path: root/plip/test/pdb/3r0t.pdb

HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       09-MAR-11   3R0T              
TITLE     CRYSTAL STRUCTURE OF HUMAN PROTEIN KINASE CK2 ALPHA SUBUNIT IN COMPLEX
TITLE    2 WITH THE INHIBITOR CX-5279                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CASEIN KINASE II SUBUNIT ALPHA;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1-337;                                        
COMPND   5 SYNONYM: CK II ALPHA;                                                
COMPND   6 EC: 2.7.11.1;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CSNK2A1, CK2A1;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PT7-7                                     
KEYWDS    KINASE, CK2-INHIBITOR COMPLEX, TRANSFERASE-TRANSFERASE INHIBITOR      
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.BATTISTUTTA,E.PAPINUTTO,G.LOLLI,F.PIERRE,M.HADDACH,D.M.RYCKMAN      
REVDAT   2   29-OCT-14 3R0T    1       AUTHOR                                   
REVDAT   1   07-DEC-11 3R0T    0                                                
JRNL        AUTH   R.BATTISTUTTA,G.COZZA,F.PIERRE,E.PAPINUTTO,G.LOLLI,S.SARNO,  
JRNL        AUTH 2 S.E.O'BRIEN,A.SIDDIQUI-JAIN,M.HADDACH,K.ANDERES,D.M.RYCKMAN, 
JRNL        AUTH 3 F.MEGGIO,L.A.PINNA                                           
JRNL        TITL   UNPRECEDENTED SELECTIVITY AND STRUCTURAL DETERMINANTS OF A   
JRNL        TITL 2 NEW CLASS OF PROTEIN KINASE CK2 INHIBITORS IN CLINICAL       
JRNL        TITL 3 TRIALS FOR THE TREATMENT OF CANCER.                          
JRNL        REF    BIOCHEMISTRY                  V.  50  8478 2011              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   21870818                                                     
JRNL        DOI    10.1021/BI2008382                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   G.COZZA,M.MAZZORANA,E.PAPINUTTO,J.BAIN,M.ELLIOTT,G.DI MAIRA, 
REMARK   1  AUTH 2 A.GIANONCELLI,M.A.PAGANO,S.SARNO,M.RUZZENE,R.BATTISTUTTA,    
REMARK   1  AUTH 3 F.MEGGIO,S.MORO,G.ZAGOTTO,L.A.PINNA                          
REMARK   1  TITL   QUINALIZARIN AS A POTENT, SELECTIVE AND CELL-PERMEABLE       
REMARK   1  TITL 2 INHIBITOR OF PROTEIN KINASE CK2.                             
REMARK   1  REF    BIOCHEM.J.                    V. 421   387 2009              
REMARK   1  REFN                   ISSN 0264-6021                               
REMARK   1  PMID   19432557                                                     
REMARK   1  DOI    10.1042/BJ20090069                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.18                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 28526                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.163                           
REMARK   3   R VALUE            (WORKING SET) : 0.160                           
REMARK   3   FREE R VALUE                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1420                            
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 35.1842 -  3.7690    0.99     3103   165  0.1437 0.1687        
REMARK   3     2  3.7690 -  2.9920    0.99     3026   162  0.1456 0.1894        
REMARK   3     3  2.9920 -  2.6140    1.00     3033   153  0.1662 0.2429        
REMARK   3     4  2.6140 -  2.3750    0.99     2975   179  0.1725 0.2541        
REMARK   3     5  2.3750 -  2.2048    0.99     3009   152  0.1654 0.2217        
REMARK   3     6  2.2048 -  2.0749    0.97     2927   145  0.1638 0.2257        
REMARK   3     7  2.0749 -  1.9710    0.92     2782   140  0.1662 0.2278        
REMARK   3     8  1.9710 -  1.8852    0.85     2580   129  0.1825 0.2350        
REMARK   3     9  1.8852 -  1.8126    0.71     2123   113  0.2041 0.2279        
REMARK   3    10  1.8126 -  1.7500    0.51     1548    82  0.2385 0.3005        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.37                                          
REMARK   3   B_SOL              : 38.79                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.080           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.83                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.07                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -6.30980                                             
REMARK   3    B22 (A**2) : 3.47990                                              
REMARK   3    B33 (A**2) : 2.82990                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.16510                                             
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           2946                                  
REMARK   3   ANGLE     :  1.036           3976                                  
REMARK   3   CHIRALITY :  0.075            406                                  
REMARK   3   PLANARITY :  0.005            501                                  
REMARK   3   DIHEDRAL  : 13.608           1109                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (chain A and resid 3:13)                               
REMARK   3    ORIGIN FOR THE GROUP (A):   1.4641 -55.6146  14.6268              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1667 T22:   0.1553                                     
REMARK   3      T33:   0.2001 T12:  -0.0541                                     
REMARK   3      T13:   0.0353 T23:  -0.0565                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0564 L22:   0.0078                                     
REMARK   3      L33:   0.0150 L12:   0.0243                                     
REMARK   3      L13:   0.0083 L23:  -0.0003                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0120 S12:   0.0526 S13:  -0.0471                       
REMARK   3      S21:  -0.0062 S22:   0.0860 S23:  -0.0703                       
REMARK   3      S31:  -0.0106 S32:  -0.0466 S33:   0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (chain A and resid 14:32)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  20.9593 -56.5547   8.8193              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2184 T22:   0.1470                                     
REMARK   3      T33:   0.3446 T12:   0.0235                                     
REMARK   3      T13:   0.0536 T23:  -0.0858                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0139 L22:   0.0999                                     
REMARK   3      L33:   0.0686 L12:  -0.0127                                     
REMARK   3      L13:   0.0311 L23:  -0.0074                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2488 S12:   0.1931 S13:  -0.1999                       
REMARK   3      S21:  -0.0211 S22:   0.0957 S23:  -0.1243                       
REMARK   3      S31:   0.1808 S32:   0.1616 S33:  -0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (chain A and resid 33:51)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  33.0192 -34.0681  15.6464              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1317 T22:   0.2292                                     
REMARK   3      T33:   0.2319 T12:  -0.0256                                     
REMARK   3      T13:   0.0088 T23:  -0.0750                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0751 L22:   0.1045                                     
REMARK   3      L33:   0.1087 L12:  -0.0117                                     
REMARK   3      L13:   0.0879 L23:   0.0255                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0732 S12:   0.0348 S13:  -0.0756                       
REMARK   3      S21:  -0.0804 S22:  -0.1905 S23:   0.2135                       
REMARK   3      S31:  -0.0276 S32:   0.0701 S33:  -0.0001                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (chain A and resid 52:71)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  32.1118 -31.5914  11.3104              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1156 T22:   0.2072                                     
REMARK   3      T33:   0.1295 T12:  -0.0180                                     
REMARK   3      T13:  -0.0353 T23:  -0.0043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0728 L22:   0.0127                                     
REMARK   3      L33:   0.0385 L12:  -0.0320                                     
REMARK   3      L13:  -0.0050 L23:   0.0035                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0461 S12:   0.1432 S13:   0.2397                       
REMARK   3      S21:  -0.1383 S22:   0.0626 S23:   0.0589                       
