7554  10310   -135    127    640       C  
ATOM     28  C   HIS A   7     -16.099   8.157  12.182  1.00 70.09           C  
ANISOU   28  C   HIS A   7    10410   6866   9354   -190    160    776       C  
ATOM     29  O   HIS A   7     -14.943   8.053  11.761  1.00 69.91           O  
ANISOU   29  O   HIS A   7    10370   6815   9379   -347    224    794       O  
ATOM     30  CB  HIS A   7     -16.243  10.521  13.014  1.00 83.06           C  
ANISOU   30  CB  HIS A   7    12248   8058  11253   -133    198    720       C  
ATOM     31  CG  HIS A   7     -17.121  10.967  11.887  1.00 91.87           C  
ANISOU   31  CG  HIS A   7    13467   9139  12300     12    228    933       C  
ATOM     32  ND1 HIS A   7     -16.618  11.396  10.677  1.00 95.33           N  
ANISOU   32  ND1 HIS A   7    13990   9477  12756    -49    323   1120       N  
ATOM     33  CD2 HIS A   7     -18.468  11.070  11.791  1.00 94.16           C  
ANISOU   33  CD2 HIS A   7    13786   9495  12498    223    176    992       C  
ATOM     34  CE1 HIS A   7     -17.617  11.736   9.883  1.00 96.53           C  
ANISOU   34  CE1 HIS A   7    14225   9634  12819    127    322   1286       C  
ATOM     35  NE2 HIS A   7     -18.750  11.546  10.534  1.00 95.92           N  
ANISOU   35  NE2 HIS A   7    14110   9658  12678    293    230   1208       N  
ATOM     36  N   TRP A   8     -17.137   7.522  11.637  1.00 61.82           N  
ANISOU   36  N   TRP A   8     9340   5991   8156    -61    115    862       N  
ATOM     37  CA  TRP A   8     -16.993   6.817  10.370  1.00 51.89           C  
ANISOU   37  CA  TRP A   8     8066   4869   6779    -86    142    996       C  
ATOM     38  C   TRP A   8     -16.773   7.831   9.254  1.00 53.03           C  
ANISOU   38  C   TRP A   8     8341   4852   6954    -79    234   1179       C  
ATOM     39  O   TRP A   8     -17.521   8.806   9.134  1.00 51.17           O  
ANISOU   39  O   TRP A   8     8209   4484   6748     49    238   1261       O  
ATOM     40  CB  TRP A   8     -18.227   5.965  10.076  1.00 46.00           C  
ANISOU   40  CB  TRP A   8     7265   4340   5875     49     61   1029       C  
ATOM     41  CG  TRP A   8     -18.493   4.885  11.082  1.00 49.18           C  
ANISOU   41  CG  TRP A   8     7541   4905   6241     39    -17    879       C  
ATOM     42  CD1 TRP A   8     -19.418   4.909  12.084  1.00 50.36           C  
ANISOU   42  CD1 TRP A   8     7650   5092   6392    141    -79    795       C  
ATOM     43  CD2 TRP A   8     -17.836   3.614  11.175  1.00 48.84           C  
ANISOU   43  CD2 TRP A   8     7398   5008   6150    -72    -32    806       C  
ATOM     44  NE1 TRP A   8     -19.372   3.738  12.801  1.00 48.88           N  
ANISOU   44  NE1 TRP A   8     7348   5062   6161     92   -126    687       N  
ATOM     45  CE2 TRP A   8     -18.409   2.926  12.264  1.00 45.54           C  
ANISOU   45  CE2 TRP A   8     6892   4699   5712    -36   -103    691       C  
ATOM     46  CE3 TRP A   8     -16.814   2.995  10.450  1.00 49.65           C  
ANISOU   46  CE3 TRP A   8     7481   5161   6225   -189     12    831       C  
ATOM     47  CZ2 TRP A   8     -17.996   1.650  12.642  1.00 40.10           C  
ANISOU   47  CZ2 TRP A   8     6106   4148   4982   -113   -132    610       C  
ATOM     48  CZ3 TRP A   8     -16.406   1.728  10.828  1.00 44.82           C  
ANISOU   48  CZ3 TRP A   8     6768   4689   5572   -257    -23    735       C  
ATOM     49  CH2 TRP A   8     -16.996   1.070  11.913  1.00 38.23           C  
ANISOU   49  CH2 TRP A   8     5859   3942   4725   -219    -95    630       C  
ATOM     50  N   ALA A   9     -15.744   7.599   8.437  1.00 54.44           N  
ANISOU   50  N   ALA A   9     8517   5046   7124   -208    313   1252       N  
ATOM     51  CA  ALA A   9     -15.356   8.583   7.431  1.00 56.00           C  
ANISOU   51  CA  ALA A   9     8836   5079   7361   -228    423   1436       C  
ATOM     52  C   ALA A   9     -16.469   8.810   6.413  1.00 61.54           C  
ANISOU   52  C   ALA A   9     9623   5837   7923    -41    408   1617       C  
ATOM     53  O   ALA A   9     -16.799   9.955   6.084  1.00 65.16           O  
ANISOU   53  O   ALA A   9    10214   6107   8437     41    455   1747       O  
ATOM     54  CB  ALA A   9     -14.069   8.139   6.735  1.00 51.85           C  
ANISOU   54  CB  ALA A   9     8265   4609   6825   -394    515   1479       C  
ATOM     55  N   THR A  10     -17.059   7.732   5.902  1.00 61.54           N  
ANISOU   55  N   THR A  10     9550   6091   7742     32    339   1625       N  
ATOM     56  CA  THR A  10     -18.083   7.824   4.872  1.00 61.78           C  
ANISOU   56  CA  THR A  10     9638   6220   7617    208    310   1783       C  
ATOM     57  C   THR A  10     -19.320   7.045   5.294  1.00 58.78           C  
ANISOU   57  C   THR A  10     9163   6034   7138    333    174   1688       C  
ATOM     58  O   THR A  10     -19.268   6.183   6.176  1.00 63.96           O  
ANISOU   58  O   THR A  10     9704   6785   7813    266    115   1520       O  
ATOM     59  CB  THR A  10     -17.580   7.293   3.521  1.00 60.18           C  
ANISOU   59  CB  THR A  10     9443   6160   7264    175    365   1908       C  
ATOM     60  OG1 THR A  10     -17.274   5.898   3.638  1.00 58.16           O  
ANISOU   60  OG1 THR A  10     9054   6115   6930     93    313   1772       O  
ATOM     61  CG2 THR A  10     -16.335   8.047   3.075  1.00 59.90           C  
ANISOU   61  CG2 THR A  10     9487   5947   7326     41    517   2018       C  
ATOM     62  N   ARG A  11     -20.443   7.365   4.647  1.00 54.23           N  
ANISOU   62  N   ARG A  11     8631   5520   6453    518    127   1806       N  
ATOM     63  CA  ARG A  11     -21.665   6.599   4.868  1.00 49.47           C  
ANISOU   63  CA  ARG A  11     7921   5130   5746    633      0   1734       C  
ATOM     64  C   ARG A  11     -21.499   5.161   4.393  1.00 47.38           C  
ANISOU   64  C   ARG A  11     7546   5104   5351    553    -48   1670       C  
ATOM     65  O   ARG A  11     -21.964   4.223   5.051  1.00 51.83           O  
ANISOU   65  O   ARG A  11     7988   5804   5901    533   -131   1534       O  
ATOM     66  CB  ARG A  11     -22.841   7.264   4.153  1.00 53.05           C  
ANISOU   66  CB  ARG A  11     8435   5618   6102    853    -42   1880       C  
ATOM     67  CG  ARG A  11     -23.111   8.698   4.574  1.00 57.77           C  
ANISOU   67  CG  ARG A  11     9155   5968   6827    963      1   1949       C  
ATOM     68  CD  ARG A  11     -24.037   9.384   3.582  1.00 61.25           C  
ANISOU   68  CD  ARG A  11     9681   6436   7154   1184    -20   2139       C  
ATOM     69  NE  ARG A  11     -24.468  10.700   4.044  1.00 63.23           N  
ANISOU   69  NE  ARG A  11    10046   6454   7525   1322      7   2193       N  
ATOM     70  CZ  ARG A  11     -25.662  10.951   4.571  1.00 63.41           C  
ANISOU   70  CZ  ARG A  11    10024   6526   7542   1506    -75   2152       C  
ATOM     71  NH1 ARG A  11     -25.970  12.179   4.964  1.00 63.39           N  
ANISOU   71  NH1 ARG A  11    10141   6291   7653   1639    -43   2198       N  
ATOM     72  NH2 ARG A  11     -26.548   9.974   4.705  1.00 64.05           N  
ANISOU   72  NH2 ARG A  11     9940   6886   7511   1557   -187   2062       N  
ATOM     73  N   LEU A  12     -20.835   4.970   3.251  1.00 48.24           N  
ANISOU   73  N   LEU A  12     7702   5264   5364    509      8   1769       N  
ATOM     74  CA  LEU A  12     -20.589   3.623   2.749  1.00 52.99           C  
ANISOU   74  CA  LEU A  12     8214   6075   5844    438    -32   1698       C  
ATOM     75  C   LEU A  12     -19.616   2.861   3.638  1.00 54.95           C  
ANISOU   75  C   LEU A  12     8383   6300   6194    262    -10   1539       C  
ATOM     76  O   LEU A  12     -19.753   1.643   3.801  1.00 53.54           O  
ANISOU   76  O   LEU A  12     8104   6276   5963    219    -80   1422       O  
ATOM     77  CB  LEU A  12     -20.063   3.688   1.316  1.00 57.89           C  
ANISOU   77  CB  LEU A  12     8911   6756   6327    449     35   1843       C  
ATOM     78  CG  LEU A  12     -19.689   2.360   0.658  1.00 61.34           C  
ANISOU   78  CG  LEU A  12     9277   7401   6629    384      6   1768       C  
ATOM     79  CD1 LEU A  12     -20.915   1.470   0.501  1.00 58.86           C  
ANISOU   79  CD1 LEU A  12     8873   7297   6195    475   -144   1689       C  
ATOM     80  CD2 LEU A  12     -19.017   2.597  -0.685  1.00 65.22           C  
ANISOU   80  CD2 LEU A  12     9856   7934   6989    397    100   1918       C  
ATOM     81  N   GLY A  13     -18.636   3.556   4.221  1.00 57.23           N  
ANISOU   81  N   GLY A  13     8714   6395   6634    160     83   1530       N  
ATOM     82  CA  GLY A  13     -17.708   2.892   5.122  1.00 55.02           C  
ANISOU   82  CA  GLY A  13     8353   6103   6449      9     95   1376       C  
ATOM     83  C   GLY A  13     -18.401   2.288   6.327  1.00 51.71           C  
ANISOU   83  C   GLY A  13     7839   5739   6068     27     -2   1228       C  
ATOM     84  O   GLY A  13     -18.036   1.202   6.786  1.00 47.79           O  
ANISOU   84  O   GLY A  13     7253   5338   5567    -54    -34   1110       O  
ATOM     85  N   LEU A  14     -19.410   2.982   6.857  1.00 54.05           N  
ANISOU   85  N   LEU A  14     8156   5981   6401    141    -45   1239       N  
ATOM     86  CA  LEU A  14     -20.207   2.413   7.938  1.00 58.21           C  
ANISOU   86  CA  LEU A  14     8585   6588   6943    175   -130   1117       C  
ATOM     87  C   LEU A  14     -21.027   1.226   7.445  1.00 60.36           C  
ANISOU   87  C   LEU A  14     8771   7081   7083    211   -217   1103       C  
ATOM     88  O   LEU A  14     -21.157   0.218   8.150  1.00 59.36           O  
ANISOU   88  O   LEU A  14     8547   7047   6961    158   -265    992       O  
ATOM     89  CB  LEU A  14     -21.112   3.490   8.541  1.00 54.34           C  
ANISOU   89  CB  LEU A  14     8136   5997   6512    307   -147   1136       C  
ATOM     90  CG  LEU A  14     -22.275   3.065   9.442  1.00 51.39           C  
ANISOU   90  CG  LEU A  14     7663   5739   6123    392   -231   1052       C  
ATOM     91  CD1 LEU A  14     -21.794   2.226  10.619  1.00 47.73           C  
ANISOU   91  CD1 LEU A  14     7110   5313   5711    283   -243    903       C  
ATOM     92  CD2 LEU A  14     -23.030   4.290   9.933  1.00 54.83           C  
ANISOU   92  CD2 LEU A  14     8155   6058   6619    538   -230   1078       C  
ATOM     93  N   ILE A  15     -21.577   1.324   6.232  1.00 58.92           N  
ANISOU   93  N   ILE A  15     8623   6983   6781    298   -238   1214       N  
ATOM     94  CA  ILE A  15     -22.371   0.228   5.680  1.00 57.24           C  
ANISOU   94  CA  ILE A  15     8325   6980   6443    326   -331   1187       C  
ATOM     95  C   ILE A  15     -21.498  -0.999   5.448  1.00 58.85           C  
ANISOU   95  C   ILE A  15     8488   7257   6615    192   -324   1105       C  
ATOM     96  O   ILE A  15     -21.911  -2.133   5.720  1.00 63.84           O  
ANISOU   96  O   ILE A  15     9026   8007   7223    155   -395   1009       O  
ATOM     97  CB  ILE A  15     -23.075   0.681   4.387  1.00 52.99           C  
ANISOU   97  CB  ILE A  15     7838   6525   5771    460   -360   1320       C  
ATOM     98  CG1 ILE A  15     -24.097   1.777   4.694  1.00 48.90           C  
ANISOU   98  CG1 ILE A  15     7345   5953   5283    618   -382   1392       C  
ATOM     99  CG2 ILE A  15     -23.747  -0.498   3.695  1.00 45.00           C  
ANISOU   99  CG2 ILE A  15     6737   5737   4625    469   -461   1272       C  
ATOM    100  CD1 ILE A  15     -24.533   2.563   3.477  1.00 42.85           C  
ANISOU  100  CD1 ILE A  15     6667   5210   4403    766   -383   1557       C  
ATOM    101  N   LEU A  16     -20.277  -0.793   4.948  1.00 56.33           N  
ANISOU  101  N   LEU A  16     8237   6865   6302    120   -235   1142       N  
ATOM    102  CA  LEU A  16     -19.374  -1.918   4.723  1.00 57.12           C  
ANISOU  102  CA  LEU A  16     8300   7032   6372     10   -221   1061       C  
ATOM    103  C   LEU A  16     -18.937  -2.550   6.039  1.00 54.44           C  
ANISOU  103  C   LEU A  16     7888   6652   6146    -84   -229    928       C  
ATOM    104  O   LEU A  16     -18.871  -3.779   6.151  1.00 54.23           O  
ANISOU  104  O   LEU A  16     7797   6716   6092   -135   -273    837       O  
ATOM    105  CB  LEU A  16     -18.159  -1.468   3.914  1.00 57.69           C  
ANISOU  105  CB  LEU A  16     8449   7046   6426    -39   -110   1140       C  
ATOM    106  CG  LEU A  16     -18.143  -1.872   2.439  1.00 60.41           C  
ANISOU  106  CG  LEU A  16     8827   7529   6597      5   -110   1204       C  
ATOM    107  CD1 LEU A  16     -16.742  -1.736   1.862  1.00 66.43           C  
ANISOU  107  CD1 LEU A  16     9631   8256   7353    -73     13   1249       C  
ATOM    108  CD2 LEU A  16     -18.666  -3.290   2.262  1.00 58.07           C  
ANISOU  108  CD2 LEU A  16     8452   7397   6213      2   -215   1086       C  
ATOM    109  N   ALA A  17     -18.632  -1.726   7.046  1.00 51.39           N  
ANISOU  109  N   ALA A  17     7515   6127   5885   -103   -188    914       N  
ATOM    110  CA  ALA A  17     -18.280  -2.266   8.355  1.00 50.32           C  
ANISOU  110  CA  ALA A  17     7311   5969   5838   -171   -202    792       C  
ATOM    111  C   ALA A  17     -19.476  -2.926   9.026  1.00 52.05           C  
ANISOU  111  C   ALA A  17     7453   6283   6041   -123   -289    740       C  
ATOM    112  O   ALA A  17     -19.305  -3.877   9.798  1.00 49.59           O  
ANISOU  112  O   ALA A  17     7076   6012   5755   -178   -314    650       O  
ATOM    113  CB  ALA A  17     -17.711  -1.164   9.247  1.00 44.68           C  
ANISOU  113  CB  ALA A  17     6631   5094   5251   -194   -147    776       C  
ATOM    114  N   MET A  18     -20.687  -2.437   8.753  1.00 49.71           N  
ANISOU  114  N   MET A  18     7160   6026   5704    -16   -333    801       N  
ATOM    115  CA  MET A  18     -21.880  -3.094   9.275  1.00 46.04           C  
ANISOU  115  CA  MET A  18     6601   5673   5219     23   -411    760       C  
ATOM    116  C   MET A  18     -22.084  -4.453   8.621  1.00 46.08           C  
ANISOU  116  C   MET A  18     6550   5811   5147    -29   -467    724       C  
ATOM    117  O   MET A  18     -22.521  -5.406   9.278  1.00 47.55           O  
ANISOU  117  O   MET A  18     6654   6061   5353    -69   -510    658       O  
ATOM    118  CB  MET A  18     -23.103  -2.205   9.062  1.00 49.97           C  
ANISOU  118  CB  MET A  18     7101   6195   5688    160   -444    835       C  
ATOM    119  CG  MET A  18     -23.372  -1.253  10.207  1.00 58.80           C  
ANISOU  119  CG  MET A  18     8229   7217   6896    224   -419    820       C  
ATOM    120  SD  MET A  18     -24.060  -2.079  11.653  1.00 61.36           S  
ANISOU  120  SD  MET A  18     8426   7634   7256    209   -456    720       S  
ATOM    121  CE  MET A  18     -24.613  -0.658  12.589  1.00 62.96           C  
ANISOU  121  CE  MET A  18     8658   7743   7520    344   -431    723       C  
ATOM    122  N   ALA A  19     -21.781  -4.561   7.325  1.00 45.77           N  
ANISOU  122  N   ALA A  19     6560   5812   5019    -27   -466    767       N  
ATOM    123  CA  ALA A  19     -21.824  -5.861   6.665  1.00 45.53           C  
ANISOU  123  CA  ALA A  19     6490   5893   4916    -80   -520    709       C  
ATOM    124  C   ALA A  19     -20.781  -6.803   7.252  1.00 46.68           C  
ANISOU  124  C   ALA A  19     6622   5994   5120   -187   -488    620       C  
ATOM    125  O   ALA A  19     -21.045  -7.996   7.441  1.00 45.12           O  
ANISOU  125  O   ALA A  19     6367   5852   4923   -239   -538    545       O  
ATOM    126  CB  ALA A  19     -21.619  -5.694   5.160  1.00 44.36           C  
ANISOU  126  CB  ALA A  19     6407   5804   4643    -39   -518    769       C  
ATOM    127  N   GLY A  20     -19.587  -6.282   7.551  1.00 51.32           N  
ANISOU  127  N   GLY A  20     7260   6479   5762   -222   -404    626       N  
ATOM    128  CA  GLY A  20     -18.594  -7.082   8.247  1.00 52.64           C  
ANISOU  128  CA  GLY A  20     7402   6610   5987   -305   -378    543       C  
ATOM    129  C   GLY A  20     -19.047  -7.496   9.632  1.00 50.96           C  
ANISOU  129  C   GLY A  20     7125   6387   5850   -320   -408    489       C  
ATOM    130  O   GLY A  20     -18.720  -8.591  10.095  1.00 47.99           O  
ANISOU  130  O   GLY A  20     6714   6025   5494   -372   -422    424       O  
ATOM    131  N   ASN A  21     -19.800  -6.630  10.311  1.00 50.41           N  
ANISOU  131  N   ASN A  21     7042   6294   5816   -264   -414    521       N  
ATOM    132  CA  ASN A  21     -20.412  -7.007  11.581  1.00 47.22           C  
ANISOU  132  CA  ASN A  21     6571   5910   5461   -261   -439    482       C  
ATOM    133  C   ASN A  21     -21.337  -8.205  11.401  1.00 51.72           C  
ANISOU  133  C   ASN A  21     7073   6580   5999   -284   -503    465       C  
ATOM    134  O   ASN A  21     -21.280  -9.172  12.169  1.00 49.23           O  
ANISOU  134  O   ASN A  21     6715   6274   5717   -334   -511    421       O  
ATOM    135  CB  ASN A  21     -21.175  -5.810  12.157  1.00 46.40           C  
ANISOU  135  CB  ASN A  21     6467   5780   5384   -175   -434    518       C  
ATOM    136  CG  ASN A  21     -21.653  -6.035  13.583  1.00 49.57           C  
ANISOU  136  CG  ASN A  21     6802   6205   5827   -160   -440    478       C  
ATOM    137  OD1 ASN A  21     -21.810  -7.168  14.036  1.00 50.99           O  
ANISOU  137  OD1 ASN A  21     6925   6443   6007   -209   -460    448       O  
ATOM    138  ND2 ASN A  21     -21.894  -4.942  14.296  1.00 56.40           N  
ANISOU  138  ND2 ASN A  21     7682   7021   6725    -88   -419    479       N  
ATOM    139  N   ALA A  22     -22.187  -8.164  10.374  1.00 52.96           N  
ANISOU  139  N   ALA A  22     7220   6811   6091   -250   -552    500       N  
ATOM    140  CA  ALA A  22     -23.176  -9.218  10.179  1.00 51.88           C  
ANISOU  140  CA  ALA A  22     7005   6771   5936   -283   -623    474       C  
ATOM    141  C   ALA A  22     -22.554 -10.469   9.567  1.00 48.37           C  
ANISOU  141  C   ALA A  22     6580   6327   5471   -365   -642    411       C  
ATOM    142  O   ALA A  22     -22.715 -11.572  10.100  1.00 50.09           O  
ANISOU  142  O   ALA A  22     6753   6545   5734   -432   -661    365       O  
ATOM    143  CB  ALA A  22     -24.321  -8.702   9.307  1.00 56.82           C  
ANISOU  143  CB  ALA A  22     7600   7494   6494   -209   -682    521       C  
ATOM    144  N   VAL A  23     -21.846 -10.321   8.449  1.00 46.66           N  
ANISOU  144  N   VAL A  23     6434   6108   5187   -355   -631    410       N  
ATOM    145  CA  VAL A  23     -21.271 -11.469   7.752  1.00 47.94           C  
ANISOU  145  CA  VAL A  23     6620   6279   5315   -412   -650    339       C  
ATOM    146  C   VAL A  23     -20.135 -12.031   8.602  1.00 52.73           C  
ANISOU  146  C   VAL A  23     7245   6797   5993   -461   -594    297       C  
ATOM    147  O   VAL A  23     -19.115 -11.368   8.810  1.00 59.05           O  
ANISOU  147  O   VAL A  23     8085   7542   6807   -447   -526    316       O  
ATOM    148  CB  VAL A  23     -20.781 -11.092   6.350  1.00 46.84           C  
ANISOU  148  CB  VAL A  23     6550   6180   5067   -371   -640    355       C  
ATOM    149  CG1 VAL A  23     -20.054 -12.267   5.712  1.00 44.82           C  
ANISOU  149  CG1 VAL A  23     6324   5930   4774   -416   -649    266       C  
ATOM    150  CG2 VAL A  23     -21.948 -10.645   5.482  1.00 47.05           C  
ANISOU  150  CG2 VAL A  23     6557   6315   5006   -307   -710    396       C  
ATOM    151  N   GLY A  24     -20.303 -13.247   9.085  1.00 48.51           N  
ANISOU  151  N   GLY A  24     6678   6247   5506   -519   -624    241       N  
ATOM    152  CA  GLY A  24     -19.301 -13.882   9.917  1.00 47.38           C  
ANISOU  152  CA  GLY A  24     6551   6028   5423   -549   -581    208       C  
ATOM    153  C   GLY A  24     -19.417 -15.386   9.870  1.00 48.47           C  
ANISOU  153  C   GLY A  24     6686   6142   5589   -605   -621    143       C  
ATOM    154  O   GLY A  24     -19.892 -15.959   8.887  1.00 54.87           O  
ANISOU  154  O   GLY A  24     7502   6988   6359   -628   -677     96       O  
ATOM    155  N   LEU A  25     -18.979 -16.032  10.953  1.00 40.98           N  
ANISOU  155  N   LEU A  25     5732   5128   4709   -625   -594    138       N  
ATOM    156  CA  LEU A  25     -19.021 -17.488  11.025  1.00 39.41           C  
ANISOU  156  CA  LEU A  25     5545   4873   4556   -677   -622     88       C  
ATOM    157  C   LEU A  25     -20.444 -18.030  11.028  1.00 44.06           C  
ANISOU  157  C   LEU A  25     6077   5484   5182   -741   -680     94       C  
ATOM    158  O   LEU A  25     -20.647 -19.202  10.698  1.00 46.32           O  
ANISOU  158  O   LEU A  25     6377   5720   5503   -801   -719     37       O  
ATOM    159  CB  LEU A  25     -18.274 -17.971  12.269  1.00 37.35           C  
ANISOU  159  CB  LEU A  25     5293   4543   4354   -666   -576    106       C  
ATOM    160  CG  LEU A  25     -16.836 -17.465  12.408  1.00 38.38           C  
ANISOU  160  CG  LEU A  25     5456   4666   4462   -608   -524     92       C  
ATOM    161  CD1 LEU A  25     -16.218 -17.926  13.719  1.00 39.11           C  
ANISOU  161  CD1 LEU A  25     5544   4714   4601   -584   -494    111       C  
ATOM    162  CD2 LEU A  25     -15.997 -17.924  11.227  1.00 27.22           C  
ANISOU  162  CD2 LEU A  25     4094   3245   3005   -596   -524     20       C  
ATOM    163  N   GLY A  26     -21.432 -17.208  11.388  1.00 46.73           N  
ANISOU  163  N   GLY A  26     6345   5893   5518   -732   -687    155       N  
ATOM    164  CA  GLY A  26     -22.809 -17.666  11.361  1.00 45.40           C  
ANISOU  164  CA  GLY A  26     6096   5767   5385   -797   -741    161       C  
ATOM    165  C   GLY A  26     -23.332 -17.910   9.961  1.00 48.71           C  
ANISOU  165  C   GLY A  26     6511   6243   5753   -823   -823     90       C  
ATOM    166  O   GLY A  26     -24.258 -18.705   9.771  1.00 51.11           O  
ANISOU  166  O   GLY A  26     6757   6560   6102   -905   -882     54       O  
ATOM    167  N   ASN A  27     -22.754 -17.239   8.962  1.00 48.19           N  
ANISOU  167  N   ASN A  27     6503   6218   5591   -756   -827     68       N  
ATOM    168  CA  ASN A  27     -23.193 -17.435   7.586  1.00 56.45           C  
ANISOU  168  CA  ASN A  27     7552   7338   6558   -761   -908     -2       C  
ATOM    169  C   ASN A  27     -22.605 -18.696   6.968  1.00 59.40           C  
ANISOU  169  C   ASN A  27     7989   7643   6935   -808   -936   -115       C  
ATOM    170  O   ASN A  27     -23.253 -19.326   6.125  1.00 63.70           O  
ANISOU  170  O   ASN A  27     8516   8229   7458   -853  -1023   -202       O  
ATOM    171  CB  ASN A  27     -22.819 -16.222   6.730  1.00 59.26           C  
ANISOU  171  CB  ASN A  27     7952   7770   6796   -661   -892     36       C  
ATOM    172  CG  ASN A  27     -23.121 -14.907   7.418  1.00 61.53           C  
ANISOU  172  CG  ASN A  27     8206   8082   7091   -598   -847    145       C  
ATOM    173  OD1 ASN A  27     -22.787 -14.716   8.587  1.00 65.88           O  
ANISOU  173  OD1 ASN A  27     8749   8566   7715   -602   -785    186       O  
ATOM    174  ND2 ASN A  27     -23.752 -13.990   6.693  1.00 56.41           N  
ANISOU  174  ND2 ASN A  27     7541   7531   6361   -529   -880    187       N  
ATOM    175  N   PHE A  28     -21.390 -19.080   7.367  1.00 52.62           N  
ANISOU  175  N   PHE A  28     7203   6684   6104   -792   -870   -126       N  
ATOM    176  CA  PHE A  28     -20.700 -20.206   6.755  1.00 48.30           C  
ANISOU  176  CA  PHE A  28     6729   6068   5553   -809   -888   -237       C  
ATOM    177  C   PHE A  28     -20.597 -21.433   7.647  1.00 49.31           C  
ANISOU  177  C   PHE A  28     6871   6056   5810   -875   -877   -257       C  
ATOM    178  O   PHE A  28     -20.371 -22.531   7.128  1.00 54.18           O  
ANISOU  178  O   PHE A  28     7542   6597   6446   -904   -913   -362       O  
ATOM    179  CB  PHE A  28     -19.286 -19.792   6.322  1.00 44.21           C  
ANISOU  179  CB  PHE A  28     6287   5554   4958   -722   -820   -244       C  
ATOM    180  CG  PHE A  28     -19.249 -18.561   5.461  1.00 37.58           C  
ANISOU  180  CG  PHE A  28     5450   4835   3996   -655   -808   -201       C  
ATOM    181  CD1 PHE A  28     -19.563 -18.631   4.114  1.00 39.32           C  
ANISOU  181  CD1 PHE A  28     5693   5148   4101   -631   -868   -268       C  
ATOM    182  CD2 PHE A  28     -18.896 -17.334   5.998  1.00 34.34           C  
ANISOU  182  CD2 PHE A  28     5026   4439   3582   -612   -738    -94       C  
ATOM    183  CE1 PHE A  28     -19.529 -17.501   3.318  1.00 37.34           C  
ANISOU  183  CE1 PHE A  28     5453   5006   3727   -559   -850   -206       C  
ATOM    184  CE2 PHE A  28     -18.859 -16.200   5.208  1.00 40.28           C  
ANISOU  184  CE2 PHE A  28     5794   5279   4234   -552   -719    -39       C  
ATOM    185  CZ  PHE A  28     -19.177 -16.284   3.866  1.00 41.25           C  
ANISOU  185  CZ  PHE A  28     5942   5496   4236   -522   -771    -84       C  
ATOM    186  N   LEU A  29     -20.746 -21.282   8.962  1.00 46.52           N  
ANISOU  186  N   LEU A  29     6477   5661   5537   -891   -828   -159       N  
ATOM    187  CA  LEU A  29     -20.686 -22.408   9.886  1.00 45.32           C  
ANISOU  187  CA  LEU A  29     6342   5377   5500   -946   -808   -148       C  
ATOM    188  C   LEU A  29     -22.019 -22.690  10.561  1.00 43.01           C  
ANISOU  188  C   LEU A  29     5960   5085   5296  -1044   -829    -91       C  
ATOM    189  O   LEU A  29     -22.444 -23.848  10.627  1.00 47.45           O  
ANISOU  189  O   LEU A  29     6529   5547   5952  -1136   -856   -126       O  
ATOM    190  CB  LEU A  29     -19.609 -22.164  10.956  1.00 43.21           C  
ANISOU  190  CB  LEU A  29     6106   5067   5246   -874   -724    -76       C  
ATOM    191  CG  LEU A  29     -18.151 -22.389  10.552  1.00 45.18           C  
ANISOU  191  CG  LEU A  29     6438   5277   5453   -794   -694   -137       C  
ATOM    192  CD1 LEU A  29     -17.231 -22.168  11.743  1.00 44.99           C  
ANISOU  192  CD1 LEU A  29     6418   5227   5449   -731   -625    -67       C  
ATOM    193  CD2 LEU A  29     -17.963 -23.783   9.977  1.00 45.38           C  
ANISOU  193  CD2 LEU A  29     6534   5190   5519   -822   -730   -239       C  
ATOM    194  N   ARG A  30     -22.698 -21.658  11.065  1.00 37.74           N  
ANISOU  194  N   ARG A  30     5207   4524   4607  -1026   -811     -3       N  
ATOM    195  CA  ARG A  30     -23.930 -21.881  11.813  1.00 36.18           C  
ANISOU  195  CA  ARG A  30     4909   4348   4491  -1109   -813     63       C  
ATOM    196  C   ARG A  30     -25.112 -22.165  10.893  1.00 37.38           C  
ANISOU  196  C   ARG A  30     4984   4564   4655  -1198   -906     -6       C  
ATOM    197  O   ARG A  30     -25.905 -23.072  11.166  1.00 37.13           O  
ANISOU  197  O   ARG A  30     4897   4483   4728  -1317   -925     -9       O  
ATOM    198  CB  ARG A  30     -24.227 -20.677  12.709  1.00 34.29           C  
ANISOU  198  CB  ARG A  30     4604   4208   4218  -1041   -760    169       C  
ATOM    199  CG  ARG A  30     -25.196 -20.974  13.842  1.00 38.36           C  
ANISOU  199  CG  ARG A  30     5025   4737   4813  -1103   -723    261       C  
ATOM    200  CD  ARG A  30     -25.663 -19.697  14.525  1.00 42.56           C  
ANISOU  200  CD  ARG A  30     5483   5393   5295  -1022   -685    340       C  
ATOM    201  NE  ARG A  30     -26.278 -19.958  15.824  1.00 45.84           N  
ANISOU  201  NE  ARG A  30     5827   5824   5766  -1051   -621    439       N  
ATOM    202  CZ  ARG A  30     -27.555 -20.285  15.999  1.00 49.87           C  
ANISOU  202  CZ  ARG A  30     6216   6398   6334  -1137   -628    476       C  
ATOM    203  NH1 ARG A  30     -28.365 -20.392  14.954  1.00 50.01           N  
ANISOU  203  NH1 ARG A  30     6164   6471   6365  -1203   -711    411       N  
ATOM    204  NH2 ARG A  30     -28.024 -20.504  17.220  1.00 50.65           N  
ANISOU  204  NH2 ARG A  30     6255   6519   6473  -1154   -552    579       N  
ATOM    205  N   PHE A  31     -25.243 -21.411   9.802  1.00 42.42           N  
ANISOU  205  N   PHE A  31     5614   5316   5189  -1144   -964    -60       N  
ATOM    206  CA  PHE A  31     -26.415 -21.558   8.939  1.00 44.72           C  
ANISOU  206  CA  PHE A  31     5815   5704   5473  -1211  -1065   -127       C  
ATOM    207  C   PHE A  31     -26.503 -22.925   8.271  1.00 44.03           C  
ANISOU  207  C   PHE A  31     5760   5521   5448  -1321  -1136   -258       C  
ATOM    208  O   PHE A  31     -27.604 -23.502   8.252  1.00 45.64           O  
ANISOU  208  O   PHE A  31     5862   5742   5736  -1443  -1194   -289       O  
ATOM    209  CB  PHE A  31     -26.447 -20.435   7.897  1.00 47.06           C  
ANISOU  209  CB  PHE A  31     6111   6145   5623  -1105  -1110   -144       C  
ATOM    210  CG  PHE A  31     -27.554 -20.582   6.891  1.00 47.72           C  
ANISOU  210  CG  PHE A  31     6107   6352   5673  -1150  -1230   -227       C  
ATOM    211  CD1 PHE A  31     -27.307 -21.071   5.616  1.00 48.53           C  
ANISOU  211  CD1 PHE A  31     6269   6469   5700  -1152  -1312   -361       C  
ATOM    212  CD2 PHE A  31     -28.852 -20.249   7.232  1.00 43.64           C  
ANISOU  212  CD2 PHE A  31     5439   5950   5194  -1185  -1262   -178       C  
ATOM    213  CE1 PHE A  31     -28.339 -21.209   4.698  1.00 47.74           C  
ANISOU  213  CE1 PHE A  31     6080   6500   5558  -1190  -1436   -450       C  
ATOM    214  CE2 PHE A  31     -29.880 -20.382   6.327  1.00 46.01           C  
ANISOU  214  CE2 PHE A  31     5639   6381   5462  -1225  -1382   -260       C  
ATOM    215  CZ  PHE A  31     -29.628 -20.863   5.059  1.00 50.03           C  
ANISOU  215  CZ  PHE A  31     6209   6906   5892  -1229  -1475   -399       C  
ATOM    216  N   PRO A  32     -25.436 -23.484   7.685  1.00 41.94           N  
ANISOU  216  N   PRO A  32     5624   5159   5152  -1289  -1138   -348       N  
ATOM    217  CA  PRO A  32     -25.575 -24.832   7.102  1.00 44.33           C  
ANISOU  217  CA  PRO A  32     5964   5352   5527  -1394  -1208   -488       C  
ATOM    218  C   PRO A  32     -26.011 -25.883   8.107  1.00 51.31           C  
ANISOU  218  C   PRO A  32     6823   6082   6591  -1527  -1177   -445       C  
ATOM    219  O   PRO A  32     -26.783 -26.787   7.763  1.00 57.67           O  
ANISOU  219  O   PRO A  32     7587   6833   7490  -1663  -1250   -536       O  
ATOM    220  CB  PRO A  32     -24.171 -25.121   6.551  1.00 42.35           C  
ANISOU  220  CB  PRO A  32     5864   5021   5207  -1299  -1183   -564       C  
ATOM    221  CG  PRO A  32     -23.584 -23.775   6.321  1.00 43.94           C  
ANISOU  221  CG  PRO A  32     6075   5354   5264  -1162  -1138   -495       C  
ATOM    222  CD  PRO A  32     -24.099 -22.920   7.424  1.00 41.73           C  
ANISOU  222  CD  PRO A  32     5706   5127   5021  -1158  -1082   -342       C  
ATOM    223  N   VAL A  33     -25.536 -25.788   9.350  1.00 47.94           N  
ANISOU  223  N   VAL A  33     6419   5583   6213  -1494  -1069   -309       N  
ATOM    224  CA  VAL A  33     -25.931 -26.753  10.370  1.00 50.71           C  
ANISOU  224  CA  VAL A  33     6753   5792   6724  -1609  -1023   -238       C  
ATOM    225  C   VAL A  33     -27.400 -26.574  10.733  1.00 54.42           C  
ANISOU  225  C   VAL A  33     7053   6364   7260  -1724  -1040   -178       C  
ATOM    226  O   VAL A  33     -28.155 -27.549  10.826  1.00 62.47           O  
ANISOU  226  O   VAL A  33     8024   7295   8417  -1881  -1065   -201       O  
ATOM    227  CB  VAL A  33     -25.022 -26.630  11.606  1.00 51.53           C  
ANISOU  227  CB  VAL A  33     6922   5824   6833  -1520   -906   -102       C  
ATOM    228  CG1 VAL A  33     -25.610 -27.400  12.779  1.00 56.10           C  
ANISOU  228  CG1 VAL A  33     7463   6300   7553  -1625   -843     16       C  
ATOM    229  CG2 VAL A  33     -23.624 -27.134  11.286  1.00 49.53           C  
ANISOU  229  CG2 VAL A  33     6823   5446   6551  -1430   -893   -172       C  
ATOM    230  N   GLN A  34     -27.831 -25.324  10.932  1.00 48.85           N  
ANISOU  230  N   GLN A  34     6252   5845   6465  -1647  -1026   -102       N  
ATOM    231  CA  GLN A  34     -29.222 -25.069  11.294  1.00 47.02           C  
ANISOU  231  CA  GLN A  34     5843   5737   6285  -1733  -1037    -42       C  
ATOM    232  C   GLN A  34     -30.174 -25.503  10.186  1.00 51.95           C  
ANISOU  232  C   GLN A  34     6377   6421   6939  -1849  -1165   -179       C  
ATOM    233  O   GLN A  34     -31.220 -26.105  10.457  1.00 55.07           O  
ANISOU  233  O   GLN A  34     6648   6817   7459  -2002  -1181   -171       O  
ATOM    234  CB  GLN A  34     -29.422 -23.586  11.616  1.00 43.81           C  
ANISOU  234  CB  GLN A  34     5368   5514   5765  -1598  -1004     48       C  
ATOM    235  CG  GLN A  34     -28.601 -23.081  12.791  1.00 47.72           C  
ANISOU  235  CG  GLN A  34     5929   5970   6230  -1491   -887    172       C  
ATOM    236  CD  GLN A  34     -28.881 -23.841  14.072  1.00 47.97           C  
ANISOU  236  CD  GLN A  34     5931   5917   6377  -1574   -798    284       C  
ATOM    237  OE1 GLN A  34     -30.024 -23.929  14.520  1.00 49.36           O  
ANISOU  237  OE1 GLN A  34     5966   6171   6619  -1659   -783    344       O  
ATOM    238  NE2 GLN A  34     -27.834 -24.397  14.670  1.00 44.37           N  
ANISOU  238  NE2 GLN A  34     5603   5312   5941  -1542   -735    319       N  
ATOM    239  N   ALA A  35     -29.830 -25.208   8.931  1.00 52.18           N  
ANISOU  239  N   ALA A  35     6461   6512   6852  -1779  -1257   -309       N  
ATOM    240  CA  ALA A  35     -30.703 -25.579   7.822  1.00 52.61           C  
ANISOU  240  CA  ALA A  35     6431   6648   6909  -1872  -1395   -457       C  
ATOM    241  C   ALA A  35     -30.749 -27.090   7.633  1.00 54.14           C  
ANISOU  241  C   ALA A  35     6669   6648   7252  -2040  -1436   -573       C  
ATOM    242  O   ALA A  35     -31.829 -27.664   7.454  1.00 54.86           O  
ANISOU  242  O   ALA A  35     6632   6762   7451  -2201  -1509   -637       O  
ATOM    243  CB  ALA A  35     -30.244 -24.890   6.538  1.00 50.17           C  
ANISOU  243  CB  ALA A  35     6187   6459   6416  -1735  -1475   -557       C  
ATOM    244  N   ALA A  36     -29.590 -27.751   7.674  1.00 54.55           N  
ANISOU  244  N   ALA A  36     6898   6505   7321  -2006  -1392   -607       N  
ATOM    245  CA  ALA A  36     -29.560 -29.198   7.486  1.00 53.32           C  
ANISOU  245  CA  ALA A  36     6811   6136   7315  -2150  -1429   -722       C  
ATOM    246  C   ALA A  36     -30.230 -29.932   8.639  1.00 53.18           C  
ANISOU  246  C   ALA A  36     6721   5989   7498  -2315  -1355   -604       C  
ATOM    247  O   ALA A  36     -30.814 -31.002   8.432  1.00 52.38           O  
ANISOU  247  O   ALA A  36     6594   5759   7550  -2494  -1409   -696       O  
ATOM    248  CB  ALA A  36     -28.120 -29.679   7.319  1.00 49.79           C  
ANISOU  248  CB  ALA A  36     6570   5515   6832  -2045  -1388   -772       C  
ATOM    249  N   GLU A  37     -30.153 -29.382   9.854  1.00 56.97           N  
ANISOU  249  N   GLU A  37     7169   6500   7979  -2259  -1231   -402       N  
ATOM    250  CA  GLU A  37     -30.820 -30.008  10.991  1.00 65.66           C  
ANISOU  250  CA  GLU A  37     8194   7506   9249  -2403  -1145   -265       C  
ATOM    251  C   GLU A  37     -32.331 -30.028  10.803  1.00 72.10           C  
ANISOU  251  C   GLU A  37     8793   8454  10148  -2570  -1208   -290       C  
ATOM    252  O   GLU A  37     -32.986 -31.038  11.085  1.00 81.28           O  
ANISOU  252  O   GLU A  37     9901   9487  11495  -2769  -1201   -287       O  
ATOM    253  CB  GLU A  37     -30.464 -29.273  12.284  1.00 73.67           C  
ANISOU  253  CB  GLU A  37     9208   8575  10208  -2283  -1006    -55       C  
ATOM    254  CG  GLU A  37     -29.150 -29.691  12.921  1.00 80.01           C  
ANISOU  254  CG  GLU A  37    10198   9194  11007  -2183   -918     12       C  
ATOM    255  CD  GLU A  37     -28.836 -28.883  14.166  1.00 83.33           C  
ANISOU  255  CD  GLU A  37    10606   9701  11354  -2058   -798    198       C  
ATOM    256  OE1 GLU A  37     -29.709 -28.102  14.600  1.00 84.26           O  
ANISOU  256  OE1 GLU A  37    10573  10000  11443  -2063   -773    280       O  
ATOM    257  OE2 GLU A  37     -27.719 -29.024  14.707  1.00 84.08           O  
ANISOU  257  OE2 GLU A  37    10837   9694  11417  -1947   -734    253       O  
ATOM    258  N   ASN A  38     -32.900 -28.923  10.319  1.00 69.55           N  
ANISOU  258  N   ASN A  38     8341   8389   9697  -2493  -1270   -312       N  
ATOM    259  CA  ASN A  38     -34.345 -28.744  10.249  1.00 66.90           C  
ANISOU  259  CA  ASN A  38     7771   8229   9419  -2616  -1323   -314       C  
ATOM    260  C   ASN A  38     -34.898 -28.949   8.841  1.00 67.93           C  
ANISOU  260  C   ASN A  38     7836   8448   9527  -2686  -1501   -533       C  
ATOM    261  O   ASN A  38     -35.898 -28.324   8.471  1.00 71.38           O  
ANISOU  261  O   ASN A  38     8086   9118   9919  -2692  -1577   -557       O  
ATOM    262  CB  ASN A  38     -34.725 -27.362  10.778  1.00 65.56           C  
ANISOU  262  CB  ASN A  38     7485   8299   9126  -2470  -1269   -178       C  
ATOM    263  CG  ASN A  38     -34.346 -27.173  12.236  1.00 62.60           C  
ANISOU  263  CG  ASN A  38     7149   7865   8772  -2413  -1100     27       C  
ATOM    264  OD1 ASN A  38     -35.125 -27.486  13.136  1.00 66.28           O  
ANISOU  264  OD1 ASN A  38     7489   8345   9351  -2525  -1020    144       O  
ATOM    265  ND2 ASN A  38     -33.143 -26.663  12.475  1.00 57.07           N  
ANISOU  265  ND2 ASN A  38     6616   7111   7958  -2238  -1043     69       N  
ATOM    266  N   GLY A  39     -34.268 -29.810   8.046  1.00 65.59           N  
ANISOU  266  N   GLY A  39     7687   7980   9254  -2725  -1575   -699       N  
ATOM    267  CA  GLY A  39     -34.825 -30.220   6.773  1.00 66.57           C  
ANISOU  267  CA  GLY A  39     7753   8165   9376  -2817  -1748   -926       C  
ATOM    268  C   GLY A  39     -34.503 -29.345   5.583  1.00 62.54           C  
ANISOU  268  C   GLY A  39     7280   7849   8632  -2634  -1857  -1041       C  
ATOM    269  O   GLY A  39     -35.124 -29.517   4.528  1.00 61.39           O  
ANISOU  269  O   GLY A  39     7054   7819   8454  -2690  -2012  -1222       O  
ATOM    270  N   GLY A  40     -33.560 -28.414   5.712  1.00 56.89           N  
ANISOU  270  N   GLY A  40     6681   7179   7755  -2419  -1780   -941       N  
ATOM    271  CA  GLY A  40     -33.157 -27.589   4.588  1.00 57.06           C  
ANISOU  271  CA  GLY A  40     6759   7367   7555  -2243  -1862  -1026       C  
ATOM    272  C   GLY A  40     -34.238 -26.660   4.076  1.00 58.99           C  
ANISOU  272  C   GLY A  40     6816   7901   7696  -2199  -1958  -1029       C  
ATOM    273  O   GLY A  40     -34.362 -25.524   4.543  1.00 59.63           O  
ANISOU  273  O   GLY A  40     6842   8118   7695  -2071  -1893   -874       O  
ATOM    274  N   GLY A  41     -35.026 -27.135   3.109  1.00 60.17           N  
ANISOU  274  N   GLY A  41     6868   8147   7848  -2296  -2119  -1214       N  
ATOM    275  CA  GLY A  41     -36.064 -26.294   2.535  1.00 58.10           C  
ANISOU  275  CA  GLY A  41     6421   8179   7475  -2240  -2229  -1229       C  
ATOM    276  C   GLY A  41     -37.176 -25.975   3.515  1.00 57.67           C  
ANISOU  276  C   GLY A  41     6145   8226   7542  -2321  -2179  -1088       C  
ATOM    277  O   GLY A  41     -37.697 -24.857   3.532  1.00 54.48           O  
ANISOU  277  O   GLY A  41     5630   8043   7028  -2188  -2184   -992       O  
ATOM    278  N   ALA A  42     -37.557 -26.951   4.344  1.00 61.61           N  
ANISOU  278  N   ALA A  42     6579   8565   8266  -2535  -2123  -1068       N  
ATOM    279  CA  ALA A  42     -38.566 -26.706   5.368  1.00 62.23           C  
ANISOU  279  CA  ALA A  42     6445   8736   8462  -2616  -2049   -919       C  
ATOM    280  C   ALA A  42     -38.116 -25.658   6.374  1.00 60.24           C  
ANISOU  280  C   ALA A  42     6242   8509   8137  -2439  -1889   -694       C  
ATOM    281  O   ALA A  42     -38.960 -25.041   7.033  1.00 59.52           O  
ANISOU  281  O   ALA A  42     5972   8577   8065  -2422  -1841   -573       O  
ATOM    282  CB  ALA A  42     -38.909 -28.008   6.093  1.00 64.41           C  
ANISOU  282  CB  ALA A  42     6673   8803   8995  -2881  -1995   -919       C  
ATOM    283  N   PHE A  43     -36.806 -25.447   6.505  1.00 61.94           N  
ANISOU  283  N   PHE A  43     6688   8577   8270  -2307  -1806   -647       N  
ATOM    284  CA  PHE A  43     -36.273 -24.433   7.402  1.00 62.30           C  
ANISOU  284  CA  PHE A  43     6794   8637   8240  -2137  -1667   -461       C  
ATOM    285  C   PHE A  43     -36.301 -23.038   6.790  1.00 64.62           C  
ANISOU  285  C   PHE A  43     7077   9141   8333  -1920  -1713   -438       C  
ATOM    286  O   PHE A  43     -36.289 -22.050   7.531  1.00 67.06           O  
ANISOU  286  O   PHE A  43     7368   9517   8595  -1791  -1619   -290       O  
ATOM    287  CB  PHE A  43     -34.840 -24.809   7.796  1.00 59.01           C  
ANISOU  287  CB  PHE A  43     6615   7979   7826  -2094  -1566   -428       C  
ATOM    288  CG  PHE A  43     -34.122 -23.754   8.589  1.00 55.44           C  
ANISOU  288  CG  PHE A  43     6244   7537   7282  -1914  -1441   -269       C  
ATOM    289  CD1 PHE A  43     -34.339 -23.624   9.950  1.00 55.72           C  
ANISOU  289  CD1 PHE A  43     6223   7552   7397  -1929  -1313   -110       C  
ATOM    290  CD2 PHE A  43     -33.218 -22.901   7.974  1.00 54.57           C  
ANISOU  290  CD2 PHE A  43     6269   7459   7007  -1734  -1450   -283       C  
ATOM    291  CE1 PHE A  43     -33.675 -22.658  10.683  1.00 57.11           C  
ANISOU  291  CE1 PHE A  43     6475   7738   7487  -1765  -1209     12       C  
ATOM    292  CE2 PHE A  43     -32.552 -21.931   8.701  1.00 55.84           C  
ANISOU  292  CE2 PHE A  43     6501   7617   7100  -1585  -1341   -152       C  
ATOM    293  CZ  PHE A  43     -32.780 -21.810  10.058  1.00 55.34           C  
ANISOU  293  CZ  PHE A  43     6380   7531   7115  -1600  -1227    -14       C  
ATOM    294  N   MET A  44     -36.363 -22.938   5.460  1.00 64.54           N  
ANISOU  294  N   MET A  44     7081   9237   8205  -1872  -1855   -580       N  
ATOM    295  CA  MET A  44     -36.222 -21.645   4.800  1.00 62.33           C  
ANISOU  295  CA  MET A  44     6832   9127   7723  -1651  -1890   -544       C  
ATOM    296  C   MET A  44     -37.473 -20.784   4.942  1.00 63.02           C  
ANISOU  296  C   MET A  44     6703   9457   7784  -1589  -1928   -475       C  
ATOM    297  O   MET A  44     -37.368 -19.558   5.050  1.00 65.96           O  
ANISOU  297  O   MET A  44     7099   9921   8041  -1397  -1884   -363       O  
ATOM    298  CB  MET A  44     -35.877 -21.844   3.324  1.00 65.18           C  
ANISOU  298  CB  MET A  44     7282   9537   7946  -1608  -2025   -709       C  
ATOM    299  CG  MET A  44     -34.460 -22.334   3.091  1.00 66.96           C  
ANISOU  299  CG  MET A  44     7743   9557   8143  -1590  -1971   -758       C  
ATOM    300  SD  MET A  44     -33.230 -21.312   3.927  1.00 69.57           S  
ANISOU  300  SD  MET A  44     8235   9784   8415  -1421  -1790   -567       S  
ATOM    301  CE  MET A  44     -33.541 -19.712   3.183  1.00 69.29           C  
ANISOU  301  CE  MET A  44     8170   9985   8171  -1199  -1833   -493       C  
ATOM    302  N   ILE A  45     -38.661 -21.396   4.936  1.00 64.59           N  
ANISOU  302  N   ILE A  45     6689   9760   8092  -1744  -2009   -542       N  
ATOM    303  CA  ILE A  45     -39.891 -20.612   5.079  1.00 68.40           C  
ANISOU  303  CA  ILE A  45     6942  10494   8553  -1678  -2046   -480       C  
ATOM    304  C   ILE A  45     -39.947 -19.889   6.415  1.00 69.06           C  
ANISOU  304  C   ILE A  45     6994  10566   8679  -1600  -1883   -289       C  
ATOM    305  O   ILE A  45     -40.177 -18.664   6.421  1.00 72.46           O  
ANISOU  305  O   ILE A  45     7396  11140   8994  -1398  -1872   -201       O  
ATOM    306  CB  ILE A  45     -41.122 -21.504   4.831  1.00 70.13           C  
ANISOU  306  CB  ILE A  45     6920  10828   8900  -1886  -2163   -600       C  
ATOM    307  CG1 ILE A  45     -40.977 -22.279   3.523  1.00 72.28           C  
ANISOU  307  CG1 ILE A  45     7244  11093   9127  -1966  -2330   -816       C  
ATOM    308  CG2 ILE A  45     -42.390 -20.662   4.813  1.00 69.08           C  
ANISOU  308  CG2 ILE A  45     6535  10992   8722  -1793  -2222   -553       C  
ATOM    309  CD1 ILE A  45     -42.068 -23.300   3.318  1.00 76.02           C  
ANISOU  309  CD1 ILE A  45     7496  11633   9756  -2208  -2446   -959       C  
ATOM    310  N   PRO A  46     -39.754 -20.539   7.570  1.00 65.75           N  
ANISOU  310  N   PRO A  46     6585   9985   8413  -1732  -1752   -215       N  
ATOM    311  CA  PRO A  46     -39.687 -19.768   8.819  1.00 63.06           C  
ANISOU  311  CA  PRO A  46     6240   9643   8077  -1626  -1597    -41       C  
ATOM    312  C   PRO A  46     -38.493 -18.836   8.869  1.00 56.05           C  
ANISOU  312  C   PRO A  46     5578   8660   7058  -1426  -1529     23       C  
ATOM    313  O   PRO A  46     -38.567 -17.776   9.501  1.00 55.29           O  
ANISOU  313  O   PRO A  46     5471   8631   6908  -1268  -1452    135       O  
ATOM    314  CB  PRO A  46     -39.606 -20.853   9.904  1.00 65.58           C  
ANISOU  314  CB  PRO A  46     6549   9794   8574  -1822  -1483     11       C  
ATOM    315  CG  PRO A  46     -40.097 -22.099   9.246  1.00 67.15           C  
ANISOU  315  CG  PRO A  46     6664   9960   8892  -2049  -1590   -129       C  
ATOM    316  CD  PRO A  46     -39.639 -21.986   7.832  1.00 66.03           C  
ANISOU  316  CD  PRO A  46     6634   9835   8621  -1977  -1737   -279       C  
ATOM    317  N   TYR A  47     -37.392 -19.204   8.212  1.00 56.41           N  
ANISOU  317  N   TYR A  47     5824   8552   7056  -1430  -1555    -52       N  
ATOM    318  CA  TYR A  47     -36.227 -18.328   8.163  1.00 55.18           C  
ANISOU  318  CA  TYR A  47     5871   8313   6782  -1255  -1493      3       C  
ATOM    319  C   TYR A  47     -36.547 -17.027   7.435  1.00 52.79           C  
ANISOU  319  C   TYR A  47     5549   8184   6327  -1056  -1555     27       C  
ATOM    320  O   TYR A  47     -36.138 -15.945   7.871  1.00 44.82           O  
ANISOU  320  O   TYR A  47     4615   7161   5255   -898  -1475    128       O  
ATOM    321  CB  TYR A  47     -35.065 -19.060   7.491  1.00 53.29           C  
ANISOU  321  CB  TYR A  47     5822   7904   6521  -1305  -1515    -94       C  
ATOM    322  CG  TYR A  47     -33.789 -18.261   7.400  1.00 51.79           C  
ANISOU  322  CG  TYR A  47     5831   7626   6223  -1150  -1448    -44       C  
ATOM    323  CD1 TYR A  47     -32.845 -18.307   8.414  1.00 49.23           C  
ANISOU  323  CD1 TYR A  47     5618   7138   5950  -1146  -1319     30       C  
ATOM    324  CD2 TYR A  47     -33.524 -17.470   6.291  1.00 52.87           C  
ANISOU  324  CD2 TYR A  47     6036   7848   6203  -1012  -1511    -69       C  
ATOM    325  CE1 TYR A  47     -31.676 -17.581   8.330  1.00 43.79           C  
ANISOU  325  CE1 TYR A  47     5090   6375   5173  -1021  -1261     66       C  
ATOM    326  CE2 TYR A  47     -32.363 -16.743   6.199  1.00 46.78           C  
ANISOU  326  CE2 TYR A  47     5435   6993   5346   -889  -1440    -17       C  
ATOM    327  CZ  TYR A  47     -31.441 -16.799   7.219  1.00 43.09           C  
ANISOU  327  CZ  TYR A  47     5062   6364   4945   -901  -1317     44       C  
ATOM    328  OH  TYR A  47     -30.281 -16.068   7.120  1.00 46.19           O  
ANISOU  328  OH  TYR A  47     5607   6681   5264   -793  -1249     86       O  
ATOM    329  N   ILE A  48     -37.284 -17.114   6.325  1.00 55.72           N  
ANISOU  329  N   ILE A  48     5821   8716   6635  -1058  -1700    -66       N  
ATOM    330  CA  ILE A  48     -37.665 -15.914   5.587  1.00 52.39           C  
ANISOU  330  CA  ILE A  48     5377   8469   6060   -856  -1766    -32       C  
ATOM    331  C   ILE A  48     -38.674 -15.095   6.383  1.00 54.20           C  
ANISOU  331  C   ILE A  48     5436   8841   6317   -765  -1726     73       C  
ATOM    332  O   ILE A  48     -38.576 -13.863   6.456  1.00 52.00           O  
ANISOU  332  O   ILE A  48     5210   8598   5948   -566  -1687    168       O  
ATOM    333  CB  ILE A  48     -38.208 -16.297   4.198  1.00 52.18           C  
ANISOU  333  CB  ILE A  48     5281   8598   5946   -876  -1943   -167       C  
ATOM    334  CG1 ILE A  48     -37.088 -16.867   3.325  1.00 49.94           C  
ANISOU  334  CG1 ILE A  48     5196   8186   5593   -908  -1972   -266       C  
ATOM    335  CG2 ILE A  48     -38.855 -15.099   3.518  1.00 48.37           C  
ANISOU  335  CG2 ILE A  48     4735   8332   5311   -663  -2020   -116       C  
ATOM    336  CD1 ILE A  48     -37.576 -17.453   2.019  1.00 49.02           C  
ANISOU  336  CD1 ILE A  48     5019   8210   5396   -952  -2149   -430       C  
ATOM    337  N   ILE A  49     -39.653 -15.763   6.997  1.00 55.09           N  
ANISOU  337  N   ILE A  49     5343   9031   6559   -907  -1729     59       N  
ATOM    338  CA  ILE A  49     -40.655 -15.058   7.791  1.00 53.86           C  
ANISOU  338  CA  ILE A  49     5004   9029   6430   -820  -1683    154       C  
ATOM    339  C   ILE A  49     -40.011 -14.394   9.002  1.00 50.62           C  
ANISOU  339  C   ILE A  49     4708   8488   6036   -726  -1516    278       C  
ATOM    340  O   ILE A  49     -40.352 -13.259   9.360  1.00 48.85           O  
ANISOU  340  O   ILE A  49     4454   8352   5756   -540  -1477    361       O  
ATOM    341  CB  ILE A  49     -41.782 -16.024   8.200  1.00 49.82           C  
ANISOU  341  CB  ILE A  49     4240   8625   6063  -1020  -1707    114       C  
ATOM    342  CG1 ILE A  49     -42.533 -16.515   6.961  1.00 57.24           C  
ANISOU  342  CG1 ILE A  49     5041   9729   6976  -1093  -1893    -26       C  
ATOM    343  CG2 ILE A  49     -42.742 -15.356   9.171  1.00 50.47           C  
ANISOU  343  CG2 ILE A  49     4132   8865   6179   -933  -1629    220       C  
ATOM    344  CD1 ILE A  49     -43.641 -17.497   7.265  1.00 62.42           C  
ANISOU  344  CD1 ILE A  49     5437  10489   7792  -1315  -1929    -81       C  
ATOM    345  N   ALA A  50     -39.066 -15.081   9.650  1.00 50.64           N  
ANISOU  345  N   ALA A  50     4846   8280   6112   -843  -1421    286       N  
ATOM    346  CA  ALA A  50     -38.369 -14.479  10.782  1.00 52.47           C  
ANISOU  346  CA  ALA A  50     5194   8394   6349   -754  -1275    386       C  
ATOM    347  C   ALA A  50     -37.483 -13.320  10.345  1.00 53.13           C  
ANISOU  347  C   ALA A  50     5467   8410   6309   -562  -1267    414       C  
ATOM    348  O   ALA A  50     -37.260 -12.386  11.122  1.00 55.33           O  
ANISOU  348  O   ALA A  50     5796   8659   6567   -428  -1177    491       O  
ATOM    349  CB  ALA A  50     -37.539 -15.531  11.517  1.00 48.80           C  
ANISOU  349  CB  ALA A  50     4828   7731   5981   -914  -1188    387       C  
ATOM    350  N   PHE A  51     -36.973 -13.360   9.112  1.00 53.58           N  
ANISOU  350  N   PHE A  51     5631   8441   6284   -548  -1356    349       N  
ATOM    351  CA  PHE A  51     -36.150 -12.260   8.622  1.00 52.33           C  
ANISOU  351  CA  PHE A  51     5649   8221   6014   -377  -1340    390       C  
ATOM    352  C   PHE A  51     -36.980 -11.009   8.361  1.00 58.44           C  
ANISOU  352  C   PHE A  51     6349   9149   6707   -177  -1376    452       C  
ATOM    353  O   PHE A  51     -36.484  -9.890   8.540  1.00 58.71           O  
ANISOU  353  O   PHE A  51     6504   9112   6692    -23  -1314    524       O  
ATOM    354  CB  PHE A  51     -35.412 -12.682   7.352  1.00 52.24           C  
ANISOU  354  CB  PHE A  51     5764   8161   5924   -412  -1416    312       C  
ATOM    355  CG  PHE A  51     -34.711 -11.552   6.655  1.00 56.34           C  
ANISOU  355  CG  PHE A  51     6441   8647   6317   -241  -1406    365       C  
ATOM    356  CD1 PHE A  51     -35.230 -11.008   5.490  1.00 57.42           C  
ANISOU  356  CD1 PHE A  51     6555   8932   6329   -123  -1509    366       C  
ATOM    357  CD2 PHE A  51     -33.534 -11.030   7.166  1.00 56.16           C  
ANISOU  357  CD2 PHE A  51     6586   8450   6303   -201  -1294    419       C  
ATOM    358  CE1 PHE A  51     -34.587  -9.966   4.849  1.00 57.33           C  
ANISOU  358  CE1 PHE A  51     6697   8880   6204     33  -1487    437       C  
ATOM    359  CE2 PHE A  51     -32.887  -9.987   6.531  1.00 53.58           C  
ANISOU  359  CE2 PHE A  51     6401   8080   5877    -62  -1274    477       C  
ATOM    360  CZ  PHE A  51     -33.412  -9.457   5.368  1.00 54.54           C  
ANISOU  360  CZ  PHE A  51     6511   8337   5877     54  -1365    494       C  
ATOM    361  N   LEU A  52     -38.235 -11.173   7.943  1.00 60.54           N  
ANISOU  361  N   LEU A  52     6416   9621   6964   -176  -1476    423       N  
ATOM    362  CA  LEU A  52     -39.093 -10.036   7.632  1.00 57.16           C  
ANISOU  362  CA  LEU A  52     5905   9358   6454     31  -1522    481       C  
ATOM    363  C   LEU A  52     -39.834  -9.502   8.848  1.00 60.98           C  
ANISOU  363  C   LEU A  52     6259   9906   7003    107  -1438    550       C  
ATOM    364  O   LEU A  52     -40.110  -8.298   8.917  1.00 59.56           O  
ANISOU  364  O   LEU A  52     6096   9770   6765    318  -1422    620       O  
ATOM    365  CB  LEU A  52     -40.108 -10.421   6.552  1.00 56.05           C  
ANISOU  365  CB  LEU A  52     5597   9441   6259     18  -1684    410       C  
ATOM    366  CG  LEU A  52     -39.555 -10.599   5.137  1.00 58.20           C  
ANISOU  366  CG  LEU A  52     5994   9710   6409     26  -1788    349       C  
ATOM    367  CD1 LEU A  52     -40.400 -11.587   4.349  1.00 48.87           C  
ANISOU  367  CD1 LEU A  52     4636   8707   5225   -100  -1941    223       C  
ATOM    368  CD2 LEU A  52     -39.473  -9.261   4.416  1.00 47.31           C  
ANISOU  368  CD2 LEU A  52     4719   8378   4880    278  -1811    439       C  
ATOM    369  N   LEU A  53     -40.164 -10.366   9.808  1.00 65.01           N  
ANISOU  369  N   LEU A  53     6646  10423   7631    -52  -1380    535       N  
ATOM    370  CA  LEU A  53     -40.909  -9.950  10.986  1.00 63.12           C  
ANISOU  370  CA  LEU A  53     6268  10271   7443     16  -1291    597       C  
ATOM    371  C   LEU A  53     -40.027  -9.637  12.186  1.00 61.13           C  
ANISOU  371  C   LEU A  53     6164   9839   7224     39  -1143    648       C  
ATOM    372  O   LEU A  53     -40.490  -8.960  13.109  1.00 65.64           O  
ANISOU  372  O   LEU A  53     6669  10470   7801    160  -1066    700       O  
ATOM    373  CB  LEU A  53     -41.922 -11.030  11.385  1.00 66.09           C  
ANISOU  373  CB  LEU A  53     6395  10791   7923   -166  -1303    568       C  
ATOM    374  CG  LEU A  53     -43.031 -11.352  10.381  1.00 68.05           C  
ANISOU  374  CG  LEU A  53     6435  11264   8158   -199  -1454    504       C  
ATOM    375  CD1 LEU A  53     -44.100 -12.225  11.024  1.00 67.18           C  
ANISOU  375  CD1 LEU A  53     6055  11299   8171   -368  -1434    495       C  
ATOM    376  CD2 LEU A  53     -43.644 -10.080   9.813  1.00 70.13           C  
ANISOU  376  CD2 LEU A  53     6653  11689   8305     64  -1522    539       C  
ATOM    377  N   VAL A  54     -38.779 -10.102  12.202  1.00 53.51           N  
ANISOU  377  N   VAL A  54     5388   8668   6274    -62  -1106    626       N  
ATOM    378  CA  VAL A  54     -37.907  -9.894  13.354  1.00 49.42           C  
ANISOU  378  CA  VAL A  54     4999   7995   5785    -50   -978    662       C  
ATOM    379  C   VAL A  54     -36.597  -9.254  12.916  1.00 45.43           C  
ANISOU  379  C   VAL A  54     4734   7305   5223     20   -968    657       C  
ATOM    380  O   VAL A  54     -36.175  -8.235  13.474  1.00 40.54           O  
ANISOU  380  O   VAL A  54     4213   6610   4581    157   -901    692       O  
ATOM    381  CB  VAL A  54     -37.645 -11.216  14.099  1.00 48.53           C  
ANISOU  381  CB  VAL A  54     4859   7815   5766   -258   -919    652       C  
ATOM    382  CG1 VAL A  54     -36.599 -11.011  15.181  1.00 50.53           C  
ANISOU  382  CG1 VAL A  54     5263   7911   6026   -233   -804    682       C  
ATOM    383  CG2 VAL A  54     -38.935 -11.750  14.698  1.00 44.71           C  
ANISOU  383  CG2 VAL A  54     4131   7507   5348   -329   -900    678       C  
ATOM    384  N   GLY A  55     -35.949  -9.845  11.917  1.00 43.49           N  
ANISOU  384  N   GLY A  55     4579   6988   4957    -75  -1031    610       N  
ATOM    385  CA  GLY A  55     -34.634  -9.408  11.488  1.00 47.54           C  
ANISOU  385  CA  GLY A  55     5307   7332   5425    -39  -1010    607       C  
ATOM    386  C   GLY A  55     -34.580  -7.987  10.968  1.00 55.55           C  
ANISOU  386  C   GLY A  55     6406   8341   6360    156  -1019    656       C  
ATOM    387  O   GLY A  55     -33.889  -7.138  11.538  1.00 59.51           O  
ANISOU  387  O   GLY A  55     7027   8717   6866    239   -941    687       O  
ATOM    388  N   ILE A  56     -35.302  -7.723   9.877  1.00 65.21           N  
ANISOU  388  N   ILE A  56     7570   9695   7510    231  -1118    662       N  
ATOM    389  CA  ILE A  56     -35.305  -6.378   9.297  1.00 65.47           C  
ANISOU  389  CA  ILE A  56     7693   9721   7463    430  -1128    728       C  
ATOM    390  C   ILE A  56     -35.806  -5.327  10.278  1.00 60.61           C  
ANISOU  390  C   ILE A  56     7045   9107   6876    585  -1064    780       C  
ATOM    391  O   ILE A  56     -35.147  -4.279  10.415  1.00 61.57           O  
ANISOU  391  O   ILE A  56     7320   9084   6988    696  -1005    823       O  
ATOM    392  CB  ILE A  56     -36.096  -6.380   7.974  1.00 67.62           C  
ANISOU  392  CB  ILE A  56     7889  10166   7637    493  -1257    727       C  
ATOM    393  CG1 ILE A  56     -35.211  -6.864   6.827  1.00 71.66           C  
ANISOU  393  CG1 ILE A  56     8529  10621   8077    417  -1299    694       C  
ATOM    394  CG2 ILE A  56     -36.642  -4.997   7.671  1.00 66.94           C  
ANISOU  394  CG2 ILE A  56     7821  10131   7483    731  -1271    815       C  
ATOM    395  CD1 ILE A  56     -34.076  -5.925   6.505  1.00 74.70           C  
ANISOU  395  CD1 ILE A  56     9129  10836   8415    505  -1229    762       C  
ATOM    396  N   PRO A  57     -36.931  -5.512  10.984  1.00 59.31           N  
ANISOU  396  N   PRO A  57     6690   9095   6750    603  -1066    775       N  
ATOM    397  CA  PRO A  57     -37.374  -4.460  11.915  1.00 59.44           C  
ANISOU  397  CA  PRO A  57     6687   9116   6782    775   -999    815       C  
ATOM    398  C   PRO A  57     -36.397  -4.193  13.046  1.00 59.77           C  
ANISOU  398  C   PRO A  57     6860   8973   6877    754   -884    803       C  
ATOM    399  O   PRO A  57     -36.163  -3.027  13.390  1.00 61.83           O  
ANISOU  399  O   PRO A  57     7225   9134   7132    908   -837    827       O  
ATOM    400  CB  PRO A  57     -38.713  -5.000  12.437  1.00 58.36           C  
ANISOU  400  CB  PRO A  57     6295   9202   6676    757  -1016    804       C  
ATOM    401  CG  PRO A  57     -38.660  -6.458  12.200  1.00 59.52           C  
ANISOU  401  CG  PRO A  57     6363   9388   6864    521  -1054    753       C  
ATOM    402  CD  PRO A  57     -37.908  -6.616  10.925  1.00 60.29           C  
ANISOU  402  CD  PRO A  57     6600   9404   6904    479  -1129    733       C  
ATOM    403  N   LEU A  58     -35.818  -5.239  13.642  1.00 54.63           N  
ANISOU  403  N   LEU A  58     6209   8270   6277    571   -842    763       N  
ATOM    404  CA  LEU A  58     -34.871  -5.023  14.730  1.00 55.75           C  
ANISOU  404  CA  LEU A  58     6467   8258   6457    557   -744    746       C  
ATOM    405  C   LEU A  58     -33.574  -4.400  14.233  1.00 55.88           C  
ANISOU  405  C   LEU A  58     6696   8074   6461    570   -731    743       C  
ATOM    406  O   LEU A  58     -32.903  -3.688  14.989  1.00 58.63           O  
ANISOU  406  O   LEU A  58     7151   8294   6832    624   -664    728       O  
ATOM    407  CB  LEU A  58     -34.586  -6.338  15.454  1.00 56.50           C  
ANISOU  407  CB  LEU A  58     6510   8356   6603    371   -706    718       C  
ATOM    408  CG  LEU A  58     -35.528  -6.668  16.613  1.00 55.13           C  
ANISOU  408  CG  LEU A  58     6169   8323   6456    376   -651    733       C  
ATOM    409  CD1 LEU A  58     -35.296  -8.085  17.105  1.00 53.26           C  
ANISOU  409  CD1 LEU A  58     5884   8082   6270    179   -621    727       C  
ATOM    410  CD2 LEU A  58     -35.357  -5.668  17.748  1.00 52.29           C  
ANISOU  410  CD2 LEU A  58     5864   7921   6082    524   -568    729       C  
ATOM    411  N   MET A  59     -33.203  -4.654  12.976  1.00 49.74           N  
ANISOU  411  N   MET A  59     5978   7274   5646    518   -792    751       N  
ATOM    412  CA  MET A  59     -32.018  -4.014  12.413  1.00 45.93           C  
ANISOU  412  CA  MET A  59     5685   6618   5148    532   -769    764       C  
ATOM    413  C   MET A  59     -32.198  -2.503  12.335  1.00 48.89           C  
ANISOU  413  C   MET A  59     6139   6926   5508    723   -751    817       C  
ATOM    414  O   MET A  59     -31.271  -1.743  12.637  1.00 51.78           O  
ANISOU  414  O   MET A  59     6649   7118   5909    746   -690    816       O  
ATOM    415  CB  MET A  59     -31.717  -4.597  11.032  1.00 51.65           C  
ANISOU  415  CB  MET A  59     6444   7366   5815    458   -836    769       C  
ATOM    416  CG  MET A  59     -30.653  -3.841  10.250  1.00 61.06           C  
ANISOU  416  CG  MET A  59     7814   8411   6974    492   -809    807       C  
ATOM    417  SD  MET A  59     -28.975  -4.177  10.821  1.00 69.69           S  
ANISOU  417  SD  MET A  59     9032   9317   8130    353   -724    757       S  
ATOM    418  CE  MET A  59     -28.617  -5.698   9.945  1.00 69.89           C  
ANISOU  418  CE  MET A  59     9032   9407   8116    196   -777    707       C  
ATOM    419  N   TRP A  60     -33.390  -2.051  11.939  1.00 48.67           N  
ANISOU  419  N   TRP A  60     6019   7034   5438    863   -804    860       N  
ATOM    420  CA  TRP A  60     -33.657  -0.618  11.874  1.00 45.46           C  
ANISOU  420  CA  TRP A  60     5691   6561   5023   1067   -788    916       C  
ATOM    421  C   TRP A  60     -33.688   0.005  13.264  1.00 44.18           C  
ANISOU  421  C   TRP A  60     5536   6327   4923   1141   -712    876       C  
ATOM    422  O   TRP A  60     -33.227   1.136  13.454  1.00 43.55           O  
ANISOU  422  O   TRP A  60     5597   6078   4873   1244   -667    888       O  
ATOM    423  CB  TRP A  60     -34.981  -0.363  11.155  1.00 40.72           C  
ANISOU  423  CB  TRP A  60     4970   6147   4354   1215   -871    970       C  
ATOM    424  CG  TRP A  60     -34.902  -0.480   9.668  1.00 47.42           C  
ANISOU  424  CG  TRP A  60     5862   7039   5115   1216   -947   1023       C  
ATOM    425  CD1 TRP A  60     -33.839  -0.163   8.875  1.00 45.66           C  
ANISOU  425  CD1 TRP A  60     5820   6666   4864   1187   -925   1066       C  
ATOM    426  CD2 TRP A  60     -35.935  -0.944   8.791  1.00 47.75           C  
ANISOU  426  CD2 TRP A  60     5758   7308   5077   1252  -1057   1036       C  
ATOM    427  NE1 TRP A  60     -34.145  -0.403   7.557  1.00 41.79           N  
ANISOU  427  NE1 TRP A  60     5314   6297   4267   1214  -1011   1109       N  
ATOM    428  CE2 TRP A  60     -35.426  -0.883   7.479  1.00 42.81           C  
ANISOU  428  CE2 TRP A  60     5245   6659   4361   1254  -1101   1084       C  
ATOM    429  CE3 TRP A  60     -37.239  -1.405   8.988  1.00 47.04           C  
ANISOU  429  CE3 TRP A  60     5443   7449   4980   1279  -1123   1007       C  
ATOM    430  CZ2 TRP A  60     -36.175  -1.267   6.369  1.00 51.61           C  
ANISOU  430  CZ2 TRP A  60     6263   7977   5370   1292  -1219   1094       C  
ATOM    431  CZ3 TRP A  60     -37.981  -1.787   7.886  1.00 47.50           C  
ANISOU  431  CZ3 TRP A  60     5394   7704   4949   1303  -1243   1014       C  
ATOM    432  CH2 TRP A  60     -37.448  -1.713   6.593  1.00 52.52           C  
ANISOU  432  CH2 TRP A  60     6154   8315   5487   1315  -1295   1053       C  
ATOM    433  N   ILE A  61     -34.230  -0.718  14.245  1.00 46.86           N  
ANISOU  433  N   ILE A  61     5729   6793   5284   1090   -695    827       N  
ATOM    434  CA  ILE A  61     -34.410  -0.155  15.581  1.00 47.32           C  
ANISOU  434  CA  ILE A  61     5775   6827   5376   1184   -626    784       C  
ATOM    435  C   ILE A  61     -33.063   0.065  16.258  1.00 43.31           C  
ANISOU  435  C   ILE A  61     5424   6114   4916   1108   -561    727       C  
ATOM    436  O   ILE A  61     -32.781   1.154  16.771  1.00 46.32           O  
ANISOU  436  O   ILE A  61     5911   6363   5326   1223   -521    699       O  
ATOM    437  CB  ILE A  61     -35.326  -1.060  16.423  1.00 48.04           C  
ANISOU  437  CB  ILE A  61     5662   7124   5466   1139   -613    762       C  
ATOM    438  CG1 ILE A  61     -36.771  -0.954  15.933  1.00 48.66           C  
ANISOU  438  CG1 ILE A  61     5568   7414   5508   1258   -671    807       C  
ATOM    439  CG2 ILE A  61     -35.234  -0.694  17.895  1.00 51.08           C  
ANISOU  439  CG2 ILE A  61     6054   7484   5870   1202   -529    707       C  
ATOM    440  CD1 ILE A  61     -37.597  -2.190  16.198  1.00 41.03           C  
ANISOU  440  CD1 ILE A  61     4384   6660   4548   1134   -684    804       C  
ATOM    441  N   GLU A  62     -32.212  -0.965  16.270  1.00 42.22           N  
ANISOU  441  N   GLU A  62     5302   5949   4792    917   -555    701       N  
ATOM    442  CA  GLU A  62     -30.911  -0.843  16.922  1.00 51.19           C  
ANISOU  442  CA  GLU A  62     6564   6917   5970    841   -502    641       C  
ATOM    443  C   GLU A  62     -30.058   0.232  16.259  1.00 53.20           C  
ANISOU  443  C   GLU A  62     6992   6971   6251    880   -494    656       C  
ATOM    444  O   GLU A  62     -29.337   0.971  16.940  1.00 51.34           O  
ANISOU  444  O   GLU A  62     6857   6588   6063    902   -450    600       O  
ATOM    445  CB  GLU A  62     -30.189  -2.189  16.907  1.00 57.71           C  
ANISOU  445  CB  GLU A  62     7368   7759   6799    645   -505    621       C  
ATOM    446  CG  GLU A  62     -30.981  -3.318  17.541  1.00 67.18           C  
ANISOU  446  CG  GLU A  62     8407   9132   7988    585   -504    621       C  
ATOM    447  CD  GLU A  62     -30.198  -4.613  17.608  1.00 78.00           C  
ANISOU  447  CD  GLU A  62     9781  10483   9373    404   -500    603       C  
ATOM    448  OE1 GLU A  62     -28.957  -4.556  17.734  1.00 80.54           O  
ANISOU  448  OE1 GLU A  62    10218  10670   9714    349   -477    566       O  
ATOM    449  OE2 GLU A  62     -30.826  -5.690  17.531  1.00 83.52           O  
ANISOU  449  OE2 GLU A  62    10363  11299  10073    318   -520    624       O  
ATOM    450  N   TRP A  63     -30.125   0.333  14.929  1.00 55.10           N  
ANISOU  450  N   TRP A  63     7269   7206   6462    884   -535    731       N  
ATOM    451  CA  TRP A  63     -29.434   1.414  14.237  1.00 53.97           C  
ANISOU  451  CA  TRP A  63     7287   6877   6341    932   -515    775       C  
ATOM    452  C   TRP A  63     -29.998   2.773  14.635  1.00 60.60           C  
ANISOU  452  C   TRP A  63     8180   7635   7209   1127   -496    784       C  
ATOM    453  O   TRP A  63     -29.254   3.757  14.710  1.00 64.31           O  
ANISOU  453  O   TRP A  63     8795   7898   7741   1150   -453    776       O  
ATOM    454  CB  TRP A  63     -29.532   1.210  12.724  1.00 47.22           C  
ANISOU  454  CB  TRP A  63     6452   6069   5422    921   -563    867       C  
ATOM    455  CG  TRP A  63     -28.440   1.873  11.936  1.00 44.03           C  
ANISOU  455  CG  TRP A  63     6213   5481   5035    889   -524    919       C  
ATOM    456  CD1 TRP A  63     -28.008   3.160  12.058  1.00 45.11           C  
ANISOU  456  CD1 TRP A  63     6486   5418   5234    966   -472    945       C  
ATOM    457  CD2 TRP A  63     -27.651   1.283  10.896  1.00 45.46           C  
ANISOU  457  CD2 TRP A  63     6439   5660   5173    770   -528    955       C  
ATOM    458  NE1 TRP A  63     -26.996   3.409  11.163  1.00 47.85           N  
ANISOU  458  NE1 TRP A  63     6953   5642   5587    890   -436   1006       N  
ATOM    459  CE2 TRP A  63     -26.758   2.272  10.437  1.00 47.07           C  
ANISOU  459  CE2 TRP A  63     6798   5672   5415    777   -467   1013       C  
ATOM    460  CE3 TRP A  63     -27.610   0.014  10.310  1.00 45.67           C  
ANISOU  460  CE3 TRP A  63     6390   5825   5136    659   -573    938       C  
ATOM    461  CZ2 TRP A  63     -25.835   2.032   9.421  1.00 36.70           C  
ANISOU  461  CZ2 TRP A  63     5556   4322   4065    682   -442   1064       C  
ATOM    462  CZ3 TRP A  63     -26.694  -0.222   9.300  1.00 47.49           C  
ANISOU  462  CZ3 TRP A  63     6701   6015   5327    577   -556    973       C  
ATOM    463  CH2 TRP A  63     -25.820   0.783   8.867  1.00 35.90           C  
ANISOU  463  CH2 TRP A  63     5378   4376   3886    591   -488   1040       C  
ATOM    464  N   ALA A  64     -31.303   2.843  14.906  1.00 60.83           N  
ANISOU  464  N   ALA A  64     8089   7820   7202   1266   -525    795       N  
ATOM    465  CA  ALA A  64     -31.905   4.100  15.337  1.00 57.72           C  
ANISOU  465  CA  ALA A  64     7739   7358   6832   1474   -506    794       C  
ATOM    466  C   ALA A  64     -31.452   4.474  16.743  1.00 55.92           C  
ANISOU  466  C   ALA A  64     7551   7033   6664   1480   -449    677       C  
ATOM    467  O   ALA A  64     -31.063   5.619  16.995  1.00 58.15           O  
ANISOU  467  O   ALA A  64     7971   7115   7007   1566   -417    647       O  
ATOM    468  CB  ALA A  64     -33.429   4.003  15.273  1.00 57.78           C  
ANISOU  468  CB  ALA A  64     7583   7590   6780   1627   -551    832       C  
ATOM    469  N   MET A  65     -31.502   3.518  17.674  1.00 56.16           N  
ANISOU  469  N   MET A  65     7465   7199   6675   1390   -437    607       N  
ATOM    470  CA  MET A  65     -31.076   3.796  19.042  1.00 58.00           C  
ANISOU  470  CA  MET A  65     7727   7371   6937   1403   -389    490       C  
ATOM    471  C   MET A  65     -29.600   4.167  19.096  1.00 59.34           C  
ANISOU  471  C   MET A  65     8055   7314   7176   1287   -366    433       C  
ATOM    472  O   MET A  65     -29.200   5.049  19.866  1.00 63.34           O  
ANISOU  472  O   MET A  65     8653   7680   7732   1349   -338    340       O  
ATOM    473  CB  MET A  65     -31.359   2.589  19.935  1.00 56.37           C  
ANISOU  473  CB  MET A  65     7370   7364   6684   1319   -375    454       C  
ATOM    474  CG  MET A  65     -32.759   2.027  19.788  1.00 60.86           C  
ANISOU  474  CG  MET A  65     7755   8172   7196   1383   -396    519       C  
ATOM    475  SD  MET A  65     -32.937   0.413  20.569  1.00 61.86           S  
ANISOU  475  SD  MET A  65     7717   8499   7287   1224   -374    513       S  
ATOM    476  CE  MET A  65     -33.007   0.886  22.292  1.00 63.83           C  
ANISOU  476  CE  MET A  65     7961   8781   7511   1343   -301    414       C  
ATOM    477  N   GLY A  66     -28.775   3.506  18.282  1.00 56.49           N  
ANISOU  477  N   GLY A  66     7723   6919   6822   1118   -378    479       N  
ATOM    478  CA  GLY A  66     -27.361   3.842  18.252  1.00 54.32           C  
ANISOU  478  CA  GLY A  66     7577   6445   6617   1001   -352    432       C  
ATOM    479  C   GLY A  66     -27.107   5.238  17.715  1.00 56.97           C  
ANISOU  479  C   GLY A  66     8064   6557   7023   1082   -334    462       C  
ATOM    480  O   GLY A  66     -26.375   6.025  18.322  1.00 60.03           O  
ANISOU  480  O   GLY A  66     8550   6768   7490   1073   -306    372       O  
ATOM    481  N   ARG A  67     -27.712   5.565  16.570  1.00 51.42           N  
ANISOU  481  N   ARG A  67     7386   5858   6294   1163   -351    589       N  
ATOM    482  CA  ARG A  67     -27.537   6.897  16.000  1.00 48.24           C  
ANISOU  482  CA  ARG A  67     7137   5233   5957   1254   -326    646       C  
ATOM    483  C   ARG A  67     -28.123   7.967  16.910  1.00 52.66           C  
ANISOU  483  C   ARG A  67     7740   5703   6564   1436   -314    570       C  
ATOM    484  O   ARG A  67     -27.542   9.048  17.065  1.00 59.59           O  
ANISOU  484  O   ARG A  67     8764   6335   7542   1455   -280    534       O  
ATOM    485  CB  ARG A  67     -28.175   6.966  14.613  1.00 47.98           C  
ANISOU  485  CB  ARG A  67     7112   5257   5859   1332   -353    808       C  
ATOM    486  CG  ARG A  67     -28.020   8.318  13.934  1.00 50.55           C  
ANISOU  486  CG  ARG A  67     7611   5351   6246   1435   -321    901       C  
ATOM    487  CD  ARG A  67     -28.816   8.396  12.643  1.00 57.29           C  
ANISOU  487  CD  ARG A  67     8462   6298   7009   1555   -357   1066       C  
ATOM    488  NE  ARG A  67     -30.257   8.371  12.876  1.00 59.78           N  
ANISOU  488  NE  ARG A  67     8658   6800   7256   1749   -412   1070       N  
ATOM    489  CZ  ARG A  67     -31.167   8.596  11.933  1.00 57.94           C  
ANISOU  489  CZ  ARG A  67     8405   6666   6941   1906   -457   1195       C  
ATOM    490  NH1 ARG A  67     -30.785   8.865  10.693  1.00 54.08           N  
ANISOU  490  NH1 ARG A  67     8023   6106   6418   1899   -452   1334       N  
ATOM    491  NH2 ARG A  67     -32.459   8.553  12.229  1.00 59.42           N  
ANISOU  491  NH2 ARG A  67     8461   7041   7076   2077   -507   1185       N  
ATOM    492  N   TYR A  68     -29.277   7.687  17.522  1.00 52.04           N  
ANISOU  492  N   TYR A  68     7536   5819   6419   1569   -338    541       N  
ATOM    493  CA  TYR A  68     -29.882   8.650  18.436  1.00 50.29           C  
ANISOU  493  CA  TYR A  68     7344   5537   6227   1761   -324    456       C  
ATOM    494  C   TYR A  68     -29.003   8.866  19.661  1.00 52.64           C  
ANISOU  494  C   TYR A  68     7695   5722   6585   1689   -296    285       C  
ATOM    495  O   TYR A  68     -28.781  10.004  20.089  1.00 53.56           O  
ANISOU  495  O   TYR A  68     7938   5629   6783   1777   -276    205       O  
ATOM    496  CB  TYR A  68     -31.277   8.180  18.851  1.00 45.87           C  
ANISOU  496  CB  TYR A  68     6609   5247   5572   1906   -346    462       C  
ATOM    497  CG  TYR A  68     -31.842   8.925  20.039  1.00 52.19           C  
ANISOU  497  CG  TYR A  68     7409   6040   6381   2093   -322    343       C  
ATOM    498  CD1 TYR A  68     -31.775   8.388  21.318  1.00 56.96           C  
ANISOU  498  CD1 TYR A  68     7928   6768   6948   2057   -302    217       C  
ATOM    499  CD2 TYR A  68     -32.442  10.167  19.882  1.00 56.19           C  
ANISOU  499  CD2 TYR A  68     8008   6418   6925   2318   -318    359       C  
ATOM    500  CE1 TYR A  68     -32.285   9.068  22.406  1.00 57.45           C  
ANISOU  500  CE1 TYR A  68     7991   6839   7000   2239   -277    100       C  
ATOM    501  CE2 TYR A  68     -32.958  10.852  20.964  1.00 60.06           C  
ANISOU  501  CE2 TYR A  68     8501   6901   7418   2503   -296    236       C  
ATOM    502  CZ  TYR A  68     -32.878  10.297  22.224  1.00 60.23           C  
ANISOU  502  CZ  TYR A  68     8432   7061   7392   2462   -275    103       C  
ATOM    503  OH  TYR A  68     -33.391  10.974  23.306  1.00 65.53           O  
ANISOU  503  OH  TYR A  68     9107   7743   8049   2657   -249    -28       O  
ATOM    504  N   GLY A  69     -28.498   7.777  20.244  1.00 52.14           N  
ANISOU  504  N   GLY A  69     7537   5793   6480   1533   -299    223       N  
ATOM    505  CA  GLY A  69     -27.610   7.907  21.384  1.00 54.68           C  
ANISOU  505  CA  GLY A  69     7898   6036   6841   1464   -284     60       C  
ATOM    506  C   GLY A  69     -26.252   8.470  21.018  1.00 54.66           C  
ANISOU  506  C   GLY A  69     8038   5778   6953   1320   -271     29       C  
ATOM    507  O   GLY A  69     -25.646   9.197  21.810  1.00 51.84           O  
ANISOU  507  O   GLY A  69     7761   5268   6667   1319   -264   -114       O  
ATOM    508  N   GLY A  70     -25.755   8.143  19.823  1.00 55.32           N  
ANISOU  508  N   GLY A  70     8145   5820   7053   1194   -267    156       N  
ATOM    509  CA  GLY A  70     -24.459   8.646  19.403  1.00 55.18           C  
ANISOU  509  CA  GLY A  70     8245   5575   7145   1046   -242    145       C  
ATOM    510  C   GLY A  70     -24.429  10.149  19.224  1.00 60.94           C  
ANISOU  510  C   GLY A  70     9135   6029   7991   1138   -216    142       C  
ATOM    511  O   GLY A  70     -23.383  10.777  19.407  1.00 63.82           O  
ANISOU  511  O   GLY A  70     9594   6181   8473   1028   -193     63       O  
ATOM    512  N   ALA A  71     -25.567  10.747  18.860  1.00 61.54           N  
ANISOU  512  N   ALA A  71     9241   6098   8043   1339   -219    226       N  
ATOM    513  CA  ALA A  71     -25.650  12.199  18.781  1.00 63.35           C  
ANISOU  513  CA  ALA A  71     9634   6050   8385   1459   -193    221       C  
ATOM    514  C   ALA A  71     -25.479  12.858  20.142  1.00 73.25           C  
ANISOU  514  C   ALA A  71    10930   7196   9705   1512   -198      5       C  
ATOM    515  O   ALA A  71     -25.092  14.029  20.206  1.00 77.39           O  
ANISOU  515  O   ALA A  71    11608   7433  10364   1534   -176    -47       O  
ATOM    516  CB  ALA A  71     -26.983  12.618  18.162  1.00 61.15           C  
ANISOU  516  CB  ALA A  71     9364   5822   8050   1694   -204    356       C  
ATOM    517  N   GLN A  72     -25.754  12.133  21.227  1.00 74.94           N  
ANISOU  517  N   GLN A  72    11016   7630   9826   1533   -226   -122       N  
ATOM    518  CA  GLN A  72     -25.597  12.645  22.582  1.00 73.55           C  
ANISOU  518  CA  GLN A  72    10867   7399   9680   1592   -237   -341       C  
ATOM    519  C   GLN A  72     -24.386  12.043  23.289  1.00 71.37           C  
ANISOU  519  C   GLN A  72    10547   7158   9413   1387   -253   -478       C  
ATOM    520  O   GLN A  72     -24.331  12.035  24.522  1.00 75.17           O  
ANISOU  520  O   GLN A  72    10995   7709   9855   1432   -275   -659       O  
ATOM    521  CB  GLN A  72     -26.871  12.396  23.389  1.00 75.98           C  
ANISOU  521  CB  GLN A  72    11068   7941   9861   1807   -249   -387       C  
ATOM    522  CG  GLN A  72     -28.121  12.977  22.744  1.00 83.06           C  
ANISOU  522  CG  GLN A  72    11984   8833  10740   2032   -240   -260       C  
ATOM    523  CD  GLN A  72     -29.395  12.586  23.467  1.00 86.43           C  
ANISOU  523  CD  GLN A  72    12267   9538  11036   2227   -244   -288       C  
ATOM    524  OE1 GLN A  72     -29.387  12.327  24.670  1.00 87.28           O  
ANISOU  524  OE1 GLN A  72    12313   9765  11083   2250   -244   -440       O  
ATOM    525  NE2 GLN A  72     -30.501  12.546  22.733  1.00 88.42           N  
ANISOU  525  NE2 GLN A  72    12456   9905  11234   2371   -248   -137       N  
ATOM    526  N   GLY A  73     -23.419  11.531  22.529  1.00 66.81           N  
ANISOU  526  N   GLY A  73     9962   6548   8874   1176   -243   -396       N  
ATOM    527  CA  GLY A  73     -22.173  11.062  23.101  1.00 64.85           C  
ANISOU  527  CA  GLY A  73     9676   6314   8651    985   -260   -521       C  
ATOM    528  C   GLY A  73     -22.235   9.739  23.827  1.00 63.87           C  
ANISOU  528  C   GLY A  73     9397   6486   8383    958   -287   -560       C  
ATOM    529  O   GLY A  73     -21.392   9.485  24.692  1.00 64.92           O  
ANISOU  529  O   GLY A  73     9499   6654   8515    868   -313   -708       O  
ATOM    530  N   HIS A  74     -23.198   8.880  23.500  1.00 64.01           N  
ANISOU  530  N   HIS A  74     9317   6720   8284   1029   -284   -428       N  
ATOM    531  CA  HIS A  74     -23.348   7.592  24.164  1.00 63.70           C  
ANISOU  531  CA  HIS A  74     9137   6950   8116   1004   -300   -442       C  
ATOM    532  C   HIS A  74     -23.512   6.501  23.117  1.00 58.41           C  
ANISOU  532  C   HIS A  74     8391   6406   7396    914   -294   -265       C  
ATOM    533  O   HIS A  74     -24.392   6.589  22.257  1.00 55.15           O  
ANISOU  533  O   HIS A  74     7974   6014   6967    991   -286   -133       O  
ATOM    534  CB  HIS A  74     -24.545   7.601  25.120  1.00 65.94           C  
ANISOU  534  CB  HIS A  74     9358   7400   8298   1202   -299   -492       C  
ATOM    535  CG  HIS A  74     -24.384   8.536  26.277  1.00 71.43           C  
ANISOU  535  CG  HIS A  74    10119   8007   9014   1303   -309   -692       C  
ATOM    536  ND1 HIS A  74     -23.172   8.748  26.898  1.00 72.56           N  
ANISOU  536  ND1 HIS A  74    10308   8054   9209   1190   -336   -851       N  
ATOM    537  CD2 HIS A  74     -25.280   9.318  26.925  1.00 74.57           C  
ANISOU  537  CD2 HIS A  74    10544   8405   9385   1511   -302   -772       C  
ATOM    538  CE1 HIS A  74     -23.328   9.619  27.880  1.00 74.28           C  
ANISOU  538  CE1 HIS A  74    10582   8212   9430   1320   -350  -1028       C  
ATOM    539  NE2 HIS A  74     -24.598   9.980  27.917  1.00 75.64           N  
ANISOU  539  NE2 HIS A  74    10749   8437   9553   1521   -325   -984       N  
ATOM    540  N   GLY A  75     -22.669   5.477  23.194  1.00 54.76           N  
ANISOU  540  N   GLY A  75     7867   6032   6907    760   -304   -271       N  
ATOM    541  CA  GLY A  75     -22.719   4.404  22.224  1.00 53.30           C  
ANISOU  541  CA  GLY A  75     7619   5953   6680    667   -302   -127       C  
ATOM    542  C   GLY A  75     -23.310   3.119  22.763  1.00 51.99           C  
ANISOU  542  C   GLY A  75     7324   6028   6401    677   -311   -101       C  
ATOM    543  O   GLY A  75     -23.833   2.303  22.000  1.00 52.44           O  
ANISOU  543  O   GLY A  75     7319   6189   6417    647   -314     18       O  
ATOM    544  N   THR A  76     -23.246   2.932  24.076  1.00 50.54           N  
ANISOU  544  N   THR A  76     7101   5934   6168    719   -315   -211       N  
ATOM    545  CA  THR A  76     -23.648   1.683  24.705  1.00 44.90           C  
ANISOU  545  CA  THR A  76     6273   5436   5352    713   -312   -180       C  
ATOM    546  C   THR A  76     -25.049   1.787  25.297  1.00 39.77           C  
ANISOU  546  C   THR A  76     5553   4927   4629    874   -292   -161       C  
ATOM    547  O   THR A  76     -25.566   2.876  25.559  1.00 41.99           O  
ANISOU  547  O   THR A  76     5880   5149   4927   1012   -285   -217       O  
ATOM    548  CB  THR A  76     -22.651   1.284  25.793  1.00 52.42           C  
ANISOU  548  CB  THR A  76     7217   6429   6273    662   -324   -294       C  
ATOM    549  OG1 THR A  76     -22.655   2.268  26.835  1.00 54.38           O  
ANISOU  549  OG1 THR A  76     7508   6642   6513    775   -330   -440       O  
ATOM    550  CG2 THR A  76     -21.259   1.181  25.206  1.00 57.87           C  
ANISOU  550  CG2 THR A  76     7953   6995   7037    506   -342   -316       C  
ATOM    551  N   THR A  77     -25.651   0.621  25.520  1.00 37.32           N  
ANISOU  551  N   THR A  77     5131   4807   4244    855   -277    -82       N  
ATOM    552  CA  THR A  77     -27.027   0.500  25.990  1.00 42.60           C  
ANISOU  552  CA  THR A  77     5699   5646   4843    982   -248    -37       C  
ATOM    553  C   THR A  77     -27.276   1.046  27.397  1.00 53.23           C  
ANISOU  553  C   THR A  77     7040   7065   6119   1128   -221   -150       C  
ATOM    554  O   THR A  77     -28.358   1.598  27.630  1.00 65.01           O  
ANISOU  554  O   THR A  77     8490   8629   7581   1281   -197   -147       O  
ATOM    555  CB  THR A  77     -27.474  -0.961  25.925  1.00 43.76           C  
ANISOU  555  CB  THR A  77     5725   5961   4941    891   -232     76       C  
ATOM    556  OG1 THR A  77     -26.457  -1.799  26.483  1.00 54.00           O  
ANISOU  556  OG1 THR A  77     7036   7268   6215    785   -233     49       O  
ATOM    557  CG2 THR A  77     -27.726  -1.373  24.484  1.00 38.57           C  
ANISOU  557  CG2 THR A  77     5049   5270   4335    798   -261    183       C  
ATOM    558  N   PRO A  78     -26.356   0.908  28.370  1.00 49.20           N  
ANISOU  558  N   PRO A  78     6564   6559   5570   1103   -226   -254       N  
ATOM    559  CA  PRO A  78     -26.663   1.453  29.706  1.00 51.96           C  
ANISOU  559  CA  PRO A  78     6910   6998   5833   1262   -204   -372       C  
ATOM    560  C   PRO A  78     -26.988   2.936  29.693  1.00 59.08           C  
ANISOU  560  C   PRO A  78     7895   7768   6784   1407   -213   -477       C  
ATOM    561  O   PRO A  78     -27.884   3.378  30.422  1.00 63.59           O  
ANISOU  561  O   PRO A  78     8431   8447   7284   1581   -180   -520       O  
ATOM    562  CB  PRO A  78     -25.389   1.157  30.508  1.00 53.56           C  
ANISOU  562  CB  PRO A  78     7156   7193   6001   1192   -232   -478       C  
ATOM    563  CG  PRO A  78     -24.798  -0.014  29.843  1.00 52.97           C  
ANISOU  563  CG  PRO A  78     7051   7120   5955   1018   -243   -366       C  
ATOM    564  CD  PRO A  78     -25.069   0.184  28.382  1.00 48.66           C  
ANISOU  564  CD  PRO A  78     6524   6449   5515    950   -253   -272       C  
ATOM    565  N   ALA A  79     -26.290   3.719  28.870  1.00 57.09           N  
ANISOU  565  N   ALA A  79     7756   7282   6655   1344   -250   -513       N  
ATOM    566  CA  ALA A  79     -26.596   5.140  28.767  1.00 56.26           C  
ANISOU  566  CA  ALA A  79     7746   7013   6615   1478   -255   -598       C  
ATOM    567  C   ALA A  79     -27.735   5.408  27.792  1.00 53.56           C  
ANISOU  567  C   ALA A  79     7376   6671   6302   1563   -238   -463       C  
ATOM    568  O   ALA A  79     -28.531   6.328  28.013  1.00 52.67           O  
ANISOU  568  O   ALA A  79     7288   6535   6189   1748   -224   -507       O  
ATOM    569  CB  ALA A  79     -25.348   5.916  28.348  1.00 53.89           C  
ANISOU  569  CB  ALA A  79     7582   6449   6444   1369   -293   -688       C  
ATOM    570  N   ILE A  80     -27.839   4.616  26.724  1.00 49.09           N  
ANISOU  570  N   ILE A  80     6757   6139   5756   1443   -244   -306       N  
ATOM    571  CA  ILE A  80     -28.867   4.863  25.717  1.00 52.95           C  
ANISOU  571  CA  ILE A  80     7215   6639   6266   1521   -243   -181       C  
ATOM    572  C   ILE A  80     -30.238   4.438  26.231  1.00 52.37           C  
ANISOU  572  C   ILE A  80     6989   6816   6095   1653   -211   -133       C  
ATOM    573  O   ILE A  80     -31.245   5.109  25.974  1.00 56.56           O  
ANISOU  573  O   ILE A  80     7496   7369   6626   1819   -204   -104       O  
ATOM    574  CB  ILE A  80     -28.498   4.159  24.399  1.00 49.60           C  
ANISOU  574  CB  ILE A  80     6785   6180   5883   1353   -267    -48       C  
ATOM    575  CG1 ILE A  80     -27.290   4.851  23.763  1.00 48.37           C  
ANISOU  575  CG1 ILE A  80     6780   5767   5830   1256   -284    -80       C  
ATOM    576  CG2 ILE A  80     -29.674   4.160  23.433  1.00 47.28           C  
ANISOU  576  CG2 ILE A  80     6421   5966   5576   1433   -276     83       C  
ATOM    577  CD1 ILE A  80     -26.877   4.268  22.437  1.00 47.60           C  
ANISOU  577  CD1 ILE A  80     6690   5635   5762   1109   -300     44       C  
ATOM    578  N   PHE A  81     -30.304   3.324  26.968  1.00 51.17           N  
ANISOU  578  N   PHE A  81     6725   6857   5860   1587   -185   -118       N  
ATOM    579  CA  PHE A  81     -31.566   2.928  27.586  1.00 50.33           C  
ANISOU  579  CA  PHE A  81     6463   6997   5663   1702   -138    -74       C  
ATOM    580  C   PHE A  81     -32.054   3.979  28.574  1.00 52.02           C  
ANISOU  580  C   PHE A  81     6702   7233   5830   1927   -107   -196       C  
ATOM    581  O   PHE A  81     -33.265   4.193  28.707  1.00 55.75           O  
ANISOU  581  O   PHE A  81     7069   7853   6258   2084    -74   -160       O  
ATOM    582  CB  PHE A  81     -31.417   1.580  28.294  1.00 48.33           C  
ANISOU  582  CB  PHE A  81     6108   6920   5334   1584   -104    -31       C  
ATOM    583  CG  PHE A  81     -31.524   0.392  27.379  1.00 47.11           C  
ANISOU  583  CG  PHE A  81     5871   6817   5210   1407   -120    109       C  
ATOM    584  CD1 PHE A  81     -31.627   0.556  26.008  1.00 48.86           C  
ANISOU  584  CD1 PHE A  81     6116   6941   5508   1357   -169    177       C  
ATOM    585  CD2 PHE A  81     -31.526  -0.893  27.896  1.00 44.88           C  
ANISOU  585  CD2 PHE A  81     5496   6680   4877   1298    -85    173       C  
ATOM    586  CE1 PHE A  81     -31.726  -0.542  25.172  1.00 47.26           C  
ANISOU  586  CE1 PHE A  81     5841   6790   5326   1199   -191    283       C  
ATOM    587  CE2 PHE A  81     -31.626  -1.992  27.065  1.00 45.45           C  
ANISOU  587  CE2 PHE A  81     5500   6780   4988   1133   -103    286       C  
ATOM    588  CZ  PHE A  81     -31.726  -1.816  25.701  1.00 44.37           C  
ANISOU  588  CZ  PHE A  81     5384   6551   4923   1084   -160    331       C  
ATOM    589  N   TYR A  82     -31.130   4.644  29.272  1.00 53.10           N  
ANISOU  589  N   TYR A  82     6969   7231   5974   1950   -120   -351       N  
ATOM    590  CA  TYR A  82     -31.522   5.676  30.225  1.00 58.50           C  
ANISOU  590  CA  TYR A  82     7694   7919   6613   2168    -97   -495       C  
ATOM    591  C   TYR A  82     -32.007   6.936  29.522  1.00 62.72           C  
ANISOU  591  C   TYR A  82     8315   8279   7237   2316   -116   -510       C  
ATOM    592  O   TYR A  82     -32.857   7.654  30.061  1.00 63.99           O  
ANISOU  592  O   TYR A  82     8458   8501   7354   2538    -86   -574       O  
ATOM    593  CB  TYR A  82     -30.355   6.002  31.156  1.00 57.18           C  
ANISOU  593  CB  TYR A  82     7641   7652   6432   2138   -120   -675       C  
ATOM    594  CG  TYR A  82     -30.741   6.866  32.334  1.00 55.22           C  
ANISOU  594  CG  TYR A  82     7423   7452   6104   2361    -97   -846       C  
ATOM    595  CD1 TYR A  82     -31.635   6.406  33.290  1.00 56.01           C  
ANISOU  595  CD1 TYR A  82     7392   7836   6053   2494    -31   -833       C  
ATOM    596  CD2 TYR A  82     -30.212   8.140  32.491  1.00 57.88           C  
ANISOU  596  CD2 TYR A  82     7922   7552   6521   2438   -136  -1023       C  
ATOM    597  CE1 TYR A  82     -31.992   7.188  34.371  1.00 60.83           C  
ANISOU  597  CE1 TYR A  82     8029   8509   6574   2713     -5   -998       C  
ATOM    598  CE2 TYR A  82     -30.564   8.932  33.568  1.00 63.83           C  
ANISOU  598  CE2 TYR A  82     8709   8344   7198   2651   -120  -1201       C  
ATOM    599  CZ  TYR A  82     -31.454   8.450  34.505  1.00 66.86           C  
ANISOU  599  CZ  TYR A  82     8960   9029   7413   2795    -55  -1190       C  
ATOM    600  OH  TYR A  82     -31.807   9.233  35.579  1.00 75.24           O  
ANISOU  600  OH  TYR A  82    10057  10147   8384   3022    -35  -1374       O  
ATOM    601  N   LEU A  83     -31.480   7.227  28.330  1.00 64.70           N  
ANISOU  601  N   LEU A  83     8661   8315   7606   2209   -159   -446       N  
ATOM    602  CA  LEU A  83     -31.962   8.379  27.575  1.00 65.38           C  
ANISOU  602  CA  LEU A  83     8836   8231   7775   2353   -173   -427       C  
ATOM    603  C   LEU A  83     -33.413   8.190  27.152  1.00 59.39           C  
ANISOU  603  C   LEU A  83     7929   7673   6964   2495   -155   -299       C  
ATOM    604  O   LEU A  83     -34.207   9.136  27.194  1.00 64.60           O  
ANISOU  604  O   LEU A  83     8610   8306   7629   2720   -145   -327       O  
ATOM    605  CB  LEU A  83     -31.076   8.616  26.351  1.00 66.31           C  
ANISOU  605  CB  LEU A  83     9079   8100   8015   2196   -212   -357       C  
ATOM    606  CG  LEU A  83     -29.618   9.004  26.602  1.00 60.85           C  
ANISOU  606  CG  LEU A  83     8535   7177   7406   2055   -232   -481       C  
ATOM    607  CD1 LEU A  83     -28.842   9.024  25.294  1.00 55.58           C  
ANISOU  607  CD1 LEU A  83     7952   6321   6843   1885   -253   -372       C  
ATOM    608  CD2 LEU A  83     -29.528  10.349  27.304  1.00 63.78           C  
ANISOU  608  CD2 LEU A  83     9041   7361   7832   2212   -231   -657       C  
ATOM    609  N   LEU A  84     -33.776   6.974  26.743  1.00 56.23           N  
ANISOU  609  N   LEU A  84     7374   7473   6516   2369   -153   -165       N  
ATOM    610  CA  LEU A  84     -35.145   6.703  26.321  1.00 57.78           C  
ANISOU  610  CA  LEU A  84     7402   7883   6668   2477   -143    -48       C  
ATOM    611  C   LEU A  84     -36.073   6.517  27.514  1.00 64.60           C  
ANISOU  611  C   LEU A  84     8116   9002   7425   2625    -79    -96       C  
ATOM    612  O   LEU A  84     -37.218   6.981  27.493  1.00 71.61           O  
ANISOU  612  O   LEU A  84     8912  10012   8286   2827    -61    -72       O  
ATOM    613  CB  LEU A  84     -35.180   5.463  25.429  1.00 57.16           C  
ANISOU  613  CB  LEU A  84     7213   7915   6591   2271   -170     96       C  
ATOM    614  CG  LEU A  84     -34.148   5.425  24.303  1.00 59.15           C  
ANISOU  614  CG  LEU A  84     7599   7950   6924   2100   -223    144       C  
ATOM    615  CD1 LEU A  84     -34.152   4.072  23.617  1.00 61.52           C  
ANISOU  615  CD1 LEU A  84     7785   8380   7210   1899   -246    255       C  
ATOM    616  CD2 LEU A  84     -34.432   6.529  23.306  1.00 59.66           C  
ANISOU  616  CD2 LEU A  84     7764   7857   7048   2235   -257    191       C  
ATOM    617  N   TRP A  85     -35.597   5.839  28.556  1.00 64.12           N  
ANISOU  617  N   TRP A  85     8027   9039   7298   2537    -40   -155       N  
ATOM    618  CA  TRP A  85     -36.388   5.553  29.752  1.00 60.39           C  
ANISOU  618  CA  TRP A  85     7413   8828   6705   2662     37   -187       C  
ATOM    619  C   TRP A  85     -35.611   6.072  30.958  1.00 62.68           C  
ANISOU  619  C   TRP A  85     7829   9042   6943   2728     55   -366       C  
ATOM    620  O   TRP A  85     -34.675   5.418  31.428  1.00 64.95           O  
ANISOU  620  O   TRP A  85     8154   9319   7203   2571     51   -395       O  
ATOM    621  CB  TRP A  85     -36.675   4.060  29.872  1.00 56.10           C  
ANISOU  621  CB  TRP A  85     6691   8516   6108   2489     74    -59       C  
ATOM    622  CG  TRP A  85     -37.609   3.704  30.985  1.00 59.46           C  
ANISOU  622  CG  TRP A  85     6948   9232   6413   2607    168    -51       C  
ATOM    623  CD1 TRP A  85     -38.515   4.524  31.592  1.00 66.03           C  
ANISOU  623  CD1 TRP A  85     7725  10182   7181   2865    217   -117       C  
ATOM    624  CD2 TRP A  85     -37.731   2.428  31.626  1.00 60.85           C  
ANISOU  624  CD2 TRP A  85     6988   9617   6514   2476    234     35       C  
ATOM    625  NE1 TRP A  85     -39.193   3.839  32.571  1.00 66.90           N  
ANISOU  625  NE1 TRP A  85     7664  10582   7175   2900    315    -76       N  
ATOM    626  CE2 TRP A  85     -38.730   2.550  32.612  1.00 65.45           C  
ANISOU  626  CE2 TRP A  85     7431  10451   6985   2659    329     25       C  
ATOM    627  CE3 TRP A  85     -37.092   1.196  31.462  1.00 58.46           C  
ANISOU  627  CE3 TRP A  85     6673   9309   6230   2228    226    124       C  
ATOM    628  CZ2 TRP A  85     -39.104   1.486  33.431  1.00 68.27           C  
ANISOU  628  CZ2 TRP A  85     7637  11053   7249   2591    423    116       C  
ATOM    629  CZ3 TRP A  85     -37.464   0.141  32.275  1.00 61.46           C  
ANISOU  629  CZ3 TRP A  85     6913   9912   6526   2165    313    210       C  
ATOM    630  CH2 TRP A  85     -38.461   0.293  33.247  1.00 66.21           C  
ANISOU  630  CH2 TRP A  85     7377  10762   7017   2340    414    212       C  
ATOM    631  N   ARG A  86     -35.998   7.246  31.456  1.00 62.48           N  
ANISOU  631  N   ARG A  86     7869   8968   6902   2969     68   -494       N  
ATOM    632  CA  ARG A  86     -35.321   7.848  32.599  1.00 65.24           C  
ANISOU  632  CA  ARG A  86     8342   9246   7200   3053     74   -694       C  
ATOM    633  C   ARG A  86     -35.603   7.059  33.873  1.00 66.69           C  
ANISOU  633  C   ARG A  86     8397   9726   7217   3084    149   -710       C  
ATOM    634  O   ARG A  86     -36.256   7.561  34.793  1.00 72.03           O  
ANISOU  634  O   ARG A  86     9037  10542   7789   3309    204   -808       O  
ATOM    635  CB  ARG A  86     -35.750   9.308  32.767  1.00 70.81           C  
ANISOU  635  CB  ARG A  86     9153   9815   7936   3317     70   -833       C  
ATOM    636  CG  ARG A  86     -34.599  10.306  32.736  1.00 74.58           C  
ANISOU  636  CG  ARG A  86     9866   9949   8521   3288      5  -1000       C  
ATOM    637  CD  ARG A  86     -33.958  10.378  31.357  1.00 75.90           C  
ANISOU  637  CD  ARG A  86    10128   9862   8847   3104    -55   -890       C  
ATOM    638  NE  ARG A  86     -34.873  10.910  30.350  1.00 78.12           N  
ANISOU  638  NE  ARG A  86    10396  10094   9194   3233    -58   -771       N  
ATOM    639  N   ASN A  87     -35.107   5.824  33.933  1.00 66.28           N  
ANISOU  639  N   ASN A  87     8281   9769   7133   2869    157   -611       N  
ATOM    640  CA  ASN A  87     -35.320   4.935  35.064  1.00 68.53           C  
ANISOU  640  CA  ASN A  87     8448  10329   7260   2873    235   -585       C  
ATOM    641  C   ASN A  87     -34.005   4.262  35.427  1.00 66.97           C  
ANISOU  641  C   ASN A  87     8335  10067   7045   2685    199   -615       C  
ATOM    642  O   ASN A  87     -33.154   4.019  34.567  1.00 66.33           O  
ANISOU  642  O   ASN A  87     8331   9793   7079   2494    130   -579       O  
ATOM    643  CB  ASN A  87     -36.390   3.871  34.748  1.00 68.70           C  
ANISOU  643  CB  ASN A  87     8250  10595   7258   2809    303   -373       C  
ATOM    644  CG  ASN A  87     -36.756   3.017  35.955  1.00 71.87           C  
ANISOU  644  CG  ASN A  87     8522  11289   7495   2833    406   -324       C  
ATOM    645  OD1 ASN A  87     -35.891   2.535  36.686  1.00 73.89           O  
ANISOU  645  OD1 ASN A  87     8842  11556   7676   2758    409   -362       O  
ATOM    646  ND2 ASN A  87     -38.053   2.822  36.162  1.00 74.21           N  
ANISOU  646  ND2 ASN A  87     8629  11835   7733   2942    496   -231       N  
ATOM    647  N   ARG A  88     -33.850   3.956  36.718  1.00 68.71           N  
ANISOU  647  N   ARG A  88     8535  10466   7106   2754    247   -680       N  
ATOM    648  CA  ARG A  88     -32.663   3.236  37.164  1.00 67.00           C  
ANISOU  648  CA  ARG A  88     8379  10229   6847   2601    215   -699       C  
ATOM    649  C   ARG A  88     -32.653   1.802  36.652  1.00 64.90           C  
ANISOU  649  C   ARG A  88     8011  10040   6608   2386    240   -481       C  
ATOM    650  O   ARG A  88     -31.583   1.258  36.358  1.00 64.99           O  
ANISOU  650  O   ARG A  88     8091   9931   6671   2209    183   -467       O  
ATOM    651  CB  ARG A  88     -32.578   3.257  38.690  1.00 67.48           C  
ANISOU  651  CB  ARG A  88     8440  10491   6709   2753    262   -813       C  
ATOM    652  N   PHE A  89     -33.828   1.176  36.534  1.00 66.23           N  
ANISOU  652  N   PHE A  89     8011  10403   6750   2396    323   -316       N  
ATOM    653  CA  PHE A  89     -33.898  -0.186  36.021  1.00 68.81           C  
ANISOU  653  CA  PHE A  89     8241  10785   7119   2186    346   -116       C  
ATOM    654  C   PHE A  89     -33.529  -0.268  34.545  1.00 71.51           C  
ANISOU  654  C   PHE A  89     8628  10905   7637   2013    260    -66       C  
ATOM    655  O   PHE A  89     -33.180  -1.352  34.066  1.00 75.70           O  
ANISOU  655  O   PHE A  89     9133  11413   8217   1818    250     54       O  
ATOM    656  CB  PHE A  89     -35.299  -0.761  36.241  1.00 71.11           C  
ANISOU  656  CB  PHE A  89     8328  11336   7355   2231    457     36       C  
ATOM    657  CG  PHE A  89     -35.378  -2.252  36.066  1.00 71.02           C  
ANISOU  657  CG  PHE A  89     8214  11406   7363   2023    500    231       C  
ATOM    658  N   ALA A  90     -33.599   0.849  33.816  1.00 67.80           N  
ANISOU  658  N   ALA A  90     8233  10269   7259   2089    202   -151       N  
ATOM    659  CA  ALA A  90     -33.166   0.847  32.424  1.00 60.93           C  
ANISOU  659  CA  ALA A  90     7423   9189   6538   1940    123   -105       C  
ATOM    660  C   ALA A  90     -31.657   0.684  32.310  1.00 59.76           C  
ANISOU  660  C   ALA A  90     7419   8854   6434   1793     58   -171       C  
ATOM    661  O   ALA A  90     -31.168   0.102  31.335  1.00 54.62           O  
ANISOU  661  O   ALA A  90     6786   8095   5872   1617     16    -91       O  
ATOM    662  CB  ALA A  90     -33.615   2.132  31.728  1.00 57.21           C  
ANISOU  662  CB  ALA A  90     7006   8587   6143   2077     85   -166       C  
ATOM    663  N   LYS A  91     -30.905   1.189  33.292  1.00 62.60           N  
ANISOU  663  N   LYS A  91     7873   9184   6727   1868     48   -324       N  
ATOM    664  CA  LYS A  91     -29.459   1.004  33.282  1.00 61.09           C  
ANISOU  664  CA  LYS A  91     7794   8846   6571   1732    -15   -394       C  
ATOM    665  C   LYS A  91     -29.075  -0.437  33.594  1.00 59.49           C  
ANISOU  665  C   LYS A  91     7529   8764   6310   1596      9   -280       C  
ATOM    666  O   LYS A  91     -28.047  -0.919  33.108  1.00 60.38           O  
ANISOU  666  O   LYS A  91     7698   8759   6486   1440    -41   -268       O  
ATOM    667  CB  LYS A  91     -28.794   1.953  34.280  1.00 63.18           C  
ANISOU  667  CB  LYS A  91     8163   9061   6780   1852    -43   -606       C  
ATOM    668  CG  LYS A  91     -29.161   3.416  34.100  1.00 66.33           C  
ANISOU  668  CG  LYS A  91     8642   9320   7242   2003    -63   -734       C  
ATOM    669  CD  LYS A  91     -28.105   4.325  34.711  1.00 66.35           C  
ANISOU  669  CD  LYS A  91     8782   9173   7255   2035   -124   -959       C  
ATOM    670  CE  LYS A  91     -28.626   5.742  34.880  1.00 69.24           C  
ANISOU  670  CE  LYS A  91     9224   9431   7652   2229   -128  -1105       C  
ATOM    671  NZ  LYS A  91     -27.530   6.739  35.022  1.00 70.55           N  
ANISOU  671  NZ  LYS A  91     9543   9358   7906   2203   -203  -1313       N  
ATOM    672  N   ILE A  92     -29.883  -1.136  34.394  1.00 59.90           N  
ANISOU  672  N   ILE A  92     7466   9049   6244   1656     91   -190       N  
ATOM    673  CA  ILE A  92     -29.574  -2.522  34.736  1.00 59.42           C  
ANISOU  673  CA  ILE A  92     7355   9091   6130   1535    124    -64       C  
ATOM    674  C   ILE A  92     -29.807  -3.431  33.535  1.00 56.63           C  
ANISOU  674  C   ILE A  92     6946   8677   5896   1352    117     94       C  
ATOM    675  O   ILE A  92     -28.973  -4.285  33.211  1.00 56.72           O  
ANISOU  675  O   ILE A  92     6993   8612   5946   1203     86    144       O  
ATOM    676  CB  ILE A  92     -30.397  -2.971  35.955  1.00 61.02           C  
ANISOU  676  CB  ILE A  92     7455   9559   6173   1653    228      1       C  
ATOM    677  CG1 ILE A  92     -30.064  -2.101  37.168  1.00 67.56           C  
ANISOU  677  CG1 ILE A  92     8350  10456   6862   1842    226   -177       C  
ATOM    678  CG2 ILE A  92     -30.135  -4.436  36.263  1.00 56.93           C  
ANISOU  678  CG2 ILE A  92     6892   9126   5611   1526    272    158       C  
ATOM    679  CD1 ILE A  92     -28.587  -2.045  37.490  1.00 69.33           C  
ANISOU  679  CD1 ILE A  92     8699  10570   7072   1794    141   -302       C  
ATOM    680  N   LEU A  93     -30.947  -3.264  32.858  1.00 53.87           N  
ANISOU  680  N   LEU A  93     6502   8366   5600   1370    139    166       N  
ATOM    681  CA  LEU A  93     -31.191  -4.025  31.638  1.00 51.04           C  
ANISOU  681  CA  LEU A  93     6091   7947   5353   1203    115    289       C  
ATOM    682  C   LEU A  93     -30.212  -3.637  30.539  1.00 50.29           C  
ANISOU  682  C   LEU A  93     6121   7620   5368   1110     22    228       C  
ATOM    683  O   LEU A  93     -29.944  -4.435  29.634  1.00 52.10           O  
ANISOU  683  O   LEU A  93     6345   7778   5671    951     -8    305       O  
ATOM    684  CB  LEU A  93     -32.632  -3.823  31.165  1.00 51.01           C  
ANISOU  684  CB  LEU A  93     5950   8056   5376   1259    147    360       C  
ATOM    685  CG  LEU A  93     -33.719  -4.446  32.042  1.00 50.49           C  
ANISOU  685  CG  LEU A  93     5721   8239   5224   1305    253    461       C  
ATOM    686  CD1 LEU A  93     -35.078  -3.844  31.720  1.00 44.09           C  
ANISOU  686  CD1 LEU A  93     4777   7548   4427   1420    277    482       C  
ATOM    687  CD2 LEU A  93     -33.744  -5.959  31.881  1.00 52.44           C  
ANISOU  687  CD2 LEU A  93     5895   8524   5504   1108    283    611       C  
ATOM    688  N   GLY A  94     -29.670  -2.419  30.600  1.00 49.49           N  
ANISOU  688  N   GLY A  94     6130   7394   5279   1204    -19     87       N  
ATOM    689  CA  GLY A  94     -28.654  -2.004  29.651  1.00 43.64           C  
ANISOU  689  CA  GLY A  94     5508   6433   4640   1113    -92     33       C  
ATOM    690  C   GLY A  94     -27.316  -2.686  29.844  1.00 41.67           C  
ANISOU  690  C   GLY A  94     5323   6118   4391    987   -120      8       C  
ATOM    691  O   GLY A  94     -26.497  -2.690  28.920  1.00 46.59           O  
ANISOU  691  O   GLY A  94     6014   6587   5101    874   -169      2       O  
ATOM    692  N   VAL A  95     -27.075  -3.260  31.026  1.00 41.35           N  
ANISOU  692  N   VAL A  95     5259   6204   4247   1016    -87     -2       N  
ATOM    693  CA  VAL A  95     -25.836  -3.997  31.257  1.00 43.80           C  
ANISOU  693  CA  VAL A  95     5618   6475   4547    915   -116    -15       C  
ATOM    694  C   VAL A  95     -25.764  -5.218  30.352  1.00 47.37           C  
ANISOU  694  C   VAL A  95     6038   6898   5065    754   -118    122       C  
ATOM    695  O   VAL A  95     -24.672  -5.657  29.969  1.00 53.18           O  
ANISOU  695  O   VAL A  95     6829   7535   5842    651   -159    107       O  
ATOM    696  CB  VAL A  95     -25.712  -4.382  32.746  1.00 48.99           C  
ANISOU  696  CB  VAL A  95     6255   7299   5059   1006    -79    -36       C  
ATOM    697  CG1 VAL A  95     -24.405  -5.118  33.009  1.00 46.04           C  
ANISOU  697  CG1 VAL A  95     5929   6894   4668    924   -117    -51       C  
ATOM    698  CG2 VAL A  95     -25.807  -3.146  33.623  1.00 53.03           C  
ANISOU  698  CG2 VAL A  95     6803   7844   5500   1175    -83   -196       C  
ATOM    699  N   PHE A  96     -26.919  -5.780  29.983  1.00 46.28           N  
ANISOU  699  N   PHE A  96     5802   6843   4938    729    -76    246       N  
ATOM    700  CA  PHE A  96     -26.930  -6.905  29.054  1.00 44.65           C  
ANISOU  700  CA  PHE A  96     5566   6595   4802    572    -86    357       C  
ATOM    701  C   PHE A  96     -26.342  -6.521  27.703  1.00 49.34           C  
ANISOU  701  C   PHE A  96     6231   7020   5497    492   -153    319       C  
ATOM    702  O   PHE A  96     -25.766  -7.369  27.013  1.00 53.65           O  
ANISOU  702  O   PHE A  96     6798   7495   6091    366   -178    359       O  
ATOM    703  CB  PHE A  96     -28.353  -7.434  28.885  1.00 43.90           C  
ANISOU  703  CB  PHE A  96     5341   6626   4714    558    -37    475       C  
ATOM    704  CG  PHE A  96     -28.829  -8.270  30.038  1.00 46.11           C  
ANISOU  704  CG  PHE A  96     5544   7065   4910    577     44    564       C  
ATOM    705  CD1 PHE A  96     -28.376  -9.569  30.202  1.00 42.04           C  
ANISOU  705  CD1 PHE A  96     5036   6537   4402    464     62    652       C  
ATOM    706  CD2 PHE A  96     -29.732  -7.759  30.955  1.00 51.03           C  
ANISOU  706  CD2 PHE A  96     6092   7851   5448    716    110    566       C  
ATOM    707  CE1 PHE A  96     -28.812 -10.342  31.261  1.00 48.00           C  
ANISOU  707  CE1 PHE A  96     5728   7429   5079    482    148    756       C  
ATOM    708  CE2 PHE A  96     -30.172  -8.528  32.017  1.00 54.96           C  
ANISOU  708  CE2 PHE A  96     6517   8507   5859    735    199    664       C  
ATOM    709  CZ  PHE A  96     -29.711  -9.821  32.169  1.00 53.54           C  
ANISOU  709  CZ  PHE A  96     6350   8305   5689    614    220    766       C  
ATOM    710  N   GLY A  97     -26.474  -5.255  27.309  1.00 48.34           N  
ANISOU  710  N   GLY A  97     6146   6823   5400    569   -178    246       N  
ATOM    711  CA  GLY A  97     -25.835  -4.781  26.095  1.00 45.36           C  
ANISOU  711  CA  GLY A  97     5846   6283   5106    503   -229    218       C  
ATOM    712  C   GLY A  97     -24.325  -4.720  26.168  1.00 45.68           C  
ANISOU  712  C   GLY A  97     5979   6208   5168    442   -258    137       C  
ATOM    713  O   GLY A  97     -23.678  -4.560  25.127  1.00 49.77           O  
ANISOU  713  O   GLY A  97     6553   6603   5753    362   -289    132       O  
ATOM    714  N   LEU A  98     -23.755  -4.817  27.367  1.00 46.25           N  
ANISOU  714  N   LEU A  98     6062   6333   5179    483   -249     72       N  
ATOM    715  CA  LEU A  98     -22.322  -5.012  27.543  1.00 47.36           C  
ANISOU  715  CA  LEU A  98     6259   6405   5330    420   -281      1       C  
ATOM    716  C   LEU A  98     -21.970  -6.446  27.901  1.00 39.15           C  
ANISOU  716  C   LEU A  98     5185   5442   4247    360   -270     74       C  
ATOM    717  O   LEU A  98     -20.902  -6.929  27.513  1.00 36.16           O  
ANISOU  717  O   LEU A  98     4839   4997   3903    277   -297     60       O  
ATOM    718  CB  LEU A  98     -21.783  -4.082  28.636  1.00 53.42           C  
ANISOU  718  CB  LEU A  98     7066   7177   6055    515   -296   -144       C  
ATOM    719  CG  LEU A  98     -21.967  -2.575  28.455  1.00 54.28           C  
ANISOU  719  CG  LEU A  98     7230   7178   6216    584   -309   -242       C  
ATOM    720  CD1 LEU A  98     -21.429  -1.834  29.669  1.00 49.54           C  
ANISOU  720  CD1 LEU A  98     6663   6594   5565    672   -330   -404       C  
ATOM    721  CD2 LEU A  98     -21.283  -2.096  27.185  1.00 55.70           C  
ANISOU  721  CD2 LEU A  98     7472   7176   6514    480   -334   -245       C  
ATOM    722  N   TRP A  99     -22.856  -7.136  28.621  1.00 41.16           N  
ANISOU  722  N   TRP A  99     5374   5833   4432    403   -223    158       N  
ATOM    723  CA  TRP A  99     -22.580  -8.503  29.048  1.00 41.88           C  
ANISOU  723  CA  TRP A  99     5444   5984   4485    355   -203    244       C  
ATOM    724  C   TRP A  99     -22.660  -9.474  27.877  1.00 43.24           C  
ANISOU  724  C   TRP A  99     5608   6082   4740    222   -211    336       C  
ATOM    725  O   TRP A  99     -21.785 -10.332  27.711  1.00 45.27           O  
ANISOU  725  O   TRP A  99     5897   6290   5014    158   -228    352       O  
ATOM    726  CB  TRP A  99     -23.556  -8.903  30.154  1.00 46.46           C  
ANISOU  726  CB  TRP A  99     5957   6727   4969    435   -137    323       C  
ATOM    727  CG  TRP A  99     -23.352 -10.286  30.681  1.00 50.16           C  
ANISOU  727  CG  TRP A  99     6413   7249   5397    395   -103    433       C  
ATOM    728  CD1 TRP A  99     -22.411 -10.689  31.582  1.00 50.99           C  
ANISOU  728  CD1 TRP A  99     6558   7394   5424    442   -111    414       C  
ATOM    729  CD2 TRP A  99     -24.114 -11.451  30.346  1.00 51.56           C  
ANISOU  729  CD2 TRP A  99     6536   7440   5615    304    -58    581       C  
ATOM    730  NE1 TRP A  99     -22.538 -12.035  31.828  1.00 51.76           N  
ANISOU  730  NE1 TRP A  99     6640   7519   5508    396    -67    556       N  
ATOM    731  CE2 TRP A  99     -23.577 -12.526  31.081  1.00 52.63           C  
ANISOU  731  CE2 TRP A  99     6696   7603   5700    301    -32    658       C  
ATOM    732  CE3 TRP A  99     -25.198 -11.690  29.495  1.00 49.52           C  
ANISOU  732  CE3 TRP A  99     6209   7171   5434    223    -41    653       C  
ATOM    733  CZ2 TRP A  99     -24.085 -13.820  30.990  1.00 52.66           C  
ANISOU  733  CZ2 TRP A  99     6668   7600   5741    212     18    807       C  
ATOM    734  CZ3 TRP A  99     -25.701 -12.975  29.407  1.00 50.47           C  
ANISOU  734  CZ3 TRP A  99     6285   7298   5592    124      1    785       C  
ATOM    735  CH2 TRP A  99     -25.144 -14.023  30.150  1.00 50.48           C  
ANISOU  735  CH2 TRP A  99     6323   7303   5556    115     34    863       C  
ATOM    736  N   ILE A 100     -23.707  -9.355  27.056  1.00 42.94           N  
ANISOU  736  N   ILE A 100     5525   6041   4751    191   -204    388       N  
ATOM    737  CA  ILE A 100     -23.856 -10.256  25.908  1.00 35.86           C  
ANISOU  737  CA  ILE A 100     4616   5082   3925     67   -221    455       C  
ATOM    738  C   ILE A 100     -22.670 -10.179  24.960  1.00 34.02           C  
ANISOU  738  C   ILE A 100     4462   4719   3744      3   -270    394       C  
ATOM    739  O   ILE A 100     -22.091 -11.236  24.643  1.00 41.60           O  
ANISOU  739  O   ILE A 100     5443   5635   4727    -74   -279    423       O  
ATOM    740  CB  ILE A 100     -25.201  -9.996  25.205  1.00 38.89           C  
ANISOU  740  CB  ILE A 100     4927   5510   4341     60   -219    503       C  
ATOM    741  CG1 ILE A 100     -26.363 -10.435  26.099  1.00 36.83           C  
ANISOU  741  CG1 ILE A 100     4562   5392   4038     92   -157    586       C  
ATOM    742  CG2 ILE A 100     -25.256 -10.722  23.869  1.00 33.03           C  
ANISOU  742  CG2 ILE A 100     4184   4699   3668    -62   -258    536       C  
ATOM    743  CD1 ILE A 100     -27.722 -10.217  25.478  1.00 33.25           C  
ANISOU  743  CD1 ILE A 100     4008   5010   3616     88   -157    630       C  
ATOM    744  N   PRO A 101     -22.234  -9.007  24.477  1.00 29.05           N  
ANISOU  744  N   PRO A 101     3880   4021   3138     32   -297    315       N  
ATOM    745  CA  PRO A 101     -21.081  -8.990  23.564  1.00 28.64           C  
ANISOU  745  CA  PRO A 101     3892   3858   3133    -38   -328    270       C  
ATOM    746  C   PRO A 101     -19.812  -9.530  24.193  1.00 38.87           C  
ANISOU  746  C   PRO A 101     5214   5143   4411    -50   -334    228       C  
ATOM    747  O   PRO A 101     -18.996 -10.143  23.494  1.00 44.47           O  
ANISOU  747  O   PRO A 101     5950   5794   5153   -119   -350    226       O  
ATOM    748  CB  PRO A 101     -20.927  -7.505  23.201  1.00 29.09           C  
ANISOU  748  CB  PRO A 101     3991   3845   3217      5   -339    204       C  
ATOM    749  CG  PRO A 101     -22.166  -6.849  23.646  1.00 28.22           C  
ANISOU  749  CG  PRO A 101     3841   3800   3080     97   -322    221       C  
ATOM    750  CD  PRO A 101     -22.695  -7.640  24.782  1.00 33.51           C  
ANISOU  750  CD  PRO A 101     4449   4594   3689    131   -292    261       C  
ATOM    751  N   LEU A 102     -19.623  -9.320  25.497  1.00 41.21           N  
ANISOU  751  N   LEU A 102     5501   5507   4648     28   -325    189       N  
ATOM    752  CA  LEU A 102     -18.419  -9.806  26.160  1.00 39.75           C  
ANISOU  752  CA  LEU A 102     5333   5336   4435     36   -341    146       C  
ATOM    753  C   LEU A 102     -18.403 -11.328  26.221  1.00 40.22           C  
ANISOU  753  C   LEU A 102     5383   5417   4481      0   -326    241       C  
ATOM    754  O   LEU A 102     -17.397 -11.961  25.879  1.00 42.68           O  
ANISOU  754  O   LEU A 102     5719   5682   4815    -37   -346    228       O  
ATOM    755  CB  LEU A 102     -18.318  -9.207  27.562  1.00 43.52           C  
ANISOU  755  CB  LEU A 102     5801   5902   4832    142   -342     77       C  
ATOM    756  CG  LEU A 102     -16.916  -8.831  28.041  1.00 48.02           C  
ANISOU  756  CG  LEU A 102     6389   6465   5391    158   -385    -43       C  
ATOM    757  CD1 LEU A 102     -16.261  -7.875  27.060  1.00 43.35           C  
ANISOU  757  CD1 LEU A 102     5826   5750   4896     89   -409   -126       C  
ATOM    758  CD2 LEU A 102     -16.978  -8.217  29.430  1.00 56.88           C  
ANISOU  758  CD2 LEU A 102     7502   7690   6420    273   -394   -125       C  
ATOM    759  N   VAL A 103     -19.514 -11.935  26.644  1.00 39.87           N  
ANISOU  759  N   VAL A 103     5302   5437   4409     12   -288    341       N  
ATOM    760  CA  VAL A 103     -19.557 -13.388  26.779  1.00 41.65           C  
ANISOU  760  CA  VAL A 103     5527   5662   4635    -27   -266    441       C  
ATOM    761  C   VAL A 103     -19.474 -14.058  25.413  1.00 39.34           C  
ANISOU  761  C   VAL A 103     5255   5262   4429   -135   -287    459       C  
ATOM    762  O   VAL A 103     -18.811 -15.091  25.255  1.00 46.09           O  
ANISOU  762  O   VAL A 103     6144   6065   5304   -166   -293    483       O  
ATOM    763  CB  VAL A 103     -20.819 -13.818  27.549  1.00 46.29           C  
ANISOU  763  CB  VAL A 103     6062   6344   5184     -5   -208    550       C  
ATOM    764  CG1 VAL A 103     -20.862 -15.331  27.696  1.00 48.50           C  
ANISOU  764  CG1 VAL A 103     6351   6595   5482    -58   -179    666       C  
ATOM    765  CG2 VAL A 103     -20.856 -13.153  28.914  1.00 49.44           C  
ANISOU  765  CG2 VAL A 103     6445   6866   5475    120   -186    523       C  
ATOM    766  N   VAL A 104     -20.135 -13.485  24.405  1.00 34.96           N  
ANISOU  766  N   VAL A 104     4684   4679   3919   -181   -300    445       N  
ATOM    767  CA  VAL A 104     -20.080 -14.067  23.067  1.00 34.02           C  
ANISOU  767  CA  VAL A 104     4585   4477   3863   -274   -325    448       C  
ATOM    768  C   VAL A 104     -18.671 -13.963  22.494  1.00 33.70           C  
ANISOU  768  C   VAL A 104     4601   4367   3837   -282   -352    371       C  
ATOM    769  O   VAL A 104     -18.156 -14.920  21.905  1.00 38.48           O  
ANISOU  769  O   VAL A 104     5237   4914   4471   -328   -363    375       O  
ATOM    770  CB  VAL A 104     -21.122 -13.408  22.145  1.00 37.48           C  
ANISOU  770  CB  VAL A 104     4990   4926   4327   -301   -340    452       C  
ATOM    771  CG1 VAL A 104     -21.009 -13.971  20.737  1.00 32.98           C  
ANISOU  771  CG1 VAL A 104     4445   4287   3801   -385   -375    440       C  
ATOM    772  CG2 VAL A 104     -22.525 -13.635  22.686  1.00 36.39           C  
ANISOU  772  CG2 VAL A 104     4772   4873   4181   -299   -311    529       C  
ATOM    773  N   ALA A 105     -18.019 -12.811  22.673  1.00 33.51           N  
ANISOU  773  N   ALA A 105     4588   4348   3798   -237   -360    297       N  
ATOM    774  CA  ALA A 105     -16.653 -12.646  22.187  1.00 33.56           C  
ANISOU  774  CA  ALA A 105     4626   4303   3822   -253   -377    226       C  
ATOM    775  C   ALA A 105     -15.665 -13.575  22.882  1.00 43.76           C  
ANISOU  775  C   ALA A 105     5925   5609   5094   -224   -381    219       C  
ATOM    776  O   ALA A 105     -14.595 -13.842  22.326  1.00 50.45           O  
ANISOU  776  O   ALA A 105     6787   6419   5961   -243   -392    176       O  
ATOM    777  CB  ALA A 105     -16.203 -11.195  22.359  1.00 27.11           C  
ANISOU  777  CB  ALA A 105     3811   3481   3009   -224   -381    148       C  
ATOM    778  N   ILE A 106     -15.993 -14.070  24.078  1.00 47.18           N  
ANISOU  778  N   ILE A 106     6345   6103   5480   -168   -369    267       N  
ATOM    779  CA  ILE A 106     -15.085 -14.977  24.779  1.00 47.17           C  
ANISOU  779  CA  ILE A 106     6355   6121   5448   -120   -375    276       C  
ATOM    780  C   ILE A 106     -14.899 -16.261  23.981  1.00 47.69           C  
ANISOU  780  C   ILE A 106     6456   6105   5560   -168   -374    321       C  
ATOM    781  O   ILE A 106     -13.775 -16.750  23.810  1.00 55.53           O  
ANISOU  781  O   ILE A 106     7466   7074   6558   -146   -390    284       O  
ATOM    782  CB  ILE A 106     -15.599 -15.262  26.202  1.00 44.84           C  
ANISOU  782  CB  ILE A 106     6045   5914   5077    -42   -353    342       C  
ATOM    783  CG1 ILE A 106     -15.392 -14.045  27.103  1.00 41.57           C  
ANISOU  783  CG1 ILE A 106     5605   5588   4601     32   -368    258       C  
ATOM    784  CG2 ILE A 106     -14.892 -16.470  26.795  1.00 42.81           C  
ANISOU  784  CG2 ILE A 106     5814   5661   4790     10   -353    394       C  
ATOM    785  CD1 ILE A 106     -16.296 -14.030  28.318  1.00 40.57           C  
ANISOU  785  CD1 ILE A 106     5459   5566   4391    107   -335    320       C  
ATOM    786  N   TYR A 107     -15.995 -16.823  23.469  1.00 45.69           N  
ANISOU  786  N   TYR A 107     6208   5808   5343   -232   -357    390       N  
ATOM    787  CA  TYR A 107     -15.915 -18.047  22.683  1.00 44.28           C  
ANISOU  787  CA  TYR A 107     6071   5537   5218   -285   -361    416       C  
ATOM    788  C   TYR A 107     -15.883 -17.803  21.180  1.00 44.04           C  
ANISOU  788  C   TYR A 107     6052   5454   5228   -354   -383    354       C  
ATOM    789  O   TYR A 107     -15.400 -18.669  20.443  1.00 47.32           O  
ANISOU  789  O   TYR A 107     6508   5798   5673   -377   -395    332       O  
ATOM    790  CB  TYR A 107     -17.080 -18.990  23.028  1.00 42.22           C  
ANISOU  790  CB  TYR A 107     5807   5250   4983   -328   -334    523       C  
ATOM    791  CG  TYR A 107     -18.464 -18.501  22.645  1.00 45.37           C  
ANISOU  791  CG  TYR A 107     6155   5681   5404   -396   -328    548       C  
ATOM    792  CD1 TYR A 107     -18.955 -18.674  21.355  1.00 47.39           C  
ANISOU  792  CD1 TYR A 107     6411   5884   5713   -483   -356    517       C  
ATOM    793  CD2 TYR A 107     -19.291 -17.896  23.582  1.00 45.32           C  
ANISOU  793  CD2 TYR A 107     6094   5771   5356   -361   -296    598       C  
ATOM    794  CE1 TYR A 107     -20.219 -18.239  21.006  1.00 46.09           C  
ANISOU  794  CE1 TYR A 107     6186   5765   5562   -533   -360    538       C  
ATOM    795  CE2 TYR A 107     -20.559 -17.463  23.242  1.00 47.25           C  
ANISOU  795  CE2 TYR A 107     6277   6057   5618   -409   -291    621       C  
ATOM    796  CZ  TYR A 107     -21.016 -17.634  21.953  1.00 48.85           C  
ANISOU  796  CZ  TYR A 107     6474   6210   5878   -495   -326    592       C  
ATOM    797  OH  TYR A 107     -22.277 -17.201  21.611  1.00 51.69           O  
ANISOU  797  OH  TYR A 107     6760   6629   6251   -532   -330    613       O  
ATOM    798  N   TYR A 108     -16.374 -16.655  20.708  1.00 39.39           N  
ANISOU  798  N   TYR A 108     5435   4899   4632   -376   -389    326       N  
ATOM    799  CA  TYR A 108     -16.337 -16.377  19.274  1.00 39.14           C  
ANISOU  799  CA  TYR A 108     5420   4833   4619   -427   -406    281       C  
ATOM    800  C   TYR A 108     -14.910 -16.150  18.792  1.00 36.58           C  
ANISOU  800  C   TYR A 108     5118   4493   4289   -407   -406    210       C  
ATOM    801  O   TYR A 108     -14.524 -16.645  17.727  1.00 35.16           O  
ANISOU  801  O   TYR A 108     4968   4274   4118   -434   -412    178       O  
ATOM    802  CB  TYR A 108     -17.212 -15.167  18.946  1.00 42.02           C  
ANISOU  802  CB  TYR A 108     5755   5236   4973   -436   -409    286       C  
ATOM    803  CG  TYR A 108     -17.522 -15.009  17.473  1.00 39.36           C  
ANISOU  803  CG  TYR A 108     5435   4881   4641   -484   -430    268       C  
ATOM    804  CD1 TYR A 108     -18.639 -15.611  16.911  1.00 42.41           C  
ANISOU  804  CD1 TYR A 108     5804   5271   5041   -534   -456    296       C  
ATOM    805  CD2 TYR A 108     -16.699 -14.255  16.647  1.00 37.59           C  
ANISOU  805  CD2 TYR A 108     5237   4644   4402   -479   -424    224       C  
ATOM    806  CE1 TYR A 108     -18.927 -15.470  15.566  1.00 45.17           C  
ANISOU  806  CE1 TYR A 108     6166   5622   5374   -564   -486    271       C  
ATOM    807  CE2 TYR A 108     -16.978 -14.108  15.302  1.00 39.22           C  
ANISOU  807  CE2 TYR A 108     5463   4848   4590   -507   -439    218       C  
ATOM    808  CZ  TYR A 108     -18.093 -14.717  14.767  1.00 42.54           C  
ANISOU  808  CZ  TYR A 108     5871   5284   5009   -543   -476    237       C  
ATOM    809  OH  TYR A 108     -18.374 -14.572  13.428  1.00 41.05           O  
ANISOU  809  OH  TYR A 108     5700   5113   4784   -559   -502    223       O  
ATOM    810  N   VAL A 109     -14.114 -15.401  19.558  1.00 41.20           N  
ANISOU  810  N   VAL A 109     5680   5115   4856   -359   -398    176       N  
ATOM    811  CA  VAL A 109     -12.727 -15.156  19.172  1.00 42.33           C  
ANISOU  811  CA  VAL A 109     5821   5258   5003   -349   -393    108       C  
ATOM    812  C   VAL A 109     -11.925 -16.452  19.215  1.00 45.42           C  
ANISOU  812  C   VAL A 109     6230   5631   5397   -316   -398     99       C  
ATOM    813  O   VAL A 109     -11.040 -16.678  18.381  1.00 48.37           O  
ANISOU  813  O   VAL A 109     6609   5992   5777   -319   -390     53       O  
ATOM    814  CB  VAL A 109     -12.108 -14.068  20.069  1.00 37.04           C  
ANISOU  814  CB  VAL A 109     5111   4636   4326   -317   -393     60       C  
ATOM    815  CG1 VAL A 109     -10.633 -13.875  19.744  1.00 36.06           C  
ANISOU  815  CG1 VAL A 109     4960   4525   4217   -318   -387    -12       C  
ATOM    816  CG2 VAL A 109     -12.860 -12.757  19.908  1.00 36.53           C  
ANISOU  816  CG2 VAL A 109     5045   4564   4270   -342   -385     62       C  
ATOM    817  N   TYR A 110     -12.228 -17.327  20.176  1.00 46.50           N  
ANISOU  817  N   TYR A 110     6377   5764   5525   -275   -404    151       N  
ATOM    818  CA  TYR A 110     -11.512 -18.595  20.270  1.00 45.74           C  
ANISOU  818  CA  TYR A 110     6311   5632   5435   -227   -409    156       C  
ATOM    819  C   TYR A 110     -11.826 -19.492  19.079  1.00 42.19           C  
ANISOU  819  C   TYR A 110     5914   5095   5020   -275   -410    151       C  
ATOM    820  O   TYR A 110     -10.921 -20.086  18.482  1.00 44.21           O  
ANISOU  820  O   TYR A 110     6191   5323   5283   -245   -410    102       O  
ATOM    821  CB  TYR A 110     -11.852 -19.300  21.582  1.00 47.98           C  
ANISOU  821  CB  TYR A 110     6608   5924   5700   -169   -407    235       C  
ATOM    822  CG  TYR A 110     -11.064 -20.572  21.804  1.00 48.12           C  
ANISOU  822  CG  TYR A 110     6665   5895   5723    -97   -411    252       C  
ATOM    823  CD1 TYR A 110      -9.687 -20.598  21.620  1.00 47.21           C  
ANISOU  823  CD1 TYR A 110     6528   5813   5595    -31   -424    179       C  
ATOM    824  CD2 TYR A 110     -11.695 -21.746  22.194  1.00 48.03           C  
ANISOU  824  CD2 TYR A 110     6710   5803   5735    -91   -399    346       C  
ATOM    825  CE1 TYR A 110      -8.961 -21.756  21.820  1.00 49.80           C  
ANISOU  825  CE1 TYR A 110     6893   6101   5927     57   -430    195       C  
ATOM    826  CE2 TYR A 110     -10.977 -22.909  22.398  1.00 50.34           C  
ANISOU  826  CE2 TYR A 110     7054   6034   6039    -12   -401    369       C  
ATOM    827  CZ  TYR A 110      -9.611 -22.909  22.209  1.00 52.20           C  
ANISOU  827  CZ  TYR A 110     7272   6309   6255     72   -419    291       C  
ATOM    828  OH  TYR A 110      -8.893 -24.067  22.410  1.00 52.93           O  
ANISOU  828  OH  TYR A 110     7414   6340   6355    172   -423    315       O  
ATOM    829  N   ILE A 111     -13.108 -19.607  18.721  1.00 43.15           N  
ANISOU  829  N   ILE A 111     6050   5180   5163   -346   -414    192       N  
ATOM    830  CA  ILE A 111     -13.477 -20.371  17.532  1.00 41.83           C  
ANISOU  830  CA  ILE A 111     5928   4940   5026   -401   -429    166       C  
ATOM    831  C   ILE A 111     -12.858 -19.743  16.290  1.00 41.75           C  
ANISOU  831  C   ILE A 111     5917   4960   4988   -410   -428     88       C  
ATOM    832  O   ILE A 111     -12.422 -20.446  15.369  1.00 43.67           O  
ANISOU  832  O   ILE A 111     6200   5162   5232   -406   -434     33       O  
ATOM    833  CB  ILE A 111     -15.009 -20.475  17.416  1.00 36.49           C  
ANISOU  833  CB  ILE A 111     5242   4246   4376   -482   -442    216       C  
ATOM    834  CG1 ILE A 111     -15.580 -21.255  18.601  1.00 32.70           C  
ANISOU  834  CG1 ILE A 111     4764   3731   3928   -481   -426    307       C  
ATOM    835  CG2 ILE A 111     -15.406 -21.145  16.109  1.00 45.01           C  
ANISOU  835  CG2 ILE A 111     6358   5264   5479   -545   -472    164       C  
ATOM    836  CD1 ILE A 111     -17.090 -21.252  18.661  1.00 33.62           C  
ANISOU  836  CD1 ILE A 111     4842   3856   4075   -564   -428    365       C  
ATOM    837  N   GLU A 112     -12.799 -18.410  16.250  1.00 39.29           N  
ANISOU  837  N   GLU A 112     5562   4717   4650   -418   -415     84       N  
ATOM    838  CA  GLU A 112     -12.114 -17.729  15.158  1.00 41.46           C  
ANISOU  838  CA  GLU A 112     5834   5022   4896   -425   -397     33       C  
ATOM    839  C   GLU A 112     -10.633 -18.086  15.119  1.00 40.95           C  
ANISOU  839  C   GLU A 112     5761   4970   4827   -371   -376    -22       C  
ATOM    840  O   GLU A 112     -10.046 -18.187  14.035  1.00 41.70           O  
ANISOU  840  O   GLU A 112     5868   5076   4899   -369   -357    -68       O  
ATOM    841  CB  GLU A 112     -12.306 -16.219  15.294  1.00 39.14           C  
ANISOU  841  CB  GLU A 112     5504   4774   4593   -444   -381     51       C  
ATOM    842  CG  GLU A 112     -11.328 -15.377  14.497  1.00 43.21           C  
ANISOU  842  CG  GLU A 112     6007   5318   5092   -451   -344     16       C  
ATOM    843  CD  GLU A 112     -11.418 -13.909  14.851  1.00 49.96           C  
ANISOU  843  CD  GLU A 112     6835   6186   5960   -468   -326     34       C  
ATOM    844  OE1 GLU A 112     -12.488 -13.480  15.327  1.00 53.87           O  
ANISOU  844  OE1 GLU A 112     7332   6675   6460   -471   -346     74       O  
ATOM    845  OE2 GLU A 112     -10.420 -13.184  14.654  1.00 55.74           O  
ANISOU  845  OE2 GLU A 112     7541   6932   6704   -480   -290      7       O  
ATOM    846  N   SER A 113     -10.016 -18.293  16.286  1.00 39.52           N  
ANISOU  846  N   SER A 113     5552   4805   4659   -316   -378    -17       N  
ATOM    847  CA  SER A 113      -8.613 -18.694  16.317  1.00 40.54           C  
ANISOU  847  CA  SER A 113     5656   4963   4784   -250   -365    -69       C  
ATOM    848  C   SER A 113      -8.412 -20.080  15.717  1.00 39.83           C  
ANISOU  848  C   SER A 113     5625   4809   4699   -210   -370    -94       C  
ATOM    849  O   SER A 113      -7.326 -20.378  15.207  1.00 39.77           O  
ANISOU  849  O   SER A 113     5603   4829   4679   -158   -351   -152       O  
ATOM    850  CB  SER A 113      -8.083 -18.653  17.751  1.00 42.62           C  
ANISOU  850  CB  SER A 113     5875   5271   5048   -186   -380    -59       C  
ATOM    851  OG  SER A 113      -8.581 -19.738  18.514  1.00 48.73           O  
ANISOU  851  OG  SER A 113     6697   5992   5828   -141   -400     -2       O  
ATOM    852  N   TRP A 114      -9.436 -20.937  15.768  1.00 40.55           N  
ANISOU  852  N   TRP A 114     5780   4813   4814   -233   -395    -55       N  
ATOM    853  CA  TRP A 114      -9.335 -22.242  15.121  1.00 38.48           C  
ANISOU  853  CA  TRP A 114     5588   4463   4569   -205   -405    -93       C  
ATOM    854  C   TRP A 114      -9.215 -22.093  13.611  1.00 39.19           C  
ANISOU  854  C   TRP A 114     5695   4572   4624   -233   -396   -167       C  
ATOM    855  O   TRP A 114      -8.428 -22.800  12.971  1.00 44.54           O  
ANISOU  855  O   TRP A 114     6401   5234   5289   -172   -386   -236       O  
ATOM    856  CB  TRP A 114     -10.547 -23.109  15.465  1.00 37.35           C  
ANISOU  856  CB  TRP A 114     5503   4212   4475   -253   -432    -38       C  
ATOM    857  CG  TRP A 114     -10.816 -23.275  16.929  1.00 38.39           C  
ANISOU  857  CG  TRP A 114     5624   4334   4628   -227   -429     56       C  
ATOM    858  CD1 TRP A 114     -10.009 -22.902  17.964  1.00 39.10           C  
ANISOU  858  CD1 TRP A 114     5669   4497   4689   -146   -419     80       C  
ATOM    859  CD2 TRP A 114     -11.981 -23.862  17.520  1.00 44.09           C  
ANISOU  859  CD2 TRP A 114     6376   4980   5396   -281   -435    140       C  
ATOM    860  NE1 TRP A 114     -10.601 -23.218  19.162  1.00 43.76           N  
ANISOU  860  NE1 TRP A 114     6270   5070   5289   -134   -418    177       N  
ATOM    861  CE2 TRP A 114     -11.813 -23.808  18.917  1.00 45.00           C  
ANISOU  861  CE2 TRP A 114     6471   5133   5496   -219   -420    223       C  
ATOM    862  CE3 TRP A 114     -13.150 -24.428  17.002  1.00 50.40           C  
ANISOU  862  CE3 TRP A 114     7209   5694   6247   -380   -452    151       C  
ATOM    863  CZ2 TRP A 114     -12.769 -24.301  19.803  1.00 45.52           C  
ANISOU  863  CZ2 TRP A 114     6552   5153   5590   -249   -406    331       C  
ATOM    864  CZ3 TRP A 114     -14.099 -24.915  17.883  1.00 50.18           C  
ANISOU  864  CZ3 TRP A 114     7186   5615   6267   -425   -442    253       C  
ATOM    865  CH2 TRP A 114     -13.902 -24.849  19.268  1.00 45.83           C  
ANISOU  865  CH2 TRP A 114     6618   5102   5693   -357   -412    349       C  
ATOM    866  N   THR A 115      -9.996 -21.182  13.025  1.00 36.54           N  
ANISOU  866  N   THR A 115     5345   4277   4263   -311   -398   -153       N  
ATOM    867  CA  THR A 115      -9.920 -20.955  11.586  1.00 40.10           C  
ANISOU  867  CA  THR A 115     5813   4766   4657   -327   -388   -210       C  
ATOM    868  C   THR A 115      -8.562 -20.404  11.179  1.00 43.04           C  
ANISOU  868  C   THR A 115     6140   5224   4990   -278   -331   -246       C  
ATOM    869  O   THR A 115      -8.078 -20.696  10.080  1.00 44.49           O  
ANISOU  869  O   THR A 115     6346   5436   5122   -249   -309   -308       O  
ATOM    870  CB  THR A 115     -11.032 -20.002  11.144  1.00 35.99           C  
ANISOU  870  CB  THR A 115     5283   4281   4111   -403   -403   -169       C  
ATOM    871  OG1 THR A 115     -10.838 -18.722  11.759  1.00 36.78           O  
ANISOU  871  OG1 THR A 115     5324   4436   4213   -414   -372   -114       O  
ATOM    872  CG2 THR A 115     -12.391 -20.550  11.551  1.00 29.37           C  
ANISOU  872  CG2 THR A 115     4464   3378   3318   -458   -456   -136       C  
ATOM    873  N   LEU A 116      -7.933 -19.607  12.046  1.00 39.49           N  
ANISOU  873  N   LEU A 116     5621   4824   4561   -271   -306   -214       N  
ATOM    874  CA  LEU A 116      -6.589 -19.119  11.757  1.00 34.37           C  
ANISOU  874  CA  LEU A 116     4907   4259   3892   -238   -250   -249       C  
ATOM    875  C   LEU A 116      -5.572 -20.250  11.832  1.00 37.44           C  
ANISOU  875  C   LEU A 116     5294   4648   4285   -138   -246   -310       C  
ATOM    876  O   LEU A 116      -4.725 -20.397  10.943  1.00 40.61           O  
ANISOU  876  O   LEU A 116     5677   5107   4646    -97   -201   -364       O  
ATOM    877  CB  LEU A 116      -6.216 -17.996  12.725  1.00 33.79           C  
ANISOU  877  CB  LEU A 116     4753   4232   3853   -266   -237   -217       C  
ATOM    878  CG  LEU A 116      -4.781 -17.473  12.618  1.00 35.44           C  
ANISOU  878  CG  LEU A 116     4870   4532   4066   -251   -184   -257       C  
ATOM    879  CD1 LEU A 116      -4.537 -16.858  11.248  1.00 34.21           C  
ANISOU  879  CD1 LEU A 116     4712   4421   3867   -294   -117   -256       C  
ATOM    880  CD2 LEU A 116      -4.481 -16.469  13.722  1.00 31.95           C  
ANISOU  880  CD2 LEU A 116     4351   4120   3670   -284   -191   -246       C  
ATOM    881  N   GLY A 117      -5.645 -21.065  12.886  1.00 40.02           N  
ANISOU  881  N   GLY A 117     5639   4914   4652    -86   -286   -295       N  
ATOM    882  CA  GLY A 117      -4.708 -22.168  13.022  1.00 44.08           C  
ANISOU  882  CA  GLY A 117     6161   5416   5173     30   -286   -343       C  
ATOM    883  C   GLY A 117      -4.861 -23.203  11.926  1.00 45.72           C  
ANISOU  883  C   GLY A 117     6456   5555   5361     64   -288   -406       C  
ATOM    884  O   GLY A 117      -3.870 -23.738  11.421  1.00 50.60           O  
ANISOU  884  O   GLY A 117     7064   6206   5955    158   -260   -475       O  
ATOM    885  N   PHE A 118      -6.104 -23.502  11.541  1.00 42.47           N  
ANISOU  885  N   PHE A 118     6126   5052   4958     -7   -323   -394       N  
ATOM    886  CA  PHE A 118      -6.329 -24.442  10.448  1.00 39.59           C  
ANISOU  886  CA  PHE A 118     5848   4621   4573     13   -337   -476       C  
ATOM    887  C   PHE A 118      -5.833 -23.873   9.125  1.00 37.39           C  
ANISOU  887  C   PHE A 118     5544   4458   4205     18   -290   -538       C  
ATOM    888  O   PHE A 118      -5.290 -24.607   8.292  1.00 34.07           O  
ANISOU  888  O   PHE A 118     5162   4038   3744     96   -276   -630       O  
ATOM    889  CB  PHE A 118      -7.812 -24.800  10.359  1.00 41.18           C  
ANISOU  889  CB  PHE A 118     6121   4717   4809    -83   -393   -457       C  
ATOM    890  CG  PHE A 118      -8.208 -25.966  11.221  1.00 43.94           C  
ANISOU  890  CG  PHE A 118     6535   4913   5246    -67   -429   -429       C  
ATOM    891  CD1 PHE A 118      -7.933 -25.967  12.579  1.00 46.54           C  
ANISOU  891  CD1 PHE A 118     6835   5232   5618    -28   -422   -341       C  
ATOM    892  CD2 PHE A 118      -8.857 -27.060  10.673  1.00 46.57           C  
ANISOU  892  CD2 PHE A 118     6964   5112   5618    -91   -470   -490       C  
ATOM    893  CE1 PHE A 118      -8.298 -27.037  13.374  1.00 49.67           C  
ANISOU  893  CE1 PHE A 118     7299   5485   6089     -9   -443   -293       C  
ATOM    894  CE2 PHE A 118      -9.224 -28.133  11.462  1.00 50.61           C  
ANISOU  894  CE2 PHE A 118     7542   5461   6225    -88   -493   -451       C  
ATOM    895  CZ  PHE A 118      -8.944 -28.122  12.815  1.00 51.74           C  
ANISOU  895  CZ  PHE A 118     7659   5595   6405    -44   -474   -341       C  
ATOM    896  N   ALA A 119      -6.005 -22.565   8.916  1.00 37.75           N  
ANISOU  896  N   ALA A 119     5530   4598   4214    -57   -261   -484       N  
ATOM    897  CA  ALA A 119      -5.533 -21.947   7.681  1.00 37.85           C  
ANISOU  897  CA  ALA A 119     5520   4725   4136    -55   -202   -515       C  
ATOM    898  C   ALA A 119      -4.014 -22.001   7.581  1.00 42.47           C  
ANISOU  898  C   ALA A 119     6031   5402   4702     34   -132   -556       C  
ATOM    899  O   ALA A 119      -3.465 -22.184   6.487  1.00 48.56           O  
ANISOU  899  O   ALA A 119     6808   6247   5394     87    -84   -618       O  
ATOM    900  CB  ALA A 119      -6.026 -20.503   7.593  1.00 31.62           C  
ANISOU  900  CB  ALA A 119     4690   3996   3329   -151   -180   -429       C  
ATOM    901  N   ILE A 120      -3.318 -21.844   8.709  1.00 37.67           N  
ANISOU  901  N   ILE A 120     5346   4807   4158     59   -127   -527       N  
ATOM    902  CA  ILE A 120      -1.859 -21.901   8.698  1.00 35.52           C  
ANISOU  902  CA  ILE A 120     4979   4639   3877    144    -68   -570       C  
ATOM    903  C   ILE A 120      -1.385 -23.295   8.306  1.00 36.11           C  
ANISOU  903  C   ILE A 120     5110   4678   3933    280    -75   -662       C  
ATOM    904  O   ILE A 120      -0.562 -23.457   7.398  1.00 36.21           O  
ANISOU  904  O   ILE A 120     5093   4784   3881    351    -13   -726       O  
ATOM    905  CB  ILE A 120      -1.294 -21.480  10.067  1.00 38.37           C  
ANISOU  905  CB  ILE A 120     5242   5029   4309    146    -82   -531       C  
ATOM    906  CG1 ILE A 120      -1.609 -20.012  10.352  1.00 36.05           C  
ANISOU  906  CG1 ILE A 120     4889   4772   4035     17    -65   -462       C  
ATOM    907  CG2 ILE A 120       0.207 -21.720  10.122  1.00 40.29           C  
ANISOU  907  CG2 ILE A 120     5374   5387   4549    249    -36   -586       C  
ATOM    908  CD1 ILE A 120      -1.321 -19.599  11.779  1.00 32.72           C  
ANISOU  908  CD1 ILE A 120     4391   4363   3677     10   -102   -437       C  
ATOM    909  N   LYS A 121      -1.908 -24.324   8.978  1.00 33.94           N  
ANISOU  909  N   LYS A 121     4922   4261   3713    323   -146   -667       N  
ATOM    910  CA  LYS A 121      -1.455 -25.685   8.713  1.00 37.55           C  
ANISOU  910  CA  LYS A 121     5446   4650   4170    461   -157   -754       C  
ATOM    911  C   LYS A 121      -1.896 -26.174   7.339  1.00 42.74           C  
ANISOU  911  C   LYS A 121     6201   5279   4761    465   -154   -844       C  
ATOM    912  O   LYS A 121      -1.180 -26.957   6.704  1.00 46.50           O  
ANISOU  912  O   LYS A 121     6701   5769   5198    591   -129   -943       O  
ATOM    913  CB  LYS A 121      -1.960 -26.623   9.808  1.00 35.18           C  
ANISOU  913  CB  LYS A 121     5226   4185   3957    493   -226   -716       C  
ATOM    914  CG  LYS A 121      -1.649 -26.130  11.212  1.00 38.54           C  
ANISOU  914  CG  LYS A 121     5565   4651   4428    494   -239   -626       C  
ATOM    915  CD  LYS A 121      -2.249 -27.036  12.272  1.00 42.37           C  
ANISOU  915  CD  LYS A 121     6139   4977   4983    524   -296   -565       C  
ATOM    916  CE  LYS A 121      -1.588 -28.402  12.271  1.00 43.51           C  
ANISOU  916  CE  LYS A 121     6351   5030   5149    691   -304   -618       C  
ATOM    917  NZ  LYS A 121      -2.074 -29.250  13.393  1.00 43.73           N  
ANISOU  917  NZ  LYS A 121     6466   4902   5249    727   -348   -532       N  
ATOM    918  N   PHE A 122      -3.061 -25.728   6.861  1.00 42.08           N  
ANISOU  918  N   PHE A 122     6168   5165   4654    342   -184   -821       N  
ATOM    919  CA  PHE A 122      -3.495 -26.107   5.520  1.00 46.23           C  
ANISOU  919  CA  PHE A 122     6776   5692   5096    347   -192   -916       C  
ATOM    920  C   PHE A 122      -2.642 -25.429   4.455  1.00 43.10           C  
ANISOU  920  C   PHE A 122     6313   5483   4580    387   -101   -945       C  
ATOM    921  O   PHE A 122      -2.352 -26.025   3.411  1.00 47.53           O  
ANISOU  921  O   PHE A 122     6923   6080   5055    473    -82  -1054       O  
ATOM    922  CB  PHE A 122      -4.973 -25.765   5.325  1.00 46.84           C  
ANISOU  922  CB  PHE A 122     6909   5712   5176    210   -255   -879       C  
ATOM    923  CG  PHE A 122      -5.906 -26.897   5.651  1.00 49.67           C  
ANISOU  923  CG  PHE A 122     7372   5881   5619    185   -343   -919       C  
ATOM    924  CD1 PHE A 122      -6.261 -27.164   6.963  1.00 50.74           C  
ANISOU  924  CD1 PHE A 122     7509   5899   5871    151   -375   -835       C  
ATOM    925  CD2 PHE A 122      -6.430 -27.693   4.646  1.00 49.63           C  
ANISOU  925  CD2 PHE A 122     7464   5818   5576    192   -391  -1043       C  
ATOM    926  CE1 PHE A 122      -7.120 -28.204   7.268  1.00 53.15           C  
ANISOU  926  CE1 PHE A 122     7907   6022   6264    114   -441   -855       C  
ATOM    927  CE2 PHE A 122      -7.289 -28.735   4.943  1.00 51.52           C  
ANISOU  927  CE2 PHE A 122     7794   5868   5913    148   -469  -1084       C  
ATOM    928  CZ  PHE A 122      -7.635 -28.990   6.256  1.00 54.63           C  
ANISOU  928  CZ  PHE A 122     8187   6137   6435    104   -489   -982       C  
ATOM    929  N   LEU A 123      -2.236 -24.183   4.702  1.00 39.51           N  
ANISOU  929  N   LEU A 123     5746   5147   4118    325    -40   -848       N  
ATOM    930  CA  LEU A 123      -1.352 -23.489   3.770  1.00 42.80           C  
ANISOU  930  CA  LEU A 123     6086   5742   4435    351     65   -851       C  
ATOM    931  C   LEU A 123       0.006 -24.175   3.696  1.00 46.16           C  
ANISOU  931  C   LEU A 123     6451   6239   4847    498    123   -931       C  
ATOM    932  O   LEU A 123       0.488 -24.513   2.609  1.00 44.58           O  
ANISOU  932  O   LEU A 123     6265   6132   4542    587    179  -1012       O  
ATOM    933  CB  LEU A 123      -1.199 -22.027   4.191  1.00 40.50           C  
ANISOU  933  CB  LEU A 123     5689   5528   4171    239    117   -727       C  
ATOM    934  CG  LEU A 123      -0.041 -21.230   3.586  1.00 40.87           C  
ANISOU  934  CG  LEU A 123     5618   5750   4160    247    243   -702       C  
ATOM    935  CD1 LEU A 123      -0.265 -21.017   2.099  1.00 40.33           C  
ANISOU  935  CD1 LEU A 123     5603   5774   3945    257    299   -712       C  
ATOM    936  CD2 LEU A 123       0.137 -19.899   4.306  1.00 35.88           C  
ANISOU  936  CD2 LEU A 123     4883   5144   3604    126    276   -591       C  
ATOM    937  N   VAL A 124       0.634 -24.397   4.853  1.00 47.04           N  
ANISOU  937  N   VAL A 124     6494   6323   5057    540    108   -913       N  
ATOM    938  CA  VAL A 124       1.937 -25.052   4.877  1.00 47.97           C  
ANISOU  938  CA  VAL A 124     6540   6518   5169    696    155   -986       C  
ATOM    939  C   VAL A 124       1.823 -26.509   4.436  1.00 50.08           C  
ANISOU  939  C   VAL A 124     6937   6675   5415    837    113  -1108       C  
ATOM    940  O   VAL A 124       2.771 -27.071   3.869  1.00 58.76           O  
ANISOU  940  O   VAL A 124     8007   7860   6458    984    169  -1199       O  
ATOM    941  CB  VAL A 124       2.559 -24.919   6.280  1.00 43.93           C  
ANISOU  941  CB  VAL A 124     5922   6009   4760    713    133   -934       C  
ATOM    942  CG1 VAL A 124       3.960 -25.505   6.308  1.00 46.85           C  
ANISOU  942  CG1 VAL A 124     6191   6489   5121    883    180  -1005       C  
ATOM    943  CG2 VAL A 124       2.587 -23.462   6.705  1.00 37.59           C  
ANISOU  943  CG2 VAL A 124     5003   5292   3986    562    164   -833       C  
ATOM    944  N   GLY A 125       0.670 -27.136   4.658  1.00 47.52           N  
ANISOU  944  N   GLY A 125     6754   6162   5138    793     18  -1118       N  
ATOM    945  CA  GLY A 125       0.480 -28.516   4.252  1.00 48.98           C  
ANISOU  945  CA  GLY A 125     7076   6209   5324    905    -29  -1241       C  
ATOM    946  C   GLY A 125       0.686 -29.514   5.371  1.00 48.96           C  
ANISOU  946  C   GLY A 125     7117   6048   5439    999    -82  -1235       C  
ATOM    947  O   GLY A 125       1.196 -30.615   5.145  1.00 42.94           O  
ANISOU  947  O   GLY A 125     6419   5215   4680   1157    -85  -1338       O  
ATOM    948  N   LEU A 126       0.298 -29.138   6.587  1.00 49.47           N  
ANISOU  948  N   LEU A 126     7149   6054   5591    914   -122  -1114       N  
ATOM    949  CA  LEU A 126       0.406 -30.023   7.745  1.00 49.29           C  
ANISOU  949  CA  LEU A 126     7172   5884   5670    999   -171  -1077       C  
ATOM    950  C   LEU A 126      -0.985 -30.549   8.097  1.00 48.45           C  
ANISOU  950  C   LEU A 126     7206   5559   5643    891   -249  -1041       C  
ATOM    951  O   LEU A 126      -1.562 -30.252   9.144  1.00 49.13           O  
ANISOU  951  O   LEU A 126     7282   5592   5794    805   -282   -923       O  
ATOM    952  CB  LEU A 126       1.055 -29.290   8.915  1.00 49.64           C  
ANISOU  952  CB  LEU A 126     7075   6042   5745   1002   -158   -972       C  
ATOM    953  CG  LEU A 126       2.386 -28.588   8.625  1.00 48.02           C  
ANISOU  953  CG  LEU A 126     6697   6071   5477   1068    -80   -999       C  
ATOM    954  CD1 LEU A 126       2.680 -27.536   9.684  1.00 50.07           C  
ANISOU  954  CD1 LEU A 126     6815   6442   5768    992    -82   -900       C  
ATOM    955  CD2 LEU A 126       3.526 -29.593   8.530  1.00 44.06           C  
ANISOU  955  CD2 LEU A 126     6181   5593   4967   1291    -60  -1085       C  
ATOM    956  N   VAL A 127      -1.519 -31.341   7.178  1.00 50.39           N  
ANISOU  956  N   VAL A 127     7578   5687   5881    894   -277  -1151       N  
ATOM    957  CA  VAL A 127      -2.889 -31.840   7.261  1.00 48.77           C  
ANISOU  957  CA  VAL A 127     7494   5285   5751    768   -349  -1142       C  
ATOM    958  C   VAL A 127      -2.830 -33.360   7.260  1.00 52.14           C  
ANISOU  958  C   VAL A 127     8067   5488   6258    879   -384  -1228       C  
ATOM    959  O   VAL A 127      -1.793 -33.952   6.920  1.00 51.35           O  
ANISOU  959  O   VAL A 127     7979   5403   6127   1059   -352  -1320       O  
ATOM    960  CB  VAL A 127      -3.763 -31.292   6.109  1.00 46.36           C  
ANISOU  960  CB  VAL A 127     7204   5044   5368    638   -366  -1204       C  
ATOM    961  CG1 VAL A 127      -3.658 -29.773   6.046  1.00 46.61           C  
ANISOU  961  CG1 VAL A 127     7100   5291   5320    556   -318  -1115       C  
ATOM    962  CG2 VAL A 127      -3.356 -31.919   4.787  1.00 43.49           C  
ANISOU  962  CG2 VAL A 127     6906   4698   4918    743   -357  -1383       C  
ATOM    963  N   PRO A 128      -3.914 -34.029   7.659  1.00 55.78           N  
ANISOU  963  N   PRO A 128     8636   5729   6828    779   -444  -1199       N  
ATOM    964  CA  PRO A 128      -3.913 -35.496   7.675  1.00 63.11           C  
ANISOU  964  CA  PRO A 128     9719   6405   7856    869   -476  -1275       C  
ATOM    965  C   PRO A 128      -3.711 -36.087   6.288  1.00 72.99           C  
ANISOU  965  C   PRO A 128    11051   7635   9047    942   -487  -1488       C  
ATOM    966  O   PRO A 128      -3.949 -35.444   5.264  1.00 67.32           O  
ANISOU  966  O   PRO A 128    10291   7071   8218    878   -487  -1570       O  
ATOM    967  CB  PRO A 128      -5.300 -35.848   8.227  1.00 58.01           C  
ANISOU  967  CB  PRO A 128     9147   5558   7334    688   -532  -1197       C  
ATOM    968  CG  PRO A 128      -5.704 -34.654   9.003  1.00 52.05           C  
ANISOU  968  CG  PRO A 128     8266   4956   6555    570   -516  -1034       C  
ATOM    969  CD  PRO A 128      -5.139 -33.483   8.265  1.00 51.33           C  
ANISOU  969  CD  PRO A 128     8052   5132   6318    584   -479  -1077       C  
ATOM    970  N   GLU A 129      -3.278 -37.344   6.270  1.00 88.60           N  
ANISOU  970  N   GLU A 129    13154   9415  11095   1087   -498  -1575       N  
ATOM    971  CA  GLU A 129      -2.981 -38.056   5.026  1.00 98.20           C  
ANISOU  971  CA  GLU A 129    14463  10591  12257   1192   -509  -1797       C  
ATOM    972  C   GLU A 129      -3.876 -39.277   4.892  1.00107.14           C  
ANISOU  972  C   GLU A 129    15778  11401  13530   1127   -585  -1892       C  
ATOM    973  O   GLU A 129      -3.723 -40.240   5.669  1.00111.70           O  
ANISOU  973  O   GLU A 129    16458  11738  14244   1203   -590  -1842       O  
ATOM    974  CB  GLU A 129      -1.511 -38.472   4.982  1.00 98.06           C  
ANISOU  974  CB  GLU A 129    14430  10637  12192   1458   -449  -1853       C  
ATOM    975  N   PRO A 130      -4.827 -39.287   3.964  1.00111.49           N  
ANISOU  975  N   PRO A 130    16374  11929  14059    983   -646  -2022       N  
ATOM    976  CA  PRO A 130      -5.591 -40.508   3.694  1.00116.40           C  
ANISOU  976  CA  PRO A 130    17166  12243  14818    921   -723  -2154       C  
ATOM    977  C   PRO A 130      -5.046 -41.232   2.476  1.00119.27           C  
ANISOU  977  C   PRO A 130    17632  12579  15106   1079   -739  -2416       C  
ATOM    978  O   PRO A 130      -4.436 -40.610   1.592  1.00122.15           O  
ANISOU  978  O   PRO A 130    17920  13208  15284   1175   -702  -2505       O  
ATOM    979  CB  PRO A 130      -7.017 -39.987   3.440  1.00115.48           C  
ANISOU  979  CB  PRO A 130    17010  12152  14715    658   -792  -2143       C  
ATOM    980  CG  PRO A 130      -6.951 -38.470   3.634  1.00113.40           C  
ANISOU  980  CG  PRO A 130    16566  12204  14319    603   -744  -1989       C  
ATOM    981  CD  PRO A 130      -5.517 -38.100   3.443  1.00111.30           C  
ANISOU  981  CD  PRO A 130    16235  12131  13921    819   -659  -1998       C  
ATOM    982  N   PRO A 131      -5.240 -42.558   2.393  1.00111.46           N  
ANISOU  982  N   PRO A 131    16821  11270  14259   1115   -789  -2546       N  
ATOM    983  CA  PRO A 131      -4.828 -43.379   1.248  1.00106.28           C  
ANISOU  983  CA  PRO A 131    16287  10546  13548   1264   -817  -2824       C  
ATOM    984  C   PRO A 131      -5.815 -43.303   0.087  1.00104.09           C  
ANISOU  984  C   PRO A 131    16035  10309  13204   1108   -908  -3024       C  
ATOM    985  O   PRO A 131      -5.643 -44.035  -0.889  1.00105.84           O  
ANISOU  985  O   PRO A 131    16373  10459  13384   1210   -949  -3279       O  
ATOM    986  CB  PRO A 131      -4.786 -44.804   1.827  1.00106.73           C  
ANISOU  986  CB  PRO A 131    16533  10199  13823   1334   -839  -2853       C  
ATOM    987  CG  PRO A 131      -4.951 -44.646   3.319  1.00106.12           C  
ANISOU  987  CG  PRO A 131    16412  10028  13880   1261   -803  -2560       C  
ATOM    988  CD  PRO A 131      -5.727 -43.389   3.503  1.00107.53           C  
ANISOU  988  CD  PRO A 131    16424  10444  13989   1041   -807  -2418       C  
ATOM    989  N   THR A 135     -11.986 -47.853   0.217  1.00116.42           N  
ANISOU  989  N   THR A 135    17950  10460  15824    -74  -1275  -3335       N  
ATOM    990  CA  THR A 135     -12.049 -46.507   0.775  1.00113.87           C  
ANISOU  990  CA  THR A 135    17512  10361  15392    -97  -1279  -3151       C  
ATOM    991  C   THR A 135     -13.480 -46.179   1.199  1.00112.98           C  
ANISOU  991  C   THR A 135    17299  10232  15395   -401  -1332  -3046       C  
ATOM    992  O   THR A 135     -14.295 -45.716   0.398  1.00115.36           O  
ANISOU  992  O   THR A 135    17505  10719  15608   -540  -1412  -3164       O  
ATOM    993  CB  THR A 135     -11.539 -45.450  -0.232  1.00112.49           C  
ANISOU  993  CB  THR A 135    17262  10556  14924     36  -1305  -3272       C  
ATOM    994  OG1 THR A 135     -10.139 -45.649  -0.464  1.00114.09           O  
ANISOU  994  OG1 THR A 135    17532  10800  15016    328  -1235  -3330       O  
ATOM    995  CG2 THR A 135     -11.751 -44.036   0.303  1.00107.21           C  
ANISOU  995  CG2 THR A 135    16469  10115  14151    -22  -1308  -3084       C  
ATOM    996  N   ASP A 136     -13.784 -46.452   2.469  1.00108.38           N  
ANISOU  996  N   ASP A 136    16734   9438  15010   -497  -1283  -2816       N  
ATOM    997  CA  ASP A 136     -15.063 -46.119   3.075  1.00101.73           C  
ANISOU  997  CA  ASP A 136    15784   8584  14285   -771  -1308  -2671       C  
ATOM    998  C   ASP A 136     -15.039 -44.681   3.582  1.00 97.88           C  
ANISOU  998  C   ASP A 136    15186   8349  13657   -765  -1313  -2495       C  
ATOM    999  O   ASP A 136     -13.975 -44.166   3.942  1.00 97.45           O  
ANISOU  999  O   ASP A 136    15113   8440  13473   -557  -1226  -2377       O  
ATOM   1000  CB  ASP A 136     -15.369 -47.069   4.231  1.00 99.10           C  
ANISOU 1000  CB  ASP A 136    15517   7922  14214   -866  -1231  -2484       C  
ATOM   1001  N   PRO A 137     -16.192 -44.005   3.618  1.00 94.05           N  
ANISOU 1001  N   PRO A 137    14550   8013  13173   -985  -1357  -2435       N  
ATOM   1002  CA  PRO A 137     -16.196 -42.596   4.049  1.00 90.27           C  
ANISOU 1002  CA  PRO A 137    13894   7871  12533   -968  -1301  -2231       C  
ATOM   1003  C   PRO A 137     -15.648 -42.394   5.449  1.00 92.36           C  
ANISOU 1003  C   PRO A 137    14149   8102  12844   -887  -1177  -1941       C  
ATOM   1004  O   PRO A 137     -15.072 -41.336   5.737  1.00 93.13           O  
ANISOU 1004  O   PRO A 137    14147   8459  12779   -772  -1116  -1812       O  
ATOM   1005  CB  PRO A 137     -17.680 -42.208   3.963  1.00 88.84           C  
ANISOU 1005  CB  PRO A 137    13576   7772  12407  -1233  -1375  -2221       C  
ATOM   1006  CG  PRO A 137     -18.418 -43.502   4.050  1.00 91.79           C  
ANISOU 1006  CG  PRO A 137    14046   7793  13036  -1415  -1429  -2312       C  
ATOM   1007  CD  PRO A 137     -17.552 -44.496   3.336  1.00 94.45           C  
ANISOU 1007  CD  PRO A 137    14535   7982  13368  -1249  -1420  -2515       C  
ATOM   1008  N   ASP A 138     -15.801 -43.386   6.327  1.00 94.01           N  
ANISOU 1008  N   ASP A 138    14459   7994  13266   -943  -1140  -1835       N  
ATOM   1009  CA  ASP A 138     -15.276 -43.267   7.681  1.00 94.75           C  
ANISOU 1009  CA  ASP A 138    14553   8056  13391   -850  -1027  -1558       C  
ATOM   1010  C   ASP A 138     -13.754 -43.191   7.676  1.00 90.78           C  
ANISOU 1010  C   ASP A 138    14111   7624  12756   -556   -972  -1565       C  
ATOM   1011  O   ASP A 138     -13.160 -42.463   8.478  1.00 89.00           O  
ANISOU 1011  O   ASP A 138    13810   7569  12438   -444   -897  -1377       O  