REMARK   3      S31:   0.0279 S32:  -0.0798 S33:   0.0007                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (chain A and resid 72:102)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  24.7116 -44.4796  11.8194              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1217 T22:   0.1772                                     
REMARK   3      T33:   0.1597 T12:   0.0066                                     
REMARK   3      T13:  -0.0140 T23:  -0.0266                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1791 L22:   0.2326                                     
REMARK   3      L33:   0.1170 L12:   0.1641                                     
REMARK   3      L13:   0.0026 L23:   0.1089                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0039 S12:  -0.1009 S13:  -0.1852                       
REMARK   3      S21:   0.0915 S22:   0.0280 S23:  -0.1044                       
REMARK   3      S31:   0.0618 S32:   0.0149 S33:  -0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (chain A and resid 103:139)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  15.9998 -29.1819  10.8388              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1312 T22:   0.1502                                     
REMARK   3      T33:   0.1780 T12:   0.0178                                     
REMARK   3      T13:  -0.0068 T23:  -0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0500 L22:   0.0814                                     
REMARK   3      L33:   0.2482 L12:  -0.0064                                     
REMARK   3      L13:  -0.0006 L23:  -0.1427                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0048 S12:   0.0020 S13:   0.2493                       
REMARK   3      S21:   0.0802 S22:   0.0149 S23:  -0.1391                       
REMARK   3      S31:  -0.0785 S32:  -0.0440 S33:   0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (chain A and resid 140:224)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   9.9353 -41.3947  15.1453              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0934 T22:   0.0745                                     
REMARK   3      T33:   0.1054 T12:  -0.0020                                     
REMARK   3      T13:  -0.0027 T23:  -0.0197                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5752 L22:   0.4700                                     
REMARK   3      L33:   0.2096 L12:   0.0653                                     
REMARK   3      L13:  -0.1833 L23:  -0.2846                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0428 S12:   0.1121 S13:  -0.0482                       
REMARK   3      S21:   0.0253 S22:   0.0386 S23:  -0.1052                       
REMARK   3      S31:   0.0006 S32:  -0.0174 S33:   0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (chain A and resid 225:247)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   0.7560 -31.9870  26.3692              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1549 T22:   0.0805                                     
REMARK   3      T33:   0.1055 T12:   0.0151                                     
REMARK   3      T13:  -0.0151 T23:   0.0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1356 L22:   0.0378                                     
REMARK   3      L33:   0.0555 L12:  -0.0798                                     
REMARK   3      L13:   0.0674 L23:  -0.0466                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0772 S12:   0.0027 S13:   0.1597                       
REMARK   3      S21:   0.1155 S22:   0.0023 S23:  -0.1846                       
REMARK   3      S31:  -0.0997 S32:  -0.0487 S33:  -0.0003                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (chain A and resid 248:329)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.9085 -37.9654  18.3039              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0920 T22:   0.1009                                     
REMARK   3      T33:   0.0675 T12:  -0.0082                                     
REMARK   3      T13:  -0.0036 T23:   0.0107                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4401 L22:   0.2274                                     
REMARK   3      L33:   0.3372 L12:  -0.1399                                     
REMARK   3      L13:  -0.2005 L23:  -0.0276                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0103 S12:   0.1025 S13:  -0.0126                       
REMARK   3      S21:   0.0164 S22:   0.0378 S23:  -0.0172                       
REMARK   3      S31:   0.0227 S32:  -0.1320 S33:   0.0000                       
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 3R0T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAR-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB064346.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-OCT-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ELETTRA                            
REMARK 200  BEAMLINE                       : 5.2R                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI111               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28551                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.180                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.6                               
REMARK 200  DATA REDUNDANCY                : 2.800                              
REMARK 200  R MERGE                    (I) : 0.08300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 57.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.46200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2PVR                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 32% PEG 4000, 0.2M LI2SO4, 0.1M TRIS     
REMARK 280  PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       23.09200            
REMARK 290   SMTRY3   2  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     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     ASP A   330                                                      
REMARK 465     GLN A   331                                                      
REMARK 465     ALA A   332                                                      
REMARK 465     ARG A   333                                                      
REMARK 465     MET A   334                                                      
REMARK 465     GLY A   335                                                      
REMARK 465     SER A   336                                                      
REMARK 465     SER A   337                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     VAL A   66   CA   CB   CG1  CG2                                  
REMARK 480     MET A  137   CA   CB   CG   SD   CE                              
REMARK 480     MET A  150   CA   CB   CG   SD   CE                              
REMARK 480     SER A  194   CA   CB   OG                                        
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    PRO A  72        7.31    -63.10                                   
REMARK 500    LYS A  74      171.94     77.25                                   
REMARK 500    LYS A  75      -94.80   -122.48                                   
REMARK 500    ASP A 156       41.13   -151.35                                   
REMARK 500    ASP A 175       76.09     53.05                                   
REMARK 500    ALA A 193      155.33     68.87                                   
REMARK 500    MET A 208       54.56    -92.13                                   
REMARK 500    HIS A 234       73.11   -103.07                                   
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 630        DISTANCE =  5.37 ANGSTROMS                       
REMARK 525    HOH A 658        DISTANCE =  5.17 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FU9 A 338                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 339                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 340                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 341                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 342                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 343                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 344                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 345                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 346                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 347                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 348                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 349                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 350                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 351                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 352                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3PE1   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN PROTEIN KINASE CK2 ALPHA SUBUNIT          
REMARK 900 IN COMPLEX WITH THE INHIBITOR CX-4945                                
REMARK 900 RELATED ID: 3PE2   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN PROTEIN KINASE CK2 ALPHA SUBUNIT          
REMARK 900 IN COMPLEX WITH THE INHIBITOR CX-5011                                
DBREF  3R0T A    1   337  UNP    P68400   CSK21_HUMAN      1    337             
SEQRES   1 A  337  MET SER GLY PRO VAL PRO SER ARG ALA ARG VAL TYR THR          
SEQRES   2 A  337  ASP VAL ASN THR HIS ARG PRO ARG GLU TYR TRP ASP TYR          
SEQRES   3 A  337  GLU SER HIS VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR          
SEQRES   4 A  337  GLN LEU VAL ARG LYS LEU GLY ARG GLY LYS TYR SER GLU          
SEQRES   5 A  337  VAL PHE GLU ALA ILE ASN ILE THR ASN ASN GLU LYS VAL          
SEQRES   6 A  337  VAL VAL LYS ILE LEU LYS PRO VAL LYS LYS LYS LYS ILE          
SEQRES   7 A  337  LYS ARG GLU ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY          
SEQRES   8 A  337  PRO ASN ILE ILE THR LEU ALA ASP ILE VAL LYS ASP PRO          
SEQRES   9 A  337  VAL SER ARG THR PRO ALA LEU VAL PHE GLU HIS VAL ASN          
SEQRES  10 A  337  ASN THR ASP PHE LYS GLN LEU TYR GLN THR LEU THR ASP          
SEQRES  11 A  337  TYR ASP ILE ARG PHE TYR MET TYR GLU ILE LEU LYS ALA          
SEQRES  12 A  337  LEU ASP TYR CYS HIS SER MET GLY ILE MET HIS ARG ASP          
SEQRES  13 A  337  VAL LYS PRO HIS ASN VAL MET ILE ASP HIS GLU HIS ARG          
SEQRES  14 A  337  LYS LEU ARG LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR          
SEQRES  15 A  337  HIS PRO GLY GLN GLU TYR ASN VAL ARG VAL ALA SER ARG          
SEQRES  16 A  337  TYR PHE LYS GLY PRO GLU LEU LEU VAL ASP TYR GLN MET          
SEQRES  17 A  337  TYR ASP TYR SER LEU ASP MET TRP SER LEU GLY CYS MET          
SEQRES  18 A  337  LEU ALA SER MET ILE PHE ARG LYS GLU PRO PHE PHE HIS          
SEQRES  19 A  337  GLY HIS ASP ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS          
SEQRES  20 A  337  VAL LEU GLY THR GLU ASP LEU TYR ASP TYR ILE ASP LYS          
SEQRES  21 A  337  TYR ASN ILE GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU          
SEQRES  22 A  337  GLY ARG HIS SER ARG LYS ARG TRP GLU ARG PHE VAL HIS          
SEQRES  23 A  337  SER GLU ASN GLN HIS LEU VAL SER PRO GLU ALA LEU ASP          
SEQRES  24 A  337  PHE LEU ASP LYS LEU LEU ARG TYR ASP HIS GLN SER ARG          
SEQRES  25 A  337  LEU THR ALA ARG GLU ALA MET GLU HIS PRO TYR PHE TYR          
SEQRES  26 A  337  THR VAL VAL LYS ASP GLN ALA ARG MET GLY SER SER              
HET    FU9  A 338      32                                                       
HET    SO4  A 339       5                                                       
HET    SO4  A 340       5                                                       
HET    SO4  A 341       5                                                       
HET    SO4  A 342       5                                                       
HET    PEG  A 343       7                                                       
HET    EDO  A 344       4                                                       
HET    EDO  A 345       4                                                       
HET    EDO  A 346       4                                                       
HET    EDO  A 347       4                                                       
HET    EDO  A 348       4                                                       
HET    EDO  A 349       4                                                       
HET    EDO  A 350       4                                                       
HET    EDO  A 351       4                                                       
HET    EDO  A 352       4                                                       
HETNAM     FU9 3-(CYCLOPROPYLAMINO)-5-{[3-(TRIFLUOROMETHYL)                     
HETNAM   2 FU9  PHENYL]AMINO}PYRIMIDO[4,5-C]QUINOLINE-8-CARBOXYLIC              
HETNAM   3 FU9  ACID                                                            
HETNAM     SO4 SULFATE ION                                                      
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     FU9 CX-5279                                                          
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  FU9    C22 H16 F3 N5 O2                                             
FORMUL   3  SO4    4(O4 S 2-)                                                   
FORMUL   7  PEG    C4 H10 O3                                                    
FORMUL   8  EDO    9(C2 H6 O2)                                                  
FORMUL  17  HOH   *334(H2 O)                                                    
HELIX    1   1 PRO A   20  ASP A   25  1                                   6    
HELIX    2   2 TYR A   26  HIS A   29  5                                   4    
HELIX    3   3 ASN A   35  ASP A   37  5                                   3    
HELIX    4   4 LYS A   76  ARG A   89  1                                  14    
HELIX    5   5 ASP A  120  TYR A  125  1                                   6    
HELIX    6   6 THR A  129  MET A  150  1                                  22    
HELIX    7   7 LYS A  158  HIS A  160  5                                   3    
HELIX    8   8 ASP A  175  ALA A  179  5                                   5    
HELIX    9   9 SER A  194  LYS A  198  5                                   5    
HELIX   10  10 GLY A  199  VAL A  204  1                                   6    
HELIX   11  11 TYR A  211  ARG A  228  1                                  18    
HELIX   12  12 ASP A  237  GLY A  250  1                                  14    
HELIX   13  13 GLY A  250  TYR A  261  1                                  12    
HELIX   14  14 ASP A  266  ILE A  272  5                                   7    
HELIX   15  15 ARG A  280  VAL A  285  5                                   6    
HELIX   16  16 ASN A  289  VAL A  293  5                                   5    
HELIX   17  17 SER A  294  LEU A  305  1                                  12    
HELIX   18  18 ASP A  308  ARG A  312  5                                   5    
HELIX   19  19 THR A  314  GLU A  320  1                                   7    
HELIX   20  20 HIS A  321  TYR A  325  5                                   5    
SHEET    1   A 5 TYR A  39  ARG A  47  0                                        
SHEET    2   A 5 SER A  51  ASN A  58 -1  O  VAL A  53   N  LEU A  45           
SHEET    3   A 5 LYS A  64  LEU A  70 -1  O  VAL A  65   N  ALA A  56           
SHEET    4   A 5 THR A 108  GLU A 114 -1  O  LEU A 111   N  LYS A  68           
SHEET    5   A 5 LEU A  97  ASP A 103 -1  N  VAL A 101   O  ALA A 110           
SHEET    1   B 2 ILE A 152  MET A 153  0                                        
SHEET    2   B 2 GLU A 180  PHE A 181 -1  O  GLU A 180   N  MET A 153           
SHEET    1   C 2 VAL A 162  ASP A 165  0                                        
SHEET    2   C 2 LYS A 170  LEU A 173 -1  O  LYS A 170   N  ASP A 165           
CISPEP   1 GLU A  230    PRO A  231          0         1.13                     
SITE     1 AC1 20 LEU A  45  GLY A  46  ARG A  47  VAL A  53                    
SITE     2 AC1 20 VAL A  66  LYS A  68  PHE A 113  GLU A 114                    
SITE     3 AC1 20 HIS A 115  VAL A 116  ASN A 118  MET A 163                    
SITE     4 AC1 20 ILE A 174  ASP A 175  EDO A 345  EDO A 351                    
SITE     5 AC1 20 HOH A 370  HOH A 381  HOH A 616  HOH A 636                    
SITE     1 AC2  6 ARG A  80  ARG A 155  ASN A 189  VAL A 192                    
SITE     2 AC2  6 HOH A 369  HOH A 677                                          
SITE     1 AC3  4 ARG A 191  LYS A 198  ASN A 238  PEG A 343                    
SITE     1 AC4  8 ASP A 253  ARG A 278  ARG A 306  TYR A 307                    
SITE     2 AC4  8 ASP A 308  HOH A 397  HOH A 442  HOH A 465                    
SITE     1 AC5  5 LYS A 170  ARG A 172  HOH A 428  HOH A 463                    
SITE     2 AC5  5 HOH A 649                                                     
SITE     1 AC6  6 SER A 194  ARG A 195  TYR A 196  SO4 A 340                    
SITE     2 AC6  6 HOH A 433  HOH A 619                                          
SITE     1 AC7  6 GLN A  36  TYR A  39  VAL A 101  ASP A 103                    
SITE     2 AC7  6 PRO A 104  ARG A 280                                          