ATOM   1012  CB  ASP A 138     -15.761 -44.444   8.530  1.00104.31           C  
ANISOU 1012  CB  ASP A 138    15879   8896  14857   -963   -996  -1446       C  
ATOM   1013  CG  ASP A 138     -15.271 -44.377   9.962  1.00108.90           C  
ANISOU 1013  CG  ASP A 138    16469   9449  15460   -860   -881  -1149       C  
ATOM   1014  OD1 ASP A 138     -14.075 -44.646  10.204  1.00110.87           O  
ANISOU 1014  OD1 ASP A 138    16810   9657  15657   -619   -836  -1124       O  
ATOM   1015  OD2 ASP A 138     -16.087 -44.053  10.849  1.00109.62           O  
ANISOU 1015  OD2 ASP A 138    16467   9572  15612  -1013   -838   -944       O  
ATOM   1016  N   SER A 139     -13.103 -43.926   6.771  1.00 88.53           N  
ANISOU 1016  N   SER A 139    13955   7222  12459   -423  -1011  -1793       N  
ATOM   1017  CA  SER A 139     -11.646 -43.925   6.713  1.00 83.29           C  
ANISOU 1017  CA  SER A 139    13340   6629  11676   -136   -957  -1814       C  
ATOM   1018  C   SER A 139     -11.073 -42.630   6.151  1.00 78.15           C  
ANISOU 1018  C   SER A 139    12542   6372  10778    -38   -942  -1843       C  
ATOM   1019  O   SER A 139      -9.861 -42.411   6.258  1.00 77.93           O  
ANISOU 1019  O   SER A 139    12507   6459  10642    185   -883  -1818       O  
ATOM   1020  CB  SER A 139     -11.153 -45.110   5.881  1.00 85.12           C  
ANISOU 1020  CB  SER A 139    13754   6621  11967    -15   -999  -2060       C  
ATOM   1021  OG  SER A 139     -11.792 -45.151   4.618  1.00 86.19           O  
ANISOU 1021  OG  SER A 139    13892   6795  12063   -129  -1098  -2318       O  
ATOM   1022  N   ILE A 140     -11.901 -41.777   5.556  1.00 76.96           N  
ANISOU 1022  N   ILE A 140    12273   6429  10540   -195   -992  -1889       N  
ATOM   1023  CA  ILE A 140     -11.448 -40.478   5.075  1.00 76.83           C  
ANISOU 1023  CA  ILE A 140    12119   6772  10300   -122   -970  -1885       C  
ATOM   1024  C   ILE A 140     -11.835 -39.410   6.090  1.00 74.85           C  
ANISOU 1024  C   ILE A 140    11723   6684  10033   -213   -921  -1635       C  
ATOM   1025  O   ILE A 140     -11.132 -38.408   6.259  1.00 75.18           O  
ANISOU 1025  O   ILE A 140    11665   6966   9935   -111   -865  -1547       O  
ATOM   1026  CB  ILE A 140     -12.039 -40.169   3.687  1.00 78.41           C  
ANISOU 1026  CB  ILE A 140    12291   7115  10387   -201  -1056  -2098       C  
ATOM   1027  N   LEU A 141     -12.956 -39.626   6.779  1.00 72.26           N  
ANISOU 1027  N   LEU A 141    11380   6223   9853   -407   -940  -1524       N  
ATOM   1028  CA  LEU A 141     -13.445 -38.646   7.742  1.00 63.43           C  
ANISOU 1028  CA  LEU A 141    10126   5255   8720   -497   -897  -1300       C  
ATOM   1029  C   LEU A 141     -12.781 -38.793   9.106  1.00 62.37           C  
ANISOU 1029  C   LEU A 141    10011   5051   8637   -390   -811  -1090       C  
ATOM   1030  O   LEU A 141     -12.678 -37.808   9.845  1.00 61.05           O  
ANISOU 1030  O   LEU A 141     9732   5072   8395   -376   -763   -929       O  
ATOM   1031  CB  LEU A 141     -14.963 -38.769   7.881  1.00 61.29           C  
ANISOU 1031  CB  LEU A 141     9809   4907   8572   -747   -948  -1270       C  
ATOM   1032  CG  LEU A 141     -15.812 -38.057   6.824  1.00 56.91           C  
ANISOU 1032  CG  LEU A 141     9154   4547   7921   -868  -1030  -1400       C  
ATOM   1033  CD1 LEU A 141     -17.204 -38.665   6.754  1.00 55.38           C  
ANISOU 1033  CD1 LEU A 141     8949   4204   7890  -1103  -1102  -1443       C  
ATOM   1034  CD2 LEU A 141     -15.893 -36.566   7.111  1.00 47.34           C  
ANISOU 1034  CD2 LEU A 141     7788   3632   6567   -860   -994  -1261       C  
ATOM   1035  N   ARG A 142     -12.333 -39.999   9.457  1.00 64.87           N  
ANISOU 1035  N   ARG A 142    10473   5100   9076   -306   -794  -1092       N  
ATOM   1036  CA  ARG A 142     -11.722 -40.209  10.769  1.00 66.39           C  
ANISOU 1036  CA  ARG A 142    10692   5225   9309   -189   -718   -885       C  
ATOM   1037  C   ARG A 142     -10.425 -39.432  10.958  1.00 68.35           C  
ANISOU 1037  C   ARG A 142    10868   5709   9393     24   -672   -849       C  
ATOM   1038  O   ARG A 142     -10.259 -38.811  12.023  1.00 70.81           O  
ANISOU 1038  O   ARG A 142    11100   6139   9668     52   -623   -662       O  
ATOM   1039  CB  ARG A 142     -11.512 -41.707  11.011  1.00 72.28           C  
ANISOU 1039  CB  ARG A 142    11623   5617  10223   -129   -712   -897       C  
ATOM   1040  CG  ARG A 142     -10.526 -42.014  12.124  1.00 80.59           C  
ANISOU 1040  CG  ARG A 142    12725   6618  11276     75   -642   -724       C  
ATOM   1041  CD  ARG A 142     -10.811 -43.357  12.771  1.00 89.96           C  
ANISOU 1041  CD  ARG A 142    14079   7437  12664     58   -620   -630       C  
ATOM   1042  NE  ARG A 142     -12.067 -43.355  13.517  1.00 94.96           N  
ANISOU 1042  NE  ARG A 142    14678   7990  13412   -173   -600   -459       N  
ATOM   1043  CZ  ARG A 142     -13.113 -44.117  13.217  1.00 98.66           C  
ANISOU 1043  CZ  ARG A 142    15216   8213  14058   -382   -630   -511       C  
ATOM   1044  NH1 ARG A 142     -13.053 -44.946  12.185  1.00 99.32           N  
ANISOU 1044  NH1 ARG A 142    15419   8095  14222   -386   -691   -741       N  
ATOM   1045  NH2 ARG A 142     -14.219 -44.054  13.947  1.00100.11           N  
ANISOU 1045  NH2 ARG A 142    15343   8355  14338   -589   -598   -340       N  
ATOM   1046  N   PRO A 143      -9.474 -39.419  10.012  1.00 67.88           N  
ANISOU 1046  N   PRO A 143    10825   5735   9231    177   -681  -1021       N  
ATOM   1047  CA  PRO A 143      -8.241 -38.648  10.249  1.00 60.74           C  
ANISOU 1047  CA  PRO A 143     9829   5066   8184    362   -631   -977       C  
ATOM   1048  C   PRO A 143      -8.485 -37.170  10.494  1.00 58.81           C  
ANISOU 1048  C   PRO A 143     9414   5103   7827    275   -613   -880       C  
ATOM   1049  O   PRO A 143      -7.744 -36.550  11.268  1.00 64.06           O  
ANISOU 1049  O   PRO A 143     9997   5917   8428    375   -569   -766       O  
ATOM   1050  CB  PRO A 143      -7.429 -38.879   8.967  1.00 61.71           C  
ANISOU 1050  CB  PRO A 143     9989   5240   8218    497   -644  -1199       C  
ATOM   1051  CG  PRO A 143      -7.937 -40.161   8.427  1.00 69.88           C  
ANISOU 1051  CG  PRO A 143    11188   5981   9381    458   -695  -1338       C  
ATOM   1052  CD  PRO A 143      -9.398 -40.178   8.749  1.00 71.80           C  
ANISOU 1052  CD  PRO A 143    11428   6115   9740    205   -733  -1263       C  
ATOM   1053  N   PHE A 144      -9.504 -36.583   9.864  1.00 53.34           N  
ANISOU 1053  N   PHE A 144     8668   4489   7111     97   -652   -928       N  
ATOM   1054  CA  PHE A 144      -9.784 -35.169  10.079  1.00 52.25           C  
ANISOU 1054  CA  PHE A 144     8381   4599   6875     21   -636   -837       C  
ATOM   1055  C   PHE A 144     -10.539 -34.930  11.380  1.00 50.14           C  
ANISOU 1055  C   PHE A 144     8070   4301   6681    -81   -617   -638       C  
ATOM   1056  O   PHE A 144     -10.426 -33.847  11.966  1.00 49.18           O  
ANISOU 1056  O   PHE A 144     7836   4365   6485    -80   -587   -532       O  
ATOM   1057  CB  PHE A 144     -10.568 -34.602   8.895  1.00 42.37           C  
ANISOU 1057  CB  PHE A 144     7087   3456   5556   -104   -686   -956       C  
ATOM   1058  CG  PHE A 144      -9.741 -34.427   7.654  1.00 42.68           C  
ANISOU 1058  CG  PHE A 144     7132   3619   5466      8   -685  -1122       C  
ATOM   1059  CD1 PHE A 144      -9.191 -33.196   7.340  1.00 46.86           C  
ANISOU 1059  CD1 PHE A 144     7550   4402   5852     51   -645  -1100       C  
ATOM   1060  CD2 PHE A 144      -9.507 -35.497   6.805  1.00 49.03           C  
ANISOU 1060  CD2 PHE A 144     8054   4283   6291     73   -719  -1300       C  
ATOM   1061  CE1 PHE A 144      -8.428 -33.032   6.198  1.00 45.33           C  
ANISOU 1061  CE1 PHE A 144     7356   4334   5532    154   -629  -1236       C  
ATOM   1062  CE2 PHE A 144      -8.744 -35.340   5.663  1.00 47.54           C  
ANISOU 1062  CE2 PHE A 144     7868   4229   5967    189   -709  -1453       C  
ATOM   1063  CZ  PHE A 144      -8.204 -34.106   5.359  1.00 43.92           C  
ANISOU 1063  CZ  PHE A 144     7292   4038   5360    229   -660  -1412       C  
ATOM   1064  N   LYS A 145     -11.309 -35.918  11.842  1.00 49.05           N  
ANISOU 1064  N   LYS A 145     8018   3931   6689   -169   -630   -587       N  
ATOM   1065  CA  LYS A 145     -11.939 -35.807  13.153  1.00 49.18           C  
ANISOU 1065  CA  LYS A 145     8000   3918   6769   -243   -595   -382       C  
ATOM   1066  C   LYS A 145     -10.894 -35.850  14.260  1.00 50.63           C  
ANISOU 1066  C   LYS A 145     8191   4126   6921    -65   -541   -252       C  
ATOM   1067  O   LYS A 145     -10.993 -35.110  15.246  1.00 52.59           O  
ANISOU 1067  O   LYS A 145     8354   4505   7122    -68   -508   -105       O  
ATOM   1068  CB  LYS A 145     -12.971 -36.920  13.333  1.00 55.47           C  
ANISOU 1068  CB  LYS A 145     8888   4450   7739   -387   -610   -353       C  
ATOM   1069  CG  LYS A 145     -13.644 -36.942  14.697  1.00 60.87           C  
ANISOU 1069  CG  LYS A 145     9544   5092   8492   -462   -558   -128       C  
ATOM   1070  CD  LYS A 145     -15.085 -37.420  14.592  1.00 67.62           C  
ANISOU 1070  CD  LYS A 145    10398   5806   9487   -693   -579   -115       C  
ATOM   1071  CE  LYS A 145     -15.662 -37.765  15.957  1.00 70.08           C  
ANISOU 1071  CE  LYS A 145    10714   6025   9888   -753   -509    119       C  
ATOM   1072  NZ  LYS A 145     -15.153 -39.069  16.466  1.00 72.55           N  
ANISOU 1072  NZ  LYS A 145    11189   6061  10316   -666   -472    190       N  
ATOM   1073  N   GLU A 146      -9.880 -36.707  14.111  1.00 51.79           N  
ANISOU 1073  N   GLU A 146     8437   4156   7084    104   -535   -311       N  
ATOM   1074  CA  GLU A 146      -8.771 -36.716  15.058  1.00 53.68           C  
ANISOU 1074  CA  GLU A 146     8669   4452   7274    300   -496   -207       C  
ATOM   1075  C   GLU A 146      -7.906 -35.472  14.913  1.00 59.69           C  
ANISOU 1075  C   GLU A 146     9288   5507   7883    382   -487   -246       C  
ATOM   1076  O   GLU A 146      -7.256 -35.053  15.878  1.00 63.47           O  
ANISOU 1076  O   GLU A 146     9705   6107   8305    488   -463   -139       O  
ATOM   1077  CB  GLU A 146      -7.927 -37.977  14.865  1.00 56.37           C  
ANISOU 1077  CB  GLU A 146     9150   4592   7675    473   -496   -270       C  
ATOM   1078  CG  GLU A 146      -8.680 -39.275  15.118  1.00 68.88           C  
ANISOU 1078  CG  GLU A 146    10891   5848   9431    401   -497   -217       C  
ATOM   1079  CD  GLU A 146      -8.020 -40.475  14.461  1.00 82.51           C  
ANISOU 1079  CD  GLU A 146    12771   7353  11228    540   -513   -352       C  
ATOM   1080  OE1 GLU A 146      -8.422 -41.618  14.767  1.00 86.91           O  
ANISOU 1080  OE1 GLU A 146    13475   7612  11936    516   -507   -299       O  
ATOM   1081  OE2 GLU A 146      -7.102 -40.275  13.639  1.00 86.18           O  
ANISOU 1081  OE2 GLU A 146    13209   7938  11598    674   -526   -510       O  
ATOM   1082  N   PHE A 147      -7.887 -34.869  13.722  1.00 61.91           N  
ANISOU 1082  N   PHE A 147     9518   5907   8098    332   -507   -395       N  
ATOM   1083  CA  PHE A 147      -7.116 -33.649  13.513  1.00 60.10           C  
ANISOU 1083  CA  PHE A 147     9154   5942   7738    385   -488   -425       C  
ATOM   1084  C   PHE A 147      -7.692 -32.493  14.322  1.00 57.54           C  
ANISOU 1084  C   PHE A 147     8720   5766   7378    281   -478   -298       C  
ATOM   1085  O   PHE A 147      -6.951 -31.744  14.970  1.00 61.29           O  
ANISOU 1085  O   PHE A 147     9101   6401   7784    358   -457   -245       O  
ATOM   1086  CB  PHE A 147      -7.083 -33.304  12.024  1.00 58.60           C  
ANISOU 1086  CB  PHE A 147     8949   5834   7483    348   -503   -593       C  
ATOM   1087  CG  PHE A 147      -6.254 -32.094  11.696  1.00 56.11           C  
ANISOU 1087  CG  PHE A 147     8503   5772   7044    394   -471   -620       C  
ATOM   1088  CD1 PHE A 147      -4.883 -32.201  11.533  1.00 57.35           C  
ANISOU 1088  CD1 PHE A 147     8628   6015   7147    567   -438   -678       C  
ATOM   1089  CD2 PHE A 147      -6.847 -30.851  11.544  1.00 54.37           C  
ANISOU 1089  CD2 PHE A 147     8189   5701   6769    265   -469   -585       C  
ATOM   1090  CE1 PHE A 147      -4.118 -31.091  11.228  1.00 58.11           C  
ANISOU 1090  CE1 PHE A 147     8595   6340   7145    590   -401   -697       C  
ATOM   1091  CE2 PHE A 147      -6.088 -29.738  11.240  1.00 54.86           C  
ANISOU 1091  CE2 PHE A 147     8139   5971   6734    294   -433   -601       C  
ATOM   1092  CZ  PHE A 147      -4.722 -29.858  11.081  1.00 57.72           C  
ANISOU 1092  CZ  PHE A 147     8463   6415   7051    447   -396   -656       C  
ATOM   1093  N   LEU A 148      -9.016 -32.331  14.293  1.00 51.69           N  
ANISOU 1093  N   LEU A 148     7982   4975   6684    107   -496   -259       N  
ATOM   1094  CA  LEU A 148      -9.646 -31.262  15.061  1.00 48.01           C  
ANISOU 1094  CA  LEU A 148     7415   4641   6184     18   -485   -145       C  
ATOM   1095  C   LEU A 148      -9.569 -31.536  16.558  1.00 47.39           C  
ANISOU 1095  C   LEU A 148     7345   4530   6131     78   -458     16       C  
ATOM   1096  O   LEU A 148      -9.357 -30.613  17.354  1.00 49.88           O  
ANISOU 1096  O   LEU A 148     7570   5004   6379    104   -442     88       O  
ATOM   1097  CB  LEU A 148     -11.100 -31.090  14.620  1.00 42.45           C  
ANISOU 1097  CB  LEU A 148     6704   3902   5525   -170   -511   -148       C  
ATOM   1098  CG  LEU A 148     -11.983 -30.193  15.491  1.00 40.06           C  
ANISOU 1098  CG  LEU A 148     6312   3699   5209   -263   -497    -20       C  
ATOM   1099  CD1 LEU A 148     -11.554 -28.737  15.381  1.00 33.46           C  
ANISOU 1099  CD1 LEU A 148     5369   3081   4264   -239   -487    -38       C  
ATOM   1100  CD2 LEU A 148     -13.449 -30.356  15.121  1.00 43.46           C  
ANISOU 1100  CD2 LEU A 148     6739   4065   5708   -438   -524    -18       C  
ATOM   1101  N   TYR A 149      -9.730 -32.799  16.960  1.00 46.22           N  
ANISOU 1101  N   TYR A 149     7310   4175   6077    106   -452     73       N  
ATOM   1102  CA  TYR A 149      -9.729 -33.129  18.381  1.00 48.87           C  
ANISOU 1102  CA  TYR A 149     7666   4477   6427    169   -420    247       C  
ATOM   1103  C   TYR A 149      -8.356 -32.923  19.008  1.00 49.47           C  
ANISOU 1103  C   TYR A 149     7705   4676   6415    371   -414    264       C  
ATOM   1104  O   TYR A 149      -8.263 -32.583  20.193  1.00 46.46           O  
ANISOU 1104  O   TYR A 149     7282   4389   5983    426   -397    389       O  
ATOM   1105  CB  TYR A 149     -10.201 -34.569  18.587  1.00 52.48           C  
ANISOU 1105  CB  TYR A 149     8265   4660   7016    150   -408    314       C  
ATOM   1106  CG  TYR A 149     -11.697 -34.750  18.441  1.00 54.95           C  
ANISOU 1106  CG  TYR A 149     8586   4866   7425    -66   -407    352       C  
ATOM   1107  CD1 TYR A 149     -12.515 -33.685  18.086  1.00 56.35           C  
ANISOU 1107  CD1 TYR A 149     8649   5200   7560   -208   -422    319       C  
ATOM   1108  CD2 TYR A 149     -12.290 -35.987  18.659  1.00 57.38           C  
ANISOU 1108  CD2 TYR A 149     9011   4916   7875   -128   -389    423       C  
ATOM   1109  CE1 TYR A 149     -13.880 -33.845  17.952  1.00 57.79           C  
ANISOU 1109  CE1 TYR A 149     8819   5309   7831   -399   -425    349       C  
ATOM   1110  CE2 TYR A 149     -13.656 -36.156  18.526  1.00 59.45           C  
ANISOU 1110  CE2 TYR A 149     9260   5093   8237   -341   -387    453       C  
ATOM   1111  CZ  TYR A 149     -14.445 -35.082  18.173  1.00 61.63           C  
ANISOU 1111  CZ  TYR A 149     9406   5552   8461   -472   -408    412       C  
ATOM   1112  OH  TYR A 149     -15.805 -35.243  18.040  1.00 68.89           O  
ANISOU 1112  OH  TYR A 149    10291   6407   9477   -676   -410    438       O  
ATOM   1113  N   SER A 150      -7.284 -33.123  18.237  1.00 53.86           N  
ANISOU 1113  N   SER A 150     8268   5250   6945    488   -428    135       N  
ATOM   1114  CA  SER A 150      -5.949 -32.835  18.750  1.00 54.86           C  
ANISOU 1114  CA  SER A 150     8328   5528   6988    673   -427    134       C  
ATOM   1115  C   SER A 150      -5.710 -31.337  18.875  1.00 57.15           C  
ANISOU 1115  C   SER A 150     8463   6071   7182    629   -429    108       C  
ATOM   1116  O   SER A 150      -4.943 -30.902  19.741  1.00 63.80           O  
ANISOU 1116  O   SER A 150     9228   7057   7957    738   -434    148       O  
ATOM   1117  CB  SER A 150      -4.889 -33.465  17.845  1.00 56.69           C  
ANISOU 1117  CB  SER A 150     8597   5720   7222    810   -433     -2       C  
ATOM   1118  OG  SER A 150      -5.141 -34.844  17.643  1.00 66.87           O  
ANISOU 1118  OG  SER A 150    10044   6749   8613    846   -434      2       O  
ATOM   1119  N   TYR A 151      -6.358 -30.538  18.026  1.00 54.37           N  
ANISOU 1119  N   TYR A 151     8065   5770   6823    475   -431     38       N  
ATOM   1120  CA  TYR A 151      -6.160 -29.092  18.055  1.00 49.56           C  
ANISOU 1120  CA  TYR A 151     7323   5371   6138    427   -429     12       C  
ATOM   1121  C   TYR A 151      -6.768 -28.482  19.312  1.00 50.90           C  
ANISOU 1121  C   TYR A 151     7448   5607   6283    386   -428    134       C  
ATOM   1122  O   TYR A 151      -6.078 -27.816  20.093  1.00 55.10           O  
ANISOU 1122  O   TYR A 151     7895   6289   6752    460   -433    149       O  
ATOM   1123  CB  TYR A 151      -6.764 -28.462  16.798  1.00 44.52           C  
ANISOU 1123  CB  TYR A 151     6666   4753   5496    287   -429    -77       C  
ATOM   1124  CG  TYR A 151      -6.439 -26.995  16.615  1.00 38.96           C  
ANISOU 1124  CG  TYR A 151     5840   4239   4723    243   -418   -112       C  
ATOM   1125  CD1 TYR A 151      -5.290 -26.597  15.943  1.00 35.81           C  
ANISOU 1125  CD1 TYR A 151     5376   3951   4279    306   -400   -206       C  
ATOM   1126  CD2 TYR A 151      -7.286 -26.009  17.105  1.00 37.45           C  
ANISOU 1126  CD2 TYR A 151     5599   4111   4520    139   -420    -50       C  
ATOM   1127  CE1 TYR A 151      -4.991 -25.259  15.770  1.00 33.20           C  
ANISOU 1127  CE1 TYR A 151     4938   3772   3903    251   -382   -228       C  
ATOM   1128  CE2 TYR A 151      -6.995 -24.669  16.937  1.00 35.37           C  
ANISOU 1128  CE2 TYR A 151     5238   3991   4209     98   -409    -82       C  
ATOM   1129  CZ  TYR A 151      -5.847 -24.300  16.270  1.00 35.89           C  
ANISOU 1129  CZ  TYR A 151     5247   4149   4241    147   -389   -167       C  
ATOM   1130  OH  TYR A 151      -5.553 -22.967  16.100  1.00 41.92           O  
ANISOU 1130  OH  TYR A 151     5919   5036   4974     92   -371   -190       O  
ATOM   1131  N   ILE A 152      -8.068 -28.701  19.527  1.00 48.91           N  
ANISOU 1131  N   ILE A 152     7246   5257   6080    270   -421    214       N  
ATOM   1132  CA  ILE A 152      -8.758 -28.107  20.669  1.00 51.41           C  
ANISOU 1132  CA  ILE A 152     7519   5648   6366    231   -410    328       C  
ATOM   1133  C   ILE A 152      -8.667 -28.961  21.924  1.00 54.24           C  
ANISOU 1133  C   ILE A 152     7935   5950   6724    336   -396    465       C  
ATOM   1134  O   ILE A 152      -9.110 -28.519  22.996  1.00 50.57           O  
ANISOU 1134  O   ILE A 152     7434   5568   6211    336   -383    565       O  
ATOM   1135  CB  ILE A 152     -10.234 -27.830  20.322  1.00 50.02           C  
ANISOU 1135  CB  ILE A 152     7344   5426   6235     57   -403    356       C  
ATOM   1136  CG1 ILE A 152     -10.944 -29.124  19.932  1.00 50.74           C  
ANISOU 1136  CG1 ILE A 152     7541   5308   6429     -5   -399    384       C  
ATOM   1137  CG2 ILE A 152     -10.326 -26.834  19.184  1.00 48.61           C  
ANISOU 1137  CG2 ILE A 152     7104   5331   6033    -27   -419    240       C  
ATOM   1138  CD1 ILE A 152     -12.372 -28.917  19.479  1.00 50.19           C  
ANISOU 1138  CD1 ILE A 152     7454   5204   6411   -182   -401    392       C  
ATOM   1139  N   GLY A 153      -8.114 -30.165  21.832  1.00 58.51           N  
ANISOU 1139  N   GLY A 153     8569   6352   7309    438   -396    476       N  
ATOM   1140  CA  GLY A 153      -7.854 -30.962  23.016  1.00 60.72           C  
ANISOU 1140  CA  GLY A 153     8910   6584   7576    570   -381    616       C  
ATOM   1141  C   GLY A 153      -9.046 -31.700  23.582  1.00 64.13           C  
ANISOU 1141  C   GLY A 153     9429   6862   8077    485   -340    772       C  
ATOM   1142  O   GLY A 153      -9.187 -31.791  24.809  1.00 68.44           O  
ANISOU 1142  O   GLY A 153     9980   7452   8570    551   -314    920       O  
ATOM   1143  N   VAL A 154      -9.906 -32.234  22.727  1.00 62.30           N  
ANISOU 1143  N   VAL A 154     9258   6457   7958    339   -331    742       N  
ATOM   1144  CA  VAL A 154     -11.046 -33.026  23.202  1.00 58.10           C  
ANISOU 1144  CA  VAL A 154     8801   5760   7516    237   -286    889       C  
ATOM   1145  C   VAL A 154     -10.525 -34.291  23.875  1.00 65.90           C  
ANISOU 1145  C   VAL A 154     9916   6582   8542    380   -261   1011       C  
ATOM   1146  O   VAL A 154      -9.649 -34.971  23.311  1.00 72.14           O  
ANISOU 1146  O   VAL A 154    10778   7265   9365    489   -286    928       O  
ATOM   1147  CB  VAL A 154     -11.977 -33.368  22.038  1.00 50.19           C  
ANISOU 1147  CB  VAL A 154     7827   4607   6635     49   -298    800       C  
ATOM   1148  CG1 VAL A 154     -13.257 -34.014  22.544  1.00 47.79           C  
ANISOU 1148  CG1 VAL A 154     7563   4160   6433    -93   -249    947       C  
ATOM   1149  CG2 VAL A 154     -12.293 -32.123  21.239  1.00 49.27           C  
ANISOU 1149  CG2 VAL A 154     7593   4660   6466    -52   -332    670       C  
ATOM   1150  N   PRO A 155     -11.011 -34.645  25.060  1.00 64.19           N  
ANISOU 1150  N   PRO A 155     9733   6341   8314    398   -207   1211       N  
ATOM   1151  CA  PRO A 155     -10.558 -35.882  25.699  1.00 66.69           C  
ANISOU 1151  CA  PRO A 155    10187   6483   8669    540   -176   1351       C  
ATOM   1152  C   PRO A 155     -11.211 -37.103  25.074  1.00 75.76           C  
ANISOU 1152  C   PRO A 155    11468   7312  10004    419   -151   1367       C  
ATOM   1153  O   PRO A 155     -12.336 -37.052  24.570  1.00 76.91           O  
ANISOU 1153  O   PRO A 155    11590   7387  10245    202   -138   1343       O  
ATOM   1154  CB  PRO A 155     -10.994 -35.714  27.162  1.00 62.99           C  
ANISOU 1154  CB  PRO A 155     9700   6122   8111    580   -117   1569       C  
ATOM   1155  CG  PRO A 155     -11.745 -34.398  27.238  1.00 60.21           C  
ANISOU 1155  CG  PRO A 155     9200   5991   7687    448   -118   1525       C  
ATOM   1156  CD  PRO A 155     -12.050 -33.966  25.847  1.00 61.35           C  
ANISOU 1156  CD  PRO A 155     9294   6107   7909    292   -163   1327       C  
ATOM   1157  N   LYS A 156     -10.480 -38.215  25.115  1.00 82.92           N  
ANISOU 1157  N   LYS A 156    12513   8025  10967    568   -149   1403       N  
ATOM   1158  CA  LYS A 156     -11.000 -39.478  24.607  1.00 88.51           C  
ANISOU 1158  CA  LYS A 156    13370   8394  11864    471   -125   1419       C  
ATOM   1159  C   LYS A 156     -12.188 -39.927  25.446  1.00 94.54           C  
ANISOU 1159  C   LYS A 156    14172   9039  12709    327    -41   1644       C  
ATOM   1160  O   LYS A 156     -12.017 -40.392  26.578  1.00 95.85           O  
ANISOU 1160  O   LYS A 156    14406   9174  12837    450     18   1861       O  
ATOM   1161  CB  LYS A 156      -9.908 -40.550  24.602  1.00 88.56           C  
ANISOU 1161  CB  LYS A 156    13526   8218  11907    694   -135   1426       C  
ATOM   1162  N   GLY A 157     -13.385 -39.783  24.909  1.00 99.33           N  
ANISOU 1162  N   GLY A 157    14728   9594  13419     73    -32   1600       N  
ATOM   1163  CA  GLY A 157     -14.600 -40.134  25.638  1.00104.64           C  
ANISOU 1163  CA  GLY A 157    15405  10177  14176    -94     56   1806       C  
ATOM   1164  C   GLY A 157     -15.187 -38.922  26.350  1.00105.31           C  
ANISOU 1164  C   GLY A 157    15323  10570  14119   -142     86   1881       C  
ATOM   1165  O   GLY A 157     -15.523 -37.929  25.705  1.00 98.26           O  
ANISOU 1165  O   GLY A 157    14300   9853  13183   -240     36   1725       O  
ATOM   1166  N   ASP A 158     -15.305 -39.011  27.673  1.00114.01           N  
ANISOU 1166  N   ASP A 158    16438  11738  15143    -60    168   2119       N  
ATOM   1167  CA  ASP A 158     -15.866 -37.935  28.482  1.00114.28           C  
ANISOU 1167  CA  ASP A 158    16327  12059  15033    -82    206   2202       C  
ATOM   1168  C   ASP A 158     -14.936 -37.646  29.649  1.00111.83           C  
ANISOU 1168  C   ASP A 158    16030  11934  14526    176    217   2319       C  
ATOM   1169  O   ASP A 158     -14.629 -38.542  30.443  1.00116.84           O  
ANISOU 1169  O   ASP A 158    16786  12448  15159    299    274   2513       O  
ATOM   1170  CB  ASP A 158     -17.267 -38.292  28.990  1.00117.90           C  
ANISOU 1170  CB  ASP A 158    16762  12445  15589   -282    312   2390       C  
ATOM   1171  CG  ASP A 158     -17.906 -37.165  29.788  1.00120.41           C  
ANISOU 1171  CG  ASP A 158    16925  13070  15754   -298    355   2462       C  
ATOM   1172  OD1 ASP A 158     -17.356 -36.042  29.803  1.00118.85           O  
ANISOU 1172  OD1 ASP A 158    16638  13124  15398   -187    291   2336       O  
ATOM   1173  OD2 ASP A 158     -18.966 -37.403  30.404  1.00123.12           O  
ANISOU 1173  OD2 ASP A 158    17235  13402  16143   -424    458   2644       O  
ATOM   1174  N   GLU A 159     -14.495 -36.395  29.743  1.00 98.84           N  
ANISOU 1174  N   GLU A 159    14260  10580  12717    257    160   2198       N  
ATOM   1175  CA  GLU A 159     -13.745 -35.863  30.869  1.00 82.03           C  
ANISOU 1175  CA  GLU A 159    12100   8685  10381    477    156   2275       C  
ATOM   1176  C   GLU A 159     -13.991 -34.365  30.895  1.00 69.72           C  
ANISOU 1176  C   GLU A 159    10375   7415   8700    435    120   2149       C  
ATOM   1177  O   GLU A 159     -14.142 -33.749  29.833  1.00 67.75           O  
ANISOU 1177  O   GLU A 159    10053   7180   8507    314     64   1956       O  
ATOM   1178  CB  GLU A 159     -12.243 -36.163  30.758  1.00 77.30           C  
ANISOU 1178  CB  GLU A 159    11565   8078   9727    706     82   2195       C  
ATOM   1179  N   PRO A 160     -14.046 -33.750  32.079  1.00 61.85           N  
ANISOU 1179  N   PRO A 160     9322   6647   7532    538    151   2252       N  
ATOM   1180  CA  PRO A 160     -14.430 -32.333  32.151  1.00 55.77           C  
ANISOU 1180  CA  PRO A 160     8404   6127   6661    488    126   2138       C  
ATOM   1181  C   PRO A 160     -13.359 -31.365  31.676  1.00 50.97           C  
ANISOU 1181  C   PRO A 160     7724   5666   5975    577     17   1913       C  
ATOM   1182  O   PRO A 160     -13.653 -30.169  31.543  1.00 51.40           O  
ANISOU 1182  O   PRO A 160     7667   5888   5975    519     -9   1795       O  
ATOM   1183  CB  PRO A 160     -14.715 -32.136  33.643  1.00 52.90           C  
ANISOU 1183  CB  PRO A 160     8024   5947   6129    601    195   2323       C  
ATOM   1184  CG  PRO A 160     -13.786 -33.096  34.307  1.00 51.85           C  
ANISOU 1184  CG  PRO A 160     8012   5749   5941    802    199   2456       C  
ATOM   1185  CD  PRO A 160     -13.728 -34.303  33.407  1.00 58.45           C  
ANISOU 1185  CD  PRO A 160     8966   6263   6981    723    206   2472       C  
ATOM   1186  N   ILE A 161     -12.143 -31.832  31.402  1.00 48.93           N  
ANISOU 1186  N   ILE A 161     7524   5350   5718    714    -42   1850       N  
ATOM   1187  CA  ILE A 161     -11.003 -30.961  31.141  1.00 47.77           C  
ANISOU 1187  CA  ILE A 161     7299   5368   5486    817   -135   1660       C  
ATOM   1188  C   ILE A 161     -10.546 -31.139  29.702  1.00 52.21           C  
ANISOU 1188  C   ILE A 161     7873   5790   6176    746   -184   1490       C  
ATOM   1189  O   ILE A 161     -10.354 -32.269  29.239  1.00 59.79           O  
ANISOU 1189  O   ILE A 161     8939   6536   7240    760   -173   1525       O  
ATOM   1190  CB  ILE A 161      -9.853 -31.242  32.120  1.00 47.37           C  
ANISOU 1190  CB  ILE A 161     7273   5429   5298   1065   -168   1719       C  
ATOM   1191  CG1 ILE A 161     -10.166 -30.569  33.447  1.00 45.64           C  
ANISOU 1191  CG1 ILE A 161     6997   5439   4903   1141   -148   1808       C  
ATOM   1192  CG2 ILE A 161      -8.529 -30.740  31.567  1.00 45.65           C  
ANISOU 1192  CG2 ILE A 161     6986   5307   5050   1159   -265   1518       C  
ATOM   1193  CD1 ILE A 161     -10.294 -29.063  33.311  1.00 42.08           C  
ANISOU 1193  CD1 ILE A 161     6410   5188   4392   1068   -193   1632       C  
ATOM   1194  N   LEU A 162     -10.360 -30.023  29.004  1.00 51.03           N  
ANISOU 1194  N   LEU A 162     7619   5759   6013    678   -235   1307       N  
ATOM   1195  CA  LEU A 162      -9.765 -30.026  27.677  1.00 51.81           C  
ANISOU 1195  CA  LEU A 162     7713   5779   6193    638   -281   1137       C  
ATOM   1196  C   LEU A 162      -8.261 -29.814  27.782  1.00 55.16           C  
ANISOU 1196  C   LEU A 162     8095   6324   6538    815   -341   1041       C  
ATOM   1197  O   LEU A 162      -7.775 -29.100  28.663  1.00 59.11           O  
ANISOU 1197  O   LEU A 162     8520   7024   6915    914   -369   1035       O  
ATOM   1198  CB  LEU A 162     -10.381 -28.934  26.802  1.00 49.48           C  
ANISOU 1198  CB  LEU A 162     7330   5543   5927    469   -295   1007       C  
ATOM   1199  CG  LEU A 162     -11.908 -28.863  26.770  1.00 49.87           C  
ANISOU 1199  CG  LEU A 162     7376   5538   6034    298   -245   1085       C  
ATOM   1200  CD1 LEU A 162     -12.368 -27.625  26.018  1.00 49.71           C  
ANISOU 1200  CD1 LEU A 162     7259   5615   6013    176   -269    956       C  
ATOM   1201  CD2 LEU A 162     -12.485 -30.121  26.144  1.00 51.65           C  
ANISOU 1201  CD2 LEU A 162     7703   5520   6403    204   -217   1137       C  
ATOM   1202  N   LYS A 163      -7.522 -30.441  26.867  1.00 57.65           N  
ANISOU 1202  N   LYS A 163     8453   6527   6924    856   -364    955       N  
ATOM   1203  CA  LYS A 163      -6.067 -30.325  26.799  1.00 61.67           C  
ANISOU 1203  CA  LYS A 163     8908   7147   7375   1018   -416    853       C  
ATOM   1204  C   LYS A 163      -5.677 -29.784  25.427  1.00 58.69           C  
ANISOU 1204  C   LYS A 163     8470   6781   7050    930   -438    666       C  
ATOM   1205  O   LYS A 163      -5.144 -30.520  24.585  1.00 56.14           O  
ANISOU 1205  O   LYS A 163     8199   6343   6790    976   -441    603       O  
ATOM   1206  CB  LYS A 163      -5.390 -31.667  27.067  1.00 64.80           C  
ANISOU 1206  CB  LYS A 163     9412   7417   7791   1198   -415    936       C  
ATOM   1207  CG  LYS A 163      -5.759 -32.294  28.402  1.00 68.14           C  
ANISOU 1207  CG  LYS A 163     9914   7818   8160   1297   -383   1147       C  
ATOM   1208  N   PRO A 164      -5.920 -28.499  25.174  1.00 54.90           N  
ANISOU 1208  N   PRO A 164     7885   6435   6541    815   -448    579       N  
ATOM   1209  CA  PRO A 164      -5.647 -27.944  23.844  1.00 53.71           C  
ANISOU 1209  CA  PRO A 164     7683   6292   6432    723   -455    425       C  
ATOM   1210  C   PRO A 164      -4.161 -27.965  23.522  1.00 56.21           C  
ANISOU 1210  C   PRO A 164     7936   6700   6722    855   -484    319       C  
ATOM   1211  O   PRO A 164      -3.300 -27.974  24.404  1.00 59.95           O  
ANISOU 1211  O   PRO A 164     8357   7294   7126   1002   -514    336       O  
ATOM   1212  CB  PRO A 164      -6.173 -26.509  23.943  1.00 48.52           C  
ANISOU 1212  CB  PRO A 164     6929   5768   5736    600   -458    386       C  
ATOM   1213  CG  PRO A 164      -6.081 -26.183  25.395  1.00 49.45           C  
ANISOU 1213  CG  PRO A 164     7009   6016   5763    690   -474    461       C  
ATOM   1214  CD  PRO A 164      -6.375 -27.467  26.121  1.00 51.17           C  
ANISOU 1214  CD  PRO A 164     7337   6120   5985    782   -452    614       C  
ATOM   1215  N   SER A 165      -3.871 -27.980  22.225  1.00 52.92           N  
ANISOU 1215  N   SER A 165     7515   6239   6353    806   -474    207       N  
ATOM   1216  CA  SER A 165      -2.490 -28.020  21.771  1.00 51.48           C  
ANISOU 1216  CA  SER A 165     7261   6149   6151    923   -486    102       C  
ATOM   1217  C   SER A 165      -1.805 -26.683  22.023  1.00 48.37           C  
ANISOU 1217  C   SER A 165     6706   5974   5699    900   -505     27       C  
ATOM   1218  O   SER A 165      -2.450 -25.635  22.116  1.00 49.38           O  
ANISOU 1218  O   SER A 165     6791   6153   5818    766   -502     24       O  
ATOM   1219  CB  SER A 165      -2.424 -28.373  20.285  1.00 54.01           C  
ANISOU 1219  CB  SER A 165     7622   6375   6524    875   -461      3       C  
ATOM   1220  OG  SER A 165      -3.059 -27.382  19.494  1.00 55.80           O  
ANISOU 1220  OG  SER A 165     7811   6634   6757    701   -443    -50       O  
ATOM   1221  N   LEU A 166      -0.476 -26.731  22.146  1.00 49.51           N  
ANISOU 1221  N   LEU A 166     6756   6245   5811   1036   -527    -38       N  
ATOM   1222  CA  LEU A 166       0.293 -25.502  22.311  1.00 51.79           C  
ANISOU 1222  CA  LEU A 166     6878   6737   6064   1003   -546   -127       C  
ATOM   1223  C   LEU A 166       0.141 -24.598  21.095  1.00 57.12           C  
ANISOU 1223  C   LEU A 166     7508   7418   6777    837   -502   -211       C  
ATOM   1224  O   LEU A 166       0.105 -23.368  21.225  1.00 59.86           O  
ANISOU 1224  O   LEU A 166     7765   7862   7118    728   -505   -249       O  
ATOM   1225  CB  LEU A 166       1.764 -25.834  22.557  1.00 46.82           C  
ANISOU 1225  CB  LEU A 166     6140   6246   5402   1178   -576   -187       C  
ATOM   1226  CG  LEU A 166       2.725 -24.646  22.644  1.00 44.95           C  
ANISOU 1226  CG  LEU A 166     5709   6223   5146   1138   -597   -297       C  
ATOM   1227  CD1 LEU A 166       2.469 -23.835  23.905  1.00 42.22           C  
ANISOU 1227  CD1 LEU A 166     5311   5982   4749   1112   -652   -278       C  
ATOM   1228  CD2 LEU A 166       4.173 -25.112  22.582  1.00 45.26           C  
ANISOU 1228  CD2 LEU A 166     5632   6396   5170   1306   -615   -367       C  
ATOM   1229  N   PHE A 167       0.043 -25.193  19.904  1.00 55.94           N  
ANISOU 1229  N   PHE A 167     7427   7163   6664    821   -462   -241       N  
ATOM   1230  CA  PHE A 167      -0.170 -24.406  18.695  1.00 49.70           C  
ANISOU 1230  CA  PHE A 167     6611   6380   5893    677   -416   -304       C  
ATOM   1231  C   PHE A 167      -1.499 -23.663  18.751  1.00 48.59           C  
ANISOU 1231  C   PHE A 167     6521   6177   5764    517   -414   -250       C  
ATOM   1232  O   PHE A 167      -1.582 -22.495  18.353  1.00 51.97           O  
ANISOU 1232  O   PHE A 167     6883   6669   6193    401   -394   -283       O  
ATOM   1233  CB  PHE A 167      -0.107 -25.314  17.467  1.00 47.41           C  
ANISOU 1233  CB  PHE A 167     6403   5991   5621    712   -381   -348       C  
ATOM   1234  CG  PHE A 167      -0.290 -24.589  16.165  1.00 46.24           C  
ANISOU 1234  CG  PHE A 167     6235   5865   5468    587   -332   -406       C  
ATOM   1235  CD1 PHE A 167       0.705 -23.763  15.671  1.00 49.04           C  
ANISOU 1235  CD1 PHE A 167     6455   6374   5805    570   -292   -472       C  
ATOM   1236  CD2 PHE A 167      -1.454 -24.741  15.431  1.00 47.71           C  
ANISOU 1236  CD2 PHE A 167     6533   5926   5667    487   -325   -389       C  
ATOM   1237  CE1 PHE A 167       0.542 -23.097  14.471  1.00 49.69           C  
ANISOU 1237  CE1 PHE A 167     6527   6479   5873    463   -236   -505       C  
ATOM   1238  CE2 PHE A 167      -1.624 -24.078  14.230  1.00 49.98           C  
ANISOU 1238  CE2 PHE A 167     6809   6249   5933    389   -283   -434       C  
ATOM   1239  CZ  PHE A 167      -0.624 -23.255  13.749  1.00 50.00           C  
ANISOU 1239  CZ  PHE A 167     6689   6399   5909    381   -234   -484       C  
ATOM   1240  N   ALA A 168      -2.547 -24.320  19.252  1.00 45.45           N  
ANISOU 1240  N   ALA A 168     6236   5653   5380    512   -431   -162       N  
ATOM   1241  CA  ALA A 168      -3.848 -23.668  19.362  1.00 41.55           C  
ANISOU 1241  CA  ALA A 168     5776   5114   4895    374   -429   -109       C  
ATOM   1242  C   ALA A 168      -3.807 -22.509  20.350  1.00 46.19           C  
ANISOU 1242  C   ALA A 168     6275   5825   5451    347   -449   -100       C  
ATOM   1243  O   ALA A 168      -4.390 -21.448  20.096  1.00 47.71           O  
ANISOU 1243  O   ALA A 168     6442   6036   5649    230   -437   -111       O  
ATOM   1244  CB  ALA A 168      -4.912 -24.684  19.773  1.00 38.24           C  
ANISOU 1244  CB  ALA A 168     5479   4548   4505    376   -436    -11       C  
ATOM   1245  N   TYR A 169      -3.123 -22.692  21.482  1.00 45.38           N  
ANISOU 1245  N   TYR A 169     6126   5805   5310    463   -483    -87       N  
ATOM   1246  CA  TYR A 169      -3.023 -21.620  22.468  1.00 45.78           C  
ANISOU 1246  CA  TYR A 169     6091   5980   5322    448   -512   -103       C  
ATOM   1247  C   TYR A 169      -2.197 -20.457  21.935  1.00 45.88           C  
ANISOU 1247  C   TYR A 169     5984   6096   5352    378   -505   -213       C  
ATOM   1248  O   TYR A 169      -2.521 -19.291  22.188  1.00 48.31           O  
ANISOU 1248  O   TYR A 169     6250   6443   5663    287   -509   -239       O  
ATOM   1249  CB  TYR A 169      -2.418 -22.158  23.764  1.00 50.58           C  
ANISOU 1249  CB  TYR A 169     6677   6673   5869    605   -559    -70       C  
ATOM   1250  CG  TYR A 169      -2.463 -21.188  24.923  1.00 51.78           C  
ANISOU 1250  CG  TYR A 169     6759   6953   5963    605   -600    -88       C  
ATOM   1251  CD1 TYR A 169      -3.555 -21.148  25.780  1.00 56.28           C  
ANISOU 1251  CD1 TYR A 169     7394   7499   6492    598   -599      2       C  
ATOM   1252  CD2 TYR A 169      -1.408 -20.316  25.167  1.00 49.82           C  
ANISOU 1252  CD2 TYR A 169     6374   6854   5701    612   -638   -204       C  
ATOM   1253  CE1 TYR A 169      -3.599 -20.266  26.842  1.00 58.14           C  
ANISOU 1253  CE1 TYR A 169     7571   7859   6662    613   -637    -29       C  
ATOM   1254  CE2 TYR A 169      -1.443 -19.430  26.226  1.00 52.82           C  
ANISOU 1254  CE2 TYR A 169     6696   7346   6029    613   -684   -243       C  
ATOM   1255  CZ  TYR A 169      -2.540 -19.409  27.060  1.00 57.56           C  
ANISOU 1255  CZ  TYR A 169     7373   7922   6576    621   -685   -159       C  
ATOM   1256  OH  TYR A 169      -2.577 -18.528  28.115  1.00 61.62           O  
ANISOU 1256  OH  TYR A 169     7833   8555   7025    636   -732   -213       O  
ATOM   1257  N   ILE A 170      -1.126 -20.754  21.198  1.00 41.35           N  
ANISOU 1257  N   ILE A 170     5354   5563   4796    420   -488   -277       N  
ATOM   1258  CA  ILE A 170      -0.303 -19.695  20.621  1.00 41.97           C  
ANISOU 1258  CA  ILE A 170     5311   5737   4901    340   -465   -370       C  
ATOM   1259  C   ILE A 170      -1.073 -18.957  19.533  1.00 42.91           C  
ANISOU 1259  C   ILE A 170     5474   5775   5054    190   -411   -361       C  
ATOM   1260  O   ILE A 170      -1.070 -17.722  19.476  1.00 39.57           O  
ANISOU 1260  O   ILE A 170     4993   5387   4656     84   -398   -393       O  
ATOM   1261  CB  ILE A 170       1.018 -20.277  20.087  1.00 42.61           C  
ANISOU 1261  CB  ILE A 170     5310   5896   4985    433   -449   -432       C  
ATOM   1262  CG1 ILE A 170       1.941 -20.653  21.246  1.00 43.70           C  
ANISOU 1262  CG1 ILE A 170     5361   6158   5085    579   -514   -456       C  
ATOM   1263  CG2 ILE A 170       1.703 -19.287  19.157  1.00 44.43           C  
ANISOU 1263  CG2 ILE A 170     5431   6198   5253    323   -394   -505       C  
ATOM   1264  CD1 ILE A 170       3.268 -21.225  20.802  1.00 49.54           C  
ANISOU 1264  CD1 ILE A 170     6002   6995   5826    691   -502   -520       C  
ATOM   1265  N   VAL A 171      -1.748 -19.704  18.654  1.00 42.42           N  
ANISOU 1265  N   VAL A 171     5521   5603   4995    182   -382   -320       N  
ATOM   1266  CA  VAL A 171      -2.534 -19.080  17.592  1.00 41.88           C  
ANISOU 1266  CA  VAL A 171     5499   5473   4941     58   -340   -306       C  
ATOM   1267  C   VAL A 171      -3.648 -18.224  18.179  1.00 43.67           C  
ANISOU 1267  C   VAL A 171     5756   5665   5174    -24   -359   -259       C  
ATOM   1268  O   VAL A 171      -3.988 -17.169  17.629  1.00 47.51           O  
ANISOU 1268  O   VAL A 171     6232   6144   5676   -124   -331   -261       O  
ATOM   1269  CB  VAL A 171      -3.082 -20.158  16.634  1.00 42.10           C  
ANISOU 1269  CB  VAL A 171     5637   5399   4962     78   -324   -288       C  
ATOM   1270  CG1 VAL A 171      -4.203 -19.602  15.769  1.00 34.22           C  
ANISOU 1270  CG1 VAL A 171     4700   4339   3964    -37   -305   -259       C  
ATOM   1271  CG2 VAL A 171      -1.964 -20.699  15.758  1.00 30.35           C  
ANISOU 1271  CG2 VAL A 171     4113   3957   3461    147   -288   -354       C  
ATOM   1272  N   PHE A 172      -4.217 -18.644  19.312  1.00 42.58           N  
ANISOU 1272  N   PHE A 172     5652   5506   5018     27   -401   -209       N  
ATOM   1273  CA  PHE A 172      -5.238 -17.830  19.963  1.00 39.79           C  
ANISOU 1273  CA  PHE A 172     5316   5141   4662    -32   -415   -171       C  
ATOM   1274  C   PHE A 172      -4.660 -16.504  20.444  1.00 44.52           C  
ANISOU 1274  C   PHE A 172     5822   5823   5270    -70   -424   -236       C  
ATOM   1275  O   PHE A 172      -5.336 -15.470  20.395  1.00 46.89           O  
ANISOU 1275  O   PHE A 172     6131   6099   5587   -148   -415   -232       O  
ATOM   1276  CB  PHE A 172      -5.865 -18.592  21.128  1.00 34.84           C  
ANISOU 1276  CB  PHE A 172     4737   4498   4004     42   -447    -99       C  
ATOM   1277  CG  PHE A 172      -6.835 -17.772  21.923  1.00 39.15           C  
ANISOU 1277  CG  PHE A 172     5286   5058   4532      4   -457    -66       C  
ATOM   1278  CD1 PHE A 172      -8.035 -17.368  21.363  1.00 43.74           C  
ANISOU 1278  CD1 PHE A 172     5912   5575   5134    -83   -435    -27       C  
ATOM   1279  CD2 PHE A 172      -6.542 -17.389  23.220  1.00 43.39           C  
ANISOU 1279  CD2 PHE A 172     5776   5686   5023     68   -491    -84       C  
ATOM   1280  CE1 PHE A 172      -8.930 -16.607  22.084  1.00 46.08           C  
ANISOU 1280  CE1 PHE A 172     6205   5892   5413   -102   -440      0       C  
ATOM   1281  CE2 PHE A 172      -7.434 -16.626  23.947  1.00 45.52           C  
ANISOU 1281  CE2 PHE A 172     6051   5977   5268     47   -496    -65       C  
ATOM   1282  CZ  PHE A 172      -8.629 -16.234  23.377  1.00 44.89           C  
ANISOU 1282  CZ  PHE A 172     6014   5826   5215    -36   -467    -22       C  
ATOM   1283  N   LEU A 173      -3.413 -16.517  20.921  1.00 46.39           N  
ANISOU 1283  N   LEU A 173     5968   6157   5502    -12   -446   -303       N  
ATOM   1284  CA  LEU A 173      -2.748 -15.269  21.283  1.00 47.13           C  
ANISOU 1284  CA  LEU A 173     5961   6325   5622    -67   -458   -386       C  
ATOM   1285  C   LEU A 173      -2.545 -14.386  20.059  1.00 44.96           C  
ANISOU 1285  C   LEU A 173     5664   6014   5406   -188   -397   -408       C  
ATOM   1286  O   LEU A 173      -2.724 -13.164  20.128  1.00 45.27           O  
ANISOU 1286  O   LEU A 173     5684   6034   5484   -277   -389   -435       O  
ATOM   1287  CB  LEU A 173      -1.409 -15.561  21.960  1.00 51.16           C  
ANISOU 1287  CB  LEU A 173     6358   6963   6116     19   -500   -461       C  
ATOM   1288  CG  LEU A 173      -1.410 -15.662  23.486  1.00 54.55           C  
ANISOU 1288  CG  LEU A 173     6768   7475   6484    115   -575   -475       C  
ATOM   1289  CD1 LEU A 173      -0.105 -16.266  23.980  1.00 51.80           C  
ANISOU 1289  CD1 LEU A 173     6318   7259   6106    231   -621   -531       C  
ATOM   1290  CD2 LEU A 173      -1.645 -14.297  24.112  1.00 55.95           C  
ANISOU 1290  CD2 LEU A 173     6908   7675   6676     38   -601   -543       C  
ATOM   1291  N   ILE A 174      -2.170 -14.989  18.929  1.00 43.87           N  
ANISOU 1291  N   ILE A 174     5536   5864   5271   -186   -349   -395       N  
ATOM   1292  CA  ILE A 174      -2.017 -14.228  17.692  1.00 43.34           C  
ANISOU 1292  CA  ILE A 174     5457   5770   5238   -289   -278   -394       C  
ATOM   1293  C   ILE A 174      -3.359 -13.660  17.250  1.00 43.58           C  
ANISOU 1293  C   ILE A 174     5590   5700   5269   -358   -263   -326       C  
ATOM   1294  O   ILE A 174      -3.439 -12.528  16.757  1.00 47.07           O  
ANISOU 1294  O   ILE A 174     6026   6111   5748   -450   -223   -319       O  
ATOM   1295  CB  ILE A 174      -1.387 -15.111  16.599  1.00 43.43           C  
ANISOU 1295  CB  ILE A 174     5465   5808   5228   -248   -231   -396       C  
ATOM   1296  CG1 ILE A 174      -0.097 -15.754  17.112  1.00 40.36           C  
ANISOU 1296  CG1 ILE A 174     4970   5529   4836   -153   -252   -462       C  
ATOM   1297  CG2 ILE A 174      -1.118 -14.297  15.343  1.00 49.39           C  
ANISOU 1297  CG2 ILE A 174     6200   6563   6003   -346   -147   -387       C  
ATOM   1298  CD1 ILE A 174       0.550 -16.699  16.122  1.00 40.34           C  
ANISOU 1298  CD1 ILE A 174     4963   5557   4808    -84   -206   -475       C  
ATOM   1299  N   THR A 175      -4.435 -14.432  17.423  1.00 37.71           N  
ANISOU 1299  N   THR A 175     4939   4902   4489   -313   -293   -270       N  
ATOM   1300  CA  THR A 175      -5.761 -13.942  17.062  1.00 38.85           C  
ANISOU 1300  CA  THR A 175     5162   4969   4629   -366   -287   -209       C  
ATOM   1301  C   THR A 175      -6.163 -12.756  17.929  1.00 46.72           C  
ANISOU 1301  C   THR A 175     6143   5957   5653   -401   -306   -218       C  
ATOM   1302  O   THR A 175      -6.712 -11.768  17.427  1.00 49.98           O  
ANISOU 1302  O   THR A 175     6583   6319   6087   -464   -280   -193       O  
ATOM   1303  CB  THR A 175      -6.790 -15.066  17.184  1.00 34.51           C  
ANISOU 1303  CB  THR A 175     4692   4374   4048   -320   -318   -155       C  
ATOM   1304  OG1 THR A 175      -6.365 -16.190  16.403  1.00 32.79           O  
ANISOU 1304  OG1 THR A 175     4498   4149   3813   -281   -306   -166       O  
ATOM   1305  CG2 THR A 175      -8.150 -14.599  16.691  1.00 29.02           C  
ANISOU 1305  CG2 THR A 175     4057   3621   3347   -373   -315    -98       C  
ATOM   1306  N   MET A 176      -5.895 -12.834  19.236  1.00 50.03           N  
ANISOU 1306  N   MET A 176     6521   6426   6064   -348   -353   -257       N  
ATOM   1307  CA  MET A 176      -6.174 -11.702  20.114  1.00 50.32           C  
ANISOU 1307  CA  MET A 176     6539   6461   6118   -370   -376   -293       C  
ATOM   1308  C   MET A 176      -5.330 -10.493  19.732  1.00 46.18           C  
ANISOU 1308  C   MET A 176     5956   5927   5663   -458   -347   -356       C  
ATOM   1309  O   MET A 176      -5.793  -9.350  19.815  1.00 43.79           O  
ANISOU 1309  O   MET A 176     5675   5564   5398   -510   -340   -365       O  
ATOM   1310  CB  MET A 176      -5.923 -12.092  21.571  1.00 51.45           C  
ANISOU 1310  CB  MET A 176     6646   6685   6219   -283   -435   -332       C  
ATOM   1311  CG  MET A 176      -7.063 -12.859  22.219  1.00 52.99           C  
ANISOU 1311  CG  MET A 176     6907   6873   6355   -214   -454   -253       C  
ATOM   1312  SD  MET A 176      -8.577 -11.888  22.319  1.00 63.12           S  
ANISOU 1312  SD  MET A 176     8245   8096   7640   -250   -442   -213       S  
ATOM   1313  CE  MET A 176      -7.980 -10.414  23.141  1.00 65.70           C  
ANISOU 1313  CE  MET A 176     8517   8452   7994   -267   -470   -333       C  
ATOM   1314  N   PHE A 177      -4.088 -10.729  19.304  1.00 44.77           N  
ANISOU 1314  N   PHE A 177     5701   5803   5507   -476   -325   -399       N  
ATOM   1315  CA  PHE A 177      -3.217  -9.629  18.903  1.00 43.01           C  
ANISOU 1315  CA  PHE A 177     5408   5573   5363   -578   -285   -452       C  
ATOM   1316  C   PHE A 177      -3.718  -8.962  17.627  1.00 49.10           C  
ANISOU 1316  C   PHE A 177     6245   6249   6162   -658   -210   -374       C  
ATOM   1317  O   PHE A 177      -3.633  -7.737  17.486  1.00 53.61           O  
ANISOU 1317  O   PHE A 177     6812   6755   6804   -746   -180   -385       O  
ATOM   1318  CB  PHE A 177      -1.790 -10.138  18.717  1.00 43.20           C  
ANISOU 1318  CB  PHE A 177     5315   5699   5399   -570   -273   -508       C  
ATOM   1319  CG  PHE A 177      -0.820  -9.079  18.286  1.00 55.15           C  
ANISOU 1319  CG  PHE A 177     6735   7215   7004   -691   -221   -558       C  
ATOM   1320  CD1 PHE A 177      -0.479  -8.046  19.143  1.00 59.76           C  
ANISOU 1320  CD1 PHE A 177     7257   7792   7658   -756   -259   -649       C  
ATOM   1321  CD2 PHE A 177      -0.245  -9.117  17.026  1.00 54.42           C  
ANISOU 1321  CD2 PHE A 177     6616   7133   6928   -744   -131   -515       C  
ATOM   1322  CE1 PHE A 177       0.415  -7.068  18.752  1.00 58.01           C  
ANISOU 1322  CE1 PHE A 177     6944   7556   7540   -887   -208   -695       C  
ATOM   1323  CE2 PHE A 177       0.650  -8.143  16.629  1.00 57.92           C  
ANISOU 1323  CE2 PHE A 177     6966   7578   7463   -868    -69   -545       C  
ATOM   1324  CZ  PHE A 177       0.980  -7.117  17.494  1.00 58.96           C  
ANISOU 1324  CZ  PHE A 177     7033   7686   7683   -948   -108   -633       C  
ATOM   1325  N   ILE A 178      -4.239  -9.752  16.686  1.00 48.34           N  
ANISOU 1325  N   ILE A 178     6215   6142   6008   -625   -182   -297       N  
ATOM   1326  CA  ILE A 178      -4.758  -9.185  15.445  1.00 43.65           C  
ANISOU 1326  CA  ILE A 178     5689   5482   5415   -681   -119   -217       C  
ATOM   1327  C   ILE A 178      -6.015  -8.367  15.718  1.00 40.23           C  
ANISOU 1327  C   ILE A 178     5335   4960   4991   -688   -140   -174       C  
ATOM   1328  O   ILE A 178      -6.210  -7.292  15.137  1.00 43.26           O  
ANISOU 1328  O   ILE A 178     5753   5270   5414   -748    -94   -131       O  
ATOM   1329  CB  ILE A 178      -5.015 -10.302  14.417  1.00 35.18           C  
ANISOU 1329  CB  ILE A 178     4664   4436   4266   -633   -100   -168       C  
ATOM   1330  CG1 ILE A 178      -3.698 -10.962  14.009  1.00 33.44           C  
ANISOU 1330  CG1 ILE A 178     4364   4303   4038   -618    -63   -213       C  
ATOM   1331  CG2 ILE A 178      -5.736  -9.754  13.197  1.00 35.16           C  
ANISOU 1331  CG2 ILE A 178     4740   4382   4236   -669    -51    -82       C  
ATOM   1332  CD1 ILE A 178      -3.873 -12.308  13.346  1.00 33.22           C  
ANISOU 1332  CD1 ILE A 178     4383   4303   3936   -541    -68   -202       C  
ATOM   1333  N   ASN A 179      -6.883  -8.858  16.606  1.00 29.24           N  
ANISOU 1333  N   ASN A 179     3973   3574   3563   -619   -204   -177       N  
ATOM   1334  CA  ASN A 179      -8.083  -8.108  16.959  1.00 30.33           C  
ANISOU 1334  CA  ASN A 179     4171   3648   3705   -609   -224   -144       C  
ATOM   1335  C   ASN A 179      -7.729  -6.791  17.637  1.00 39.18           C  
ANISOU 1335  C   ASN A 179     5269   4717   4901   -653   -224   -206       C  
ATOM   1336  O   ASN A 179      -8.333  -5.751  17.345  1.00 43.99           O  
ANISOU 1336  O   ASN A 179     5932   5237   5545   -677   -202   -171       O  
ATOM   1337  CB  ASN A 179      -8.981  -8.952  17.864  1.00 31.89           C  
ANISOU 1337  CB  ASN A 179     4385   3883   3849   -530   -281   -135       C  
ATOM   1338  CG  ASN A 179      -9.673 -10.072  17.117  1.00 43.30           C  
ANISOU 1338  CG  ASN A 179     5872   5340   5239   -505   -283    -67       C  
ATOM   1339  OD1 ASN A 179     -10.853  -9.973  16.781  1.00 48.47           O  
ANISOU 1339  OD1 ASN A 179     6574   5969   5874   -497   -289     -8       O  
ATOM   1340  ND2 ASN A 179      -8.941 -11.148  16.851  1.00 46.23           N  
ANISOU 1340  ND2 ASN A 179     6222   5751   5591   -490   -281    -84       N  
ATOM   1341  N   VAL A 180      -6.750  -6.815  18.545  1.00 38.02           N  
ANISOU 1341  N   VAL A 180     5042   4623   4781   -658   -254   -306       N  
ATOM   1342  CA  VAL A 180      -6.329  -5.592  19.221  1.00 40.24           C  
ANISOU 1342  CA  VAL A 180     5294   4855   5142   -710   -266   -394       C  
ATOM   1343  C   VAL A 180      -5.707  -4.620  18.227  1.00 43.15           C  
ANISOU 1343  C   VAL A 180     5658   5135   5600   -824   -191   -373       C  
ATOM   1344  O   VAL A 180      -5.977  -3.415  18.268  1.00 40.89           O  
ANISOU 1344  O   VAL A 180     5414   4734   5386   -871   -175   -381       O  
ATOM   1345  CB  VAL A 180      -5.361  -5.925  20.372  1.00 42.63           C  
ANISOU 1345  CB  VAL A 180     5497   5259   5440   -687   -326   -515       C  
ATOM   1346  CG1 VAL A 180      -4.701  -4.660  20.901  1.00 31.15           C  
ANISOU 1346  CG1 VAL A 180     3995   3755   4084   -768   -339   -630       C  
ATOM   1347  CG2 VAL A 180      -6.097  -6.647  21.485  1.00 36.81           C  
ANISOU 1347  CG2 VAL A 180     4780   4593   4611   -570   -391   -521       C  
ATOM   1348  N   SER A 181      -4.874  -5.127  17.315  1.00 50.46           N  
ANISOU 1348  N   SER A 181     6537   6111   6524   -865   -138   -340       N  
ATOM   1349  CA  SER A 181      -4.226  -4.264  16.331  1.00 57.69           C  
ANISOU 1349  CA  SER A 181     7442   6959   7519   -977    -50   -301       C  
ATOM   1350  C   SER A 181      -5.241  -3.484  15.505  1.00 58.26           C  
ANISOU 1350  C   SER A 181     7635   6909   7594   -985     -2   -186       C  
ATOM   1351  O   SER A 181      -4.988  -2.329  15.140  1.00 63.75           O  
ANISOU 1351  O   SER A 181     8350   7491   8380  -1073     56   -161       O  
ATOM   1352  CB  SER A 181      -3.334  -5.095  15.415  1.00 63.60           C  
ANISOU 1352  CB  SER A 181     8127   7806   8232   -991      7   -270       C  
ATOM   1353  OG  SER A 181      -4.107  -5.970  14.613  1.00 70.21           O  
ANISOU 1353  OG  SER A 181     9041   8671   8965   -914     16   -180       O  
ATOM   1354  N   ILE A 182      -6.391  -4.088  15.209  1.00 46.19           N  
ANISOU 1354  N   ILE A 182     6185   5397   5970   -894    -27   -113       N  
ATOM   1355  CA  ILE A 182      -7.420  -3.398  14.439  1.00 46.14           C  
ANISOU 1355  CA  ILE A 182     6284   5297   5951   -878      5     -3       C  
ATOM   1356  C   ILE A 182      -8.201  -2.438  15.327  1.00 48.55           C  
ANISOU 1356  C   ILE A 182     6638   5501   6307   -851    -36    -37       C  
ATOM   1357  O   ILE A 182      -8.444  -1.283  14.956  1.00 51.95           O  
ANISOU 1357  O   ILE A 182     7134   5805   6802   -882      5     13       O  
ATOM   1358  CB  ILE A 182      -8.349  -4.418  13.754  1.00 43.13           C  
ANISOU 1358  CB  ILE A 182     5951   4987   5451   -796    -15     73       C  
ATOM   1359  CG1 ILE A 182      -7.628  -5.101  12.591  1.00 37.15           C  
ANISOU 1359  CG1 ILE A 182     5171   4302   4641   -820     43    114       C  
ATOM   1360  CG2 ILE A 182      -9.627  -3.743  13.267  1.00 42.83           C  
ANISOU 1360  CG2 ILE A 182     6008   4876   5388   -750    -15    167       C  
ATOM   1361  CD1 ILE A 182      -8.293  -6.376  12.126  1.00 29.71           C  
ANISOU 1361  CD1 ILE A 182     4254   3444   3590   -745      4    136       C  
ATOM   1362  N   LEU A 183      -8.598  -2.897  16.516  1.00 46.20           N  
ANISOU 1362  N   LEU A 183     6314   5259   5979   -784   -114   -118       N  
ATOM   1363  CA  LEU A 183      -9.388  -2.057  17.411  1.00 44.72           C  
ANISOU 1363  CA  LEU A 183     6171   4999   5822   -737   -153   -161       C  
ATOM   1364  C   LEU A 183      -8.573  -0.898  17.972  1.00 51.10           C  
ANISOU 1364  C   LEU A 183     6961   5705   6751   -817   -146   -262       C  
ATOM   1365  O   LEU A 183      -9.132   0.168  18.255  1.00 56.26           O  
ANISOU 1365  O   LEU A 183     7680   6237   7459   -800   -148   -277       O  
ATOM   1366  CB  LEU A 183      -9.962  -2.902  18.550  1.00 41.95           C  
ANISOU 1366  CB  LEU A 183     5790   4754   5393   -643   -226   -215       C  
ATOM   1367  CG  LEU A 183     -11.154  -3.795  18.198  1.00 40.15           C  
ANISOU 1367  CG  LEU A 183     5593   4591   5070   -564   -240   -120       C  
ATOM   1368  CD1 LEU A 183     -11.331  -4.888  19.239  1.00 38.69           C  
ANISOU 1368  CD1 LEU A 183     5360   4522   4817   -502   -293   -161       C  
ATOM   1369  CD2 LEU A 183     -12.425  -2.971  18.060  1.00 39.92           C  
ANISOU 1369  CD2 LEU A 183     5635   4493   5041   -505   -238    -64       C  
ATOM   1370  N   ILE A 184      -7.260  -1.080  18.139  1.00 49.72           N  
ANISOU 1370  N   ILE A 184     6692   5575   6623   -902   -140   -340       N  
ATOM   1371  CA  ILE A 184      -6.436  -0.023  18.714  1.00 49.50           C  
ANISOU 1371  CA  ILE A 184     6629   5459   6721   -995   -143   -457       C  
ATOM   1372  C   ILE A 184      -6.293   1.163  17.770  1.00 51.62           C  
ANISOU 1372  C   ILE A 184     6961   5551   7103  -1095    -56   -380       C  
ATOM   1373  O   ILE A 184      -6.015   2.278  18.224  1.00 52.84           O  
ANISOU 1373  O   ILE A 184     7130   5570   7378  -1163    -58   -463       O  
ATOM   1374  CB  ILE A 184      -5.051  -0.572  19.113  1.00 47.25           C  
ANISOU 1374  CB  ILE A 184     6204   5293   6456  -1061   -165   -561       C  
ATOM   1375  CG1 ILE A 184      -4.450   0.260  20.247  1.00 39.41           C  
ANISOU 1375  CG1 ILE A 184     5156   4262   5556  -1115   -223   -737       C  
ATOM   1376  CG2 ILE A 184      -4.115  -0.626  17.913  1.00 50.64           C  
ANISOU 1376  CG2 ILE A 184     6585   5724   6934  -1169    -72   -485       C  
ATOM   1377  CD1 ILE A 184      -4.929  -0.161  21.613  1.00 37.96           C  
ANISOU 1377  CD1 ILE A 184     4964   4178   5281   -992   -326   -843       C  
ATOM   1378  N   ARG A 185      -6.482   0.957  16.465  1.00 51.91           N  
ANISOU 1378  N   ARG A 185     7042   5580   7101  -1102     20   -224       N  
ATOM   1379  CA  ARG A 185      -6.380   2.055  15.514  1.00 54.20           C  
ANISOU 1379  CA  ARG A 185     7404   5706   7482  -1184    114   -121       C  
ATOM   1380  C   ARG A 185      -7.648   2.894  15.455  1.00 54.32           C  
ANISOU 1380  C   ARG A 185     7557   5581   7502  -1098    109    -54       C  
ATOM   1381  O   ARG A 185      -7.595   4.042  15.002  1.00 55.35           O  
ANISOU 1381  O   ARG A 185     7762   5531   7737  -1157    173      6       O  
ATOM   1382  CB  ARG A 185      -6.044   1.522  14.121  1.00 57.96           C  
ANISOU 1382  CB  ARG A 185     7875   6251   7896  -1211    202     23       C  
ATOM   1383  CG  ARG A 185      -4.686   0.850  14.032  1.00 65.13           C  
ANISOU 1383  CG  ARG A 185     8645   7286   8817  -1298    229    -35       C  
ATOM   1384  CD  ARG A 185      -4.228   0.746  12.590  1.00 74.69           C  
ANISOU 1384  CD  ARG A 185     9859   8524   9994  -1347    345    108       C  
ATOM   1385  NE  ARG A 185      -3.972   2.062  12.011  1.00 82.86           N  
ANISOU 1385  NE  ARG A 185    10949   9386  11148  -1455    445    197       N  
ATOM   1386  CZ  ARG A 185      -4.128   2.352  10.723  1.00 84.35           C  
ANISOU 1386  CZ  ARG A 185    11213   9540  11295  -1460    548    371       C  
ATOM   1387  NH1 ARG A 185      -4.542   1.418   9.877  1.00 82.38           N  
ANISOU 1387  NH1 ARG A 185    10988   9429  10884  -1362    556    455       N  
ATOM   1388  NH2 ARG A 185      -3.873   3.576  10.280  1.00 86.11           N  
ANISOU 1388  NH2 ARG A 185    11492   9589  11638  -1561    644    461       N  
ATOM   1389  N   GLY A 186      -8.774   2.353  15.892  1.00 52.27           N  
ANISOU 1389  N   GLY A 186     7327   5396   7136   -960     39    -55       N  
ATOM   1390  CA  GLY A 186      -9.983   3.128  16.058  1.00 54.95           C  
ANISOU 1390  CA  GLY A 186     7773   5626   7479   -859     21    -20       C  
ATOM   1391  C   GLY A 186     -11.060   2.759  15.054  1.00 59.23           C  
ANISOU 1391  C   GLY A 186     8380   6216   7909   -760     36    140       C  
ATOM   1392  O   GLY A 186     -10.977   1.766  14.327  1.00 60.53           O  
ANISOU 1392  O   GLY A 186     8509   6512   7979   -759     47    207       O  
ATOM   1393  N   ILE A 187     -12.093   3.601  15.030  1.00 61.73           N  
ANISOU 1393  N   ILE A 187     8792   6425   8238   -667     32    191       N  
ATOM   1394  CA  ILE A 187     -13.245   3.364  14.166  1.00 58.02           C  
ANISOU 1394  CA  ILE A 187     8375   6008   7661   -554     30    332       C  
ATOM   1395  C   ILE A 187     -12.864   3.559  12.703  1.00 53.44           C  
ANISOU 1395  C   ILE A 187     7845   5394   7067   -604    113    486       C  
ATOM   1396  O   ILE A 187     -12.986   2.643  11.882  1.00 50.22           O  
ANISOU 1396  O   ILE A 187     7410   5126   6545   -588    114    557       O  
ATOM   1397  CB  ILE A 187     -14.412   4.281  14.570  1.00 58.24           C  
ANISOU 1397  CB  ILE A 187     8483   5935   7710   -425      3    341       C  
ATOM   1398  CG1 ILE A 187     -14.999   3.841  15.914  1.00 56.32           C  
ANISOU 1398  CG1 ILE A 187     8179   5788   7430   -347    -76    209       C  
ATOM   1399  CG2 ILE A 187     -15.480   4.296  13.496  1.00 57.04           C  
ANISOU 1399  CG2 ILE A 187     8389   5817   7465   -316     10    502       C  
ATOM   1400  CD1 ILE A 187     -15.432   2.392  15.946  1.00 55.80           C  
ANISOU 1400  CD1 ILE A 187     8027   5938   7237   -315   -122    218       C  
ATOM   1401  N   SER A 188     -12.390   4.757  12.358  1.00 55.68           N  
ANISOU 1401  N   SER A 188     8204   5487   7465   -665    186    540       N  
ATOM   1402  CA  SER A 188     -12.111   5.081  10.963  1.00 59.68           C  
ANISOU 1402  CA  SER A 188     8774   5953   7951   -698    279    713       C  
ATOM   1403  C   SER A 188     -10.817   4.433  10.482  1.00 59.52           C  
ANISOU 1403  C   SER A 188     8668   6022   7925   -834    340    708       C  
ATOM   1404  O   SER A 188     -10.813   3.675   9.506  1.00 59.23           O  
ANISOU 1404  O   SER A 188     8618   6124   7765   -813    363    796       O  
ATOM   1405  CB  SER A 188     -12.053   6.600  10.782  1.00 67.39           C  
ANISOU 1405  CB  SER A 188     9867   6675   9062   -719    349    788       C  
ATOM   1406  OG  SER A 188     -11.622   6.945   9.476  1.00 73.14           O  
ANISOU 1406  OG  SER A 188    10655   7360   9776   -766    456    967       O  
ATOM   1407  N   LYS A 189      -9.704   4.720  11.162  1.00 59.27           N  
ANISOU 1407  N   LYS A 189     8572   5923   8025   -969    362    595       N  
ATOM   1408  CA  LYS A 189      -8.403   4.251  10.700  1.00 52.40           C  
ANISOU 1408  CA  LYS A 189     7610   5133   7168  -1101    431    594       C  
ATOM   1409  C   LYS A 189      -8.207   2.754  10.904  1.00 47.07           C  
ANISOU 1409  C   LYS A 189     6824   4683   6375  -1071    370    511       C  
ATOM   1410  O   LYS A 189      -7.304   2.174  10.291  1.00 52.96           O  
ANISOU 1410  O   LYS A 189     7501   5532   7089  -1137    428    531       O  
ATOM   1411  CB  LYS A 189      -7.287   5.021  11.408  1.00 50.50           C  
ANISOU 1411  CB  LYS A 189     7313   4761   7112  -1258    462    485       C  
ATOM   1412  CG  LYS A 189      -7.292   6.516  11.130  1.00 49.38           C  
ANISOU 1412  CG  LYS A 189     7283   4362   7116  -1318    540    571       C  
ATOM   1413  CD  LYS A 189      -5.891   7.099  11.208  1.00 50.30           C  
ANISOU 1413  CD  LYS A 189     7324   4385   7404  -1523    621    524       C  
ATOM   1414  N   GLY A 190      -9.023   2.116  11.738  1.00 43.64           N  
ANISOU 1414  N   GLY A 190     6375   4327   5879   -970    264    423       N  
ATOM   1415  CA  GLY A 190      -8.847   0.704  12.014  1.00 40.61           C  
ANISOU 1415  CA  GLY A 190     5899   4129   5400   -943    207    349       C  
ATOM   1416  C   GLY A 190      -9.920  -0.186  11.424  1.00 43.80           C  
ANISOU 1416  C   GLY A 190     6338   4648   5656   -828    165    419       C  
ATOM   1417  O   GLY A 190      -9.663  -0.935  10.476  1.00 45.34           O  
ANISOU 1417  O   GLY A 190     6520   4946   5762   -828    196    474       O  
ATOM   1418  N   ILE A 191     -11.130  -0.114  11.979  1.00 50.19           N  
ANISOU 1418  N   ILE A 191     7211   5807   6052   -480   -277    270       N  
ATOM   1419  CA  ILE A 191     -12.202  -1.008  11.550  1.00 48.75           C  
ANISOU 1419  CA  ILE A 191     6997   5695   5829   -391   -305    325       C  
ATOM   1420  C   ILE A 191     -12.681  -0.639  10.151  1.00 47.80           C  
ANISOU 1420  C   ILE A 191     6945   5549   5668   -378   -272    404       C  
ATOM   1421  O   ILE A 191     -12.783  -1.498   9.268  1.00 46.28           O  
ANISOU 1421  O   ILE A 191     6711   5426   5448   -377   -275    430       O  
ATOM   1422  CB  ILE A 191     -13.357  -0.985  12.566  1.00 46.07           C  
ANISOU 1422  CB  ILE A 191     6668   5360   5478   -288   -346    330       C  
ATOM   1423  CG1 ILE A 191     -12.860  -1.420  13.947  1.00 43.69           C  
ANISOU 1423  CG1 ILE A 191     6309   5091   5200   -296   -379    255       C  
ATOM   1424  CG2 ILE A 191     -14.495  -1.874  12.094  1.00 46.52           C  
ANISOU 1424  CG2 ILE A 191     6682   5490   5502   -209   -373    384       C  
ATOM   1425  CD1 ILE A 191     -13.930  -1.395  15.017  1.00 43.17           C  
ANISOU 1425  CD1 ILE A 191     6258   5030   5117   -198   -406    257       C  
ATOM   1426  N   GLU A 192     -12.990   0.642   9.932  1.00 52.72           N  
ANISOU 1426  N   GLU A 192     7682   6069   6281   -365   -242    443       N  
ATOM   1427  CA  GLU A 192     -13.452   1.082   8.618  1.00 57.05           C  
ANISOU 1427  CA  GLU A 192     8310   6587   6778   -341   -214    527       C  
ATOM   1428  C   GLU A 192     -12.402   0.817   7.549  1.00 56.68           C  
ANISOU 1428  C   GLU A 192     8255   6558   6723   -441   -162    530       C  
ATOM   1429  O   GLU A 192     -12.735   0.459   6.413  1.00 52.61           O  
ANISOU 1429  O   GLU A 192     7756   6082   6151   -421   -157    585       O  
ATOM   1430  CB  GLU A 192     -13.810   2.568   8.659  1.00 56.10           C  
ANISOU 1430  CB  GLU A 192     8326   6334   6655   -311   -183    566       C  
ATOM   1431  CG  GLU A 192     -14.420   3.102   7.375  1.00 56.04           C  
ANISOU 1431  CG  GLU A 192     8418   6290   6585   -262   -162    665       C  
ATOM   1432  CD  GLU A 192     -14.746   4.580   7.458  1.00 60.90           C  
ANISOU 1432  CD  GLU A 192     9179   6759   7200   -223   -127    707       C  
ATOM   1433  OE1 GLU A 192     -15.459   5.085   6.564  1.00 61.94           O  
ANISOU 1433  OE1 GLU A 192     9401   6857   7277   -148   -124    797       O  
ATOM   1434  OE2 GLU A 192     -14.290   5.237   8.417  1.00 62.51           O  
ANISOU 1434  OE2 GLU A 192     9413   6880   7456   -264   -107    649       O  
ATOM   1435  N   ARG A 193     -11.125   0.982   7.898  1.00 58.90           N  
ANISOU 1435  N   ARG A 193     8507   6816   7058   -550   -122    467       N  
ATOM   1436  CA  ARG A 193     -10.053   0.710   6.948  1.00 59.37           C  
ANISOU 1436  CA  ARG A 193     8543   6899   7117   -649    -60    463       C  
ATOM   1437  C   ARG A 193      -9.969  -0.775   6.620  1.00 55.22           C  
ANISOU 1437  C   ARG A 193     7906   6499   6575   -634    -89    443       C  
ATOM   1438  O   ARG A 193      -9.736  -1.150   5.464  1.00 57.53           O  
ANISOU 1438  O   ARG A 193     8207   6826   6826   -658    -50    474       O  
ATOM   1439  CB  ARG A 193      -8.726   1.212   7.515  1.00 66.28           C  
ANISOU 1439  CB  ARG A 193     9389   7730   8066   -768    -17    391       C  
ATOM   1440  CG  ARG A 193      -7.677   1.541   6.475  1.00 72.65           C  
ANISOU 1440  CG  ARG A 193    10215   8512   8878   -881     78    404       C  
ATOM   1441  CD  ARG A 193      -6.986   2.853   6.807  1.00 78.46           C  
ANISOU 1441  CD  ARG A 193    11019   9125   9668   -981    135    381       C  
ATOM   1442  NE  ARG A 193      -7.924   3.973   6.829  1.00 82.86           N  
ANISOU 1442  NE  ARG A 193    11728   9560  10193   -920    137    444       N  
ATOM   1443  CZ  ARG A 193      -7.567   5.245   6.974  1.00 86.36           C  
ANISOU 1443  CZ  ARG A 193    12275   9867  10672   -991    193    442       C  
ATOM   1444  NH1 ARG A 193      -6.287   5.564   7.112  1.00 87.72           N  
ANISOU 1444  NH1 ARG A 193    12403  10013  10913  -1138    250    379       N  
ATOM   1445  NH2 ARG A 193      -8.488   6.199   6.981  1.00 85.75           N  
ANISOU 1445  NH2 ARG A 193    12342   9677  10564   -915    194    503       N  
ATOM   1446  N   PHE A 194     -10.161  -1.636   7.621  1.00 53.56           N  
ANISOU 1446  N   PHE A 194     7602   6354   6394   -593   -153    393       N  
ATOM   1447  CA  PHE A 194     -10.030  -3.071   7.406  1.00 53.48           C  
ANISOU 1447  CA  PHE A 194     7493   6448   6377   -580   -177    369       C  
ATOM   1448  C   PHE A 194     -11.257  -3.670   6.732  1.00 49.48           C  
ANISOU 1448  C   PHE A 194     7006   5987   5809   -499   -214    423       C  
ATOM   1449  O   PHE A 194     -11.125  -4.619   5.951  1.00 46.62           O  
ANISOU 1449  O   PHE A 194     6605   5689   5419   -506   -208    421       O  
ATOM   1450  CB  PHE A 194      -9.769  -3.783   8.734  1.00 52.58           C  
ANISOU 1450  CB  PHE A 194     7284   6381   6314   -565   -229    301       C  
ATOM   1451  CG  PHE A 194      -9.505  -5.253   8.587  1.00 51.51           C  
ANISOU 1451  CG  PHE A 194     7053   6337   6181   -554   -247    274       C  
ATOM   1452  CD1 PHE A 194      -8.257  -5.709   8.197  1.00 52.04           C  
ANISOU 1452  CD1 PHE A 194     7056   6439   6277   -621   -206    232       C  
ATOM   1453  CD2 PHE A 194     -10.506  -6.180   8.831  1.00 52.79           C  
ANISOU 1453  CD2 PHE A 194     7191   6546   6322   -477   -299    289       C  
ATOM   1454  CE1 PHE A 194      -8.011  -7.061   8.057  1.00 52.73           C  
ANISOU 1454  CE1 PHE A 194     7066   6600   6369   -600   -219    205       C  
ATOM   1455  CE2 PHE A 194     -10.265  -7.533   8.692  1.00 50.68           C  
ANISOU 1455  CE2 PHE A 194     6850   6345   6059   -469   -311    263       C  
ATOM   1456  CZ  PHE A 194      -9.016  -7.974   8.303  1.00 52.30           C  
ANISOU 1456  CZ  PHE A 194     7002   6579   6291   -525   -271    221       C  
ATOM   1457  N   ALA A 195     -12.448  -3.143   7.023  1.00 50.78           N  
ANISOU 1457  N   ALA A 195     7222   6121   5950   -419   -252    467       N  
ATOM   1458  CA  ALA A 195     -13.656  -3.662   6.392  1.00 50.04           C  
ANISOU 1458  CA  ALA A 195     7133   6079   5803   -344   -295    515       C  
ATOM   1459  C   ALA A 195     -13.662  -3.403   4.892  1.00 52.75           C  
ANISOU 1459  C   ALA A 195     7549   6419   6076   -358   -264    570       C  
ATOM   1460  O   ALA A 195     -14.202  -4.211   4.128  1.00 56.37           O  
ANISOU 1460  O   ALA A 195     7987   6946   6486   -332   -294    585       O  
ATOM   1461  CB  ALA A 195     -14.896  -3.049   7.043  1.00 47.40           C  
ANISOU 1461  CB  ALA A 195     6829   5716   5466   -252   -338    550       C  
ATOM   1462  N   LYS A 196     -13.065  -2.292   4.454  1.00 53.38           N  
ANISOU 1462  N   LYS A 196     7718   6417   6146   -404   -201    599       N  
ATOM   1463  CA  LYS A 196     -13.003  -1.992   3.028  1.00 53.64           C  
ANISOU 1463  CA  LYS A 196     7837   6442   6103   -418   -161    658       C  
ATOM   1464  C   LYS A 196     -12.188  -3.035   2.272  1.00 58.32           C  
ANISOU 1464  C   LYS A 196     8375   7108   6676   -481   -127    622       C  
ATOM   1465  O   LYS A 196     -12.409  -3.247   1.075  1.00 64.29           O  
ANISOU 1465  O   LYS A 196     9182   7897   7349   -471   -117    660       O  
ATOM   1466  CB  LYS A 196     -12.417  -0.595   2.818  1.00 55.38           C  
ANISOU 1466  CB  LYS A 196     8169   6547   6327   -467    -85    696       C  
ATOM   1467  CG  LYS A 196     -12.355  -0.143   1.368  1.00 62.92           C  
ANISOU 1467  CG  LYS A 196     9235   7479   7191   -478    -32    771       C  
ATOM   1468  CD  LYS A 196     -11.244   0.873   1.155  1.00 69.33           C  
ANISOU 1468  CD  LYS A 196    10125   8189   8028   -580     75    781       C  
ATOM   1469  CE  LYS A 196     -10.922   1.044  -0.321  1.00 72.10           C  
ANISOU 1469  CE  LYS A 196    10571   8537   8286   -612    147    846       C  
ATOM   1470  NZ  LYS A 196      -9.630   1.757  -0.528  1.00 73.42           N  
ANISOU 1470  NZ  LYS A 196    10779   8626   8492   -739    269    840       N  
ATOM   1471  N   ILE A 197     -11.260  -3.702   2.950  1.00 59.54           N  
ANISOU 1471  N   ILE A 197     8430   7292   6900   -537   -111    546       N  
ATOM   1472  CA  ILE A 197     -10.412  -4.707   2.327  1.00 59.12           C  
ANISOU 1472  CA  ILE A 197     8319   7305   6840   -588    -72    503       C  
ATOM   1473  C   ILE A 197     -10.966  -6.113   2.522  1.00 56.00           C  
ANISOU 1473  C   ILE A 197     7841   6992   6443   -539   -139    467       C  
ATOM   1474  O   ILE A 197     -10.861  -6.952   1.628  1.00 53.30           O  
ANISOU 1474  O   ILE A 197     7493   6705   6054   -546   -127    455       O  
ATOM   1475  CB  ILE A 197      -8.974  -4.599   2.879  1.00 58.76           C  
ANISOU 1475  CB  ILE A 197     8207   7243   6875   -676    -12    442       C  
ATOM   1476  CG1 ILE A 197      -8.574  -3.131   3.033  1.00 64.13           C  
ANISOU 1476  CG1 ILE A 197     8963   7824   7579   -730     41    469       C  
ATOM   1477  CG2 ILE A 197      -7.999  -5.337   1.977  1.00 55.03           C  
ANISOU 1477  CG2 ILE A 197     7696   6825   6388   -731     57    412       C  
ATOM   1478  CD1 ILE A 197      -7.349  -2.916   3.899  1.00 65.46           C  
ANISOU 1478  CD1 ILE A 197     9052   7978   7843   -813     73    398       C  
ATOM   1479  N   ALA A 198     -11.559  -6.386   3.686  1.00 56.38           N  
ANISOU 1479  N   ALA A 198     7835   7046   6539   -492   -205    447       N  
ATOM   1480  CA  ALA A 198     -11.946  -7.755   4.011  1.00 54.74           C  
ANISOU 1480  CA  ALA A 198     7547   6906   6345   -459   -255    409       C  
ATOM   1481  C   ALA A 198     -13.210  -8.173   3.269  1.00 54.52           C  
ANISOU 1481  C   ALA A 198     7547   6918   6251   -407   -307    445       C  
ATOM   1482  O   ALA A 198     -13.324  -9.322   2.828  1.00 53.25           O  
ANISOU 1482  O   ALA A 198     7350   6811   6072   -408   -323    415       O  
ATOM   1483  CB  ALA A 198     -12.133  -7.903   5.521  1.00 45.46           C  
ANISOU 1483  CB  ALA A 198     6312   5724   5238   -429   -298    380       C  
ATOM   1484  N   MET A 199     -14.170  -7.258   3.123  1.00 56.01           N  
ANISOU 1484  N   MET A 199     7797   7080   6403   -358   -337    505       N  
ATOM   1485  CA  MET A 199     -15.432  -7.609   2.474  1.00 61.01           C  
ANISOU 1485  CA  MET A 199     8440   7763   6976   -303   -401    537       C  
ATOM   1486  C   MET A 199     -15.257  -8.023   1.017  1.00 62.17           C  
ANISOU 1486  C   MET A 199     8634   7951   7038   -328   -386    542       C  
ATOM   1487  O   MET A 199     -15.854  -9.038   0.616  1.00 63.77           O  
ANISOU 1487  O   MET A 199     8800   8216   7213   -318   -435    517       O  
ATOM   1488  CB  MET A 199     -16.427  -6.452   2.619  1.00 65.73           C  
ANISOU 1488  CB  MET A 199     9092   8325   7555   -234   -434    604       C  
ATOM   1489  CG  MET A 199     -16.746  -6.093   4.061  1.00 66.02           C  
ANISOU 1489  CG  MET A 199     9089   8328   7667   -199   -448    594       C  
ATOM   1490  SD  MET A 199     -17.127  -7.541   5.066  1.00 64.96           S  
ANISOU 1490  SD  MET A 199     8832   8258   7592   -194   -489    535       S  
ATOM   1491  CE  MET A 199     -18.651  -8.100   4.306  1.00 62.17           C  
ANISOU 1491  CE  MET A 199     8450   7981   7189   -140   -564    564       C  
ATOM   1492  N   PRO A 200     -14.487  -7.316   0.177  1.00 62.71           N  
ANISOU 1492  N   PRO A 200     8785   7986   7058   -365   -319    569       N  
ATOM   1493  CA  PRO A 200     -14.251  -7.843  -1.179  1.00 63.28           C  
ANISOU 1493  CA  PRO A 200     8901   8103   7040   -390   -298    565       C  
ATOM   1494  C   PRO A 200     -13.494  -9.159  -1.180  1.00 63.39           C  
ANISOU 1494  C   PRO A 200     8843   8159   7084   -436   -271    484       C  
ATOM   1495  O   PRO A 200     -13.766 -10.025  -2.021  1.00 64.88           O  
ANISOU 1495  O   PRO A 200     9040   8402   7210   -435   -292    459       O  
ATOM   1496  CB  PRO A 200     -13.451  -6.721  -1.857  1.00 67.83           C  
ANISOU 1496  CB  PRO A 200     9579   8621   7572   -426   -210    614       C  
ATOM   1497  CG  PRO A 200     -13.779  -5.497  -1.080  1.00 69.39           C  
ANISOU 1497  CG  PRO A 200     9809   8744   7813   -396   -218    664       C  
ATOM   1498  CD  PRO A 200     -13.920  -5.965   0.333  1.00 65.15           C  
ANISOU 1498  CD  PRO A 200     9163   8211   7380   -385   -260    611       C  
ATOM   1499  N   THR A 201     -12.544  -9.334  -0.257  1.00 60.79           N  
ANISOU 1499  N   THR A 201     8446   7805   6848   -472   -228    440       N  
ATOM   1500  CA  THR A 201     -11.852 -10.614  -0.143  1.00 55.32           C  
ANISOU 1500  CA  THR A 201     7680   7148   6192   -497   -207    365       C  
ATOM   1501  C   THR A 201     -12.810 -11.716   0.293  1.00 53.90           C  
ANISOU 1501  C   THR A 201     7445   7004   6031   -459   -287    336       C  
ATOM   1502  O   THR A 201     -12.729 -12.848  -0.198  1.00 55.03           O  
ANISOU 1502  O   THR A 201     7573   7182   6156   -469   -288    288       O  
ATOM   1503  CB  THR A 201     -10.685 -10.498   0.838  1.00 52.20           C  
ANISOU 1503  CB  THR A 201     7216   6724   5893   -532   -158    329       C  
ATOM   1504  OG1 THR A 201      -9.838  -9.408   0.450  1.00 57.57           O  
ANISOU 1504  OG1 THR A 201     7942   7366   6565   -581    -81    354       O  
ATOM   1505  CG2 THR A 201      -9.869 -11.782   0.854  1.00 43.62           C  
ANISOU 1505  CG2 THR A 201     6059   5673   4842   -546   -130    257       C  
ATOM   1506  N   LEU A 202     -13.723 -11.402   1.216  1.00 55.40           N  
ANISOU 1506  N   LEU A 202     7609   7182   6259   -419   -349    363       N  
ATOM   1507  CA  LEU A 202     -14.757 -12.357   1.602  1.00 59.38           C  
ANISOU 1507  CA  LEU A 202     8062   7719   6780   -389   -419    344       C  
ATOM   1508  C   LEU A 202     -15.602 -12.767   0.404  1.00 59.88           C  
ANISOU 1508  C   LEU A 202     8162   7831   6758   -384   -463    348       C  
ATOM   1509  O   LEU A 202     -15.919 -13.949   0.230  1.00 62.14           O  
ANISOU 1509  O   LEU A 202     8417   8149   7046   -396   -490    300       O  
ATOM   1510  CB  LEU A 202     -15.645 -11.750   2.688  1.00 62.14           C  
ANISOU 1510  CB  LEU A 202     8385   8052   7175   -344   -465    381       C  
ATOM   1511  CG  LEU A 202     -15.384 -12.122   4.146  1.00 64.71           C  
ANISOU 1511  CG  LEU A 202     8643   8355   7587   -336   -463    355       C  
ATOM   1512  CD1 LEU A 202     -15.937 -11.046   5.065  1.00 66.40           C  
ANISOU 1512  CD1 LEU A 202     8864   8540   7827   -294   -481    396       C  
ATOM   1513  CD2 LEU A 202     -16.010 -13.463   4.465  1.00 66.38           C  
ANISOU 1513  CD2 LEU A 202     8798   8598   7825   -331   -498    322       C  
ATOM   1514  N   PHE A 203     -15.971 -11.798  -0.436  1.00 59.66           N  
ANISOU 1514  N   PHE A 203     8209   7809   6652   -366   -473    403       N  
ATOM   1515  CA  PHE A 203     -16.857 -12.075  -1.560  1.00 65.67           C  
ANISOU 1515  CA  PHE A 203     9007   8626   7319   -351   -532    410       C  
ATOM   1516  C   PHE A 203     -16.153 -12.890  -2.639  1.00 64.25           C  
ANISOU 1516  C   PHE A 203     8866   8471   7074   -396   -492    358       C  
ATOM   1517  O   PHE A 203     -16.754 -13.793  -3.232  1.00 71.10           O  
ANISOU 1517  O   PHE A 203     9729   9387   7899   -403   -544    318       O  
ATOM   1518  CB  PHE A 203     -17.384 -10.759  -2.132  1.00 73.90           C  
ANISOU 1518  CB  PHE A 203    10128   9663   8288   -305   -554    492       C  
ATOM   1519  CG  PHE A 203     -18.294 -10.926  -3.314  1.00 81.04           C  
ANISOU 1519  CG  PHE A 203    11075  10635   9083   -280   -626    506       C  
ATOM   1520  CD1 PHE A 203     -19.429 -11.715  -3.227  1.00 80.96           C  
ANISOU 1520  CD1 PHE A 203    10993  10686   9083   -264   -719    475       C  
ATOM   1521  CD2 PHE A 203     -18.020 -10.284  -4.511  1.00 83.23           C  
ANISOU 1521  CD2 PHE A 203    11464  10915   9243   -273   -603    549       C  
ATOM   1522  CE1 PHE A 203     -20.270 -11.865  -4.313  1.00 80.59           C  
ANISOU 1522  CE1 PHE A 203    10977  10710   8933   -244   -799    480       C  
ATOM   1523  CE2 PHE A 203     -18.857 -10.430  -5.601  1.00 82.60           C  
ANISOU 1523  CE2 PHE A 203    11429  10905   9050   -243   -681    561       C  
ATOM   1524  CZ  PHE A 203     -19.983 -11.222  -5.501  1.00 82.20           C  
ANISOU 1524  CZ  PHE A 203    11297  10923   9013   -228   -785    522       C  
ATOM   1525  N   ILE A 204     -14.881 -12.589  -2.905  1.00 55.77           N  
ANISOU 1525  N   ILE A 204     7830   7365   5994   -429   -397    354       N  
ATOM   1526  CA  ILE A 204     -14.161 -13.286  -3.967  1.00 56.04           C  
ANISOU 1526  CA  ILE A 204     7906   7424   5961   -465   -343    306       C  
ATOM   1527  C   ILE A 204     -13.883 -14.732  -3.572  1.00 56.09           C  
ANISOU 1527  C   ILE A 204     7843   7438   6030   -484   -341    220       C  
ATOM   1528  O   ILE A 204     -14.056 -15.653  -4.379  1.00 60.34           O  
ANISOU 1528  O   ILE A 204     8408   8010   6510   -497   -354    168       O  
ATOM   1529  CB  ILE A 204     -12.864 -12.532  -4.314  1.00 55.40           C  
ANISOU 1529  CB  ILE A 204     7872   7310   5866   -498   -230    326       C  
ATOM   1530  CG1 ILE A 204     -13.189 -11.189  -4.971  1.00 54.11           C  
ANISOU 1530  CG1 ILE A 204     7810   7133   5618   -480   -226    414       C  
ATOM   1531  CG2 ILE A 204     -11.983 -13.372  -5.227  1.00 51.91           C  
ANISOU 1531  CG2 ILE A 204     7455   6894   5376   -532   -156    265       C  
ATOM   1532  CD1 ILE A 204     -12.012 -10.242  -5.034  1.00 53.31           C  
ANISOU 1532  CD1 ILE A 204     7746   6979   5530   -522   -113    446       C  
ATOM   1533  N   LEU A 205     -13.451 -14.956  -2.328  1.00 53.48           N  
ANISOU 1533  N   LEU A 205     7432   7072   5814   -483   -325    204       N  
ATOM   1534  CA  LEU A 205     -13.162 -16.315  -1.880  1.00 53.56           C  
ANISOU 1534  CA  LEU A 205     7386   7079   5887   -491   -320    132       C  
ATOM   1535  C   LEU A 205     -14.418 -17.176  -1.875  1.00 55.71           C  
ANISOU 1535  C   LEU A 205     7642   7372   6153   -485   -406    109       C  
ATOM   1536  O   LEU A 205     -14.390 -18.330  -2.317  1.00 61.60           O  
ANISOU 1536  O   LEU A 205     8394   8123   6887   -503   -405     44       O  
ATOM   1537  CB  LEU A 205     -12.532 -16.287  -0.487  1.00 50.68           C  
ANISOU 1537  CB  LEU A 205     6945   6676   5636   -481   -298    131       C  
ATOM   1538  CG  LEU A 205     -11.113 -15.731  -0.374  1.00 43.12           C  
ANISOU 1538  CG  LEU A 205     5973   5701   4709   -498   -212    128       C  
ATOM   1539  CD1 LEU A 205     -10.786 -15.423   1.077  1.00 44.28           C  
ANISOU 1539  CD1 LEU A 205     6050   5820   4954   -483   -222    137       C  
ATOM   1540  CD2 LEU A 205     -10.107 -16.707  -0.959  1.00 38.62           C  
ANISOU 1540  CD2 LEU A 205     5395   5142   4136   -511   -144     62       C  
ATOM   1541  N   ALA A 206     -15.530 -16.631  -1.377  1.00 54.60           N  
ANISOU 1541  N   ALA A 206     7479   7242   6026   -462   -478    158       N  
ATOM   1542  CA  ALA A 206     -16.762 -17.408  -1.292  1.00 52.16           C  
ANISOU 1542  CA  ALA A 206     7135   6958   5725   -465   -557    136       C  
ATOM   1543  C   ALA A 206     -17.273 -17.787  -2.676  1.00 53.43           C  
ANISOU 1543  C   ALA A 206     7352   7169   5780   -486   -598    105       C  
ATOM   1544  O   ALA A 206     -17.684 -18.932  -2.901  1.00 58.25           O  
ANISOU 1544  O   ALA A 206     7949   7789   6395   -516   -629     42       O  
ATOM   1545  CB  ALA A 206     -17.824 -16.625  -0.522  1.00 53.87           C  
ANISOU 1545  CB  ALA A 206     7308   7185   5975   -430   -616    198       C  
ATOM   1546  N   VAL A 207     -17.250 -16.841  -3.618  1.00 52.36           N  
ANISOU 1546  N   VAL A 207     7287   7063   5545   -470   -600    147       N  
ATOM   1547  CA  VAL A 207     -17.701 -17.134  -4.976  1.00 50.64           C  
ANISOU 1547  CA  VAL A 207     7134   6900   5206   -483   -644    119       C  
ATOM   1548  C   VAL A 207     -16.831 -18.215  -5.603  1.00 51.56           C  
ANISOU 1548  C   VAL A 207     7290   7005   5296   -522   -583     34       C  
ATOM   1549  O   VAL A 207     -17.332 -19.122  -6.280  1.00 50.51           O  
ANISOU 1549  O   VAL A 207     7177   6902   5113   -549   -630    -31       O  
ATOM   1550  CB  VAL A 207     -17.713 -15.847  -5.824  1.00 45.07           C  
ANISOU 1550  CB  VAL A 207     6514   6219   4392   -449   -645    193       C  
ATOM   1551  CG1 VAL A 207     -17.823 -16.179  -7.305  1.00 46.12           C  
ANISOU 1551  CG1 VAL A 207     6737   6407   4379   -462   -668    159       C  
ATOM   1552  CG2 VAL A 207     -18.857 -14.945  -5.394  1.00 43.27           C  
ANISOU 1552  CG2 VAL A 207     6253   6013   4176   -398   -728    266       C  
ATOM   1553  N   PHE A 208     -15.517 -18.147  -5.374  1.00 51.33           N  
ANISOU 1553  N   PHE A 208     7269   6933   5303   -526   -478     28       N  
ATOM   1554  CA  PHE A 208     -14.623 -19.176  -5.894  1.00 48.25           C  
ANISOU 1554  CA  PHE A 208     6906   6528   4897   -550   -408    -53       C  
ATOM   1555  C   PHE A 208     -14.940 -20.538  -5.288  1.00 45.89           C  
ANISOU 1555  C   PHE A 208     6555   6200   4682   -567   -436   -123       C  
ATOM   1556  O   PHE A 208     -14.961 -21.551  -5.998  1.00 44.41           O  
ANISOU 1556  O   PHE A 208     6408   6014   4451   -591   -436   -202       O  
ATOM   1557  CB  PHE A 208     -13.168 -18.791  -5.623  1.00 46.34           C  
ANISOU 1557  CB  PHE A 208     6657   6253   4698   -546   -292    -42       C  
ATOM   1558  CG  PHE A 208     -12.173 -19.810  -6.100  1.00 53.13           C  
ANISOU 1558  CG  PHE A 208     7534   7099   5553   -556   -209   -124       C  
ATOM   1559  CD1 PHE A 208     -11.771 -19.837  -7.424  1.00 56.57           C  
ANISOU 1559  CD1 PHE A 208     8059   7566   5868   -568   -157   -152       C  
ATOM   1560  CD2 PHE A 208     -11.639 -20.742  -5.224  1.00 56.30           C  
ANISOU 1560  CD2 PHE A 208     7869   7458   6066   -547   -181   -171       C  
ATOM   1561  CE1 PHE A 208     -10.856 -20.774  -7.867  1.00 59.43           C  
ANISOU 1561  CE1 PHE A 208     8438   7916   6225   -569    -72   -232       C  
ATOM   1562  CE2 PHE A 208     -10.725 -21.681  -5.661  1.00 55.09           C  
ANISOU 1562  CE2 PHE A 208     7732   7289   5912   -543   -103   -247       C  
ATOM   1563  CZ  PHE A 208     -10.333 -21.697  -6.984  1.00 55.97           C  
ANISOU 1563  CZ  PHE A 208     7926   7431   5907   -554    -46   -280       C  
ATOM   1564  N   LEU A 209     -15.191 -20.583  -3.977  1.00 44.96           N  
ANISOU 1564  N   LEU A 209     6355   6048   4679   -555   -456    -97       N  
ATOM   1565  CA  LEU A 209     -15.525 -21.849  -3.333  1.00 43.39           C  
ANISOU 1565  CA  LEU A 209     6114   5811   4561   -572   -476   -151       C  
ATOM   1566  C   LEU A 209     -16.866 -22.382  -3.822  1.00 47.78           C  
ANISOU 1566  C   LEU A 209     6676   6400   5079   -608   -569   -184       C  
ATOM   1567  O   LEU A 209     -17.016 -23.589  -4.040  1.00 46.98           O  
ANISOU 1567  O   LEU A 209     6588   6271   4989   -643   -574   -260       O  
ATOM   1568  CB  LEU A 209     -15.539 -21.679  -1.814  1.00 41.40           C  
ANISOU 1568  CB  LEU A 209     5783   5521   4425   -548   -475   -105       C  
ATOM   1569  CG  LEU A 209     -14.207 -21.328  -1.147  1.00 44.63           C  
ANISOU 1569  CG  LEU A 209     6170   5898   4890   -516   -396    -87       C  
ATOM   1570  CD1 LEU A 209     -14.428 -20.922   0.302  1.00 43.50           C  
ANISOU 1570  CD1 LEU A 209     5960   5733   4836   -491   -415    -35       C  
ATOM   1571  CD2 LEU A 209     -13.227 -22.488  -1.241  1.00 44.82           C  
ANISOU 1571  CD2 LEU A 209     6204   5883   4945   -512   -331   -157       C  
ATOM   1572  N   VAL A 210     -17.850 -21.497  -4.000  1.00 50.95           N  
ANISOU 1572  N   VAL A 210     7064   6859   5438   -600   -645   -129       N  
ATOM   1573  CA  VAL A 210     -19.159 -21.925  -4.488  1.00 50.02           C  
ANISOU 1573  CA  VAL A 210     6932   6789   5284   -634   -745   -161       C  
ATOM   1574  C   VAL A 210     -19.037 -22.530  -5.881  1.00 51.33           C  
ANISOU 1574  C   VAL A 210     7184   6983   5336   -666   -756   -239       C  
ATOM   1575  O   VAL A 210     -19.658 -23.555  -6.187  1.00 51.06           O  
ANISOU 1575  O   VAL A 210     7148   6950   5302   -718   -804   -316       O  
ATOM   1576  CB  VAL A 210     -20.149 -20.745  -4.467  1.00 50.50           C  
ANISOU 1576  CB  VAL A 210     6959   6914   5314   -600   -823    -82       C  
ATOM   1577  CG1 VAL A 210     -21.408 -21.087  -5.250  1.00 53.22           C  
ANISOU 1577  CG1 VAL A 210     7291   7331   5597   -630   -935   -119       C  
ATOM   1578  CG2 VAL A 210     -20.498 -20.369  -3.036  1.00 45.39           C  
ANISOU 1578  CG2 VAL A 210     6223   6239   4784   -574   -820    -23       C  
ATOM   1579  N   ILE A 211     -18.227 -21.912  -6.744  1.00 53.14           N  
ANISOU 1579  N   ILE A 211     7495   7231   5465   -642   -706   -224       N  
ATOM   1580  CA  ILE A 211     -18.037 -22.438  -8.092  1.00 54.90           C  
ANISOU 1580  CA  ILE A 211     7813   7482   5563   -666   -705   -298       C  
ATOM   1581  C   ILE A 211     -17.317 -23.781  -8.046  1.00 58.42           C  
ANISOU 1581  C   ILE A 211     8280   7861   6057   -696   -635   -395       C  
ATOM   1582  O   ILE A 211     -17.656 -24.708  -8.791  1.00 59.64           O  
ANISOU 1582  O   ILE A 211     8482   8021   6156   -737   -668   -486       O  
ATOM   1583  CB  ILE A 211     -17.284 -21.415  -8.961  1.00 50.89           C  
ANISOU 1583  CB  ILE A 211     7392   7006   4938   -630   -648   -248       C  
ATOM   1584  CG1 ILE A 211     -18.138 -20.163  -9.172  1.00 48.71           C  
ANISOU 1584  CG1 ILE A 211     7118   6792   4598   -595   -730   -156       C  
ATOM   1585  CG2 ILE A 211     -16.898 -22.024 -10.299  1.00 45.97           C  
ANISOU 1585  CG2 ILE A 211     6877   6406   4182   -651   -622   -329       C  
ATOM   1586  CD1 ILE A 211     -17.387 -19.012  -9.805  1.00 48.15           C  
ANISOU 1586  CD1 ILE A 211     7132   6731   4432   -560   -661    -84       C  
ATOM   1587  N   ARG A 212     -16.320 -23.912  -7.167  1.00 60.37           N  
ANISOU 1587  N   ARG A 212     8491   8042   6405   -671   -542   -380       N  
ATOM   1588  CA  ARG A 212     -15.595 -25.174  -7.061  1.00 58.21           C  
ANISOU 1588  CA  ARG A 212     8236   7699   6184   -681   -473   -465       C  
ATOM   1589  C   ARG A 212     -16.473 -26.269  -6.466  1.00 56.85           C  
ANISOU 1589  C   ARG A 212     8026   7481   6096   -725   -531   -513       C  
ATOM   1590  O   ARG A 212     -16.420 -27.423  -6.907  1.00 57.50           O  
ANISOU 1590  O   ARG A 212     8158   7519   6170   -756   -518   -608       O  
ATOM   1591  CB  ARG A 212     -14.330 -24.987  -6.225  1.00 56.67           C  
ANISOU 1591  CB  ARG A 212     8000   7454   6076   -635   -371   -431       C  
ATOM   1592  CG  ARG A 212     -13.499 -26.251  -6.083  1.00 59.68           C  
ANISOU 1592  CG  ARG A 212     8397   7763   6515   -624   -296   -510       C  
ATOM   1593  CD  ARG A 212     -13.074 -26.782  -7.443  1.00 68.30           C  
ANISOU 1593  CD  ARG A 212     9590   8867   7496   -634   -251   -597       C  
ATOM   1594  NE  ARG A 212     -12.475 -28.111  -7.357  1.00 69.14           N  
ANISOU 1594  NE  ARG A 212     9720   8893   7655   -621   -189   -684       N  
ATOM   1595  CZ  ARG A 212     -13.150 -29.246  -7.510  1.00 68.15           C  
ANISOU 1595  CZ  ARG A 212     9636   8718   7540   -662   -231   -763       C  
ATOM   1596  NH1 ARG A 212     -14.453 -29.219  -7.757  1.00 69.00           N  
ANISOU 1596  NH1 ARG A 212     9748   8859   7609   -724   -339   -769       N  
ATOM   1597  NH2 ARG A 212     -12.522 -30.410  -7.415  1.00 68.78           N  
ANISOU 1597  NH2 ARG A 212     9749   8713   7671   -640   -164   -837       N  
ATOM   1598  N   VAL A 213     -17.285 -25.927  -5.464  1.00 52.58           N  
ANISOU 1598  N   VAL A 213     7399   6942   5636   -728   -587   -451       N  
ATOM   1599  CA  VAL A 213     -18.180 -26.913  -4.866  1.00 49.76           C  
ANISOU 1599  CA  VAL A 213     7001   6543   5363   -779   -634   -488       C  
ATOM   1600  C   VAL A 213     -19.231 -27.360  -5.875  1.00 54.74           C  
ANISOU 1600  C   VAL A 213     7660   7221   5916   -846   -724   -560       C  
ATOM   1601  O   VAL A 213     -19.593 -28.542  -5.933  1.00 56.53           O  
ANISOU 1601  O   VAL A 213     7903   7396   6178   -905   -736   -642       O  
ATOM   1602  CB  VAL A 213     -18.819 -26.343  -3.586  1.00 43.61           C  
ANISOU 1602  CB  VAL A 213     6122   5768   4679   -764   -664   -401       C  
ATOM   1603  CG1 VAL A 213     -20.012 -27.184  -3.153  1.00 41.30           C  
ANISOU 1603  CG1 VAL A 213     5781   5457   4455   -830   -722   -432       C  
ATOM   1604  CG2 VAL A 213     -17.789 -26.266  -2.468  1.00 37.77           C  
ANISOU 1604  CG2 VAL A 213     5358   4965   4027   -709   -580   -355       C  
ATOM   1605  N   PHE A 214     -19.714 -26.432  -6.705  1.00 53.40           N  
ANISOU 1605  N   PHE A 214     7503   7148   5636   -837   -792   -532       N  
ATOM   1606  CA  PHE A 214     -20.762 -26.751  -7.668  1.00 51.75           C  
ANISOU 1606  CA  PHE A 214     7314   7005   5345   -894   -898   -597       C  
ATOM   1607  C   PHE A 214     -20.316 -27.777  -8.703  1.00 56.28           C  
ANISOU 1607  C   PHE A 214     7994   7549   5840   -933   -873   -717       C  
ATOM   1608  O   PHE A 214     -21.168 -28.428  -9.318  1.00 63.24           O  
ANISOU 1608  O   PHE A 214     8889   8458   6682  -1002   -957   -801       O  
ATOM   1609  CB  PHE A 214     -21.231 -25.475  -8.370  1.00 53.34           C  
ANISOU 1609  CB  PHE A 214     7520   7316   5429   -855   -971   -532       C  
ATOM   1610  CG  PHE A 214     -22.520 -25.637  -9.124  1.00 64.10           C  
ANISOU 1610  CG  PHE A 214     8866   8768   6723   -903  -1108   -580       C  
ATOM   1611  CD1 PHE A 214     -23.729 -25.696  -8.450  1.00 63.27           C  
ANISOU 1611  CD1 PHE A 214     8641   8692   6706   -936  -1191   -564       C  
ATOM   1612  CD2 PHE A 214     -22.524 -25.731 -10.506  1.00 70.09           C  
ANISOU 1612  CD2 PHE A 214     9722   9584   7323   -915  -1153   -643       C  
ATOM   1613  CE1 PHE A 214     -24.917 -25.845  -9.139  1.00 64.93           C  
ANISOU 1613  CE1 PHE A 214     8817   8994   6859   -983  -1324   -613       C  
ATOM   1614  CE2 PHE A 214     -23.710 -25.880 -11.203  1.00 65.67           C  
ANISOU 1614  CE2 PHE A 214     9141   9116   6694   -958  -1292   -692       C  
ATOM   1615  CZ  PHE A 214     -24.908 -25.937 -10.517  1.00 65.10           C  
ANISOU 1615  CZ  PHE A 214     8936   9078   6722   -993  -1381   -678       C  
ATOM   1616  N   LEU A 215     -19.012 -27.942  -8.907  1.00 55.28           N  
ANISOU 1616  N   LEU A 215     7940   7370   5693   -892   -760   -734       N  
ATOM   1617  CA  LEU A 215     -18.493 -28.906  -9.867  1.00 51.10           C  
ANISOU 1617  CA  LEU A 215     7520   6807   5090   -916   -719   -851       C  
ATOM   1618  C   LEU A 215     -18.287 -30.294  -9.271  1.00 52.61           C  
ANISOU 1618  C   LEU A 215     7715   6878   5396   -950   -669   -927       C  
ATOM   1619  O   LEU A 215     -17.777 -31.179  -9.965  1.00 51.55           O  
ANISOU 1619  O   LEU A 215     7676   6695   5217   -963   -621  -1029       O  
ATOM   1620  CB  LEU A 215     -17.172 -28.401 -10.456  1.00 46.40           C  
ANISOU 1620  CB  LEU A 215     6998   6220   4412   -851   -611   -834       C  
ATOM   1621  CG  LEU A 215     -17.233 -27.083 -11.230  1.00 47.74           C  
ANISOU 1621  CG  LEU A 215     7199   6494   4447   -818   -640   -762       C  
ATOM   1622  CD1 LEU A 215     -15.834 -26.597 -11.574  1.00 46.71           C  
ANISOU 1622  CD1 LEU A 215     7123   6356   4269   -761   -507   -735       C  
ATOM   1623  CD2 LEU A 215     -18.079 -27.229 -12.488  1.00 44.74           C  
ANISOU 1623  CD2 LEU A 215     6894   6192   3913   -858   -742   -829       C  
ATOM   1624  N   LEU A 216     -18.668 -30.507  -8.014  1.00 56.46           N  
ANISOU 1624  N   LEU A 216     8114   7312   6027   -962   -674   -879       N  
ATOM   1625  CA  LEU A 216     -18.450 -31.791  -7.362  1.00 53.56           C  
ANISOU 1625  CA  LEU A 216     7759   6818   5772   -986   -619   -935       C  
ATOM   1626  C   LEU A 216     -19.593 -32.747  -7.673  1.00 54.03           C  
ANISOU 1626  C   LEU A 216     7831   6855   5843  -1093   -699  -1028       C  
ATOM   1627  O   LEU A 216     -20.767 -32.369  -7.631  1.00 55.58           O  
ANISOU 1627  O   LEU A 216     7954   7124   6038  -1148   -801  -1007       O  
ATOM   1628  CB  LEU A 216     -18.314 -31.608  -5.851  1.00 53.24           C  
ANISOU 1628  CB  LEU A 216     7630   6728   5871   -948   -583   -838       C  
ATOM   1629  CG  LEU A 216     -16.954 -31.110  -5.357  1.00 56.03           C  
ANISOU 1629  CG  LEU A 216     7979   7063   6249   -849   -485   -775       C  
ATOM   1630  CD1 LEU A 216     -17.053 -30.598  -3.930  1.00 54.81           C  
ANISOU 1630  CD1 LEU A 216     7728   6896   6201   -816   -482   -670       C  
ATOM   1631  CD2 LEU A 216     -15.903 -32.206  -5.465  1.00 56.88           C  
ANISOU 1631  CD2 LEU A 216     8160   7067   6383   -816   -389   -849       C  
ATOM   1632  N   GLU A 217     -19.242 -33.992  -7.990  1.00 55.19           N  
ANISOU 1632  N   GLU A 217     8067   6899   6003  -1124   -650  -1135       N  
ATOM   1633  CA  GLU A 217     -20.237 -34.998  -8.335  1.00 56.56           C  
ANISOU 1633  CA  GLU A 217     8266   7034   6190  -1239   -716  -1241       C  
ATOM   1634  C   GLU A 217     -19.667 -36.379  -8.048  1.00 59.24           C  
ANISOU 1634  C   GLU A 217     8690   7208   6611  -1250   -625  -1317       C  
ATOM   1635  O   GLU A 217     -18.549 -36.688  -8.469  1.00 64.74           O  
ANISOU 1635  O   GLU A 217     9476   7855   7267  -1181   -536  -1359       O  
ATOM   1636  CB  GLU A 217     -20.649 -34.882  -9.808  1.00 57.54           C  
ANISOU 1636  CB  GLU A 217     8456   7252   6154  -1284   -799  -1334       C  
ATOM   1637  CG  GLU A 217     -21.593 -35.974 -10.276  1.00 61.11           C  
ANISOU 1637  CG  GLU A 217     8943   7665   6611  -1412   -872  -1466       C  
ATOM   1638  N   THR A 218     -20.428 -37.192  -7.329  1.00 61.68           N  
ANISOU 1638  N   THR A 218     8969   7431   7037  -1332   -640  -1333       N  
ATOM   1639  CA  THR A 218     -20.083 -38.569  -7.008  1.00 60.28           C  
ANISOU 1639  CA  THR A 218     8879   7079   6946  -1355   -561  -1403       C  
ATOM   1640  C   THR A 218     -21.278 -39.457  -7.299  1.00 60.05           C  
ANISOU 1640  C   THR A 218     8864   7007   6947  -1508   -632  -1506       C  
ATOM   1641  O   THR A 218     -22.397 -38.970  -7.490  1.00 64.56           O  
ANISOU 1641  O   THR A 218     9346   7688   7497  -1590   -741  -1502       O  
ATOM   1642  CB  THR A 218     -19.669 -38.712  -5.532  1.00 62.62           C  
ANISOU 1642  CB  THR A 218     9129   7282   7380  -1292   -482  -1294       C  
ATOM   1643  OG1 THR A 218     -20.802 -38.470  -4.689  1.00 61.80           O  
ANISOU 1643  OG1 THR A 218     8915   7207   7358  -1365   -539  -1226       O  
ATOM   1644  CG2 THR A 218     -18.551 -37.740  -5.180  1.00 62.56           C  
ANISOU 1644  CG2 THR A 218     9087   7334   7350  -1151   -427  -1194       C  
ATOM   1645  N   PRO A 219     -21.074 -40.784  -7.361  1.00 62.84           N  
ANISOU 1645  N   PRO A 219     9327   7197   7351  -1552   -572  -1604       N  
ATOM   1646  CA  PRO A 219     -22.210 -41.702  -7.534  1.00 67.40           C  
ANISOU 1646  CA  PRO A 219     9917   7712   7978  -1715   -630  -1705       C  
ATOM   1647  C   PRO A 219     -23.326 -41.516  -6.514  1.00 75.50           C  
ANISOU 1647  C   PRO A 219    10805   8761   9120  -1798   -675  -1621       C  
ATOM   1648  O   PRO A 219     -24.468 -41.910  -6.769  1.00 79.66           O  
ANISOU 1648  O   PRO A 219    11294   9302   9672  -1945   -754  -1693       O  
ATOM   1649  CB  PRO A 219     -21.570 -43.089  -7.388  1.00 65.66           C  
ANISOU 1649  CB  PRO A 219     9842   7279   7826  -1713   -522  -1782       C  
ATOM   1650  CG  PRO A 219     -20.103 -42.898  -7.617  1.00 64.60           C  
ANISOU 1650  CG  PRO A 219     9784   7128   7632  -1550   -428  -1765       C  
ATOM   1651  CD  PRO A 219     -19.786 -41.433  -7.665  1.00 63.93           C  
ANISOU 1651  CD  PRO A 219     9599   7224   7469  -1458   -461  -1658       C  
ATOM   1652  N   ASN A 220     -23.014 -40.923  -5.359  1.00 78.50           N  
ANISOU 1652  N   ASN A 220    11108   9147   9571  -1708   -624  -1473       N  
ATOM   1653  CA  ASN A 220     -23.992 -40.789  -4.286  1.00 77.40           C  
ANISOU 1653  CA  ASN A 220    10847   9017   9545  -1774   -642  -1388       C  
ATOM   1654  C   ASN A 220     -24.759 -39.476  -4.322  1.00 73.54           C  
ANISOU 1654  C   ASN A 220    10207   8724   9011  -1772   -744  -1316       C  
ATOM   1655  O   ASN A 220     -25.874 -39.416  -3.793  1.00 77.67           O  
ANISOU 1655  O   ASN A 220    10619   9284   9609  -1862   -787  -1287       O  
ATOM   1656  CB  ASN A 220     -23.310 -40.933  -2.921  1.00 78.25           C  
ANISOU 1656  CB  ASN A 220    10961   9017   9754  -1680   -531  -1268       C  
ATOM   1657  CG  ASN A 220     -22.690 -42.300  -2.724  1.00 82.18           C  
ANISOU 1657  CG  ASN A 220    11603   9307  10316  -1680   -431  -1325       C  
ATOM   1658  OD1 ASN A 220     -23.017 -43.251  -3.434  1.00 86.14           O  
ANISOU 1658  OD1 ASN A 220    12190   9724  10817  -1784   -440  -1453       O  
ATOM   1659  ND2 ASN A 220     -21.787 -42.407  -1.757  1.00 79.75           N  
ANISOU 1659  ND2 ASN A 220    11326   8912  10062  -1559   -337  -1231       N  
ATOM   1660  N   GLY A 221     -24.210 -38.431  -4.931  1.00 68.84           N  
ANISOU 1660  N   GLY A 221     9606   8251   8298  -1672   -776  -1287       N  
ATOM   1661  CA  GLY A 221     -24.908 -37.160  -4.917  1.00 64.97           C  
ANISOU 1661  CA  GLY A 221     8984   7933   7768  -1655   -866  -1209       C  
ATOM   1662  C   GLY A 221     -24.308 -36.173  -5.893  1.00 57.53           C  
ANISOU 1662  C   GLY A 221     8074   7109   6676  -1564   -904  -1205       C  
ATOM   1663  O   GLY A 221     -23.328 -36.456  -6.587  1.00 50.33           O  
ANISOU 1663  O   GLY A 221     7280   6154   5688  -1516   -855  -1262       O  
ATOM   1664  N   THR A 222     -24.927 -34.995  -5.930  1.00 54.99           N  
ANISOU 1664  N   THR A 222     7646   6935   6312  -1539   -986  -1132       N  
ATOM   1665  CA  THR A 222     -24.525 -33.897  -6.793  1.00 50.96           C  
ANISOU 1665  CA  THR A 222     7157   6545   5660  -1455  -1028  -1105       C  
ATOM   1666  C   THR A 222     -24.579 -32.614  -5.978  1.00 44.55           C  
ANISOU 1666  C   THR A 222     6244   5808   4876  -1368  -1028   -960       C  
ATOM   1667  O   THR A 222     -25.382 -32.490  -5.050  1.00 48.32           O  
ANISOU 1667  O   THR A 222     6611   6295   5453  -1397  -1045   -903       O  
ATOM   1668  CB  THR A 222     -25.438 -33.802  -8.034  1.00 58.86           C  
ANISOU 1668  CB  THR A 222     8153   7662   6547  -1526  -1164  -1192       C  
ATOM   1669  OG1 THR A 222     -25.297 -34.990  -8.822  1.00 63.37           O  
ANISOU 1669  OG1 THR A 222     8836   8157   7083  -1606  -1160  -1338       O  
ATOM   1670  CG2 THR A 222     -25.093 -32.594  -8.897  1.00 62.00           C  
ANISOU 1670  CG2 THR A 222     8579   8187   6791  -1434  -1207  -1147       C  
ATOM   1671  N   ALA A 223     -23.696 -31.668  -6.309  1.00 43.73           N  
ANISOU 1671  N   ALA A 223     6182   5751   4684  -1264   -999   -904       N  
ATOM   1672  CA  ALA A 223     -23.726 -30.369  -5.645  1.00 45.97           C  
ANISOU 1672  CA  ALA A 223     6383   6102   4980  -1183  -1003   -774       C  
ATOM   1673  C   ALA A 223     -25.082 -29.694  -5.814  1.00 48.39           C  
ANISOU 1673  C   ALA A 223     6585   6533   5269  -1211  -1125   -748       C  
ATOM   1674  O   ALA A 223     -25.563 -29.010  -4.903  1.00 51.05           O  
ANISOU 1674  O   ALA A 223     6821   6900   5675  -1179  -1132   -656       O  
ATOM   1675  CB  ALA A 223     -22.612 -29.478  -6.187  1.00 46.97           C  
ANISOU 1675  CB  ALA A 223     6582   6261   5004  -1086   -958   -733       C  
ATOM   1676  N   ALA A 224     -25.716 -29.875  -6.975  1.00 54.62           N  
ANISOU 1676  N   ALA A 224     7393   7398   5960  -1266  -1226   -830       N  
ATOM   1677  CA  ALA A 224     -27.053 -29.333  -7.183  1.00 53.94           C  
ANISOU 1677  CA  ALA A 224     7196   7439   5859  -1293  -1355   -815       C  
ATOM   1678  C   ALA A 224     -28.106 -30.063  -6.361  1.00 55.26           C  
ANISOU 1678  C   ALA A 224     7244   7582   6168  -1391  -1376   -838       C  
ATOM   1679  O   ALA A 224     -29.163 -29.488  -6.083  1.00 56.94           O  
ANISOU 1679  O   ALA A 224     7328   7892   6414  -1393  -1453   -793       O  
ATOM   1680  CB  ALA A 224     -27.419 -29.385  -8.666  1.00 55.63           C  
ANISOU 1680  CB  ALA A 224     7467   7747   5923  -1324  -1466   -904       C  
ATOM   1681  N   ASP A 225     -27.845 -31.315  -5.972  1.00 58.51           N  
ANISOU 1681  N   ASP A 225     7699   7866   6667  -1470  -1304   -906       N  
ATOM   1682  CA  ASP A 225     -28.779 -32.027  -5.105  1.00 64.13           C  
ANISOU 1682  CA  ASP A 225     8307   8537   7521  -1569  -1300   -917       C  
ATOM   1683  C   ASP A 225     -28.871 -31.361  -3.739  1.00 62.83           C  
ANISOU 1683  C   ASP A 225     8050   8367   7456  -1503  -1238   -787       C  
ATOM   1684  O   ASP A 225     -29.944 -31.333  -3.124  1.00 66.42           O  
ANISOU 1684  O   ASP A 225     8374   8864   7998  -1554  -1268   -762       O  
ATOM   1685  CB  ASP A 225     -28.356 -33.489  -4.958  1.00 72.20           C  
ANISOU 1685  CB  ASP A 225     9421   9401   8610  -1656  -1220  -1007       C  
ATOM   1686  CG  ASP A 225     -28.589 -34.293  -6.219  1.00 84.85           C  
ANISOU 1686  CG  ASP A 225    11096  11009  10135  -1753  -1292  -1156       C  
ATOM   1687  OD1 ASP A 225     -29.216 -33.760  -7.157  1.00 90.79           O  
ANISOU 1687  OD1 ASP A 225    11811  11900  10786  -1763  -1417  -1191       O  
ATOM   1688  OD2 ASP A 225     -28.144 -35.459  -6.270  1.00 88.71           O  
ANISOU 1688  OD2 ASP A 225    11686  11360  10659  -1814  -1227  -1240       O  
ATOM   1689  N   GLY A 226     -27.754 -30.824  -3.245  1.00 57.25           N  
ANISOU 1689  N   GLY A 226     7406   7609   6736  -1393  -1150   -708       N  
ATOM   1690  CA  GLY A 226     -27.789 -30.103  -1.984  1.00 54.46           C  
ANISOU 1690  CA  GLY A 226     6977   7255   6459  -1323  -1098   -589       C  
ATOM   1691  C   GLY A 226     -28.526 -28.782  -2.093  1.00 52.64           C  
ANISOU 1691  C   GLY A 226     6648   7166   6188  -1262  -1180   -519       C  
ATOM   1692  O   GLY A 226     -29.216 -28.368  -1.157  1.00 55.08           O  
ANISOU 1692  O   GLY A 226     6849   7504   6576  -1248  -1172   -451       O  
ATOM   1693  N   LEU A 227     -28.389 -28.101  -3.234  1.00 49.74           N  
ANISOU 1693  N   LEU A 227     6323   6885   5693  -1219  -1254   -534       N  
ATOM   1694  CA  LEU A 227     -29.144 -26.872  -3.452  1.00 48.71           C  
ANISOU 1694  CA  LEU A 227     6108   6886   5514  -1154  -1343   -469       C  
ATOM   1695  C   LEU A 227     -30.635 -27.161  -3.561  1.00 50.90           C  
ANISOU 1695  C   LEU A 227     6247   7254   5838  -1234  -1443   -510       C  
ATOM   1696  O   LEU A 227     -31.464 -26.370  -3.096  1.00 51.41           O  
ANISOU 1696  O   LEU A 227     6192   7401   5939  -1189  -1482   -442       O  
ATOM   1697  CB  LEU A 227     -28.638 -26.160  -4.706  1.00 45.85           C  
ANISOU 1697  CB  LEU A 227     5841   6586   4994  -1091  -1396   -474       C  
ATOM   1698  CG  LEU A 227     -27.223 -25.583  -4.618  1.00 46.93           C  
ANISOU 1698  CG  LEU A 227     6091   6657   5084  -1003  -1298   -418       C  
ATOM   1699  CD1 LEU A 227     -26.706 -25.201  -5.995  1.00 42.10           C  
ANISOU 1699  CD1 LEU A 227     5589   6093   4312   -971  -1336   -445       C  
ATOM   1700  CD2 LEU A 227     -27.184 -24.389  -3.675  1.00 50.85           C  
ANISOU 1700  CD2 LEU A 227     6534   7164   5623   -908  -1264   -297       C  
ATOM   1701  N   ASN A 228     -30.996 -28.292  -4.172  1.00 54.31           N  
ANISOU 1701  N   ASN A 228     6689   7673   6274  -1354  -1485   -625       N  
ATOM   1702  CA  ASN A 228     -32.396 -28.697  -4.201  1.00 59.93           C  
ANISOU 1702  CA  ASN A 228     7256   8465   7050  -1453  -1575   -676       C  
ATOM   1703  C   ASN A 228     -32.890 -29.084  -2.815  1.00 55.75           C  
ANISOU 1703  C   ASN A 228     6622   7877   6683  -1499  -1490   -633       C  
ATOM   1704  O   ASN A 228     -34.061 -28.860  -2.491  1.00 53.15           O  
ANISOU 1704  O   ASN A 228     6134   7639   6419  -1528  -1543   -617       O  
ATOM   1705  CB  ASN A 228     -32.589 -29.856  -5.178  1.00 66.57           C  
ANISOU 1705  CB  ASN A 228     8147   9292   7857  -1583  -1635   -821       C  
ATOM   1706  CG  ASN A 228     -32.830 -29.386  -6.597  1.00 69.37           C  
ANISOU 1706  CG  ASN A 228     8529   9774   8053  -1559  -1775   -871       C  
ATOM   1707  OD1 ASN A 228     -31.969 -28.756  -7.210  1.00 67.32           O  
ANISOU 1707  OD1 ASN A 228     8389   9522   7668  -1462  -1767   -840       O  
ATOM   1708  ND2 ASN A 228     -34.009 -29.689  -7.127  1.00 75.07           N  
ANISOU 1708  ND2 ASN A 228     9141  10603   8778  -1648  -1904   -949       N  
ATOM   1709  N   PHE A 229     -32.018 -29.661  -1.985  1.00 55.01           N  
ANISOU 1709  N   PHE A 229     6613   7636   6651  -1502  -1358   -611       N  
ATOM   1710  CA  PHE A 229     -32.412 -30.003  -0.624  1.00 53.89           C  
ANISOU 1710  CA  PHE A 229     6393   7433   6650  -1536  -1268   -559       C  
ATOM   1711  C   PHE A 229     -32.618 -28.759   0.230  1.00 56.14           C  
ANISOU 1711  C   PHE A 229     6596   7783   6953  -1417  -1247   -437       C  
ATOM   1712  O   PHE A 229     -33.445 -28.768   1.149  1.00 60.01           O  
ANISOU 1712  O   PHE A 229     6966   8291   7543  -1444  -1214   -396       O  
ATOM   1713  CB  PHE A 229     -31.363 -30.916   0.014  1.00 51.26           C  
ANISOU 1713  CB  PHE A 229     6187   6926   6362  -1551  -1139   -561       C  
ATOM   1714  CG  PHE A 229     -31.497 -31.042   1.504  1.00 51.86           C  
ANISOU 1714  CG  PHE A 229     6217   6935   6553  -1544  -1032   -478       C  
ATOM   1715  CD1 PHE A 229     -32.551 -31.746   2.060  1.00 53.45           C  
ANISOU 1715  CD1 PHE A 229     6316   7126   6865  -1659  -1012   -495       C  
ATOM   1716  CD2 PHE A 229     -30.574 -30.448   2.349  1.00 52.65           C  
ANISOU 1716  CD2 PHE A 229     6374   6985   6645  -1425   -951   -385       C  
ATOM   1717  CE1 PHE A 229     -32.680 -31.862   3.431  1.00 56.70           C  
ANISOU 1717  CE1 PHE A 229     6696   7477   7371  -1651   -905   -414       C  
ATOM   1718  CE2 PHE A 229     -30.698 -30.560   3.721  1.00 55.28           C  
ANISOU 1718  CE2 PHE A 229     6674   7261   7067  -1413   -856   -310       C  
ATOM   1719  CZ  PHE A 229     -31.753 -31.267   4.262  1.00 56.74           C  
ANISOU 1719  CZ  PHE A 229     6769   7435   7355  -1523   -829   -321       C  
ATOM   1720  N   LEU A 230     -31.888 -27.684  -0.061  1.00 54.79           N  
ANISOU 1720  N   LEU A 230     6489   7642   6686  -1290  -1259   -380       N  
ATOM   1721  CA  LEU A 230     -31.960 -26.468   0.735  1.00 56.22           C  
ANISOU 1721  CA  LEU A 230     6617   7866   6878  -1173  -1233   -269       C  
ATOM   1722  C   LEU A 230     -33.099 -25.544   0.328  1.00 60.04           C  
ANISOU 1722  C   LEU A 230     6972   8502   7339  -1131  -1342   -245       C  
ATOM   1723  O   LEU A 230     -33.540 -24.733   1.150  1.00 64.41           O  
ANISOU 1723  O   LEU A 230     7443   9093   7936  -1057  -1318   -165       O  
ATOM   1724  CB  LEU A 230     -30.635 -25.702   0.643  1.00 57.95           C  
ANISOU 1724  CB  LEU A 230     6966   8039   7014  -1061  -1191   -218       C  
ATOM   1725  CG  LEU A 230     -30.400 -24.573   1.649  1.00 55.97           C  
ANISOU 1725  CG  LEU A 230     6697   7786   6782   -947  -1136   -111       C  
ATOM   1726  CD1 LEU A 230     -29.625 -25.085   2.850  1.00 57.39           C  
ANISOU 1726  CD1 LEU A 230     6928   7846   7033   -947  -1015    -82       C  
ATOM   1727  CD2 LEU A 230     -29.673 -23.408   0.994  1.00 51.72           C  
ANISOU 1727  CD2 LEU A 230     6239   7278   6135   -843  -1163    -70       C  
ATOM   1728  N   TRP A 231     -33.596 -25.649  -0.906  1.00 58.76           N  
ANISOU 1728  N   TRP A 231     6791   8430   7104  -1171  -1463   -315       N  
ATOM   1729  CA  TRP A 231     -34.560 -24.687  -1.419  1.00 59.05           C  
ANISOU 1729  CA  TRP A 231     6719   8618   7098  -1106  -1581   -287       C  
ATOM   1730  C   TRP A 231     -35.925 -25.268  -1.754  1.00 68.40           C  
ANISOU 1730  C   TRP A 231     7744   9907   8337  -1210  -1679   -360       C  
ATOM   1731  O   TRP A 231     -36.870 -24.491  -1.929  1.00 73.75           O  
ANISOU 1731  O   TRP A 231     8295  10717   9008  -1150  -1769   -328       O  
ATOM   1732  CB  TRP A 231     -33.999 -23.984  -2.665  1.00 56.50           C  
ANISOU 1732  CB  TRP A 231     6509   8341   6616  -1028  -1660   -287       C  
ATOM   1733  CG  TRP A 231     -32.837 -23.096  -2.350  1.00 58.10           C  
ANISOU 1733  CG  TRP A 231     6835   8471   6769   -913  -1576   -201       C  
ATOM   1734  CD1 TRP A 231     -31.526 -23.323  -2.650  1.00 57.88           C  
ANISOU 1734  CD1 TRP A 231     6964   8347   6679   -910  -1509   -216       C  
ATOM   1735  CD2 TRP A 231     -32.879 -21.842  -1.658  1.00 60.94           C  
ANISOU 1735  CD2 TRP A 231     7166   8847   7142   -789  -1546    -93       C  
ATOM   1736  NE1 TRP A 231     -30.750 -22.285  -2.193  1.00 56.02           N  
ANISOU 1736  NE1 TRP A 231     6791   8072   6422   -801  -1443   -125       N  
ATOM   1737  CE2 TRP A 231     -31.557 -21.363  -1.580  1.00 57.58           C  
ANISOU 1737  CE2 TRP A 231     6885   8331   6662   -727  -1465    -50       C  
ATOM   1738  CE3 TRP A 231     -33.908 -21.077  -1.100  1.00 65.76           C  
ANISOU 1738  CE3 TRP A 231     7641   9539   7807   -723  -1577    -32       C  
ATOM   1739  CZ2 TRP A 231     -31.236 -20.154  -0.967  1.00 61.85           C  
ANISOU 1739  CZ2 TRP A 231     7446   8855   7202   -612  -1419     47       C  
ATOM   1740  CZ3 TRP A 231     -33.587 -19.877  -0.492  1.00 64.95           C  
ANISOU 1740  CZ3 TRP A 231     7566   9414   7697   -597  -1527     66       C  
ATOM   1741  CH2 TRP A 231     -32.262 -19.427  -0.430  1.00 63.57           C  
ANISOU 1741  CH2 TRP A 231     7544   9142   7468   -548  -1451    103       C  
ATOM   1742  N   THR A 232     -36.064 -26.588  -1.856  1.00 68.41           N  
ANISOU 1742  N   THR A 232     7745   9853   8393  -1361  -1666   -458       N  
ATOM   1743  CA  THR A 232     -37.390 -27.165  -2.042  1.00 68.65           C  
ANISOU 1743  CA  THR A 232     7606   9979   8497  -1478  -1750   -529       C  
ATOM   1744  C   THR A 232     -38.123 -27.143  -0.706  1.00 70.22           C  
ANISOU 1744  C   THR A 232     7658  10178   8846  -1493  -1663   -469       C  
ATOM   1745  O   THR A 232     -37.717 -27.832   0.238  1.00 64.26           O  
ANISOU 1745  O   THR A 232     6948   9291   8175  -1548  -1530   -454       O  
ATOM   1746  CB  THR A 232     -37.312 -28.591  -2.591  1.00 68.60           C  
ANISOU 1746  CB  THR A 232     7657   9903   8506  -1647  -1760   -660       C  
ATOM   1747  OG1 THR A 232     -36.411 -29.369  -1.792  1.00 70.80           O  
ANISOU 1747  OG1 THR A 232     8052  10002   8846  -1687  -1608   -651       O  
ATOM   1748  CG2 THR A 232     -36.834 -28.582  -4.039  1.00 64.52           C  
ANISOU 1748  CG2 THR A 232     7262   9423   7832  -1635  -1868   -735       C  
ATOM   1749  N   PRO A 233     -39.199 -26.372  -0.588  1.00 75.83           N  
ANISOU 1749  N   PRO A 233     8194  11031   9586  -1437  -1730   -429       N  
ATOM   1750  CA  PRO A 233     -39.849 -26.198   0.712  1.00 74.81           C  
ANISOU 1750  CA  PRO A 233     7930  10907   9587  -1427  -1633   -361       C  
ATOM   1751  C   PRO A 233     -40.721 -27.388   1.085  1.00 76.78           C  
ANISOU 1751  C   PRO A 233     8051  11150   9972  -1610  -1602   -433       C  
ATOM   1752  O   PRO A 233     -41.148 -28.179   0.242  1.00 77.10           O  
ANISOU 1752  O   PRO A 233     8055  11226  10012  -1741  -1693   -542       O  
ATOM   1753  CB  PRO A 233     -40.697 -24.940   0.506  1.00 76.11           C  
ANISOU 1753  CB  PRO A 233     7954  11237   9726  -1295  -1731   -305       C  
ATOM   1754  CG  PRO A 233     -41.057 -24.988  -0.940  1.00 77.96           C  
ANISOU 1754  CG  PRO A 233     8170  11585   9865  -1321  -1906   -386       C  
ATOM   1755  CD  PRO A 233     -39.873 -25.604  -1.651  1.00 77.66           C  
ANISOU 1755  CD  PRO A 233     8347  11431   9729  -1370  -1899   -443       C  
ATOM   1756  N   ASP A 234     -40.977 -27.499   2.387  1.00 78.76           N  
ANISOU 1756  N   ASP A 234     8239  11350  10337  -1621  -1467   -371       N  
ATOM   1757  CA  ASP A 234     -41.849 -28.531   2.948  1.00 81.80           C  
ANISOU 1757  CA  ASP A 234     8494  11722  10864  -1790  -1406   -416       C  
ATOM   1758  C   ASP A 234     -42.795 -27.844   3.929  1.00 81.12           C  
ANISOU 1758  C   ASP A 234     8223  11730  10868  -1727  -1349   -336       C  
ATOM   1759  O   ASP A 234     -42.410 -27.533   5.060  1.00 80.39           O  
ANISOU 1759  O   ASP A 234     8182  11562  10802  -1653  -1213   -245       O  
ATOM   1760  CB  ASP A 234     -41.040 -29.633   3.627  1.00 84.29           C  
ANISOU 1760  CB  ASP A 234     8963  11839  11226  -1885  -1261   -421       C  
ATOM   1761  CG  ASP A 234     -41.908 -30.776   4.125  1.00 89.89           C  
ANISOU 1761  CG  ASP A 234     9559  12515  12079  -2076  -1192   -471       C  
ATOM   1762  OD1 ASP A 234     -43.114 -30.803   3.800  1.00 93.15           O  
ANISOU 1762  OD1 ASP A 234     9770  13066  12556  -2155  -1270   -521       O  
ATOM   1763  OD2 ASP A 234     -41.380 -31.652   4.843  1.00 90.83           O  
ANISOU 1763  OD2 ASP A 234     9793  12471  12249  -2147  -1058   -458       O  
ATOM   1764  N   PHE A 235     -44.032 -27.609   3.491  1.00 80.33           N  
ANISOU 1764  N   PHE A 235     7907  11801  10812  -1754  -1455   -374       N  
ATOM   1765  CA  PHE A 235     -45.025 -26.942   4.322  1.00 78.28           C  
ANISOU 1765  CA  PHE A 235     7450  11652  10642  -1689  -1408   -308       C  
ATOM   1766  C   PHE A 235     -45.598 -27.844   5.406  1.00 81.68           C  
ANISOU 1766  C   PHE A 235     7785  12027  11224  -1834  -1256   -307       C  
ATOM   1767  O   PHE A 235     -46.274 -27.342   6.311  1.00 86.72           O  
ANISOU 1767  O   PHE A 235     8285  12727  11936  -1777  -1173   -240       O  
ATOM   1768  CB  PHE A 235     -46.161 -26.403   3.449  1.00 78.24           C  
ANISOU 1768  CB  PHE A 235     7232  11859  10635  -1662  -1580   -351       C  
ATOM   1769  CG  PHE A 235     -45.692 -25.553   2.302  1.00 78.79           C  
ANISOU 1769  CG  PHE A 235     7396  11991  10549  -1524  -1737   -351       C  
ATOM   1770  CD1 PHE A 235     -45.472 -24.196   2.473  1.00 79.78           C  
ANISOU 1770  CD1 PHE A 235     7553  12155  10604  -1311  -1744   -251       C  
ATOM   1771  CD2 PHE A 235     -45.472 -26.110   1.053  1.00 80.72           C  
ANISOU 1771  CD2 PHE A 235     7708  12248  10713  -1611  -1871   -452       C  
ATOM   1772  CE1 PHE A 235     -45.040 -23.411   1.420  1.00 79.53           C  
ANISOU 1772  CE1 PHE A 235     7620  12171  10428  -1188  -1878   -242       C  
ATOM   1773  CE2 PHE A 235     -45.039 -25.331  -0.003  1.00 82.15           C  
ANISOU 1773  CE2 PHE A 235     7987  12486  10741  -1484  -2007   -445       C  
ATOM   1774  CZ  PHE A 235     -44.823 -23.979   0.181  1.00 80.86           C  
ANISOU 1774  CZ  PHE A 235     7855  12358  10511  -1273  -2008   -336       C  
ATOM   1775  N   GLU A 236     -45.353 -29.155   5.340  1.00 80.50           N  
ANISOU 1775  N   GLU A 236     7710  11755  11120  -2018  -1209   -377       N  
ATOM   1776  CA  GLU A 236     -45.835 -30.046   6.390  1.00 81.85           C  
ANISOU 1776  CA  GLU A 236     7816  11852  11430  -2161  -1050   -367       C  
ATOM   1777  C   GLU A 236     -45.094 -29.820   7.700  1.00 83.73           C  
ANISOU 1777  C   GLU A 236     8192  11960  11663  -2064   -871   -250       C  
ATOM   1778  O   GLU A 236     -45.680 -29.973   8.778  1.00 86.11           O  
ANISOU 1778  O   GLU A 236     8399  12256  12062  -2099   -734   -198       O  
ATOM   1779  CB  GLU A 236     -45.700 -31.503   5.947  1.00 81.71           C  
ANISOU 1779  CB  GLU A 236     7870  11718  11458  -2378  -1046   -471       C  
ATOM   1780  N   LYS A 237     -43.814 -29.458   7.632  1.00 80.90           N  
ANISOU 1780  N   LYS A 237     8051  11499  11187  -1943   -870   -211       N  
ATOM   1781  CA  LYS A 237     -43.019 -29.176   8.819  1.00 78.18           C  
ANISOU 1781  CA  LYS A 237     7845  11039  10821  -1839   -722   -107       C  
ATOM   1782  C   LYS A 237     -43.181 -27.743   9.311  1.00 73.66           C  
ANISOU 1782  C   LYS A 237     7213  10566  10209  -1645   -719    -19       C  
ATOM   1783  O   LYS A 237     -42.472 -27.340  10.240  1.00 71.74           O  
ANISOU 1783  O   LYS A 237     7089  10240   9929  -1540   -615     63       O  
ATOM   1784  CB  LYS A 237     -41.541 -29.465   8.541  1.00 79.79           C  
ANISOU 1784  CB  LYS A 237     8301  11091  10926  -1803   -721   -110       C  
ATOM   1785  CG  LYS A 237     -41.180 -30.942   8.556  1.00 84.17           C  
ANISOU 1785  CG  LYS A 237     8963  11489  11528  -1969   -657   -165       C  
ATOM   1786  CD  LYS A 237     -40.709 -31.382   9.934  1.00 87.22           C  
ANISOU 1786  CD  LYS A 237     9456  11732  11951  -1962   -477    -80       C  
ATOM   1787  CE  LYS A 237     -40.313 -32.851   9.939  1.00 89.19           C  
ANISOU 1787  CE  LYS A 237     9830  11811  12246  -2114   -411   -128       C  
ATOM   1788  NZ  LYS A 237     -39.657 -33.247  11.216  1.00 86.66           N  
ANISOU 1788  NZ  LYS A 237     9650  11342  11936  -2080   -249    -36       N  
ATOM   1789  N   LEU A 238     -44.089 -26.969   8.711  1.00 70.97           N  
ANISOU 1789  N   LEU A 238     6694  10400   9873  -1590   -833    -37       N  
ATOM   1790  CA  LEU A 238     -44.306 -25.598   9.159  1.00 67.45           C  
ANISOU 1790  CA  LEU A 238     6191  10042   9395  -1400   -828     43       C  
ATOM   1791  C   LEU A 238     -44.922 -25.553  10.551  1.00 70.43           C  
ANISOU 1791  C   LEU A 238     6474  10422   9864  -1392   -663    110       C  
ATOM   1792  O   LEU A 238     -44.738 -24.571  11.279  1.00 70.04           O  
ANISOU 1792  O   LEU A 238     6455  10378   9778  -1234   -603    188       O  
ATOM   1793  CB  LEU A 238     -45.199 -24.854   8.166  1.00 66.78           C  
ANISOU 1793  CB  LEU A 238     5931  10144   9299  -1340   -992      9       C  
ATOM   1794  CG  LEU A 238     -44.498 -24.045   7.073  1.00 63.35           C  
ANISOU 1794  CG  LEU A 238     5613   9731   8725  -1217  -1138      4       C  
ATOM   1795  CD1 LEU A 238     -45.496 -23.610   6.011  1.00 64.16           C  
ANISOU 1795  CD1 LEU A 238     5536  10020   8823  -1193  -1310    -42       C  
ATOM   1796  CD2 LEU A 238     -43.785 -22.841   7.667  1.00 57.41           C  
ANISOU 1796  CD2 LEU A 238     4982   8932   7898  -1021  -1083    101       C  
ATOM   1797  N   LYS A 239     -45.653 -26.596  10.938  1.00 73.18           N  
ANISOU 1797  N   LYS A 239     6712  10763  10329  -1564   -582     79       N  
ATOM   1798  CA  LYS A 239     -46.283 -26.653  12.249  1.00 73.56           C  
ANISOU 1798  CA  LYS A 239     6670  10814  10464  -1573   -411    141       C  
ATOM   1799  C   LYS A 239     -45.328 -27.083  13.354  1.00 81.06           C  
ANISOU 1799  C   LYS A 239     7830  11586  11385  -1568   -251    207       C  
ATOM   1800  O   LYS A 239     -45.717 -27.066  14.526  1.00 85.26           O  
ANISOU 1800  O   LYS A 239     8323  12108  11964  -1557    -97    271       O  
ATOM   1801  CB  LYS A 239     -47.482 -27.601  12.210  1.00 68.19           C  
ANISOU 1801  CB  LYS A 239     5782  10201   9927  -1770   -380     83       C  
ATOM   1802  CG  LYS A 239     -47.248 -28.863  11.387  1.00 65.55           C  
ANISOU 1802  CG  LYS A 239     5506   9784   9615  -1968   -442    -12       C  
ATOM   1803  N   ASP A 240     -44.105 -27.466  13.016  1.00 85.54           N  
ANISOU 1803  N   ASP A 240     8613  12017  11870  -1572   -282    195       N  
ATOM   1804  CA  ASP A 240     -43.128 -27.867  14.022  1.00 90.13           C  
ANISOU 1804  CA  ASP A 240     9397  12434  12415  -1553   -147    258       C  
ATOM   1805  C   ASP A 240     -42.596 -26.638  14.746  1.00 88.07           C  
ANISOU 1805  C   ASP A 240     9214  12181  12069  -1351   -113    338       C  
ATOM   1806  O   ASP A 240     -41.967 -25.781  14.111  1.00 89.87           O  
ANISOU 1806  O   ASP A 240     9508  12430  12207  -1232   -222    333       O  
ATOM   1807  CB  ASP A 240     -41.985 -28.639  13.366  1.00 98.99           C  
ANISOU 1807  CB  ASP A 240    10712  13419  13481  -1610   -200    213       C  
ATOM   1808  CG  ASP A 240     -41.011 -29.216  14.377  1.00106.00           C  
ANISOU 1808  CG  ASP A 240    11799  14136  14340  -1600    -68    273       C  
ATOM   1809  OD1 ASP A 240     -41.358 -29.289  15.575  1.00108.86           O  
ANISOU 1809  OD1 ASP A 240    12146  14477  14739  -1594     74    342       O  
ATOM   1810  OD2 ASP A 240     -39.894 -29.600  13.969  1.00106.20           O  
ANISOU 1810  OD2 ASP A 240    11996  14053  14303  -1593   -106    252       O  
ATOM   1811  N   PRO A 241     -42.821 -26.503  16.057  1.00 81.46           N  
ANISOU 1811  N   PRO A 241     8376  11323  11251  -1309     39    411       N  
ATOM   1812  CA  PRO A 241     -42.308 -25.317  16.762  1.00 73.85           C  
ANISOU 1812  CA  PRO A 241     7495  10363  10202  -1119     69    478       C  
ATOM   1813  C   PRO A 241     -40.792 -25.271  16.839  1.00 63.03           C  
ANISOU 1813  C   PRO A 241     6361   8861   8725  -1052     50    495       C  
ATOM   1814  O   PRO A 241     -40.224 -24.178  16.949  1.00 56.70           O  
ANISOU 1814  O   PRO A 241     5629   8071   7842   -901     15    523       O  
ATOM   1815  CB  PRO A 241     -42.940 -25.434  18.159  1.00 76.08           C  
ANISOU 1815  CB  PRO A 241     7730  10646  10532  -1121    248    542       C  
ATOM   1816  CG  PRO A 241     -44.070 -26.415  18.001  1.00 78.84           C  
ANISOU 1816  CG  PRO A 241     7906  11041  11009  -1300    292    507       C  
ATOM   1817  CD  PRO A 241     -43.622 -27.365  16.939  1.00 79.98           C  
ANISOU 1817  CD  PRO A 241     8108  11116  11163  -1434    192    435       C  
ATOM   1818  N   GLY A 242     -40.118 -26.423  16.786  1.00 60.21           N  
ANISOU 1818  N   GLY A 242     6127   8378   8371  -1158     75    479       N  
ATOM   1819  CA  GLY A 242     -38.667 -26.426  16.845  1.00 59.31           C  
ANISOU 1819  CA  GLY A 242     6223   8147   8163  -1092     56    493       C  
ATOM   1820  C   GLY A 242     -38.016 -25.775  15.642  1.00 60.57           C  
ANISOU 1820  C   GLY A 242     6421   8337   8256  -1029    -96    446       C  
ATOM   1821  O   GLY A 242     -36.905 -25.245  15.745  1.00 60.19           O  
ANISOU 1821  O   GLY A 242     6511   8235   8123   -927   -117    466       O  
ATOM   1822  N   VAL A 243     -38.689 -25.803  14.491  1.00 60.63           N  
ANISOU 1822  N   VAL A 243     6305   8433   8297  -1091   -202    382       N  
ATOM   1823  CA  VAL A 243     -38.149 -25.153  13.301  1.00 58.21           C  
ANISOU 1823  CA  VAL A 243     6035   8163   7917  -1030   -344    343       C  
ATOM   1824  C   VAL A 243     -38.215 -23.638  13.447  1.00 57.83           C  
ANISOU 1824  C   VAL A 243     5960   8196   7816   -865   -376    387       C  
ATOM   1825  O   VAL A 243     -37.269 -22.924  13.092  1.00 54.09           O  
ANISOU 1825  O   VAL A 243     5600   7694   7257   -770   -431    394       O  
ATOM   1826  CB  VAL A 243     -38.895 -25.636  12.044  1.00 57.69           C  
ANISOU 1826  CB  VAL A 243     5851   8175   7892  -1142   -454    261       C  
ATOM   1827  CG1 VAL A 243     -38.310 -24.991  10.797  1.00 57.94           C  
ANISOU 1827  CG1 VAL A 243     5938   8242   7832  -1076   -595    225       C  
ATOM   1828  CG2 VAL A 243     -38.835 -27.153  11.944  1.00 59.07           C  
ANISOU 1828  CG2 VAL A 243     6065   8253   8125  -1313   -413    212       C  
ATOM   1829  N   TRP A 244     -39.330 -23.122  13.973  1.00 59.49           N  
ANISOU 1829  N   TRP A 244     6020   8504   8080   -828   -336    416       N  
ATOM   1830  CA  TRP A 244     -39.458 -21.684  14.180  1.00 58.33           C  
ANISOU 1830  CA  TRP A 244     5851   8424   7889   -663   -356    458       C  
ATOM   1831  C   TRP A 244     -38.472 -21.176  15.223  1.00 60.80           C  
ANISOU 1831  C   TRP A 244     6324   8642   8136   -563   -272    512       C  
ATOM   1832  O   TRP A 244     -37.976 -20.049  15.108  1.00 64.03           O  
ANISOU 1832  O   TRP A 244     6797   9054   8477   -437   -316    531       O  
ATOM   1833  CB  TRP A 244     -40.887 -21.338  14.594  1.00 55.95           C  
ANISOU 1833  CB  TRP A 244     5347   8245   7665   -644   -316    474       C  
ATOM   1834  CG  TRP A 244     -41.898 -21.593  13.523  1.00 56.71           C  
ANISOU 1834  CG  TRP A 244     5265   8462   7820   -718   -422    418       C  
ATOM   1835  CD1 TRP A 244     -42.635 -22.727  13.345  1.00 59.52           C  
ANISOU 1835  CD1 TRP A 244     5502   8844   8267   -883   -408    372       C  
ATOM   1836  CD2 TRP A 244     -42.286 -20.693  12.479  1.00 60.31           C  
ANISOU 1836  CD2 TRP A 244     5643   9029   8245   -631   -563    401       C  
ATOM   1837  NE1 TRP A 244     -43.458 -22.589  12.254  1.00 64.22           N  
ANISOU 1837  NE1 TRP A 244     5941   9570   8890   -907   -541    320       N  
ATOM   1838  CE2 TRP A 244     -43.263 -21.349  11.705  1.00 64.38           C  
ANISOU 1838  CE2 TRP A 244     5985   9646   8831   -747   -639    340       C  
ATOM   1839  CE3 TRP A 244     -41.904 -19.395  12.125  1.00 60.38           C  
ANISOU 1839  CE3 TRP A 244     5715   9057   8170   -467   -633    432       C  
ATOM   1840  CZ2 TRP A 244     -43.862 -20.753  10.597  1.00 65.41           C  
ANISOU 1840  CZ2 TRP A 244     6003   9907   8943   -694   -791    312       C  
ATOM   1841  CZ3 TRP A 244     -42.499 -18.806  11.024  1.00 61.42           C  
ANISOU 1841  CZ3 TRP A 244     5746   9306   8285   -413   -773    412       C  
ATOM   1842  CH2 TRP A 244     -43.467 -19.484  10.274  1.00 63.69           C  
ANISOU 1842  CH2 TRP A 244     5859   9703   8636   -521   -855    353       C  
ATOM   1843  N   ILE A 245     -38.178 -21.985  16.242  1.00 57.60           N  
ANISOU 1843  N   ILE A 245     5988   8150   7749   -618   -155    537       N  
ATOM   1844  CA  ILE A 245     -37.207 -21.582  17.254  1.00 52.65           C  
ANISOU 1844  CA  ILE A 245     5515   7437   7053   -527    -85    583       C  
ATOM   1845  C   ILE A 245     -35.812 -21.491  16.649  1.00 49.66           C  
ANISOU 1845  C   ILE A 245     5291   6979   6597   -503   -163    562       C  
ATOM   1846  O   ILE A 245     -35.069 -20.536  16.907  1.00 45.37           O  
ANISOU 1846  O   ILE A 245     4840   6414   5986   -393   -177    582       O  
ATOM   1847  CB  ILE A 245     -37.249 -22.554  18.447  1.00 50.60           C  
ANISOU 1847  CB  ILE A 245     5297   7106   6822   -591     53    619       C  
ATOM   1848  CG1 ILE A 245     -38.584 -22.433  19.185  1.00 53.04           C  
ANISOU 1848  CG1 ILE A 245     5456   7499   7198   -594    151    648       C  
ATOM   1849  CG2 ILE A 245     -36.090 -22.295  19.396  1.00 47.09           C  
ANISOU 1849  CG2 ILE A 245     5028   6569   6294   -506    103    657       C  
ATOM   1850  CD1 ILE A 245     -38.778 -23.473  20.265  1.00 54.91           C  
ANISOU 1850  CD1 ILE A 245     5724   7671   7469   -676    297    686       C  
ATOM   1851  N   ALA A 246     -35.436 -22.474  15.827  1.00 48.47           N  
ANISOU 1851  N   ALA A 246     5171   6786   6460   -609   -211    517       N  
ATOM   1852  CA  ALA A 246     -34.113 -22.459  15.212  1.00 45.74           C  
ANISOU 1852  CA  ALA A 246     4962   6369   6046   -590   -275    494       C  
ATOM   1853  C   ALA A 246     -33.983 -21.348  14.179  1.00 47.72           C  
ANISOU 1853  C   ALA A 246     5201   6685   6247   -516   -385    476       C  
ATOM   1854  O   ALA A 246     -32.883 -20.824  13.972  1.00 52.19           O  
ANISOU 1854  O   ALA A 246     5879   7203   6745   -456   -416    477       O  
ATOM   1855  CB  ALA A 246     -33.813 -23.814  14.572  1.00 38.16           C  
ANISOU 1855  CB  ALA A 246     4038   5347   5115   -717   -291    446       C  
ATOM   1856  N   ALA A 247     -35.084 -20.977  13.524  1.00 47.15           N  
ANISOU 1856  N   ALA A 247     4990   6718   6205   -519   -444    462       N  
ATOM   1857  CA  ALA A 247     -35.021 -19.935  12.504  1.00 42.60           C  
ANISOU 1857  CA  ALA A 247     4410   6202   5575   -443   -551    453       C  
ATOM   1858  C   ALA A 247     -34.826 -18.561  13.133  1.00 45.22           C  
ANISOU 1858  C   ALA A 247     4781   6537   5866   -299   -527    504       C  
ATOM   1859  O   ALA A 247     -33.965 -17.786  12.701  1.00 51.91           O  
ANISOU 1859  O   ALA A 247     5728   7351   6643   -234   -572    509       O  
ATOM   1860  CB  ALA A 247     -36.286 -19.964  11.646  1.00 41.13           C  
ANISOU 1860  CB  ALA A 247     4061   6136   5430   -479   -630    424       C  
ATOM   1861  N   VAL A 248     -35.618 -18.243  14.158  1.00 47.83           N  
ANISOU 1861  N   VAL A 248     5036   6900   6237   -252   -450    539       N  
ATOM   1862  CA  VAL A 248     -35.505 -16.940  14.807  1.00 47.52           C  
ANISOU 1862  CA  VAL A 248     5037   6858   6159   -114   -421    580       C  
ATOM   1863  C   VAL A 248     -34.157 -16.805  15.501  1.00 50.36           C  
ANISOU 1863  C   VAL A 248     5565   7108   6461    -87   -376    591       C  
ATOM   1864  O   VAL A 248     -33.509 -15.753  15.429  1.00 52.49           O  
ANISOU 1864  O   VAL A 248     5921   7350   6675      0   -402    602       O  
ATOM   1865  CB  VAL A 248     -36.675 -16.731  15.784  1.00 45.29           C  
ANISOU 1865  CB  VAL A 248     4637   6638   5934    -73   -335    609       C  
ATOM   1866  CG1 VAL A 248     -36.493 -15.440  16.566  1.00 42.15           C  
ANISOU 1866  CG1 VAL A 248     4302   6220   5492     71   -293    644       C  
ATOM   1867  CG2 VAL A 248     -37.989 -16.719  15.027  1.00 43.78           C  
ANISOU 1867  CG2 VAL A 248     4262   6570   5802    -86   -395    595       C  
ATOM   1868  N   GLY A 249     -33.709 -17.863  16.179  1.00 51.65           N  
ANISOU 1868  N   GLY A 249     5778   7209   6638   -162   -309    589       N  
ATOM   1869  CA  GLY A 249     -32.388 -17.833  16.783  1.00 50.33           C  
ANISOU 1869  CA  GLY A 249     5761   6948   6415   -137   -281    595       C  
ATOM   1870  C   GLY A 249     -31.287 -17.650  15.756  1.00 44.82           C  
ANISOU 1870  C   GLY A 249     5147   6212   5669   -145   -365    566       C  
ATOM   1871  O   GLY A 249     -30.299 -16.955  16.006  1.00 40.04           O  
ANISOU 1871  O   GLY A 249     4642   5558   5012    -87   -369    570       O  
ATOM   1872  N   GLN A 250     -31.445 -18.266  14.583  1.00 47.92           N  
ANISOU 1872  N   GLN A 250     5499   6629   6078   -221   -430    532       N  
ATOM   1873  CA  GLN A 250     -30.481 -18.055  13.510  1.00 43.73           C  
ANISOU 1873  CA  GLN A 250     5045   6073   5497   -226   -503    504       C  
ATOM   1874  C   GLN A 250     -30.518 -16.614  13.016  1.00 47.66           C  
ANISOU 1874  C   GLN A 250     5553   6605   5951   -132   -554    521       C  
ATOM   1875  O   GLN A 250     -29.467 -16.004  12.793  1.00 46.47           O  
ANISOU 1875  O   GLN A 250     5501   6407   5749    -98   -570    521       O  
ATOM   1876  CB  GLN A 250     -30.752 -19.027  12.362  1.00 38.53           C  
ANISOU 1876  CB  GLN A 250     4343   5438   4857   -325   -559    459       C  
ATOM   1877  CG  GLN A 250     -29.923 -18.774  11.113  1.00 40.72           C  
ANISOU 1877  CG  GLN A 250     4691   5707   5074   -328   -633    429       C  
ATOM   1878  CD  GLN A 250     -28.444 -19.039  11.322  1.00 48.11           C  
ANISOU 1878  CD  GLN A 250     5749   6553   5978   -331   -603    419       C  
ATOM   1879  OE1 GLN A 250     -28.052 -19.794  12.213  1.00 49.90           O  
ANISOU 1879  OE1 GLN A 250     6007   6722   6231   -354   -540    422       O  
ATOM   1880  NE2 GLN A 250     -27.611 -18.417  10.494  1.00 50.24           N  
ANISOU 1880  NE2 GLN A 250     6086   6813   6189   -304   -645    408       N  
ATOM   1881  N   ILE A 251     -31.719 -16.050  12.856  1.00 48.20           N  
ANISOU 1881  N   ILE A 251     5518   6753   6042    -88   -577    539       N  
ATOM   1882  CA  ILE A 251     -31.848 -14.678  12.370  1.00 45.15           C  
ANISOU 1882  CA  ILE A 251     5146   6394   5616     13   -625    563       C  
ATOM   1883  C   ILE A 251     -31.205 -13.699  13.345  1.00 44.18           C  
ANISOU 1883  C   ILE A 251     5116   6206   5465     98   -569    589       C  
ATOM   1884  O   ILE A 251     -30.545 -12.735  12.936  1.00 44.81           O  
ANISOU 1884  O   ILE A 251     5281   6250   5496    150   -598    597       O  
ATOM   1885  CB  ILE A 251     -33.331 -14.343  12.118  1.00 46.55           C  
ANISOU 1885  CB  ILE A 251     5181   6675   5831     55   -658    578       C  
ATOM   1886  CG1 ILE A 251     -33.845 -15.089  10.886  1.00 50.58           C  
ANISOU 1886  CG1 ILE A 251     5612   7254   6349    -24   -744    543       C  
ATOM   1887  CG2 ILE A 251     -33.527 -12.845  11.945  1.00 43.63           C  
ANISOU 1887  CG2 ILE A 251     4835   6317   5426    187   -685    615       C  
ATOM   1888  CD1 ILE A 251     -33.188 -14.656   9.594  1.00 48.82           C  
ANISOU 1888  CD1 ILE A 251     5473   7024   6050    -13   -831    534       C  
ATOM   1889  N   PHE A 252     -31.383 -13.930  14.649  1.00 44.52           N  
ANISOU 1889  N   PHE A 252     5150   6232   5536    109   -486    600       N  
ATOM   1890  CA  PHE A 252     -30.777 -13.053  15.647  1.00 43.65           C  
ANISOU 1890  CA  PHE A 252     5132   6062   5392    185   -436    614       C  
ATOM   1891  C   PHE A 252     -29.256 -13.089  15.564  1.00 37.93           C  
ANISOU 1891  C   PHE A 252     4532   5257   4623    154   -448    593       C  
ATOM   1892  O   PHE A 252     -28.592 -12.059  15.725  1.00 38.71           O  
ANISOU 1892  O   PHE A 252     4714   5309   4683    209   -451    595       O  
ATOM   1893  CB  PHE A 252     -31.237 -13.454  17.049  1.00 47.62           C  
ANISOU 1893  CB  PHE A 252     5608   6566   5920    195   -343    628       C  
ATOM   1894  CG  PHE A 252     -32.448 -12.706  17.531  1.00 52.42           C  
ANISOU 1894  CG  PHE A 252     6135   7230   6552    283   -305    652       C  
ATOM   1895  CD1 PHE A 252     -32.319 -11.464  18.130  1.00 48.87           C  
ANISOU 1895  CD1 PHE A 252     5751   6750   6068    390   -280    663       C  
ATOM   1896  CD2 PHE A 252     -33.714 -13.251  17.396  1.00 58.20           C  
ANISOU 1896  CD2 PHE A 252     6720   8046   7345    257   -292    661       C  
ATOM   1897  CE1 PHE A 252     -33.430 -10.777  18.577  1.00 50.86           C  
ANISOU 1897  CE1 PHE A 252     5930   7051   6343    483   -239    683       C  
ATOM   1898  CE2 PHE A 252     -34.829 -12.568  17.843  1.00 58.06           C  
ANISOU 1898  CE2 PHE A 252     6614   8089   7355    346   -252    682       C  
ATOM   1899  CZ  PHE A 252     -34.686 -11.330  18.434  1.00 53.20           C  
ANISOU 1899  CZ  PHE A 252     6071   7440   6702    465   -223    694       C  
ATOM   1900  N   PHE A 253     -28.688 -14.267  15.304  1.00 37.31           N  
ANISOU 1900  N   PHE A 253     4464   5160   4553     64   -454    571       N  
ATOM   1901  CA  PHE A 253     -27.238 -14.423  15.321  1.00 38.61           C  
ANISOU 1901  CA  PHE A 253     4729   5257   4684     38   -458    549       C  
ATOM   1902  C   PHE A 253     -26.584 -13.784  14.100  1.00 40.57           C  
ANISOU 1902  C   PHE A 253     5022   5495   4897     36   -519    536       C  
ATOM   1903  O   PHE A 253     -25.611 -13.033  14.233  1.00 47.51           O  
ANISOU 1903  O   PHE A 253     5982   6326   5744     61   -518    531       O  
ATOM   1904  CB  PHE A 253     -26.876 -15.907  15.409  1.00 41.17           C  
ANISOU 1904  CB  PHE A 253     5051   5560   5030    -44   -441    530       C  
ATOM   1905  CG  PHE A 253     -25.448 -16.160  15.797  1.00 43.58           C  
ANISOU 1905  CG  PHE A 253     5447   5802   5310    -53   -431    513       C  
ATOM   1906  CD1 PHE A 253     -25.096 -16.311  17.128  1.00 42.82           C  
ANISOU 1906  CD1 PHE A 253     5392   5675   5204    -23   -381    525       C  
ATOM   1907  CD2 PHE A 253     -24.456 -16.248  14.833  1.00 45.19           C  
ANISOU 1907  CD2 PHE A 253     5691   5984   5494    -86   -472    484       C  
ATOM   1908  CE1 PHE A 253     -23.785 -16.541  17.492  1.00 43.80           C  
ANISOU 1908  CE1 PHE A 253     5587   5751   5303    -23   -384    507       C  
ATOM   1909  CE2 PHE A 253     -23.141 -16.478  15.190  1.00 41.86           C  
ANISOU 1909  CE2 PHE A 253     5335   5514   5055    -89   -464    465       C  
ATOM   1910  CZ  PHE A 253     -22.805 -16.625  16.522  1.00 41.96           C  
ANISOU 1910  CZ  PHE A 253     5380   5501   5063    -56   -426    476       C  
ATOM   1911  N   THR A 254     -27.104 -14.068  12.902  1.00 43.18           N  
ANISOU 1911  N   THR A 254     5305   5872   5230      2   -571    530       N  
ATOM   1912  CA  THR A 254     -26.428 -13.627  11.685  1.00 44.67           C  
ANISOU 1912  CA  THR A 254     5547   6050   5374     -8   -621    520       C  
ATOM   1913  C   THR A 254     -26.488 -12.116  11.509  1.00 40.93           C  
ANISOU 1913  C   THR A 254     5117   5567   4868     73   -635    551       C  
ATOM   1914  O   THR A 254     -25.559 -11.524  10.950  1.00 42.21           O  
ANISOU 1914  O   THR A 254     5359   5687   4991     72   -646    548       O  
ATOM   1915  CB  THR A 254     -27.027 -14.313  10.455  1.00 51.90           C  
ANISOU 1915  CB  THR A 254     6408   7024   6287    -61   -678    503       C  
ATOM   1916  OG1 THR A 254     -26.543 -13.670   9.268  1.00 62.10           O  
ANISOU 1916  OG1 THR A 254     7759   8316   7521    -51   -725    504       O  
ATOM   1917  CG2 THR A 254     -28.543 -14.229  10.470  1.00 50.61           C  
ANISOU 1917  CG2 THR A 254     6136   6938   6156    -33   -702    522       C  
ATOM   1918  N   LEU A 255     -27.559 -11.478  11.969  1.00 36.31           N  
ANISOU 1918  N   LEU A 255     4481   5014   4301    146   -629    580       N  
ATOM   1919  CA  LEU A 255     -27.723 -10.041  11.803  1.00 39.63           C  
ANISOU 1919  CA  LEU A 255     4947   5416   4694    235   -641    613       C  
ATOM   1920  C   LEU A 255     -27.199  -9.240  12.988  1.00 43.71           C  
ANISOU 1920  C   LEU A 255     5535   5863   5210    284   -584    614       C  
ATOM   1921  O   LEU A 255     -27.362  -8.015  13.005  1.00 47.38           O  
ANISOU 1921  O   LEU A 255     6047   6297   5658    361   -582    637       O  
ATOM   1922  CB  LEU A 255     -29.197  -9.704  11.563  1.00 44.98           C  
ANISOU 1922  CB  LEU A 255     5529   6170   5390    304   -671    643       C  
ATOM   1923  CG  LEU A 255     -29.792 -10.072  10.203  1.00 49.07           C  
ANISOU 1923  CG  LEU A 255     5989   6763   5892    281   -752    645       C  
ATOM   1924  CD1 LEU A 255     -31.257  -9.678  10.148  1.00 53.55           C  
ANISOU 1924  CD1 LEU A 255     6446   7414   6486    362   -783    674       C  
ATOM   1925  CD2 LEU A 255     -29.016  -9.404   9.083  1.00 48.89           C  
ANISOU 1925  CD2 LEU A 255     6071   6703   5802    287   -792    658       C  
ATOM   1926  N   SER A 256     -26.577  -9.900  13.968  1.00 44.72           N  
ANISOU 1926  N   SER A 256     5677   5963   5351    242   -540    587       N  
ATOM   1927  CA  SER A 256     -26.022  -9.240  15.153  1.00 41.91           C  
ANISOU 1927  CA  SER A 256     5391   5549   4986    281   -494    578       C  
ATOM   1928  C   SER A 256     -27.101  -8.492  15.934  1.00 45.70           C  
ANISOU 1928  C   SER A 256     5845   6042   5476    376   -460    600       C  
ATOM   1929  O   SER A 256     -26.869  -7.400  16.459  1.00 50.06           O  
ANISOU 1929  O   SER A 256     6471   6540   6009    436   -438    598       O  
ATOM   1930  CB  SER A 256     -24.871  -8.301  14.782  1.00 37.35           C  
ANISOU 1930  CB  SER A 256     4916   4900   4375    275   -506    566       C  
ATOM   1931  OG  SER A 256     -23.912  -8.964  13.975  1.00 39.83           O  
ANISOU 1931  OG  SER A 256     5244   5210   4681    193   -530    545       O  
ATOM   1932  N   LEU A 257     -28.290  -9.084  16.014  1.00 44.92           N  
ANISOU 1932  N   LEU A 257     5641   6017   5412    388   -450    618       N  
ATOM   1933  CA  LEU A 257     -29.395  -8.507  16.766  1.00 48.60           C  
ANISOU 1933  CA  LEU A 257     6060   6510   5894    480   -407    638       C  
ATOM   1934  C   LEU A 257     -29.318  -8.932  18.225  1.00 48.99           C  
ANISOU 1934  C   LEU A 257     6124   6548   5944    480   -333    625       C  
ATOM   1935  O   LEU A 257     -29.019 -10.089  18.533  1.00 44.80           O  
ANISOU 1935  O   LEU A 257     5573   6025   5421    406   -317    616       O  
ATOM   1936  CB  LEU A 257     -30.739  -8.932  16.173  1.00 47.50           C  
ANISOU 1936  CB  LEU A 257     5783   6466   5797    490   -430    661       C  
ATOM   1937  CG  LEU A 257     -30.811  -8.982  14.649  1.00 48.42           C  
ANISOU 1937  CG  LEU A 257     5874   6616   5906    462   -516    668       C  
ATOM   1938  CD1 LEU A 257     -32.125  -9.592  14.179  1.00 45.38           C  
ANISOU 1938  CD1 LEU A 257     5337   6337   5566    455   -545    678       C  
ATOM   1939  CD2 LEU A 257     -30.622  -7.589  14.073  1.00 48.37           C  
ANISOU 1939  CD2 LEU A 257     5949   6567   5863    547   -549    691       C  
ATOM   1940  N   GLY A 258     -29.602  -7.990  19.122  1.00 53.84           N  
ANISOU 1940  N   GLY A 258     6778   7136   6542    570   -285    626       N  
ATOM   1941  CA  GLY A 258     -29.489  -8.241  20.542  1.00 58.82           C  
ANISOU 1941  CA  GLY A 258     7443   7753   7153    583   -214    613       C  
ATOM   1942  C   GLY A 258     -28.074  -8.335  21.065  1.00 59.71           C  
ANISOU 1942  C   GLY A 258     7667   7799   7221    538   -223    579       C  
ATOM   1943  O   GLY A 258     -27.891  -8.554  22.268  1.00 58.22           O  
ANISOU 1943  O   GLY A 258     7519   7600   7002    552   -173    567       O  
ATOM   1944  N   PHE A 259     -27.069  -8.182  20.206  1.00 59.87           N  
ANISOU 1944  N   PHE A 259     7734   7779   7233    487   -284    563       N  
ATOM   1945  CA  PHE A 259     -25.672  -8.223  20.612  1.00 58.13           C  
ANISOU 1945  CA  PHE A 259     7603   7505   6979    443   -300    526       C  
ATOM   1946  C   PHE A 259     -25.112  -6.848  20.943  1.00 61.70           C  
ANISOU 1946  C   PHE A 259     8156   7887   7400    487   -303    496       C  
ATOM   1947  O   PHE A 259     -23.910  -6.736  21.197  1.00 62.68           O  
ANISOU 1947  O   PHE A 259     8347   7969   7501    446   -325    458       O  
ATOM   1948  CB  PHE A 259     -24.814  -8.860  19.514  1.00 54.66           C  
ANISOU 1948  CB  PHE A 259     7153   7062   6552    356   -354    518       C  
ATOM   1949  CG  PHE A 259     -25.056 -10.328  19.324  1.00 55.80           C  
ANISOU 1949  CG  PHE A 259     7225   7254   6723    297   -352    531       C  
ATOM   1950  CD1 PHE A 259     -24.368 -11.262  20.081  1.00 57.73           C  
ANISOU 1950  CD1 PHE A 259     7491   7489   6955    263   -337    518       C  
ATOM   1951  CD2 PHE A 259     -25.963 -10.776  18.379  1.00 59.17           C  
ANISOU 1951  CD2 PHE A 259     7566   7730   7184    278   -369    555       C  
ATOM   1952  CE1 PHE A 259     -24.587 -12.615  19.903  1.00 61.19           C  
ANISOU 1952  CE1 PHE A 259     7877   7954   7420    209   -329    532       C  
ATOM   1953  CE2 PHE A 259     -26.187 -12.127  18.196  1.00 63.27           C  
ANISOU 1953  CE2 PHE A 259     8026   8281   7732    213   -365    560       C  
ATOM   1954  CZ  PHE A 259     -25.497 -13.048  18.959  1.00 65.60           C  
ANISOU 1954  CZ  PHE A 259     8353   8553   8018    179   -340    549       C  
ATOM   1955  N   GLY A 260     -25.935  -5.802  20.914  1.00 62.16           N  
ANISOU 1955  N   GLY A 260     8224   7932   7462    570   -282    510       N  
ATOM   1956  CA  GLY A 260     -25.477  -4.461  21.227  1.00 60.82           C  
ANISOU 1956  CA  GLY A 260     8162   7681   7266    613   -278    480       C  
ATOM   1957  C   GLY A 260     -24.357  -3.950  20.342  1.00 61.11           C  
ANISOU 1957  C   GLY A 260     8261   7656   7303    550   -326    463       C  
ATOM   1958  O   GLY A 260     -23.777  -2.895  20.617  1.00 63.38           O  
ANISOU 1958  O   GLY A 260     8645   7864   7574    560   -323    430       O  
ATOM   1959  N   ALA A 261     -24.039  -4.688  19.277  1.00 56.44           N  
ANISOU 1959  N   ALA A 261     7617   7097   6731    480   -365    482       N  
ATOM   1960  CA  ALA A 261     -22.975  -4.302  18.360  1.00 50.59           C  
ANISOU 1960  CA  ALA A 261     6926   6306   5989    414   -400    471       C  
ATOM   1961  C   ALA A 261     -23.453  -3.349  17.276  1.00 53.01           C  
ANISOU 1961  C   ALA A 261     7261   6580   6299    454   -411    510       C  
ATOM   1962  O   ALA A 261     -22.692  -2.473  16.851  1.00 57.93           O  
ANISOU 1962  O   ALA A 261     7968   7128   6916    428   -415    501       O  
ATOM   1963  CB  ALA A 261     -22.360  -5.545  17.712  1.00 43.33           C  
ANISOU 1963  CB  ALA A 261     5948   5434   5080    326   -429    469       C  
ATOM   1964  N   ILE A 262     -24.697  -3.506  16.818  1.00 49.49           N  
ANISOU 1964  N   ILE A 262     6746   6191   5866    515   -416    557       N  
ATOM   1965  CA  ILE A 262     -25.262  -2.567  15.854  1.00 46.86           C  
ANISOU 1965  CA  ILE A 262     6442   5833   5529    577   -433    602       C  
ATOM   1966  C   ILE A 262     -25.388  -1.184  16.477  1.00 51.12           C  
ANISOU 1966  C   ILE A 262     7080   6282   6062    659   -398    595       C  
ATOM   1967  O   ILE A 262     -25.174  -0.162  15.813  1.00 35.04           O  
ANISOU 1967  O   ILE A 262     5131   4169   4015    681   -403    617       O  
ATOM   1968  CB  ILE A 262     -26.620  -3.089  15.343  1.00 46.92           C  
ANISOU 1968  CB  ILE A 262     6336   5938   5554    632   -456    646       C  
ATOM   1969  CG1 ILE A 262     -26.430  -4.362  14.518  1.00 45.01           C  
ANISOU 1969  CG1 ILE A 262     6017   5768   5315    540   -497    647       C  
ATOM   1970  CG2 ILE A 262     -27.347  -2.028  14.527  1.00 35.07           C  
ANISOU 1970  CG2 ILE A 262     4864   4417   4045    727   -477    697       C  
ATOM   1971  CD1 ILE A 262     -27.730  -5.022  14.125  1.00 44.98           C  
ANISOU 1971  CD1 ILE A 262     5888   5867   5334    572   -523    675       C  
ATOM   1972  N   ILE A 263     -25.715  -1.132  17.770  1.00 50.41           N  
ANISOU 1972  N   ILE A 263     6990   6192   5973    706   -356    565       N  
ATOM   1973  CA  ILE A 263     -25.957   0.144  18.436  1.00 49.62           C  
ANISOU 1973  CA  ILE A 263     6984   6006   5864    795   -316    550       C  
ATOM   1974  C   ILE A 263     -24.678   0.971  18.496  1.00 52.25           C  
ANISOU 1974  C   ILE A 263     7448   6224   6183    731   -315    507       C  
ATOM   1975  O   ILE A 263     -24.661   2.146  18.112  1.00 61.29           O  
ANISOU 1975  O   ILE A 263     8689   7272   7326    773   -305    521       O  
ATOM   1976  CB  ILE A 263     -26.547  -0.092  19.838  1.00 44.81           C  
ANISOU 1976  CB  ILE A 263     6346   5431   5248    853   -266    521       C  
ATOM   1977  CG1 ILE A 263     -27.973  -0.636  19.737  1.00 38.51           C  
ANISOU 1977  CG1 ILE A 263     5419   4736   4476    929   -253    567       C  
ATOM   1978  CG2 ILE A 263     -26.527   1.186  20.650  1.00 43.60           C  
ANISOU 1978  CG2 ILE A 263     6313   5176   5076    928   -223    484       C  
ATOM   1979  CD1 ILE A 263     -28.063  -2.137  19.889  1.00 37.36           C  
ANISOU 1979  CD1 ILE A 263     5160   4693   4342    855   -259    570       C  
ATOM   1980  N   THR A 264     -23.586   0.370  18.976  1.00 50.35           N  
ANISOU 1980  N   THR A 264     7209   5989   5933    629   -325    455       N  
ATOM   1981  CA  THR A 264     -22.338   1.115  19.109  1.00 56.10           C  
ANISOU 1981  CA  THR A 264     8041   6618   6654    557   -326    404       C  
ATOM   1982  C   THR A 264     -21.782   1.517  17.748  1.00 51.78           C  
ANISOU 1982  C   THR A 264     7530   6024   6119    498   -344    439       C  
ATOM   1983  O   THR A 264     -21.248   2.621  17.594  1.00 56.00           O  
ANISOU 1983  O   THR A 264     8174   6448   6656    480   -327    424       O  
ATOM   1984  CB  THR A 264     -21.309   0.293  19.885  1.00 61.74           C  
ANISOU 1984  CB  THR A 264     8729   7369   7358    467   -344    343       C  
ATOM   1985  OG1 THR A 264     -21.066  -0.943  19.202  1.00 73.65           O  
ANISOU 1985  OG1 THR A 264    10140   8963   8879    405   -374    369       O  
ATOM   1986  CG2 THR A 264     -21.815  -0.002  21.286  1.00 53.97           C  
ANISOU 1986  CG2 THR A 264     7736   6423   6348    529   -320    312       C  
ATOM   1987  N   TYR A 265     -21.898   0.636  16.751  1.00 45.28           N  
ANISOU 1987  N   TYR A 265     6625   5279   5301    466   -373    483       N  
ATOM   1988  CA  TYR A 265     -21.428   0.971  15.409  1.00 44.04           C  
ANISOU 1988  CA  TYR A 265     6507   5086   5142    417   -384    521       C  
ATOM   1989  C   TYR A 265     -22.192   2.159  14.838  1.00 45.73           C  
ANISOU 1989  C   TYR A 265     6802   5227   5347    512   -371    578       C  
ATOM   1990  O   TYR A 265     -21.606   3.032  14.187  1.00 49.62           O  
ANISOU 1990  O   TYR A 265     7394   5624   5834    479   -355    594       O  
ATOM   1991  CB  TYR A 265     -21.568  -0.238  14.486  1.00 40.38           C  
ANISOU 1991  CB  TYR A 265     5942   4727   4674    380   -419    553       C  
ATOM   1992  CG  TYR A 265     -20.304  -1.046  14.308  1.00 45.10           C  
ANISOU 1992  CG  TYR A 265     6509   5349   5277    259   -427    513       C  
ATOM   1993  CD1 TYR A 265     -19.490  -1.347  15.392  1.00 48.08           C  
ANISOU 1993  CD1 TYR A 265     6878   5723   5667    210   -422    447       C  
ATOM   1994  CD2 TYR A 265     -19.932  -1.520  13.057  1.00 47.40           C  
ANISOU 1994  CD2 TYR A 265     6781   5672   5558    202   -442    539       C  
ATOM   1995  CE1 TYR A 265     -18.336  -2.091  15.232  1.00 47.32           C  
ANISOU 1995  CE1 TYR A 265     6745   5655   5580    113   -432    411       C  