SITE     1 AC8  6 ASN A 118  ASP A 120  HIS A 160  FU9 A 338                    
SITE     2 AC8  6 EDO A 348  EDO A 351                                          
SITE     1 AC9  4 ASP A  37  PRO A 295  HIS A 321  HOH A 620                    
SITE     1 BC1  5 PHE A 232  HOH A 372  HOH A 573  HOH A 621                    
SITE     2 BC1  5 HOH A 668                                                     
SITE     1 BC2  9 ASN A 118  THR A 119  ASP A 120  PHE A 121                    
SITE     2 BC2  9 PRO A 159  VAL A 162  MET A 163  ILE A 164                    
SITE     3 BC2  9 EDO A 345                                                     
SITE     1 BC3  6 LYS A 158  HIS A 160  SER A 194  EDO A 350                    
SITE     2 BC3  6 HOH A 618  HOH A 619                                          
SITE     1 BC4  5 PRO A 159  PHE A 197  GLU A 230  EDO A 349                    
SITE     2 BC4  5 HOH A 618                                                     
SITE     1 BC5  5 ASN A 118  FU9 A 338  EDO A 345  HOH A 455                    
SITE     2 BC5  5 HOH A 575                                                     
SITE     1 BC6  7 PRO A 104  ARG A 278  LYS A 279  ASP A 302                    
SITE     2 BC6  7 HOH A 531  HOH A 642  HOH A 679                               
CRYST1   58.352   46.184   63.300  90.00 111.51  90.00 P 1 21 1      2          
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      0.017137  0.000000  0.006753        0.00000                         
SCALE2      0.000000  0.021653  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016980        0.00000                         
ATOM      1  N   GLY A   3      -1.502 -62.453  29.985  1.00 40.82           N  
ANISOU    1  N   GLY A   3     5111   4857   5540   -349     80   -403       N  
ATOM      2  CA  GLY A   3      -0.651 -61.305  29.715  1.00 44.52           C  
ANISOU    2  CA  GLY A   3     5587   5318   6013   -345     98   -421       C  
ATOM      3  C   GLY A   3      -1.188 -60.418  28.604  1.00 39.81           C  
ANISOU    3  C   GLY A   3     4994   4745   5387   -353    122   -411       C  
ATOM      4  O   GLY A   3      -2.322 -60.588  28.164  1.00 36.32           O  
ANISOU    4  O   GLY A   3     4552   4328   4919   -359    125   -385       O  
ATOM      5  N   PRO A   4      -0.368 -59.467  28.133  1.00 38.43           N  
ANISOU    5  N   PRO A   4     4823   4562   5216   -353    140   -431       N  
ATOM      6  CA  PRO A   4      -0.839 -58.542  27.100  1.00 28.04           C  
ANISOU    6  CA  PRO A   4     3512   3269   3872   -360    164   -421       C  
ATOM      7  C   PRO A   4      -1.077 -59.249  25.772  1.00 26.24           C  
ANISOU    7  C   PRO A   4     3274   3054   3640   -386    172   -431       C  
ATOM      8  O   PRO A   4      -0.480 -60.287  25.482  1.00 29.56           O  
ANISOU    8  O   PRO A   4     3684   3461   4086   -400    164   -457       O  
ATOM      9  CB  PRO A   4       0.313 -57.540  26.978  1.00 34.55           C  
ANISOU    9  CB  PRO A   4     4342   4077   4709   -355    178   -446       C  
ATOM     10  CG  PRO A   4       1.524 -58.326  27.371  1.00 39.33           C  
ANISOU   10  CG  PRO A   4     4939   4652   5354   -358    165   -481       C  
ATOM     11  CD  PRO A   4       1.055 -59.258  28.461  1.00 39.89           C  
ANISOU   11  CD  PRO A   4     5007   4717   5431   -349    140   -465       C  
ATOM     12  N   VAL A   5      -1.971 -58.679  24.977  1.00 21.32           N  
ANISOU   12  N   VAL A   5     2656   2459   2987   -392    188   -409       N  
ATOM     13  CA  VAL A   5      -2.286 -59.191  23.656  1.00 25.36           C  
ANISOU   13  CA  VAL A   5     3158   2986   3490   -416    198   -415       C  
ATOM     14  C   VAL A   5      -1.179 -58.723  22.726  1.00 20.62           C  
ANISOU   14  C   VAL A   5     2556   2376   2904   -429    216   -450       C  
ATOM     15  O   VAL A   5      -0.725 -57.591  22.846  1.00 22.01           O  
ANISOU   15  O   VAL A   5     2740   2547   3076   -418    228   -453       O  
ATOM     16  CB  VAL A   5      -3.629 -58.612  23.180  1.00 14.07           C  
ANISOU   16  CB  VAL A   5     1735   1590   2021   -416    209   -378       C  
ATOM     17  CG1 VAL A   5      -3.854 -58.886  21.709  1.00 17.54           C  
ANISOU   17  CG1 VAL A   5     2167   2047   2450   -442    224   -386       C  
ATOM     18  CG2 VAL A   5      -4.773 -59.147  24.037  1.00 23.46           C  
ANISOU   18  CG2 VAL A   5     2926   2792   3196   -405    192   -344       C  
ATOM     19  N   PRO A   6      -0.720 -59.591  21.809  1.00 19.05           N  
ANISOU   19  N   PRO A   6     2345   2173   2721   -451    218   -477       N  
ATOM     20  CA  PRO A   6       0.332 -59.161  20.879  1.00 22.26           C  
ANISOU   20  CA  PRO A   6     2749   2571   3140   -464    235   -511       C  
ATOM     21  C   PRO A   6      -0.180 -58.203  19.796  1.00 19.43           C  
ANISOU   21  C   PRO A   6     2395   2237   2751   -473    259   -498       C  
ATOM     22  O   PRO A   6      -1.380 -58.098  19.579  1.00 23.70           O  
ANISOU   22  O   PRO A   6     2938   2804   3262   -474    262   -466       O  
ATOM     23  CB  PRO A   6       0.816 -60.479  20.258  1.00 22.71           C  
ANISOU   23  CB  PRO A   6     2791   2618   3221   -486    229   -541       C  
ATOM     24  CG  PRO A   6      -0.334 -61.414  20.398  1.00 24.95           C  
ANISOU   24  CG  PRO A   6     3071   2918   3492   -490    215   -515       C  
ATOM     25  CD  PRO A   6      -1.050 -61.022  21.661  1.00 24.62           C  
ANISOU   25  CD  PRO A   6     3039   2879   3436   -465    203   -481       C  
ATOM     26  N   SER A   7       0.745 -57.506  19.142  1.00 17.65           N  
ANISOU   26  N   SER A   7     2170   2004   2534   -480    276   -524       N  
ATOM     27  CA  SER A   7       0.417 -56.544  18.097  1.00 16.35           C  
ANISOU   27  CA  SER A   7     2008   1861   2343   -488    300   -515       C  
ATOM     28  C   SER A   7       1.444 -56.657  16.984  1.00 20.63           C  
ANISOU   28  C   SER A   7     2542   2394   2901   -510    313   -554       C  
ATOM     29  O   SER A   7       2.597 -57.000  17.244  1.00 20.28           O  
ANISOU   29  O   SER A   7     2493   2324   2888   -510    307   -587       O  
ATOM     30  CB  SER A   7       0.466 -55.121  18.661  1.00 17.57           C  
ANISOU   30  CB  SER A   7     2177   2015   2485   -467    308   -500       C  
ATOM     31  OG  SER A   7       0.286 -54.152  17.636  1.00 19.00           O  
ANISOU   31  OG  SER A   7     2361   2214   2643   -476    331   -495       O  
ATOM     32  N   ARG A   8       1.025 -56.363  15.754  1.00 20.45           N  
ANISOU   32  N   ARG A   8     2517   2395   2857   -527    331   -550       N  
ATOM     33  CA  ARG A   8       1.917 -56.328  14.585  1.00 21.97           C  
ANISOU   33  CA  ARG A   8     2703   2585   3062   -548    347   -584       C  
ATOM     34  C   ARG A   8       1.691 -55.027  13.836  1.00 21.54           C  
ANISOU   34  C   ARG A   8     2655   2548   2981   -550    370   -572       C  
ATOM     35  O   ARG A   8       0.571 -54.501  13.838  1.00 18.25           O  
ANISOU   35  O   ARG A   8     2246   2155   2534   -544    374   -536       O  
ATOM     36  CB  ARG A   8       1.572 -57.455  13.608  1.00 29.94           C  
ANISOU   36  CB  ARG A   8     3698   3606   4070   -574    346   -593       C  
ATOM     37  CG  ARG A   8       1.835 -58.846  14.104  1.00 37.53           C  
ANISOU   37  CG  ARG A   8     4651   4551   5059   -577    325   -610       C  
ATOM     38  CD  ARG A   8       3.325 -59.102  14.202  1.00 40.04           C  
ANISOU   38  CD  ARG A   8     4963   4838   5414   -580    323   -653       C  
ATOM     39  NE  ARG A   8       3.601 -60.471  14.624  1.00 40.22           N  
ANISOU   39  NE  ARG A   8     4975   4844   5464   -584    303   -669       N  
ATOM     40  CZ  ARG A   8       3.575 -60.878  15.889  1.00 42.42           C  
ANISOU   40  CZ  ARG A   8     5256   5106   5755   -566    282   -661       C  
ATOM     41  NH1 ARG A   8       3.283 -60.018  16.864  1.00 33.21           N  
ANISOU   41  NH1 ARG A   8     4102   3938   4577   -542    279   -636       N  
ATOM     42  NH2 ARG A   8       3.841 -62.146  16.180  1.00 45.87           N  
ANISOU   42  NH2 ARG A   8     5683   5528   6218   -572    264   -677       N  
ATOM     43  N   ALA A   9       2.731 -54.532  13.165  1.00 15.62           N  
ANISOU   43  N   ALA A   9     1904   1789   2243   -560    384   -602       N  
ATOM     44  CA  ALA A   9       2.572 -53.402  12.257  1.00 18.46           C  