ATOM   1996  CE2 TYR A 265     -18.781  -2.265  12.888  1.00 49.51           C  
ANISOU 1996  CE2 TYR A 265     7016   5963   5833    102   -443    500       C  
ATOM   1997  CZ  TYR A 265     -17.987  -2.547  13.979  1.00 48.93           C  
ANISOU 1997  CZ  TYR A 265     6924   5886   5780     60   -438    437       C  
ATOM   1998  OH  TYR A 265     -16.840  -3.289  13.817  1.00 50.32           O  
ANISOU 1998  OH  TYR A 265     7059   6092   5970    -26   -442    399       O  
ATOM   1999  N   ALA A 266     -23.505   2.207  15.072  1.00 43.80           N  
ANISOU 1999  N   ALA A 266     6515   5024   5103    633   -373    611       N  
ATOM   2000  CA  ALA A 266     -24.320   3.295  14.549  1.00 48.00           C  
ANISOU 2000  CA  ALA A 266     7115   5495   5628    746   -366    670       C  
ATOM   2001  C   ALA A 266     -24.097   4.601  15.297  1.00 48.94           C  
ANISOU 2001  C   ALA A 266     7369   5473   5752    787   -318    638       C  
ATOM   2002  O   ALA A 266     -24.464   5.664  14.783  1.00 55.31           O  
ANISOU 2002  O   ALA A 266     8271   6191   6553    865   -305    686       O  
ATOM   2003  CB  ALA A 266     -25.799   2.914  14.606  1.00 37.38           C  
ANISOU 2003  CB  ALA A 266     5663   4250   4290    867   -384    710       C  
ATOM   2004  N   SER A 267     -23.503   4.549  16.490  1.00 43.24           N  
ANISOU 2004  N   SER A 267     6666   4727   5037    739   -294    559       N  
ATOM   2005  CA  SER A 267     -23.355   5.751  17.302  1.00 43.80           C  
ANISOU 2005  CA  SER A 267     6865   4667   5109    777   -251    514       C  
ATOM   2006  C   SER A 267     -22.286   6.695  16.769  1.00 42.02           C  
ANISOU 2006  C   SER A 267     6772   4303   4890    690   -235    504       C  
ATOM   2007  O   SER A 267     -22.271   7.869  17.152  1.00 46.12           O  
ANISOU 2007  O   SER A 267     7421   4688   5414    729   -197    482       O  
ATOM   2008  CB  SER A 267     -23.035   5.368  18.748  1.00 47.56           C  
ANISOU 2008  CB  SER A 267     7322   5168   5578    749   -238    427       C  
ATOM   2009  OG  SER A 267     -21.826   4.634  18.830  1.00 51.83           O  
ANISOU 2009  OG  SER A 267     7828   5746   6120    607   -265    379       O  
ATOM   2010  N   TYR A 268     -21.399   6.220  15.896  1.00 42.41           N  
ANISOU 2010  N   TYR A 268     6796   4376   4940    570   -255    518       N  
ATOM   2011  CA  TYR A 268     -20.299   7.029  15.395  1.00 44.21           C  
ANISOU 2011  CA  TYR A 268     7137   4483   5180    466   -229    507       C  
ATOM   2012  C   TYR A 268     -20.635   7.748  14.092  1.00 55.21           C  
ANISOU 2012  C   TYR A 268     8613   5805   6559    511   -215    602       C  
ATOM   2013  O   TYR A 268     -19.721   8.190  13.386  1.00 63.76           O  
ANISOU 2013  O   TYR A 268     9772   6810   7646    411   -190    613       O  
ATOM   2014  CB  TYR A 268     -19.050   6.165  15.217  1.00 40.48           C  
ANISOU 2014  CB  TYR A 268     6592   4073   4717    310   -247    464       C  
ATOM   2015  CG  TYR A 268     -18.567   5.521  16.498  1.00 48.45           C  
ANISOU 2015  CG  TYR A 268     7535   5142   5735    265   -266    371       C  
ATOM   2016  CD1 TYR A 268     -18.702   4.156  16.705  1.00 50.10           C  
ANISOU 2016  CD1 TYR A 268     7607   5493   5935    261   -303    367       C  
ATOM   2017  CD2 TYR A 268     -17.979   6.281  17.500  1.00 53.09           C  
ANISOU 2017  CD2 TYR A 268     8202   5637   6331    226   -250    287       C  
ATOM   2018  CE1 TYR A 268     -18.263   3.563  17.875  1.00 49.84           C  
ANISOU 2018  CE1 TYR A 268     7525   5511   5900    229   -322    292       C  
ATOM   2019  CE2 TYR A 268     -17.537   5.697  18.673  1.00 52.50           C  
ANISOU 2019  CE2 TYR A 268     8073   5624   6251    193   -276    204       C  
ATOM   2020  CZ  TYR A 268     -17.682   4.338  18.855  1.00 48.18           C  
ANISOU 2020  CZ  TYR A 268     7395   5220   5691    199   -311    212       C  
ATOM   2021  OH  TYR A 268     -17.244   3.751  20.020  1.00 44.47           O  
ANISOU 2021  OH  TYR A 268     6882   4808   5206    175   -338    139       O  
ATOM   2022  N   ARG A 270     -21.918   7.876  13.759  1.00 53.54           N  
ANISOU 2022  N   ARG A 270     8389   5624   6330    661   -229    673       N  
ATOM   2023  CA  ARG A 270     -22.334   8.619  12.573  1.00 57.69           C  
ANISOU 2023  CA  ARG A 270     9004   6083   6831    729   -224    771       C  
ATOM   2024  C   ARG A 270     -23.718   9.195  12.816  1.00 61.73           C  
ANISOU 2024  C   ARG A 270     9533   6581   7340    920   -227    815       C  
ATOM   2025  O   ARG A 270     -24.677   8.444  13.020  1.00 63.40           O  
ANISOU 2025  O   ARG A 270     9612   6926   7550   1003   -264    826       O  
ATOM   2026  CB  ARG A 270     -22.334   7.730  11.328  1.00 58.88           C  
ANISOU 2026  CB  ARG A 270     9073   6349   6949    693   -268    833       C  
ATOM   2027  CG  ARG A 270     -21.117   7.921  10.442  1.00 57.63           C  
ANISOU 2027  CG  ARG A 270     8990   6127   6778    554   -238    846       C  
ATOM   2028  CD  ARG A 270     -21.416   7.585   8.991  1.00 54.77           C  
ANISOU 2028  CD  ARG A 270     8619   5829   6362    576   -269    937       C  
ATOM   2029  NE  ARG A 270     -22.063   8.695   8.297  1.00 60.07           N  
ANISOU 2029  NE  ARG A 270     9423   6401   6999    694   -258   1030       N  
ATOM   2030  CZ  ARG A 270     -21.406   9.680   7.694  1.00 64.08           C  
ANISOU 2030  CZ  ARG A 270    10092   6763   7493    649   -201   1073       C  
ATOM   2031  NH1 ARG A 270     -22.074  10.652   7.087  1.00 65.24           N  
ANISOU 2031  NH1 ARG A 270    10365   6819   7605    774   -194   1166       N  
ATOM   2032  NH2 ARG A 270     -20.080   9.694   7.697  1.00 64.34           N  
ANISOU 2032  NH2 ARG A 270    10158   6741   7548    480   -148   1024       N  
ATOM   2033  N   LYS A 271     -23.818  10.524  12.791  1.00 61.38           N  
ANISOU 2033  N   LYS A 271     9650   6373   7299    988   -183    840       N  
ATOM   2034  CA  LYS A 271     -25.099  11.200  12.944  1.00 61.16           C  
ANISOU 2034  CA  LYS A 271     9652   6316   7270   1185   -180    887       C  
ATOM   2035  C   LYS A 271     -25.811  11.386  11.610  1.00 63.21           C  
ANISOU 2035  C   LYS A 271     9925   6600   7493   1289   -218   1008       C  
ATOM   2036  O   LYS A 271     -27.036  11.243  11.538  1.00 68.67           O  
ANISOU 2036  O   LYS A 271    10532   7380   8180   1444   -255   1052       O  
ATOM   2037  CB  LYS A 271     -24.901  12.558  13.622  1.00 58.43           C  
ANISOU 2037  CB  LYS A 271     9486   5770   6946   1223   -112    851       C  
ATOM   2038  N   ASP A 272     -25.067  11.701  10.552  1.00 59.34           N  
ANISOU 2038  N   ASP A 272     9535   6038   6973   1208   -209   1061       N  
ATOM   2039  CA  ASP A 272     -25.640  11.899   9.221  1.00 59.64           C  
ANISOU 2039  CA  ASP A 272     9606   6096   6959   1301   -248   1179       C  
ATOM   2040  C   ASP A 272     -25.670  10.553   8.511  1.00 61.48           C  
ANISOU 2040  C   ASP A 272     9678   6521   7159   1236   -318   1191       C  
ATOM   2041  O   ASP A 272     -24.695  10.132   7.886  1.00 62.27           O  
ANISOU 2041  O   ASP A 272     9792   6632   7237   1089   -310   1187       O  
ATOM   2042  CB  ASP A 272     -24.839  12.930   8.436  1.00 63.66           C  
ANISOU 2042  CB  ASP A 272    10319   6425   7443   1247   -194   1236       C  
ATOM   2043  CG  ASP A 272     -24.988  14.331   8.992  1.00 75.01           C  
ANISOU 2043  CG  ASP A 272    11932   7658   8909   1336   -129   1238       C  
ATOM   2044  OD1 ASP A 272     -25.626  14.484  10.055  1.00 78.80           O  
ANISOU 2044  OD1 ASP A 272    12374   8138   9427   1432   -123   1183       O  
ATOM   2045  OD2 ASP A 272     -24.469  15.278   8.367  1.00 81.74           O  
ANISOU 2045  OD2 ASP A 272    12968   8344   9745   1310    -77   1295       O  
ATOM   2046  N   GLN A 273     -26.808   9.870   8.601  1.00 62.75           N  
ANISOU 2046  N   GLN A 273     9685   6836   7321   1344   -382   1202       N  
ATOM   2047  CA  GLN A 273     -26.943   8.549   8.007  1.00 62.80           C  
ANISOU 2047  CA  GLN A 273     9534   7024   7302   1284   -450   1202       C  
ATOM   2048  C   GLN A 273     -28.414   8.248   7.766  1.00 66.66           C  
ANISOU 2048  C   GLN A 273     9898   7647   7783   1444   -524   1248       C  
ATOM   2049  O   GLN A 273     -29.263   8.557   8.606  1.00 72.55           O  
ANISOU 2049  O   GLN A 273    10599   8397   8571   1564   -514   1233       O  
ATOM   2050  CB  GLN A 273     -26.328   7.470   8.908  1.00 64.39           C  
ANISOU 2050  CB  GLN A 273     9618   7303   7546   1144   -437   1099       C  
ATOM   2051  CG  GLN A 273     -26.082   6.139   8.215  1.00 66.57           C  
ANISOU 2051  CG  GLN A 273     9773   7725   7797   1042   -490   1090       C  
ATOM   2052  CD  GLN A 273     -24.787   6.120   7.429  1.00 68.44           C  
ANISOU 2052  CD  GLN A 273    10099   7906   8001    899   -462   1094       C  
ATOM   2053  OE1 GLN A 273     -24.128   7.147   7.270  1.00 66.56           O  
ANISOU 2053  OE1 GLN A 273    10014   7520   7756    875   -406   1115       O  
ATOM   2054  NE2 GLN A 273     -24.413   4.946   6.933  1.00 70.52           N  
ANISOU 2054  NE2 GLN A 273    10266   8282   8245    800   -494   1071       N  
ATOM   2055  N   ASP A 274     -28.703   7.648   6.614  1.00 66.08           N  
ANISOU 2055  N   ASP A 274     9766   7686   7655   1444   -598   1300       N  
ATOM   2056  CA  ASP A 274     -30.025   7.093   6.333  1.00 66.92           C  
ANISOU 2056  CA  ASP A 274     9714   7955   7757   1560   -685   1327       C  
ATOM   2057  C   ASP A 274     -30.024   5.668   6.868  1.00 59.97           C  
ANISOU 2057  C   ASP A 274     8652   7217   6916   1448   -703   1245       C  
ATOM   2058  O   ASP A 274     -29.555   4.742   6.202  1.00 61.49           O  
ANISOU 2058  O   ASP A 274     8800   7488   7076   1332   -738   1231       O  
ATOM   2059  CB  ASP A 274     -30.334   7.139   4.840  1.00 74.13           C  
ANISOU 2059  CB  ASP A 274    10660   8922   8584   1611   -764   1415       C  
ATOM   2060  CG  ASP A 274     -31.665   6.484   4.490  1.00 82.13           C  
ANISOU 2060  CG  ASP A 274    11492  10120   9592   1714   -869   1433       C  
ATOM   2061  OD1 ASP A 274     -31.797   5.251   4.641  1.00 83.29           O  
ANISOU 2061  OD1 ASP A 274    11478  10404   9763   1622   -903   1372       O  
ATOM   2062  OD2 ASP A 274     -32.586   7.203   4.053  1.00 86.90           O  
ANISOU 2062  OD2 ASP A 274    12114  10732  10172   1889   -918   1508       O  
ATOM   2063  N   ILE A 275     -30.547   5.488   8.083  1.00 54.01           N  
ANISOU 2063  N   ILE A 275     7801   6491   6227   1486   -672   1192       N  
ATOM   2064  CA  ILE A 275     -30.515   4.174   8.712  1.00 55.75           C  
ANISOU 2064  CA  ILE A 275     7868   6829   6488   1380   -675   1119       C  
ATOM   2065  C   ILE A 275     -31.454   3.193   8.024  1.00 56.03           C  
ANISOU 2065  C   ILE A 275     7736   7040   6515   1397   -764   1135       C  
ATOM   2066  O   ILE A 275     -31.308   1.978   8.197  1.00 62.96           O  
ANISOU 2066  O   ILE A 275     8500   8010   7411   1284   -776   1082       O  
ATOM   2067  CB  ILE A 275     -30.852   4.295  10.208  1.00 52.04           C  
ANISOU 2067  CB  ILE A 275     7354   6339   6081   1422   -610   1064       C  
ATOM   2068  CG1 ILE A 275     -32.360   4.452  10.401  1.00 58.28           C  
ANISOU 2068  CG1 ILE A 275     8025   7219   6900   1588   -635   1094       C  
ATOM   2069  CG2 ILE A 275     -30.116   5.476  10.820  1.00 44.69           C  
ANISOU 2069  CG2 ILE A 275     6600   5228   5153   1435   -534   1050       C  
ATOM   2070  CD1 ILE A 275     -32.764   4.707  11.824  1.00 61.16           C  
ANISOU 2070  CD1 ILE A 275     8361   7559   7317   1650   -559   1048       C  
ATOM   2071  N   VAL A 276     -32.414   3.687   7.240  1.00 52.17           N  
ANISOU 2071  N   VAL A 276     7229   6598   5998   1535   -830   1204       N  
ATOM   2072  CA  VAL A 276     -33.337   2.796   6.543  1.00 53.96           C  
ANISOU 2072  CA  VAL A 276     7289   6998   6214   1549   -927   1213       C  
ATOM   2073  C   VAL A 276     -32.618   2.069   5.413  1.00 53.41           C  
ANISOU 2073  C   VAL A 276     7250   6966   6076   1421   -979   1212       C  
ATOM   2074  O   VAL A 276     -32.615   0.834   5.346  1.00 55.46           O  
ANISOU 2074  O   VAL A 276     7393   7331   6351   1311  -1008   1160       O  
ATOM   2075  CB  VAL A 276     -34.554   3.579   6.023  1.00 54.18           C  
ANISOU 2075  CB  VAL A 276     7286   7071   6227   1746   -993   1287       C  
ATOM   2076  CG1 VAL A 276     -35.594   2.624   5.461  1.00 46.30           C  
ANISOU 2076  CG1 VAL A 276     6088   6270   5233   1755  -1098   1281       C  
ATOM   2077  CG2 VAL A 276     -35.147   4.432   7.133  1.00 53.02           C  
ANISOU 2077  CG2 VAL A 276     7137   6863   6144   1883   -925   1288       C  
ATOM   2078  N   LEU A 277     -31.995   2.827   4.508  1.00 48.66           N  
ANISOU 2078  N   LEU A 277     6816   6274   5400   1434   -983   1270       N  
ATOM   2079  CA  LEU A 277     -31.276   2.211   3.398  1.00 47.05           C  
ANISOU 2079  CA  LEU A 277     6657   6101   5121   1319  -1020   1271       C  
ATOM   2080  C   LEU A 277     -30.002   1.526   3.877  1.00 49.86           C  
ANISOU 2080  C   LEU A 277     7037   6407   5502   1142   -946   1198       C  
ATOM   2081  O   LEU A 277     -29.636   0.460   3.369  1.00 51.75           O  
ANISOU 2081  O   LEU A 277     7224   6722   5717   1029   -974   1159       O  
ATOM   2082  CB  LEU A 277     -30.955   3.262   2.336  1.00 51.60           C  
ANISOU 2082  CB  LEU A 277     7414   6588   5604   1385  -1030   1360       C  
ATOM   2083  CG  LEU A 277     -30.276   2.787   1.051  1.00 53.51           C  
ANISOU 2083  CG  LEU A 277     7725   6861   5748   1290  -1064   1375       C  
ATOM   2084  CD1 LEU A 277     -31.222   1.928   0.228  1.00 56.15           C  
ANISOU 2084  CD1 LEU A 277     7924   7374   6035   1318  -1189   1373       C  
ATOM   2085  CD2 LEU A 277     -29.787   3.979   0.244  1.00 53.25           C  
ANISOU 2085  CD2 LEU A 277     7902   6701   5631   1345  -1036   1467       C  
ATOM   2086  N   SER A 278     -29.316   2.120   4.856  1.00 54.28           N  
ANISOU 2086  N   SER A 278     7676   6840   6109   1119   -853   1175       N  
ATOM   2087  CA  SER A 278     -28.089   1.518   5.367  1.00 53.73           C  
ANISOU 2087  CA  SER A 278     7623   6727   6066    961   -790   1105       C  
ATOM   2088  C   SER A 278     -28.376   0.208   6.090  1.00 54.08           C  
ANISOU 2088  C   SER A 278     7501   6879   6166    896   -801   1034       C  
ATOM   2089  O   SER A 278     -27.659  -0.782   5.899  1.00 51.79           O  
ANISOU 2089  O   SER A 278     7182   6625   5872    770   -799    988       O  
ATOM   2090  CB  SER A 278     -27.370   2.497   6.294  1.00 53.22           C  
ANISOU 2090  CB  SER A 278     7674   6510   6039    958   -700   1091       C  
ATOM   2091  OG  SER A 278     -27.031   3.693   5.614  1.00 57.12           O  
ANISOU 2091  OG  SER A 278     8333   6885   6484   1002   -678   1158       O  
ATOM   2092  N   GLY A 279     -29.418   0.182   6.923  1.00 57.01           N  
ANISOU 2092  N   GLY A 279     7767   7301   6591    981   -807   1026       N  
ATOM   2093  CA  GLY A 279     -29.786  -1.052   7.595  1.00 54.84           C  
ANISOU 2093  CA  GLY A 279     7340   7127   6370    921   -811    967       C  
ATOM   2094  C   GLY A 279     -30.324  -2.104   6.648  1.00 53.81           C  
ANISOU 2094  C   GLY A 279     7100   7129   6217    880   -893    964       C  
ATOM   2095  O   GLY A 279     -30.134  -3.303   6.874  1.00 53.87           O  
ANISOU 2095  O   GLY A 279     7025   7193   6251    775   -892    910       O  
ATOM   2096  N   LEU A 280     -30.999  -1.678   5.578  1.00 55.61           N  
ANISOU 2096  N   LEU A 280     7332   7405   6392    964   -969   1019       N  
ATOM   2097  CA  LEU A 280     -31.493  -2.630   4.590  1.00 50.91           C  
ANISOU 2097  CA  LEU A 280     6643   6938   5763    923  -1060   1009       C  
ATOM   2098  C   LEU A 280     -30.356  -3.183   3.742  1.00 51.92           C  
ANISOU 2098  C   LEU A 280     6857   7042   5828    798  -1060    987       C  
ATOM   2099  O   LEU A 280     -30.335  -4.377   3.422  1.00 52.49           O  
ANISOU 2099  O   LEU A 280     6852   7193   5901    701  -1092    936       O  
ATOM   2100  CB  LEU A 280     -32.549  -1.967   3.707  1.00 50.21           C  
ANISOU 2100  CB  LEU A 280     6534   6915   5626   1061  -1152   1075       C  
ATOM   2101  CG  LEU A 280     -33.486  -2.901   2.942  1.00 53.24           C  
ANISOU 2101  CG  LEU A 280     6770   7462   5995   1046  -1262   1055       C  
ATOM   2102  CD1 LEU A 280     -34.578  -3.429   3.857  1.00 58.78           C  
ANISOU 2102  CD1 LEU A 280     7281   8257   6797   1068  -1263   1020       C  
ATOM   2103  CD2 LEU A 280     -34.088  -2.181   1.745  1.00 53.40           C  
ANISOU 2103  CD2 LEU A 280     6831   7531   5928   1167  -1362   1126       C  
ATOM   2104  N   THR A 281     -29.400  -2.328   3.367  1.00 49.44           N  
ANISOU 2104  N   THR A 281     6706   6617   5462    796  -1017   1023       N  
ATOM   2105  CA  THR A 281     -28.262  -2.790   2.577  1.00 46.69           C  
ANISOU 2105  CA  THR A 281     6441   6244   5056    681  -1000   1003       C  
ATOM   2106  C   THR A 281     -27.412  -3.782   3.362  1.00 48.35           C  
ANISOU 2106  C   THR A 281     6606   6438   5325    553   -940    924       C  
ATOM   2107  O   THR A 281     -26.991  -4.812   2.824  1.00 50.44           O  
ANISOU 2107  O   THR A 281     6845   6751   5567    457   -955    881       O  
ATOM   2108  CB  THR A 281     -27.415  -1.599   2.124  1.00 45.20           C  
ANISOU 2108  CB  THR A 281     6431   5932   4811    702   -949   1060       C  
ATOM   2109  OG1 THR A 281     -28.227  -0.693   1.365  1.00 45.13           O  
ANISOU 2109  OG1 THR A 281     6475   5932   4739    833  -1008   1142       O  
ATOM   2110  CG2 THR A 281     -26.251  -2.069   1.262  1.00 40.76           C  
ANISOU 2110  CG2 THR A 281     5946   5353   4188    584   -922   1041       C  
ATOM   2111  N   ALA A 282     -27.155  -3.491   4.640  1.00 47.60           N  
ANISOU 2111  N   ALA A 282     6508   6277   5303    555   -873    904       N  
ATOM   2112  CA  ALA A 282     -26.362  -4.398   5.463  1.00 46.38           C  
ANISOU 2112  CA  ALA A 282     6314   6109   5200    449   -821    835       C  
ATOM   2113  C   ALA A 282     -27.065  -5.733   5.672  1.00 44.87           C  
ANISOU 2113  C   ALA A 282     5980   6023   5047    410   -859    791       C  
ATOM   2114  O   ALA A 282     -26.404  -6.776   5.740  1.00 42.90           O  
ANISOU 2114  O   ALA A 282     5707   5782   4810    310   -841    740       O  
ATOM   2115  CB  ALA A 282     -26.051  -3.748   6.810  1.00 50.47           C  
ANISOU 2115  CB  ALA A 282     6860   6540   5774    473   -753    823       C  
ATOM   2116  N   ALA A 283     -28.395  -5.727   5.768  1.00 48.58           N  
ANISOU 2116  N   ALA A 283     6351   6569   5537    487   -907    810       N  
ATOM   2117  CA  ALA A 283     -29.124  -6.977   5.953  1.00 50.98           C  
ANISOU 2117  CA  ALA A 283     6515   6971   5885    438   -939    769       C  
ATOM   2118  C   ALA A 283     -29.109  -7.815   4.682  1.00 54.66           C  
ANISOU 2118  C   ALA A 283     6966   7505   6297    370  -1007    747       C  
ATOM   2119  O   ALA A 283     -28.819  -9.016   4.722  1.00 53.56           O  
ANISOU 2119  O   ALA A 283     6782   7387   6179    270  -1000    691       O  
ATOM   2120  CB  ALA A 283     -30.559  -6.688   6.392  1.00 48.34           C  
ANISOU 2120  CB  ALA A 283     6066   6707   5594    536   -967    793       C  
ATOM   2121  N   THR A 284     -29.423  -7.198   3.539  1.00 59.14           N  
ANISOU 2121  N   THR A 284     7578   8103   6788    428  -1073    790       N  
ATOM   2122  CA  THR A 284     -29.431  -7.939   2.282  1.00 61.47           C  
ANISOU 2122  CA  THR A 284     7871   8468   7016    370  -1143    765       C  
ATOM   2123  C   THR A 284     -28.036  -8.419   1.909  1.00 58.43           C  
ANISOU 2123  C   THR A 284     7587   8020   6595    268  -1091    730       C  
ATOM   2124  O   THR A 284     -27.886  -9.503   1.335  1.00 63.70           O  
ANISOU 2124  O   THR A 284     8228   8732   7241    183  -1117    676       O  
ATOM   2125  CB  THR A 284     -30.017  -7.081   1.161  1.00 65.56           C  
ANISOU 2125  CB  THR A 284     8435   9030   7445    468  -1226    827       C  
ATOM   2126  OG1 THR A 284     -29.248  -5.879   1.023  1.00 73.80           O  
ANISOU 2126  OG1 THR A 284     9630   9968   8442    520  -1174    887       O  
ATOM   2127  CG2 THR A 284     -31.465  -6.724   1.465  1.00 63.22           C  
ANISOU 2127  CG2 THR A 284     8014   8816   7189    575  -1288    855       C  
ATOM   2128  N   LEU A 285     -27.005  -7.632   2.226  1.00 54.62           N  
ANISOU 2128  N   LEU A 285     7214   7433   6106    273  -1014    755       N  
ATOM   2129  CA  LEU A 285     -25.637  -8.101   2.034  1.00 50.52           C  
ANISOU 2129  CA  LEU A 285     6766   6858   5570    176   -953    716       C  
ATOM   2130  C   LEU A 285     -25.357  -9.327   2.891  1.00 46.53           C  
ANISOU 2130  C   LEU A 285     6181   6357   5143     95   -920    648       C  
ATOM   2131  O   LEU A 285     -24.695 -10.271   2.443  1.00 45.36           O  
ANISOU 2131  O   LEU A 285     6042   6215   4978     13   -909    598       O  
ATOM   2132  CB  LEU A 285     -24.643  -6.987   2.362  1.00 50.44           C  
ANISOU 2132  CB  LEU A 285     6869   6738   5558    190   -877    751       C  
ATOM   2133  CG  LEU A 285     -24.323  -5.975   1.262  1.00 54.97           C  
ANISOU 2133  CG  LEU A 285     7571   7277   6039    225   -877    812       C  
ATOM   2134  CD1 LEU A 285     -23.184  -5.068   1.702  1.00 50.56           C  
ANISOU 2134  CD1 LEU A 285     7112   6600   5498    204   -786    828       C  
ATOM   2135  CD2 LEU A 285     -23.983  -6.679  -0.043  1.00 57.17           C  
ANISOU 2135  CD2 LEU A 285     7882   7608   6230    167   -904    792       C  
ATOM   2136  N   ASN A 286     -25.858  -9.332   4.128  1.00 44.96           N  
ANISOU 2136  N   ASN A 286     5909   6152   5023    123   -900    646       N  
ATOM   2137  CA  ASN A 286     -25.639 -10.472   5.012  1.00 47.97           C  
ANISOU 2137  CA  ASN A 286     6224   6531   5473     55   -864    592       C  
ATOM   2138  C   ASN A 286     -26.446 -11.684   4.566  1.00 44.67           C  
ANISOU 2138  C   ASN A 286     5713   6195   5064      6   -919    553       C  
ATOM   2139  O   ASN A 286     -25.948 -12.816   4.603  1.00 45.42           O  
ANISOU 2139  O   ASN A 286     5797   6281   5179    -76   -898    501       O  
ATOM   2140  CB  ASN A 286     -25.992 -10.092   6.449  1.00 47.18           C  
ANISOU 2140  CB  ASN A 286     6083   6403   5441    103   -822    606       C  
ATOM   2141  CG  ASN A 286     -25.973 -11.282   7.386  1.00 44.92           C  
ANISOU 2141  CG  ASN A 286     5728   6122   5218     44   -789    563       C  
ATOM   2142  OD1 ASN A 286     -24.913 -11.708   7.845  1.00 42.45           O  
ANISOU 2142  OD1 ASN A 286     5454   5756   4918     -4   -743    534       O  
ATOM   2143  ND2 ASN A 286     -27.149 -11.828   7.674  1.00 47.90           N  
ANISOU 2143  ND2 ASN A 286     6000   6563   5636     50   -812    560       N  
ATOM   2144  N   GLU A 287     -27.694 -11.471   4.142  1.00 45.48           N  
ANISOU 2144  N   GLU A 287     5748   6377   5157     54   -989    575       N  
ATOM   2145  CA  GLU A 287     -28.525 -12.591   3.716  1.00 47.15           C  
ANISOU 2145  CA  GLU A 287     5861   6670   5383     -3  -1047    531       C  
ATOM   2146  C   GLU A 287     -28.042 -13.182   2.399  1.00 45.96           C  
ANISOU 2146  C   GLU A 287     5767   6540   5155    -66  -1089    492       C  
ATOM   2147  O   GLU A 287     -28.234 -14.378   2.152  1.00 46.59           O  
ANISOU 2147  O   GLU A 287     5800   6651   5253   -149  -1110    431       O  
ATOM   2148  CB  GLU A 287     -29.982 -12.149   3.602  1.00 50.01           C  
ANISOU 2148  CB  GLU A 287     6119   7124   5757     69  -1118    561       C  
ATOM   2149  CG  GLU A 287     -30.696 -12.062   4.936  1.00 60.11           C  
ANISOU 2149  CG  GLU A 287     7302   8407   7129    105  -1072    575       C  
ATOM   2150  CD  GLU A 287     -30.407 -13.249   5.828  1.00 68.55           C  
ANISOU 2150  CD  GLU A 287     8334   9443   8269     11  -1007    529       C  
ATOM   2151  OE1 GLU A 287     -29.893 -13.045   6.946  1.00 72.04           O  
ANISOU 2151  OE1 GLU A 287     8809   9816   8746     27   -927    542       O  
ATOM   2152  OE2 GLU A 287     -30.688 -14.389   5.407  1.00 75.82           O  
ANISOU 2152  OE2 GLU A 287     9200  10403   9204    -78  -1037    479       O  
ATOM   2153  N   LYS A 288     -27.421 -12.368   1.543  1.00 46.79           N  
ANISOU 2153  N   LYS A 288     5981   6623   5173    -31  -1096    524       N  
ATOM   2154  CA  LYS A 288     -26.820 -12.901   0.325  1.00 48.51           C  
ANISOU 2154  CA  LYS A 288     6272   6854   5307    -89  -1118    486       C  
ATOM   2155  C   LYS A 288     -25.660 -13.832   0.656  1.00 52.70           C  
ANISOU 2155  C   LYS A 288     6835   7318   5870   -175  -1040    430       C  
ATOM   2156  O   LYS A 288     -25.578 -14.949   0.135  1.00 57.99           O  
ANISOU 2156  O   LYS A 288     7497   8009   6528   -248  -1056    366       O  
ATOM   2157  CB  LYS A 288     -26.354 -11.758  -0.579  1.00 52.56           C  
ANISOU 2157  CB  LYS A 288     6905   7350   5718    -31  -1123    544       C  
ATOM   2158  CG  LYS A 288     -27.462 -11.119  -1.403  1.00 55.42           C  
ANISOU 2158  CG  LYS A 288     7253   7795   6010     49  -1225    589       C  
ATOM   2159  CD  LYS A 288     -26.970  -9.864  -2.106  1.00 58.24           C  
ANISOU 2159  CD  LYS A 288     7746   8111   6273    119  -1212    664       C  
ATOM   2160  CE  LYS A 288     -28.081  -9.203  -2.906  1.00 65.34           C  
ANISOU 2160  CE  LYS A 288     8637   9093   7096    217  -1321    717       C  
ATOM   2161  NZ  LYS A 288     -27.661  -7.888  -3.466  1.00 65.71           N  
ANISOU 2161  NZ  LYS A 288     8827   9082   7057    297  -1299    805       N  
ATOM   2162  N   ALA A 289     -24.756 -13.391   1.533  1.00 52.75           N  
ANISOU 2162  N   ALA A 289     6880   7244   5919   -164   -957    450       N  
ATOM   2163  CA  ALA A 289     -23.651 -14.247   1.947  1.00 52.73           C  
ANISOU 2163  CA  ALA A 289     6897   7183   5953   -230   -888    400       C  
ATOM   2164  C   ALA A 289     -24.130 -15.458   2.734  1.00 56.46           C  
ANISOU 2164  C   ALA A 289     7283   7662   6507   -276   -885    356       C  
ATOM   2165  O   ALA A 289     -23.413 -16.462   2.806  1.00 62.41           O  
ANISOU 2165  O   ALA A 289     8051   8381   7282   -334   -847    306       O  
ATOM   2166  CB  ALA A 289     -22.649 -13.446   2.778  1.00 48.97           C  
ANISOU 2166  CB  ALA A 289     6468   6632   5508   -205   -813    430       C  
ATOM   2167  N   GLU A 290     -25.327 -15.391   3.317  1.00 53.02           N  
ANISOU 2167  N   GLU A 290     6758   7267   6119   -250   -919    376       N  
ATOM   2168  CA  GLU A 290     -25.823 -16.486   4.143  1.00 50.53           C  
ANISOU 2168  CA  GLU A 290     6362   6952   5885   -299   -904    343       C  
ATOM   2169  C   GLU A 290     -26.436 -17.595   3.294  1.00 52.03           C  
ANISOU 2169  C   GLU A 290     6513   7192   6066   -373   -959    285       C  
ATOM   2170  O   GLU A 290     -26.014 -18.754   3.370  1.00 47.19           O  
ANISOU 2170  O   GLU A 290     5910   6538   5481   -443   -929    232       O  
ATOM   2171  CB  GLU A 290     -26.845 -15.955   5.151  1.00 49.93           C  
ANISOU 2171  CB  GLU A 290     6203   6902   5867   -244   -902    387       C  
ATOM   2172  CG  GLU A 290     -27.388 -17.009   6.101  1.00 54.03           C  
ANISOU 2172  CG  GLU A 290     6642   7416   6469   -294   -870    365       C  
ATOM   2173  CD  GLU A 290     -27.210 -16.623   7.557  1.00 57.13           C  
ANISOU 2173  CD  GLU A 290     7032   7762   6911   -248   -799    402       C  
ATOM   2174  OE1 GLU A 290     -26.223 -15.924   7.867  1.00 56.69           O  
ANISOU 2174  OE1 GLU A 290     7055   7653   6832   -208   -764    420       O  
ATOM   2175  OE2 GLU A 290     -28.055 -17.016   8.388  1.00 55.40           O  
ANISOU 2175  OE2 GLU A 290     6734   7562   6753   -256   -775    409       O  
ATOM   2176  N   VAL A 291     -27.432 -17.256   2.475  1.00 58.66           N  
ANISOU 2176  N   VAL A 291     7308   8115   6863   -356  -1044    290       N  
ATOM   2177  CA  VAL A 291     -28.191 -18.278   1.760  1.00 59.48           C  
ANISOU 2177  CA  VAL A 291     7356   8278   6966   -432  -1110    227       C  
ATOM   2178  C   VAL A 291     -27.660 -18.568   0.360  1.00 56.51           C  
ANISOU 2178  C   VAL A 291     7067   7916   6489   -465  -1151    180       C  
ATOM   2179  O   VAL A 291     -27.953 -19.639  -0.190  1.00 60.34           O  
ANISOU 2179  O   VAL A 291     7535   8421   6972   -547  -1187    107       O  
ATOM   2180  CB  VAL A 291     -29.678 -17.886   1.678  1.00 62.28           C  
ANISOU 2180  CB  VAL A 291     7590   8735   7337   -400  -1191    248       C  
ATOM   2181  CG1 VAL A 291     -30.206 -17.523   3.060  1.00 58.28           C  
ANISOU 2181  CG1 VAL A 291     7001   8217   6924   -357  -1138    296       C  
ATOM   2182  CG2 VAL A 291     -29.879 -16.735   0.702  1.00 64.60           C  
ANISOU 2182  CG2 VAL A 291     7923   9090   7532   -315  -1266    291       C  
ATOM   2183  N   ILE A 292     -26.893 -17.658  -0.232  1.00 50.41           N  
ANISOU 2183  N   ILE A 292     6393   7131   5632   -409  -1142    217       N  
ATOM   2184  CA  ILE A 292     -26.329 -17.862  -1.563  1.00 51.38           C  
ANISOU 2184  CA  ILE A 292     6610   7266   5645   -435  -1167    178       C  
ATOM   2185  C   ILE A 292     -24.899 -18.376  -1.489  1.00 56.47           C  
ANISOU 2185  C   ILE A 292     7341   7824   6292   -471  -1071    146       C  
ATOM   2186  O   ILE A 292     -24.529 -19.308  -2.202  1.00 65.27           O  
ANISOU 2186  O   ILE A 292     8499   8931   7370   -531  -1070     74       O  
ATOM   2187  CB  ILE A 292     -26.410 -16.560  -2.393  1.00 46.35           C  
ANISOU 2187  CB  ILE A 292     6035   6674   4903   -352  -1212    244       C  
ATOM   2188  CG1 ILE A 292     -27.864 -16.129  -2.582  1.00 45.91           C  
ANISOU 2188  CG1 ILE A 292     5886   6718   4841   -305  -1321    271       C  
ATOM   2189  CG2 ILE A 292     -25.724 -16.741  -3.739  1.00 39.02           C  
ANISOU 2189  CG2 ILE A 292     5220   5756   3851   -376  -1220    210       C  
ATOM   2190  CD1 ILE A 292     -28.011 -14.804  -3.297  1.00 47.11           C  
ANISOU 2190  CD1 ILE A 292     6102   6905   4892   -205  -1366    348       C  
ATOM   2191  N   LEU A 293     -24.076 -17.778  -0.630  1.00 49.42           N  
ANISOU 2191  N   LEU A 293     6472   6865   5441   -433   -991    192       N  
ATOM   2192  CA  LEU A 293     -22.681 -18.187  -0.505  1.00 46.41           C  
ANISOU 2192  CA  LEU A 293     6156   6410   5069   -458   -903    164       C  
ATOM   2193  C   LEU A 293     -22.503 -19.249   0.576  1.00 46.04           C  
ANISOU 2193  C   LEU A 293     6060   6307   5125   -496   -857    129       C  
ATOM   2194  O   LEU A 293     -22.048 -20.361   0.293  1.00 50.08           O  
ANISOU 2194  O   LEU A 293     6596   6787   5643   -547   -833     64       O  
ATOM   2195  CB  LEU A 293     -21.802 -16.964  -0.220  1.00 46.85           C  
ANISOU 2195  CB  LEU A 293     6264   6428   5111   -403   -847    226       C  
ATOM   2196  CG  LEU A 293     -21.832 -15.888  -1.306  1.00 47.74           C  
ANISOU 2196  CG  LEU A 293     6448   6576   5115   -365   -875    271       C  
ATOM   2197  CD1 LEU A 293     -20.953 -14.707  -0.924  1.00 46.76           C  
ANISOU 2197  CD1 LEU A 293     6375   6396   4993   -326   -808    330       C  
ATOM   2198  CD2 LEU A 293     -21.408 -16.468  -2.648  1.00 45.20           C  
ANISOU 2198  CD2 LEU A 293     6198   6278   4696   -405   -879    219       C  
ATOM   2199  N   GLY A 294     -22.863 -18.921   1.819  1.00 45.99           N  
ANISOU 2199  N   GLY A 294     5993   6283   5196   -466   -840    173       N  
ATOM   2200  CA  GLY A 294     -22.709 -19.877   2.902  1.00 49.78           C  
ANISOU 2200  CA  GLY A 294     6439   6708   5765   -493   -793    152       C  
ATOM   2201  C   GLY A 294     -23.559 -21.119   2.731  1.00 51.69           C  
ANISOU 2201  C   GLY A 294     6637   6962   6041   -563   -824     99       C  
ATOM   2202  O   GLY A 294     -23.169 -22.207   3.163  1.00 52.48           O  
ANISOU 2202  O   GLY A 294     6748   7001   6191   -603   -780     62       O  
ATOM   2203  N   GLY A 295     -24.726 -20.981   2.097  1.00 56.54           N  
ANISOU 2203  N   GLY A 295     7201   7653   6630   -580   -902     93       N  
ATOM   2204  CA  GLY A 295     -25.595 -22.124   1.888  1.00 56.15           C  
ANISOU 2204  CA  GLY A 295     7100   7618   6615   -661   -938     34       C  
ATOM   2205  C   GLY A 295     -25.211 -23.007   0.721  1.00 55.75           C  
ANISOU 2205  C   GLY A 295     7116   7559   6509   -723   -957    -49       C  
ATOM   2206  O   GLY A 295     -25.686 -24.144   0.640  1.00 53.30           O  
ANISOU 2206  O   GLY A 295     6783   7230   6237   -803   -969   -112       O  
ATOM   2207  N   SER A 296     -24.356 -22.519  -0.178  1.00 61.10           N  
ANISOU 2207  N   SER A 296     7879   8243   7093   -691   -955    -54       N  
ATOM   2208  CA  SER A 296     -23.981 -23.258  -1.376  1.00 62.58           C  
ANISOU 2208  CA  SER A 296     8141   8429   7207   -740   -970   -135       C  
ATOM   2209  C   SER A 296     -22.586 -23.870  -1.284  1.00 62.32           C  
ANISOU 2209  C   SER A 296     8189   8307   7184   -739   -876   -167       C  
ATOM   2210  O   SER A 296     -22.022 -24.258  -2.312  1.00 66.53           O  
ANISOU 2210  O   SER A 296     8799   8837   7642   -758   -869   -226       O  
ATOM   2211  CB  SER A 296     -24.072 -22.355  -2.606  1.00 63.37           C  
ANISOU 2211  CB  SER A 296     8287   8610   7181   -705  -1032   -121       C  
ATOM   2212  OG  SER A 296     -25.257 -21.578  -2.585  1.00 65.60           O  
ANISOU 2212  OG  SER A 296     8493   8976   7457   -675  -1116    -73       O  
ATOM   2213  N   ILE A 297     -22.021 -23.971  -0.082  1.00 57.02           N  
ANISOU 2213  N   ILE A 297     7499   7567   6598   -713   -806   -132       N  
ATOM   2214  CA  ILE A 297     -20.687 -24.541   0.077  1.00 51.68           C  
ANISOU 2214  CA  ILE A 297     6885   6814   5938   -699   -722   -159       C  
ATOM   2215  C   ILE A 297     -20.764 -25.839   0.870  1.00 53.71           C  
ANISOU 2215  C   ILE A 297     7130   6989   6287   -737   -687   -192       C  
ATOM   2216  O   ILE A 297     -20.521 -26.923   0.330  1.00 56.11           O  
ANISOU 2216  O   ILE A 297     7486   7247   6587   -779   -670   -268       O  
ATOM   2217  CB  ILE A 297     -19.728 -23.544   0.752  1.00 45.69           C  
ANISOU 2217  CB  ILE A 297     6128   6043   5191   -628   -669    -92       C  
ATOM   2218  CG1 ILE A 297     -19.567 -22.291  -0.109  1.00 43.78           C  
ANISOU 2218  CG1 ILE A 297     5916   5863   4856   -597   -691    -58       C  
ATOM   2219  CG2 ILE A 297     -18.374 -24.191   0.994  1.00 42.61           C  
ANISOU 2219  CG2 ILE A 297     5779   5583   4829   -609   -589   -123       C  
ATOM   2220  CD1 ILE A 297     -18.610 -21.270   0.467  1.00 42.41           C  
ANISOU 2220  CD1 ILE A 297     5748   5673   4694   -543   -637     -1       C  
ATOM   2221  N   SER A 298     -21.108 -25.736   2.156  1.00 54.82           N  
ANISOU 2221  N   SER A 298     7214   7108   6507   -719   -670   -136       N  
ATOM   2222  CA  SER A 298     -21.055 -26.899   3.037  1.00 53.63           C  
ANISOU 2222  CA  SER A 298     7067   6870   6441   -743   -622   -149       C  
ATOM   2223  C   SER A 298     -22.098 -27.941   2.652  1.00 53.87           C  
ANISOU 2223  C   SER A 298     7085   6886   6498   -837   -655   -209       C  
ATOM   2224  O   SER A 298     -21.770 -29.117   2.452  1.00 54.00           O  
ANISOU 2224  O   SER A 298     7159   6823   6537   -875   -622   -270       O  
ATOM   2225  CB  SER A 298     -21.242 -26.463   4.490  1.00 53.45           C  
ANISOU 2225  CB  SER A 298     6993   6836   6482   -700   -597    -70       C  
ATOM   2226  OG  SER A 298     -20.128 -25.717   4.944  1.00 56.27           O  
ANISOU 2226  OG  SER A 298     7369   7187   6825   -622   -563    -30       O  
ATOM   2227  N   ILE A 299     -23.364 -27.531   2.550  1.00 53.52           N  
ANISOU 2227  N   ILE A 299     6963   6916   6455   -875   -719   -195       N  
ATOM   2228  CA  ILE A 299     -24.432 -28.490   2.266  1.00 58.02           C  
ANISOU 2228  CA  ILE A 299     7503   7481   7063   -978   -754   -254       C  
ATOM   2229  C   ILE A 299     -24.282 -29.133   0.887  1.00 58.64           C  
ANISOU 2229  C   ILE A 299     7647   7559   7075  -1034   -791   -355       C  
ATOM   2230  O   ILE A 299     -24.346 -30.367   0.800  1.00 61.05           O  
ANISOU 2230  O   ILE A 299     7992   7783   7421  -1106   -767   -422       O  
ATOM   2231  CB  ILE A 299     -25.807 -27.829   2.469  1.00 57.73           C  
ANISOU 2231  CB  ILE A 299     7348   7540   7045   -999   -817   -217       C  
ATOM   2232  CG1 ILE A 299     -25.934 -27.295   3.896  1.00 54.57           C  
ANISOU 2232  CG1 ILE A 299     6895   7131   6710   -943   -766   -125       C  
ATOM   2233  CG2 ILE A 299     -26.924 -28.816   2.166  1.00 56.67           C  
ANISOU 2233  CG2 ILE A 299     7165   7410   6959  -1118   -855   -284       C  
ATOM   2234  CD1 ILE A 299     -25.684 -28.338   4.960  1.00 55.26           C  
ANISOU 2234  CD1 ILE A 299     7010   7106   6880   -968   -681   -116       C  
ATOM   2235  N   PRO A 300     -24.087 -28.381  -0.205  1.00 51.05           N  
ANISOU 2235  N   PRO A 300     6711   6677   6008  -1005   -844   -370       N  
ATOM   2236  CA  PRO A 300     -23.930 -29.054  -1.508  1.00 47.97           C  
ANISOU 2236  CA  PRO A 300     6398   6286   5544  -1057   -874   -472       C  
ATOM   2237  C   PRO A 300     -22.725 -29.973  -1.578  1.00 50.26           C  
ANISOU 2237  C   PRO A 300     6791   6463   5841  -1046   -788   -523       C  
ATOM   2238  O   PRO A 300     -22.791 -31.011  -2.247  1.00 54.21           O  
ANISOU 2238  O   PRO A 300     7350   6917   6329  -1113   -792   -620       O  
ATOM   2239  CB  PRO A 300     -23.803 -27.882  -2.492  1.00 43.39           C  
ANISOU 2239  CB  PRO A 300     5834   5811   4841  -1003   -931   -451       C  
ATOM   2240  CG  PRO A 300     -24.478 -26.755  -1.814  1.00 43.33           C  
ANISOU 2240  CG  PRO A 300     5730   5873   4859   -956   -965   -355       C  
ATOM   2241  CD  PRO A 300     -24.124 -26.918  -0.369  1.00 43.53           C  
ANISOU 2241  CD  PRO A 300     5727   5819   4994   -929   -882   -299       C  
ATOM   2242  N   ALA A 301     -21.623 -29.629  -0.908  1.00 46.00           N  
ANISOU 2242  N   ALA A 301     6275   5881   5323   -961   -711   -465       N  
ATOM   2243  CA  ALA A 301     -20.458 -30.508  -0.920  1.00 45.24           C  
ANISOU 2243  CA  ALA A 301     6264   5684   5242   -936   -628   -510       C  
ATOM   2244  C   ALA A 301     -20.717 -31.775  -0.115  1.00 47.22           C  
ANISOU 2244  C   ALA A 301     6525   5819   5596   -982   -588   -532       C  
ATOM   2245  O   ALA A 301     -20.339 -32.874  -0.539  1.00 48.51           O  
ANISOU 2245  O   ALA A 301     6769   5896   5765  -1010   -552   -612       O  
ATOM   2246  CB  ALA A 301     -19.232 -29.769  -0.384  1.00 41.14           C  
ANISOU 2246  CB  ALA A 301     5747   5161   4722   -834   -566   -444       C  
ATOM   2247  N   ALA A 302     -21.363 -31.644   1.046  1.00 46.65           N  
ANISOU 2247  N   ALA A 302     6381   5739   5604   -989   -587   -461       N  
ATOM   2248  CA  ALA A 302     -21.669 -32.817   1.860  1.00 49.38           C  
ANISOU 2248  CA  ALA A 302     6744   5972   6047  -1037   -541   -468       C  
ATOM   2249  C   ALA A 302     -22.664 -33.734   1.159  1.00 57.13           C  
ANISOU 2249  C   ALA A 302     7736   6932   7041  -1163   -581   -560       C  
ATOM   2250  O   ALA A 302     -22.512 -34.962   1.189  1.00 61.44           O  
ANISOU 2250  O   ALA A 302     8354   7356   7633  -1208   -535   -616       O  
ATOM   2251  CB  ALA A 302     -22.206 -32.384   3.223  1.00 43.71           C  
ANISOU 2251  CB  ALA A 302     5947   5264   5397  -1018   -526   -368       C  
ATOM   2252  N   VAL A 303     -23.686 -33.159   0.521  1.00 52.57           N  
ANISOU 2252  N   VAL A 303     7085   6467   6422  -1221   -671   -578       N  
ATOM   2253  CA  VAL A 303     -24.671 -33.970  -0.188  1.00 52.62           C  
ANISOU 2253  CA  VAL A 303     7087   6470   6436  -1349   -725   -674       C  
ATOM   2254  C   VAL A 303     -24.035 -34.651  -1.394  1.00 53.24           C  
ANISOU 2254  C   VAL A 303     7283   6506   6442  -1368   -727   -787       C  
ATOM   2255  O   VAL A 303     -24.339 -35.810  -1.703  1.00 54.06           O  
ANISOU 2255  O   VAL A 303     7439   6522   6578  -1463   -720   -879       O  
ATOM   2256  CB  VAL A 303     -25.879 -33.106  -0.596  1.00 52.34           C  
ANISOU 2256  CB  VAL A 303     6934   6585   6368  -1389   -833   -664       C  
ATOM   2257  CG1 VAL A 303     -26.806 -33.879  -1.522  1.00 50.80           C  
ANISOU 2257  CG1 VAL A 303     6732   6408   6163  -1521   -909   -780       C  
ATOM   2258  CG2 VAL A 303     -26.633 -32.631   0.636  1.00 54.82           C  
ANISOU 2258  CG2 VAL A 303     7133   6929   6769  -1382   -819   -566       C  
ATOM   2259  N   ALA A 304     -23.134 -33.950  -2.087  1.00 53.92           N  
ANISOU 2259  N   ALA A 304     7415   6646   6426  -1281   -728   -785       N  
ATOM   2260  CA  ALA A 304     -22.528 -34.504  -3.293  1.00 53.80           C  
ANISOU 2260  CA  ALA A 304     7512   6605   6326  -1291   -724   -893       C  
ATOM   2261  C   ALA A 304     -21.684 -35.737  -2.995  1.00 56.37           C  
ANISOU 2261  C   ALA A 304     7939   6767   6711  -1280   -624   -940       C  
ATOM   2262  O   ALA A 304     -21.559 -36.617  -3.852  1.00 59.71           O  
ANISOU 2262  O   ALA A 304     8455   7132   7098  -1329   -620  -1054       O  
ATOM   2263  CB  ALA A 304     -21.678 -33.443  -3.991  1.00 52.22           C  
ANISOU 2263  CB  ALA A 304     7337   6493   6010  -1195   -724   -865       C  
ATOM   2264  N   PHE A 305     -21.105 -35.824  -1.798  1.00 56.57           N  
ANISOU 2264  N   PHE A 305     7954   6717   6822  -1211   -546   -857       N  
ATOM   2265  CA  PHE A 305     -20.222 -36.931  -1.453  1.00 54.47           C  
ANISOU 2265  CA  PHE A 305     7786   6298   6612  -1175   -452   -887       C  
ATOM   2266  C   PHE A 305     -20.910 -38.040  -0.670  1.00 57.80           C  
ANISOU 2266  C   PHE A 305     8223   6592   7146  -1256   -424   -893       C  
ATOM   2267  O   PHE A 305     -20.505 -39.202  -0.785  1.00 58.33           O  
ANISOU 2267  O   PHE A 305     8395   6520   7246  -1268   -365   -959       O  
ATOM   2268  CB  PHE A 305     -19.024 -36.422  -0.644  1.00 54.86           C  
ANISOU 2268  CB  PHE A 305     7826   6339   6680  -1037   -384   -795       C  
ATOM   2269  CG  PHE A 305     -17.780 -36.232  -1.461  1.00 59.04           C  
ANISOU 2269  CG  PHE A 305     8414   6887   7132   -952   -344   -836       C  
ATOM   2270  CD1 PHE A 305     -17.673 -35.172  -2.345  1.00 61.62           C  
ANISOU 2270  CD1 PHE A 305     8715   7344   7353   -938   -387   -838       C  
ATOM   2271  CD2 PHE A 305     -16.719 -37.115  -1.348  1.00 61.76           C  
ANISOU 2271  CD2 PHE A 305     8840   7117   7508   -882   -259   -869       C  
ATOM   2272  CE1 PHE A 305     -16.531 -34.993  -3.101  1.00 63.90           C  
ANISOU 2272  CE1 PHE A 305     9057   7652   7572   -867   -336   -874       C  
ATOM   2273  CE2 PHE A 305     -15.573 -36.942  -2.101  1.00 64.64           C  
ANISOU 2273  CE2 PHE A 305     9247   7506   7807   -803   -212   -909       C  
ATOM   2274  CZ  PHE A 305     -15.479 -35.880  -2.979  1.00 66.47           C  
ANISOU 2274  CZ  PHE A 305     9450   7870   7934   -801   -247   -912       C  
ATOM   2275  N   PHE A 306     -21.934 -37.718   0.119  1.00 60.67           N  
ANISOU 2275  N   PHE A 306     8488   6995   7569  -1313   -455   -825       N  
ATOM   2276  CA  PHE A 306     -22.586 -38.702   0.975  1.00 59.28           C  
ANISOU 2276  CA  PHE A 306     8322   6699   7504  -1392   -413   -814       C  
ATOM   2277  C   PHE A 306     -24.089 -38.819   0.774  1.00 56.72           C  
ANISOU 2277  C   PHE A 306     7916   6424   7212  -1544   -481   -852       C  
ATOM   2278  O   PHE A 306     -24.672 -39.804   1.243  1.00 59.99           O  
ANISOU 2278  O   PHE A 306     8352   6726   7717  -1641   -442   -870       O  
ATOM   2279  CB  PHE A 306     -22.320 -38.386   2.455  1.00 56.64           C  
ANISOU 2279  CB  PHE A 306     7949   6338   7234  -1309   -354   -681       C  
ATOM   2280  CG  PHE A 306     -20.878 -38.116   2.768  1.00 54.81           C  
ANISOU 2280  CG  PHE A 306     7766   6084   6974  -1155   -302   -634       C  
ATOM   2281  CD1 PHE A 306     -19.988 -39.161   2.950  1.00 59.10           C  
ANISOU 2281  CD1 PHE A 306     8423   6480   7551  -1102   -225   -658       C  
ATOM   2282  CD2 PHE A 306     -20.412 -36.817   2.885  1.00 54.50           C  
ANISOU 2282  CD2 PHE A 306     7657   6170   6880  -1064   -330   -569       C  
ATOM   2283  CE1 PHE A 306     -18.660 -38.916   3.240  1.00 59.13           C  
ANISOU 2283  CE1 PHE A 306     8455   6476   7536   -958   -183   -618       C  
ATOM   2284  CE2 PHE A 306     -19.086 -36.566   3.175  1.00 56.26           C  
ANISOU 2284  CE2 PHE A 306     7911   6380   7085   -934   -284   -533       C  
ATOM   2285  CZ  PHE A 306     -18.209 -37.617   3.353  1.00 56.26           C  
ANISOU 2285  CZ  PHE A 306     8009   6247   7120   -879   -214   -558       C  
ATOM   2286  N   GLY A 307     -24.733 -37.868   0.110  1.00 55.12           N  
ANISOU 2286  N   GLY A 307     7619   6382   6942  -1569   -579   -863       N  
ATOM   2287  CA  GLY A 307     -26.175 -37.865  -0.023  1.00 57.63           C  
ANISOU 2287  CA  GLY A 307     7831   6771   7295  -1700   -653   -892       C  
ATOM   2288  C   GLY A 307     -26.843 -36.994   1.028  1.00 57.93           C  
ANISOU 2288  C   GLY A 307     7733   6893   7383  -1676   -656   -772       C  
ATOM   2289  O   GLY A 307     -26.236 -36.556   2.008  1.00 58.42           O  
ANISOU 2289  O   GLY A 307     7797   6933   7466  -1571   -593   -668       O  
ATOM   2290  N   VAL A 308     -28.135 -36.744   0.807  1.00 54.95           N  
ANISOU 2290  N   VAL A 308     7234   6619   7026  -1774   -735   -793       N  
ATOM   2291  CA  VAL A 308     -28.884 -35.861   1.697  1.00 53.04           C  
ANISOU 2291  CA  VAL A 308     6852   6473   6828  -1749   -743   -689       C  
ATOM   2292  C   VAL A 308     -29.014 -36.481   3.083  1.00 53.91           C  
ANISOU 2292  C   VAL A 308     6964   6468   7053  -1771   -632   -617       C  
ATOM   2293  O   VAL A 308     -28.814 -35.810   4.102  1.00 56.25           O  
ANISOU 2293  O   VAL A 308     7225   6782   7364  -1678   -584   -506       O  
ATOM   2294  CB  VAL A 308     -30.262 -35.534   1.094  1.00 54.76           C  
ANISOU 2294  CB  VAL A 308     6928   6831   7046  -1847   -854   -736       C  
ATOM   2295  CG1 VAL A 308     -31.205 -35.007   2.166  1.00 45.87           C  
ANISOU 2295  CG1 VAL A 308     5654   5770   6003  -1852   -834   -643       C  
ATOM   2296  CG2 VAL A 308     -30.121 -34.527  -0.037  1.00 53.49           C  
ANISOU 2296  CG2 VAL A 308     6755   6814   6757  -1778   -965   -760       C  
ATOM   2297  N   ALA A 309     -29.343 -37.775   3.141  1.00 54.26           N  
ANISOU 2297  N   ALA A 309     7058   6384   7173  -1895   -586   -679       N  
ATOM   2298  CA  ALA A 309     -29.578 -38.429   4.425  1.00 53.03           C  
ANISOU 2298  CA  ALA A 309     6912   6112   7125  -1930   -475   -608       C  
ATOM   2299  C   ALA A 309     -28.340 -38.385   5.312  1.00 58.27           C  
ANISOU 2299  C   ALA A 309     7683   6682   7775  -1784   -385   -516       C  
ATOM   2300  O   ALA A 309     -28.437 -38.100   6.511  1.00 59.68           O  
ANISOU 2300  O   ALA A 309     7829   6854   7993  -1735   -321   -408       O  
ATOM   2301  CB  ALA A 309     -30.025 -39.873   4.201  1.00 48.35           C  
ANISOU 2301  CB  ALA A 309     6381   5378   6611  -2091   -438   -699       C  
ATOM   2302  N   ASN A 310     -27.166 -38.664   4.742  1.00 59.01           N  
ANISOU 2302  N   ASN A 310     7902   6709   7810  -1709   -379   -559       N  
ATOM   2303  CA  ASN A 310     -25.944 -38.628   5.537  1.00 55.15           C  
ANISOU 2303  CA  ASN A 310     7503   6144   7309  -1565   -304   -479       C  
ATOM   2304  C   ASN A 310     -25.498 -37.199   5.819  1.00 55.24           C  
ANISOU 2304  C   ASN A 310     7445   6290   7255  -1433   -339   -399       C  
ATOM   2305  O   ASN A 310     -24.845 -36.945   6.837  1.00 55.73           O  
ANISOU 2305  O   ASN A 310     7530   6322   7322  -1328   -283   -308       O  
ATOM   2306  CB  ASN A 310     -24.833 -39.405   4.833  1.00 52.40           C  
ANISOU 2306  CB  ASN A 310     7298   5685   6929  -1523   -281   -556       C  
ATOM   2307  CG  ASN A 310     -25.080 -40.899   4.832  1.00 54.42           C  
ANISOU 2307  CG  ASN A 310     7655   5763   7260  -1629   -220   -617       C  
ATOM   2308  OD1 ASN A 310     -25.807 -41.420   5.678  1.00 60.81           O  
ANISOU 2308  OD1 ASN A 310     8450   6502   8154  -1707   -166   -572       O  
ATOM   2309  ND2 ASN A 310     -24.475 -41.598   3.879  1.00 52.59           N  
ANISOU 2309  ND2 ASN A 310     7533   5453   6997  -1635   -221   -722       N  
ATOM   2310  N   ALA A 311     -25.837 -36.256   4.935  1.00 56.21           N  
ANISOU 2310  N   ALA A 311     7487   6559   7311  -1436   -432   -432       N  
ATOM   2311  CA  ALA A 311     -25.484 -34.861   5.177  1.00 55.79           C  
ANISOU 2311  CA  ALA A 311     7374   6625   7199  -1321   -462   -358       C  
ATOM   2312  C   ALA A 311     -26.266 -34.280   6.348  1.00 54.36           C  
ANISOU 2312  C   ALA A 311     7094   6494   7068  -1312   -441   -260       C  
ATOM   2313  O   ALA A 311     -25.739 -33.443   7.090  1.00 54.31           O  
ANISOU 2313  O   ALA A 311     7078   6520   7039  -1203   -421   -179       O  
ATOM   2314  CB  ALA A 311     -25.718 -34.031   3.916  1.00 56.74           C  
ANISOU 2314  CB  ALA A 311     7447   6879   7234  -1326   -563   -412       C  
ATOM   2315  N   VAL A 312     -27.517 -34.707   6.528  1.00 55.24           N  
ANISOU 2315  N   VAL A 312     7129   6613   7247  -1429   -441   -273       N  
ATOM   2316  CA  VAL A 312     -28.301 -34.247   7.670  1.00 55.34           C  
ANISOU 2316  CA  VAL A 312     7048   6668   7311  -1425   -404   -183       C  
ATOM   2317  C   VAL A 312     -27.744 -34.825   8.964  1.00 55.59           C  
ANISOU 2317  C   VAL A 312     7163   6574   7384  -1378   -294   -106       C  
ATOM   2318  O   VAL A 312     -27.677 -34.137   9.990  1.00 54.29           O  
ANISOU 2318  O   VAL A 312     6971   6442   7213  -1295   -259    -15       O  
ATOM   2319  CB  VAL A 312     -29.785 -34.611   7.477  1.00 55.76           C  
ANISOU 2319  CB  VAL A 312     6986   6767   7433  -1571   -427   -222       C  
ATOM   2320  CG1 VAL A 312     -30.595 -34.230   8.707  1.00 56.65           C  
ANISOU 2320  CG1 VAL A 312     7002   6917   7604  -1568   -368   -130       C  
ATOM   2321  CG2 VAL A 312     -30.339 -33.929   6.238  1.00 56.33           C  
ANISOU 2321  CG2 VAL A 312     6969   6982   7451  -1597   -552   -290       C  
ATOM   2322  N   ALA A 313     -27.329 -36.094   8.938  1.00 57.40           N  
ANISOU 2322  N   ALA A 313     7505   6656   7650  -1424   -239   -142       N  
ATOM   2323  CA  ALA A 313     -26.770 -36.714  10.134  1.00 56.15           C  
ANISOU 2323  CA  ALA A 313     7441   6369   7523  -1370   -138    -65       C  
ATOM   2324  C   ALA A 313     -25.419 -36.114  10.501  1.00 58.49           C  
ANISOU 2324  C   ALA A 313     7799   6671   7753  -1205   -138    -16       C  
ATOM   2325  O   ALA A 313     -25.070 -36.058  11.686  1.00 59.46           O  
ANISOU 2325  O   ALA A 313     7956   6756   7879  -1127    -79     73       O  
ATOM   2326  CB  ALA A 313     -26.644 -38.223   9.934  1.00 54.84           C  
ANISOU 2326  CB  ALA A 313     7390   6034   7413  -1453    -82   -118       C  
ATOM   2327  N   ILE A 314     -24.649 -35.665   9.508  1.00 58.41           N  
ANISOU 2327  N   ILE A 314     7804   6711   7680  -1154   -201    -73       N  
ATOM   2328  CA  ILE A 314     -23.354 -35.055   9.794  1.00 55.33           C  
ANISOU 2328  CA  ILE A 314     7454   6334   7233  -1009   -202    -35       C  
ATOM   2329  C   ILE A 314     -23.536 -33.717  10.500  1.00 56.39           C  
ANISOU 2329  C   ILE A 314     7504   6586   7337   -940   -224     42       C  
ATOM   2330  O   ILE A 314     -22.850 -33.421  11.487  1.00 57.04           O  
ANISOU 2330  O   ILE A 314     7615   6653   7404   -840   -192    111       O  
ATOM   2331  CB  ILE A 314     -22.535 -34.909   8.498  1.00 53.20           C  
ANISOU 2331  CB  ILE A 314     7216   6091   6906   -983   -252   -118       C  
ATOM   2332  CG1 ILE A 314     -21.967 -36.263   8.065  1.00 54.04           C  
ANISOU 2332  CG1 ILE A 314     7438   6056   7037  -1004   -210   -183       C  
ATOM   2333  CG2 ILE A 314     -21.416 -33.900   8.683  1.00 53.46           C  
ANISOU 2333  CG2 ILE A 314     7244   6187   6880   -852   -268    -79       C  
ATOM   2334  CD1 ILE A 314     -21.150 -36.200   6.791  1.00 53.67           C  
ANISOU 2334  CD1 ILE A 314     7430   6031   6930   -977   -245   -270       C  
ATOM   2335  N   ALA A 315     -24.466 -32.891  10.014  1.00 58.12           N  
ANISOU 2335  N   ALA A 315     7619   6922   7544   -988   -281     29       N  
ATOM   2336  CA  ALA A 315     -24.743 -31.612  10.658  1.00 58.26           C  
ANISOU 2336  CA  ALA A 315     7559   7043   7536   -924   -298     97       C  
ATOM   2337  C   ALA A 315     -25.351 -31.777  12.044  1.00 61.07           C  
ANISOU 2337  C   ALA A 315     7898   7371   7937   -924   -228    176       C  
ATOM   2338  O   ALA A 315     -25.214 -30.875  12.877  1.00 62.73           O  
ANISOU 2338  O   ALA A 315     8085   7631   8120   -841   -220    241       O  
ATOM   2339  CB  ALA A 315     -25.672 -30.773   9.782  1.00 55.25           C  
ANISOU 2339  CB  ALA A 315     7073   6785   7134   -969   -375     65       C  
ATOM   2340  N   LYS A 316     -26.014 -32.902  12.311  1.00 61.94           N  
ANISOU 2340  N   LYS A 316     8023   7397   8112  -1019   -173    172       N  
ATOM   2341  CA  LYS A 316     -26.576 -33.162  13.629  1.00 63.45           C  
ANISOU 2341  CA  LYS A 316     8213   7553   8344  -1025    -89    252       C  
ATOM   2342  C   LYS A 316     -25.560 -33.748  14.599  1.00 64.32           C  
ANISOU 2342  C   LYS A 316     8448   7551   8441   -940    -25    309       C  
ATOM   2343  O   LYS A 316     -25.849 -33.826  15.797  1.00 66.92           O  
ANISOU 2343  O   LYS A 316     8792   7855   8778   -917     44    388       O  
ATOM   2344  CB  LYS A 316     -27.775 -34.108  13.514  1.00 62.90           C  
ANISOU 2344  CB  LYS A 316     8103   7440   8355  -1175    -48    227       C  
ATOM   2345  CG  LYS A 316     -29.052 -33.438  13.031  1.00 59.05           C  
ANISOU 2345  CG  LYS A 316     7460   7084   7891  -1249    -98    200       C  
ATOM   2346  CD  LYS A 316     -30.166 -34.452  12.828  1.00 58.96           C  
ANISOU 2346  CD  LYS A 316     7402   7032   7969  -1413    -64    161       C  
ATOM   2347  CE  LYS A 316     -31.461 -33.770  12.421  1.00 61.13           C  
ANISOU 2347  CE  LYS A 316     7502   7453   8272  -1477   -117    137       C  
ATOM   2348  NZ  LYS A 316     -32.504 -34.754  12.022  1.00 65.00           N  
ANISOU 2348  NZ  LYS A 316     7931   7915   8851  -1653   -103     76       N  
ATOM   2349  N   ALA A 317     -24.387 -34.161  14.114  1.00 65.58           N  
ANISOU 2349  N   ALA A 317     8695   7646   8575   -886    -45    273       N  
ATOM   2350  CA  ALA A 317     -23.374 -34.718  15.004  1.00 66.33           C  
ANISOU 2350  CA  ALA A 317     8903   7643   8657   -790      5    326       C  
ATOM   2351  C   ALA A 317     -22.703 -33.628  15.830  1.00 67.36           C  
ANISOU 2351  C   ALA A 317     9020   7850   8724   -661    -16    386       C  
ATOM   2352  O   ALA A 317     -22.370 -33.844  17.001  1.00 71.79           O  
ANISOU 2352  O   ALA A 317     9643   8364   9269   -591     31    459       O  
ATOM   2353  CB  ALA A 317     -22.337 -35.497  14.196  1.00 65.73           C  
ANISOU 2353  CB  ALA A 317     8913   7482   8580   -766     -8    263       C  
ATOM   2354  N   GLY A 318     -22.498 -32.455  15.241  1.00 64.01           N  
ANISOU 2354  N   GLY A 318     8523   7539   8259   -631    -86    355       N  
ATOM   2355  CA  GLY A 318     -21.875 -31.358  15.952  1.00 63.48           C  
ANISOU 2355  CA  GLY A 318     8442   7542   8136   -523   -110    398       C  
ATOM   2356  C   GLY A 318     -21.956 -30.081  15.149  1.00 64.77           C  
ANISOU 2356  C   GLY A 318     8522   7821   8268   -521   -180    361       C  
ATOM   2357  O   GLY A 318     -22.229 -30.096  13.944  1.00 67.17           O  
ANISOU 2357  O   GLY A 318     8791   8150   8580   -585   -218    299       O  
ATOM   2358  N   ALA A 319     -21.711 -28.966  15.841  1.00 60.48           N  
ANISOU 2358  N   ALA A 319     7954   7344   7682   -445   -196    400       N  
ATOM   2359  CA  ALA A 319     -21.755 -27.666  15.180  1.00 53.91           C  
ANISOU 2359  CA  ALA A 319     7057   6610   6818   -434   -255    375       C  
ATOM   2360  C   ALA A 319     -20.549 -27.466  14.271  1.00 50.86           C  
ANISOU 2360  C   ALA A 319     6694   6228   6404   -403   -298    324       C  
ATOM   2361  O   ALA A 319     -20.666 -26.856  13.201  1.00 51.83           O  
ANISOU 2361  O   ALA A 319     6779   6406   6510   -431   -342    284       O  
ATOM   2362  CB  ALA A 319     -21.836 -26.550  16.221  1.00 50.70           C  
ANISOU 2362  CB  ALA A 319     6630   6258   6376   -364   -253    427       C  
ATOM   2363  N   PHE A 320     -19.385 -27.972  14.675  1.00 49.72           N  
ANISOU 2363  N   PHE A 320     6610   6029   6253   -342   -284    326       N  
ATOM   2364  CA  PHE A 320     -18.161 -27.848  13.896  1.00 49.50           C  
ANISOU 2364  CA  PHE A 320     6596   6006   6207   -308   -312    278       C  
ATOM   2365  C   PHE A 320     -17.865 -29.091  13.066  1.00 52.30           C  
ANISOU 2365  C   PHE A 320     6997   6288   6588   -342   -293    227       C  
ATOM   2366  O   PHE A 320     -16.810 -29.159  12.428  1.00 54.74           O  
ANISOU 2366  O   PHE A 320     7322   6593   6885   -309   -302    185       O  
ATOM   2367  CB  PHE A 320     -16.977 -27.543  14.817  1.00 45.65           C  
ANISOU 2367  CB  PHE A 320     6129   5518   5696   -210   -316    304       C  
ATOM   2368  CG  PHE A 320     -17.302 -26.583  15.926  1.00 46.70           C  
ANISOU 2368  CG  PHE A 320     6243   5699   5803   -172   -324    356       C  
ATOM   2369  CD1 PHE A 320     -17.543 -25.246  15.656  1.00 48.14           C  
ANISOU 2369  CD1 PHE A 320     6375   5955   5959   -179   -356    350       C  
ATOM   2370  CD2 PHE A 320     -17.368 -27.018  17.240  1.00 41.43           C  
ANISOU 2370  CD2 PHE A 320     5617   4996   5130   -125   -295    411       C  
ATOM   2371  CE1 PHE A 320     -17.843 -24.361  16.677  1.00 46.42           C  
ANISOU 2371  CE1 PHE A 320     6149   5774   5716   -141   -359    389       C  
ATOM   2372  CE2 PHE A 320     -17.668 -26.139  18.263  1.00 38.92           C  
ANISOU 2372  CE2 PHE A 320     5289   4722   4777    -87   -299    451       C  
ATOM   2373  CZ  PHE A 320     -17.906 -24.809  17.981  1.00 40.53           C  
ANISOU 2373  CZ  PHE A 320     5442   4998   4961    -96   -330    437       C  
ATOM   2374  N   ASN A 321     -18.770 -30.072  13.057  1.00 52.89           N  
ANISOU 2374  N   ASN A 321     7094   6301   6702   -411   -262    227       N  
ATOM   2375  CA  ASN A 321     -18.508 -31.310  12.332  1.00 55.06           C  
ANISOU 2375  CA  ASN A 321     7427   6489   7004   -445   -239    173       C  
ATOM   2376  C   ASN A 321     -18.507 -31.100  10.823  1.00 56.04           C  
ANISOU 2376  C   ASN A 321     7531   6656   7106   -499   -276     94       C  
ATOM   2377  O   ASN A 321     -17.860 -31.861  10.095  1.00 55.99           O  
ANISOU 2377  O   ASN A 321     7576   6594   7102   -497   -262     37       O  
ATOM   2378  CB  ASN A 321     -19.540 -32.370  12.717  1.00 59.12           C  
ANISOU 2378  CB  ASN A 321     7972   6921   7569   -521   -194    190       C  
ATOM   2379  CG  ASN A 321     -18.949 -33.762  12.772  1.00 68.48           C  
ANISOU 2379  CG  ASN A 321     9256   7975   8788   -505   -146    175       C  
ATOM   2380  OD1 ASN A 321     -18.733 -34.397  11.741  1.00 71.97           O  
ANISOU 2380  OD1 ASN A 321     9732   8374   9240   -543   -147    101       O  
ATOM   2381  ND2 ASN A 321     -18.681 -34.244  13.980  1.00 74.16           N  
ANISOU 2381  ND2 ASN A 321    10031   8627   9519   -441   -102    245       N  
ATOM   2382  N   LEU A 322     -19.214 -30.080  10.337  1.00 56.67           N  
ANISOU 2382  N   LEU A 322     7542   6832   7158   -538   -320     91       N  
ATOM   2383  CA  LEU A 322     -19.319 -29.829   8.904  1.00 54.58           C  
ANISOU 2383  CA  LEU A 322     7265   6615   6857   -587   -360     24       C  
ATOM   2384  C   LEU A 322     -18.149 -29.006   8.373  1.00 51.87           C  
ANISOU 2384  C   LEU A 322     6924   6321   6463   -522   -375      9       C  
ATOM   2385  O   LEU A 322     -17.476 -29.420   7.425  1.00 51.21           O  
ANISOU 2385  O   LEU A 322     6880   6220   6359   -525   -367    -52       O  
ATOM   2386  CB  LEU A 322     -20.643 -29.124   8.593  1.00 55.98           C  
ANISOU 2386  CB  LEU A 322     7368   6876   7025   -650   -406     32       C  
ATOM   2387  CG  LEU A 322     -21.628 -29.858   7.681  1.00 56.77           C  
ANISOU 2387  CG  LEU A 322     7460   6970   7139   -756   -430    -30       C  
ATOM   2388  CD1 LEU A 322     -22.783 -28.946   7.301  1.00 60.71           C  
ANISOU 2388  CD1 LEU A 322     7871   7577   7618   -794   -491    -20       C  
ATOM   2389  CD2 LEU A 322     -20.928 -30.390   6.440  1.00 52.86           C  
ANISOU 2389  CD2 LEU A 322     7028   6450   6607   -773   -439   -113       C  
ATOM   2390  N   GLY A 323     -17.891 -27.842   8.977  1.00 48.94           N  
ANISOU 2390  N   GLY A 323     6514   6009   6074   -468   -389     60       N  
ATOM   2391  CA  GLY A 323     -16.892 -26.933   8.444  1.00 44.39           C  
ANISOU 2391  CA  GLY A 323     5931   5483   5454   -426   -400     47       C  
ATOM   2392  C   GLY A 323     -15.464 -27.246   8.832  1.00 39.86           C  
ANISOU 2392  C   GLY A 323     5381   4873   4891   -354   -367     40       C  
ATOM   2393  O   GLY A 323     -14.540 -26.775   8.162  1.00 44.81           O  
ANISOU 2393  O   GLY A 323     6004   5532   5491   -334   -362     11       O  
ATOM   2394  N   PHE A 324     -15.257 -28.024   9.894  1.00 37.30           N  
ANISOU 2394  N   PHE A 324     5078   4485   4607   -313   -342     67       N  
ATOM   2395  CA  PHE A 324     -13.916 -28.340  10.363  1.00 38.31           C  
ANISOU 2395  CA  PHE A 324     5220   4587   4749   -231   -322     65       C  
ATOM   2396  C   PHE A 324     -13.493 -29.777  10.091  1.00 39.53           C  
ANISOU 2396  C   PHE A 324     5434   4651   4934   -214   -284     27       C  
ATOM   2397  O   PHE A 324     -12.297 -30.077  10.177  1.00 42.40           O  
ANISOU 2397  O   PHE A 324     5803   5000   5308   -140   -266     11       O  
ATOM   2398  CB  PHE A 324     -13.796 -28.062  11.870  1.00 40.40           C  
ANISOU 2398  CB  PHE A 324     5474   4851   5024   -169   -329    130       C  
ATOM   2399  CG  PHE A 324     -13.663 -26.605  12.211  1.00 44.95           C  
ANISOU 2399  CG  PHE A 324     5999   5509   5571   -156   -362    154       C  
ATOM   2400  CD1 PHE A 324     -12.443 -25.960  12.096  1.00 46.15           C  
ANISOU 2400  CD1 PHE A 324     6120   5702   5712   -114   -371    133       C  
ATOM   2401  CD2 PHE A 324     -14.758 -25.880  12.653  1.00 44.73           C  
ANISOU 2401  CD2 PHE A 324     5953   5512   5530   -186   -378    194       C  
ATOM   2402  CE1 PHE A 324     -12.317 -24.619  12.412  1.00 43.62           C  
ANISOU 2402  CE1 PHE A 324     5761   5443   5369   -111   -398    150       C  
ATOM   2403  CE2 PHE A 324     -14.638 -24.538  12.971  1.00 42.99           C  
ANISOU 2403  CE2 PHE A 324     5698   5352   5284   -171   -404    212       C  
ATOM   2404  CZ  PHE A 324     -13.416 -23.908  12.850  1.00 41.23           C  
ANISOU 2404  CZ  PHE A 324     5454   5160   5050   -137   -415    189       C  
ATOM   2405  N   ILE A 325     -14.428 -30.671   9.770  1.00 41.88           N  
ANISOU 2405  N   ILE A 325     5774   4888   5251   -280   -270     10       N  
ATOM   2406  CA  ILE A 325     -14.099 -32.080   9.581  1.00 44.71           C  
ANISOU 2406  CA  ILE A 325     6205   5141   5643   -267   -228    -26       C  
ATOM   2407  C   ILE A 325     -14.534 -32.546   8.198  1.00 52.40           C  
ANISOU 2407  C   ILE A 325     7208   6098   6602   -349   -225   -107       C  
ATOM   2408  O   ILE A 325     -13.719 -33.047   7.415  1.00 57.61           O  
ANISOU 2408  O   ILE A 325     7904   6729   7254   -322   -199   -168       O  
ATOM   2409  CB  ILE A 325     -14.743 -32.952  10.675  1.00 39.31           C  
ANISOU 2409  CB  ILE A 325     5567   4366   5001   -269   -203     28       C  
ATOM   2410  CG1 ILE A 325     -14.269 -32.513  12.061  1.00 39.12           C  
ANISOU 2410  CG1 ILE A 325     5526   4362   4975   -178   -209    106       C  
ATOM   2411  CG2 ILE A 325     -14.424 -34.420  10.444  1.00 36.92           C  
ANISOU 2411  CG2 ILE A 325     5355   3936   4736   -256   -155     -8       C  
ATOM   2412  CD1 ILE A 325     -14.901 -33.292  13.192  1.00 41.61           C  
ANISOU 2412  CD1 ILE A 325     5896   4594   5319   -175   -177    171       C  
ATOM   2413  N   THR A 326     -15.822 -32.383   7.888  1.00 53.02           N  
ANISOU 2413  N   THR A 326     7270   6201   6675   -448   -252   -111       N  
ATOM   2414  CA  THR A 326     -16.364 -32.942   6.654  1.00 54.51           C  
ANISOU 2414  CA  THR A 326     7491   6371   6849   -534   -259   -192       C  
ATOM   2415  C   THR A 326     -15.856 -32.189   5.430  1.00 53.04           C  
ANISOU 2415  C   THR A 326     7291   6270   6594   -532   -282   -243       C  
ATOM   2416  O   THR A 326     -15.363 -32.801   4.475  1.00 54.11           O  
ANISOU 2416  O   THR A 326     7480   6372   6707   -537   -259   -318       O  
ATOM   2417  CB  THR A 326     -17.892 -32.928   6.700  1.00 54.99           C  
ANISOU 2417  CB  THR A 326     7519   6449   6925   -639   -292   -182       C  
ATOM   2418  OG1 THR A 326     -18.337 -33.555   7.908  1.00 59.52           O  
ANISOU 2418  OG1 THR A 326     8107   6947   7561   -642   -257   -124       O  
ATOM   2419  CG2 THR A 326     -18.467 -33.679   5.508  1.00 55.08           C  
ANISOU 2419  CG2 THR A 326     7569   6433   6925   -736   -306   -275       C  
ATOM   2420  N   LEU A 327     -15.972 -30.862   5.437  1.00 47.16           N  
ANISOU 2420  N   LEU A 327     6480   5628   5809   -524   -319   -202       N  
ATOM   2421  CA  LEU A 327     -15.534 -30.082   4.282  1.00 50.16           C  
ANISOU 2421  CA  LEU A 327     6854   6085   6118   -525   -334   -238       C  
ATOM   2422  C   LEU A 327     -14.042 -30.218   3.989  1.00 54.41           C  
ANISOU 2422  C   LEU A 327     7417   6609   6647   -452   -282   -268       C  
ATOM   2423  O   LEU A 327     -13.690 -30.338   2.802  1.00 59.69           O  
ANISOU 2423  O   LEU A 327     8122   7294   7264   -468   -267   -333       O  
ATOM   2424  CB  LEU A 327     -15.924 -28.610   4.471  1.00 46.16           C  
ANISOU 2424  CB  LEU A 327     6284   5676   5580   -522   -377   -178       C  
ATOM   2425  CG  LEU A 327     -16.005 -27.785   3.186  1.00 48.36           C  
ANISOU 2425  CG  LEU A 327     6565   6034   5775   -550   -405   -204       C  
ATOM   2426  CD1 LEU A 327     -16.905 -28.467   2.169  1.00 47.95           C  
ANISOU 2426  CD1 LEU A 327     6548   5981   5690   -628   -439   -269       C  
ATOM   2427  CD2 LEU A 327     -16.501 -26.383   3.481  1.00 53.18           C  
ANISOU 2427  CD2 LEU A 327     7123   6722   6364   -542   -447   -137       C  
ATOM   2428  N   PRO A 328     -13.130 -30.203   4.971  1.00 52.79           N  
ANISOU 2428  N   PRO A 328     7189   6382   6485   -370   -254   -229       N  
ATOM   2429  CA  PRO A 328     -11.719 -30.466   4.634  1.00 49.69           C  
ANISOU 2429  CA  PRO A 328     6806   5980   6093   -300   -203   -267       C  
ATOM   2430  C   PRO A 328     -11.487 -31.858   4.075  1.00 47.64           C  
ANISOU 2430  C   PRO A 328     6622   5629   5848   -294   -160   -338       C  
ATOM   2431  O   PRO A 328     -10.705 -32.021   3.130  1.00 45.89           O  
ANISOU 2431  O   PRO A 328     6423   5418   5596   -274   -119   -400       O  
ATOM   2432  CB  PRO A 328     -10.994 -30.269   5.974  1.00 49.23           C  
ANISOU 2432  CB  PRO A 328     6703   5918   6085   -216   -201   -207       C  
ATOM   2433  CG  PRO A 328     -11.903 -29.431   6.783  1.00 47.25           C  
ANISOU 2433  CG  PRO A 328     6414   5705   5833   -247   -249   -138       C  
ATOM   2434  CD  PRO A 328     -13.284 -29.826   6.388  1.00 51.54           C  
ANISOU 2434  CD  PRO A 328     6990   6226   6368   -333   -271   -150       C  
ATOM   2435  N   ALA A 329     -12.143 -32.873   4.643  1.00 44.44           N  
ANISOU 2435  N   ALA A 329     6264   5130   5491   -312   -160   -332       N  
ATOM   2436  CA  ALA A 329     -11.980 -34.234   4.142  1.00 42.42           C  
ANISOU 2436  CA  ALA A 329     6094   4768   5254   -310   -116   -403       C  
ATOM   2437  C   ALA A 329     -12.540 -34.375   2.732  1.00 51.35           C  
ANISOU 2437  C   ALA A 329     7269   5915   6325   -399   -125   -488       C  
ATOM   2438  O   ALA A 329     -11.976 -35.100   1.904  1.00 55.50           O  
ANISOU 2438  O   ALA A 329     7859   6394   6834   -381    -80   -568       O  
ATOM   2439  CB  ALA A 329     -12.653 -35.226   5.090  1.00 37.96           C  
ANISOU 2439  CB  ALA A 329     5577   4091   4756   -324   -110   -370       C  
ATOM   2440  N   ILE A 330     -13.649 -33.691   2.441  1.00 50.50           N  
ANISOU 2440  N   ILE A 330     7130   5876   6180   -488   -185   -475       N  
ATOM   2441  CA  ILE A 330     -14.202 -33.718   1.091  1.00 50.84           C  
ANISOU 2441  CA  ILE A 330     7211   5953   6151   -568   -211   -553       C  
ATOM   2442  C   ILE A 330     -13.243 -33.054   0.112  1.00 52.67           C  
ANISOU 2442  C   ILE A 330     7446   6261   6307   -527   -184   -585       C  
ATOM   2443  O   ILE A 330     -12.992 -33.572  -0.983  1.00 59.32           O  
ANISOU 2443  O   ILE A 330     8356   7088   7096   -542   -158   -672       O  
ATOM   2444  CB  ILE A 330     -15.589 -33.051   1.071  1.00 48.92           C  
ANISOU 2444  CB  ILE A 330     6918   5781   5887   -657   -290   -522       C  
ATOM   2445  CG1 ILE A 330     -16.629 -33.967   1.716  1.00 45.92           C  
ANISOU 2445  CG1 ILE A 330     6549   5320   5580   -726   -302   -521       C  
ATOM   2446  CG2 ILE A 330     -15.998 -32.697  -0.351  1.00 48.58           C  
ANISOU 2446  CG2 ILE A 330     6898   5814   5747   -717   -332   -587       C  
ATOM   2447  CD1 ILE A 330     -18.008 -33.362   1.782  1.00 47.33           C  
ANISOU 2447  CD1 ILE A 330     6658   5572   5752   -808   -375   -491       C  
ATOM   2448  N   PHE A 331     -12.685 -31.902   0.494  1.00 48.65           N  
ANISOU 2448  N   PHE A 331     6865   5830   5788   -478   -185   -518       N  
ATOM   2449  CA  PHE A 331     -11.727 -31.221  -0.370  1.00 47.13           C  
ANISOU 2449  CA  PHE A 331     6669   5707   5530   -445   -146   -539       C  
ATOM   2450  C   PHE A 331     -10.483 -32.071  -0.591  1.00 54.62           C  
ANISOU 2450  C   PHE A 331     7654   6599   6502   -371    -62   -596       C  
ATOM   2451  O   PHE A 331      -9.953 -32.129  -1.707  1.00 57.80           O  
ANISOU 2451  O   PHE A 331     8098   7026   6839   -368    -17   -661       O  
ATOM   2452  CB  PHE A 331     -11.346 -29.867   0.230  1.00 42.77           C  
ANISOU 2452  CB  PHE A 331     6035   5234   4982   -413   -157   -455       C  
ATOM   2453  CG  PHE A 331     -12.423 -28.826   0.118  1.00 44.05           C  
ANISOU 2453  CG  PHE A 331     6171   5466   5099   -472   -228   -407       C  
ATOM   2454  CD1 PHE A 331     -12.420 -27.717   0.948  1.00 44.67           C  
ANISOU 2454  CD1 PHE A 331     6183   5589   5199   -452   -251   -326       C  
ATOM   2455  CD2 PHE A 331     -13.436 -28.953  -0.818  1.00 48.43           C  
ANISOU 2455  CD2 PHE A 331     6770   6043   5589   -543   -275   -446       C  
ATOM   2456  CE1 PHE A 331     -13.408 -26.754   0.848  1.00 50.78           C  
ANISOU 2456  CE1 PHE A 331     6937   6423   5935   -493   -312   -280       C  
ATOM   2457  CE2 PHE A 331     -14.428 -27.995  -0.922  1.00 51.09           C  
ANISOU 2457  CE2 PHE A 331     7076   6450   5886   -583   -345   -398       C  
ATOM   2458  CZ  PHE A 331     -14.413 -26.894  -0.088  1.00 51.67           C  
ANISOU 2458  CZ  PHE A 331     7086   6561   5986   -553   -360   -313       C  
ATOM   2459  N   SER A 332     -10.014 -32.754   0.458  1.00 56.91           N  
ANISOU 2459  N   SER A 332     7929   6814   6879   -304    -39   -573       N  
ATOM   2460  CA  SER A 332      -8.791 -33.546   0.366  1.00 57.57           C  
ANISOU 2460  CA  SER A 332     8034   6846   6995   -213     38   -620       C  
ATOM   2461  C   SER A 332      -8.885 -34.650  -0.679  1.00 60.99           C  
ANISOU 2461  C   SER A 332     8572   7206   7395   -234     78   -724       C  
ATOM   2462  O   SER A 332      -7.849 -35.149  -1.131  1.00 64.35           O  
ANISOU 2462  O   SER A 332     9021   7608   7822   -162    153   -779       O  
ATOM   2463  CB  SER A 332      -8.454 -34.152   1.729  1.00 56.35           C  
ANISOU 2463  CB  SER A 332     7858   6616   6935   -134     41   -569       C  
ATOM   2464  OG  SER A 332      -9.322 -35.229   2.036  1.00 57.46           O  
ANISOU 2464  OG  SER A 332     8076   6644   7111   -170     27   -581       O  
ATOM   2465  N   GLN A 333     -10.095 -35.045  -1.070  1.00 59.19           N  
ANISOU 2465  N   GLN A 333     8407   6944   7140   -331     31   -757       N  
ATOM   2466  CA  GLN A 333     -10.279 -36.046  -2.113  1.00 56.56           C  
ANISOU 2466  CA  GLN A 333     8181   6543   6766   -367     59   -867       C  
ATOM   2467  C   GLN A 333     -10.188 -35.462  -3.516  1.00 59.61           C  
ANISOU 2467  C   GLN A 333     8595   7022   7033   -404     66   -926       C  
ATOM   2468  O   GLN A 333     -10.361 -36.205  -4.489  1.00 63.51           O  
ANISOU 2468  O   GLN A 333     9184   7473   7472   -439     84  -1026       O  
ATOM   2469  CB  GLN A 333     -11.628 -36.748  -1.936  1.00 54.93           C  
ANISOU 2469  CB  GLN A 333     8025   6262   6585   -468      1   -886       C  
ATOM   2470  CG  GLN A 333     -11.759 -37.519  -0.635  1.00 57.04           C  
ANISOU 2470  CG  GLN A 333     8295   6414   6962   -438     11   -833       C  
ATOM   2471  CD  GLN A 333     -10.805 -38.694  -0.557  1.00 60.29           C  
ANISOU 2471  CD  GLN A 333     8783   6701   7423   -344     93   -881       C  
ATOM   2472  OE1 GLN A 333      -9.874 -38.701   0.249  1.00 60.70           O  
ANISOU 2472  OE1 GLN A 333     8796   6738   7529   -230    129   -826       O  
ATOM   2473  NE2 GLN A 333     -11.033 -39.697  -1.397  1.00 61.41           N  
ANISOU 2473  NE2 GLN A 333     9034   6752   7546   -387    120   -988       N  
ATOM   2474  N   THR A 334      -9.926 -34.165  -3.647  1.00 58.87           N  
ANISOU 2474  N   THR A 334     8429   7047   6892   -399     55   -867       N  
ATOM   2475  CA  THR A 334      -9.839 -33.501  -4.937  1.00 59.14           C  
ANISOU 2475  CA  THR A 334     8495   7172   6804   -431     65   -905       C  
ATOM   2476  C   THR A 334      -8.446 -32.914  -5.128  1.00 57.74           C  
ANISOU 2476  C   THR A 334     8272   7051   6616   -352    155   -890       C  
ATOM   2477  O   THR A 334      -7.722 -32.647  -4.164  1.00 57.01           O  
ANISOU 2477  O   THR A 334     8094   6959   6608   -287    178   -830       O  
ATOM   2478  CB  THR A 334     -10.894 -32.393  -5.071  1.00 60.46           C  
ANISOU 2478  CB  THR A 334     8629   7433   6912   -507    -28   -845       C  
ATOM   2479  OG1 THR A 334     -10.574 -31.314  -4.183  1.00 56.16           O  
ANISOU 2479  OG1 THR A 334     7985   6941   6414   -472    -35   -741       O  
ATOM   2480  CG2 THR A 334     -12.278 -32.929  -4.732  1.00 61.92           C  
ANISOU 2480  CG2 THR A 334     8826   7573   7127   -586   -117   -853       C  
ATOM   2481  N   ALA A 335      -8.079 -32.717  -6.394  1.00 57.46           N  
ANISOU 2481  N   ALA A 335     8294   7068   6473   -361    206   -947       N  
ATOM   2482  CA  ALA A 335      -6.775 -32.154  -6.720  1.00 52.99           C  
ANISOU 2482  CA  ALA A 335     7684   6560   5889   -299    305   -940       C  
ATOM   2483  C   ALA A 335      -6.671 -30.725  -6.203  1.00 55.11           C  
ANISOU 2483  C   ALA A 335     7856   6915   6170   -312    279   -833       C  
ATOM   2484  O   ALA A 335      -7.545 -29.892  -6.459  1.00 54.72           O  
ANISOU 2484  O   ALA A 335     7818   6918   6054   -378    209   -789       O  
ATOM   2485  CB  ALA A 335      -6.547 -32.190  -8.231  1.00 52.06           C  
ANISOU 2485  CB  ALA A 335     7662   6483   5636   -317    367  -1019       C  
ATOM   2486  N   GLY A 336      -5.595 -30.444  -5.471  1.00 53.77           N  
ANISOU 2486  N   GLY A 336     7588   6757   6084   -246    332   -796       N  
ATOM   2487  CA  GLY A 336      -5.452 -29.148  -4.842  1.00 47.89           C  
ANISOU 2487  CA  GLY A 336     6751   6079   5367   -261    306   -703       C  