ANISOU   44  CA  ALA A   9     2267   2166   2579   -566    407   -594       C  
ATOM     45  C   ALA A   9       1.606 -53.796  11.137  1.00 21.46           C  
ANISOU   45  C   ALA A   9     2642   2578   2936   -587    416   -580       C  
ATOM     46  O   ALA A   9       1.625 -54.930  10.662  1.00 21.38           O  
ANISOU   46  O   ALA A   9     2621   2568   2936   -605    409   -595       O  
ATOM     47  CB  ALA A   9       3.914 -52.996  11.673  1.00 14.16           C  
ANISOU   47  CB  ALA A   9     1720   1606   2055   -576    420   -633       C  
ATOM     48  N   ARG A  10       0.762 -52.862  10.709  1.00 13.86           N  
ANISOU   48  N   ARG A  10     1687   1639   1940   -586    429   -550       N  
ATOM     49  CA  ARG A  10      -0.195 -53.164   9.653  1.00 16.17           C  
ANISOU   49  CA  ARG A  10     1974   1962   2208   -605    438   -534       C  
ATOM     50  C   ARG A  10       0.395 -52.974   8.263  1.00 16.19           C  
ANISOU   50  C   ARG A  10     1970   1972   2210   -630    457   -560       C  
ATOM     51  O   ARG A  10      -0.245 -53.311   7.260  1.00 20.93           O  
ANISOU   51  O   ARG A  10     2563   2595   2793   -649    465   -553       O  
ATOM     52  CB  ARG A  10      -1.463 -52.325   9.813  1.00 20.15           C  
ANISOU   52  CB  ARG A  10     2489   2491   2677   -593    443   -489       C  
ATOM     53  CG  ARG A  10      -2.278 -52.639  11.048  1.00 33.68           C  
ANISOU   53  CG  ARG A  10     4208   4204   4385   -572    424   -460       C  
ATOM     54  CD  ARG A  10      -3.552 -51.806  11.037  1.00 41.52           C  
ANISOU   54  CD  ARG A  10     5211   5224   5342   -563    431   -416       C  
ATOM     55  NE  ARG A  10      -3.245 -50.409  10.738  1.00 55.14           N  
ANISOU   55  NE  ARG A  10     6944   6952   7056   -557    450   -413       N  
ATOM     56  CZ  ARG A  10      -4.138 -49.512  10.325  1.00 57.27           C  
ANISOU   56  CZ  ARG A  10     7221   7246   7295   -555    463   -382       C  
ATOM     57  NH1 ARG A  10      -5.406 -49.859  10.157  1.00 51.33           N  
ANISOU   57  NH1 ARG A  10     6468   6519   6518   -558    460   -351       N  
ATOM     58  NH2 ARG A  10      -3.756 -48.265  10.082  1.00 58.40           N  
ANISOU   58  NH2 ARG A  10     7370   7388   7430   -550    479   -382       N  
ATOM     59  N   VAL A  11       1.614 -52.434   8.208  1.00 17.69           N  
ANISOU   59  N   VAL A  11     2160   2142   2420   -629    465   -589       N  
ATOM     60  CA  VAL A  11       2.346 -52.276   6.954  1.00 18.09           C  
ANISOU   60  CA  VAL A  11     2203   2196   2474   -652    483   -618       C  
ATOM     61  C   VAL A  11       3.819 -52.578   7.179  1.00 22.01           C  
ANISOU   61  C   VAL A  11     2695   2661   3008   -653    479   -661       C  
ATOM     62  O   VAL A  11       4.294 -52.538   8.311  1.00 20.68           O  
ANISOU   62  O   VAL A  11     2531   2469   2858   -633    466   -665       O  
ATOM     63  CB  VAL A  11       2.206 -50.858   6.352  1.00 17.11           C  
ANISOU   63  CB  VAL A  11     2088   2088   2327   -652    504   -604       C  
ATOM     64  CG1 VAL A  11       0.766 -50.601   5.959  1.00 21.02           C  
ANISOU   64  CG1 VAL A  11     2586   2615   2785   -654    509   -563       C  
ATOM     65  CG2 VAL A  11       2.716 -49.791   7.320  1.00 21.76           C  
ANISOU   65  CG2 VAL A  11     2689   2658   2922   -626    504   -600       C  
ATOM     66  N   TYR A  12       4.526 -52.889   6.097  1.00 17.12           N  
ANISOU   66  N   TYR A  12     2064   2041   2398   -677    490   -693       N  
ATOM     67  CA  TYR A  12       5.951 -53.168   6.155  1.00 19.55           C  
ANISOU   67  CA  TYR A  12     2367   2322   2741   -681    488   -736       C  
ATOM     68  C   TYR A  12       6.273 -54.144   7.269  1.00 21.70           C  
ANISOU   68  C   TYR A  12     2636   2568   3041   -668    465   -747       C  
ATOM     69  O   TYR A  12       7.320 -54.030   7.919  1.00 22.08           O  
ANISOU   69  O   TYR A  12     2686   2589   3115   -658    459   -770       O  
ATOM     70  CB  TYR A  12       6.708 -51.872   6.405  1.00 15.19           C  
ANISOU   70  CB  TYR A  12     1824   1757   2191   -668    499   -742       C  
ATOM     71  CG  TYR A  12       6.436 -50.806   5.380  1.00 18.71           C  
ANISOU   71  CG  TYR A  12     2273   2225   2610   -678    522   -731       C  
ATOM     72  CD1 TYR A  12       6.473 -51.100   4.028  1.00 19.73           C  
ANISOU   72  CD1 TYR A  12     2393   2372   2733   -706    535   -746       C  
ATOM     73  CD2 TYR A  12       6.138 -49.507   5.764  1.00 17.74           C  
ANISOU   73  CD2 TYR A  12     2163   2107   2469   -660    529   -705       C  
ATOM     74  CE1 TYR A  12       6.241 -50.128   3.081  1.00 18.96           C  
ANISOU   74  CE1 TYR A  12     2298   2296   2611   -716    556   -735       C  
ATOM     75  CE2 TYR A  12       5.887 -48.528   4.829  1.00 21.09           C  
ANISOU   75  CE2 TYR A  12     2591   2553   2869   -670    550   -694       C  
ATOM     76  CZ  TYR A  12       5.938 -48.849   3.485  1.00 16.76           C  
ANISOU   76  CZ  TYR A  12     2033   2022   2315   -697    563   -709       C  
ATOM     77  OH  TYR A  12       5.705 -47.877   2.541  1.00 22.86           O  
ANISOU   77  OH  TYR A  12     2808   2815   3064   -707    583   -699       O  
ATOM     78  N   THR A  13       5.373 -55.095   7.495  1.00 19.83           N  
ANISOU   78  N   THR A  13     2396   2342   2799   -670    451   -729       N  
ATOM     79  CA  THR A  13       5.482 -55.969   8.655  1.00 22.60           C  
ANISOU   79  CA  THR A  13     2745   2671   3172   -656    428   -732       C  
ATOM     80  C   THR A  13       6.719 -56.847   8.586  1.00 25.56           C  
ANISOU   80  C   THR A  13     3108   3019   3583   -666    421   -776       C  
ATOM     81  O   THR A  13       7.417 -57.034   9.587  1.00 24.25           O  
ANISOU   81  O   THR A  13     2944   2827   3443   -651    408   -789       O  
ATOM     82  CB  THR A  13       4.245 -56.876   8.814  1.00 20.97           C  
ANISOU   82  CB  THR A  13     2535   2481   2950   -658    415   -704       C  
ATOM     83  OG1 THR A  13       3.054 -56.090   8.692  1.00 26.40           O  
ANISOU   83  OG1 THR A  13     3232   3196   3601   -652    423   -664       O  
ATOM     84  CG2 THR A  13       4.268 -57.546  10.168  1.00 18.64           C  
ANISOU   84  CG2 THR A  13     2241   2165   2674   -639    391   -700       C  
ATOM     85  N   ASP A  14       7.000 -57.363   7.393  1.00 25.50           N  
ANISOU   85  N   ASP A  14     3469   2039   4180   -271    566  -1070       N  
ATOM     86  CA  ASP A  14       8.052 -58.358   7.223  1.00 28.16           C  
ANISOU   86  CA  ASP A  14     3792   2362   4546   -223    643  -1099       C  
ATOM     87  C   ASP A  14       9.233 -57.872   6.392  1.00 23.39           C  
ANISOU   87  C   ASP A  14     3131   1840   3917   -248    629  -1101       C  
ATOM     88  O   ASP A  14       9.986 -58.690   5.854  1.00 20.94           O  
ANISOU   88  O   ASP A  14     2805   1531   3619   -234    699  -1140       O  
ATOM     89  CB  ASP A  14       7.484 -59.634   6.594  1.00 38.57           C  
ANISOU   89  CB  ASP A  14     5141   3635   5878   -246    740  -1168       C  
ATOM     90  CG  ASP A  14       6.515 -60.358   7.517  1.00 43.55           C  
ANISOU   90  CG  ASP A  14     5828   4175   6545   -204    770  -1167       C  
ATOM     91  OD1 ASP A  14       6.987 -61.012   8.472  1.00 44.76           O  
ANISOU   91  OD1 ASP A  14     5996   4269   6740   -114    800  -1150       O  
ATOM     92  OD2 ASP A  14       5.290 -60.274   7.284  1.00 38.57           O  
ANISOU   92  OD2 ASP A  14     5227   3530   5899   -259    763  -1184       O  
ATOM     93  N   VAL A  15       9.409 -56.558   6.296  1.00 22.43           N  
ANISOU   93  N   VAL A  15     2978   1785   3760   -282    540  -1060       N  
ATOM     94  CA  VAL A  15      10.496 -56.020   5.487  1.00 22.29           C  
ANISOU   94  CA  VAL A  15     2906   1849   3715   -310    522  -1060       C  
ATOM     95  C   VAL A  15      11.853 -56.585   5.890  1.00 24.88           C  
ANISOU   95  C   VAL A  15     3210   2167   4078   -228    560  -1052       C  
ATOM     96  O   VAL A  15      12.652 -56.938   5.027  1.00 26.13           O  
ANISOU   96  O   VAL A  15     3337   2362   4230   -245    605  -1086       O  
ATOM     97  CB  VAL A  15      10.549 -54.476   5.535  1.00 24.94           C  
ANISOU   97  CB  VAL A  15     3212   2252   4012   -347    413  -1007       C  
ATOM     98  CG1 VAL A  15       9.453 -53.872   4.667  1.00 18.51           C  