ATOM   2488  C   GLY A 336      -6.419 -28.893  -3.710  1.00 47.40           C  
ANISOU 2488  C   GLY A 336     6653   5995   5362   -286    199   -632       C  
ATOM   2489  O   GLY A 336      -6.632 -27.736  -3.339  1.00 51.84           O  
ANISOU 2489  O   GLY A 336     7165   6608   5921   -314    161   -559       O  
ATOM   2490  N   GLY A 337      -7.012 -29.949  -3.145  1.00 44.01           N  
ANISOU 2490  N   GLY A 337     6252   5483   4985   -276    156   -653       N  
ATOM   2491  CA  GLY A 337      -7.990 -29.770  -2.086  1.00 45.66           C  
ANISOU 2491  CA  GLY A 337     6432   5671   5246   -302     65   -588       C  
ATOM   2492  C   GLY A 337      -7.399 -29.248  -0.794  1.00 51.02           C  
ANISOU 2492  C   GLY A 337     7013   6362   6012   -250     58   -518       C  
ATOM   2493  O   GLY A 337      -8.107 -28.634   0.010  1.00 51.24           O  
ANISOU 2493  O   GLY A 337     7006   6403   6061   -275     -9   -451       O  
ATOM   2494  N   THR A 338      -6.105 -29.490  -0.567  1.00 52.84           N  
ANISOU 2494  N   THR A 338     7194   6592   6292   -174    124   -536       N  
ATOM   2495  CA  THR A 338      -5.442 -28.906   0.594  1.00 55.03           C  
ANISOU 2495  CA  THR A 338     7370   6897   6642   -126    110   -477       C  
ATOM   2496  C   THR A 338      -5.418 -27.387   0.493  1.00 52.57           C  
ANISOU 2496  C   THR A 338     7009   6669   6295   -178     97   -427       C  
ATOM   2497  O   THR A 338      -5.581 -26.685   1.499  1.00 58.63           O  
ANISOU 2497  O   THR A 338     7722   7453   7100   -179     45   -366       O  
ATOM   2498  CB  THR A 338      -4.023 -29.461   0.730  1.00 59.83           C  
ANISOU 2498  CB  THR A 338     7923   7502   7307    -33    181   -515       C  
ATOM   2499  OG1 THR A 338      -4.067 -30.894   0.733  1.00 65.67           O  
ANISOU 2499  OG1 THR A 338     8728   8149   8075     22    199   -563       O  
ATOM   2500  CG2 THR A 338      -3.382 -28.980   2.026  1.00 59.45           C  
ANISOU 2500  CG2 THR A 338     7770   7484   7336     20    148   -461       C  
ATOM   2501  N   PHE A 339      -5.227 -26.861  -0.719  1.00 46.15           N  
ANISOU 2501  N   PHE A 339     6226   5904   5404   -221    148   -451       N  
ATOM   2502  CA  PHE A 339      -5.318 -25.420  -0.920  1.00 44.86           C  
ANISOU 2502  CA  PHE A 339     6041   5805   5199   -276    139   -398       C  
ATOM   2503  C   PHE A 339      -6.759 -24.942  -0.794  1.00 46.74           C  
ANISOU 2503  C   PHE A 339     6325   6038   5396   -329     50   -350       C  
ATOM   2504  O   PHE A 339      -7.011 -23.841  -0.290  1.00 46.97           O  
ANISOU 2504  O   PHE A 339     6320   6095   5431   -352     14   -288       O  
ATOM   2505  CB  PHE A 339      -4.742 -25.044  -2.285  1.00 44.52           C  
ANISOU 2505  CB  PHE A 339     6032   5808   5074   -303    226   -431       C  
ATOM   2506  CG  PHE A 339      -4.508 -23.570  -2.460  1.00 47.36           C  
ANISOU 2506  CG  PHE A 339     6366   6224   5406   -352    244   -376       C  
ATOM   2507  CD1 PHE A 339      -3.530 -22.918  -1.728  1.00 48.59           C  
ANISOU 2507  CD1 PHE A 339     6418   6405   5637   -340    272   -353       C  
ATOM   2508  CD2 PHE A 339      -5.264 -22.838  -3.361  1.00 46.66           C  
ANISOU 2508  CD2 PHE A 339     6359   6159   5212   -408    231   -347       C  
ATOM   2509  CE1 PHE A 339      -3.311 -21.564  -1.888  1.00 47.94           C  
ANISOU 2509  CE1 PHE A 339     6321   6361   5534   -395    294   -305       C  
ATOM   2510  CE2 PHE A 339      -5.050 -21.482  -3.526  1.00 44.58           C  
ANISOU 2510  CE2 PHE A 339     6086   5931   4922   -450    253   -290       C  
ATOM   2511  CZ  PHE A 339      -4.072 -20.845  -2.789  1.00 46.88           C  
ANISOU 2511  CZ  PHE A 339     6280   6237   5297   -448    289   -270       C  
ATOM   2512  N   LEU A 340      -7.716 -25.755  -1.250  1.00 48.64           N  
ANISOU 2512  N   LEU A 340     6638   6244   5598   -350     15   -382       N  
ATOM   2513  CA  LEU A 340      -9.124 -25.420  -1.067  1.00 48.76           C  
ANISOU 2513  CA  LEU A 340     6679   6261   5588   -396    -74   -341       C  
ATOM   2514  C   LEU A 340      -9.483 -25.366   0.411  1.00 45.82           C  
ANISOU 2514  C   LEU A 340     6247   5861   5302   -374   -126   -287       C  
ATOM   2515  O   LEU A 340     -10.277 -24.518   0.836  1.00 45.00           O  
ANISOU 2515  O   LEU A 340     6126   5780   5191   -398   -182   -229       O  
ATOM   2516  CB  LEU A 340     -10.007 -26.433  -1.793  1.00 53.56           C  
ANISOU 2516  CB  LEU A 340     7362   6837   6150   -429   -102   -399       C  
ATOM   2517  CG  LEU A 340      -9.930 -26.434  -3.319  1.00 56.60           C  
ANISOU 2517  CG  LEU A 340     7825   7257   6422   -458    -69   -453       C  
ATOM   2518  CD1 LEU A 340     -10.883 -27.470  -3.891  1.00 62.30           C  
ANISOU 2518  CD1 LEU A 340     8617   7945   7107   -498   -113   -518       C  
ATOM   2519  CD2 LEU A 340     -10.237 -25.050  -3.869  1.00 53.47           C  
ANISOU 2519  CD2 LEU A 340     7437   6933   5944   -489    -90   -395       C  
ATOM   2520  N   GLY A 341      -8.914 -26.272   1.208  1.00 43.63           N  
ANISOU 2520  N   GLY A 341     5944   5532   5100   -321   -107   -305       N  
ATOM   2521  CA  GLY A 341      -9.073 -26.172   2.648  1.00 39.61           C  
ANISOU 2521  CA  GLY A 341     5385   5003   4663   -290   -147   -251       C  
ATOM   2522  C   GLY A 341      -8.519 -24.871   3.194  1.00 41.82           C  
ANISOU 2522  C   GLY A 341     5600   5336   4954   -281   -152   -202       C  
ATOM   2523  O   GLY A 341      -9.173 -24.193   3.989  1.00 41.83           O  
ANISOU 2523  O   GLY A 341     5582   5347   4967   -292   -203   -148       O  
ATOM   2524  N   PHE A 342      -7.313 -24.495   2.758  1.00 42.42           N  
ANISOU 2524  N   PHE A 342     5642   5448   5029   -266    -93   -225       N  
ATOM   2525  CA  PHE A 342      -6.723 -23.234   3.194  1.00 42.77           C  
ANISOU 2525  CA  PHE A 342     5625   5538   5088   -274    -92   -189       C  
ATOM   2526  C   PHE A 342      -7.627 -22.059   2.847  1.00 42.47           C  
ANISOU 2526  C   PHE A 342     5620   5524   4992   -333   -124   -142       C  
ATOM   2527  O   PHE A 342      -7.891 -21.193   3.689  1.00 42.61           O  
ANISOU 2527  O   PHE A 342     5611   5549   5031   -337   -164    -95       O  
ATOM   2528  CB  PHE A 342      -5.340 -23.053   2.566  1.00 44.00           C  
ANISOU 2528  CB  PHE A 342     5737   5731   5250   -266    -11   -228       C  
ATOM   2529  CG  PHE A 342      -4.900 -21.619   2.477  1.00 41.05           C  
ANISOU 2529  CG  PHE A 342     5328   5404   4866   -312      8   -197       C  
ATOM   2530  CD1 PHE A 342      -4.579 -20.905   3.620  1.00 39.60           C  
ANISOU 2530  CD1 PHE A 342     5078   5231   4738   -305    -29   -167       C  
ATOM   2531  CD2 PHE A 342      -4.811 -20.983   1.250  1.00 43.84           C  
ANISOU 2531  CD2 PHE A 342     5724   5783   5149   -364     64   -199       C  
ATOM   2532  CE1 PHE A 342      -4.176 -19.586   3.540  1.00 40.12           C  
ANISOU 2532  CE1 PHE A 342     5118   5326   4800   -356     -9   -145       C  
ATOM   2533  CE2 PHE A 342      -4.409 -19.664   1.163  1.00 42.43           C  
ANISOU 2533  CE2 PHE A 342     5524   5633   4964   -412     91   -166       C  
ATOM   2534  CZ  PHE A 342      -4.091 -18.965   2.309  1.00 42.92           C  
ANISOU 2534  CZ  PHE A 342     5518   5697   5092   -412     55   -141       C  
ATOM   2535  N   LEU A 343      -8.120 -22.019   1.606  1.00 40.98           N  
ANISOU 2535  N   LEU A 343     5497   5348   4726   -372   -110   -155       N  
ATOM   2536  CA  LEU A 343      -9.027 -20.948   1.204  1.00 37.98           C  
ANISOU 2536  CA  LEU A 343     5155   4990   4284   -414   -146   -107       C  
ATOM   2537  C   LEU A 343     -10.316 -20.969   2.014  1.00 41.03           C  
ANISOU 2537  C   LEU A 343     5541   5360   4689   -411   -228    -68       C  
ATOM   2538  O   LEU A 343     -10.921 -19.916   2.240  1.00 44.52           O  
ANISOU 2538  O   LEU A 343     5985   5816   5114   -423   -263    -16       O  
ATOM   2539  CB  LEU A 343      -9.340 -21.054  -0.289  1.00 41.74           C  
ANISOU 2539  CB  LEU A 343     5708   5489   4663   -447   -125   -132       C  
ATOM   2540  CG  LEU A 343      -8.190 -20.792  -1.262  1.00 40.36           C  
ANISOU 2540  CG  LEU A 343     5548   5340   4447   -458    -32   -159       C  
ATOM   2541  CD1 LEU A 343      -8.691 -20.830  -2.697  1.00 38.69           C  
ANISOU 2541  CD1 LEU A 343     5429   5153   4117   -487    -23   -176       C  
ATOM   2542  CD2 LEU A 343      -7.518 -19.462  -0.959  1.00 34.10           C  
ANISOU 2542  CD2 LEU A 343     4719   4565   3674   -475      2   -111       C  
ATOM   2543  N   TRP A 344     -10.750 -22.150   2.460  1.00 43.25           N  
ANISOU 2543  N   TRP A 344     5821   5605   5007   -395   -251    -93       N  
ATOM   2544  CA  TRP A 344     -11.992 -22.243   3.222  1.00 43.37           C  
ANISOU 2544  CA  TRP A 344     5829   5606   5043   -399   -315    -57       C  
ATOM   2545  C   TRP A 344     -11.842 -21.613   4.602  1.00 41.41           C  
ANISOU 2545  C   TRP A 344     5532   5353   4851   -366   -332     -9       C  
ATOM   2546  O   TRP A 344     -12.654 -20.769   5.000  1.00 45.92           O  
ANISOU 2546  O   TRP A 344     6096   5938   5412   -372   -371     38       O  
ATOM   2547  CB  TRP A 344     -12.428 -23.704   3.338  1.00 43.27           C  
ANISOU 2547  CB  TRP A 344     5834   5546   5059   -400   -322    -96       C  
ATOM   2548  CG  TRP A 344     -13.466 -23.938   4.393  1.00 44.46           C  
ANISOU 2548  CG  TRP A 344     5964   5674   5254   -400   -367    -58       C  
ATOM   2549  CD1 TRP A 344     -13.323 -24.673   5.534  1.00 44.51           C  
ANISOU 2549  CD1 TRP A 344     5955   5631   5325   -366   -360    -47       C  
ATOM   2550  CD2 TRP A 344     -14.808 -23.434   4.406  1.00 48.19           C  
ANISOU 2550  CD2 TRP A 344     6428   6176   5708   -432   -421    -24       C  
ATOM   2551  NE1 TRP A 344     -14.493 -24.659   6.256  1.00 45.22           N  
ANISOU 2551  NE1 TRP A 344     6031   5715   5435   -382   -396     -7       N  
ATOM   2552  CE2 TRP A 344     -15.419 -23.904   5.586  1.00 47.71           C  
ANISOU 2552  CE2 TRP A 344     6342   6081   5705   -422   -434      5       C  
ATOM   2553  CE3 TRP A 344     -15.551 -22.631   3.535  1.00 44.35           C  
ANISOU 2553  CE3 TRP A 344     5951   5741   5158   -461   -458    -11       C  
ATOM   2554  CZ2 TRP A 344     -16.739 -23.600   5.915  1.00 46.14           C  
ANISOU 2554  CZ2 TRP A 344     6116   5904   5511   -445   -476     40       C  
ATOM   2555  CZ3 TRP A 344     -16.860 -22.329   3.864  1.00 42.41           C  
ANISOU 2555  CZ3 TRP A 344     5676   5519   4918   -476   -511     25       C  
ATOM   2556  CH2 TRP A 344     -17.440 -22.813   5.044  1.00 42.68           C  
ANISOU 2556  CH2 TRP A 344     5675   5524   5019   -470   -516     47       C  
ATOM   2557  N   PHE A 345     -10.809 -22.011   5.349  1.00 37.47           N  
ANISOU 2557  N   PHE A 345     4998   4834   4404   -326   -306    -24       N  
ATOM   2558  CA  PHE A 345     -10.616 -21.454   6.684  1.00 39.45           C  
ANISOU 2558  CA  PHE A 345     5207   5084   4696   -293   -328     14       C  
ATOM   2559  C   PHE A 345     -10.112 -20.018   6.630  1.00 44.82           C  
ANISOU 2559  C   PHE A 345     5869   5798   5361   -310   -321     33       C  
ATOM   2560  O   PHE A 345     -10.418 -19.224   7.526  1.00 50.63           O  
ANISOU 2560  O   PHE A 345     6592   6536   6110   -301   -352     69       O  
ATOM   2561  CB  PHE A 345      -9.658 -22.331   7.491  1.00 32.10           C  
ANISOU 2561  CB  PHE A 345     4246   4130   3820   -237   -314     -7       C  
ATOM   2562  CG  PHE A 345     -10.112 -23.755   7.622  1.00 31.03           C  
ANISOU 2562  CG  PHE A 345     4143   3943   3705   -218   -313    -21       C  
ATOM   2563  CD1 PHE A 345      -9.535 -24.754   6.859  1.00 31.63           C  
ANISOU 2563  CD1 PHE A 345     4239   3994   3784   -207   -272    -73       C  
ATOM   2564  CD2 PHE A 345     -11.125 -24.092   8.501  1.00 30.78           C  
ANISOU 2564  CD2 PHE A 345     4127   3881   3688   -214   -345     17       C  
ATOM   2565  CE1 PHE A 345      -9.957 -26.063   6.974  1.00 31.97           C  
ANISOU 2565  CE1 PHE A 345     4325   3974   3850   -194   -267    -88       C  
ATOM   2566  CE2 PHE A 345     -11.550 -25.396   8.623  1.00 31.14           C  
ANISOU 2566  CE2 PHE A 345     4208   3867   3756   -209   -336      7       C  
ATOM   2567  CZ  PHE A 345     -10.965 -26.383   7.860  1.00 31.73           C  
ANISOU 2567  CZ  PHE A 345     4311   3908   3838   -200   -299    -47       C  
ATOM   2568  N   PHE A 346      -9.337 -19.667   5.600  1.00 40.28           N  
ANISOU 2568  N   PHE A 346     5298   5245   4760   -336   -275      8       N  
ATOM   2569  CA  PHE A 346      -8.997 -18.264   5.384  1.00 40.47           C  
ANISOU 2569  CA  PHE A 346     5322   5290   4766   -368   -259     32       C  
ATOM   2570  C   PHE A 346     -10.245 -17.442   5.094  1.00 43.68           C  
ANISOU 2570  C   PHE A 346     5778   5696   5123   -388   -296     80       C  
ATOM   2571  O   PHE A 346     -10.332 -16.276   5.497  1.00 45.79           O  
ANISOU 2571  O   PHE A 346     6049   5959   5391   -395   -306    114       O  
ATOM   2572  CB  PHE A 346      -7.986 -18.141   4.243  1.00 46.69           C  
ANISOU 2572  CB  PHE A 346     6112   6099   5530   -397   -188      0       C  
ATOM   2573  CG  PHE A 346      -7.647 -16.725   3.873  1.00 53.90           C  
ANISOU 2573  CG  PHE A 346     7037   7021   6420   -442   -158     27       C  
ATOM   2574  CD1 PHE A 346      -7.294 -15.804   4.845  1.00 59.46           C  
ANISOU 2574  CD1 PHE A 346     7705   7718   7169   -448   -174     44       C  
ATOM   2575  CD2 PHE A 346      -7.669 -16.318   2.549  1.00 56.03           C  
ANISOU 2575  CD2 PHE A 346     7366   7304   6620   -480   -112     35       C  
ATOM   2576  CE1 PHE A 346      -6.980 -14.502   4.505  1.00 62.70           C  
ANISOU 2576  CE1 PHE A 346     8137   8123   7564   -497   -141     68       C  
ATOM   2577  CE2 PHE A 346      -7.354 -15.016   2.202  1.00 59.41           C  
ANISOU 2577  CE2 PHE A 346     7818   7728   7026   -523    -75     68       C  
ATOM   2578  CZ  PHE A 346      -7.009 -14.107   3.182  1.00 61.81           C  
ANISOU 2578  CZ  PHE A 346     8085   8014   7385   -534    -88     84       C  
ATOM   2579  N   LEU A 347     -11.221 -18.034   4.400  1.00 45.23           N  
ANISOU 2579  N   LEU A 347     6012   5895   5278   -394   -318     79       N  
ATOM   2580  CA  LEU A 347     -12.517 -17.386   4.234  1.00 45.84           C  
ANISOU 2580  CA  LEU A 347     6120   5982   5316   -399   -366    124       C  
ATOM   2581  C   LEU A 347     -13.211 -17.215   5.579  1.00 47.59           C  
ANISOU 2581  C   LEU A 347     6310   6188   5583   -369   -408    156       C  
ATOM   2582  O   LEU A 347     -13.803 -16.164   5.852  1.00 51.90           O  
ANISOU 2582  O   LEU A 347     6866   6735   6117   -359   -431    199       O  
ATOM   2583  CB  LEU A 347     -13.382 -18.206   3.272  1.00 46.86           C  
ANISOU 2583  CB  LEU A 347     6280   6126   5397   -416   -391    104       C  
ATOM   2584  CG  LEU A 347     -14.774 -17.744   2.828  1.00 43.09           C  
ANISOU 2584  CG  LEU A 347     5825   5676   4871   -420   -450    140       C  
ATOM   2585  CD1 LEU A 347     -15.867 -18.174   3.807  1.00 42.37           C  
ANISOU 2585  CD1 LEU A 347     5690   5580   4829   -405   -498    156       C  
ATOM   2586  CD2 LEU A 347     -14.805 -16.244   2.595  1.00 50.13           C  
ANISOU 2586  CD2 LEU A 347     6747   6576   5724   -410   -449    195       C  
ATOM   2587  N   LEU A 348     -13.141 -18.237   6.436  1.00 45.03           N  
ANISOU 2587  N   LEU A 348     5954   5846   5308   -348   -413    137       N  
ATOM   2588  CA  LEU A 348     -13.795 -18.161   7.739  1.00 46.83           C  
ANISOU 2588  CA  LEU A 348     6160   6061   5572   -317   -443    169       C  
ATOM   2589  C   LEU A 348     -13.098 -17.164   8.654  1.00 44.76           C  
ANISOU 2589  C   LEU A 348     5883   5794   5329   -297   -439    183       C  
ATOM   2590  O   LEU A 348     -13.758 -16.447   9.417  1.00 44.37           O  
ANISOU 2590  O   LEU A 348     5836   5742   5282   -277   -462    216       O  
ATOM   2591  CB  LEU A 348     -13.827 -19.541   8.394  1.00 47.79           C  
ANISOU 2591  CB  LEU A 348     6267   6158   5734   -300   -442    150       C  
ATOM   2592  CG  LEU A 348     -14.533 -20.665   7.640  1.00 47.85           C  
ANISOU 2592  CG  LEU A 348     6290   6156   5733   -330   -445    127       C  
ATOM   2593  CD1 LEU A 348     -14.373 -21.981   8.385  1.00 50.65           C  
ANISOU 2593  CD1 LEU A 348     6644   6466   6135   -310   -431    113       C  
ATOM   2594  CD2 LEU A 348     -15.995 -20.328   7.453  1.00 45.15           C  
ANISOU 2594  CD2 LEU A 348     5944   5838   5372   -350   -484    156       C  
ATOM   2595  N   PHE A 349     -11.765 -17.110   8.600  1.00 43.64           N  
ANISOU 2595  N   PHE A 349     5724   5653   5204   -302   -410    151       N  
ATOM   2596  CA  PHE A 349     -11.021 -16.225   9.490  1.00 42.86           C  
ANISOU 2596  CA  PHE A 349     5605   5552   5129   -293   -412    152       C  
ATOM   2597  C   PHE A 349     -11.376 -14.765   9.237  1.00 43.94           C  
ANISOU 2597  C   PHE A 349     5774   5681   5238   -315   -413    181       C  
ATOM   2598  O   PHE A 349     -11.637 -14.007  10.178  1.00 48.31           O  
ANISOU 2598  O   PHE A 349     6334   6221   5801   -297   -434    199       O  
ATOM   2599  CB  PHE A 349      -9.519 -16.451   9.324  1.00 43.03           C  
ANISOU 2599  CB  PHE A 349     5585   5586   5178   -302   -380    107       C  
ATOM   2600  CG  PHE A 349      -8.676 -15.543  10.174  1.00 45.85           C  
ANISOU 2600  CG  PHE A 349     5910   5949   5563   -306   -389     95       C  
ATOM   2601  CD1 PHE A 349      -8.654 -15.687  11.551  1.00 46.87           C  
ANISOU 2601  CD1 PHE A 349     6020   6077   5713   -262   -431     96       C  
ATOM   2602  CD2 PHE A 349      -7.910 -14.545   9.597  1.00 47.91           C  
ANISOU 2602  CD2 PHE A 349     6165   6214   5826   -358   -354     83       C  
ATOM   2603  CE1 PHE A 349      -7.882 -14.853  12.337  1.00 50.51           C  
ANISOU 2603  CE1 PHE A 349     6452   6546   6193   -269   -449     75       C  
ATOM   2604  CE2 PHE A 349      -7.135 -13.708  10.378  1.00 49.64           C  
ANISOU 2604  CE2 PHE A 349     6350   6434   6075   -375   -365     63       C  
ATOM   2605  CZ  PHE A 349      -7.121 -13.862  11.749  1.00 49.81           C  
ANISOU 2605  CZ  PHE A 349     6350   6460   6115   -330   -418     54       C  
ATOM   2606  N   PHE A 350     -11.391 -14.352   7.968  1.00 45.95           N  
ANISOU 2606  N   PHE A 350     6063   5941   5455   -351   -386    189       N  
ATOM   2607  CA  PHE A 350     -11.783 -12.983   7.650  1.00 46.83           C  
ANISOU 2607  CA  PHE A 350     6221   6035   5536   -365   -384    227       C  
ATOM   2608  C   PHE A 350     -13.247 -12.731   7.984  1.00 46.36           C  
ANISOU 2608  C   PHE A 350     6183   5972   5459   -326   -428    269       C  
ATOM   2609  O   PHE A 350     -13.615 -11.607   8.344  1.00 43.08           O  
ANISOU 2609  O   PHE A 350     5798   5532   5038   -311   -435    299       O  
ATOM   2610  CB  PHE A 350     -11.513 -12.685   6.176  1.00 50.08           C  
ANISOU 2610  CB  PHE A 350     6676   6454   5899   -404   -344    233       C  
ATOM   2611  CG  PHE A 350     -10.211 -11.978   5.931  1.00 57.02           C  
ANISOU 2611  CG  PHE A 350     7552   7319   6792   -451   -287    215       C  
ATOM   2612  CD1 PHE A 350      -9.066 -12.352   6.615  1.00 56.88           C  
ANISOU 2612  CD1 PHE A 350     7466   7311   6833   -461   -271    168       C  
ATOM   2613  CD2 PHE A 350     -10.131 -10.939   5.019  1.00 64.18           C  
ANISOU 2613  CD2 PHE A 350     8523   8206   7656   -486   -248    248       C  
ATOM   2614  CE1 PHE A 350      -7.866 -11.704   6.394  1.00 59.63           C  
ANISOU 2614  CE1 PHE A 350     7795   7657   7205   -514   -218    146       C  
ATOM   2615  CE2 PHE A 350      -8.933 -10.286   4.793  1.00 64.05           C  
ANISOU 2615  CE2 PHE A 350     8502   8176   7661   -543   -185    233       C  
ATOM   2616  CZ  PHE A 350      -7.799 -10.670   5.482  1.00 64.01           C  
ANISOU 2616  CZ  PHE A 350     8413   8187   7722   -562   -169    178       C  
ATOM   2617  N   ALA A 351     -14.091 -13.760   7.873  1.00 47.49           N  
ANISOU 2617  N   ALA A 351     6308   6137   5597   -310   -453    270       N  
ATOM   2618  CA  ALA A 351     -15.495 -13.609   8.239  1.00 45.49           C  
ANISOU 2618  CA  ALA A 351     6054   5893   5338   -275   -492    306       C  
ATOM   2619  C   ALA A 351     -15.653 -13.391   9.738  1.00 42.88           C  
ANISOU 2619  C   ALA A 351     5703   5545   5044   -238   -500    313       C  
ATOM   2620  O   ALA A 351     -16.432 -12.534  10.168  1.00 45.14           O  
ANISOU 2620  O   ALA A 351     6004   5823   5324   -205   -513    346       O  
ATOM   2621  CB  ALA A 351     -16.291 -14.835   7.791  1.00 46.00           C  
ANISOU 2621  CB  ALA A 351     6095   5985   5397   -283   -513    296       C  
ATOM   2622  N   GLY A 352     -14.920 -14.156  10.550  1.00 36.61           N  
ANISOU 2622  N   GLY A 352     4881   4745   4282   -235   -491    284       N  
ATOM   2623  CA  GLY A 352     -15.022 -14.003  11.989  1.00 38.35           C  
ANISOU 2623  CA  GLY A 352     5093   4954   4524   -197   -501    289       C  
ATOM   2624  C   GLY A 352     -14.256 -12.818  12.534  1.00 44.04           C  
ANISOU 2624  C   GLY A 352     5835   5653   5246   -197   -497    278       C  
ATOM   2625  O   GLY A 352     -14.667 -12.224  13.536  1.00 52.21           O  
ANISOU 2625  O   GLY A 352     6884   6674   6279   -162   -507    289       O  
ATOM   2626  N   LEU A 353     -13.142 -12.455  11.893  1.00 42.64           N  
ANISOU 2626  N   LEU A 353     5659   5469   5072   -239   -479    252       N  
ATOM   2627  CA  LEU A 353     -12.333 -11.346  12.389  1.00 44.90           C  
ANISOU 2627  CA  LEU A 353     5960   5732   5370   -256   -474    232       C  
ATOM   2628  C   LEU A 353     -13.076 -10.021  12.273  1.00 46.35           C  
ANISOU 2628  C   LEU A 353     6202   5879   5531   -248   -470    266       C  
ATOM   2629  O   LEU A 353     -12.996  -9.178  13.175  1.00 51.54           O  
ANISOU 2629  O   LEU A 353     6883   6506   6194   -236   -478    256       O  
ATOM   2630  CB  LEU A 353     -11.005 -11.289  11.634  1.00 46.29           C  
ANISOU 2630  CB  LEU A 353     6115   5913   5561   -313   -444    198       C  
ATOM   2631  CG  LEU A 353     -10.041 -10.149  11.963  1.00 48.81           C  
ANISOU 2631  CG  LEU A 353     6438   6206   5900   -355   -432    169       C  
ATOM   2632  CD1 LEU A 353      -9.548 -10.251  13.397  1.00 46.38           C  
ANISOU 2632  CD1 LEU A 353     6097   5909   5616   -331   -471    132       C  
ATOM   2633  CD2 LEU A 353      -8.872 -10.165  10.995  1.00 55.71           C  
ANISOU 2633  CD2 LEU A 353     7283   7094   6792   -418   -387    143       C  
ATOM   2634  N   THR A 354     -13.806  -9.818  11.175  1.00 42.55           N  
ANISOU 2634  N   THR A 354     5749   5397   5021   -249   -462    304       N  
ATOM   2635  CA  THR A 354     -14.586  -8.597  11.009  1.00 39.98           C  
ANISOU 2635  CA  THR A 354     5483   5035   4674   -225   -462    344       C  
ATOM   2636  C   THR A 354     -15.819  -8.563  11.900  1.00 41.54           C  
ANISOU 2636  C   THR A 354     5675   5238   4870   -156   -486    367       C  
ATOM   2637  O   THR A 354     -16.465  -7.513  11.994  1.00 40.09           O  
ANISOU 2637  O   THR A 354     5538   5020   4674   -119   -485    396       O  
ATOM   2638  CB  THR A 354     -15.002  -8.429   9.546  1.00 35.87           C  
ANISOU 2638  CB  THR A 354     4995   4521   4112   -235   -454    382       C  
ATOM   2639  OG1 THR A 354     -15.283  -9.712   8.974  1.00 31.00           O  
ANISOU 2639  OG1 THR A 354     4333   3958   3486   -241   -468    375       O  
ATOM   2640  CG2 THR A 354     -13.891  -7.759   8.754  1.00 36.67           C  
ANISOU 2640  CG2 THR A 354     5137   4590   4205   -297   -410    374       C  
ATOM   2641  N   SER A 355     -16.160  -9.676  12.548  1.00 40.99           N  
ANISOU 2641  N   SER A 355     5554   5206   4814   -136   -501    357       N  
ATOM   2642  CA  SER A 355     -17.262  -9.721  13.500  1.00 43.82           C  
ANISOU 2642  CA  SER A 355     5901   5575   5175    -77   -510    378       C  
ATOM   2643  C   SER A 355     -16.801  -9.665  14.949  1.00 47.13           C  
ANISOU 2643  C   SER A 355     6325   5979   5603    -57   -508    349       C  
ATOM   2644  O   SER A 355     -17.524  -9.131  15.796  1.00 46.63           O  
ANISOU 2644  O   SER A 355     6282   5906   5532     -5   -503    361       O  
ATOM   2645  CB  SER A 355     -18.096 -10.989  13.286  1.00 45.71           C  
ANISOU 2645  CB  SER A 355     6085   5862   5421    -72   -520    392       C  
ATOM   2646  OG  SER A 355     -18.738 -10.971  12.023  1.00 50.44           O  
ANISOU 2646  OG  SER A 355     6679   6483   6003    -81   -534    416       O  
ATOM   2647  N   SER A 356     -15.616 -10.199  15.253  1.00 48.39           N  
ANISOU 2647  N   SER A 356     6468   6144   5775    -90   -513    309       N  
ATOM   2648  CA  SER A 356     -15.117 -10.154  16.624  1.00 47.18           C  
ANISOU 2648  CA  SER A 356     6321   5985   5619    -68   -524    279       C  
ATOM   2649  C   SER A 356     -14.743  -8.734  17.029  1.00 52.60           C  
ANISOU 2649  C   SER A 356     7060   6626   6298    -73   -524    255       C  
ATOM   2650  O   SER A 356     -14.955  -8.334  18.180  1.00 59.93           O  
ANISOU 2650  O   SER A 356     8019   7544   7209    -33   -530    241       O  
ATOM   2651  CB  SER A 356     -13.922 -11.091  16.781  1.00 40.50           C  
ANISOU 2651  CB  SER A 356     5437   5163   4789    -93   -538    244       C  
ATOM   2652  OG  SER A 356     -12.941 -10.831  15.793  1.00 42.00           O  
ANISOU 2652  OG  SER A 356     5613   5348   4997   -151   -531    220       O  
ATOM   2653  N   ILE A 357     -14.183  -7.956  16.098  1.00 47.32           N  
ANISOU 2653  N   ILE A 357     6412   5927   5640   -123   -512    248       N  
ATOM   2654  CA  ILE A 357     -13.903  -6.554  16.379  1.00 48.31           C  
ANISOU 2654  CA  ILE A 357     6599   5993   5764   -137   -505    227       C  
ATOM   2655  C   ILE A 357     -15.188  -5.764  16.580  1.00 54.77           C  
ANISOU 2655  C   ILE A 357     7472   6777   6562    -72   -492    265       C  
ATOM   2656  O   ILE A 357     -15.164  -4.691  17.195  1.00 59.68           O  
ANISOU 2656  O   ILE A 357     8155   7343   7178    -59   -486    243       O  
ATOM   2657  CB  ILE A 357     -13.059  -5.931  15.251  1.00 48.61           C  
ANISOU 2657  CB  ILE A 357     6653   5998   5819   -212   -481    221       C  
ATOM   2658  CG1 ILE A 357     -13.809  -6.008  13.918  1.00 46.26           C  
ANISOU 2658  CG1 ILE A 357     6367   5703   5505   -204   -462    280       C  
ATOM   2659  CG2 ILE A 357     -11.709  -6.623  15.149  1.00 30.72           C  
ANISOU 2659  CG2 ILE A 357     4322   3769   3580   -272   -488    175       C  
ATOM   2660  CD1 ILE A 357     -13.082  -5.346  12.767  1.00 45.33           C  
ANISOU 2660  CD1 ILE A 357     6284   5550   5391   -272   -427    286       C  
ATOM   2661  N   ALA A 358     -16.316  -6.273  16.081  1.00 52.75           N  
ANISOU 2661  N   ALA A 358     7192   6553   6298    -28   -489    316       N  
ATOM   2662  CA  ALA A 358     -17.588  -5.580  16.238  1.00 48.76           C  
ANISOU 2662  CA  ALA A 358     6719   6029   5779     45   -477    354       C  
ATOM   2663  C   ALA A 358     -18.240  -5.865  17.584  1.00 47.04           C  
ANISOU 2663  C   ALA A 358     6491   5833   5550    107   -473    346       C  
ATOM   2664  O   ALA A 358     -18.946  -5.002  18.116  1.00 48.07           O  
ANISOU 2664  O   ALA A 358     6665   5931   5669    168   -456    353       O  
ATOM   2665  CB  ALA A 358     -18.540  -5.969  15.106  1.00 47.84           C  
ANISOU 2665  CB  ALA A 358     6569   5950   5660     64   -482    409       C  
ATOM   2666  N   ILE A 359     -18.028  -7.060  18.147  1.00 44.81           N  
ANISOU 2666  N   ILE A 359     6157   5600   5268     97   -483    334       N  
ATOM   2667  CA  ILE A 359     -18.624  -7.406  19.434  1.00 45.58           C  
ANISOU 2667  CA  ILE A 359     6253   5720   5346    154   -470    334       C  
ATOM   2668  C   ILE A 359     -17.725  -7.053  20.608  1.00 42.68           C  
ANISOU 2668  C   ILE A 359     5932   5331   4954    153   -483    279       C  
ATOM   2669  O   ILE A 359     -18.135  -7.224  21.764  1.00 49.24           O  
ANISOU 2669  O   ILE A 359     6779   6176   5753    204   -470    275       O  
ATOM   2670  CB  ILE A 359     -18.990  -8.902  19.505  1.00 43.55           C  
ANISOU 2670  CB  ILE A 359     5930   5521   5098    150   -467    358       C  
ATOM   2671  CG1 ILE A 359     -17.829  -9.765  19.013  1.00 45.21           C  
ANISOU 2671  CG1 ILE A 359     6112   5743   5323     87   -492    336       C  
ATOM   2672  CG2 ILE A 359     -20.247  -9.178  18.700  1.00 40.91           C  
ANISOU 2672  CG2 ILE A 359     5546   5216   4782    166   -454    407       C  
ATOM   2673  CD1 ILE A 359     -18.126 -11.248  19.038  1.00 47.79           C  
ANISOU 2673  CD1 ILE A 359     6389   6107   5660     82   -487    358       C  
ATOM   2674  N   MET A 360     -16.510  -6.571  20.355  1.00 38.11           N  
ANISOU 2674  N   MET A 360     5373   4723   4385     94   -507    235       N  
ATOM   2675  CA  MET A 360     -15.653  -6.083  21.424  1.00 37.17           C  
ANISOU 2675  CA  MET A 360     5296   4584   4243     86   -530    173       C  
ATOM   2676  C   MET A 360     -15.693  -4.568  21.575  1.00 42.44           C  
ANISOU 2676  C   MET A 360     6044   5177   4905     88   -518    143       C  
ATOM   2677  O   MET A 360     -15.382  -4.063  22.659  1.00 41.33           O  
ANISOU 2677  O   MET A 360     5954   5018   4733    102   -532     90       O  
ATOM   2678  CB  MET A 360     -14.207  -6.540  21.197  1.00 34.02           C  
ANISOU 2678  CB  MET A 360     4854   4207   3865     15   -567    131       C  
ATOM   2679  CG  MET A 360     -13.917  -7.926  21.754  1.00 46.33           C  
ANISOU 2679  CG  MET A 360     6363   5829   5411     36   -591    135       C  
ATOM   2680  SD  MET A 360     -12.173  -8.366  21.655  1.00 62.38           S  
ANISOU 2680  SD  MET A 360     8339   7892   7469    -26   -640     79       S  
ATOM   2681  CE  MET A 360     -12.015  -8.727  19.910  1.00 61.14           C  
ANISOU 2681  CE  MET A 360     8131   7735   7366    -84   -609    110       C  
ATOM   2682  N   GLN A 361     -16.075  -3.844  20.521  1.00 47.68           N  
ANISOU 2682  N   GLN A 361     6729   5794   5593     78   -493    175       N  
ATOM   2683  CA  GLN A 361     -16.200  -2.391  20.612  1.00 50.66           C  
ANISOU 2683  CA  GLN A 361     7197   6083   5968     89   -474    155       C  
ATOM   2684  C   GLN A 361     -17.267  -1.926  21.601  1.00 49.34           C  
ANISOU 2684  C   GLN A 361     7081   5899   5766    186   -449    157       C  
ATOM   2685  O   GLN A 361     -17.054  -0.879  22.238  1.00 52.43           O  
ANISOU 2685  O   GLN A 361     7558   6221   6143    192   -443    106       O  
ATOM   2686  CB  GLN A 361     -16.465  -1.805  19.218  1.00 51.56           C  
ANISOU 2686  CB  GLN A 361     7330   6152   6108     72   -451    206       C  
ATOM   2687  CG  GLN A 361     -16.509  -0.286  19.180  1.00 52.44           C  
ANISOU 2687  CG  GLN A 361     7549   6153   6222     78   -425    193       C  
ATOM   2688  CD  GLN A 361     -15.130   0.344  19.226  1.00 51.80           C  
ANISOU 2688  CD  GLN A 361     7505   6014   6162    -27   -432    127       C  
ATOM   2689  OE1 GLN A 361     -14.128  -0.299  18.910  1.00 45.60           O  
ANISOU 2689  OE1 GLN A 361     6655   5274   5396   -107   -453    105       O  
ATOM   2690  NE2 GLN A 361     -15.073   1.612  19.616  1.00 56.83           N  
ANISOU 2690  NE2 GLN A 361     8245   6548   6799    -27   -413     92       N  
ATOM   2691  N   PRO A 362     -18.411  -2.609  21.775  1.00 51.25           N  
ANISOU 2691  N   PRO A 362     7278   6197   5996    259   -429    207       N  
ATOM   2692  CA  PRO A 362     -19.366  -2.155  22.806  1.00 50.90           C  
ANISOU 2692  CA  PRO A 362     7280   6143   5919    353   -395    202       C  
ATOM   2693  C   PRO A 362     -18.752  -2.016  24.188  1.00 49.58           C  
ANISOU 2693  C   PRO A 362     7167   5968   5703    354   -407    131       C  
ATOM   2694  O   PRO A 362     -18.935  -0.983  24.844  1.00 49.66           O  
ANISOU 2694  O   PRO A 362     7265   5916   5687    395   -388     90       O  
ATOM   2695  CB  PRO A 362     -20.453  -3.236  22.763  1.00 48.79           C  
ANISOU 2695  CB  PRO A 362     6926   5958   5654    403   -373    264       C  
ATOM   2696  CG  PRO A 362     -20.445  -3.703  21.364  1.00 49.72           C  
ANISOU 2696  CG  PRO A 362     6981   6098   5813    356   -392    309       C  
ATOM   2697  CD  PRO A 362     -19.005  -3.660  20.926  1.00 51.03           C  
ANISOU 2697  CD  PRO A 362     7162   6237   5990    261   -429    270       C  
ATOM   2698  N   MET A 363     -18.023  -3.032  24.652  1.00 51.98           N  
ANISOU 2698  N   MET A 363     7428   6333   5989    316   -443    112       N  
ATOM   2699  CA  MET A 363     -17.311  -2.901  25.916  1.00 55.78           C  
ANISOU 2699  CA  MET A 363     7962   6817   6416    314   -472     41       C  
ATOM   2700  C   MET A 363     -16.208  -1.852  25.821  1.00 56.78           C  
ANISOU 2700  C   MET A 363     8144   6874   6557    241   -508    -34       C  
ATOM   2701  O   MET A 363     -15.905  -1.178  26.813  1.00 59.18           O  
ANISOU 2701  O   MET A 363     8524   7147   6816    250   -522   -105       O  
ATOM   2702  CB  MET A 363     -16.747  -4.259  26.337  1.00 59.68           C  
ANISOU 2702  CB  MET A 363     8395   7391   6889    298   -508     47       C  
ATOM   2703  CG  MET A 363     -16.030  -4.261  27.674  1.00 66.61           C  
ANISOU 2703  CG  MET A 363     9323   8289   7697    308   -550    -20       C  
ATOM   2704  SD  MET A 363     -16.952  -3.469  29.002  1.00 77.94           S  
ANISOU 2704  SD  MET A 363    10866   9697   9049    403   -504    -48       S  
ATOM   2705  CE  MET A 363     -15.704  -3.421  30.288  1.00 81.05           C  
ANISOU 2705  CE  MET A 363    11316  10116   9362    383   -585   -144       C  
ATOM   2706  N   ILE A 364     -15.618  -1.683  24.635  1.00 53.20           N  
ANISOU 2706  N   ILE A 364     7656   6394   6163    164   -518    -23       N  
ATOM   2707  CA  ILE A 364     -14.618  -0.638  24.438  1.00 46.54           C  
ANISOU 2707  CA  ILE A 364     6861   5476   5345     82   -538    -89       C  
ATOM   2708  C   ILE A 364     -15.271   0.739  24.460  1.00 52.96           C  
ANISOU 2708  C   ILE A 364     7783   6183   6157    118   -493    -98       C  
ATOM   2709  O   ILE A 364     -14.768   1.670  25.101  1.00 58.08           O  
ANISOU 2709  O   ILE A 364     8513   6765   6792     89   -505   -177       O  
ATOM   2710  CB  ILE A 364     -13.849  -0.878  23.126  1.00 36.65           C  
ANISOU 2710  CB  ILE A 364     5543   4227   4154     -9   -544    -65       C  
ATOM   2711  CG1 ILE A 364     -12.948  -2.106  23.249  1.00 39.25           C  
ANISOU 2711  CG1 ILE A 364     5776   4651   4487    -48   -592    -80       C  
ATOM   2712  CG2 ILE A 364     -13.027   0.342  22.751  1.00 35.04           C  
ANISOU 2712  CG2 ILE A 364     5397   3930   3986    -98   -540   -117       C  
ATOM   2713  CD1 ILE A 364     -12.308  -2.517  21.945  1.00 37.98           C  
ANISOU 2713  CD1 ILE A 364     5544   4506   4382   -121   -587    -52       C  
ATOM   2714  N   ALA A 365     -16.402   0.890  23.765  1.00 48.19           N  
ANISOU 2714  N   ALA A 365     7182   5559   5567    186   -445    -21       N  
ATOM   2715  CA  ALA A 365     -17.082   2.180  23.722  1.00 41.79           C  
ANISOU 2715  CA  ALA A 365     6475   4644   4758    240   -401    -20       C  
ATOM   2716  C   ALA A 365     -17.586   2.596  25.097  1.00 40.30           C  
ANISOU 2716  C   ALA A 365     6360   4438   4513    320   -385    -73       C  
ATOM   2717  O   ALA A 365     -17.654   3.794  25.395  1.00 42.96           O  
ANISOU 2717  O   ALA A 365     6809   4670   4845    338   -361   -117       O  
ATOM   2718  CB  ALA A 365     -18.240   2.136  22.725  1.00 35.76           C  
ANISOU 2718  CB  ALA A 365     5684   3885   4017    312   -364     77       C  
ATOM   2719  N   PHE A 366     -17.947   1.630  25.943  1.00 38.80           N  
ANISOU 2719  N   PHE A 366     6120   4344   4277    370   -390    -68       N  
ATOM   2720  CA  PHE A 366     -18.394   1.958  27.293  1.00 44.21           C  
ANISOU 2720  CA  PHE A 366     6880   5022   4894    448   -369   -118       C  
ATOM   2721  C   PHE A 366     -17.262   2.568  28.109  1.00 51.89           C  
ANISOU 2721  C   PHE A 366     7933   5950   5834    380   -416   -230       C  
ATOM   2722  O   PHE A 366     -17.448   3.586  28.786  1.00 57.83           O  
ANISOU 2722  O   PHE A 366     8797   6622   6553    416   -394   -292       O  
ATOM   2723  CB  PHE A 366     -18.945   0.709  27.982  1.00 45.08           C  
ANISOU 2723  CB  PHE A 366     6922   5247   4959    505   -360    -81       C  
ATOM   2724  CG  PHE A 366     -19.225   0.900  29.443  1.00 47.54           C  
ANISOU 2724  CG  PHE A 366     7313   5567   5184    574   -339   -135       C  
ATOM   2725  CD1 PHE A 366     -20.367   1.561  29.861  1.00 47.70           C  
ANISOU 2725  CD1 PHE A 366     7391   5551   5181    681   -265   -128       C  
ATOM   2726  CD2 PHE A 366     -18.346   0.418  30.400  1.00 50.05           C  
ANISOU 2726  CD2 PHE A 366     7647   5933   5438    540   -394   -195       C  
ATOM   2727  CE1 PHE A 366     -20.627   1.741  31.206  1.00 52.00           C  
ANISOU 2727  CE1 PHE A 366     8016   6105   5637    748   -237   -181       C  
ATOM   2728  CE2 PHE A 366     -18.600   0.595  31.745  1.00 50.74           C  
ANISOU 2728  CE2 PHE A 366     7818   6031   5430    607   -376   -245       C  
ATOM   2729  CZ  PHE A 366     -19.743   1.257  32.150  1.00 52.10           C  
ANISOU 2729  CZ  PHE A 366     8055   6165   5576    709   -293   -240       C  
ATOM   2730  N   LEU A 367     -16.076   1.956  28.059  1.00 51.43           N  
ANISOU 2730  N   LEU A 367     7815   5943   5784    283   -484   -261       N  
ATOM   2731  CA  LEU A 367     -14.930   2.511  28.769  1.00 49.72           C  
ANISOU 2731  CA  LEU A 367     7653   5696   5543    207   -542   -373       C  
ATOM   2732  C   LEU A 367     -14.508   3.855  28.189  1.00 50.64           C  
ANISOU 2732  C   LEU A 367     7846   5680   5715    135   -528   -418       C  
ATOM   2733  O   LEU A 367     -14.025   4.722  28.926  1.00 53.68           O  
ANISOU 2733  O   LEU A 367     8323   6000   6073    100   -549   -519       O  
ATOM   2734  CB  LEU A 367     -13.762   1.526  28.732  1.00 49.41           C  
ANISOU 2734  CB  LEU A 367     7512   5750   5513    127   -618   -390       C  
ATOM   2735  CG  LEU A 367     -14.037   0.114  29.254  1.00 49.98           C  
ANISOU 2735  CG  LEU A 367     7513   5942   5535    191   -634   -340       C  
ATOM   2736  CD1 LEU A 367     -12.749  -0.691  29.319  1.00 51.84           C  
ANISOU 2736  CD1 LEU A 367     7664   6255   5777    119   -717   -372       C  
ATOM   2737  CD2 LEU A 367     -14.710   0.161  30.618  1.00 46.95           C  
ANISOU 2737  CD2 LEU A 367     7212   5576   5051    288   -617   -366       C  
ATOM   2738  N   GLU A 368     -14.688   4.048  26.881  1.00 53.17           N  
ANISOU 2738  N   GLU A 368     8139   5957   6106    108   -492   -347       N  
ATOM   2739  CA  GLU A 368     -14.317   5.315  26.259  1.00 52.07           C  
ANISOU 2739  CA  GLU A 368     8084   5681   6019     39   -467   -375       C  
ATOM   2740  C   GLU A 368     -15.312   6.414  26.607  1.00 56.52           C  
ANISOU 2740  C   GLU A 368     8781   6132   6561    136   -407   -381       C  
ATOM   2741  O   GLU A 368     -14.923   7.511  27.024  1.00 63.01           O  
ANISOU 2741  O   GLU A 368     9717   6841   7383     96   -402   -465       O  
ATOM   2742  CB  GLU A 368     -14.225   5.147  24.742  1.00 52.03           C  
ANISOU 2742  CB  GLU A 368     8020   5668   6083     -9   -444   -287       C  
ATOM   2743  CG  GLU A 368     -12.996   4.401  24.258  1.00 55.76           C  
ANISOU 2743  CG  GLU A 368     8381   6213   6592   -128   -491   -301       C  
ATOM   2744  CD  GLU A 368     -12.869   4.419  22.747  1.00 58.30           C  
ANISOU 2744  CD  GLU A 368     8669   6509   6972   -179   -456   -224       C  
ATOM   2745  OE1 GLU A 368     -13.409   3.503  22.092  1.00 57.53           O  
ANISOU 2745  OE1 GLU A 368     8495   6491   6875   -131   -449   -140       O  
ATOM   2746  OE2 GLU A 368     -12.235   5.352  22.213  1.00 63.73           O  
ANISOU 2746  OE2 GLU A 368     9415   7097   7704   -271   -432   -247       O  
ATOM   2747  N   ASP A 369     -16.605   6.137  26.443  1.00 55.43           N  
ANISOU 2747  N   ASP A 369     8629   6023   6409    265   -359   -296       N  
ATOM   2748  CA  ASP A 369     -17.631   7.165  26.571  1.00 55.28           C  
ANISOU 2748  CA  ASP A 369     8721   5900   6382    374   -294   -285       C  
ATOM   2749  C   ASP A 369     -18.096   7.373  28.008  1.00 52.82           C  
ANISOU 2749  C   ASP A 369     8483   5592   5995    460   -279   -357       C  
ATOM   2750  O   ASP A 369     -18.333   8.514  28.418  1.00 58.47           O  
ANISOU 2750  O   ASP A 369     9331   6186   6698    500   -242   -412       O  
ATOM   2751  CB  ASP A 369     -18.831   6.819  25.684  1.00 58.73           C  
ANISOU 2751  CB  ASP A 369     9096   6374   6844    477   -252   -163       C  
ATOM   2752  CG  ASP A 369     -18.445   6.628  24.229  1.00 64.27           C  
ANISOU 2752  CG  ASP A 369     9739   7074   7605    401   -265    -90       C  
ATOM   2753  OD1 ASP A 369     -17.462   7.256  23.783  1.00 64.71           O  
ANISOU 2753  OD1 ASP A 369     9848   7044   7695    291   -275   -126       O  
ATOM   2754  OD2 ASP A 369     -19.126   5.846  23.531  1.00 66.02           O  
ANISOU 2754  OD2 ASP A 369     9864   7382   7839    449   -262     -1       O  
ATOM   2755  N   GLU A 370     -18.238   6.302  28.787  1.00 49.35           N  
ANISOU 2755  N   GLU A 370     7969   5284   5499    493   -300   -357       N  
ATOM   2756  CA  GLU A 370     -18.832   6.409  30.114  1.00 51.17           C  
ANISOU 2756  CA  GLU A 370     8268   5531   5645    592   -271   -408       C  
ATOM   2757  C   GLU A 370     -17.812   6.551  31.234  1.00 54.66           C  
ANISOU 2757  C   GLU A 370     8775   5974   6019    524   -332   -532       C  
ATOM   2758  O   GLU A 370     -18.091   7.246  32.218  1.00 56.96           O  
ANISOU 2758  O   GLU A 370     9184   6212   6246    582   -306   -609       O  
ATOM   2759  CB  GLU A 370     -19.728   5.195  30.392  1.00 54.98           C  
ANISOU 2759  CB  GLU A 370     8647   6149   6093    680   -245   -330       C  
ATOM   2760  CG  GLU A 370     -20.784   4.956  29.324  1.00 63.69           C  
ANISOU 2760  CG  GLU A 370     9667   7272   7260    745   -196   -213       C  
ATOM   2761  CD  GLU A 370     -21.667   6.169  29.089  1.00 70.85           C  
ANISOU 2761  CD  GLU A 370    10662   8067   8189    844   -129   -204       C  
ATOM   2762  OE1 GLU A 370     -21.981   6.882  30.066  1.00 74.03           O  
ANISOU 2762  OE1 GLU A 370    11173   8416   8540    916    -89   -271       O  
ATOM   2763  OE2 GLU A 370     -22.047   6.410  27.924  1.00 70.87           O  
ANISOU 2763  OE2 GLU A 370    10631   8037   8258    857   -118   -130       O  
ATOM   2764  N   LEU A 371     -16.644   5.916  31.119  1.00 52.84           N  
ANISOU 2764  N   LEU A 371     8470   5807   5801    407   -414   -558       N  
ATOM   2765  CA  LEU A 371     -15.583   6.053  32.109  1.00 52.52           C  
ANISOU 2765  CA  LEU A 371     8475   5778   5701    335   -490   -679       C  
ATOM   2766  C   LEU A 371     -14.409   6.884  31.610  1.00 55.60           C  
ANISOU 2766  C   LEU A 371     8892   6077   6157    189   -536   -755       C  
ATOM   2767  O   LEU A 371     -13.403   6.996  32.318  1.00 44.18           O  
ANISOU 2767  O   LEU A 371     7463   4648   4677    108   -613   -863       O  
ATOM   2768  CB  LEU A 371     -15.092   4.669  32.562  1.00 42.08           C  
ANISOU 2768  CB  LEU A 371     7046   4610   4331    323   -556   -661       C  
ATOM   2769  CG  LEU A 371     -16.108   3.900  33.410  1.00 46.22           C  
ANISOU 2769  CG  LEU A 371     7573   5222   4768    454   -512   -612       C  
ATOM   2770  CD1 LEU A 371     -15.748   2.423  33.498  1.00 44.95           C  
ANISOU 2770  CD1 LEU A 371     7296   5197   4587    445   -560   -556       C  
ATOM   2771  CD2 LEU A 371     -16.229   4.518  34.794  1.00 43.27           C  
ANISOU 2771  CD2 LEU A 371     7335   4824   4282    510   -510   -713       C  
ATOM   2772  N   LYS A 372     -14.514   7.465  30.414  1.00 55.25           N  
ANISOU 2772  N   LYS A 372     8851   5938   6205    151   -491   -702       N  
ATOM   2773  CA  LYS A 372     -13.558   8.434  29.879  1.00 52.46           C  
ANISOU 2773  CA  LYS A 372     8545   5468   5921     15   -506   -765       C  
ATOM   2774  C   LYS A 372     -12.161   7.851  29.702  1.00 52.32           C  
ANISOU 2774  C   LYS A 372     8414   5530   5935   -129   -591   -807       C  
ATOM   2775  O   LYS A 372     -11.175   8.592  29.703  1.00 57.57           O  
ANISOU 2775  O   LYS A 372     9113   6124   6639   -258   -622   -899       O  
ATOM   2776  CB  LYS A 372     -13.492   9.694  30.753  1.00 53.34           C  
ANISOU 2776  CB  LYS A 372     8822   5450   5997      8   -497   -887       C  
ATOM   2777  CG  LYS A 372     -14.851  10.262  31.133  1.00 58.03           C  
ANISOU 2777  CG  LYS A 372     9531   5970   6546    168   -413   -862       C  
ATOM   2778  CD  LYS A 372     -15.726  10.491  29.911  1.00 61.70           C  
ANISOU 2778  CD  LYS A 372     9987   6374   7081    234   -334   -734       C  
ATOM   2779  CE  LYS A 372     -17.146  10.853  30.314  1.00 65.69           C  
ANISOU 2779  CE  LYS A 372    10570   6843   7545    413   -254   -699       C  
ATOM   2780  NZ  LYS A 372     -18.069  10.853  29.145  1.00 66.47           N  
ANISOU 2780  NZ  LYS A 372    10628   6923   7704    494   -195   -564       N  
ATOM   2781  N   LEU A 373     -12.050   6.536  29.539  1.00 51.95           N  
ANISOU 2781  N   LEU A 373     8229   5628   5880   -111   -626   -743       N  
ATOM   2782  CA  LEU A 373     -10.756   5.920  29.294  1.00 54.43           C  
ANISOU 2782  CA  LEU A 373     8424   6026   6232   -231   -701   -774       C  
ATOM   2783  C   LEU A 373     -10.321   6.145  27.850  1.00 57.69           C  
ANISOU 2783  C   LEU A 373     8785   6386   6750   -328   -664   -720       C  
ATOM   2784  O   LEU A 373     -11.145   6.207  26.933  1.00 61.55           O  
ANISOU 2784  O   LEU A 373     9286   6831   7268   -275   -593   -618       O  
ATOM   2785  CB  LEU A 373     -10.802   4.421  29.593  1.00 54.34           C  
ANISOU 2785  CB  LEU A 373     8296   6175   6176   -168   -744   -720       C  
ATOM   2786  CG  LEU A 373     -10.412   3.977  31.006  1.00 60.79           C  
ANISOU 2786  CG  LEU A 373     9120   7082   6896   -137   -825   -801       C  
ATOM   2787  CD1 LEU A 373     -11.442   4.432  32.029  1.00 61.23           C  
ANISOU 2787  CD1 LEU A 373     9309   7100   6857    -22   -786   -823       C  
ATOM   2788  CD2 LEU A 373     -10.235   2.468  31.057  1.00 64.71           C  
ANISOU 2788  CD2 LEU A 373     9494   7724   7370    -96   -867   -736       C  
ATOM   2789  N   SER A 374      -9.010   6.274  27.657  1.00 57.27           N  
ANISOU 2789  N   SER A 374     8670   6341   6748   -470   -713   -789       N  
ATOM   2790  CA  SER A 374      -8.469   6.413  26.313  1.00 56.23           C  
ANISOU 2790  CA  SER A 374     8482   6173   6711   -573   -672   -740       C  
ATOM   2791  C   SER A 374      -8.741   5.150  25.505  1.00 57.07           C  
ANISOU 2791  C   SER A 374     8467   6390   6828   -520   -661   -627       C  
ATOM   2792  O   SER A 374      -8.908   4.059  26.056  1.00 58.35           O  
ANISOU 2792  O   SER A 374     8558   6672   6940   -445   -706   -610       O  
ATOM   2793  CB  SER A 374      -6.965   6.686  26.369  1.00 54.93           C  
ANISOU 2793  CB  SER A 374     8251   6018   6601   -738   -727   -844       C  
ATOM   2794  OG  SER A 374      -6.266   5.567  26.887  1.00 51.07           O  
ANISOU 2794  OG  SER A 374     7627   5688   6089   -737   -815   -874       O  
ATOM   2795  N   ARG A 375      -8.793   5.308  24.180  1.00 55.42           N  
ANISOU 2795  N   ARG A 375     8245   6133   6679   -560   -598   -549       N  
ATOM   2796  CA  ARG A 375      -9.045   4.160  23.314  1.00 52.01           C  
ANISOU 2796  CA  ARG A 375     7708   5797   6257   -518   -585   -449       C  
ATOM   2797  C   ARG A 375      -7.978   3.090  23.494  1.00 51.90           C  
ANISOU 2797  C   ARG A 375     7550   5914   6255   -570   -651   -485       C  
ATOM   2798  O   ARG A 375      -8.277   1.891  23.456  1.00 56.30           O  
ANISOU 2798  O   ARG A 375     8028   6574   6788   -498   -669   -430       O  
ATOM   2799  CB  ARG A 375      -9.113   4.601  21.853  1.00 52.60           C  
ANISOU 2799  CB  ARG A 375     7802   5797   6386   -566   -510   -372       C  
ATOM   2800  CG  ARG A 375      -9.455   3.468  20.899  1.00 52.10           C  
ANISOU 2800  CG  ARG A 375     7646   5825   6325   -522   -496   -274       C  
ATOM   2801  CD  ARG A 375      -9.527   3.942  19.461  1.00 56.54           C  
ANISOU 2801  CD  ARG A 375     8242   6317   6924   -564   -425   -199       C  
ATOM   2802  NE  ARG A 375      -8.217   4.288  18.918  1.00 59.93           N  
ANISOU 2802  NE  ARG A 375     8635   6723   7413   -713   -407   -242       N  
ATOM   2803  CZ  ARG A 375      -7.911   5.473  18.400  1.00 62.91           C  
ANISOU 2803  CZ  ARG A 375     9104   6971   7827   -798   -349   -246       C  
ATOM   2804  NH1 ARG A 375      -8.822   6.435  18.351  1.00 65.74           N  
ANISOU 2804  NH1 ARG A 375     9604   7207   8165   -736   -309   -208       N  
ATOM   2805  NH2 ARG A 375      -6.692   5.695  17.929  1.00 61.22           N  
ANISOU 2805  NH2 ARG A 375     8841   6749   7673   -942   -326   -286       N  
ATOM   2806  N   LYS A 376      -6.726   3.504  23.698  1.00 51.33           N  
ANISOU 2806  N   LYS A 376     7439   5838   6225   -693   -687   -579       N  
ATOM   2807  CA  LYS A 376      -5.654   2.540  23.921  1.00 49.46           C  
ANISOU 2807  CA  LYS A 376     7057   5731   6004   -734   -757   -620       C  
ATOM   2808  C   LYS A 376      -5.910   1.721  25.179  1.00 53.07           C  
ANISOU 2808  C   LYS A 376     7498   6286   6380   -629   -835   -644       C  
ATOM   2809  O   LYS A 376      -5.888   0.485  25.145  1.00 54.07           O  
ANISOU 2809  O   LYS A 376     7535   6519   6492   -568   -861   -597       O  
ATOM   2810  CB  LYS A 376      -4.312   3.266  24.008  1.00 46.02           C  
ANISOU 2810  CB  LYS A 376     6580   5275   5631   -888   -785   -728       C  
ATOM   2811  CG  LYS A 376      -3.151   2.379  24.418  1.00 49.39           C  
ANISOU 2811  CG  LYS A 376     6851   5843   6074   -921   -872   -788       C  
ATOM   2812  CD  LYS A 376      -1.890   3.200  24.630  1.00 56.46           C  
ANISOU 2812  CD  LYS A 376     7700   6720   7032  -1078   -908   -908       C  
ATOM   2813  CE  LYS A 376      -0.778   2.364  25.239  1.00 63.17           C  
ANISOU 2813  CE  LYS A 376     8391   7722   7888  -1092  -1014   -979       C  
ATOM   2814  NZ  LYS A 376       0.424   3.189  25.546  1.00 70.37           N  
ANISOU 2814  NZ  LYS A 376     9247   8627   8862  -1248  -1061  -1109       N  
ATOM   2815  N   HIS A 377      -6.168   2.395  26.302  1.00 52.64           N  
ANISOU 2815  N   HIS A 377     7542   6191   6268   -603   -869   -715       N  
ATOM   2816  CA  HIS A 377      -6.444   1.681  27.543  1.00 50.85           C  
ANISOU 2816  CA  HIS A 377     7320   6053   5950   -500   -936   -734       C  
ATOM   2817  C   HIS A 377      -7.768   0.931  27.478  1.00 50.96           C  
ANISOU 2817  C   HIS A 377     7363   6087   5914   -363   -886   -623       C  
ATOM   2818  O   HIS A 377      -7.910  -0.125  28.105  1.00 56.67           O  
ANISOU 2818  O   HIS A 377     8046   6906   6580   -282   -925   -599       O  
ATOM   2819  CB  HIS A 377      -6.444   2.654  28.721  1.00 57.01           C  
ANISOU 2819  CB  HIS A 377     8212   6778   6670   -506   -975   -841       C  
ATOM   2820  CG  HIS A 377      -5.115   3.293  28.974  1.00 61.15           C  
ANISOU 2820  CG  HIS A 377     8698   7299   7237   -645  -1044   -966       C  
ATOM   2821  ND1 HIS A 377      -4.981   4.497  29.632  1.00 61.99           N  
ANISOU 2821  ND1 HIS A 377     8915   7313   7326   -703  -1060  -1074       N  
ATOM   2822  CD2 HIS A 377      -3.860   2.896  28.656  1.00 60.98           C  
ANISOU 2822  CD2 HIS A 377     8534   7358   7278   -741  -1099  -1006       C  
ATOM   2823  CE1 HIS A 377      -3.700   4.813  29.709  1.00 64.19           C  
ANISOU 2823  CE1 HIS A 377     9116   7615   7657   -838  -1126  -1177       C  
ATOM   2824  NE2 HIS A 377      -2.999   3.858  29.125  1.00 63.21           N  
ANISOU 2824  NE2 HIS A 377     8832   7601   7584   -861  -1150  -1136       N  
ATOM   2825  N   ALA A 378      -8.742   1.456  26.732  1.00 45.65           N  
ANISOU 2825  N   ALA A 378     6757   5324   5263   -336   -799   -555       N  
ATOM   2826  CA  ALA A 378     -10.024   0.770  26.605  1.00 40.75           C  
ANISOU 2826  CA  ALA A 378     6147   4728   4607   -216   -751   -453       C  
ATOM   2827  C   ALA A 378      -9.867  -0.548  25.859  1.00 47.23           C  
ANISOU 2827  C   ALA A 378     6847   5640   5456   -209   -754   -379       C  
ATOM   2828  O   ALA A 378     -10.356  -1.589  26.310  1.00 49.64           O  
ANISOU 2828  O   ALA A 378     7124   6021   5718   -126   -765   -335       O  
ATOM   2829  CB  ALA A 378     -11.038   1.672  25.902  1.00 38.51           C  
ANISOU 2829  CB  ALA A 378     5951   4336   4346   -188   -668   -400       C  
ATOM   2830  N   VAL A 379      -9.178  -0.525  24.716  1.00 46.14           N  
ANISOU 2830  N   VAL A 379     6645   5492   5392   -298   -739   -366       N  
ATOM   2831  CA  VAL A 379      -8.986  -1.748  23.940  1.00 40.83           C  
ANISOU 2831  CA  VAL A 379     5866   4899   4748   -293   -737   -304       C  
ATOM   2832  C   VAL A 379      -8.197  -2.774  24.744  1.00 43.01           C  
ANISOU 2832  C   VAL A 379     6062   5279   4999   -276   -812   -341       C  
ATOM   2833  O   VAL A 379      -8.543  -3.961  24.773  1.00 43.38           O  
ANISOU 2833  O   VAL A 379     6064   5391   5025   -208   -816   -284       O  
ATOM   2834  CB  VAL A 379      -8.297  -1.427  22.600  1.00 38.11           C  
ANISOU 2834  CB  VAL A 379     5478   4523   4481   -395   -700   -294       C  
ATOM   2835  CG1 VAL A 379      -7.889  -2.709  21.886  1.00 35.68           C  
ANISOU 2835  CG1 VAL A 379     5057   4301   4199   -396   -703   -251       C  
ATOM   2836  CG2 VAL A 379      -9.210  -0.593  21.719  1.00 35.29           C  
ANISOU 2836  CG2 VAL A 379     5205   4068   4135   -388   -625   -233       C  
ATOM   2837  N   LEU A 380      -7.136  -2.331  25.422  1.00 44.89           N  
ANISOU 2837  N   LEU A 380     6284   5534   5239   -335   -876   -437       N  
ATOM   2838  CA  LEU A 380      -6.276  -3.266  26.143  1.00 44.50           C  
ANISOU 2838  CA  LEU A 380     6151   5591   5167   -314   -960   -474       C  
ATOM   2839  C   LEU A 380      -7.003  -3.904  27.320  1.00 46.29           C  
ANISOU 2839  C   LEU A 380     6433   5860   5297   -195   -989   -451       C  
ATOM   2840  O   LEU A 380      -6.809  -5.093  27.603  1.00 48.48           O  
ANISOU 2840  O   LEU A 380     6653   6218   5550   -136  -1023   -419       O  
ATOM   2841  CB  LEU A 380      -5.013  -2.555  26.620  1.00 37.94           C  
ANISOU 2841  CB  LEU A 380     5285   4772   4358   -408  -1030   -589       C  
ATOM   2842  CG  LEU A 380      -4.011  -2.127  25.546  1.00 43.27           C  
ANISOU 2842  CG  LEU A 380     5875   5431   5135   -538  -1006   -619       C  
ATOM   2843  CD1 LEU A 380      -2.685  -1.741  26.179  1.00 47.16           C  
ANISOU 2843  CD1 LEU A 380     6297   5972   5650   -622  -1094   -737       C  
ATOM   2844  CD2 LEU A 380      -3.815  -3.227  24.513  1.00 41.22           C  
ANISOU 2844  CD2 LEU A 380     5512   5226   4922   -523   -972   -546       C  
ATOM   2845  N   TRP A 381      -7.848  -3.139  28.016  1.00 41.33           N  
ANISOU 2845  N   TRP A 381     5919   5174   4609   -155   -968   -465       N  
ATOM   2846  CA  TRP A 381      -8.517  -3.681  29.194  1.00 38.00           C  
ANISOU 2846  CA  TRP A 381     5557   4794   4088    -46   -985   -447       C  
ATOM   2847  C   TRP A 381      -9.607  -4.673  28.809  1.00 39.22           C  
ANISOU 2847  C   TRP A 381     5703   4963   4236     34   -918   -333       C  
ATOM   2848  O   TRP A 381      -9.740  -5.728  29.439  1.00 39.82           O  
ANISOU 2848  O   TRP A 381     5768   5104   4259    107   -938   -296       O  
ATOM   2849  CB  TRP A 381      -9.088  -2.549  30.047  1.00 40.41           C  
ANISOU 2849  CB  TRP A 381     5990   5034   4331    -25   -972   -502       C  
ATOM   2850  CG  TRP A 381      -8.147  -2.082  31.120  1.00 47.15           C  
ANISOU 2850  CG  TRP A 381     6869   5916   5131    -55  -1067   -618       C  
ATOM   2851  CD1 TRP A 381      -7.687  -0.812  31.310  1.00 52.54           C  
ANISOU 2851  CD1 TRP A 381     7606   6531   5827   -136  -1089   -719       C  
ATOM   2852  CD2 TRP A 381      -7.548  -2.883  32.149  1.00 49.36           C  
ANISOU 2852  CD2 TRP A 381     7123   6298   5332     -6  -1159   -646       C  
ATOM   2853  NE1 TRP A 381      -6.841  -0.771  32.392  1.00 51.84           N  
ANISOU 2853  NE1 TRP A 381     7520   6504   5673   -146  -1194   -818       N  
ATOM   2854  CE2 TRP A 381      -6.739  -2.029  32.924  1.00 49.72           C  
ANISOU 2854  CE2 TRP A 381     7203   6344   5343    -61  -1242   -772       C  
ATOM   2855  CE3 TRP A 381      -7.618  -4.238  32.490  1.00 52.86           C  
ANISOU 2855  CE3 TRP A 381     7526   6828   5729     81  -1180   -577       C  
ATOM   2856  CZ2 TRP A 381      -6.005  -2.484  34.018  1.00 51.98           C  
ANISOU 2856  CZ2 TRP A 381     7477   6727   5544    -27  -1354   -830       C  
ATOM   2857  CZ3 TRP A 381      -6.889  -4.688  33.576  1.00 52.20           C  
ANISOU 2857  CZ3 TRP A 381     7440   6832   5561    121  -1284   -625       C  
ATOM   2858  CH2 TRP A 381      -6.094  -3.814  34.327  1.00 51.90           C  
ANISOU 2858  CH2 TRP A 381     7430   6805   5484     71  -1374   -751       C  
ATOM   2859  N   THR A 382     -10.396  -4.358  27.778  1.00 40.18           N  
ANISOU 2859  N   THR A 382     5831   5025   4412     21   -840   -276       N  
ATOM   2860  CA  THR A 382     -11.393  -5.314  27.305  1.00 41.73           C  
ANISOU 2860  CA  THR A 382     6002   5241   4613     80   -784   -176       C  
ATOM   2861  C   THR A 382     -10.727  -6.554  26.723  1.00 41.17           C  
ANISOU 2861  C   THR A 382     5830   5230   4580     63   -808   -144       C  
ATOM   2862  O   THR A 382     -11.243  -7.669  26.868  1.00 47.65           O  
ANISOU 2862  O   THR A 382     6634   6089   5381    122   -792    -82       O  
ATOM   2863  CB  THR A 382     -12.308  -4.665  26.265  1.00 45.85           C  
ANISOU 2863  CB  THR A 382     6544   5694   5183     69   -711   -129       C  
ATOM   2864  OG1 THR A 382     -11.588  -4.475  25.042  1.00 57.19           O  
ANISOU 2864  OG1 THR A 382     7925   7111   6693    -18   -710   -132       O  
ATOM   2865  CG2 THR A 382     -12.814  -3.324  26.762  1.00 44.90           C  
ANISOU 2865  CG2 THR A 382     6526   5499   5035     86   -686   -169       C  
ATOM   2866  N   ALA A 383      -9.580  -6.380  26.063  1.00 38.95           N  
ANISOU 2866  N   ALA A 383     5485   4957   4360    -18   -841   -187       N  
ATOM   2867  CA  ALA A 383      -8.845  -7.528  25.544  1.00 40.11           C  
ANISOU 2867  CA  ALA A 383     5534   5162   4543    -27   -863   -167       C  
ATOM   2868  C   ALA A 383      -8.353  -8.420  26.674  1.00 43.27           C  
ANISOU 2868  C   ALA A 383     5921   5633   4886     38   -930   -180       C  
ATOM   2869  O   ALA A 383      -8.368  -9.651  26.555  1.00 44.11           O  
ANISOU 2869  O   ALA A 383     5989   5777   4995     84   -928   -128       O  
ATOM   2870  CB  ALA A 383      -7.674  -7.059  24.684  1.00 41.63           C  
ANISOU 2870  CB  ALA A 383     5656   5353   4810   -127   -876   -218       C  
ATOM   2871  N   ALA A 384      -7.910  -7.816  27.780  1.00 50.04           N  
ANISOU 2871  N   ALA A 384     6819   6506   5689     45   -992   -250       N  
ATOM   2872  CA  ALA A 384      -7.493  -8.604  28.934  1.00 51.60           C  
ANISOU 2872  CA  ALA A 384     7019   6774   5813    120  -1063   -259       C  
ATOM   2873  C   ALA A 384      -8.672  -9.355  29.540  1.00 48.74           C  
ANISOU 2873  C   ALA A 384     6730   6409   5380    217  -1016   -177       C  
ATOM   2874  O   ALA A 384      -8.521 -10.494  29.996  1.00 51.45           O  
ANISOU 2874  O   ALA A 384     7063   6799   5688    283  -1040   -136       O  
ATOM   2875  CB  ALA A 384      -6.832  -7.702  29.976  1.00 57.20           C  
ANISOU 2875  CB  ALA A 384     7765   7502   6468    103  -1143   -359       C  
ATOM   2876  N   ILE A 385      -9.855  -8.735  29.549  1.00 44.57           N  
ANISOU 2876  N   ILE A 385     6276   5825   4834    227   -944   -152       N  
ATOM   2877  CA  ILE A 385     -11.048  -9.418  30.038  1.00 46.77           C  
ANISOU 2877  CA  ILE A 385     6610   6103   5058    307   -883    -73       C  
ATOM   2878  C   ILE A 385     -11.393 -10.597  29.137  1.00 51.55           C  
ANISOU 2878  C   ILE A 385     7153   6711   5722    310   -837      9       C  
ATOM   2879  O   ILE A 385     -11.700 -11.695  29.617  1.00 58.29           O  
ANISOU 2879  O   ILE A 385     8021   7589   6538    370   -824     67       O  
ATOM   2880  CB  ILE A 385     -12.223  -8.429  30.147  1.00 47.51           C  
ANISOU 2880  CB  ILE A 385     6778   6141   5134    318   -812    -69       C  
ATOM   2881  CG1 ILE A 385     -11.906  -7.326  31.157  1.00 52.37           C  
ANISOU 2881  CG1 ILE A 385     7472   6745   5679    324   -854   -156       C  
ATOM   2882  CG2 ILE A 385     -13.498  -9.158  30.538  1.00 44.72           C  
ANISOU 2882  CG2 ILE A 385     6459   5793   4740    391   -736     15       C  
ATOM   2883  CD1 ILE A 385     -12.937  -6.218  31.192  1.00 53.51           C  
ANISOU 2883  CD1 ILE A 385     7692   6824   5816    336   -785   -164       C  
ATOM   2884  N   VAL A 386     -11.342 -10.392  27.819  1.00 43.43           N  
ANISOU 2884  N   VAL A 386     6064   5654   4782    243   -811     14       N  
ATOM   2885  CA  VAL A 386     -11.695 -11.456  26.883  1.00 42.60           C  
ANISOU 2885  CA  VAL A 386     5906   5549   4731    237   -769     81       C  
ATOM   2886  C   VAL A 386     -10.657 -12.572  26.925  1.00 43.46           C  
ANISOU 2886  C   VAL A 386     5962   5700   4849    254   -819     80       C  
ATOM   2887  O   VAL A 386     -11.001 -13.759  26.980  1.00 44.64           O  
ANISOU 2887  O   VAL A 386     6113   5855   4994    296   -795    140       O  
ATOM   2888  CB  VAL A 386     -11.857 -10.888  25.461  1.00 39.09           C  
ANISOU 2888  CB  VAL A 386     5422   5068   4364    165   -733     81       C  
ATOM   2889  CG1 VAL A 386     -11.948 -12.013  24.437  1.00 32.72           C  
ANISOU 2889  CG1 VAL A 386     4556   4268   3609    151   -706    129       C  
ATOM   2890  CG2 VAL A 386     -13.085  -9.991  25.385  1.00 32.55           C  
ANISOU 2890  CG2 VAL A 386     4645   4197   3526    174   -678    101       C  
ATOM   2891  N   PHE A 387      -9.371 -12.209  26.906  1.00 43.80           N  
ANISOU 2891  N   PHE A 387     5958   5772   4911    221   -886     13       N  
ATOM   2892  CA  PHE A 387      -8.317 -13.220  26.895  1.00 48.91           C  
ANISOU 2892  CA  PHE A 387     6542   6466   5576    246   -937      8       C  
ATOM   2893  C   PHE A 387      -8.314 -14.038  28.180  1.00 54.01           C  
ANISOU 2893  C   PHE A 387     7239   7144   6138    343   -975     37       C  
ATOM   2894  O   PHE A 387      -8.132 -15.261  28.143  1.00 57.45           O  
ANISOU 2894  O   PHE A 387     7658   7590   6579    393   -975     83       O  
ATOM   2895  CB  PHE A 387      -6.955 -12.561  26.681  1.00 49.69           C  
ANISOU 2895  CB  PHE A 387     6566   6599   5715    189  -1002    -77       C  
ATOM   2896  CG  PHE A 387      -5.798 -13.508  26.824  1.00 54.57           C  
ANISOU 2896  CG  PHE A 387     7109   7279   6348    230  -1064    -90       C  
ATOM   2897  CD1 PHE A 387      -5.537 -14.452  25.845  1.00 58.20           C  
ANISOU 2897  CD1 PHE A 387     7506   7736   6871    231  -1030    -58       C  
ATOM   2898  CD2 PHE A 387      -4.975 -13.459  27.937  1.00 55.86           C  
ANISOU 2898  CD2 PHE A 387     7264   7502   6457    275  -1160   -138       C  
ATOM   2899  CE1 PHE A 387      -4.477 -15.328  25.972  1.00 59.19           C  
ANISOU 2899  CE1 PHE A 387     7560   7915   7013    282  -1083    -70       C  
ATOM   2900  CE2 PHE A 387      -3.912 -14.333  28.070  1.00 54.40           C  
ANISOU 2900  CE2 PHE A 387     7003   7380   6287    327  -1223   -148       C  
ATOM   2901  CZ  PHE A 387      -3.662 -15.268  27.085  1.00 55.72           C  
ANISOU 2901  CZ  PHE A 387     7107   7540   6526    334  -1182   -112       C  
ATOM   2902  N   PHE A 388      -8.509 -13.382  29.325  1.00 52.01           N  
ANISOU 2902  N   PHE A 388     7057   6904   5801    374  -1005     10       N  
ATOM   2903  CA  PHE A 388      -8.513 -14.098  30.597  1.00 49.89           C  
ANISOU 2903  CA  PHE A 388     6853   6669   5435    471  -1041     40       C  
ATOM   2904  C   PHE A 388      -9.713 -15.031  30.698  1.00 50.69           C  
ANISOU 2904  C   PHE A 388     7014   6733   5514    518   -953    140       C  
ATOM   2905  O   PHE A 388      -9.573 -16.202  31.072  1.00 49.51           O  
ANISOU 2905  O   PHE A 388     6882   6593   5337    584   -959    195       O  
ATOM   2906  CB  PHE A 388      -8.504 -13.101  31.756  1.00 47.82           C  
ANISOU 2906  CB  PHE A 388     6664   6427   5079    488  -1088    -18       C  
ATOM   2907  CG  PHE A 388      -8.644 -13.739  33.106  1.00 49.04           C  
ANISOU 2907  CG  PHE A 388     6907   6616   5111    591  -1115     18       C  
ATOM   2908  CD1 PHE A 388      -7.551 -14.317  33.729  1.00 52.08           C  
ANISOU 2908  CD1 PHE A 388     7271   7066   5452    650  -1218     -1       C  
ATOM   2909  CD2 PHE A 388      -9.868 -13.758  33.754  1.00 47.23           C  
ANISOU 2909  CD2 PHE A 388     6779   6358   4809    634  -1037     72       C  
ATOM   2910  CE1 PHE A 388      -7.676 -14.904  34.972  1.00 51.76           C  
ANISOU 2910  CE1 PHE A 388     7325   7056   5286    753  -1245     40       C  
ATOM   2911  CE2 PHE A 388     -10.000 -14.344  34.996  1.00 49.94           C  
ANISOU 2911  CE2 PHE A 388     7214   6730   5030    729  -1052    111       C  
ATOM   2912  CZ  PHE A 388      -8.901 -14.916  35.605  1.00 51.06           C  
ANISOU 2912  CZ  PHE A 388     7350   6934   5119    789  -1158     97       C  
ATOM   2913  N   SER A 389     -10.904 -14.529  30.365  1.00 49.10           N  
ANISOU 2913  N   SER A 389     6842   6487   5327    485   -869    164       N  
ATOM   2914  CA  SER A 389     -12.107 -15.348  30.454  1.00 47.19           C  
ANISOU 2914  CA  SER A 389     6642   6214   5073    515   -780    252       C  
ATOM   2915  C   SER A 389     -12.083 -16.502  29.461  1.00 49.90           C  
ANISOU 2915  C   SER A 389     6929   6535   5496    495   -750    301       C  
ATOM   2916  O   SER A 389     -12.718 -17.536  29.700  1.00 54.19           O  
ANISOU 2916  O   SER A 389     7508   7057   6026    528   -696    373       O  
ATOM   2917  CB  SER A 389     -13.345 -14.483  30.225  1.00 44.04           C  
ANISOU 2917  CB  SER A 389     6265   5784   4685    485   -703    259       C  
ATOM   2918  OG  SER A 389     -13.416 -13.431  31.171  1.00 44.92           O  
ANISOU 2918  OG  SER A 389     6441   5906   4720    510   -721    212       O  
ATOM   2919  N   ALA A 390     -11.360 -16.348  28.350  1.00 49.03           N  
ANISOU 2919  N   ALA A 390     6737   6425   5467    438   -778    260       N  
ATOM   2920  CA  ALA A 390     -11.326 -17.387  27.328  1.00 46.84           C  
ANISOU 2920  CA  ALA A 390     6410   6123   5262    416   -747    294       C  
ATOM   2921  C   ALA A 390     -10.678 -18.673  27.822  1.00 45.65           C  
ANISOU 2921  C   ALA A 390     6275   5979   5091    487   -775    327       C  
ATOM   2922  O   ALA A 390     -10.913 -19.733  27.231  1.00 47.30           O  
ANISOU 2922  O   ALA A 390     6476   6151   5345    485   -732    371       O  
ATOM   2923  CB  ALA A 390     -10.594 -16.880  26.088  1.00 40.96           C  
ANISOU 2923  CB  ALA A 390     5582   5384   4596    346   -767    239       C  
ATOM   2924  N   HIS A 391      -9.876 -18.609  28.887  1.00 44.53           N  
ANISOU 2924  N   HIS A 391     6159   5881   4881    553   -849    307       N  
ATOM   2925  CA  HIS A 391      -9.294 -19.822  29.450  1.00 45.14           C  
ANISOU 2925  CA  HIS A 391     6261   5962   4926    640   -880    349       C  
ATOM   2926  C   HIS A 391     -10.358 -20.770  29.985  1.00 40.77           C  
ANISOU 2926  C   HIS A 391     5801   5358   4332    680   -802    442       C  
ATOM   2927  O   HIS A 391     -10.077 -21.958  30.177  1.00 39.79           O  
ANISOU 2927  O   HIS A 391     5707   5209   4202    741   -800    493       O  
ATOM   2928  CB  HIS A 391      -8.299 -19.466  30.556  1.00 47.67           C  
ANISOU 2928  CB  HIS A 391     6594   6351   5167    708   -985    307       C  
ATOM   2929  CG  HIS A 391      -7.025 -18.865  30.049  1.00 50.25           C  
ANISOU 2929  CG  HIS A 391     6813   6732   5548    674  -1067    219       C  
ATOM   2930  ND1 HIS A 391      -6.956 -17.586  29.541  1.00 51.87           N  
ANISOU 2930  ND1 HIS A 391     6970   6947   5792    582  -1071    148       N  
ATOM   2931  CD2 HIS A 391      -5.771 -19.370  29.967  1.00 52.54           C  
ANISOU 2931  CD2 HIS A 391     7031   7068   5865    718  -1141    192       C  
ATOM   2932  CE1 HIS A 391      -5.715 -17.328  29.170  1.00 52.88           C  
ANISOU 2932  CE1 HIS A 391     6999   7124   5968    560  -1140     80       C  
ATOM   2933  NE2 HIS A 391      -4.976 -18.394  29.418  1.00 53.74           N  
ANISOU 2933  NE2 HIS A 391     7084   7261   6073    644  -1185    102       N  
ATOM   2934  N   LEU A 392     -11.572 -20.272  30.227  1.00 40.64           N  
ANISOU 2934  N   LEU A 392     5829   5323   4289    648   -732    466       N  
ATOM   2935  CA  LEU A 392     -12.662 -21.144  30.651  1.00 40.67           C  
ANISOU 2935  CA  LEU A 392     5907   5278   4266    668   -642    553       C  
ATOM   2936  C   LEU A 392     -13.115 -22.046  29.509  1.00 44.32           C  
ANISOU 2936  C   LEU A 392     6330   5681   4828    611   -578    585       C  
ATOM   2937  O   LEU A 392     -13.216 -23.267  29.671  1.00 45.65           O  
ANISOU 2937  O   LEU A 392     6546   5801   4998    643   -543    646       O  
ATOM   2938  CB  LEU A 392     -13.825 -20.304  31.177  1.00 39.19           C  
ANISOU 2938  CB  LEU A 392     5760   5097   4034    649   -580    562       C  
ATOM   2939  CG  LEU A 392     -14.539 -20.842  32.417  1.00 46.21           C  
ANISOU 2939  CG  LEU A 392     6756   5974   4827    711   -519    638       C  
ATOM   2940  CD1 LEU A 392     -13.555 -21.044  33.558  1.00 46.98           C  
ANISOU 2940  CD1 LEU A 392     6925   6108   4817    809   -600    639       C  
ATOM   2941  CD2 LEU A 392     -15.659 -19.904  32.831  1.00 46.09           C  
ANISOU 2941  CD2 LEU A 392     6764   5972   4777    692   -452    635       C  
ATOM   2942  N   VAL A 393     -13.388 -21.463  28.338  1.00 47.39           N  
ANISOU 2942  N   VAL A 393     6641   6069   5295    527   -565    542       N  
ATOM   2943  CA  VAL A 393     -13.815 -22.252  27.188  1.00 49.40           C  
ANISOU 2943  CA  VAL A 393     6859   6275   5636    468   -514    559       C  
ATOM   2944  C   VAL A 393     -12.672 -23.018  26.542  1.00 50.15           C  
ANISOU 2944  C   VAL A 393     6921   6356   5777    485   -557    536       C  
ATOM   2945  O   VAL A 393     -12.922 -23.920  25.735  1.00 50.18           O  
ANISOU 2945  O   VAL A 393     6916   6309   5841    452   -515    553       O  
ATOM   2946  CB  VAL A 393     -14.494 -21.358  26.130  1.00 50.04           C  
ANISOU 2946  CB  VAL A 393     6874   6365   5773    381   -492    523       C  
ATOM   2947  CG1 VAL A 393     -15.453 -20.388  26.795  1.00 50.08           C  
ANISOU 2947  CG1 VAL A 393     6902   6393   5732    381   -460    532       C  
ATOM   2948  CG2 VAL A 393     -13.454 -20.613  25.305  1.00 51.37           C  
ANISOU 2948  CG2 VAL A 393     6977   6566   5977    355   -556    451       C  
ATOM   2949  N   MET A 394     -11.424 -22.686  26.877  1.00 49.93           N  
ANISOU 2949  N   MET A 394     6870   6375   5725    537   -639    494       N  
ATOM   2950  CA  MET A 394     -10.286 -23.395  26.306  1.00 47.44           C  
ANISOU 2950  CA  MET A 394     6512   6057   5456    566   -677    471       C  
ATOM   2951  C   MET A 394     -10.017 -24.714  27.016  1.00 43.42           C  
ANISOU 2951  C   MET A 394     6073   5507   4917    659   -675    532       C  
ATOM   2952  O   MET A 394      -9.605 -25.685  26.373  1.00 40.34           O  
ANISOU 2952  O   MET A 394     5673   5073   4581    675   -661    537       O  
ATOM   2953  CB  MET A 394      -9.036 -22.516  26.358  1.00 53.02           C  
ANISOU 2953  CB  MET A 394     7148   6838   6159    581   -766    398       C  
ATOM   2954  CG  MET A 394      -9.002 -21.426  25.301  1.00 62.24           C  
ANISOU 2954  CG  MET A 394     8239   8028   7380    485   -762    335       C  
ATOM   2955  SD  MET A 394      -7.351 -20.746  25.040  1.00 68.87           S  
ANISOU 2955  SD  MET A 394     8977   8941   8250    484   -847    248       S  
ATOM   2956  CE  MET A 394      -7.106 -19.845  26.567  1.00 66.65           C  
ANISOU 2956  CE  MET A 394     8733   8716   7877    528   -925    226       C  
ATOM   2957  N   PHE A 395     -10.250 -24.773  28.327  1.00 48.59           N  
ANISOU 2957  N   PHE A 395     6811   6170   5483    726   -684    581       N  
ATOM   2958  CA  PHE A 395      -9.885 -25.934  29.126  1.00 48.89           C  
ANISOU 2958  CA  PHE A 395     6930   6173   5475    831   -692    646       C  
ATOM   2959  C   PHE A 395     -11.068 -26.679  29.719  1.00 51.64           C  
ANISOU 2959  C   PHE A 395     7387   6447   5787    832   -597    738       C  
ATOM   2960  O   PHE A 395     -10.948 -27.874  29.992  1.00 61.20           O  
ANISOU 2960  O   PHE A 395     8671   7591   6992    893   -572    801       O  
ATOM   2961  CB  PHE A 395      -8.947 -25.517  30.264  1.00 49.97           C  
ANISOU 2961  CB  PHE A 395     7081   6386   5520    929   -794    632       C  
ATOM   2962  CG  PHE A 395      -7.616 -25.013  29.792  1.00 55.31           C  
ANISOU 2962  CG  PHE A 395     7644   7135   6237    940   -890    546       C  
ATOM   2963  CD1 PHE A 395      -6.572 -25.891  29.560  1.00 58.18           C  
ANISOU 2963  CD1 PHE A 395     7975   7496   6635   1018   -933    546       C  
ATOM   2964  CD2 PHE A 395      -7.410 -23.661  29.574  1.00 57.98           C  
ANISOU 2964  CD2 PHE A 395     7907   7539   6583    871   -931    466       C  
ATOM   2965  CE1 PHE A 395      -5.347 -25.432  29.122  1.00 60.95           C  
ANISOU 2965  CE1 PHE A 395     8206   7921   7030   1025  -1014    466       C  
ATOM   2966  CE2 PHE A 395      -6.186 -23.195  29.136  1.00 61.51           C  
ANISOU 2966  CE2 PHE A 395     8244   8051   7074    867  -1010    387       C  
ATOM   2967  CZ  PHE A 395      -5.154 -24.081  28.910  1.00 62.86           C  
ANISOU 2967  CZ  PHE A 395     8370   8232   7283    942  -1051    386       C  
ATOM   2968  N   LEU A 396     -12.199 -26.014  29.933  1.00 44.72           N  
ANISOU 2968  N   LEU A 396     6525   5577   4889    767   -539    749       N  
ATOM   2969  CA  LEU A 396     -13.370 -26.659  30.511  1.00 46.18           C  
ANISOU 2969  CA  LEU A 396     6801   5701   5044    757   -438    834       C  
ATOM   2970  C   LEU A 396     -14.264 -27.178  29.392  1.00 53.42           C  
ANISOU 2970  C   LEU A 396     7680   6551   6065    652   -354    839       C  
ATOM   2971  O   LEU A 396     -14.759 -26.396  28.573  1.00 51.29           O  
ANISOU 2971  O   LEU A 396     7328   6311   5847    566   -346    787       O  
ATOM   2972  CB  LEU A 396     -14.138 -25.690  31.408  1.00 46.74           C  
ANISOU 2972  CB  LEU A 396     6903   5821   5034    753   -413    842       C  
ATOM   2973  CG  LEU A 396     -13.894 -25.804  32.913  1.00 56.13           C  
ANISOU 2973  CG  LEU A 396     8204   7033   6090    860   -432    893       C  
ATOM   2974  CD1 LEU A 396     -12.408 -25.757  33.230  1.00 58.19           C  
ANISOU 2974  CD1 LEU A 396     8457   7344   6308    954   -561    856       C  
ATOM   2975  CD2 LEU A 396     -14.636 -24.706  33.655  1.00 60.58           C  
ANISOU 2975  CD2 LEU A 396     8789   7650   6579    850   -405    881       C  
ATOM   2976  N   ASN A 397     -14.460 -28.494  29.354  1.00 59.52           N  
ANISOU 2976  N   ASN A 397     8518   7233   6866    659   -295    898       N  
ATOM   2977  CA  ASN A 397     -15.377 -29.081  28.389  1.00 67.38           C  
ANISOU 2977  CA  ASN A 397     9487   8159   7953    552   -215    901       C  
ATOM   2978  C   ASN A 397     -16.798 -28.592  28.646  1.00 69.32           C  
ANISOU 2978  C   ASN A 397     9722   8421   8194    475   -135    926       C  
ATOM   2979  O   ASN A 397     -17.201 -28.375  29.792  1.00 78.17           O  
ANISOU 2979  O   ASN A 397    10906   9561   9234    517   -101    978       O  