ANISOU   98  CG1 VAL A  15     2406   1475   3153   -449    382  -1029       C  
ATOM     99  CG2 VAL A  15      10.416 -54.002   6.957  1.00 35.48           C  
ANISOU   99  CG2 VAL A  15     4565   3547   5369   -277    353   -943       C  
ATOM    100  N   ASN A  16      12.122 -56.667   7.190  1.00 24.52           N  
ANISOU  100  N   ASN A  16     3178   2070   4069   -139    543  -1006       N  
ATOM    101  CA  ASN A  16      13.408 -57.186   7.659  1.00 27.34           C  
ANISOU  101  CA  ASN A  16     3513   2413   4461    -57    575   -994       C  
ATOM    102  C   ASN A  16      13.463 -58.705   7.613  1.00 29.82           C  
ANISOU  102  C   ASN A  16     3853   2662   4813    -17    682  -1045       C  
ATOM    103  O   ASN A  16      14.539 -59.292   7.465  1.00 31.81           O  
ANISOU  103  O   ASN A  16     4082   2919   5086     24    730  -1060       O  
ATOM    104  CB  ASN A  16      13.731 -56.692   9.072  1.00 23.17           C  
ANISOU  104  CB  ASN A  16     2990   1856   3958     25    514   -925       C  
ATOM    105  CG  ASN A  16      14.065 -55.224   9.109  1.00 22.63           C  
ANISOU  105  CG  ASN A  16     2885   1858   3854     -1    412   -872       C  
ATOM    106  OD1 ASN A  16      14.844 -54.740   8.294  1.00 24.80           O  
ANISOU  106  OD1 ASN A  16     3113   2207   4104    -39    397   -877       O  
ATOM    107  ND2 ASN A  16      13.463 -54.498  10.043  1.00 17.96           N  
ANISOU  107  ND2 ASN A  16     2315   1246   3262     17    340   -821       N  
ATOM    108  N   THR A  17      12.298 -59.332   7.744  1.00 34.34           N  
ANISOU  108  N   THR A  17     4476   3175   5396    -30    718  -1072       N  
ATOM    109  CA  THR A  17      12.194 -60.784   7.694  1.00 33.88           C  
ANISOU  109  CA  THR A  17     4448   3050   5373      2    819  -1123       C  
ATOM    110  C   THR A  17      12.802 -61.307   6.399  1.00 34.28           C  
ANISOU  110  C   THR A  17     4470   3144   5409    -42    883  -1180       C  
ATOM    111  O   THR A  17      13.375 -62.394   6.363  1.00 41.50           O  
ANISOU  111  O   THR A  17     5388   4024   6355      4    961  -1212       O  
ATOM    112  CB  THR A  17      10.718 -61.231   7.783  1.00 30.25           C  
ANISOU  112  CB  THR A  17     4043   2534   4916    -29    843  -1148       C  
ATOM    113  OG1 THR A  17      10.090 -60.625   8.924  1.00 39.37           O  
ANISOU  113  OG1 THR A  17     5224   3655   6079      3    777  -1093       O  
ATOM    114  CG2 THR A  17      10.617 -62.750   7.882  1.00 31.13           C  
ANISOU  114  CG2 THR A  17     4189   2569   5068     14    945  -1195       C  
ATOM    115  N   HIS A  18      12.694 -60.512   5.342  1.00 32.28           N  
ANISOU  115  N   HIS A  18     4187   2968   5108   -129    847  -1193       N  
ATOM    116  CA  HIS A  18      13.097 -60.948   4.008  1.00 36.98           C  
ANISOU  116  CA  HIS A  18     4759   3608   5684   -184    905  -1250       C  
ATOM    117  C   HIS A  18      14.301 -60.203   3.431  1.00 35.82           C  
ANISOU  117  C   HIS A  18     4552   3547   5513   -200    871  -1235       C  
ATOM    118  O   HIS A  18      14.665 -60.401   2.272  1.00 33.08           O  
ANISOU  118  O   HIS A  18     4179   3246   5143   -251    909  -1279       O  
ATOM    119  CB  HIS A  18      11.904 -60.867   3.061  1.00 37.24           C  
ANISOU  119  CB  HIS A  18     4813   3656   5682   -282    911  -1292       C  
ATOM    120  CG  HIS A  18      10.808 -61.825   3.409  1.00 38.02           C  
ANISOU  120  CG  HIS A  18     4968   3670   5806   -271    964  -1322       C  
ATOM    121  ND1 HIS A  18       9.590 -61.419   3.913  1.00 34.86           N  
ANISOU  121  ND1 HIS A  18     4605   3241   5401   -292    921  -1302       N  
ATOM    122  CD2 HIS A  18      10.758 -63.177   3.347  1.00 35.48           C  
ANISOU  122  CD2 HIS A  18     4674   3288   5517   -240   1058  -1369       C  
ATOM    123  CE1 HIS A  18       8.830 -62.480   4.128  1.00 35.92           C  
ANISOU  123  CE1 HIS A  18     4785   3301   5563   -276    986  -1336       C  
ATOM    124  NE2 HIS A  18       9.516 -63.558   3.791  1.00 35.59           N  
ANISOU  124  NE2 HIS A  18     4740   3239   5545   -245   1069  -1377       N  
ATOM    125  N   ARG A  19      14.903 -59.344   4.247  1.00 36.48           N  
ANISOU  125  N   ARG A  19     4611   3649   5600   -155    799  -1171       N  
ATOM    126  CA  ARG A  19      16.174 -58.707   3.911  1.00 32.17           C  
ANISOU  126  CA  ARG A  19     4007   3175   5040   -152    768  -1150       C  
ATOM    127  C   ARG A  19      17.295 -59.661   4.277  1.00 34.10           C  
ANISOU  127  C   ARG A  19     4240   3388   5327    -67    832  -1158       C  
ATOM    128  O   ARG A  19      17.129 -60.485   5.172  1.00 32.12           O  
ANISOU  128  O   ARG A  19     4025   3059   5119      4    870  -1155       O  
ATOM    129  CB  ARG A  19      16.353 -57.415   4.714  1.00 27.42           C  
ANISOU  129  CB  ARG A  19     3388   2603   4428   -134    663  -1076       C  
ATOM    130  CG  ARG A  19      15.479 -56.258   4.275  1.00 33.58           C  
ANISOU  130  CG  ARG A  19     4167   3432   5159   -220    586  -1062       C  
ATOM    131  CD  ARG A  19      16.222 -55.352   3.330  1.00 38.85           C  
ANISOU  131  CD  ARG A  19     4780   4196   5786   -278    546  -1057       C  
ATOM    132  NE  ARG A  19      15.389 -54.281   2.794  1.00 42.19           N  
ANISOU  132  NE  ARG A  19     5201   4668   6159   -366    477  -1049       N  
ATOM    133  CZ  ARG A  19      15.812 -53.412   1.882  1.00 44.31           C  
ANISOU  133  CZ  ARG A  19     5427   5023   6385   -431    437  -1047       C  
ATOM    134  NH1 ARG A  19      17.053 -53.494   1.411  1.00 41.81           N  
ANISOU  134  NH1 ARG A  19     5065   4751   6069   -419    459  -1053       N  
ATOM    135  NH2 ARG A  19      15.001 -52.469   1.432  1.00 40.28           N  
ANISOU  135  NH2 ARG A  19     4919   4553   5832   -510    375  -1040       N  
ATOM    136  N   PRO A  20      18.455 -59.541   3.603  1.00 34.02           N  
ANISOU  136  N   PRO A  20     4181   3439   5308    -73    844  -1166       N  
ATOM    137  CA  PRO A  20      19.609 -60.329   4.042  1.00 34.71           C  
ANISOU  137  CA  PRO A  20     4252   3500   5436     12    896  -1166       C  
ATOM    138  C   PRO A  20      19.906 -60.020   5.504  1.00 37.28           C  
ANISOU  138  C   PRO A  20     4585   3786   5795    100    845  -1101       C  
ATOM    139  O   PRO A  20      19.670 -58.899   5.955  1.00 30.21           O  
ANISOU  139  O   PRO A  20     3682   2916   4880     88    756  -1050       O  
ATOM    140  CB  PRO A  20      20.755 -59.812   3.162  1.00 33.68           C  
ANISOU  140  CB  PRO A  20     4059   3457   5281    -17    885  -1168       C  
ATOM    141  CG  PRO A  20      20.107 -59.121   2.020  1.00 36.39           C  
ANISOU  141  CG  PRO A  20     4394   3863   5571   -126    857  -1191       C  
ATOM    142  CD  PRO A  20      18.797 -58.598   2.524  1.00 31.96           C  
ANISOU  142  CD  PRO A  20     3873   3273   4998   -153    803  -1169       C  
ATOM    143  N   ARG A  21      20.419 -61.005   6.230  1.00 37.42           N  
ANISOU  143  N   ARG A  21     4617   3741   5861    188    900  -1104       N  
ATOM    144  CA  ARG A  21      20.750 -60.838   7.641  1.00 36.04           C  
ANISOU  144  CA  ARG A  21     4451   3521   5720    278    859  -1046       C  
ATOM    145  C   ARG A  21      21.672 -59.640   7.898  1.00 32.18           C  
ANISOU  145  C   ARG A  21     3912   3097   5217    289    775   -987       C  
ATOM    146  O   ARG A  21      21.509 -58.937   8.888  1.00 30.57           O  
ANISOU  146  O   ARG A  21     3718   2879   5019    323    703   -930       O  
ATOM    147  CB  ARG A  21      21.373 -62.126   8.183  1.00 40.30           C  
ANISOU  147  CB  ARG A  21     5005   3995   6313    367    939  -1064       C  
ATOM    148  CG  ARG A  21      21.677 -62.128   9.669  1.00 42.05           C  
ANISOU  148  CG  ARG A  21     5242   4160   6574    466    909  -1009       C  
ATOM    149  CD  ARG A  21      21.910 -63.551  10.157  1.00 50.92           C  
ANISOU  149  CD  ARG A  21     6395   5203   7747    543    997  -1038       C  
ATOM    150  NE  ARG A  21      22.545 -63.597  11.472  1.00 59.73           N  
ANISOU  150  NE  ARG A  21     7516   6276   8904    643    974   -987       N  
ATOM    151  CZ  ARG A  21      21.925 -63.936  12.599  1.00 65.53           C  
ANISOU  151  CZ  ARG A  21     8299   6932   9668    700    971   -965       C  