ATOM   2980  CB  ASN A 397     -15.321 -30.608  28.456  1.00 72.44           C  
ANISOU 2980  CB  ASN A 397    10219   8685   8619    575   -162    963       C  
ATOM   2981  CG  ASN A 397     -15.979 -31.266  27.260  1.00 74.45           C  
ANISOU 2981  CG  ASN A 397    10439   8867   8980    462   -102    939       C  
ATOM   2982  OD1 ASN A 397     -15.759 -30.861  26.119  1.00 70.83           O  
ANISOU 2982  OD1 ASN A 397     9890   8441   8581    409   -141    862       O  
ATOM   2983  ND2 ASN A 397     -16.798 -32.280  27.515  1.00 79.34           N  
ANISOU 2983  ND2 ASN A 397    11136   9389   9621    420     -6   1005       N  
ATOM   2984  N   LYS A 398     -17.549 -28.395  27.561  1.00 61.53           N  
ANISOU 2984  N   LYS A 398     8653   7435   7291    367   -107    886       N  
ATOM   2985  CA  LYS A 398     -18.934 -27.925  27.536  1.00 56.27           C  
ANISOU 2985  CA  LYS A 398     7943   6792   6644    287    -37    897       C  
ATOM   2986  C   LYS A 398     -19.092 -26.508  28.078  1.00 50.77           C  
ANISOU 2986  C   LYS A 398     7215   6189   5886    318    -65    874       C  
ATOM   2987  O   LYS A 398     -20.226 -26.020  28.164  1.00 51.50           O  
ANISOU 2987  O   LYS A 398     7269   6309   5988    271     -7    884       O  
ATOM   2988  CB  LYS A 398     -19.882 -28.852  28.311  1.00 57.08           C  
ANISOU 2988  CB  LYS A 398     8120   6829   6738    265     75    982       C  
ATOM   2989  CG  LYS A 398     -19.879 -30.296  27.829  1.00 58.29           C  
ANISOU 2989  CG  LYS A 398     8321   6871   6958    222    119   1008       C  
ATOM   2990  N   SER A 399     -18.002 -25.832  28.455  1.00 51.58           N  
ANISOU 2990  N   SER A 399     7330   6339   5930    396   -151    841       N  
ATOM   2991  CA  SER A 399     -18.105 -24.455  28.930  1.00 52.54           C  
ANISOU 2991  CA  SER A 399     7430   6537   5995    420   -180    808       C  
ATOM   2992  C   SER A 399     -18.449 -23.508  27.790  1.00 52.30           C  
ANISOU 2992  C   SER A 399     7297   6544   6032    349   -202    745       C  
ATOM   2993  O   SER A 399     -19.177 -22.529  27.985  1.00 54.68           O  
ANISOU 2993  O   SER A 399     7572   6887   6316    340   -181    734       O  
ATOM   2994  CB  SER A 399     -16.798 -24.031  29.603  1.00 53.83           C  
ANISOU 2994  CB  SER A 399     7630   6738   6083    510   -274    780       C  
ATOM   2995  OG  SER A 399     -16.866 -22.705  30.104  1.00 57.02           O  
ANISOU 2995  OG  SER A 399     8028   7207   6432    529   -302    741       O  
ATOM   2996  N   LEU A 400     -17.924 -23.782  26.594  1.00 52.74           N  
ANISOU 2996  N   LEU A 400     7299   6584   6158    306   -242    704       N  
ATOM   2997  CA  LEU A 400     -18.258 -22.968  25.430  1.00 52.42           C  
ANISOU 2997  CA  LEU A 400     7172   6573   6172    240   -261    652       C  
ATOM   2998  C   LEU A 400     -19.733 -23.105  25.071  1.00 53.03           C  
ANISOU 2998  C   LEU A 400     7209   6646   6295    172   -189    678       C  
ATOM   2999  O   LEU A 400     -20.366 -22.136  24.637  1.00 48.44           O  
ANISOU 2999  O   LEU A 400     6569   6107   5728    146   -192    655       O  
ATOM   3000  CB  LEU A 400     -17.369 -23.366  24.250  1.00 49.75           C  
ANISOU 3000  CB  LEU A 400     6797   6217   5888    212   -309    607       C  
ATOM   3001  CG  LEU A 400     -17.560 -22.666  22.903  1.00 49.84           C  
ANISOU 3001  CG  LEU A 400     6732   6255   5949    145   -331    556       C  
ATOM   3002  CD1 LEU A 400     -16.210 -22.420  22.250  1.00 52.58           C  
ANISOU 3002  CD1 LEU A 400     7057   6615   6306    156   -395    502       C  
ATOM   3003  CD2 LEU A 400     -18.454 -23.479  21.979  1.00 47.12           C  
ANISOU 3003  CD2 LEU A 400     6358   5878   5666     69   -289    563       C  
ATOM   3004  N   ASP A 401     -20.296 -24.302  25.249  1.00 53.32           N  
ANISOU 3004  N   ASP A 401     7273   6630   6356    143   -124    726       N  
ATOM   3005  CA  ASP A 401     -21.705 -24.514  24.939  1.00 54.90           C  
ANISOU 3005  CA  ASP A 401     7422   6831   6608     68    -54    747       C  
ATOM   3006  C   ASP A 401     -22.612 -23.756  25.900  1.00 52.67           C  
ANISOU 3006  C   ASP A 401     7135   6593   6282     96      0    778       C  
ATOM   3007  O   ASP A 401     -23.684 -23.287  25.498  1.00 48.55           O  
ANISOU 3007  O   ASP A 401     6536   6110   5800     52     29    772       O  
ATOM   3008  CB  ASP A 401     -22.028 -26.008  24.973  1.00 65.69           C  
ANISOU 3008  CB  ASP A 401     8827   8118   8014     21      9    788       C  
ATOM   3009  CG  ASP A 401     -20.991 -26.847  24.245  1.00 78.49           C  
ANISOU 3009  CG  ASP A 401    10478   9682   9664     19    -37    760       C  
ATOM   3010  OD1 ASP A 401     -21.381 -27.740  23.463  1.00 83.88           O  
ANISOU 3010  OD1 ASP A 401    11145  10312  10412    -58    -11    750       O  
ATOM   3011  OD2 ASP A 401     -19.782 -26.609  24.452  1.00 81.65           O  
ANISOU 3011  OD2 ASP A 401    10913  10090  10022     93    -98    742       O  
ATOM   3012  N   GLU A 402     -22.205 -23.628  27.165  1.00 51.56           N  
ANISOU 3012  N   GLU A 402     7078   6454   6058    176     13    810       N  
ATOM   3013  CA  GLU A 402     -23.021 -22.909  28.137  1.00 48.82           C  
ANISOU 3013  CA  GLU A 402     6741   6149   5659    212     72    837       C  
ATOM   3014  C   GLU A 402     -23.008 -21.408  27.880  1.00 44.15           C  
ANISOU 3014  C   GLU A 402     6103   5619   5054    238     21    781       C  
ATOM   3015  O   GLU A 402     -24.015 -20.732  28.121  1.00 39.89           O  
ANISOU 3015  O   GLU A 402     5525   5118   4515    243     73    788       O  
ATOM   3016  CB  GLU A 402     -22.537 -23.213  29.555  1.00 55.19           C  
ANISOU 3016  CB  GLU A 402     7665   6940   6364    294     96    883       C  
ATOM   3017  CG  GLU A 402     -23.453 -22.700  30.656  1.00 60.04           C  
ANISOU 3017  CG  GLU A 402     8307   7589   6915    330    182    919       C  
ATOM   3018  CD  GLU A 402     -24.645 -23.606  30.901  1.00 65.55           C  
ANISOU 3018  CD  GLU A 402     8994   8260   7651    273    308    987       C  
ATOM   3019  OE1 GLU A 402     -25.457 -23.288  31.794  1.00 66.31           O  
ANISOU 3019  OE1 GLU A 402     9109   8386   7700    299    397   1021       O  
ATOM   3020  OE2 GLU A 402     -24.772 -24.634  30.203  1.00 68.37           O  
ANISOU 3020  OE2 GLU A 402     9326   8564   8086    199    323   1002       O  
ATOM   3021  N   MET A 403     -21.886 -20.870  27.395  1.00 45.76           N  
ANISOU 3021  N   MET A 403     6309   5828   5250    257    -74    728       N  
ATOM   3022  CA  MET A 403     -21.826 -19.447  27.078  1.00 46.54           C  
ANISOU 3022  CA  MET A 403     6373   5968   5342    273   -120    676       C  
ATOM   3023  C   MET A 403     -22.629 -19.126  25.825  1.00 48.42           C  
ANISOU 3023  C   MET A 403     6514   6222   5660    211   -119    659       C  
ATOM   3024  O   MET A 403     -23.310 -18.096  25.763  1.00 47.83           O  
ANISOU 3024  O   MET A 403     6406   6182   5587    227   -108    647       O  
ATOM   3025  CB  MET A 403     -20.373 -19.004  26.906  1.00 48.65           C  
ANISOU 3025  CB  MET A 403     6666   6234   5584    297   -215    624       C  
ATOM   3026  CG  MET A 403     -19.586 -18.935  28.200  1.00 50.48           C  
ANISOU 3026  CG  MET A 403     6986   6471   5724    372   -238    625       C  
ATOM   3027  SD  MET A 403     -17.974 -18.162  27.976  1.00 57.50           S  
ANISOU 3027  SD  MET A 403     7876   7376   6595    388   -353    549       S  
ATOM   3028  CE  MET A 403     -17.330 -18.225  29.646  1.00 61.00           C  
ANISOU 3028  CE  MET A 403     8421   7836   6919    479   -378    557       C  
ATOM   3029  N   ASP A 404     -22.556 -19.994  24.813  1.00 51.73           N  
ANISOU 3029  N   ASP A 404     6894   6619   6142    146   -134    656       N  
ATOM   3030  CA  ASP A 404     -23.337 -19.783  23.599  1.00 50.40           C  
ANISOU 3030  CA  ASP A 404     6637   6473   6040     87   -141    639       C  
ATOM   3031  C   ASP A 404     -24.832 -19.878  23.872  1.00 47.25           C  
ANISOU 3031  C   ASP A 404     6181   6103   5670     68    -66    675       C  
ATOM   3032  O   ASP A 404     -25.633 -19.262  23.160  1.00 48.70           O  
ANISOU 3032  O   ASP A 404     6286   6328   5890     51    -75    663       O  
ATOM   3033  CB  ASP A 404     -22.923 -20.793  22.529  1.00 51.97           C  
ANISOU 3033  CB  ASP A 404     6817   6639   6289     21   -170    622       C  
ATOM   3034  CG  ASP A 404     -23.725 -20.651  21.251  1.00 55.26           C  
ANISOU 3034  CG  ASP A 404     7149   7086   6763    -42   -188    601       C  
ATOM   3035  OD1 ASP A 404     -23.598 -19.603  20.585  1.00 58.45           O  
ANISOU 3035  OD1 ASP A 404     7526   7520   7160    -29   -236    572       O  
ATOM   3036  OD2 ASP A 404     -24.481 -21.587  20.913  1.00 58.93           O  
ANISOU 3036  OD2 ASP A 404     7574   7539   7276   -107   -155    613       O  
ATOM   3037  N   PHE A 405     -25.226 -20.634  24.897  1.00 46.18           N  
ANISOU 3037  N   PHE A 405     6081   5948   5516     74     11    723       N  
ATOM   3038  CA  PHE A 405     -26.641 -20.762  25.226  1.00 50.31           C  
ANISOU 3038  CA  PHE A 405     6542   6503   6072     50     98    758       C  
ATOM   3039  C   PHE A 405     -27.161 -19.521  25.941  1.00 53.49           C  
ANISOU 3039  C   PHE A 405     6938   6954   6431    126    127    760       C  
ATOM   3040  O   PHE A 405     -28.144 -18.912  25.506  1.00 54.95           O  
ANISOU 3040  O   PHE A 405     7032   7190   6657    122    140    753       O  
ATOM   3041  CB  PHE A 405     -26.868 -22.007  26.085  1.00 51.02           C  
ANISOU 3041  CB  PHE A 405     6683   6547   6156     25    185    814       C  
ATOM   3042  CG  PHE A 405     -28.227 -22.062  26.724  1.00 51.89           C  
ANISOU 3042  CG  PHE A 405     6741   6691   6285     11    294    856       C  
ATOM   3043  CD1 PHE A 405     -29.351 -22.347  25.967  1.00 53.37           C  
ANISOU 3043  CD1 PHE A 405     6806   6910   6563    -72    321    852       C  
ATOM   3044  CD2 PHE A 405     -28.379 -21.828  28.081  1.00 53.23           C  
ANISOU 3044  CD2 PHE A 405     6979   6867   6378     79    370    897       C  
ATOM   3045  CE1 PHE A 405     -30.603 -22.399  26.552  1.00 56.51           C  
ANISOU 3045  CE1 PHE A 405     7137   7347   6986    -88    427    889       C  
ATOM   3046  CE2 PHE A 405     -29.628 -21.878  28.672  1.00 54.86           C  
ANISOU 3046  CE2 PHE A 405     7133   7109   6602     66    485    936       C  
ATOM   3047  CZ  PHE A 405     -30.741 -22.164  27.906  1.00 56.05           C  
ANISOU 3047  CZ  PHE A 405     7149   7293   6856    -19    515    932       C  
ATOM   3048  N   TRP A 406     -26.509 -19.128  27.037  1.00 51.25           N  
ANISOU 3048  N   TRP A 406     6753   6658   6060    201    134    765       N  
ATOM   3049  CA  TRP A 406     -27.039 -18.049  27.865  1.00 49.28           C  
ANISOU 3049  CA  TRP A 406     6516   6447   5761    276    177    764       C  
ATOM   3050  C   TRP A 406     -26.918 -16.696  27.175  1.00 48.28           C  
ANISOU 3050  C   TRP A 406     6357   6342   5644    308    109    713       C  
ATOM   3051  O   TRP A 406     -27.839 -15.874  27.245  1.00 42.96           O  
ANISOU 3051  O   TRP A 406     5635   5707   4981    346    146    712       O  
ATOM   3052  CB  TRP A 406     -26.326 -18.030  29.217  1.00 46.86           C  
ANISOU 3052  CB  TRP A 406     6335   6121   5348    345    194    776       C  
ATOM   3053  CG  TRP A 406     -26.760 -19.139  30.125  1.00 45.48           C  
ANISOU 3053  CG  TRP A 406     6202   5929   5148    335    292    842       C  
ATOM   3054  CD1 TRP A 406     -26.017 -20.210  30.524  1.00 46.58           C  
ANISOU 3054  CD1 TRP A 406     6424   6021   5255    327    288    875       C  
ATOM   3055  CD2 TRP A 406     -28.045 -19.290  30.742  1.00 44.61           C  
ANISOU 3055  CD2 TRP A 406     6057   5848   5045    333    417    888       C  
ATOM   3056  NE1 TRP A 406     -26.757 -21.018  31.354  1.00 50.24           N  
ANISOU 3056  NE1 TRP A 406     6918   6473   5700    318    403    943       N  
ATOM   3057  CE2 TRP A 406     -28.006 -20.474  31.503  1.00 49.01           C  
ANISOU 3057  CE2 TRP A 406     6686   6366   5568    316    488    950       C  
ATOM   3058  CE3 TRP A 406     -29.224 -18.538  30.725  1.00 41.60           C  
ANISOU 3058  CE3 TRP A 406     5588   5523   4696    349    479    883       C  
ATOM   3059  CZ2 TRP A 406     -29.099 -20.924  32.241  1.00 48.67           C  
ANISOU 3059  CZ2 TRP A 406     6632   6336   5524    302    627   1009       C  
ATOM   3060  CZ3 TRP A 406     -30.308 -18.986  31.457  1.00 42.86           C  
ANISOU 3060  CZ3 TRP A 406     5722   5705   4858    341    614    936       C  
ATOM   3061  CH2 TRP A 406     -30.238 -20.167  32.205  1.00 45.93           C  
ANISOU 3061  CH2 TRP A 406     6186   6052   5214    311    690    999       C  
ATOM   3062  N   ALA A 407     -25.797 -16.443  26.503  1.00 50.12           N  
ANISOU 3062  N   ALA A 407     6618   6550   5874    297     14    673       N  
ATOM   3063  CA  ALA A 407     -25.572 -15.128  25.918  1.00 52.10           C  
ANISOU 3063  CA  ALA A 407     6862   6808   6127    326    -44    629       C  
ATOM   3064  C   ALA A 407     -25.948 -15.068  24.443  1.00 56.45           C  
ANISOU 3064  C   ALA A 407     7323   7375   6753    274    -87    621       C  
ATOM   3065  O   ALA A 407     -26.529 -14.074  23.994  1.00 63.34           O  
ANISOU 3065  O   ALA A 407     8156   8268   7641    305    -96    611       O  
ATOM   3066  CB  ALA A 407     -24.108 -14.716  26.097  1.00 50.70           C  
ANISOU 3066  CB  ALA A 407     6768   6598   5899    342   -117    587       C  
ATOM   3067  N   GLY A 408     -25.631 -16.110  23.681  1.00 52.29           N  
ANISOU 3067  N   GLY A 408     6769   6835   6265    202   -114    623       N  
ATOM   3068  CA  GLY A 408     -25.815 -16.073  22.244  1.00 54.45           C  
ANISOU 3068  CA  GLY A 408     6975   7123   6592    152   -166    606       C  
ATOM   3069  C   GLY A 408     -27.135 -16.632  21.757  1.00 56.47           C  
ANISOU 3069  C   GLY A 408     7127   7420   6909    108   -134    629       C  
ATOM   3070  O   GLY A 408     -27.528 -16.389  20.612  1.00 57.00           O  
ANISOU 3070  O   GLY A 408     7130   7516   7011     82   -180    615       O  
ATOM   3071  N   THR A 409     -27.835 -17.379  22.610  1.00 55.19           N  
ANISOU 3071  N   THR A 409     6947   7264   6757     96    -55    663       N  
ATOM   3072  CA  THR A 409     -29.074 -18.041  22.224  1.00 55.56           C  
ANISOU 3072  CA  THR A 409     6887   7352   6873     37    -17    681       C  
ATOM   3073  C   THR A 409     -30.290 -17.444  22.922  1.00 58.50           C  
ANISOU 3073  C   THR A 409     7194   7779   7254     88     55    706       C  
ATOM   3074  O   THR A 409     -31.183 -16.912  22.257  1.00 60.41           O  
ANISOU 3074  O   THR A 409     7336   8080   7538     96     36    700       O  
ATOM   3075  CB  THR A 409     -28.968 -19.548  22.504  1.00 55.53           C  
ANISOU 3075  CB  THR A 409     6904   7304   6892    -40     28    700       C  
ATOM   3076  OG1 THR A 409     -28.032 -20.137  21.594  1.00 65.30           O  
ANISOU 3076  OG1 THR A 409     8175   8498   8137    -90    -41    669       O  
ATOM   3077  CG2 THR A 409     -30.314 -20.222  22.334  1.00 48.02           C  
ANISOU 3077  CG2 THR A 409     5841   6391   6013   -111     84    718       C  
ATOM   3078  N   ILE A 410     -30.352 -17.514  24.250  1.00 56.95           N  
ANISOU 3078  N   ILE A 410     7054   7569   7014    130    140    735       N  
ATOM   3079  CA  ILE A 410     -31.494 -16.957  24.968  1.00 56.79           C  
ANISOU 3079  CA  ILE A 410     6976   7604   7000    185    224    758       C  
ATOM   3080  C   ILE A 410     -31.292 -15.477  25.293  1.00 54.07           C  
ANISOU 3080  C   ILE A 410     6679   7266   6601    296    205    737       C  
ATOM   3081  O   ILE A 410     -32.269 -14.727  25.393  1.00 52.01           O  
ANISOU 3081  O   ILE A 410     6346   7056   6360    354    242    742       O  
ATOM   3082  CB  ILE A 410     -31.777 -17.780  26.241  1.00 57.87           C  
ANISOU 3082  CB  ILE A 410     7153   7725   7112    174    341    803       C  
ATOM   3083  CG1 ILE A 410     -32.991 -17.233  26.997  1.00 60.32           C  
ANISOU 3083  CG1 ILE A 410     7396   8097   7427    231    444    825       C  
ATOM   3084  CG2 ILE A 410     -30.572 -17.789  27.158  1.00 61.72           C  
ANISOU 3084  CG2 ILE A 410     7797   8153   7503    222    335    805       C  
ATOM   3085  CD1 ILE A 410     -34.266 -17.214  26.187  1.00 63.65           C  
ANISOU 3085  CD1 ILE A 410     7642   8594   7948    193    451    823       C  
ATOM   3086  N   GLY A 411     -30.042 -15.031  25.430  1.00 50.70           N  
ANISOU 3086  N   GLY A 411     6367   6785   6110    326    146    711       N  
ATOM   3087  CA  GLY A 411     -29.799 -13.650  25.819  1.00 46.46           C  
ANISOU 3087  CA  GLY A 411     5891   6240   5521    421    133    685       C  
ATOM   3088  C   GLY A 411     -30.231 -12.653  24.760  1.00 42.76           C  
ANISOU 3088  C   GLY A 411     5359   5794   5095    450     78    668       C  
ATOM   3089  O   GLY A 411     -30.913 -11.669  25.060  1.00 43.85           O  
ANISOU 3089  O   GLY A 411     5481   5953   5227    534    112    667       O  
ATOM   3090  N   VAL A 412     -29.843 -12.894  23.505  1.00 42.73           N  
ANISOU 3090  N   VAL A 412     5323   5784   5127    389     -5    656       N  
ATOM   3091  CA  VAL A 412     -30.131 -11.927  22.449  1.00 47.02           C  
ANISOU 3091  CA  VAL A 412     5826   6343   5694    422    -66    645       C  
ATOM   3092  C   VAL A 412     -31.624 -11.872  22.144  1.00 46.63           C  
ANISOU 3092  C   VAL A 412     5641   6371   5704    446    -36    669       C  
ATOM   3093  O   VAL A 412     -32.141 -10.824  21.738  1.00 45.73           O  
ANISOU 3093  O   VAL A 412     5499   6276   5598    522    -58    670       O  
ATOM   3094  CB  VAL A 412     -29.305 -12.251  21.190  1.00 44.99           C  
ANISOU 3094  CB  VAL A 412     5580   6066   5450    350   -157    628       C  
ATOM   3095  CG1 VAL A 412     -27.821 -12.112  21.488  1.00 43.63           C  
ANISOU 3095  CG1 VAL A 412     5527   5826   5226    338   -186    600       C  
ATOM   3096  CG2 VAL A 412     -29.623 -13.649  20.684  1.00 40.62           C  
ANISOU 3096  CG2 VAL A 412     4950   5540   4943    254   -159    637       C  
ATOM   3097  N   VAL A 413     -32.340 -12.983  22.332  1.00 47.39           N  
ANISOU 3097  N   VAL A 413     5650   6512   5845    384     13    689       N  
ATOM   3098  CA  VAL A 413     -33.788 -12.964  22.150  1.00 49.49           C  
ANISOU 3098  CA  VAL A 413     5768   6862   6174    401     48    708       C  
ATOM   3099  C   VAL A 413     -34.450 -12.160  23.261  1.00 51.98           C  
ANISOU 3099  C   VAL A 413     6083   7196   6470    509    140    721       C  
ATOM   3100  O   VAL A 413     -35.353 -11.352  23.011  1.00 53.55           O  
ANISOU 3100  O   VAL A 413     6199   7448   6698    588    143    726       O  
ATOM   3101  CB  VAL A 413     -34.336 -14.400  22.081  1.00 53.55           C  
ANISOU 3101  CB  VAL A 413     6189   7410   6747    288     84    721       C  
ATOM   3102  CG1 VAL A 413     -35.857 -14.391  22.075  1.00 57.17           C  
ANISOU 3102  CG1 VAL A 413     6481   7965   7276    301    133    737       C  
ATOM   3103  CG2 VAL A 413     -33.797 -15.113  20.850  1.00 54.90           C  
ANISOU 3103  CG2 VAL A 413     6356   7565   6939    191    -12    698       C  
ATOM   3104  N   PHE A 414     -34.006 -12.362  24.505  1.00 51.82           N  
ANISOU 3104  N   PHE A 414     6161   7135   6394    521    217    726       N  
ATOM   3105  CA  PHE A 414     -34.526 -11.573  25.617  1.00 56.21           C  
ANISOU 3105  CA  PHE A 414     6740   7702   6914    628    310    731       C  
ATOM   3106  C   PHE A 414     -34.137 -10.106  25.480  1.00 51.65           C  
ANISOU 3106  C   PHE A 414     6243   7084   6296    732    262    702       C  
ATOM   3107  O   PHE A 414     -34.956  -9.214  25.734  1.00 50.41           O  
ANISOU 3107  O   PHE A 414     6049   6956   6148    835    307    704       O  
ATOM   3108  CB  PHE A 414     -34.019 -12.147  26.941  1.00 64.22           C  
ANISOU 3108  CB  PHE A 414     7862   8679   7860    616    391    741       C  
ATOM   3109  CG  PHE A 414     -34.157 -11.207  28.106  1.00 73.10           C  
ANISOU 3109  CG  PHE A 414     9067   9794   8914    730    468    730       C  
ATOM   3110  CD1 PHE A 414     -35.388 -11.003  28.708  1.00 77.04           C  
ANISOU 3110  CD1 PHE A 414     9482  10355   9434    791    580    750       C  
ATOM   3111  CD2 PHE A 414     -33.053 -10.533  28.604  1.00 74.36           C  
ANISOU 3111  CD2 PHE A 414     9383   9883   8986    773    430    694       C  
ATOM   3112  CE1 PHE A 414     -35.516 -10.140  29.781  1.00 78.54           C  
ANISOU 3112  CE1 PHE A 414     9754  10534   9553    901    657    734       C  
ATOM   3113  CE2 PHE A 414     -33.175  -9.669  29.676  1.00 75.63           C  
ANISOU 3113  CE2 PHE A 414     9628  10032   9077    875    497    674       C  
ATOM   3114  CZ  PHE A 414     -34.408  -9.472  30.266  1.00 77.31           C  
ANISOU 3114  CZ  PHE A 414     9767  10302   9304    943    613    694       C  
ATOM   3115  N   PHE A 415     -32.894  -9.837  25.074  1.00 49.12           N  
ANISOU 3115  N   PHE A 415     6033   6693   5936    707    177    676       N  
ATOM   3116  CA  PHE A 415     -32.454  -8.457  24.906  1.00 50.78           C  
ANISOU 3116  CA  PHE A 415     6332   6851   6113    790    134    648       C  
ATOM   3117  C   PHE A 415     -33.100  -7.802  23.692  1.00 51.92           C  
ANISOU 3117  C   PHE A 415     6392   7024   6311    829     76    660       C  
ATOM   3118  O   PHE A 415     -33.317  -6.585  23.689  1.00 54.34           O  
ANISOU 3118  O   PHE A 415     6737   7303   6607    930     76    652       O  
ATOM   3119  CB  PHE A 415     -30.931  -8.400  24.794  1.00 52.37           C  
ANISOU 3119  CB  PHE A 415     6661   6974   6264    738     64    616       C  
ATOM   3120  CG  PHE A 415     -30.363  -7.021  24.958  1.00 56.57           C  
ANISOU 3120  CG  PHE A 415     7306   7435   6752    809     42    580       C  
ATOM   3121  CD1 PHE A 415     -30.438  -6.369  26.178  1.00 57.35           C  
ANISOU 3121  CD1 PHE A 415     7487   7508   6795    888    108    556       C  
ATOM   3122  CD2 PHE A 415     -29.752  -6.376  23.895  1.00 58.41           C  
ANISOU 3122  CD2 PHE A 415     7574   7623   6998    793    -40    569       C  
ATOM   3123  CE1 PHE A 415     -29.916  -5.100  26.336  1.00 56.98           C  
ANISOU 3123  CE1 PHE A 415     7553   7386   6712    945     88    515       C  
ATOM   3124  CE2 PHE A 415     -29.227  -5.105  24.047  1.00 59.92           C  
ANISOU 3124  CE2 PHE A 415     7876   7736   7155    848    -53    535       C  
ATOM   3125  CZ  PHE A 415     -29.310  -4.467  25.269  1.00 59.57           C  
ANISOU 3125  CZ  PHE A 415     7911   7661   7061    921      9    505       C  
ATOM   3126  N   GLY A 416     -33.409  -8.584  22.655  1.00 49.18           N  
ANISOU 3126  N   GLY A 416     5939   6729   6020    753     22    678       N  
ATOM   3127  CA  GLY A 416     -34.085  -8.023  21.497  1.00 47.92           C  
ANISOU 3127  CA  GLY A 416     5696   6611   5902    795    -41    692       C  
ATOM   3128  C   GLY A 416     -35.494  -7.562  21.815  1.00 50.42           C  
ANISOU 3128  C   GLY A 416     5896   7001   6260    897     18    712       C  
ATOM   3129  O   GLY A 416     -35.946  -6.526  21.319  1.00 52.90           O  
ANISOU 3129  O   GLY A 416     6197   7320   6583    998    -13    721       O  
ATOM   3130  N   LEU A 417     -36.210  -8.324  22.645  1.00 47.04           N  
ANISOU 3130  N   LEU A 417     5383   6630   5859    874    110    722       N  
ATOM   3131  CA  LEU A 417     -37.534  -7.897  23.078  1.00 52.14           C  
ANISOU 3131  CA  LEU A 417     5911   7352   6547    973    185    738       C  
ATOM   3132  C   LEU A 417     -37.451  -6.720  24.041  1.00 57.62           C  
ANISOU 3132  C   LEU A 417     6716   7989   7187   1105    253    724       C  
ATOM   3133  O   LEU A 417     -38.374  -5.898  24.096  1.00 59.88           O  
ANISOU 3133  O   LEU A 417     6937   8315   7501   1228    286    732       O  
ATOM   3134  CB  LEU A 417     -38.276  -9.068  23.725  1.00 52.20           C  
ANISOU 3134  CB  LEU A 417     5803   7433   6599    899    279    753       C  
ATOM   3135  CG  LEU A 417     -39.701  -8.809  24.218  1.00 49.01           C  
ANISOU 3135  CG  LEU A 417     5249   7124   6250    984    374    769       C  
ATOM   3136  CD1 LEU A 417     -40.561  -8.255  23.096  1.00 51.56           C  
ANISOU 3136  CD1 LEU A 417     5429   7525   6638   1048    292    776       C  
ATOM   3137  CD2 LEU A 417     -40.312 -10.078  24.789  1.00 48.61           C  
ANISOU 3137  CD2 LEU A 417     5091   7134   6245    880    471    786       C  
ATOM   3138  N   THR A 418     -36.356  -6.617  24.797  1.00 59.75           N  
ANISOU 3138  N   THR A 418     7152   8168   7380   1086    271    699       N  
ATOM   3139  CA  THR A 418     -36.207  -5.524  25.752  1.00 57.81           C  
ANISOU 3139  CA  THR A 418     7028   7862   7076   1201    333    674       C  
ATOM   3140  C   THR A 418     -36.030  -4.188  25.038  1.00 56.76           C  
ANISOU 3140  C   THR A 418     6959   7669   6940   1293    265    663       C  
ATOM   3141  O   THR A 418     -36.681  -3.197  25.386  1.00 59.68           O  
ANISOU 3141  O   THR A 418     7334   8030   7310   1427    316    659       O  
ATOM   3142  CB  THR A 418     -35.025  -5.797  26.683  1.00 49.92           C  
ANISOU 3142  CB  THR A 418     6186   6788   5992   1147    351    644       C  
ATOM   3143  OG1 THR A 418     -35.234  -7.037  27.371  1.00 52.01           O  
ANISOU 3143  OG1 THR A 418     6404   7104   6254   1072    421    665       O  
ATOM   3144  CG2 THR A 418     -34.881  -4.678  27.704  1.00 43.46           C  
ANISOU 3144  CG2 THR A 418     5499   5909   5105   1259    411    606       C  
ATOM   3145  N   GLU A 419     -35.146  -4.141  24.037  1.00 55.97           N  
ANISOU 3145  N   GLU A 419     6912   7517   6835   1227    157    661       N  
ATOM   3146  CA  GLU A 419     -34.942  -2.899  23.299  1.00 60.63           C  
ANISOU 3146  CA  GLU A 419     7576   8040   7421   1305     97    660       C  
ATOM   3147  C   GLU A 419     -36.162  -2.537  22.462  1.00 62.40           C  
ANISOU 3147  C   GLU A 419     7663   8339   7706   1396     73    699       C  
ATOM   3148  O   GLU A 419     -36.382  -1.357  22.170  1.00 63.89           O  
ANISOU 3148  O   GLU A 419     7904   8478   7893   1514     60    706       O  
ATOM   3149  CB  GLU A 419     -33.700  -3.010  22.414  1.00 63.18           C  
ANISOU 3149  CB  GLU A 419     7984   8299   7722   1202      0    652       C  
ATOM   3150  CG  GLU A 419     -33.726  -4.182  21.450  1.00 69.44           C  
ANISOU 3150  CG  GLU A 419     8666   9165   8552   1091    -64    675       C  
ATOM   3151  CD  GLU A 419     -32.358  -4.494  20.878  1.00 74.81           C  
ANISOU 3151  CD  GLU A 419     9439   9783   9202    979   -134    658       C  
ATOM   3152  OE1 GLU A 419     -31.355  -3.975  21.412  1.00 74.69           O  
ANISOU 3152  OE1 GLU A 419     9560   9679   9141    972   -125    624       O  
ATOM   3153  OE2 GLU A 419     -32.286  -5.260  19.895  1.00 77.00           O  
ANISOU 3153  OE2 GLU A 419     9650  10104   9502    899   -196    672       O  
ATOM   3154  N   LEU A 420     -36.962  -3.530  22.072  1.00 63.66           N  
ANISOU 3154  N   LEU A 420     7650   8615   7922   1345     65    725       N  
ATOM   3155  CA  LEU A 420     -38.205  -3.249  21.362  1.00 61.77           C  
ANISOU 3155  CA  LEU A 420     7257   8468   7745   1434     38    758       C  
ATOM   3156  C   LEU A 420     -39.192  -2.516  22.260  1.00 58.72           C  
ANISOU 3156  C   LEU A 420     6828   8107   7375   1586    141    758       C  
ATOM   3157  O   LEU A 420     -39.795  -1.515  21.854  1.00 62.10           O  
ANISOU 3157  O   LEU A 420     7238   8536   7822   1726    122    776       O  
ATOM   3158  CB  LEU A 420     -38.816  -4.552  20.850  1.00 66.27           C  
ANISOU 3158  CB  LEU A 420     7646   9159   8374   1326     10    772       C  
ATOM   3159  CG  LEU A 420     -38.867  -4.769  19.341  1.00 66.79           C  
ANISOU 3159  CG  LEU A 420     7647   9270   8460   1282   -121    790       C  
ATOM   3160  CD1 LEU A 420     -39.460  -6.131  19.052  1.00 69.69           C  
ANISOU 3160  CD1 LEU A 420     7844   9748   8886   1161   -133    788       C  
ATOM   3161  CD2 LEU A 420     -39.685  -3.678  18.680  1.00 67.73           C  
ANISOU 3161  CD2 LEU A 420     7714   9422   8598   1438   -169    819       C  
ATOM   3162  N   ILE A 421     -39.365  -3.002  23.490  1.00 55.97           N  
ANISOU 3162  N   ILE A 421     6471   7778   7017   1566    256    740       N  
ATOM   3163  CA  ILE A 421     -40.329  -2.402  24.406  1.00 55.29           C  
ANISOU 3163  CA  ILE A 421     6338   7725   6944   1707    371    737       C  
ATOM   3164  C   ILE A 421     -39.872  -1.013  24.837  1.00 54.24           C  
ANISOU 3164  C   ILE A 421     6388   7468   6753   1834    392    710       C  
ATOM   3165  O   ILE A 421     -40.669  -0.070  24.886  1.00 52.87           O  
ANISOU 3165  O   ILE A 421     6185   7302   6603   1994    428    717       O  
ATOM   3166  CB  ILE A 421     -40.552  -3.331  25.614  1.00 54.94           C  
ANISOU 3166  CB  ILE A 421     6256   7728   6890   1642    495    728       C  
ATOM   3167  CG1 ILE A 421     -41.328  -4.580  25.188  1.00 58.55           C  
ANISOU 3167  CG1 ILE A 421     6505   8313   7427   1538    493    756       C  
ATOM   3168  CG2 ILE A 421     -41.280  -2.600  26.732  1.00 53.66           C  
ANISOU 3168  CG2 ILE A 421     6101   7574   6714   1789    631    714       C  
ATOM   3169  CD1 ILE A 421     -41.256  -5.714  26.187  1.00 59.06           C  
ANISOU 3169  CD1 ILE A 421     6564   8400   7476   1429    597    756       C  
ATOM   3170  N   ILE A 422     -38.584  -0.861  25.149  1.00 55.24           N  
ANISOU 3170  N   ILE A 422     6703   7478   6807   1767    371    677       N  
ATOM   3171  CA  ILE A 422     -38.080   0.431  25.608  1.00 57.01           C  
ANISOU 3171  CA  ILE A 422     7111   7574   6976   1867    392    640       C  
ATOM   3172  C   ILE A 422     -38.193   1.474  24.502  1.00 61.23           C  
ANISOU 3172  C   ILE A 422     7673   8056   7538   1958    311    665       C  
ATOM   3173  O   ILE A 422     -38.539   2.634  24.756  1.00 66.34           O  
ANISOU 3173  O   ILE A 422     8391   8637   8178   2107    352    655       O  
ATOM   3174  CB  ILE A 422     -36.631   0.287  26.113  1.00 48.76           C  
ANISOU 3174  CB  ILE A 422     6244   6429   5853   1755    372    594       C  
ATOM   3175  CG1 ILE A 422     -36.591  -0.592  27.364  1.00 45.62           C  
ANISOU 3175  CG1 ILE A 422     5844   6076   5413   1700    463    574       C  
ATOM   3176  CG2 ILE A 422     -36.020   1.651  26.401  1.00 44.20           C  
ANISOU 3176  CG2 ILE A 422     5859   5708   5227   1835    374    550       C  
ATOM   3177  CD1 ILE A 422     -35.219  -0.701  27.991  1.00 47.99           C  
ANISOU 3177  CD1 ILE A 422     6313   6289   5630   1611    442    525       C  
ATOM   3178  N   PHE A 423     -37.927   1.075  23.258  1.00 60.71           N  
ANISOU 3178  N   PHE A 423     7556   8014   7497   1878    200    700       N  
ATOM   3179  CA  PHE A 423     -37.927   2.029  22.155  1.00 60.19           C  
ANISOU 3179  CA  PHE A 423     7537   7892   7442   1957    118    732       C  
ATOM   3180  C   PHE A 423     -39.337   2.320  21.650  1.00 62.82           C  
ANISOU 3180  C   PHE A 423     7706   8325   7837   2101    112    777       C  
ATOM   3181  O   PHE A 423     -39.666   3.477  21.363  1.00 62.83           O  
ANISOU 3181  O   PHE A 423     7767   8265   7842   2251    105    796       O  
ATOM   3182  CB  PHE A 423     -37.050   1.505  21.016  1.00 60.55           C  
ANISOU 3182  CB  PHE A 423     7605   7925   7477   1818      5    750       C  
ATOM   3183  CG  PHE A 423     -36.634   2.559  20.029  1.00 59.99           C  
ANISOU 3183  CG  PHE A 423     7652   7753   7387   1872    -66    777       C  
ATOM   3184  CD1 PHE A 423     -36.001   3.715  20.454  1.00 60.71           C  
ANISOU 3184  CD1 PHE A 423     7934   7691   7441   1928    -31    750       C  
ATOM   3185  CD2 PHE A 423     -36.865   2.387  18.674  1.00 62.22           C  
ANISOU 3185  CD2 PHE A 423     7865   8091   7687   1862   -166    828       C  
ATOM   3186  CE1 PHE A 423     -35.613   4.683  19.547  1.00 62.49           C  
ANISOU 3186  CE1 PHE A 423     8279   7812   7652   1970    -86    780       C  
ATOM   3187  CE2 PHE A 423     -36.478   3.351  17.761  1.00 62.29           C  
ANISOU 3187  CE2 PHE A 423     7994   8003   7670   1913   -225    862       C  
ATOM   3188  CZ  PHE A 423     -35.852   4.501  18.198  1.00 62.23           C  
ANISOU 3188  CZ  PHE A 423     8178   7835   7631   1966   -180    842       C  
ATOM   3189  N   PHE A 424     -40.185   1.297  21.541  1.00 64.99           N  
ANISOU 3189  N   PHE A 424     7774   8754   8165   2059    114    795       N  
ATOM   3190  CA  PHE A 424     -41.476   1.446  20.882  1.00 69.51           C  
ANISOU 3190  CA  PHE A 424     8162   9444   8804   2174     81    837       C  
ATOM   3191  C   PHE A 424     -42.662   1.487  21.840  1.00 76.11           C  
ANISOU 3191  C   PHE A 424     8860  10369   9687   2286    200    829       C  
ATOM   3192  O   PHE A 424     -43.756   1.878  21.420  1.00 86.30           O  
ANISOU 3192  O   PHE A 424    10007  11747  11034   2422    184    860       O  
ATOM   3193  CB  PHE A 424     -41.687   0.313  19.870  1.00 70.29           C  
ANISOU 3193  CB  PHE A 424     8102   9666   8940   2047    -19    860       C  
ATOM   3194  CG  PHE A 424     -41.596   0.758  18.439  1.00 73.30           C  
ANISOU 3194  CG  PHE A 424     8501  10039   9311   2081   -155    901       C  
ATOM   3195  CD1 PHE A 424     -42.741   0.928  17.678  1.00 76.10           C  
ANISOU 3195  CD1 PHE A 424     8686  10513   9715   2189   -219    939       C  
ATOM   3196  CD2 PHE A 424     -40.366   1.011  17.854  1.00 73.71           C  
ANISOU 3196  CD2 PHE A 424     8736   9970   9299   2006   -218    902       C  
ATOM   3197  CE1 PHE A 424     -42.662   1.338  16.361  1.00 76.40           C  
ANISOU 3197  CE1 PHE A 424     8753  10548   9730   2228   -348    982       C  
ATOM   3198  CE2 PHE A 424     -40.280   1.422  16.536  1.00 73.44           C  
ANISOU 3198  CE2 PHE A 424     8730   9928   9245   2038   -334    946       C  
ATOM   3199  CZ  PHE A 424     -41.430   1.586  15.790  1.00 75.92           C  
ANISOU 3199  CZ  PHE A 424     8889  10359   9598   2152   -401    987       C  
ATOM   3200  N   TRP A 425     -42.487   1.094  23.099  1.00 70.91           N  
ANISOU 3200  N   TRP A 425     8238   9699   9006   2240    319    791       N  
ATOM   3201  CA  TRP A 425     -43.572   1.131  24.073  1.00 69.74           C  
ANISOU 3201  CA  TRP A 425     7971   9633   8895   2343    452    782       C  
ATOM   3202  C   TRP A 425     -43.366   2.166  25.167  1.00 69.91           C  
ANISOU 3202  C   TRP A 425     8163   9539   8859   2469    561    743       C  
ATOM   3203  O   TRP A 425     -44.300   2.900  25.496  1.00 72.71           O  
ANISOU 3203  O   TRP A 425     8459   9922   9245   2644    633    745       O  
ATOM   3204  CB  TRP A 425     -43.762  -0.248  24.717  1.00 71.40           C  
ANISOU 3204  CB  TRP A 425     8064   9942   9124   2195    524    774       C  
ATOM   3205  CG  TRP A 425     -44.354  -1.281  23.802  1.00 76.64           C  
ANISOU 3205  CG  TRP A 425     8512  10744   9865   2092    448    804       C  
ATOM   3206  CD1 TRP A 425     -44.528  -1.182  22.452  1.00 75.97           C  
ANISOU 3206  CD1 TRP A 425     8351  10699   9814   2099    306    832       C  
ATOM   3207  CD2 TRP A 425     -44.851  -2.572  24.176  1.00 83.47           C  
ANISOU 3207  CD2 TRP A 425     9217  11720  10777   1964    510    805       C  
ATOM   3208  NE1 TRP A 425     -45.101  -2.331  21.963  1.00 78.19           N  
ANISOU 3208  NE1 TRP A 425     8432  11114  10162   1979    269    842       N  
ATOM   3209  CE2 TRP A 425     -45.310  -3.200  23.002  1.00 81.86           C  
ANISOU 3209  CE2 TRP A 425     8842  11620  10643   1891    396    826       C  
ATOM   3210  CE3 TRP A 425     -44.952  -3.257  25.391  1.00 86.69           C  
ANISOU 3210  CE3 TRP A 425     9618  12146  11173   1901    653    792       C  
ATOM   3211  CZ2 TRP A 425     -45.861  -4.480  23.006  1.00 83.52           C  
ANISOU 3211  CZ2 TRP A 425     8872  11944  10917   1750    421    828       C  
ATOM   3212  CZ3 TRP A 425     -45.500  -4.527  25.394  1.00 85.50           C  
ANISOU 3212  CZ3 TRP A 425     9294  12105  11086   1765    686    804       C  
ATOM   3213  CH2 TRP A 425     -45.948  -5.125  24.209  1.00 84.35           C  
ANISOU 3213  CH2 TRP A 425     8977  12055  11018   1687    570    819       C  
ATOM   3214  N   ILE A 426     -42.165   2.246  25.739  1.00 65.91           N  
ANISOU 3214  N   ILE A 426     7866   8907   8271   2386    572    703       N  
ATOM   3215  CA  ILE A 426     -41.909   3.210  26.805  1.00 60.99           C  
ANISOU 3215  CA  ILE A 426     7418   8170   7583   2492    669    653       C  
ATOM   3216  C   ILE A 426     -41.556   4.574  26.225  1.00 60.43           C  
ANISOU 3216  C   ILE A 426     7501   7960   7499   2607    609    651       C  
ATOM   3217  O   ILE A 426     -42.146   5.596  26.596  1.00 52.84           O  
ANISOU 3217  O   ILE A 426     6580   6955   6543   2785    677    638       O  
ATOM   3218  CB  ILE A 426     -40.799   2.692  27.738  1.00 57.50           C  
ANISOU 3218  CB  ILE A 426     7129   7664   7056   2355    704    605       C  
ATOM   3219  CG1 ILE A 426     -41.189   1.339  28.336  1.00 59.46           C  
ANISOU 3219  CG1 ILE A 426     7238   8038   7314   2251    774    617       C  
ATOM   3220  CG2 ILE A 426     -40.514   3.705  28.837  1.00 54.35           C  
ANISOU 3220  CG2 ILE A 426     6920   7149   6582   2459    794    542       C  
ATOM   3221  CD1 ILE A 426     -40.150   0.765  29.278  1.00 48.55           C  
ANISOU 3221  CD1 ILE A 426     6001   6604   5842   2130    805    578       C  
ATOM   3222  N   PHE A 427     -40.587   4.610  25.308  1.00 61.89           N  
ANISOU 3222  N   PHE A 427     7779   8069   7666   2507    488    664       N  
ATOM   3223  CA  PHE A 427     -40.175   5.872  24.703  1.00 67.04           C  
ANISOU 3223  CA  PHE A 427     8591   8577   8304   2596    434    669       C  
ATOM   3224  C   PHE A 427     -41.290   6.489  23.867  1.00 77.66           C  
ANISOU 3224  C   PHE A 427     9822   9972   9713   2769    402    728       C  
ATOM   3225  O   PHE A 427     -41.372   7.717  23.755  1.00 77.28           O  
ANISOU 3225  O   PHE A 427     9896   9808   9659   2917    412    731       O  
ATOM   3226  CB  PHE A 427     -38.926   5.650  23.849  1.00 60.67           C  
ANISOU 3226  CB  PHE A 427     7887   7697   7469   2437    320    677       C  
ATOM   3227  CG  PHE A 427     -38.408   6.893  23.186  1.00 59.15           C  
ANISOU 3227  CG  PHE A 427     7868   7346   7260   2503    270    688       C  
ATOM   3228  CD1 PHE A 427     -38.006   7.982  23.941  1.00 60.27           C  
ANISOU 3228  CD1 PHE A 427     8205   7333   7362   2576    336    634       C  
ATOM   3229  CD2 PHE A 427     -38.310   6.968  21.807  1.00 58.01           C  
ANISOU 3229  CD2 PHE A 427     7702   7203   7134   2487    161    751       C  
ATOM   3230  CE1 PHE A 427     -37.523   9.125  23.333  1.00 61.05           C  
ANISOU 3230  CE1 PHE A 427     8473   7272   7452   2626    298    646       C  
ATOM   3231  CE2 PHE A 427     -37.828   8.108  21.192  1.00 59.19           C  
ANISOU 3231  CE2 PHE A 427     8024   7200   7266   2544    125    769       C  
ATOM   3232  CZ  PHE A 427     -37.434   9.188  21.956  1.00 60.97           C  
ANISOU 3232  CZ  PHE A 427     8441   7262   7461   2611    196    718       C  
ATOM   3233  N   GLY A 428     -42.154   5.662  23.285  1.00 89.22           N  
ANISOU 3233  N   GLY A 428    11056  11605  11240   2756    362    774       N  
ATOM   3234  CA  GLY A 428     -43.217   6.152  22.430  1.00 88.81           C  
ANISOU 3234  CA  GLY A 428    10873  11624  11248   2917    312    831       C  
ATOM   3235  C   GLY A 428     -43.105   5.622  21.016  1.00 86.03           C  
ANISOU 3235  C   GLY A 428    10437  11339  10912   2830    163    885       C  
ATOM   3236  O   GLY A 428     -42.083   5.825  20.352  1.00 89.27           O  
ANISOU 3236  O   GLY A 428    11000  11642  11275   2747     85    895       O  
ATOM   3237  N   ALA A 429     -44.150   4.937  20.545  1.00 79.26           N  
ANISOU 3237  N   ALA A 429     9332  10661  10120   2845    125    917       N  
ATOM   3238  CA  ALA A 429     -44.104   4.343  19.213  1.00 68.03           C  
ANISOU 3238  CA  ALA A 429     7822   9319   8708   2756    -20    959       C  
ATOM   3239  C   ALA A 429     -43.978   5.410  18.133  1.00 64.68           C  
ANISOU 3239  C   ALA A 429     7509   8810   8257   2880   -120   1012       C  
ATOM   3240  O   ALA A 429     -43.254   5.224  17.147  1.00 61.53           O  
ANISOU 3240  O   ALA A 429     7185   8377   7817   2780   -226   1037       O  
ATOM   3241  CB  ALA A 429     -45.345   3.484  18.976  1.00 63.74           C  
ANISOU 3241  CB  ALA A 429     6984   8987   8245   2758    -41    973       C  
ATOM   3242  N   ASP A 430     -44.674   6.536  18.299  1.00 65.25           N  
ANISOU 3242  N   ASP A 430     7600   8843   8347   3102    -83   1034       N  
ATOM   3243  CA  ASP A 430     -44.605   7.595  17.299  1.00 67.13           C  
ANISOU 3243  CA  ASP A 430     7958   8992   8558   3237   -171   1095       C  
ATOM   3244  C   ASP A 430     -43.258   8.305  17.339  1.00 66.03           C  
ANISOU 3244  C   ASP A 430     8113   8629   8345   3177   -156   1083       C  
ATOM   3245  O   ASP A 430     -42.712   8.671  16.291  1.00 65.52           O  
ANISOU 3245  O   ASP A 430     8165   8492   8239   3161   -249   1131       O  
ATOM   3246  CB  ASP A 430     -45.749   8.586  17.503  1.00 70.68           C  
ANISOU 3246  CB  ASP A 430     8346   9458   9053   3504   -130   1122       C  
ATOM   3247  CG  ASP A 430     -47.090   8.018  17.084  1.00 73.67           C  
ANISOU 3247  CG  ASP A 430     8421  10066   9505   3580   -185   1150       C  
ATOM   3248  OD1 ASP A 430     -47.136   6.831  16.697  1.00 73.42           O  
ANISOU 3248  OD1 ASP A 430     8232  10174   9491   3412   -248   1141       O  
ATOM   3249  OD2 ASP A 430     -48.095   8.756  17.136  1.00 76.28           O  
ANISOU 3249  OD2 ASP A 430     8667  10437   9881   3806   -166   1177       O  
ATOM   3250  N   LYS A 431     -42.707   8.509  18.539  1.00 66.96           N  
ANISOU 3250  N   LYS A 431     8357   8639   8445   3138    -38   1017       N  
ATOM   3251  CA  LYS A 431     -41.368   9.080  18.647  1.00 66.27           C  
ANISOU 3251  CA  LYS A 431     8533   8351   8295   3051    -25    991       C  
ATOM   3252  C   LYS A 431     -40.325   8.147  18.044  1.00 62.63           C  
ANISOU 3252  C   LYS A 431     8091   7906   7800   2820   -102    988       C  
ATOM   3253  O   LYS A 431     -39.370   8.601  17.402  1.00 61.75           O  
ANISOU 3253  O   LYS A 431     8151   7667   7644   2759   -149   1005       O  
ATOM   3254  CB  LYS A 431     -41.038   9.380  20.109  1.00 62.85           C  
ANISOU 3254  CB  LYS A 431     8210   7825   7847   3049    108    910       C  
ATOM   3255  CG  LYS A 431     -41.578  10.708  20.611  1.00 62.37           C  
ANISOU 3255  CG  LYS A 431     8254   7650   7795   3272    188    904       C  
ATOM   3256  CD  LYS A 431     -40.908  11.117  21.913  1.00 63.56           C  
ANISOU 3256  CD  LYS A 431     8580   7666   7905   3239    301    814       C  
ATOM   3257  N   ALA A 432     -40.494   6.838  18.240  1.00 51.00           N  
ANISOU 3257  N   ALA A 432     6446   6585   6349   2689   -109    966       N  
ATOM   3258  CA  ALA A 432     -39.572   5.875  17.647  1.00 49.30           C  
ANISOU 3258  CA  ALA A 432     6235   6392   6105   2480   -180    961       C  
ATOM   3259  C   ALA A 432     -39.731   5.816  16.133  1.00 63.44           C  
ANISOU 3259  C   ALA A 432     7981   8235   7888   2486   -309   1029       C  
ATOM   3260  O   ALA A 432     -38.738   5.710  15.404  1.00 65.54           O  
ANISOU 3260  O   ALA A 432     8359   8436   8108   2369   -368   1039       O  
ATOM   3261  CB  ALA A 432     -39.791   4.495  18.265  1.00 48.47           C  
ANISOU 3261  CB  ALA A 432     5962   6425   6028   2351   -148    922       C  
ATOM   3262  N   TRP A 433     -40.972   5.880  15.643  1.00 62.82           N  
ANISOU 3262  N   TRP A 433     7737   8282   7849   2624   -356   1073       N  
ATOM   3263  CA  TRP A 433     -41.197   5.890  14.202  1.00 61.50           C  
ANISOU 3263  CA  TRP A 433     7532   8172   7662   2650   -488   1139       C  
ATOM   3264  C   TRP A 433     -40.619   7.146  13.565  1.00 62.16           C  
ANISOU 3264  C   TRP A 433     7841   8085   7689   2740   -513   1190       C  
ATOM   3265  O   TRP A 433     -40.045   7.087  12.471  1.00 65.53           O  
ANISOU 3265  O   TRP A 433     8344   8491   8065   2672   -600   1229       O  
ATOM   3266  CB  TRP A 433     -42.689   5.779  13.898  1.00 63.73           C  
ANISOU 3266  CB  TRP A 433     7583   8630   8001   2795   -535   1171       C  
ATOM   3267  CG  TRP A 433     -42.973   5.413  12.477  1.00 62.83           C  
ANISOU 3267  CG  TRP A 433     7384   8624   7864   2783   -684   1222       C  
ATOM   3268  CD1 TRP A 433     -43.534   6.207  11.520  1.00 55.12           C  
ANISOU 3268  CD1 TRP A 433     6416   7661   6865   2954   -776   1295       C  
ATOM   3269  CD2 TRP A 433     -42.705   4.155  11.850  1.00 60.06           C  
ANISOU 3269  CD2 TRP A 433     6937   8381   7502   2593   -762   1202       C  
ATOM   3270  NE1 TRP A 433     -43.632   5.520  10.334  1.00 55.09           N  
ANISOU 3270  NE1 TRP A 433     6325   7775   6829   2880   -911   1319       N  
ATOM   3271  CE2 TRP A 433     -43.130   4.257  10.511  1.00 56.55           C  
ANISOU 3271  CE2 TRP A 433     6446   8018   7024   2656   -903   1259       C  
ATOM   3272  CE3 TRP A 433     -42.146   2.952  12.291  1.00 57.25           C  
ANISOU 3272  CE3 TRP A 433     6536   8057   7158   2383   -727   1141       C  
ATOM   3273  CZ2 TRP A 433     -43.015   3.202   9.610  1.00 54.88           C  
ANISOU 3273  CZ2 TRP A 433     6146   7918   6787   2509  -1007   1248       C  
ATOM   3274  CZ3 TRP A 433     -42.032   1.907  11.396  1.00 56.09           C  
ANISOU 3274  CZ3 TRP A 433     6303   8012   6995   2241   -825   1134       C  
ATOM   3275  CH2 TRP A 433     -42.466   2.038  10.072  1.00 55.36           C  
ANISOU 3275  CH2 TRP A 433     6168   8000   6868   2302   -963   1182       C  
ATOM   3276  N   GLU A 434     -40.768   8.293  14.230  1.00 62.35           N  
ANISOU 3276  N   GLU A 434     7984   7983   7722   2892   -432   1189       N  
ATOM   3277  CA  GLU A 434     -40.151   9.518  13.734  1.00 65.14           C  
ANISOU 3277  CA  GLU A 434     8576   8146   8027   2964   -438   1234       C  
ATOM   3278  C   GLU A 434     -38.633   9.398  13.724  1.00 67.05           C  
ANISOU 3278  C   GLU A 434     9000   8254   8220   2764   -420   1200       C  
ATOM   3279  O   GLU A 434     -37.979   9.780  12.748  1.00 70.21           O  
ANISOU 3279  O   GLU A 434     9535   8570   8570   2729   -474   1249       O  
ATOM   3280  CB  GLU A 434     -40.590  10.708  14.587  1.00 65.06           C  
ANISOU 3280  CB  GLU A 434     8662   8015   8042   3155   -340   1225       C  
ATOM   3281  CG  GLU A 434     -40.731  12.008  13.817  1.00 67.84           C  
ANISOU 3281  CG  GLU A 434     9173   8235   8368   3333   -372   1305       C  
ATOM   3282  CD  GLU A 434     -42.177  12.421  13.636  1.00 70.70           C  
ANISOU 3282  CD  GLU A 434     9390   8700   8773   3582   -399   1358       C  
ATOM   3283  N   GLU A 435     -38.059   8.852  14.799  1.00 63.07           N  
ANISOU 3283  N   GLU A 435     8498   7738   7729   2632   -343   1117       N  
ATOM   3284  CA  GLU A 435     -36.607   8.748  14.904  1.00 59.19           C  
ANISOU 3284  CA  GLU A 435     8164   7127   7198   2447   -325   1076       C  
ATOM   3285  C   GLU A 435     -36.028   7.814  13.848  1.00 58.39           C  
ANISOU 3285  C   GLU A 435     8015   7104   7067   2288   -414   1098       C  
ATOM   3286  O   GLU A 435     -34.921   8.050  13.349  1.00 57.68           O  
ANISOU 3286  O   GLU A 435     8075   6905   6936   2183   -426   1103       O  
ATOM   3287  CB  GLU A 435     -36.223   8.272  16.306  1.00 59.49           C  
ANISOU 3287  CB  GLU A 435     8192   7162   7251   2356   -236    983       C  
ATOM   3288  CG  GLU A 435     -34.726   8.156  16.555  1.00 57.73           C  
ANISOU 3288  CG  GLU A 435     8115   6828   6993   2172   -219    930       C  
ATOM   3289  CD  GLU A 435     -34.006   9.485  16.434  1.00 56.98           C  
ANISOU 3289  CD  GLU A 435     8252   6525   6874   2203   -191    934       C  
ATOM   3290  OE1 GLU A 435     -32.938   9.527  15.789  1.00 55.45           O  
ANISOU 3290  OE1 GLU A 435     8162   6256   6652   2075   -222    941       O  
ATOM   3291  OE2 GLU A 435     -34.507  10.487  16.986  1.00 57.51           O  
ANISOU 3291  OE2 GLU A 435     8398   6499   6952   2354   -132    927       O  
ATOM   3292  N   ILE A 436     -36.758   6.758  13.490  1.00 59.21           N  
ANISOU 3292  N   ILE A 436     7913   7392   7191   2266   -474   1109       N  
ATOM   3293  CA  ILE A 436     -36.233   5.781  12.541  1.00 58.66           C  
ANISOU 3293  CA  ILE A 436     7797   7400   7092   2112   -554   1118       C  
ATOM   3294  C   ILE A 436     -36.214   6.358  11.131  1.00 61.32           C  
ANISOU 3294  C   ILE A 436     8214   7709   7377   2171   -640   1198       C  
ATOM   3295  O   ILE A 436     -35.198   6.295  10.430  1.00 61.37           O  
ANISOU 3295  O   ILE A 436     8335   7651   7333   2055   -664   1209       O  
ATOM   3296  CB  ILE A 436     -37.050   4.478  12.611  1.00 54.26           C  
ANISOU 3296  CB  ILE A 436     7002   7040   6576   2064   -590   1097       C  
ATOM   3297  CG1 ILE A 436     -36.720   3.724  13.899  1.00 53.44           C  
ANISOU 3297  CG1 ILE A 436     6855   6947   6504   1955   -503   1021       C  
ATOM   3298  CG2 ILE A 436     -36.782   3.609  11.390  1.00 48.36           C  
ANISOU 3298  CG2 ILE A 436     6202   6379   5794   1948   -691   1116       C  
ATOM   3299  CD1 ILE A 436     -37.368   2.374  13.997  1.00 53.54           C  
ANISOU 3299  CD1 ILE A 436     6656   7130   6558   1877   -523    999       C  
ATOM   3300  N   ASN A 437     -37.333   6.933  10.696  1.00 61.23           N  
ANISOU 3300  N   ASN A 437     8143   7748   7373   2357   -685   1259       N  
ATOM   3301  CA  ASN A 437     -37.440   7.472   9.347  1.00 58.94           C  
ANISOU 3301  CA  ASN A 437     7926   7446   7024   2435   -776   1345       C  
ATOM   3302  C   ASN A 437     -36.820   8.856   9.202  1.00 64.15           C  
ANISOU 3302  C   ASN A 437     8836   7893   7646   2510   -729   1391       C  
ATOM   3303  O   ASN A 437     -36.845   9.413   8.100  1.00 71.19           O  
ANISOU 3303  O   ASN A 437     9820   8751   8479   2582   -791   1473       O  
ATOM   3304  CB  ASN A 437     -38.909   7.518   8.920  1.00 58.13           C  
ANISOU 3304  CB  ASN A 437     7652   7493   6943   2615   -855   1394       C  
ATOM   3305  CG  ASN A 437     -39.569   6.155   8.963  1.00 61.89           C  
ANISOU 3305  CG  ASN A 437     7874   8179   7460   2530   -906   1349       C  
ATOM   3306  OD1 ASN A 437     -39.570   5.423   7.975  1.00 63.39           O  
ANISOU 3306  OD1 ASN A 437     7999   8476   7613   2451  -1006   1362       O  
ATOM   3307  ND2 ASN A 437     -40.136   5.807  10.113  1.00 67.10           N  
ANISOU 3307  ND2 ASN A 437     8400   8898   8197   2542   -832   1294       N  
ATOM   3308  N   ARG A 438     -36.260   9.417  10.270  1.00 60.97           N  
ANISOU 3308  N   ARG A 438     8188   7155   7825   1184   -824   1404       N  
ATOM   3309  CA  ARG A 438     -35.709  10.763  10.219  1.00 65.60           C  
ANISOU 3309  CA  ARG A 438     8993   7433   8500   1094  -1058   1595       C  
ATOM   3310  C   ARG A 438     -34.354  10.776   9.523  1.00 70.48           C  
ANISOU 3310  C   ARG A 438     9582   8168   9030    778  -1081   1875       C  
ATOM   3311  O   ARG A 438     -33.551   9.850   9.671  1.00 69.90           O  
ANISOU 3311  O   ARG A 438     9383   8320   8854    646   -912   1845       O  
ATOM   3312  CB  ARG A 438     -35.573  11.334  11.632  1.00 65.52           C  
ANISOU 3312  CB  ARG A 438     9182   7104   8608   1180  -1131   1424       C  
ATOM   3313  CG  ARG A 438     -35.145  12.793  11.696  1.00 68.81           C  
ANISOU 3313  CG  ARG A 438     9875   7117   9151   1115  -1440   1584       C  
ATOM   3314  CD  ARG A 438     -33.682  12.921  12.085  1.00 70.27           C  
ANISOU 3314  CD  ARG A 438    10138   7215   9346    807  -1496   1718       C  
ATOM   3315  NE  ARG A 438     -33.383  12.209  13.324  1.00 63.81           N  
ANISOU 3315  NE  ARG A 438     9304   6438   8504    846  -1332   1462       N  
ATOM   3316  CZ  ARG A 438     -32.217  12.275  13.957  1.00 63.13           C  
ANISOU 3316  CZ  ARG A 438     9293   6259   8436    631  -1378   1506       C  
ATOM   3317  NH1 ARG A 438     -31.238  13.020  13.465  1.00 60.63           N  
ANISOU 3317  NH1 ARG A 438     9055   5813   8169    343  -1584   1811       N  
ATOM   3318  NH2 ARG A 438     -32.029  11.596  15.080  1.00 67.71           N  
ANISOU 3318  NH2 ARG A 438     9857   6888   8982    691  -1229   1269       N  
ATOM   3319  N   GLY A 439     -34.105  11.839   8.762  1.00 77.54           N  
ANISOU 3319  N   GLY A 439    10583   8920   9959    662  -1299   2166       N  
ATOM   3320  CA  GLY A 439     -32.794  12.060   8.187  1.00 81.38           C  
ANISOU 3320  CA  GLY A 439    11037   9513  10372    344  -1349   2488       C  
ATOM   3321  C   GLY A 439     -32.457  11.210   6.986  1.00 85.18           C  
ANISOU 3321  C   GLY A 439    11276  10464  10625    257  -1186   2635       C  
ATOM   3322  O   GLY A 439     -31.296  10.824   6.818  1.00 89.47           O  
ANISOU 3322  O   GLY A 439    11703  11239  11050     51  -1098   2779       O  
ATOM   3323  N   GLY A 440     -33.434  10.909   6.138  1.00 82.85           N  
ANISOU 3323  N   GLY A 440    10896  10332  10250    428  -1154   2595       N  
ATOM   3324  CA  GLY A 440     -33.164  10.121   4.952  1.00 79.85           C  
ANISOU 3324  CA  GLY A 440    10314  10398   9628    385  -1027   2707       C  
ATOM   3325  C   GLY A 440     -34.273  10.255   3.937  1.00 78.17           C  
ANISOU 3325  C   GLY A 440    10075  10265   9363    546  -1100   2742       C  
ATOM   3326  O   GLY A 440     -35.397  10.648   4.261  1.00 79.05           O  
ANISOU 3326  O   GLY A 440    10275  10134   9626    736  -1192   2601       O  
ATOM   3327  N   ILE A 441     -33.939   9.927   2.692  1.00 76.63           N  
ANISOU 3327  N   ILE A 441     9745  10440   8932    487  -1061   2932       N  
ATOM   3328  CA  ILE A 441     -34.929   9.949   1.623  1.00 74.32           C  
ANISOU 3328  CA  ILE A 441     9413  10277   8549    635  -1131   2969       C  
ATOM   3329  C   ILE A 441     -35.708   8.637   1.556  1.00 74.24           C  
ANISOU 3329  C   ILE A 441     9278  10470   8460    833   -992   2632       C  
ATOM   3330  O   ILE A 441     -36.871   8.629   1.139  1.00 75.16           O  
ANISOU 3330  O   ILE A 441     9381  10570   8604    999  -1069   2550       O  
ATOM   3331  CB  ILE A 441     -34.250  10.262   0.280  1.00 72.10           C  
ANISOU 3331  CB  ILE A 441     9054  10316   8023    493  -1174   3346       C  
ATOM   3332  CG1 ILE A 441     -33.249  11.405   0.453  1.00 70.81           C  
ANISOU 3332  CG1 ILE A 441     8982   9981   7942    222  -1305   3715       C  
ATOM   3333  CG2 ILE A 441     -35.284  10.622  -0.775  1.00 72.27           C  
ANISOU 3333  CG2 ILE A 441     9086  10389   7983    629  -1311   3442       C  
ATOM   3334  CD1 ILE A 441     -32.290  11.561  -0.702  1.00 72.68           C  
ANISOU 3334  CD1 ILE A 441     9082  10625   7906     31  -1291   4121       C  
ATOM   3335  N   ILE A 442     -35.097   7.529   1.966  1.00 72.46           N  
ANISOU 3335  N   ILE A 442     8962  10422   8148    811   -815   2444       N  
ATOM   3336  CA  ILE A 442     -35.783   6.243   2.010  1.00 70.28           C  
ANISOU 3336  CA  ILE A 442     8592  10283   7828    966   -721   2128       C  
ATOM   3337  C   ILE A 442     -36.549   6.152   3.324  1.00 70.34           C  
ANISOU 3337  C   ILE A 442     8645   9992   8089   1049   -697   1885       C  
ATOM   3338  O   ILE A 442     -35.964   6.282   4.404  1.00 76.96           O  
ANISOU 3338  O   ILE A 442     9545  10658   9039    974   -635   1835       O  
ATOM   3339  CB  ILE A 442     -34.791   5.080   1.864  1.00 68.44           C  
ANISOU 3339  CB  ILE A 442     8262  10353   7389    929   -570   2032       C  
ATOM   3340  CG1 ILE A 442     -34.090   5.143   0.506  1.00 70.79           C  
ANISOU 3340  CG1 ILE A 442     8486  11027   7384    897   -577   2268       C  
ATOM   3341  CG2 ILE A 442     -35.502   3.746   2.030  1.00 68.16           C  
ANISOU 3341  CG2 ILE A 442     8168  10377   7351   1068   -522   1702       C  
ATOM   3342  CD1 ILE A 442     -34.976   4.746  -0.653  1.00 69.90           C  
ANISOU 3342  CD1 ILE A 442     8332  11116   7111   1055   -658   2214       C  
ATOM   3343  N   LYS A 443     -37.857   5.931   3.234  1.00 65.51           N  
ANISOU 3343  N   LYS A 443     7988   9347   7555   1207   -749   1745       N  
ATOM   3344  CA  LYS A 443     -38.721   5.839   4.402  1.00 62.73           C  
ANISOU 3344  CA  LYS A 443     7634   8789   7412   1312   -718   1539       C  
ATOM   3345  C   LYS A 443     -39.242   4.417   4.551  1.00 61.97           C  
ANISOU 3345  C   LYS A 443     7401   8852   7292   1355   -634   1306       C  
ATOM   3346  O   LYS A 443     -39.504   3.733   3.556  1.00 62.11           O  
ANISOU 3346  O   LYS A 443     7342   9083   7175   1376   -680   1286       O  
ATOM   3347  CB  LYS A 443     -39.898   6.812   4.294  1.00 61.06           C  
ANISOU 3347  CB  LYS A 443     7451   8415   7333   1469   -861   1590       C  
ATOM   3348  CG  LYS A 443     -39.491   8.246   4.007  1.00 63.21           C  
ANISOU 3348  CG  LYS A 443     7887   8488   7642   1431  -1009   1840       C  
ATOM   3349  CD  LYS A 443     -39.400   9.066   5.283  1.00 67.01           C  
ANISOU 3349  CD  LYS A 443     8518   8630   8312   1473  -1036   1781       C  
ATOM   3350  CE  LYS A 443     -38.296  10.104   5.187  1.00 71.43           C  
ANISOU 3350  CE  LYS A 443     9255   9002   8882   1296  -1156   2031       C  
ATOM   3351  NZ  LYS A 443     -38.594  11.330   5.977  1.00 76.69           N  
ANISOU 3351  NZ  LYS A 443    10127   9268   9744   1406  -1323   2025       N  
ATOM   3352  N   VAL A 444     -39.391   3.977   5.793  1.00 61.13           N  
ANISOU 3352  N   VAL A 444     7277   8638   7314   1363   -533   1137       N  
ATOM   3353  CA  VAL A 444     -39.935   2.639   6.047  1.00 58.78           C  
ANISOU 3353  CA  VAL A 444     6853   8454   7027   1372   -480    948       C  
ATOM   3354  C   VAL A 444     -41.418   2.628   5.689  1.00 59.52           C  
ANISOU 3354  C   VAL A 444     6823   8592   7199   1492   -578    923       C  
ATOM   3355  O   VAL A 444     -42.142   3.577   6.040  1.00 60.84           O  
ANISOU 3355  O   VAL A 444     6991   8643   7484   1612   -614    968       O  
ATOM   3356  CB  VAL A 444     -39.722   2.243   7.509  1.00 55.20           C  
ANISOU 3356  CB  VAL A 444     6404   7888   6683   1339   -348    818       C  
ATOM   3357  CG1 VAL A 444     -40.220   0.829   7.748  1.00 54.58           C  
ANISOU 3357  CG1 VAL A 444     6201   7914   6622   1308   -319    667       C  
ATOM   3358  CG2 VAL A 444     -38.255   2.368   7.888  1.00 54.04           C  
ANISOU 3358  CG2 VAL A 444     6373   7691   6470   1222   -270    857       C  
ATOM   3359  N   PRO A 445     -41.907   1.609   4.983  1.00 59.08           N  
ANISOU 3359  N   PRO A 445     6665   8701   7081   1479   -646    850       N  
ATOM   3360  CA  PRO A 445     -43.350   1.507   4.737  1.00 60.89           C  
ANISOU 3360  CA  PRO A 445     6743   8987   7405   1566   -751    833       C  
ATOM   3361  C   PRO A 445     -44.144   1.521   6.036  1.00 61.97           C  
ANISOU 3361  C   PRO A 445     6765   9055   7726   1616   -663    772       C  
ATOM   3362  O   PRO A 445     -43.688   1.046   7.078  1.00 60.28           O  
ANISOU 3362  O   PRO A 445     6564   8786   7553   1547   -535    692       O  
ATOM   3363  CB  PRO A 445     -43.496   0.165   4.003  1.00 59.22           C  
ANISOU 3363  CB  PRO A 445     6471   8927   7104   1494   -847    731       C  
ATOM   3364  CG  PRO A 445     -42.129  -0.485   4.045  1.00 57.07           C  
ANISOU 3364  CG  PRO A 445     6321   8668   6697   1404   -766    664       C  
ATOM   3365  CD  PRO A 445     -41.146   0.621   4.204  1.00 58.31           C  
ANISOU 3365  CD  PRO A 445     6598   8755   6803   1405   -669    794       C  
ATOM   3366  N   ARG A 446     -45.353   2.083   5.955  1.00 63.43           N  
ANISOU 3366  N   ARG A 446     6825   9272   8004   1755   -734    817       N  
ATOM   3367  CA  ARG A 446     -46.172   2.282   7.147  1.00 59.06           C  
ANISOU 3367  CA  ARG A 446     6136   8712   7591   1861   -641    779       C  
ATOM   3368  C   ARG A 446     -46.587   0.961   7.784  1.00 62.30           C  
ANISOU 3368  C   ARG A 446     6369   9243   8061   1733   -584    705       C  
ATOM   3369  O   ARG A 446     -46.850   0.911   8.991  1.00 64.19           O  
ANISOU 3369  O   ARG A 446     6521   9496   8372   1768   -451    674       O  
ATOM   3370  CB  ARG A 446     -47.405   3.115   6.788  1.00 56.64           C  
ANISOU 3370  CB  ARG A 446     5704   8463   7352   2066   -745    849       C  
ATOM   3371  CG  ARG A 446     -48.309   3.459   7.960  1.00 59.93           C  
ANISOU 3371  CG  ARG A 446     5960   8931   7880   2245   -645    812       C  
ATOM   3372  CD  ARG A 446     -47.665   4.473   8.887  1.00 63.53           C  
ANISOU 3372  CD  ARG A 446     6617   9182   8340   2380   -551    769       C  
ATOM   3373  NE  ARG A 446     -48.389   4.588  10.149  1.00 68.51           N  
ANISOU 3373  NE  ARG A 446     7098   9905   9028   2559   -424    698       N  
ATOM   3374  CZ  ARG A 446     -48.032   5.392  11.144  1.00 68.54           C  
ANISOU 3374  CZ  ARG A 446     7253   9760   9029   2724   -348    620       C  
ATOM   3375  NH1 ARG A 446     -48.751   5.432  12.258  1.00 67.93           N  
ANISOU 3375  NH1 ARG A 446     7017   9828   8964   2918   -224    549       N  
ATOM   3376  NH2 ARG A 446     -46.956   6.156  11.026  1.00 69.05           N  
ANISOU 3376  NH2 ARG A 446     7623   9545   9069   2696   -407    621       N  
ATOM   3377  N   ILE A 447     -46.641  -0.118   6.998  1.00 63.06           N  
ANISOU 3377  N   ILE A 447     6419   9425   8119   1585   -701    683       N  
ATOM   3378  CA  ILE A 447     -47.091  -1.403   7.527  1.00 66.17           C  
ANISOU 3378  CA  ILE A 447     6653   9896   8591   1432   -706    641       C  
ATOM   3379  C   ILE A 447     -46.157  -1.899   8.624  1.00 63.71           C  
ANISOU 3379  C   ILE A 447     6439   9490   8277   1333   -546    575       C  
ATOM   3380  O   ILE A 447     -46.597  -2.565   9.571  1.00 64.60           O  
ANISOU 3380  O   ILE A 447     6407   9657   8480   1250   -482    581       O  
ATOM   3381  CB  ILE A 447     -47.225  -2.429   6.382  1.00 71.58           C  
ANISOU 3381  CB  ILE A 447     7335  10634   9230   1306   -921    605       C  
ATOM   3382  CG1 ILE A 447     -47.678  -3.790   6.918  1.00 73.62           C  
ANISOU 3382  CG1 ILE A 447     7454  10921   9597   1113   -982    580       C  
ATOM   3383  CG2 ILE A 447     -45.916  -2.550   5.611  1.00 71.69           C  
ANISOU 3383  CG2 ILE A 447     7600  10575   9066   1287   -944    533       C  
ATOM   3384  CD1 ILE A 447     -47.751  -4.871   5.859  1.00 73.31           C  
ANISOU 3384  CD1 ILE A 447     7459  10878   9518    992  -1240    510       C  
ATOM   3385  N   TYR A 448     -44.866  -1.570   8.535  1.00 61.85           N  
ANISOU 3385  N   TYR A 448     6432   9134   7935   1332   -482    534       N  
ATOM   3386  CA  TYR A 448     -43.915  -2.026   9.541  1.00 58.68           C  
ANISOU 3386  CA  TYR A 448     6126   8644   7524   1243   -345    472       C  
ATOM   3387  C   TYR A 448     -44.138  -1.368  10.896  1.00 62.93           C  
ANISOU 3387  C   TYR A 448     6623   9156   8133   1333   -180    485       C  
ATOM   3388  O   TYR A 448     -43.684  -1.907  11.910  1.00 67.16           O  
ANISOU 3388  O   TYR A 448     7176   9660   8680   1254    -71    444       O  
ATOM   3389  CB  TYR A 448     -42.484  -1.776   9.067  1.00 51.57           C  
ANISOU 3389  CB  TYR A 448     5446   7661   6487   1224   -325    448       C  
ATOM   3390  CG  TYR A 448     -41.849  -2.980   8.409  1.00 49.47           C  
ANISOU 3390  CG  TYR A 448     5241   7428   6126   1119   -413    365       C  
ATOM   3391  CD1 TYR A 448     -41.588  -2.995   7.046  1.00 51.40           C  
ANISOU 3391  CD1 TYR A 448     5548   7752   6229   1155   -538    364       C  
ATOM   3392  CD2 TYR A 448     -41.516  -4.105   9.153  1.00 47.51           C  
ANISOU 3392  CD2 TYR A 448     4998   7137   5916   1007   -385    283       C  
ATOM   3393  CE1 TYR A 448     -41.010  -4.095   6.441  1.00 52.11           C  
ANISOU 3393  CE1 TYR A 448     5710   7886   6205   1114   -631    254       C  
ATOM   3394  CE2 TYR A 448     -40.938  -5.209   8.557  1.00 47.77           C  
ANISOU 3394  CE2 TYR A 448     5114   7175   5863    952   -496    182       C  
ATOM   3395  CZ  TYR A 448     -40.687  -5.199   7.201  1.00 50.77           C  
ANISOU 3395  CZ  TYR A 448     5560   7640   6089   1022   -618    153       C  
ATOM   3396  OH  TYR A 448     -40.112  -6.295   6.601  1.00 51.69           O  
ANISOU 3396  OH  TYR A 448     5774   7775   6092   1021   -740     19       O  
ATOM   3397  N   TYR A 449     -44.822  -0.221  10.938  1.00 65.40           N  
ANISOU 3397  N   TYR A 449     6890   9481   8478   1520   -173    532       N  
ATOM   3398  CA  TYR A 449     -45.153   0.396  12.219  1.00 66.99           C  
ANISOU 3398  CA  TYR A 449     7050   9684   8721   1664    -34    514       C  
ATOM   3399  C   TYR A 449     -45.952  -0.561  13.096  1.00 71.74           C  
ANISOU 3399  C   TYR A 449     7411  10466   9381   1596     46    530       C  
ATOM   3400  O   TYR A 449     -45.738  -0.627  14.311  1.00 74.43           O  
ANISOU 3400  O   TYR A 449     7753  10820   9709   1615    192    499       O  
ATOM   3401  CB  TYR A 449     -45.928   1.696  11.989  1.00 67.99           C  
ANISOU 3401  CB  TYR A 449     7154   9807   8873   1917    -83    547       C  
ATOM   3402  CG  TYR A 449     -46.387   2.389  13.255  1.00 69.48           C  
ANISOU 3402  CG  TYR A 449     7300  10021   9077   2141     40    497       C  
ATOM   3403  CD1 TYR A 449     -45.595   3.351  13.869  1.00 70.02           C  
ANISOU 3403  CD1 TYR A 449     7615   9879   9112   2256     72    428       C  
ATOM   3404  CD2 TYR A 449     -47.618   2.092  13.829  1.00 70.67           C  
ANISOU 3404  CD2 TYR A 449     7159  10427   9264   2246    110    523       C  
ATOM   3405  CE1 TYR A 449     -46.012   3.990  15.023  1.00 71.33           C  
ANISOU 3405  CE1 TYR A 449     7770  10067   9264   2503    163    348       C  
ATOM   3406  CE2 TYR A 449     -48.041   2.723  14.983  1.00 73.12           C  
ANISOU 3406  CE2 TYR A 449     7422  10814   9545   2498    233    465       C  
ATOM   3407  CZ  TYR A 449     -47.235   3.672  15.575  1.00 73.88           C  
ANISOU 3407  CZ  TYR A 449     7798  10679   9592   2644    255    358       C  
ATOM   3408  OH  TYR A 449     -47.656   4.304  16.722  1.00 76.74           O  
ANISOU 3408  OH  TYR A 449     8140  11118   9900   2935    358    267       O  
ATOM   3409  N   TYR A 450     -46.872  -1.316  12.493  1.00 73.73           N  
ANISOU 3409  N   TYR A 450     7452  10869   9693   1503    -63    597       N  
ATOM   3410  CA  TYR A 450     -47.668  -2.274  13.251  1.00 72.56           C  
ANISOU 3410  CA  TYR A 450     7048  10907   9616   1386    -18    668       C  
ATOM   3411  C   TYR A 450     -46.913  -3.570  13.505  1.00 69.70           C  
ANISOU 3411  C   TYR A 450     6767  10457   9259   1125    -38    647       C  
ATOM   3412  O   TYR A 450     -47.199  -4.266  14.486  1.00 74.21           O  
ANISOU 3412  O   TYR A 450     7197  11130   9870   1018     42    712       O  
ATOM   3413  CB  TYR A 450     -48.979  -2.559  12.517  1.00 74.14           C  
ANISOU 3413  CB  TYR A 450     6976  11294   9898   1362   -165    772       C  
ATOM   3414  CG  TYR A 450     -49.754  -1.309  12.173  1.00 75.45           C  
ANISOU 3414  CG  TYR A 450     7059  11549  10062   1641   -172    793       C  
ATOM   3415  CD1 TYR A 450     -50.336  -0.535  13.168  1.00 76.28           C  
ANISOU 3415  CD1 TYR A 450     7030  11800  10154   1884    -13    805       C  
ATOM   3416  CD2 TYR A 450     -49.897  -0.897  10.854  1.00 75.89           C  
ANISOU 3416  CD2 TYR A 450     7179  11546  10110   1689   -348    795       C  
ATOM   3417  CE1 TYR A 450     -51.043   0.611  12.861  1.00 77.93           C  
ANISOU 3417  CE1 TYR A 450     7179  12070  10361   2179    -43    807       C  
ATOM   3418  CE2 TYR A 450     -50.603   0.248  10.537  1.00 78.08           C  
ANISOU 3418  CE2 TYR A 450     7392  11882  10392   1953   -377    823       C  
ATOM   3419  CZ  TYR A 450     -51.173   0.998  11.544  1.00 79.89           C  
ANISOU 3419  CZ  TYR A 450     7497  12231  10626   2203   -230    823       C  
ATOM   3420  OH  TYR A 450     -51.876   2.139  11.233  1.00 84.30           O  
ANISOU 3420  OH  TYR A 450     8009  12831  11190   2503   -282    834       O  
ATOM   3421  N   VAL A 451     -45.955  -3.912  12.642  1.00 62.05           N  
ANISOU 3421  N   VAL A 451     6018   9319   8239   1036   -147    566       N  
ATOM   3422  CA  VAL A 451     -45.143  -5.101  12.878  1.00 60.80           C  
ANISOU 3422  CA  VAL A 451     5969   9056   8075    839   -180    518       C  
ATOM   3423  C   VAL A 451     -44.234  -4.892  14.082  1.00 58.69           C  
ANISOU 3423  C   VAL A 451     5824   8717   7760    862     12    478       C  
ATOM   3424  O   VAL A 451     -44.087  -5.782  14.928  1.00 61.84           O  
ANISOU 3424  O   VAL A 451     6192   9114   8191    723     51    502       O  
ATOM   3425  CB  VAL A 451     -44.337  -5.461  11.616  1.00 59.29           C  
ANISOU 3425  CB  VAL A 451     5974   8748   7804    801   -339    421       C  
ATOM   3426  CG1 VAL A 451     -43.703  -6.836  11.767  1.00 60.05           C  
ANISOU 3426  CG1 VAL A 451     6165   8743   7908    628   -426    357       C  
ATOM   3427  CG2 VAL A 451     -45.228  -5.413  10.386  1.00 58.28           C  
ANISOU 3427  CG2 VAL A 451     5750   8700   7693    825   -529    450       C  
ATOM   3428  N   MET A 452     -43.624  -3.711  14.188  1.00 54.56           N  
ANISOU 3428  N   MET A 452     5445   8122   7164   1025    112    429       N  
ATOM   3429  CA  MET A 452     -42.670  -3.442  15.257  1.00 53.05           C  
ANISOU 3429  CA  MET A 452     5397   7840   6919   1047    259    379       C  
ATOM   3430  C   MET A 452     -43.339  -3.025  16.559  1.00 56.84           C  
ANISOU 3430  C   MET A 452     5751   8436   7410   1160    411    410       C  
ATOM   3431  O   MET A 452     -42.689  -3.057  17.610  1.00 57.51           O  
ANISOU 3431  O   MET A 452     5925   8478   7448   1154    526    373       O  
ATOM   3432  CB  MET A 452     -41.688  -2.360  14.808  1.00 55.76           C  
ANISOU 3432  CB  MET A 452     5957   8041   7188   1144    260    331       C  
ATOM   3433  CG  MET A 452     -41.037  -2.669  13.475  1.00 67.55           C  
ANISOU 3433  CG  MET A 452     7547   9493   8626   1069    132    318       C  
ATOM   3434  SD  MET A 452     -40.635  -1.208  12.504  1.00 79.23           S  
ANISOU 3434  SD  MET A 452     9158  10904  10041   1190     77    366       S  
ATOM   3435  CE  MET A 452     -39.479  -0.399  13.595  1.00 73.00           C  
ANISOU 3435  CE  MET A 452     8550   9959   9228   1205    190    345       C  
ATOM   3436  N   ARG A 453     -44.612  -2.637  16.519  1.00 57.63           N  
ANISOU 3436  N   ARG A 453     5637   8708   7551   1281    415    476       N  
ATOM   3437  CA  ARG A 453     -45.337  -2.260  17.725  1.00 53.94           C  
ANISOU 3437  CA  ARG A 453     5013   8423   7058   1435    570    506       C  
ATOM   3438  C   ARG A 453     -46.195  -3.384  18.285  1.00 49.75           C  
ANISOU 3438  C   ARG A 453     4197   8130   6575   1277    605    647       C  
ATOM   3439  O   ARG A 453     -46.454  -3.407  19.492  1.00 51.12           O  
ANISOU 3439  O   ARG A 453     4262   8472   6690   1340    762    687       O  
ATOM   3440  CB  ARG A 453     -46.226  -1.040  17.456  1.00 53.10           C  
ANISOU 3440  CB  ARG A 453     4825   8402   6949   1721    565    498       C  
ATOM   3441  CG  ARG A 453     -46.667  -0.306  18.713  1.00 53.17           C  
ANISOU 3441  CG  ARG A 453     4769   8556   6875   1989    727    458       C  
ATOM   3442  CD  ARG A 453     -47.760   0.707  18.418  1.00 57.48           C  
ANISOU 3442  CD  ARG A 453     5179   9234   7427   2294    702    457       C  
ATOM   3443  NE  ARG A 453     -48.119   1.474  19.607  1.00 64.57           N  
ANISOU 3443  NE  ARG A 453     6049  10269   8215   2617    845    377       N  
ATOM   3444  CZ  ARG A 453     -49.216   2.215  19.716  1.00 72.58           C  
ANISOU 3444  CZ  ARG A 453     6881  11495   9200   2942    869    372       C  
ATOM   3445  NH1 ARG A 453     -50.070   2.296  18.704  1.00 78.78           N  
ANISOU 3445  NH1 ARG A 453     7486  12373  10075   2963    757    460       N  
ATOM   3446  NH2 ARG A 453     -49.460   2.878  20.838  1.00 73.02           N  
ANISOU 3446  NH2 ARG A 453     6938  11684   9122   3272    996    268       N  
ATOM   3447  N   TYR A 454     -46.634  -4.320  17.444  1.00 48.56           N  
ANISOU 3447  N   TYR A 454     3927   8002   6523   1067    445    733       N  
ATOM   3448  CA  TYR A 454     -47.525  -5.380  17.900  1.00 55.81           C  
ANISOU 3448  CA  TYR A 454     4558   9132   7515    873    430    910       C  
ATOM   3449  C   TYR A 454     -47.015  -6.759  17.504  1.00 59.97           C  
ANISOU 3449  C   TYR A 454     5177   9486   8121    559    254    933       C  
ATOM   3450  O   TYR A 454     -46.929  -7.658  18.346  1.00 64.96           O  
ANISOU 3450  O   TYR A 454     5754  10150   8776    377    282   1032       O  
ATOM   3451  CB  TYR A 454     -48.934  -5.165  17.343  1.00 61.03           C  
ANISOU 3451  CB  TYR A 454     4908  10032   8246    929    358   1031       C  
ATOM   3452  CG  TYR A 454     -49.535  -3.823  17.692  1.00 62.04           C  
ANISOU 3452  CG  TYR A 454     4936  10339   8296   1285    506    998       C  
ATOM   3453  CD1 TYR A 454     -50.050  -3.579  18.959  1.00 61.64           C  
ANISOU 3453  CD1 TYR A 454     4689  10571   8162   1434    713   1065       C  
ATOM   3454  CD2 TYR A 454     -49.588  -2.800  16.755  1.00 63.34           C  
ANISOU 3454  CD2 TYR A 454     5212  10398   8457   1492    426    899       C  
ATOM   3455  CE1 TYR A 454     -50.600  -2.354  19.283  1.00 63.48           C  
ANISOU 3455  CE1 TYR A 454     4850  10963   8307   1814    828   1000       C  
ATOM   3456  CE2 TYR A 454     -50.137  -1.572  17.070  1.00 63.07           C  
ANISOU 3456  CE2 TYR A 454     5115  10487   8360   1843    523    855       C  
ATOM   3457  CZ  TYR A 454     -50.641  -1.354  18.335  1.00 64.44           C  
ANISOU 3457  CZ  TYR A 454     5106  10929   8449   2019    720    889       C  
ATOM   3458  OH  TYR A 454     -51.188  -0.132  18.652  1.00 68.16           O  
ANISOU 3458  OH  TYR A 454     5535  11521   8842   2420    798    812       O  
ATOM   3459  N   ILE A 455     -46.673  -6.937  16.227  1.00 58.88           N  
ANISOU 3459  N   ILE A 455     5191   9168   8015    511     59    841       N  
ATOM   3460  CA  ILE A 455     -46.327  -8.265  15.725  1.00 57.81           C  
ANISOU 3460  CA  ILE A 455     5146   8868   7950    259   -157    835       C  
ATOM   3461  C   ILE A 455     -45.000  -8.732  16.313  1.00 60.96           C  
ANISOU 3461  C   ILE A 455     5796   9078   8290    206    -99    740       C  
ATOM   3462  O   ILE A 455     -44.932  -9.773  16.976  1.00 65.48           O  
ANISOU 3462  O   ILE A 455     6346   9613   8920     11   -144    822       O  
ATOM   3463  CB  ILE A 455     -46.292  -8.270  14.187  1.00 56.57           C  
ANISOU 3463  CB  ILE A 455     5096   8602   7794    279   -377    734       C  
ATOM   3464  CG1 ILE A 455     -47.661  -7.885  13.622  1.00 54.31           C  
ANISOU 3464  CG1 ILE A 455     4546   8511   7579    316   -459    844       C  
ATOM   3465  CG2 ILE A 455     -45.861  -9.633  13.668  1.00 60.00           C  
ANISOU 3465  CG2 ILE A 455     5673   8846   8278     73   -625    679       C  
ATOM   3466  CD1 ILE A 455     -48.800  -8.725  14.157  1.00 57.40           C  
ANISOU 3466  CD1 ILE A 455     4626   9074   8109     99   -535   1055       C  
ATOM   3467  N   THR A 456     -43.930  -7.969  16.077  1.00 58.57           N  
ANISOU 3467  N   THR A 456     5724   8656   7875    369    -14    587       N  
ATOM   3468  CA  THR A 456     -42.602  -8.391  16.521  1.00 57.27           C  
ANISOU 3468  CA  THR A 456     5785   8327   7649    330     25    492       C  
ATOM   3469  C   THR A 456     -42.522  -8.657  18.021  1.00 62.60           C  
ANISOU 3469  C   THR A 456     6407   9057   8321    270    180    575       C  
ATOM   3470  O   THR A 456     -41.962  -9.697  18.406  1.00 64.83           O  
ANISOU 3470  O   THR A 456     6778   9227   8629    119    113    581       O  
ATOM   3471  CB  THR A 456     -41.554  -7.359  16.088  1.00 58.65           C  
ANISOU 3471  CB  THR A 456     6161   8419   7705    504    104    363       C  
ATOM   3472  OG1 THR A 456     -41.855  -6.896  14.766  1.00 63.79           O  