ATOM    152  NH1 ARG A  21      20.638 -64.264  12.586  1.00 68.26           N  
ANISOU  152  NH1 ARG A  21     8693   7234  10008    666    990   -988       N  
ATOM    153  NH2 ARG A  21      22.597 -63.951  13.743  1.00 65.89           N  
ANISOU  153  NH2 ARG A  21     8344   6943   9748    791    948   -919       N  
ATOM    154  N   GLU A  22      22.639 -59.413   7.011  1.00 26.59           N  
ANISOU  154  N   GLU A  22     3152   2459   4491    261    782  -1001       N  
ATOM    155  CA  GLU A  22      23.559 -58.283   7.140  1.00 27.88           C  
ANISOU  155  CA  GLU A  22     3264   2689   4639    266    705   -949       C  
ATOM    156  C   GLU A  22      22.824 -56.942   7.224  1.00 26.97           C  
ANISOU  156  C   GLU A  22     3149   2613   4484    209    606   -908       C  
ATOM    157  O   GLU A  22      23.340 -55.981   7.798  1.00 29.49           O  
ANISOU  157  O   GLU A  22     3443   2962   4799    232    528   -850       O  
ATOM    158  CB  GLU A  22      24.540 -58.252   5.963  1.00 29.37           C  
ANISOU  158  CB  GLU A  22     3399   2953   4807    226    733   -979       C  
ATOM    159  CG  GLU A  22      23.853 -58.257   4.602  1.00 47.78           C  
ANISOU  159  CG  GLU A  22     5732   5326   7096    123    761  -1034       C  
ATOM    160  CD  GLU A  22      24.822 -58.191   3.430  1.00 62.08           C  
ANISOU  160  CD  GLU A  22     7489   7212   8885     82    788  -1062       C  
ATOM    161  OE1 GLU A  22      26.051 -58.129   3.664  1.00 61.20           O  
ANISOU  161  OE1 GLU A  22     7337   7123   8791    134    785  -1039       O  
ATOM    162  OE2 GLU A  22      24.347 -58.200   2.270  1.00 65.47           O  
ANISOU  162  OE2 GLU A  22     7917   7678   9278     -2    812  -1108       O  
ATOM    163  N   TYR A  23      21.627 -56.875   6.644  1.00 24.08           N  
ANISOU  163  N   TYR A  23     2814   2247   4090    134    609   -938       N  
ATOM    164  CA  TYR A  23      20.863 -55.632   6.635  1.00 18.77           C  
ANISOU  164  CA  TYR A  23     2143   1612   3378     74    518   -904       C  
ATOM    165  C   TYR A  23      20.475 -55.171   8.042  1.00 22.62           C  
ANISOU  165  C   TYR A  23     2658   2051   3884    134    454   -843       C  
ATOM    166  O   TYR A  23      20.655 -54.005   8.389  1.00 21.90           O  
ANISOU  166  O   TYR A  23     2546   2000   3774    127    365   -790       O  
ATOM    167  CB  TYR A  23      19.615 -55.749   5.751  1.00 19.50           C  
ANISOU  167  CB  TYR A  23     2264   1707   3438    -15    540   -951       C  
ATOM    168  CG  TYR A  23      18.807 -54.468   5.689  1.00 20.47           C  
ANISOU  168  CG  TYR A  23     2389   1870   3518    -80    448   -919       C  
ATOM    169  CD1 TYR A  23      19.171 -53.446   4.831  1.00 24.15           C  
ANISOU  169  CD1 TYR A  23     2811   2426   3940   -149    396   -911       C  
ATOM    170  CD2 TYR A  23      17.690 -54.278   6.500  1.00 19.19           C  
ANISOU  170  CD2 TYR A  23     2273   1656   3361    -71    412   -895       C  
ATOM    171  CE1 TYR A  23      18.454 -52.260   4.772  1.00 18.81           C  
ANISOU  171  CE1 TYR A  23     2136   1786   3224   -208    310   -880       C  
ATOM    172  CE2 TYR A  23      16.961 -53.090   6.454  1.00 17.09           C  
ANISOU  172  CE2 TYR A  23     2008   1427   3057   -129    326   -865       C  
ATOM    173  CZ  TYR A  23      17.351 -52.083   5.582  1.00 17.84           C  
ANISOU  173  CZ  TYR A  23     2059   1612   3108   -198    275   -857       C  
ATOM    174  OH  TYR A  23      16.655 -50.893   5.497  1.00 17.48           O  
ANISOU  174  OH  TYR A  23     2013   1606   3022   -257    189   -828       O  
ATOM    175  N   TRP A  24      19.940 -56.087   8.844  1.00 21.93           N  
ANISOU  175  N   TRP A  24     2620   1877   3835    191    499   -852       N  
ATOM    176  CA  TRP A  24      19.401 -55.725  10.162  1.00 21.58           C  
ANISOU  176  CA  TRP A  24     2610   1780   3809    243    444   -799       C  
ATOM    177  C   TRP A  24      20.253 -56.195  11.353  1.00 22.11           C  
ANISOU  177  C   TRP A  24     2679   1795   3925    355    454   -765       C  
ATOM    178  O   TRP A  24      20.078 -55.721  12.479  1.00 19.22           O  
ANISOU  178  O   TRP A  24     2332   1398   3573    404    396   -711       O  
ATOM    179  CB  TRP A  24      17.965 -56.241  10.304  1.00 20.96           C  
ANISOU  179  CB  TRP A  24     2590   1640   3734    221    472   -825       C  
ATOM    180  CG  TRP A  24      17.844 -57.693  10.030  1.00 20.25           C  
ANISOU  180  CG  TRP A  24     2526   1494   3673    240    579   -885       C  
ATOM    181  CD1 TRP A  24      17.385 -58.281   8.882  1.00 27.80           C  
ANISOU  181  CD1 TRP A  24     3489   2463   4612    173    642   -949       C  
ATOM    182  CD2 TRP A  24      18.205 -58.760  10.910  1.00 21.59           C  
ANISOU  182  CD2 TRP A  24     2721   1587   3894    334    637   -886       C  
ATOM    183  NE1 TRP A  24      17.437 -59.651   9.000  1.00 28.10           N  
ANISOU  183  NE1 TRP A  24     3553   2435   4688    219    736   -990       N  
ATOM    184  CE2 TRP A  24      17.932 -59.969  10.238  1.00 25.70           C  
ANISOU  184  CE2 TRP A  24     3262   2077   4427    318    734   -952       C  
ATOM    185  CE3 TRP A  24      18.724 -58.812  12.205  1.00 21.98           C  
ANISOU  185  CE3 TRP A  24     2779   1592   3982    430    615   -837       C  
ATOM    186  CZ2 TRP A  24      18.166 -61.215  10.819  1.00 32.78           C  
ANISOU  186  CZ2 TRP A  24     4186   2898   5372    395    809   -971       C  
ATOM    187  CZ3 TRP A  24      18.957 -60.051  12.780  1.00 23.29           C  
ANISOU  187  CZ3 TRP A  24     2972   1683   4195    506    690   -856       C  
ATOM    188  CH2 TRP A  24      18.673 -61.234  12.088  1.00 32.48           C  
ANISOU  188  CH2 TRP A  24     4155   2817   5370    488    786   -922       C  
ATOM    189  N   ASP A  25      21.167 -57.130  11.108  1.00 25.51           N  
ANISOU  189  N   ASP A  25     3094   2216   4384    395    528   -795       N  
ATOM    190  CA  ASP A  25      22.022 -57.664  12.168  1.00 23.59           C  
ANISOU  190  CA  ASP A  25     2852   1924   4189    501    544   -768       C  
ATOM    191  C   ASP A  25      23.178 -56.701  12.412  1.00 21.98           C  
ANISOU  191  C   ASP A  25     2595   1778   3979    525    474   -716       C  
ATOM    192  O   ASP A  25      24.328 -56.996  12.075  1.00 25.57           O  
ANISOU  192  O   ASP A  25     3010   2260   4445    549    506   -726       O  
ATOM    193  CB  ASP A  25      22.538 -59.051  11.778  1.00 26.72           C  
ANISOU  193  CB  ASP A  25     3250   2287   4617    533    651   -823       C  
ATOM    194  CG  ASP A  25      23.374 -59.709  12.871  1.00 29.58           C  
ANISOU  194  CG  ASP A  25     3618   2591   5031    644    675   -799       C  
ATOM    195  OD1 ASP A  25      23.339 -59.260  14.035  1.00 34.11           O  
ANISOU  195  OD1 ASP A  25     4207   3134   5621    700    618   -744       O  
ATOM    196  OD2 ASP A  25      24.069 -60.696  12.560  1.00 39.64           O  
ANISOU  196  OD2 ASP A  25     4882   3851   6330    676    753   -837       O  
ATOM    197  N   TYR A  26      22.863 -55.547  12.991  1.00 19.11           N  
ANISOU  197  N   TYR A  26     2232   1433   3597    518    379   -660       N  
ATOM    198  CA  TYR A  26      23.839 -54.474  13.156  1.00 24.13           C  
ANISOU  198  CA  TYR A  26     2819   2131   4220    528    302   -608       C  
ATOM    199  C   TYR A  26      24.998 -54.829  14.081  1.00 26.18           C  
ANISOU  199  C   TYR A  26     3063   2361   4524    630    309   -576       C  
ATOM    200  O   TYR A  26      26.073 -54.239  13.984  1.00 25.78           O  
ANISOU  200  O   TYR A  26     2962   2365   4468    640    271   -548       O  
ATOM    201  CB  TYR A  26      23.165 -53.187  13.635  1.00 25.24           C  
ANISOU  201  CB  TYR A  26     2968   2291   4331    499    199   -555       C  
ATOM    202  CG  TYR A  26      22.463 -53.309  14.971  1.00 29.33           C  
ANISOU  202  CG  TYR A  26     3537   2730   4875    562    176   -520       C  
ATOM    203  CD1 TYR A  26      23.164 -53.170  16.161  1.00 25.55           C  
ANISOU  203  CD1 TYR A  26     3057   2221   4429    653    141   -467       C  
ATOM    204  CD2 TYR A  26      21.096 -53.553  15.039  1.00 28.83           C  
ANISOU  204  CD2 TYR A  26     3526   2622   4806    531    189   -539       C  
ATOM    205  CE1 TYR A  26      22.523 -53.272  17.385  1.00 30.86           C  