ANISOU 3472  OG1 THR A 456     6814   9084   8339    582     -9    333       O  
ATOM   3473  CG2 THR A 456     -40.164  -7.979  16.097  1.00 59.07           C  
ANISOU 3473  CG2 THR A 456     6428   8322   7695    454     77    261       C  
ATOM   3474  N   PRO A 457     -43.036  -7.797  18.912  1.00 64.65           N  
ANISOU 3474  N   PRO A 457     6538   9488   8538    398    374    636       N  
ATOM   3475  CA  PRO A 457     -42.969  -8.149  20.340  1.00 66.15           C  
ANISOU 3475  CA  PRO A 457     6673   9768   8694    344    515    722       C  
ATOM   3476  C   PRO A 457     -43.810  -9.363  20.693  1.00 70.47           C  
ANISOU 3476  C   PRO A 457     7007  10424   9343    100    427    925       C  
ATOM   3477  O   PRO A 457     -43.372 -10.199  21.494  1.00 68.47           O  
ANISOU 3477  O   PRO A 457     6801  10123   9092    -49    430    993       O  
ATOM   3478  CB  PRO A 457     -43.470  -6.878  21.040  1.00 67.73           C  
ANISOU 3478  CB  PRO A 457     6778  10158   8801    592    717    716       C  
ATOM   3479  CG  PRO A 457     -44.308  -6.197  20.026  1.00 68.03           C  
ANISOU 3479  CG  PRO A 457     6704  10261   8883    710    650    711       C  
ATOM   3480  CD  PRO A 457     -43.635  -6.463  18.716  1.00 65.78           C  
ANISOU 3480  CD  PRO A 457     6602   9748   8641    629    466    615       C  
ATOM   3481  N   ALA A 458     -45.007  -9.488  20.115  1.00 73.30           N  
ANISOU 3481  N   ALA A 458     7128  10928   9795     40    330   1045       N  
ATOM   3482  CA  ALA A 458     -45.827 -10.668  20.371  1.00 71.71           C  
ANISOU 3482  CA  ALA A 458     6710  10819   9716   -241    200   1276       C  
ATOM   3483  C   ALA A 458     -45.219 -11.910  19.734  1.00 75.47           C  
ANISOU 3483  C   ALA A 458     7389  10987  10299   -468    -81   1230       C  
ATOM   3484  O   ALA A 458     -45.295 -13.005  20.302  1.00 78.92           O  
ANISOU 3484  O   ALA A 458     7790  11379  10819   -714   -187   1387       O  
ATOM   3485  CB  ALA A 458     -47.250 -10.445  19.861  1.00 66.80           C  
ANISOU 3485  CB  ALA A 458     5767  10441   9174   -252    143   1422       C  
ATOM   3486  N   PHE A 459     -44.611 -11.759  18.555  1.00 75.77           N  
ANISOU 3486  N   PHE A 459     7646  10818  10325   -375   -216   1018       N  
ATOM   3487  CA  PHE A 459     -43.956 -12.891  17.907  1.00 76.27           C  
ANISOU 3487  CA  PHE A 459     7932  10597  10452   -514   -487    922       C  
ATOM   3488  C   PHE A 459     -42.817 -13.430  18.764  1.00 74.91           C  
ANISOU 3488  C   PHE A 459     7959  10271  10233   -547   -433    877       C  
ATOM   3489  O   PHE A 459     -42.646 -14.648  18.888  1.00 79.51           O  
ANISOU 3489  O   PHE A 459     8627  10674  10909   -741   -645    925       O  
ATOM   3490  CB  PHE A 459     -43.448 -12.474  16.526  1.00 76.83           C  
ANISOU 3490  CB  PHE A 459     8186  10549  10455   -345   -590    696       C  
ATOM   3491  CG  PHE A 459     -42.895 -13.606  15.710  1.00 79.25           C  
ANISOU 3491  CG  PHE A 459     8713  10601  10796   -425   -891    564       C  
ATOM   3492  CD1 PHE A 459     -43.730 -14.388  14.931  1.00 84.85           C  
ANISOU 3492  CD1 PHE A 459     9368  11242  11629   -579  -1200    603       C  
ATOM   3493  CD2 PHE A 459     -41.537 -13.877  15.708  1.00 77.81           C  
ANISOU 3493  CD2 PHE A 459     8794  10255  10516   -327   -882    389       C  
ATOM   3494  CE1 PHE A 459     -43.223 -15.427  14.174  1.00 86.75           C  
ANISOU 3494  CE1 PHE A 459     9846  11227  11887   -612  -1510    445       C  
ATOM   3495  CE2 PHE A 459     -41.024 -14.912  14.951  1.00 79.26           C  
ANISOU 3495  CE2 PHE A 459     9188  10221  10706   -341  -1165    239       C  
ATOM   3496  CZ  PHE A 459     -41.868 -15.689  14.184  1.00 82.60           C  
ANISOU 3496  CZ  PHE A 459     9588  10550  11245   -473  -1487    253       C  
ATOM   3497  N   LEU A 460     -42.031 -12.538  19.370  1.00 70.54           N  
ANISOU 3497  N   LEU A 460     7492   9770   9542   -361   -178    789       N  
ATOM   3498  CA  LEU A 460     -40.946 -12.978  20.240  1.00 66.75           C  
ANISOU 3498  CA  LEU A 460     7184   9169   9009   -383   -120    753       C  
ATOM   3499  C   LEU A 460     -41.486 -13.579  21.531  1.00 71.44           C  
ANISOU 3499  C   LEU A 460     7620   9875   9647   -566    -64    992       C  
ATOM   3500  O   LEU A 460     -41.097 -14.684  21.924  1.00 77.05           O  
ANISOU 3500  O   LEU A 460     8429  10426  10419   -736   -207   1053       O  
ATOM   3501  CB  LEU A 460     -40.010 -11.809  20.549  1.00 58.13           C  
ANISOU 3501  CB  LEU A 460     6212   8109   7764   -155    111    612       C  
ATOM   3502  CG  LEU A 460     -39.246 -11.178  19.385  1.00 52.88           C  
ANISOU 3502  CG  LEU A 460     5708   7354   7029     10     76    415       C  
ATOM   3503  CD1 LEU A 460     -38.421 -10.000  19.879  1.00 50.47           C  
ANISOU 3503  CD1 LEU A 460     5493   7081   6601    177    285    338       C  
ATOM   3504  CD2 LEU A 460     -38.363 -12.207  18.699  1.00 49.98           C  
ANISOU 3504  CD2 LEU A 460     5534   6789   6668    -29   -128    294       C  
ATOM   3505  N   ALA A 461     -42.390 -12.859  22.204  1.00 68.24           N  
ANISOU 3505  N   ALA A 461     6968   9762   9200   -519    138   1136       N  
ATOM   3506  CA  ALA A 461     -42.896 -13.312  23.496  1.00 67.08           C  
ANISOU 3506  CA  ALA A 461     6638   9805   9044   -664    238   1385       C  
ATOM   3507  C   ALA A 461     -43.596 -14.659  23.381  1.00 69.60           C  
ANISOU 3507  C   ALA A 461     6837  10067   9541   -998    -21   1619       C  
ATOM   3508  O   ALA A 461     -43.398 -15.542  24.225  1.00 73.05           O  
ANISOU 3508  O   ALA A 461     7291  10458  10005  -1190    -70   1785       O  
ATOM   3509  CB  ALA A 461     -43.845 -12.267  24.081  1.00 65.18           C  
ANISOU 3509  CB  ALA A 461     6124   9939   8701   -502    492   1481       C  
ATOM   3510  N   VAL A 462     -44.423 -14.836  22.349  1.00 69.79           N  
ANISOU 3510  N   VAL A 462     6746  10079   9693  -1084   -214   1650       N  
ATOM   3511  CA  VAL A 462     -45.090 -16.120  22.152  1.00 72.20           C  
ANISOU 3511  CA  VAL A 462     6958  10283  10193  -1427   -524   1870       C  
ATOM   3512  C   VAL A 462     -44.063 -17.211  21.889  1.00 78.05           C  
ANISOU 3512  C   VAL A 462     8041  10608  11007  -1532   -796   1744       C  
ATOM   3513  O   VAL A 462     -44.159 -18.319  22.429  1.00 85.71           O  
ANISOU 3513  O   VAL A 462     9017  11459  12092  -1806   -982   1950       O  
ATOM   3514  CB  VAL A 462     -46.122 -16.021  21.014  1.00 71.14           C  
ANISOU 3514  CB  VAL A 462     6654  10201  10173  -1477   -705   1892       C  
ATOM   3515  CG1 VAL A 462     -46.558 -17.407  20.565  1.00 72.53           C  
ANISOU 3515  CG1 VAL A 462     6845  10146  10569  -1828  -1122   2042       C  
ATOM   3516  CG2 VAL A 462     -47.321 -15.203  21.465  1.00 74.33           C  
ANISOU 3516  CG2 VAL A 462     6655  11056  10532  -1423   -471   2099       C  
ATOM   3517  N   LEU A 463     -43.051 -16.911  21.072  1.00 77.46           N  
ANISOU 3517  N   LEU A 463     8251  10320  10858  -1305   -827   1416       N  
ATOM   3518  CA  LEU A 463     -41.998 -17.883  20.810  1.00 82.46           C  
ANISOU 3518  CA  LEU A 463     9210  10595  11527  -1328  -1066   1260       C  
ATOM   3519  C   LEU A 463     -41.067 -18.068  22.002  1.00 78.70           C  
ANISOU 3519  C   LEU A 463     8849  10084  10968  -1312   -916   1289       C  
ATOM   3520  O   LEU A 463     -40.401 -19.104  22.093  1.00 80.47           O  
ANISOU 3520  O   LEU A 463     9292  10029  11256  -1396  -1140   1255       O  
ATOM   3521  CB  LEU A 463     -41.191 -17.472  19.577  1.00 87.79           C  
ANISOU 3521  CB  LEU A 463    10113  11134  12110  -1065  -1118    919       C  
ATOM   3522  CG  LEU A 463     -41.807 -17.773  18.208  1.00 94.57           C  
ANISOU 3522  CG  LEU A 463    10985  11893  13053  -1090  -1409    831       C  
ATOM   3523  CD1 LEU A 463     -40.755 -17.630  17.128  1.00 95.84           C  
ANISOU 3523  CD1 LEU A 463    11416  11915  13085   -825  -1477    500       C  
ATOM   3524  CD2 LEU A 463     -42.422 -19.164  18.177  1.00 97.54           C  
ANISOU 3524  CD2 LEU A 463    11379  12046  13638  -1397  -1802    983       C  
ATOM   3525  N   LEU A 464     -41.009 -17.099  22.918  1.00 75.74           N  
ANISOU 3525  N   LEU A 464     8349   9979  10451  -1190   -565   1342       N  
ATOM   3526  CA  LEU A 464     -40.129 -17.231  24.075  1.00 76.53           C  
ANISOU 3526  CA  LEU A 464     8559  10062  10455  -1168   -427   1366       C  
ATOM   3527  C   LEU A 464     -40.742 -18.125  25.148  1.00 84.90           C  
ANISOU 3527  C   LEU A 464     9473  11192  11593  -1457   -485   1709       C  
ATOM   3528  O   LEU A 464     -40.035 -18.935  25.759  1.00 86.41           O  
ANISOU 3528  O   LEU A 464     9831  11202  11799  -1548   -586   1754       O  
ATOM   3529  CB  LEU A 464     -39.801 -15.849  24.646  1.00 71.55           C  
ANISOU 3529  CB  LEU A 464     7884   9671   9633   -918    -69   1271       C  
ATOM   3530  CG  LEU A 464     -38.400 -15.639  25.230  1.00 68.99           C  
ANISOU 3530  CG  LEU A 464     7787   9244   9181   -772     39   1112       C  
ATOM   3531  CD1 LEU A 464     -38.193 -14.182  25.614  1.00 65.44           C  
ANISOU 3531  CD1 LEU A 464     7305   8993   8565   -534    331   1004       C  
ATOM   3532  CD2 LEU A 464     -38.157 -16.541  26.431  1.00 74.33           C  
ANISOU 3532  CD2 LEU A 464     8491   9891   9859   -939     11   1301       C  
ATOM   3533  N   VAL A 465     -42.049 -18.001  25.391  1.00 89.43           N  
ANISOU 3533  N   VAL A 465     9724  12046  12211  -1605   -427   1974       N  
ATOM   3534  CA  VAL A 465     -42.680 -18.831  26.414  1.00 90.30           C  
ANISOU 3534  CA  VAL A 465     9649  12281  12379  -1906   -472   2358       C  
ATOM   3535  C   VAL A 465     -42.935 -20.239  25.889  1.00 93.63           C  
ANISOU 3535  C   VAL A 465    10156  12372  13047  -2233   -912   2497       C  
ATOM   3536  O   VAL A 465     -42.879 -21.210  26.652  1.00 96.49           O  
ANISOU 3536  O   VAL A 465    10543  12637  13481  -2486  -1055   2748       O  
ATOM   3537  CB  VAL A 465     -43.968 -18.165  26.941  1.00 88.62           C  
ANISOU 3537  CB  VAL A 465     9017  12559  12096  -1929   -228   2618       C  
ATOM   3538  CG1 VAL A 465     -43.714 -16.691  27.241  1.00 83.38           C  
ANISOU 3538  CG1 VAL A 465     8329  12150  11200  -1547    145   2402       C  
ATOM   3539  CG2 VAL A 465     -45.136 -18.323  25.972  1.00 89.51           C  
ANISOU 3539  CG2 VAL A 465     8907  12722  12379  -2083   -420   2729       C  
ATOM   3540  N   VAL A 466     -43.185 -20.388  24.587  1.00 95.75           N  
ANISOU 3540  N   VAL A 466    10496  12440  13443  -2231  -1162   2335       N  
ATOM   3541  CA  VAL A 466     -43.315 -21.719  23.996  1.00100.89           C  
ANISOU 3541  CA  VAL A 466    11302  12708  14324  -2500  -1638   2397       C  
ATOM   3542  C   VAL A 466     -41.979 -22.446  23.963  1.00100.59           C  
ANISOU 3542  C   VAL A 466    11674  12259  14287  -2406  -1827   2169       C  
ATOM   3543  O   VAL A 466     -41.938 -23.661  23.738  1.00102.21           O  
ANISOU 3543  O   VAL A 466    12060  12102  14672  -2616  -2240   2229       O  
ATOM   3544  CB  VAL A 466     -44.015 -21.510  22.636  1.00102.09           C  
ANISOU 3544  CB  VAL A 466    11397  12824  14569  -2477  -1821   2266       C  
ATOM   3545  CG1 VAL A 466     -43.811 -22.670  21.679  1.00103.12           C  
ANISOU 3545  CG1 VAL A 466    11817  12482  14883  -2600  -2332   2135       C  
ATOM   3546  CG2 VAL A 466     -45.505 -21.244  22.856  1.00106.51           C  
ANISOU 3546  CG2 VAL A 466    11512  13759  15198  -2696  -1748   2617       C  
ATOM   3547  N   TRP A 467     -40.887 -21.739  24.249  1.00 99.37           N  
ANISOU 3547  N   TRP A 467    11665  12156  13936  -2097  -1548   1927       N  
ATOM   3548  CA  TRP A 467     -39.581 -22.374  24.361  1.00 99.97           C  
ANISOU 3548  CA  TRP A 467    12084  11911  13989  -1985  -1685   1736       C  
ATOM   3549  C   TRP A 467     -39.475 -23.232  25.616  1.00100.52           C  
ANISOU 3549  C   TRP A 467    12168  11913  14112  -2224  -1754   2034       C  
ATOM   3550  O   TRP A 467     -38.780 -24.254  25.607  1.00105.09           O  
ANISOU 3550  O   TRP A 467    13025  12126  14780  -2262  -2055   1977       O  
ATOM   3551  CB  TRP A 467     -38.500 -21.295  24.364  1.00 97.28           C  
ANISOU 3551  CB  TRP A 467    11839  11698  13426  -1620  -1357   1442       C  
ATOM   3552  CG  TRP A 467     -37.116 -21.753  24.048  1.00 95.21           C  
ANISOU 3552  CG  TRP A 467    11905  11151  13119  -1419  -1493   1161       C  
ATOM   3553  CD1 TRP A 467     -36.560 -22.971  24.315  1.00 96.54           C  
ANISOU 3553  CD1 TRP A 467    12301  10998  13383  -1503  -1789   1180       C  
ATOM   3554  CD2 TRP A 467     -36.097 -20.978  23.416  1.00 92.20           C  
ANISOU 3554  CD2 TRP A 467    11647  10808  12577  -1087  -1339    835       C  
ATOM   3555  NE1 TRP A 467     -35.258 -23.002  23.881  1.00 94.78           N  
ANISOU 3555  NE1 TRP A 467    12323  10631  13057  -1210  -1816    864       N  
ATOM   3556  CE2 TRP A 467     -34.950 -21.789  23.324  1.00 91.63           C  
ANISOU 3556  CE2 TRP A 467    11850  10469  12498   -966  -1535    663       C  
ATOM   3557  CE3 TRP A 467     -36.044 -19.675  22.913  1.00 90.87           C  
ANISOU 3557  CE3 TRP A 467    11377  10878  12274   -884  -1069    691       C  
ATOM   3558  CZ2 TRP A 467     -33.766 -21.340  22.750  1.00 89.49           C  
ANISOU 3558  CZ2 TRP A 467    11715  10214  12074   -654  -1446    368       C  
ATOM   3559  CZ3 TRP A 467     -34.870 -19.232  22.345  1.00 90.38           C  
ANISOU 3559  CZ3 TRP A 467    11467  10798  12075   -611   -998    418       C  
ATOM   3560  CH2 TRP A 467     -33.747 -20.061  22.267  1.00 89.34           C  
ANISOU 3560  CH2 TRP A 467    11571  10450  11925   -499  -1174    265       C  
ATOM   3561  N   ALA A 468     -40.166 -22.840  26.692  1.00 96.87           N  
ANISOU 3561  N   ALA A 468    11412  11812  13583  -2369  -1490   2356       N  
ATOM   3562  CA  ALA A 468     -39.947 -23.436  28.008  1.00 95.25           C  
ANISOU 3562  CA  ALA A 468    11205  11630  13355  -2546  -1468   2641       C  
ATOM   3563  C   ALA A 468     -40.113 -24.954  28.006  1.00 96.47           C  
ANISOU 3563  C   ALA A 468    11501  11402  13751  -2884  -1941   2865       C  
ATOM   3564  O   ALA A 468     -39.419 -25.652  28.756  1.00 94.41           O  
ANISOU 3564  O   ALA A 468    11421  10956  13493  -2946  -2045   2954       O  
ATOM   3565  CB  ALA A 468     -40.897 -22.803  29.022  1.00 95.19           C  
ANISOU 3565  CB  ALA A 468    10809  12134  13224  -2651  -1131   2976       C  
ATOM   3566  N   ARG A 469     -41.012 -25.480  27.180  1.00 95.97           N  
ANISOU 3566  N   ARG A 469    11372  11195  13897  -3108  -2257   2961       N  
ATOM   3567  CA  ARG A 469     -41.266 -26.918  27.128  1.00 96.81           C  
ANISOU 3567  CA  ARG A 469    11624  10895  14263  -3462  -2770   3189       C  
ATOM   3568  C   ARG A 469     -40.013 -27.712  26.766  1.00 96.60           C  
ANISOU 3568  C   ARG A 469    12068  10351  14286  -3283  -3085   2873       C  
ATOM   3569  O   ARG A 469     -39.457 -27.557  25.679  1.00 96.01           O  
ANISOU 3569  O   ARG A 469    12214  10078  14186  -2990  -3185   2452       O  
ATOM   3570  CB  ARG A 469     -42.380 -27.226  26.127  1.00 97.80           C  
ANISOU 3570  CB  ARG A 469    11627  10933  14599  -3688  -3082   3270       C  
ATOM   3571  N   HIS A 480     -23.435 -32.963  35.462  1.00 92.30           N  
ANISOU 3571  N   HIS A 480    14460   7895  12715   -701  -3764   1741       N  
ATOM   3572  CA  HIS A 480     -22.159 -32.333  35.147  1.00 86.68           C  
ANISOU 3572  CA  HIS A 480    13721   7388  11824   -272  -3569   1365       C  
ATOM   3573  C   HIS A 480     -22.035 -30.973  35.822  1.00 78.62           C  
ANISOU 3573  C   HIS A 480    12419   6882  10573   -310  -3059   1414       C  
ATOM   3574  O   HIS A 480     -22.728 -30.023  35.457  1.00 70.65           O  
ANISOU 3574  O   HIS A 480    11199   6140   9504   -404  -2765   1391       O  
ATOM   3575  CB  HIS A 480     -21.992 -32.186  33.634  1.00 89.19           C  
ANISOU 3575  CB  HIS A 480    14070   7655  12163     26  -3624    957       C  
ATOM   3576  CG  HIS A 480     -21.621 -33.460  32.941  1.00 98.46           C  
ANISOU 3576  CG  HIS A 480    15568   8347  13495    251  -4134    766       C  
ATOM   3577  ND1 HIS A 480     -20.834 -34.425  33.531  1.00102.82           N  
ANISOU 3577  ND1 HIS A 480    16304   8691  14072    368  -4400    776       N  
ATOM   3578  CD2 HIS A 480     -21.930 -33.928  31.709  1.00101.14           C  
ANISOU 3578  CD2 HIS A 480    16031   8466  13931    386  -4387    513       C  
ATOM   3579  CE1 HIS A 480     -20.673 -35.432  32.692  1.00106.49           C  
ANISOU 3579  CE1 HIS A 480    16934   8921  14605    551  -4741    508       C  
ATOM   3580  NE2 HIS A 480     -21.328 -35.156  31.579  1.00105.08           N  
ANISOU 3580  NE2 HIS A 480    16724   8742  14460    568  -4742    345       N  
ATOM   3581  N   TRP A 481     -21.144 -30.885  36.810  1.00 79.35           N  
ANISOU 3581  N   TRP A 481    12522   7093  10533   -225  -2981   1472       N  
ATOM   3582  CA  TRP A 481     -20.933 -29.638  37.532  1.00 79.59           C  
ANISOU 3582  CA  TRP A 481    12331   7571  10340   -244  -2555   1502       C  
ATOM   3583  C   TRP A 481     -20.023 -28.667  36.794  1.00 75.68           C  
ANISOU 3583  C   TRP A 481    11722   7314   9718     77  -2334   1133       C  
ATOM   3584  O   TRP A 481     -19.851 -27.534  37.258  1.00 68.75           O  
ANISOU 3584  O   TRP A 481    10670   6781   8671     64  -2005   1124       O  
ATOM   3585  CB  TRP A 481     -20.358 -29.923  38.922  1.00 86.33           C  
ANISOU 3585  CB  TRP A 481    13246   8465  11092   -297  -2582   1724       C  
ATOM   3586  CG  TRP A 481     -19.008 -30.574  38.905  1.00 89.41           C  
ANISOU 3586  CG  TRP A 481    13810   8668  11492     13  -2826   1545       C  
ATOM   3587  CD1 TRP A 481     -18.717 -31.850  38.517  1.00 92.62           C  
ANISOU 3587  CD1 TRP A 481    14468   8648  12076    134  -3255   1503       C  
ATOM   3588  CD2 TRP A 481     -17.765 -29.983  39.304  1.00 90.23           C  
ANISOU 3588  CD2 TRP A 481    13850   9011  11423    256  -2676   1384       C  
ATOM   3589  NE1 TRP A 481     -17.370 -32.088  38.646  1.00 94.82           N  
ANISOU 3589  NE1 TRP A 481    14829   8909  12290    466  -3362   1318       N  
ATOM   3590  CE2 TRP A 481     -16.764 -30.957  39.128  1.00 93.26           C  
ANISOU 3590  CE2 TRP A 481    14424   9129  11882    530  -3007   1256       C  
ATOM   3591  CE3 TRP A 481     -17.402 -28.724  39.789  1.00 87.35           C  
ANISOU 3591  CE3 TRP A 481    13289   9047  10854    270  -2321   1334       C  
ATOM   3592  CZ2 TRP A 481     -15.425 -30.713  39.424  1.00 91.12           C  
ANISOU 3592  CZ2 TRP A 481    14116   9023  11483    807  -2971   1101       C  
ATOM   3593  CZ3 TRP A 481     -16.071 -28.484  40.084  1.00 85.05           C  
ANISOU 3593  CZ3 TRP A 481    12979   8886  10450    513  -2309   1186       C  
ATOM   3594  CH2 TRP A 481     -15.099 -29.472  39.898  1.00 85.23           C  
ANISOU 3594  CH2 TRP A 481    13157   8680  10547    774  -2621   1080       C  
ATOM   3595  N   THR A 482     -19.441 -29.073  35.662  1.00 81.50           N  
ANISOU 3595  N   THR A 482    12553   7889  10525    364  -2519    838       N  
ATOM   3596  CA  THR A 482     -18.592 -28.169  34.896  1.00 79.79           C  
ANISOU 3596  CA  THR A 482    12196   7942  10180    652  -2309    529       C  
ATOM   3597  C   THR A 482     -19.375 -27.005  34.302  1.00 76.05           C  
ANISOU 3597  C   THR A 482    11519   7717   9658    538  -2001    485       C  
ATOM   3598  O   THR A 482     -18.770 -26.000  33.916  1.00 75.39           O  
ANISOU 3598  O   THR A 482    11281   7914   9449    687  -1768    314       O  
ATOM   3599  CB  THR A 482     -17.867 -28.935  33.786  1.00 86.12           C  
ANISOU 3599  CB  THR A 482    13133   8552  11037   1013  -2579    235       C  
ATOM   3600  OG1 THR A 482     -16.755 -28.163  33.315  1.00 89.78           O  
ANISOU 3600  OG1 THR A 482    13438   9334  11342   1305  -2384     -3       O  
ATOM   3601  CG2 THR A 482     -18.806 -29.224  32.622  1.00 87.06           C  
ANISOU 3601  CG2 THR A 482    13310   8493  11277    985  -2706    133       C  
ATOM   3602  N   VAL A 483     -20.703 -27.114  34.225  1.00 71.38           N  
ANISOU 3602  N   VAL A 483    10917   7034   9169    269  -2010    654       N  
ATOM   3603  CA  VAL A 483     -21.498 -25.996  33.732  1.00 62.65           C  
ANISOU 3603  CA  VAL A 483     9616   6169   8017    168  -1724    627       C  
ATOM   3604  C   VAL A 483     -21.697 -24.951  34.822  1.00 56.20           C  
ANISOU 3604  C   VAL A 483     8644   5655   7053     13  -1405    790       C  
ATOM   3605  O   VAL A 483     -21.868 -23.764  34.523  1.00 53.75           O  
ANISOU 3605  O   VAL A 483     8177   5592   6652     31  -1138    699       O  
ATOM   3606  CB  VAL A 483     -22.846 -26.493  33.181  1.00 62.70           C  
ANISOU 3606  CB  VAL A 483     9645   5991   8188    -42  -1864    739       C  
ATOM   3607  CG1 VAL A 483     -22.623 -27.484  32.049  1.00 60.41           C  
ANISOU 3607  CG1 VAL A 483     9541   5384   8028    146  -2212    530       C  
ATOM   3608  CG2 VAL A 483     -23.682 -27.121  34.287  1.00 69.34           C  
ANISOU 3608  CG2 VAL A 483    10514   6730   9102   -371  -1956   1113       C  
ATOM   3609  N   TRP A 484     -21.668 -25.361  36.094  1.00 54.06           N  
ANISOU 3609  N   TRP A 484     8429   5367   6744   -125  -1444   1026       N  
ATOM   3610  CA  TRP A 484     -21.878 -24.411  37.179  1.00 52.40           C  
ANISOU 3610  CA  TRP A 484     8094   5454   6361   -240  -1161   1164       C  
ATOM   3611  C   TRP A 484     -20.735 -23.410  37.280  1.00 52.57           C  
ANISOU 3611  C   TRP A 484     8059   5684   6231    -39   -992    956       C  
ATOM   3612  O   TRP A 484     -20.962 -22.254  37.652  1.00 54.17           O  
ANISOU 3612  O   TRP A 484     8145   6135   6303    -75   -738    947       O  
ATOM   3613  CB  TRP A 484     -22.057 -25.152  38.504  1.00 54.93           C  
ANISOU 3613  CB  TRP A 484     8492   5728   6649   -419  -1258   1475       C  
ATOM   3614  CG  TRP A 484     -23.432 -25.721  38.688  1.00 57.25           C  
ANISOU 3614  CG  TRP A 484     8750   5961   7040   -708  -1319   1776       C  
ATOM   3615  CD1 TRP A 484     -23.780 -27.041  38.682  1.00 60.49           C  
ANISOU 3615  CD1 TRP A 484     9296   6058   7628   -863  -1643   1978       C  
ATOM   3616  CD2 TRP A 484     -24.644 -24.988  38.905  1.00 54.86           C  
ANISOU 3616  CD2 TRP A 484     8252   5927   6665   -881  -1066   1927       C  
ATOM   3617  NE1 TRP A 484     -25.133 -27.175  38.882  1.00 59.16           N  
ANISOU 3617  NE1 TRP A 484     9006   5963   7510  -1158  -1606   2274       N  
ATOM   3618  CE2 TRP A 484     -25.686 -25.929  39.021  1.00 55.55           C  
ANISOU 3618  CE2 TRP A 484     8331   5883   6891  -1158  -1239   2244       C  
ATOM   3619  CE3 TRP A 484     -24.948 -23.627  39.012  1.00 51.52           C  
ANISOU 3619  CE3 TRP A 484     7662   5838   6077   -821   -731   1828       C  
ATOM   3620  CZ2 TRP A 484     -27.010 -25.553  39.240  1.00 55.54           C  
ANISOU 3620  CZ2 TRP A 484     8121   6129   6855  -1369  -1059   2475       C  
ATOM   3621  CZ3 TRP A 484     -26.264 -23.256  39.229  1.00 51.82           C  
ANISOU 3621  CZ3 TRP A 484     7521   6094   6074   -991   -558   2025       C  
ATOM   3622  CH2 TRP A 484     -27.278 -24.216  39.340  1.00 54.39           C  
ANISOU 3622  CH2 TRP A 484     7804   6337   6527  -1260   -708   2350       C  
ATOM   3623  N   ILE A 485     -19.509 -23.828  36.955  1.00 49.97           N  
ANISOU 3623  N   ILE A 485     7808   5261   5917    178  -1147    792       N  
ATOM   3624  CA  ILE A 485     -18.390 -22.890  36.941  1.00 47.27           C  
ANISOU 3624  CA  ILE A 485     7379   5133   5450    347  -1010    616       C  
ATOM   3625  C   ILE A 485     -18.627 -21.804  35.901  1.00 46.91           C  
ANISOU 3625  C   ILE A 485     7189   5242   5393    390   -820    451       C  
ATOM   3626  O   ILE A 485     -18.384 -20.617  36.152  1.00 47.29           O  
ANISOU 3626  O   ILE A 485     7135   5501   5331    378   -625    408       O  
ATOM   3627  CB  ILE A 485     -17.064 -23.633  36.688  1.00 44.67           C  
ANISOU 3627  CB  ILE A 485     7122   4709   5142    591  -1221    485       C  
ATOM   3628  CG1 ILE A 485     -16.670 -24.467  37.907  1.00 49.31           C  
ANISOU 3628  CG1 ILE A 485     7844   5182   5709    553  -1388    658       C  
ATOM   3629  CG2 ILE A 485     -15.955 -22.651  36.349  1.00 40.99           C  
ANISOU 3629  CG2 ILE A 485     6510   4493   4570    755  -1086    309       C  
ATOM   3630  CD1 ILE A 485     -17.127 -25.897  37.831  1.00 54.32           C  
ANISOU 3630  CD1 ILE A 485     8663   5478   6499    518  -1682    769       C  
ATOM   3631  N   THR A 486     -19.114 -22.191  34.720  1.00 44.82           N  
ANISOU 3631  N   THR A 486     6929   4858   5241    438   -898    360       N  
ATOM   3632  CA  THR A 486     -19.400 -21.207  33.681  1.00 37.45           C  
ANISOU 3632  CA  THR A 486     5864   4070   4295    475   -731    225       C  
ATOM   3633  C   THR A 486     -20.550 -20.296  34.087  1.00 36.47           C  
ANISOU 3633  C   THR A 486     5657   4061   4139    276   -520    342       C  
ATOM   3634  O   THR A 486     -20.475 -19.076  33.902  1.00 34.95           O  
ANISOU 3634  O   THR A 486     5359   4048   3870    290   -333    269       O  
ATOM   3635  CB  THR A 486     -19.709 -21.912  32.362  1.00 51.88           C  
ANISOU 3635  CB  THR A 486     7734   5744   6232    583   -888    100       C  
ATOM   3636  OG1 THR A 486     -18.808 -23.013  32.186  1.00 56.66           O  
ANISOU 3636  OG1 THR A 486     8463   6196   6868    786  -1134      8       O  
ATOM   3637  CG2 THR A 486     -19.554 -20.949  31.199  1.00 48.66           C  
ANISOU 3637  CG2 THR A 486     7190   5525   5774    695   -739    -65       C  
ATOM   3638  N   ARG A 487     -21.622 -20.867  34.643  1.00 38.99           N  
ANISOU 3638  N   ARG A 487     6015   4286   4512     94   -558    534       N  
ATOM   3639  CA  ARG A 487     -22.721 -20.047  35.145  1.00 40.09           C  
ANISOU 3639  CA  ARG A 487     6053   4588   4592    -60   -349    658       C  
ATOM   3640  C   ARG A 487     -22.246 -19.125  36.259  1.00 44.43           C  
ANISOU 3640  C   ARG A 487     6584   5332   4965    -47   -185    672       C  
ATOM   3641  O   ARG A 487     -22.577 -17.934  36.280  1.00 49.85           O  
ANISOU 3641  O   ARG A 487     7188   6182   5568    -38      4    614       O  
ATOM   3642  CB  ARG A 487     -23.863 -20.936  35.636  1.00 43.05           C  
ANISOU 3642  CB  ARG A 487     6441   4875   5040   -267   -431    910       C  
ATOM   3643  CG  ARG A 487     -24.408 -21.896  34.593  1.00 52.56           C  
ANISOU 3643  CG  ARG A 487     7689   5844   6437   -311   -649    908       C  
ATOM   3644  CD  ARG A 487     -25.882 -22.180  34.829  1.00 57.98           C  
ANISOU 3644  CD  ARG A 487     8286   6551   7192   -558   -639   1161       C  
ATOM   3645  NE  ARG A 487     -26.321 -23.398  34.155  1.00 58.18           N  
ANISOU 3645  NE  ARG A 487     8404   6284   7419   -656   -942   1222       N  
ATOM   3646  CZ  ARG A 487     -26.667 -24.515  34.787  1.00 59.81           C  
ANISOU 3646  CZ  ARG A 487     8690   6315   7719   -853  -1157   1482       C  
ATOM   3647  NH1 ARG A 487     -26.626 -24.568  36.111  1.00 59.54           N  
ANISOU 3647  NH1 ARG A 487     8638   6413   7572   -963  -1072   1714       N  
ATOM   3648  NH2 ARG A 487     -27.054 -25.579  34.096  1.00 62.33           N  
ANISOU 3648  NH2 ARG A 487     9119   6323   8239   -943  -1478   1517       N  
ATOM   3649  N   PHE A 488     -21.463 -19.663  37.197  1.00 47.30           N  
ANISOU 3649  N   PHE A 488     7040   5664   5268    -35   -281    740       N  
ATOM   3650  CA  PHE A 488     -20.902 -18.841  38.264  1.00 47.24           C  
ANISOU 3650  CA  PHE A 488     7038   5827   5084    -10   -168    733       C  
ATOM   3651  C   PHE A 488     -20.025 -17.731  37.699  1.00 46.38           C  
ANISOU 3651  C   PHE A 488     6877   5803   4942    113   -101    521       C  
ATOM   3652  O   PHE A 488     -20.072 -16.591  38.172  1.00 50.33           O  
ANISOU 3652  O   PHE A 488     7354   6443   5325    111     34    476       O  
ATOM   3653  CB  PHE A 488     -20.110 -19.726  39.229  1.00 48.53           C  
ANISOU 3653  CB  PHE A 488     7314   5923   5202     -6   -324    838       C  
ATOM   3654  CG  PHE A 488     -19.327 -18.968  40.260  1.00 52.01           C  
ANISOU 3654  CG  PHE A 488     7778   6520   5462     40   -260    804       C  
ATOM   3655  CD1 PHE A 488     -19.940 -18.496  41.408  1.00 55.95           C  
ANISOU 3655  CD1 PHE A 488     8287   7187   5786    -33   -130    920       C  
ATOM   3656  CD2 PHE A 488     -17.971 -18.747  40.090  1.00 51.05           C  
ANISOU 3656  CD2 PHE A 488     7663   6399   5336    164   -343    659       C  
ATOM   3657  CE1 PHE A 488     -19.216 -17.806  42.363  1.00 55.52           C  
ANISOU 3657  CE1 PHE A 488     8282   7259   5553     21   -105    865       C  
ATOM   3658  CE2 PHE A 488     -17.242 -18.058  41.038  1.00 54.05           C  
ANISOU 3658  CE2 PHE A 488     8069   6907   5563    185   -322    632       C  
ATOM   3659  CZ  PHE A 488     -17.865 -17.587  42.176  1.00 54.88           C  
ANISOU 3659  CZ  PHE A 488     8219   7139   5494    116   -215    722       C  
ATOM   3660  N   TYR A 489     -19.237 -18.041  36.669  1.00 46.84           N  
ANISOU 3660  N   TYR A 489     6916   5787   5095    226   -205    395       N  
ATOM   3661  CA  TYR A 489     -18.305 -17.057  36.131  1.00 46.15           C  
ANISOU 3661  CA  TYR A 489     6749   5813   4974    318   -156    245       C  
ATOM   3662  C   TYR A 489     -19.035 -15.934  35.403  1.00 45.86           C  
ANISOU 3662  C   TYR A 489     6629   5848   4949    283     -3    184       C  
ATOM   3663  O   TYR A 489     -18.815 -14.752  35.689  1.00 46.69           O  
ANISOU 3663  O   TYR A 489     6709   6051   4979    264     83    142       O  
ATOM   3664  CB  TYR A 489     -17.305 -17.738  35.200  1.00 48.28           C  
ANISOU 3664  CB  TYR A 489     6987   6047   5310    474   -293    146       C  
ATOM   3665  CG  TYR A 489     -16.223 -16.808  34.712  1.00 53.34           C  
ANISOU 3665  CG  TYR A 489     7505   6857   5903    548   -251     48       C  
ATOM   3666  CD1 TYR A 489     -15.151 -16.476  35.529  1.00 57.09           C  
ANISOU 3666  CD1 TYR A 489     7966   7426   6299    553   -291     64       C  
ATOM   3667  CD2 TYR A 489     -16.277 -16.253  33.441  1.00 50.04           C  
ANISOU 3667  CD2 TYR A 489     6976   6520   5518    595   -185    -34       C  
ATOM   3668  CE1 TYR A 489     -14.161 -15.623  35.093  1.00 58.33           C  
ANISOU 3668  CE1 TYR A 489     7987   7749   6427    580   -275     16       C  
ATOM   3669  CE2 TYR A 489     -15.291 -15.398  32.996  1.00 52.56           C  
ANISOU 3669  CE2 TYR A 489     7159   7018   5793    629   -153    -72       C  
ATOM   3670  CZ  TYR A 489     -14.234 -15.087  33.826  1.00 58.84           C  
ANISOU 3670  CZ  TYR A 489     7929   7902   6527    610   -203    -38       C  
ATOM   3671  OH  TYR A 489     -13.245 -14.235  33.394  1.00 61.09           O  
ANISOU 3671  OH  TYR A 489     8056   8375   6782    604   -193    -36       O  
ATOM   3672  N   ILE A 490     -19.906 -16.281  34.451  1.00 44.03           N  
ANISOU 3672  N   ILE A 490     6365   5550   4815    277      4    176       N  
ATOM   3673  CA  ILE A 490     -20.584 -15.252  33.670  1.00 44.02           C  
ANISOU 3673  CA  ILE A 490     6282   5614   4829    260    133    121       C  
ATOM   3674  C   ILE A 490     -21.551 -14.441  34.522  1.00 43.04           C  
ANISOU 3674  C   ILE A 490     6165   5557   4631    177    273    184       C  
ATOM   3675  O   ILE A 490     -21.855 -13.293  34.179  1.00 41.59           O  
ANISOU 3675  O   ILE A 490     5939   5435   4428    187    372    123       O  
ATOM   3676  CB  ILE A 490     -21.309 -15.870  32.459  1.00 42.55           C  
ANISOU 3676  CB  ILE A 490     6064   5347   4758    279     87     96       C  
ATOM   3677  CG1 ILE A 490     -22.428 -16.807  32.915  1.00 45.62           C  
ANISOU 3677  CG1 ILE A 490     6498   5629   5207    168     38    233       C  
ATOM   3678  CG2 ILE A 490     -20.317 -16.598  31.561  1.00 37.44           C  
ANISOU 3678  CG2 ILE A 490     5418   4664   4145    425    -53     -8       C  
ATOM   3679  CD1 ILE A 490     -23.060 -17.595  31.789  1.00 45.55           C  
ANISOU 3679  CD1 ILE A 490     6487   5494   5326    173    -78    208       C  
ATOM   3680  N   ILE A 491     -22.044 -15.003  35.628  1.00 49.19           N  
ANISOU 3680  N   ILE A 491     6996   6341   5354    111    278    312       N  
ATOM   3681  CA  ILE A 491     -22.831 -14.208  36.565  1.00 49.93           C  
ANISOU 3681  CA  ILE A 491     7089   6560   5320     85    420    359       C  
ATOM   3682  C   ILE A 491     -21.955 -13.146  37.216  1.00 49.36           C  
ANISOU 3682  C   ILE A 491     7080   6548   5125    145    435    255       C  
ATOM   3683  O   ILE A 491     -22.377 -11.998  37.401  1.00 52.37           O  
ANISOU 3683  O   ILE A 491     7469   6997   5433    185    528    186       O  
ATOM   3684  CB  ILE A 491     -23.504 -15.117  37.609  1.00 47.26           C  
ANISOU 3684  CB  ILE A 491     6769   6265   4921     -1    423    555       C  
ATOM   3685  CG1 ILE A 491     -24.768 -15.753  37.027  1.00 46.29           C  
ANISOU 3685  CG1 ILE A 491     6554   6122   4914    -96    436    680       C  
ATOM   3686  CG2 ILE A 491     -23.844 -14.337  38.871  1.00 46.91           C  
ANISOU 3686  CG2 ILE A 491     6749   6407   4669     31    554    582       C  
ATOM   3687  CD1 ILE A 491     -25.554 -16.570  38.029  1.00 44.79           C  
ANISOU 3687  CD1 ILE A 491     6341   6013   4665   -222    445    931       C  
ATOM   3688  N   GLY A 492     -20.716 -13.506  37.560  1.00 50.65           N  
ANISOU 3688  N   GLY A 492     7297   6676   5272    158    317    239       N  
ATOM   3689  CA  GLY A 492     -19.777 -12.515  38.054  1.00 52.10           C  
ANISOU 3689  CA  GLY A 492     7531   6898   5367    188    285    145       C  
ATOM   3690  C   GLY A 492     -19.403 -11.484  37.010  1.00 51.37           C  
ANISOU 3690  C   GLY A 492     7378   6788   5352    199    285     38       C  
ATOM   3691  O   GLY A 492     -19.088 -10.340  37.349  1.00 53.56           O  
ANISOU 3691  O   GLY A 492     7705   7075   5570    197    269    -33       O  
ATOM   3692  N   LEU A 493     -19.427 -11.870  35.732  1.00 50.55           N  
ANISOU 3692  N   LEU A 493     7178   6656   5375    209    280     31       N  
ATOM   3693  CA  LEU A 493     -19.193 -10.902  34.665  1.00 48.98           C  
ANISOU 3693  CA  LEU A 493     6904   6470   5237    209    293    -32       C  
ATOM   3694  C   LEU A 493     -20.294  -9.851  34.632  1.00 53.14           C  
ANISOU 3694  C   LEU A 493     7459   6983   5748    204    392    -64       C  
ATOM   3695  O   LEU A 493     -20.026  -8.665  34.405  1.00 63.66           O  
ANISOU 3695  O   LEU A 493     8806   8300   7084    188    370   -113       O  
ATOM   3696  CB  LEU A 493     -19.096 -11.618  33.318  1.00 49.51           C  
ANISOU 3696  CB  LEU A 493     6866   6542   5403    253    275    -36       C  
ATOM   3697  CG  LEU A 493     -17.702 -11.742  32.701  1.00 54.00           C  
ANISOU 3697  CG  LEU A 493     7341   7195   5982    296    190    -52       C  
ATOM   3698  CD1 LEU A 493     -17.755 -12.563  31.421  1.00 53.86           C  
ANISOU 3698  CD1 LEU A 493     7243   7201   6021    396    174    -84       C  
ATOM   3699  CD2 LEU A 493     -17.112 -10.367  32.436  1.00 55.76           C  
ANISOU 3699  CD2 LEU A 493     7507   7485   6195    228    189    -49       C  
ATOM   3700  N   PHE A 494     -21.542 -10.268  34.859  1.00 46.96           N  
ANISOU 3700  N   PHE A 494     6680   6209   4953    219    484    -25       N  
ATOM   3701  CA  PHE A 494     -22.647  -9.317  34.891  1.00 49.00           C  
ANISOU 3701  CA  PHE A 494     6948   6489   5182    256    583    -58       C  
ATOM   3702  C   PHE A 494     -22.553  -8.401  36.105  1.00 55.11           C  
ANISOU 3702  C   PHE A 494     7846   7284   5810    305    582   -121       C  
ATOM   3703  O   PHE A 494     -22.830  -7.200  36.006  1.00 57.67           O  
ANISOU 3703  O   PHE A 494     8222   7572   6117    359    584   -208       O  
ATOM   3704  CB  PHE A 494     -23.981 -10.065  34.881  1.00 51.18           C  
ANISOU 3704  CB  PHE A 494     7155   6818   5472    252    679     29       C  
ATOM   3705  CG  PHE A 494     -25.182  -9.168  34.788  1.00 52.47           C  
ANISOU 3705  CG  PHE A 494     7287   7042   5607    319    789      1       C  
ATOM   3706  CD1 PHE A 494     -25.628  -8.713  33.559  1.00 53.72           C  
ANISOU 3706  CD1 PHE A 494     7375   7162   5876    331    801    -32       C  
ATOM   3707  CD2 PHE A 494     -25.868  -8.783  35.929  1.00 54.83           C  
ANISOU 3707  CD2 PHE A 494     7622   7459   5751    397    879      6       C  
ATOM   3708  CE1 PHE A 494     -26.733  -7.889  33.468  1.00 56.18           C  
ANISOU 3708  CE1 PHE A 494     7653   7528   6165    414    889    -59       C  
ATOM   3709  CE2 PHE A 494     -26.974  -7.958  35.845  1.00 57.92           C  
ANISOU 3709  CE2 PHE A 494     7974   7931   6103    506    978    -34       C  
ATOM   3710  CZ  PHE A 494     -27.407  -7.511  34.612  1.00 59.08           C  
ANISOU 3710  CZ  PHE A 494     8050   8014   6382    512    978    -66       C  
ATOM   3711  N   LEU A 495     -22.165  -8.950  37.259  1.00 55.54           N  
ANISOU 3711  N   LEU A 495     7968   7385   5750    303    556    -85       N  
ATOM   3712  CA  LEU A 495     -22.012  -8.129  38.456  1.00 55.39           C  
ANISOU 3712  CA  LEU A 495     8088   7395   5563    372    532   -166       C  
ATOM   3713  C   LEU A 495     -20.861  -7.142  38.304  1.00 50.25           C  
ANISOU 3713  C   LEU A 495     7516   6631   4948    338    377   -263       C  
ATOM   3714  O   LEU A 495     -20.931  -6.015  38.808  1.00 50.30           O  
ANISOU 3714  O   LEU A 495     7652   6588   4871    403    323   -376       O  
ATOM   3715  CB  LEU A 495     -21.793  -9.020  39.679  1.00 59.22           C  
ANISOU 3715  CB  LEU A 495     8621   7973   5908    367    528    -84       C  
ATOM   3716  CG  LEU A 495     -23.043  -9.599  40.342  1.00 60.44           C  
ANISOU 3716  CG  LEU A 495     8731   8291   5942    408    676     28       C  
ATOM   3717  CD1 LEU A 495     -22.707 -10.889  41.074  1.00 54.80           C  
ANISOU 3717  CD1 LEU A 495     8018   7625   5178    332    641    187       C  
ATOM   3718  CD2 LEU A 495     -23.670  -8.586  41.289  1.00 65.79           C  
ANISOU 3718  CD2 LEU A 495     9501   9096   6401    567    750    -73       C  
ATOM   3719  N   PHE A 496     -19.796  -7.550  37.613  1.00 46.23           N  
ANISOU 3719  N   PHE A 496     6925   6084   4557    241    288   -216       N  
ATOM   3720  CA  PHE A 496     -18.654  -6.665  37.408  1.00 42.67           C  
ANISOU 3720  CA  PHE A 496     6499   5562   4153    167    133   -254       C  
ATOM   3721  C   PHE A 496     -19.016  -5.501  36.494  1.00 40.72           C  
ANISOU 3721  C   PHE A 496     6248   5227   3996    151    121   -293       C  
ATOM   3722  O   PHE A 496     -18.642  -4.353  36.762  1.00 43.83           O  
ANISOU 3722  O   PHE A 496     6754   5515   4383    120    -14   -354       O  
ATOM   3723  CB  PHE A 496     -17.482  -7.465  36.840  1.00 41.62           C  
ANISOU 3723  CB  PHE A 496     6229   5482   4104     95     67   -171       C  
ATOM   3724  CG  PHE A 496     -16.451  -6.629  36.136  1.00 43.73           C  
ANISOU 3724  CG  PHE A 496     6422   5737   4458     -8    -55   -147       C  
ATOM   3725  CD1 PHE A 496     -16.374  -6.620  34.752  1.00 45.06           C  
ANISOU 3725  CD1 PHE A 496     6433   5953   4732    -35    -14    -90       C  
ATOM   3726  CD2 PHE A 496     -15.548  -5.868  36.857  1.00 43.41           C  
ANISOU 3726  CD2 PHE A 496     6458   5653   4382    -89   -225   -162       C  
ATOM   3727  CE1 PHE A 496     -15.422  -5.859  34.101  1.00 43.51           C  
ANISOU 3727  CE1 PHE A 496     6137   5793   4602   -150   -119    -19       C  
ATOM   3728  CE2 PHE A 496     -14.592  -5.105  36.213  1.00 46.07           C  
ANISOU 3728  CE2 PHE A 496     6700   5993   4810   -226   -356    -92       C  
ATOM   3729  CZ  PHE A 496     -14.527  -5.103  34.833  1.00 45.74           C  
ANISOU 3729  CZ  PHE A 496     6479   6031   4869   -261   -293     -5       C  
ATOM   3730  N   LEU A 497     -19.750  -5.777  35.413  1.00 38.12           N  
ANISOU 3730  N   LEU A 497     5804   4922   3756    169    234   -255       N  
ATOM   3731  CA  LEU A 497     -20.161  -4.711  34.506  1.00 40.07           C  
ANISOU 3731  CA  LEU A 497     6047   5090   4087    160    222   -274       C  
ATOM   3732  C   LEU A 497     -21.223  -3.819  35.133  1.00 39.10           C  
ANISOU 3732  C   LEU A 497     6072   4898   3888    282    247   -382       C  
ATOM   3733  O   LEU A 497     -21.232  -2.607  34.890  1.00 46.92           O  
ANISOU 3733  O   LEU A 497     7155   5755   4918    281    142   -432       O  
ATOM   3734  CB  LEU A 497     -20.666  -5.308  33.194  1.00 43.97           C  
ANISOU 3734  CB  LEU A 497     6382   5647   4677    161    327   -209       C  
ATOM   3735  CG  LEU A 497     -19.596  -6.048  32.391  1.00 43.48           C  
ANISOU 3735  CG  LEU A 497     6175   5674   4672     94    290   -130       C  
ATOM   3736  CD1 LEU A 497     -20.224  -6.915  31.315  1.00 39.73           C  
ANISOU 3736  CD1 LEU A 497     5584   5263   4251    143    384   -105       C  
ATOM   3737  CD2 LEU A 497     -18.610  -5.063  31.787  1.00 43.81           C  
ANISOU 3737  CD2 LEU A 497     6169   5710   4766    -16    174    -72       C  
ATOM   3738  N   THR A 498     -22.124  -4.393  35.935  1.00 38.77           N  
ANISOU 3738  N   THR A 498     6050   4953   3728    397    374   -408       N  
ATOM   3739  CA  THR A 498     -23.061  -3.575  36.698  1.00 44.96           C  
ANISOU 3739  CA  THR A 498     6964   5732   4387    566    406   -524       C  
ATOM   3740  C   THR A 498     -22.326  -2.638  37.647  1.00 56.38           C  
ANISOU 3740  C   THR A 498     8622   7062   5739    595    225   -646       C  
ATOM   3741  O   THR A 498     -22.777  -1.511  37.886  1.00 62.13           O  
ANISOU 3741  O   THR A 498     9502   7685   6418    726    152   -779       O  
ATOM   3742  CB  THR A 498     -24.028  -4.469  37.479  1.00 41.99           C  
ANISOU 3742  CB  THR A 498     6530   5552   3870    666    581   -484       C  
ATOM   3743  OG1 THR A 498     -24.659  -5.396  36.586  1.00 43.35           O  
ANISOU 3743  OG1 THR A 498     6516   5800   4156    602    699   -360       O  
ATOM   3744  CG2 THR A 498     -25.097  -3.638  38.172  1.00 43.19           C  
ANISOU 3744  CG2 THR A 498     6771   5774   3864    888    646   -602       C  
ATOM   3745  N   PHE A 499     -21.186  -3.079  38.182  1.00 57.50           N  
ANISOU 3745  N   PHE A 499     8786   7207   5855    486    125   -611       N  
ATOM   3746  CA  PHE A 499     -20.413  -2.242  39.094  1.00 54.23           C  
ANISOU 3746  CA  PHE A 499     8574   6675   5357    490    -84   -722       C  
ATOM   3747  C   PHE A 499     -19.815  -1.041  38.372  1.00 49.41           C  
ANISOU 3747  C   PHE A 499     8029   5843   4900    375   -296   -739       C  
ATOM   3748  O   PHE A 499     -19.848   0.080  38.892  1.00 50.25           O  
ANISOU 3748  O   PHE A 499     8356   5779   4958    449   -473   -880       O  
ATOM   3749  CB  PHE A 499     -19.318  -3.077  39.759  1.00 52.84           C  
ANISOU 3749  CB  PHE A 499     8372   6573   5131    386   -147   -655       C  
ATOM   3750  CG  PHE A 499     -18.465  -2.308  40.725  1.00 49.92           C  
ANISOU 3750  CG  PHE A 499     8202   6091   4673    370   -386   -761       C  
ATOM   3751  CD1 PHE A 499     -19.029  -1.686  41.826  1.00 53.99           C  
ANISOU 3751  CD1 PHE A 499     8940   6589   4984    565   -428   -936       C  
ATOM   3752  CD2 PHE A 499     -17.097  -2.213  40.536  1.00 52.08           C  
ANISOU 3752  CD2 PHE A 499     8434   6298   5056    172   -580   -686       C  
ATOM   3753  CE1 PHE A 499     -18.244  -0.980  42.719  1.00 57.59           C  
ANISOU 3753  CE1 PHE A 499     9608   6921   5351    559   -685  -1056       C  
ATOM   3754  CE2 PHE A 499     -16.306  -1.509  41.426  1.00 56.20           C  
ANISOU 3754  CE2 PHE A 499     9139   6706   5510    133   -835   -775       C  
ATOM   3755  CZ  PHE A 499     -16.881  -0.892  42.519  1.00 57.90           C  
ANISOU 3755  CZ  PHE A 499     9611   6863   5527    325   -900   -971       C  
ATOM   3756  N   LEU A 500     -19.267  -1.253  37.170  1.00 45.63           N  
ANISOU 3756  N   LEU A 500     7371   5368   4601    200   -296   -589       N  
ATOM   3757  CA  LEU A 500     -18.681  -0.144  36.421  1.00 48.22           C  
ANISOU 3757  CA  LEU A 500     7728   5517   5076     52   -496   -543       C  
ATOM   3758  C   LEU A 500     -19.746   0.824  35.923  1.00 48.95           C  
ANISOU 3758  C   LEU A 500     7920   5467   5211    166   -497   -617       C  
ATOM   3759  O   LEU A 500     -19.501   2.033  35.869  1.00 52.57           O  
ANISOU 3759  O   LEU A 500     8541   5695   5737    115   -729   -654       O  
ATOM   3760  CB  LEU A 500     -17.856  -0.662  35.243  1.00 42.92           C  
ANISOU 3760  CB  LEU A 500     6805   4960   4543   -137   -467   -345       C  
ATOM   3761  CG  LEU A 500     -16.868  -1.789  35.526  1.00 41.94           C  
ANISOU 3761  CG  LEU A 500     6536   5013   4385   -206   -438   -265       C  
ATOM   3762  CD1 LEU A 500     -16.181  -2.191  34.235  1.00 36.92           C  
ANISOU 3762  CD1 LEU A 500     5647   4522   3860   -328   -399    -94       C  
ATOM   3763  CD2 LEU A 500     -15.854  -1.370  36.577  1.00 48.45           C  
ANISOU 3763  CD2 LEU A 500     7482   5764   5163   -294   -663   -295       C  
ATOM   3764  N   VAL A 501     -20.921   0.317  35.545  1.00 43.05           N  
ANISOU 3764  N   VAL A 501     7080   4840   4436    314   -267   -631       N  
ATOM   3765  CA  VAL A 501     -22.035   1.206  35.226  1.00 46.59           C  
ANISOU 3765  CA  VAL A 501     7625   5179   4899    473   -261   -721       C  
ATOM   3766  C   VAL A 501     -22.404   2.037  36.449  1.00 52.61           C  
ANISOU 3766  C   VAL A 501     8657   5822   5512    681   -382   -934       C  
ATOM   3767  O   VAL A 501     -22.741   3.223  36.341  1.00 59.57           O  
ANISOU 3767  O   VAL A 501     9719   6485   6428    775   -547  -1037       O  
ATOM   3768  CB  VAL A 501     -23.235   0.392  34.704  1.00 45.80           C  
ANISOU 3768  CB  VAL A 501     7346   5272   4784    589      7   -685       C  
ATOM   3769  CG1 VAL A 501     -24.472   1.264  34.583  1.00 43.83           C  
ANISOU 3769  CG1 VAL A 501     7184   4953   4514    804     26   -795       C  
ATOM   3770  CG2 VAL A 501     -22.904  -0.251  33.365  1.00 35.35           C  
ANISOU 3770  CG2 VAL A 501     5800   4026   3604    417     77   -511       C  
ATOM   3771  N   PHE A 502     -22.338   1.424  37.633  1.00 55.71           N  
ANISOU 3771  N   PHE A 502     9093   6353   5720    774   -317  -1009       N  
ATOM   3772  CA  PHE A 502     -22.540   2.169  38.871  1.00 54.28           C  
ANISOU 3772  CA  PHE A 502     9180   6092   5352    990   -447  -1227       C  
ATOM   3773  C   PHE A 502     -21.454   3.222  39.058  1.00 50.41           C  
ANISOU 3773  C   PHE A 502     8915   5296   4943    856   -809  -1287       C  
ATOM   3774  O   PHE A 502     -21.744   4.361  39.442  1.00 54.21           O  
ANISOU 3774  O   PHE A 502     9660   5555   5380   1021  -1015  -1474       O  
ATOM   3775  CB  PHE A 502     -22.572   1.200  40.055  1.00 57.32           C  
ANISOU 3775  CB  PHE A 502     9541   6726   5512   1082   -302  -1250       C  
ATOM   3776  CG  PHE A 502     -22.681   1.871  41.395  1.00 67.40           C  
ANISOU 3776  CG  PHE A 502    11091   7971   6546   1322   -433  -1481       C  
ATOM   3777  CD1 PHE A 502     -23.921   2.173  41.933  1.00 72.23           C  
ANISOU 3777  CD1 PHE A 502    11768   8724   6952   1663   -302  -1633       C  
ATOM   3778  CD2 PHE A 502     -21.546   2.180  42.128  1.00 67.02           C  
ANISOU 3778  CD2 PHE A 502    11225   7780   6458   1225   -691  -1547       C  
ATOM   3779  CE1 PHE A 502     -24.026   2.783  43.170  1.00 70.41           C  
ANISOU 3779  CE1 PHE A 502    11797   8498   6459   1934   -421  -1870       C  
ATOM   3780  CE2 PHE A 502     -21.645   2.791  43.363  1.00 67.28           C  
ANISOU 3780  CE2 PHE A 502    11534   7782   6247   1467   -833  -1784       C  
ATOM   3781  CZ  PHE A 502     -22.887   3.092  43.885  1.00 69.43           C  
ANISOU 3781  CZ  PHE A 502    11885   8202   6292   1837   -695  -1955       C  
ATOM   3782  N   LEU A 503     -20.196   2.860  38.789  1.00 45.82           N  
ANISOU 3782  N   LEU A 503     8230   4698   4481    562   -911  -1127       N  
ATOM   3783  CA  LEU A 503     -19.103   3.819  38.928  1.00 49.89           C  
ANISOU 3783  CA  LEU A 503     8917   4943   5097    376  -1275  -1131       C  
ATOM   3784  C   LEU A 503     -19.228   4.953  37.920  1.00 54.95           C  
ANISOU 3784  C   LEU A 503     9625   5318   5936    286  -1458  -1080       C  
ATOM   3785  O   LEU A 503     -19.037   6.125  38.268  1.00 57.92           O  
ANISOU 3785  O   LEU A 503    10280   5383   6345    295  -1785  -1196       O  
ATOM   3786  CB  LEU A 503     -17.755   3.116  38.767  1.00 50.40           C  
ANISOU 3786  CB  LEU A 503     8787   5116   5245     83  -1316   -932       C  
ATOM   3787  CG  LEU A 503     -17.427   1.960  39.713  1.00 50.17           C  
ANISOU 3787  CG  LEU A 503     8690   5323   5048    131  -1183   -945       C  
ATOM   3788  CD1 LEU A 503     -16.066   1.372  39.374  1.00 53.86           C  
ANISOU 3788  CD1 LEU A 503     8948   5888   5627   -142  -1247   -742       C  
ATOM   3789  CD2 LEU A 503     -17.475   2.414  41.160  1.00 49.14           C  
ANISOU 3789  CD2 LEU A 503     8854   5110   4709    307  -1345  -1171       C  
ATOM   3790  N   ALA A 504     -19.545   4.625  36.664  1.00 57.57           N  
ANISOU 3790  N   ALA A 504     9720   5754   6400    199  -1275   -904       N  
ATOM   3791  CA  ALA A 504     -19.674   5.653  35.637  1.00 54.97           C  
ANISOU 3791  CA  ALA A 504     9435   5198   6255    101  -1438   -816       C  
ATOM   3792  C   ALA A 504     -20.839   6.591  35.921  1.00 58.53           C  
ANISOU 3792  C   ALA A 504    10147   5442   6649    404  -1514  -1041       C  
ATOM   3793  O   ALA A 504     -20.817   7.751  35.494  1.00 65.18           O  
ANISOU 3793  O   ALA A 504    11166   5973   7626    351  -1787  -1033       O  
ATOM   3794  CB  ALA A 504     -19.837   5.005  34.263  1.00 50.89           C  
ANISOU 3794  CB  ALA A 504     8605   4885   5845    -15  -1202   -595       C  
ATOM   3795  N   GLU A 505     -21.861   6.112  36.632  1.00 58.83           N  
ANISOU 3795  N   GLU A 505    10207   5661   6486    727  -1285  -1228       N  
ATOM   3796  CA  GLU A 505     -22.973   6.981  36.998  1.00 65.76           C  
ANISOU 3796  CA  GLU A 505    11317   6399   7271   1076  -1345  -1463       C  
ATOM   3797  C   GLU A 505     -22.585   7.946  38.111  1.00 71.63           C  
ANISOU 3797  C   GLU A 505    12436   6861   7920   1199  -1693  -1700       C  
ATOM   3798  O   GLU A 505     -23.108   9.063  38.172  1.00 78.95           O  
ANISOU 3798  O   GLU A 505    13632   7511   8856   1409  -1915  -1876       O  
ATOM   3799  CB  GLU A 505     -24.180   6.141  37.415  1.00 68.05           C  
ANISOU 3799  CB  GLU A 505    11463   7037   7356   1377   -981  -1554       C  
ATOM   3800  CG  GLU A 505     -25.458   6.940  37.601  1.00 77.92           C  
ANISOU 3800  CG  GLU A 505    12866   8235   8503   1771   -980  -1767       C  
ATOM   3801  CD  GLU A 505     -26.575   6.117  38.210  1.00 89.04           C  
ANISOU 3801  CD  GLU A 505    14111  10045   9675   2060   -632  -1835       C  
ATOM   3802  OE1 GLU A 505     -27.603   6.707  38.601  1.00 95.67           O  
ANISOU 3802  OE1 GLU A 505    15059  10923  10367   2438   -610  -2031       O  
ATOM   3803  OE2 GLU A 505     -26.426   4.879  38.296  1.00 90.62           O  
ANISOU 3803  OE2 GLU A 505    14068  10530   9834   1912   -390  -1681       O  
ATOM   3804  N   ARG A 506     -21.670   7.538  38.993  1.00 73.08           N  
ANISOU 3804  N   ARG A 506    12660   7097   8010   1087  -1770  -1719       N  
ATOM   3805  CA  ARG A 506     -21.219   8.424  40.060  1.00 82.60           C  
ANISOU 3805  CA  ARG A 506    14236   8027   9120   1186  -2137  -1951       C  
ATOM   3806  C   ARG A 506     -20.257   9.490  39.551  1.00 90.06           C  
ANISOU 3806  C   ARG A 506    15349   8545  10323    873  -2583  -1849       C  
ATOM   3807  O   ARG A 506     -20.228  10.600  40.096  1.00 96.64           O  
ANISOU 3807  O   ARG A 506    16557   9018  11144    999  -2963  -2062       O  
ATOM   3808  CB  ARG A 506     -20.560   7.617  41.178  1.00 82.07           C  
ANISOU 3808  CB  ARG A 506    14151   8171   8860   1163  -2084  -1992       C  
ATOM   3809  CG  ARG A 506     -20.604   8.289  42.540  1.00 88.42           C  
ANISOU 3809  CG  ARG A 506    15336   8834   9427   1451  -2336  -2321       C  
ATOM   3810  CD  ARG A 506     -19.293   8.989  42.862  1.00 90.25           C  
ANISOU 3810  CD  ARG A 506    15765   8735   9791   1171  -2793  -2302       C  
ATOM   3811  NE  ARG A 506     -19.458   9.993  43.909  1.00 95.25           N  
ANISOU 3811  NE  ARG A 506    16635   9228  10328   1431  -3025  -2493       N  
ATOM   3812  CZ  ARG A 506     -18.727  11.098  44.012  1.00100.76           C  
ANISOU 3812  CZ  ARG A 506    17535   9556  11195   1278  -3463  -2479       C  
ATOM   3813  NH1 ARG A 506     -17.771  11.351  43.128  1.00102.78           N  
ANISOU 3813  NH1 ARG A 506    17744   9574  11736    837  -3703  -2246       N  
ATOM   3814  NH2 ARG A 506     -18.952  11.952  45.000  1.00103.44           N  
ANISOU 3814  NH2 ARG A 506    18109   9781  11414   1561  -3668  -2678       N  
ATOM   3815  N   ARG A 507     -19.471   9.179  38.515  1.00 90.72           N  
ANISOU 3815  N   ARG A 507    15164   8671  10634    471  -2560  -1519       N  
ATOM   3816  CA  ARG A 507     -18.594  10.190  37.932  1.00 93.00           C  
ANISOU 3816  CA  ARG A 507    15561   8598  11176    134  -2971  -1352       C  
ATOM   3817  C   ARG A 507     -19.403  11.308  37.291  1.00 97.00           C  
ANISOU 3817  C   ARG A 507    16272   8781  11804    263  -3147  -1407       C  
ATOM   3818  O   ARG A 507     -19.013  12.481  37.348  1.00104.53           O  
ANISOU 3818  O   ARG A 507    17522   9298  12895    154  -3606  -1432       O  
ATOM   3819  CB  ARG A 507     -17.655   9.551  36.910  1.00 89.76           C  
ANISOU 3819  CB  ARG A 507    14764   8400  10940   -284  -2851   -967       C  
ATOM   3820  N   ARG A 508     -20.536  10.967  36.686  1.00 92.73           N  
ANISOU 3820  N   ARG A 508    15583   8431  11219    493  -2815  -1422       N  
ATOM   3821  CA  ARG A 508     -21.421  11.958  36.086  1.00 91.43           C  
ANISOU 3821  CA  ARG A 508    15595   7993  11150    670  -2952  -1486       C  
ATOM   3822  C   ARG A 508     -22.286  12.626  37.150  1.00 92.96           C  
ANISOU 3822  C   ARG A 508    16148   8024  11149   1151  -3083  -1885       C  
ATOM   3823  O   ARG A 508     -22.207  13.837  37.359  1.00 95.17           O  
ANISOU 3823  O   ARG A 508    16635   8023  11503   1189  -3430  -1920       O  
ATOM   3824  CB  ARG A 508     -22.306  11.312  35.016  1.00 84.62           C  
ANISOU 3824  CB  ARG A 508    14412   7429  10310    735  -2552  -1342       C  
TER    3825      ARG A 508                                                      
HETATM 3826  N   LEU A 601     -23.116 -11.898  12.585  1.00 51.21           N  
HETATM 3827  CA  LEU A 601     -22.035 -12.580  13.288  1.00 52.18           C  
HETATM 3828  C   LEU A 601     -21.762 -13.947  12.675  1.00 56.58           C  
HETATM 3829  O   LEU A 601     -22.640 -14.544  12.053  1.00 56.84           O  
HETATM 3830  CB  LEU A 601     -22.370 -12.727  14.773  1.00 48.66           C  
HETATM 3831  CG  LEU A 601     -21.467 -11.975  15.751  1.00 47.67           C  
HETATM 3832  CD1 LEU A 601     -21.964 -12.150  17.177  1.00 47.96           C  
HETATM 3833  CD2 LEU A 601     -21.387 -10.502  15.384  1.00 51.16           C  
HETATM 3834  OXT LEU A 601     -20.662 -14.488  12.790  1.00 60.08           O  
HETATM 3835 NA    NA A 602     -17.262 -10.374  10.111  1.00 42.05          NA  
HETATM 3836 NA    NA A 603     -24.235 -13.404   9.927  1.00 40.14          NA  
HETATM 3837  C1  GOL A 604     -48.319  -0.520  24.267  1.00 69.31           C  
HETATM 3838  O1  GOL A 604     -47.677   0.410  23.423  1.00 70.60           O  
HETATM 3839  C2  GOL A 604     -48.902  -1.651  23.427  1.00 68.53           C  
HETATM 3840  O2  GOL A 604     -48.150  -1.791  22.242  1.00 66.48           O  
HETATM 3841  C3  GOL A 604     -48.852  -2.953  24.219  1.00 68.95           C  
HETATM 3842  O3  GOL A 604     -49.377  -4.002  23.436  1.00 68.95           O  
HETATM 3843  C1  GOL A 605      -8.387 -18.356  -5.432  1.00 78.55           C  
HETATM 3844  O1  GOL A 605      -9.045 -17.110  -5.458  1.00 78.94           O  
HETATM 3845  C2  GOL A 605      -7.752 -18.627  -6.791  1.00 79.02           C  
HETATM 3846  O2  GOL A 605      -6.786 -17.638  -7.065  1.00 80.21           O  
HETATM 3847  C3  GOL A 605      -7.080 -19.995  -6.771  1.00 78.33           C  
HETATM 3848  O3  GOL A 605      -6.427 -20.215  -8.001  1.00 78.87           O  
HETATM 3849  C1  PEG A 606      -0.494 -10.330  12.271  1.00 63.46           C  
HETATM 3850  O1  PEG A 606      -0.130 -11.403  11.447  1.00 61.74           O  
HETATM 3851  C2  PEG A 606       0.232  -9.064  11.818  1.00 61.80           C  
HETATM 3852  O2  PEG A 606      -0.184  -7.981  12.601  1.00 59.35           O  
HETATM 3853  C3  PEG A 606       0.308  -6.744  12.168  1.00 56.24           C  
HETATM 3854  C4  PEG A 606      -0.151  -5.650  13.130  1.00 56.15           C  
HETATM 3855  O4  PEG A 606       0.294  -4.405  12.667  1.00 57.14           O  
HETATM 3856  C1  PEG A 607      -4.071 -10.696   8.544  1.00 65.35           C  
HETATM 3857  O1  PEG A 607      -3.648 -11.967   8.957  1.00 63.45           O  
HETATM 3858  C2  PEG A 607      -4.352  -9.827   9.768  1.00 69.94           C  
HETATM 3859  O2  PEG A 607      -4.363  -8.477   9.397  1.00 70.71           O  
HETATM 3860  C3  PEG A 607      -4.549  -7.597  10.468  1.00 68.90           C  
HETATM 3861  C4  PEG A 607      -3.905  -6.250  10.145  1.00 66.91           C  
HETATM 3862  O4  PEG A 607      -4.132  -5.356  11.199  1.00 63.84           O  
HETATM 3863  C1  PEG A 608       0.168   2.610   8.721  1.00 76.45           C  
HETATM 3864  O1  PEG A 608       1.124   1.588   8.794  1.00 75.37           O  
HETATM 3865  C2  PEG A 608       0.382   3.593   9.871  1.00 78.03           C  
HETATM 3866  O2  PEG A 608       0.156   2.941  11.089  1.00 79.36           O  
HETATM 3867  C3  PEG A 608       0.708   3.595  12.196  1.00 79.29           C  
HETATM 3868  C4  PEG A 608       0.588   2.705  13.432  1.00 79.49           C  
HETATM 3869  O4  PEG A 608       1.633   1.771  13.445  1.00 79.75           O  
HETATM 3870  C   TRS A 609      -5.146   2.435   3.212  1.00 99.64           C  
HETATM 3871  C1  TRS A 609      -4.915   0.953   2.943  1.00100.15           C  
HETATM 3872  C2  TRS A 609      -6.639   2.742   3.256  1.00 98.92           C  
HETATM 3873  C3  TRS A 609      -4.487   3.278   2.128  1.00 98.33           C  
HETATM 3874  N   TRS A 609      -4.546   2.778   4.505  1.00 99.53           N  
HETATM 3875  O1  TRS A 609      -5.731   0.183   3.797  1.00 99.07           O  
HETATM 3876  O2  TRS A 609      -7.380   1.569   3.001  1.00 98.65           O  
HETATM 3877  O3  TRS A 609      -5.216   3.141   0.929  1.00 96.58           O  
HETATM 3878  C   TRS A 610       1.372   4.072  29.050  1.00 79.62           C  
HETATM 3879  C1  TRS A 610       1.011   4.459  30.479  1.00 82.32           C  
HETATM 3880  C2  TRS A 610       1.288   5.292  28.141  1.00 77.85           C  
HETATM 3881  C3  TRS A 610       2.772   3.470  29.000  1.00 78.45           C  
HETATM 3882  N   TRS A 610       0.411   3.071  28.581  1.00 78.94           N  
HETATM 3883  O1  TRS A 610      -0.274   5.039  30.496  1.00 83.30           O  
HETATM 3884  O2  TRS A 610       0.056   5.946  28.347  1.00 75.42           O  
HETATM 3885  O3  TRS A 610       3.715   4.428  29.427  1.00 75.20           O  
HETATM 3886  C1  BOG A 611      -0.872 -24.631  28.348  1.00106.71           C  
HETATM 3887  O1  BOG A 611      -1.150 -23.296  28.415  1.00 95.80           O  
HETATM 3888  C2  BOG A 611      -2.033 -25.374  27.690  1.00112.12           C  
HETATM 3889  O2  BOG A 611      -2.382 -26.510  28.507  1.00114.93           O  
HETATM 3890  C3  BOG A 611      -1.748 -25.854  26.307  1.00113.86           C  
HETATM 3891  O3  BOG A 611      -1.740 -24.713  25.412  1.00114.15           O  
HETATM 3892  C4  BOG A 611      -0.449 -26.596  26.148  1.00115.48           C  
HETATM 3893  O4  BOG A 611      -0.698 -28.005  26.201  1.00116.87           O  
HETATM 3894  C5  BOG A 611       0.586 -26.232  27.214  1.00113.84           C  
HETATM 3895  O5  BOG A 611       0.431 -24.829  27.628  1.00111.19           O  
HETATM 3896  C6  BOG A 611       1.962 -26.450  26.661  1.00113.31           C  
HETATM 3897  O6  BOG A 611       2.117 -27.804  26.331  1.00112.10           O  
HETATM 3898  C1' BOG A 611      -1.367 -22.847  29.726  1.00 87.17           C  
HETATM 3899  C2' BOG A 611      -1.166 -21.330  29.799  1.00 82.05           C  
HETATM 3900  C3' BOG A 611      -1.802 -20.804  31.082  1.00 81.33           C  
HETATM 3901  C4' BOG A 611      -1.699 -19.282  31.129  1.00 82.48           C  
HETATM 3902  C5' BOG A 611      -2.790 -18.735  32.039  1.00 82.59           C  
HETATM 3903  C6' BOG A 611      -2.845 -17.218  31.928  1.00 79.32           C  
HETATM 3904  C7' BOG A 611      -3.955 -16.678  32.828  1.00 74.31           C  
HETATM 3905  C8' BOG A 611      -4.036 -15.158  32.683  1.00 71.15           C  
HETATM 3906  C1  OCT A 612      -9.428 -23.722  34.486  1.00 61.93           C  
HETATM 3907  C2  OCT A 612      -9.197 -25.195  34.811  1.00 61.21           C  
HETATM 3908  C3  OCT A 612      -7.900 -25.667  34.160  1.00 62.56           C  
HETATM 3909  C4  OCT A 612      -7.662 -27.126  34.541  1.00 66.02           C  
HETATM 3910  C5  OCT A 612      -6.256 -27.558  34.138  1.00 71.46           C  
HETATM 3911  C6  OCT A 612      -6.067 -29.057  34.351  1.00 70.13           C  
HETATM 3912  C7  OCT A 612      -4.607 -29.417  34.083  1.00 69.89           C  
HETATM 3913  C8  OCT A 612      -4.102 -30.382  35.154  1.00 68.93           C  
HETATM 3914  C1  OCT A 613      -5.190 -22.240  33.246  1.00 69.34           C  
HETATM 3915  C2  OCT A 613      -4.711 -23.504  32.538  1.00 70.74           C  
HETATM 3916  C3  OCT A 613      -3.555 -24.120  33.324  1.00 71.81           C  
HETATM 3917  C4  OCT A 613      -3.624 -25.640  33.221  1.00 70.91           C  
HETATM 3918  C5  OCT A 613      -2.395 -26.187  32.503  1.00 73.35           C  
HETATM 3919  C6  OCT A 613      -1.168 -25.938  33.376  1.00 76.56           C  
HETATM 3920  C7  OCT A 613      -0.162 -27.079  33.227  1.00 76.38           C  
HETATM 3921  C8  OCT A 613      -0.031 -27.474  31.758  1.00 77.11           C  
HETATM 3922  O   HOH A 701     -15.132 -25.726  26.421  1.00 48.59           O  
HETATM 3923  O   HOH A 702     -30.013 -38.775   8.047  1.00 60.43           O  
HETATM 3924  O   HOH A 703     -21.537 -29.918  11.733  1.00 68.82           O  
HETATM 3925  O   HOH A 704     -21.433 -25.596   9.419  1.00 65.29           O  
HETATM 3926  O   HOH A 705     -36.211 -30.135   0.507  1.00 56.14           O  
HETATM 3927  O   HOH A 706     -19.862 -25.322   7.358  1.00 57.54           O  
HETATM 3928  O   HOH A 707     -12.854   2.905  19.546  1.00 48.44           O  
HETATM 3929  O   HOH A 708     -21.035 -22.865   4.270  1.00 48.49           O  
HETATM 3930  O   HOH A 709      -3.715   2.683  -1.028  1.00 74.05           O  
HETATM 3931  O   HOH A 710     -11.531 -43.120  15.961  1.00 78.78           O  
HETATM 3932  O   HOH A 711     -19.960 -26.797  10.773  1.00 55.05           O  
HETATM 3933  O   HOH A 712     -11.584   0.901  18.566  1.00 41.31           O  
HETATM 3934  O   HOH A 713     -16.751  -4.958  11.779  1.00 45.33           O  
HETATM 3935  O   HOH A 714     -16.021   5.181  21.845  1.00 82.34           O  
HETATM 3936  O   HOH A 715     -23.907 -24.717   2.996  1.00 78.30           O  
HETATM 3937  O   HOH A 716      -6.876 -21.751  18.434  1.00 53.00           O  
HETATM 3938  O   HOH A 717      -6.956   6.308  29.994  1.00 38.48           O  
HETATM 3939  O   HOH A 718     -25.709   6.182  11.947  1.00 57.27           O  
HETATM 3940  O   HOH A 719      -9.408   9.010  17.654  1.00 63.70           O  
HETATM 3941  O   HOH A 720      -4.312 -37.101  16.346  1.00 56.61           O  
HETATM 3942  O   HOH A 721     -10.413 -26.089  23.756  1.00 46.39           O  
HETATM 3943  O   HOH A 722     -38.486  10.885   1.233  1.00 46.58           O  
HETATM 3944  O   HOH A 723     -15.919 -39.578  19.123  1.00 67.44           O  
HETATM 3945  O   HOH A 724     -21.464   4.554  25.701  1.00 58.01           O  
HETATM 3946  O   HOH A 725      -5.468  -1.157   9.200  1.00 56.67           O  
HETATM 3947  O   HOH A 726     -12.703   9.024  14.124  1.00 62.10           O  
HETATM 3948  O   HOH A 727     -10.916   6.403  14.146  1.00 50.72           O  
HETATM 3949  O   HOH A 728      -8.267 -30.725   2.445  1.00 54.99           O  
HETATM 3950  O   HOH A 729     -15.270   9.192  23.727  1.00 54.21           O  
HETATM 3951  O   HOH A 730      -5.420 -32.371  -1.406  1.00 57.94           O  
HETATM 3952  O   HOH A 731     -21.681  11.772  10.592  1.00 35.51           O  
HETATM 3953  O   HOH A 732     -31.720 -33.713  -3.518  1.00 50.48           O  
HETATM 3954  O   HOH A 733     -44.743   8.635  20.765  1.00 44.96           O  
HETATM 3955  O   HOH A 734     -29.831 -17.761  18.907  1.00 38.80           O  
HETATM 3956  O   HOH A 735     -20.021   9.538   2.531  1.00 52.26           O  
HETATM 3957  O   HOH A 736     -35.291  14.048   6.983  1.00 61.90           O  
HETATM 3958  O   HOH A 737     -35.480   5.458  38.863  1.00 47.73           O  
HETATM 3959  O   HOH A 738     -24.694 -24.382  15.115  1.00 50.17           O  
HETATM 3960  O   HOH A 739     -47.015   0.103   3.856  1.00 51.55           O  
HETATM 3961  O   HOH A 740     -38.010 -17.754  20.378  1.00 62.57           O  
HETATM 3962  O   HOH A 741     -26.315   6.757   4.342  1.00 44.11           O  
HETATM 3963  O   HOH A 742     -15.438   7.153  20.612  1.00 56.44           O  
HETATM 3964  O   HOH A 743      -1.609 -28.193  16.627  1.00 54.31           O  
HETATM 3965  O   HOH A 744       0.002 -14.765  11.162  1.00 53.36           O  
HETATM 3966  O   HOH A 745     -23.829   4.640  31.842  1.00 46.98           O  
HETATM 3967  O   HOH A 746     -46.830   3.896  22.781  1.00 48.29           O  
HETATM 3968  O   HOH A 747     -26.638   1.868  -0.290  1.00 53.62           O  
HETATM 3969  O   HOH A 748     -25.607 -23.404  18.213  1.00 41.90           O  
HETATM 3970  O   HOH A 749       0.027 -31.931  11.879  1.00 61.51           O  
HETATM 3971  O   HOH A 750     -40.331 -33.401  14.810  1.00 77.22           O  
HETATM 3972  O   HOH A 751     -10.477  -0.189  -3.511  1.00 69.39           O  
HETATM 3973  O   HOH A 752     -27.843 -26.053  28.502  1.00 65.82           O  
HETATM 3974  O   HOH A 753      -1.856 -34.576  10.800  1.00 52.68           O  
HETATM 3975  O   HOH A 754       0.350 -16.426  29.398  1.00 60.81           O  
HETATM 3976  O   HOH A 755      -5.369 -12.069  31.625  1.00 75.17           O  
HETATM 3977  O   HOH A 756     -11.905 -27.583 -11.162  1.00 48.77           O  
HETATM 3978  O   HOH A 757       5.690 -26.261  26.631  1.00 53.42           O  
HETATM 3979  O   HOH A 758     -22.676 -25.008  20.018  1.00 37.43           O  
HETATM 3980  O   HOH A 759     -28.758   8.791   1.486  1.00 59.87           O  
HETATM 3981  O   HOH A 760     -26.681 -18.128  34.263  1.00 40.88           O  
HETATM 3982  O   HOH A 761      -7.991 -25.985  -8.017  1.00 54.71           O  
HETATM 3983  O   HOH A 762      -3.721  -2.497  30.033  1.00 45.86           O  
HETATM 3984  O   HOH A 763     -18.587  -6.027  -1.123  1.00 72.89           O  
HETATM 3985  O   HOH A 764     -28.059 -19.636  35.964  1.00 50.77           O  
HETATM 3986  O   HOH A 765      -2.276  -0.582  29.630  1.00 48.08           O  
HETATM 3987  O   HOH A 766       4.333 -24.709  18.200  1.00 48.81           O  
HETATM 3988  O   HOH A 767       1.790 -11.538  20.337  1.00 58.10           O  
HETATM 3989  O   HOH A 768      -3.636 -10.329  31.401  1.00 43.31           O  
HETATM 3990  O   HOH A 769      -3.787 -23.303 -11.192  1.00 51.90           O  
HETATM 3991  O   HOH A 770     -39.503   8.247  -3.314  1.00 62.79           O  
HETATM 3992  O   HOH A 771      -1.391  -8.146  22.916  1.00 43.01           O  
HETATM 3993  O   HOH A 772      -3.373  -5.981  31.468  1.00 46.92           O  
HETATM 3994  O   HOH A 773     -36.276 -34.524   6.118  1.00 62.12           O  
HETATM 3995  O   HOH A 774     -22.287  -7.699  -3.606  1.00 56.25           O  
HETATM 3996  O   HOH A 775       1.283 -23.893  33.180  1.00 58.31           O  
HETATM 3997  O   HOH A 776     -27.450 -12.297  35.349  1.00 47.38           O  
HETATM 3998  O   HOH A 777     -22.645 -17.136  -7.085  1.00 54.38           O  
HETATM 3999  O   HOH A 778       3.941 -22.220  16.143  1.00 58.27           O  
HETATM 4000  O   HOH A 779       3.212 -24.891  12.887  1.00 45.03           O  
HETATM 4001  O   HOH A 780     -17.199  -1.750  -3.034  1.00 54.87           O  
CONECT  130 3835                                                                
CONECT  142 3836                                                                
CONECT  147 3835                                                                
CONECT  173 3836                                                                
CONECT 1914 3836                                                                
CONECT 1916 3836                                                                
CONECT 2142 3836                                                                
CONECT 2620 3835                                                                
CONECT 2639 3835                                                                
CONECT 2646 3835                                                                
CONECT 3829 3836                                                                
CONECT 3835  130  147 2620 2639                                                 
CONECT 3835 2646                                                                
CONECT 3836  142  173 1914 1916                                                 
CONECT 3836 2142 3829                                                           
CONECT 3837 3838 3839                                                           
CONECT 3838 3837                                                                
CONECT 3839 3837 3840 3841                                                      
CONECT 3840 3839                                                                
CONECT 3841 3839 3842                                                           
CONECT 3842 3841                                                                
CONECT 3843 3844 3845                                                           
CONECT 3844 3843                                                                
CONECT 3845 3843 3846 3847                                                      
CONECT 3846 3845                                                                
CONECT 3847 3845 3848                                                           
CONECT 3848 3847                                                                
CONECT 3849 3850 3851                                                           
CONECT 3850 3849                                                                
CONECT 3851 3849 3852                                                           
CONECT 3852 3851 3853                                                           
CONECT 3853 3852 3854                                                           
CONECT 3854 3853 3855                                                           
CONECT 3855 3854                                                                
CONECT 3856 3857 3858                                                           
CONECT 3857 3856                                                                
CONECT 3858 3856 3859                                                           
CONECT 3859 3858 3860                                                           
CONECT 3860 3859 3861                                                           
CONECT 3861 3860 3862                                                           
CONECT 3862 3861                                                                
CONECT 3863 3864 3865                                                           
CONECT 3864 3863                                                                
CONECT 3865 3863 3866                                                           
CONECT 3866 3865 3867                                                           
CONECT 3867 3866 3868                                                           
CONECT 3868 3867 3869                                                           
CONECT 3869 3868                                                                
CONECT 3870 3871 3872 3873 3874                                                 
CONECT 3871 3870 3875                                                           
CONECT 3872 3870 3876                                                           
CONECT 3873 3870 3877                                                           
CONECT 3874 3870                                                                
CONECT 3875 3871                                                                
CONECT 3876 3872                                                                
CONECT 3877 3873                                                                
CONECT 3878 3879 3880 3881 3882                                                 
CONECT 3879 3878 3883                                                           
CONECT 3880 3878 3884                                                           
CONECT 3881 3878 3885                                                           
CONECT 3882 3878                                                                
CONECT 3883 3879                                                                
CONECT 3884 3880                                                                
CONECT 3885 3881                                                                
CONECT 3886 3887 3888 3895                                                      
CONECT 3887 3886 3898                                                           
CONECT 3888 3886 3889 3890                                                      
CONECT 3889 3888                                                                
CONECT 3890 3888 3891 3892                                                      
CONECT 3891 3890                                                                
CONECT 3892 3890 3893 3894                                                      
CONECT 3893 3892                                                                
CONECT 3894 3892 3895 3896                                                      
CONECT 3895 3886 3894                                                           
CONECT 3896 3894 3897                                                           
CONECT 3897 3896                                                                
CONECT 3898 3887 3899                                                           
CONECT 3899 3898 3900                                                           
CONECT 3900 3899 3901                                                           
CONECT 3901 3900 3902                                                           
CONECT 3902 3901 3903                                                           
CONECT 3903 3902 3904                                                           
CONECT 3904 3903 3905                                                           
CONECT 3905 3904                                                                
CONECT 3906 3907                                                                
CONECT 3907 3906 3908                                                           
CONECT 3908 3907 3909                                                           
CONECT 3909 3908 3910                                                           
CONECT 3910 3909 3911                                                           
CONECT 3911 3910 3912                                                           
CONECT 3912 3911 3913                                                           
CONECT 3913 3912                                                                
CONECT 3914 3915                                                                
CONECT 3915 3914 3916                                                           
CONECT 3916 3915 3917                                                           
CONECT 3917 3916 3918                                                           
CONECT 3918 3917 3919                                                           
CONECT 3919 3918 3920                                                           
CONECT 3920 3919 3921                                                           
CONECT 3921 3920                                                                
MASTER      371    0   13   28    2    0    0    6 4000    1  100   39          
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.