ANISOU  205  CE1 TYR A  26     3779   2821   5126    711    120   -434       C  
ATOM    206  CE2 TYR A  26      20.447 -53.655  16.261  1.00 31.11           C  
ANISOU  206  CE2 TYR A  26     3862   2839   5119    589    169   -507       C  
ATOM    207  CZ  TYR A  26      21.169 -53.517  17.427  1.00 32.80           C  
ANISOU  207  CZ  TYR A  26     4074   3024   5363    678    135   -454       C  
ATOM    208  OH  TYR A  26      20.534 -53.616  18.640  1.00 46.14           O  
ANISOU  208  OH  TYR A  26     5813   4643   7077    736    115   -422       O  
ATOM    209  N   GLU A  27      24.781 -55.787  14.975  1.00 30.09           N  
ANISOU  209  N   GLU A  27     3601   2769   5062    704    355   -580       N  
ATOM    210  CA  GLU A  27      25.817 -56.172  15.926  1.00 33.50           C  
ANISOU  210  CA  GLU A  27     4024   3166   5539    805    362   -549       C  
ATOM    211  C   GLU A  27      27.064 -56.717  15.227  1.00 34.74           C  
ANISOU  211  C   GLU A  27     4134   3359   5708    818    419   -579       C  
ATOM    212  O   GLU A  27      28.171 -56.640  15.770  1.00 31.43           O  
ANISOU  212  O   GLU A  27     3686   2944   5314    883    403   -547       O  
ATOM    213  CB  GLU A  27      25.273 -57.172  16.952  1.00 39.01           C  
ANISOU  213  CB  GLU A  27     4781   3763   6280    879    409   -553       C  
ATOM    214  CG  GLU A  27      24.503 -56.523  18.096  1.00 41.96           C  
ANISOU  214  CG  GLU A  27     5192   4096   6653    906    336   -499       C  
ATOM    215  CD  GLU A  27      23.580 -57.496  18.817  1.00 51.75           C  
ANISOU  215  CD  GLU A  27     6497   5241   7924    948    387   -515       C  
ATOM    216  OE1 GLU A  27      22.369 -57.520  18.497  1.00 59.76           O  
ANISOU  216  OE1 GLU A  27     7545   6242   8918    891    395   -539       O  
ATOM    217  OE2 GLU A  27      24.059 -58.232  19.705  1.00 53.70           O  
ANISOU  217  OE2 GLU A  27     6761   5427   8216   1037    419   -504       O  
ATOM    218  N   SER A  28      26.886 -57.236  14.014  1.00 30.96           N  
ANISOU  218  N   SER A  28     3646   2906   5211    754    484   -641       N  
ATOM    219  CA  SER A  28      27.990 -57.828  13.269  1.00 36.58           C  
ANISOU  219  CA  SER A  28     4316   3650   5933    761    546   -676       C  
ATOM    220  C   SER A  28      28.534 -56.868  12.216  1.00 30.71           C  
ANISOU  220  C   SER A  28     3514   3008   5146    687    505   -674       C  
ATOM    221  O   SER A  28      29.439 -57.215  11.458  1.00 32.55           O  
ANISOU  221  O   SER A  28     3707   3280   5380    680    550   -703       O  
ATOM    222  CB  SER A  28      27.553 -59.137  12.608  1.00 44.54           C  
ANISOU  222  CB  SER A  28     5352   4619   6952    746    652   -748       C  
ATOM    223  OG  SER A  28      26.789 -58.886  11.439  1.00 53.21           O  
ANISOU  223  OG  SER A  28     6449   5761   8006    644    660   -788       O  
ATOM    224  N   HIS A  29      27.977 -55.663  12.173  1.00 25.16           N  
ANISOU  224  N   HIS A  29     2807   2347   4404    631    419   -640       N  
ATOM    225  CA  HIS A  29      28.439 -54.637  11.241  1.00 21.69           C  
ANISOU  225  CA  HIS A  29     2315   2004   3922    559    370   -632       C  
ATOM    226  C   HIS A  29      29.912 -54.280  11.461  1.00 26.62           C  
ANISOU  226  C   HIS A  29     2884   2669   4561    608    344   -597       C  
ATOM    227  O   HIS A  29      30.346 -54.020  12.583  1.00 27.29           O  
ANISOU  227  O   HIS A  29     2971   2726   4674    681    299   -545       O  
ATOM    228  CB  HIS A  29      27.585 -53.373  11.353  1.00 23.44           C  
ANISOU  228  CB  HIS A  29     2546   2256   4104    502    276   -594       C  
ATOM    229  CG  HIS A  29      27.979 -52.301  10.384  1.00 27.70           C  
ANISOU  229  CG  HIS A  29     3034   2894   4598    424    224   -587       C  
ATOM    230  ND1 HIS A  29      27.807 -52.433   9.024  1.00 25.50           N  
ANISOU  230  ND1 HIS A  29     2739   2665   4285    341    265   -640       N  
ATOM    231  CD2 HIS A  29      28.567 -51.096  10.575  1.00 29.49           C  
ANISOU  231  CD2 HIS A  29     3222   3178   4805    418    135   -532       C  
ATOM    232  CE1 HIS A  29      28.260 -51.350   8.417  1.00 32.65           C  
ANISOU  232  CE1 HIS A  29     3598   3655   5154    286    204   -618       C  
ATOM    233  NE2 HIS A  29      28.725 -50.521   9.336  1.00 30.23           N  
ANISOU  233  NE2 HIS A  29     3277   3354   4855    331    125   -553       N  
ATOM    234  N   VAL A  30      30.679 -54.267  10.380  1.00 25.27           N  
ANISOU  234  N   VAL A  30     2664   2564   4373    566    372   -626       N  
ATOM    235  CA  VAL A  30      32.069 -53.837  10.449  1.00 27.58           C  
ANISOU  235  CA  VAL A  30     2899   2905   4675    600    344   -594       C  
ATOM    236  C   VAL A  30      32.195 -52.409   9.928  1.00 31.06           C  
ANISOU  236  C   VAL A  30     3299   3434   5068    529    256   -560       C  
ATOM    237  O   VAL A  30      31.979 -52.142   8.742  1.00 31.42           O  
ANISOU  237  O   VAL A  30     3326   3538   5074    443    266   -594       O  
ATOM    238  CB  VAL A  30      32.991 -54.763   9.647  1.00 32.05           C  
ANISOU  238  CB  VAL A  30     3433   3488   5256    609    433   -643       C  
ATOM    239  CG1 VAL A  30      34.410 -54.192   9.598  1.00 37.88           C  
ANISOU  239  CG1 VAL A  30     4107   4288   5999    632    399   -610       C  
ATOM    240  CG2 VAL A  30      32.992 -56.153  10.259  1.00 36.74           C  
ANISOU  240  CG2 VAL A  30     4064   3994   5900    688    516   -671       C  
ATOM    241  N   VAL A  31      32.548 -51.492  10.821  1.00 26.69           N  
ANISOU  241  N   VAL A  31     2733   2889   4519    566    169   -494       N  
ATOM    242  CA  VAL A  31      32.630 -50.086  10.462  1.00 29.93           C  
ANISOU  242  CA  VAL A  31     3109   3377   4885    504     78   -457       C  
ATOM    243  C   VAL A  31      33.782 -49.805   9.501  1.00 29.17           C  
ANISOU  243  C   VAL A  31     2946   3363   4773    472     86   -467       C  
ATOM    244  O   VAL A  31      34.892 -50.299   9.690  1.00 32.69           O  
ANISOU  244  O   VAL A  31     3363   3807   5253    532    120   -465       O  
ATOM    245  CB  VAL A  31      32.763 -49.203  11.714  1.00 29.72           C  
ANISOU  245  CB  VAL A  31     3086   3336   4869    557    -17   -382       C  
ATOM    246  CG1 VAL A  31      33.047 -47.759  11.324  1.00 31.63           C  
ANISOU  246  CG1 VAL A  31     3285   3664   5068    498   -110   -342       C  
ATOM    247  CG2 VAL A  31      31.494 -49.294  12.554  1.00 31.17           C  
ANISOU  247  CG2 VAL A  31     3336   3449   5059    573    -35   -370       C  
ATOM    248  N   GLU A  32      33.506 -49.022   8.463  1.00 30.99           N  
ANISOU  248  N   GLU A  32     3154   3667   4954    377     56   -478       N  
ATOM    249  CA  GLU A  32      34.537 -48.569   7.534  1.00 35.78           C  
ANISOU  249  CA  GLU A  32     3697   4359   5539    337     51   -482       C  
ATOM    250  C   GLU A  32      34.983 -47.149   7.904  1.00 36.55           C  
ANISOU  250  C   GLU A  32     3760   4511   5616    329    -59   -415       C  
ATOM    251  O   GLU A  32      34.229 -46.180   7.732  1.00 28.88           O  
ANISOU  251  O   GLU A  32     2798   3569   4605    266   -128   -395       O  
ATOM    252  CB  GLU A  32      34.016 -48.616   6.095  1.00 44.73           C  
ANISOU  252  CB  GLU A  32     4826   5541   6630    236     90   -539       C  
ATOM    253  CG  GLU A  32      35.001 -48.118   5.044  1.00 58.64           C  
ANISOU  253  CG  GLU A  32     6522   7393   8364    187     86   -546       C  
ATOM    254  CD  GLU A  32      34.422 -48.158   3.636  1.00 68.68           C  
ANISOU  254  CD  GLU A  32     7793   8710   9591     86    123   -602       C  
ATOM    255  OE1 GLU A  32      33.430 -48.891   3.422  1.00 69.49           O  
ANISOU  255  OE1 GLU A  32     7943   8767   9693     66    176   -646       O  
ATOM    256  OE2 GLU A  32      34.954 -47.454   2.748  1.00 71.27           O  
ANISOU  256  OE2 GLU A  32     8074   9121   9885     26     98   -601       O  
ATOM    257  N   TRP A  33      36.207 -47.033   8.415  1.00 28.21           N  
ANISOU  257  N   TRP A  33     2892   3925   3902     74    582   -704       N  
ATOM    258  CA  TRP A  33      36.697 -45.766   8.962  1.00 29.78           C  
ANISOU  258  CA  TRP A  33     3106   4157   4053     41    544   -647       C  
ATOM    259  C   TRP A  33      37.291 -44.837   7.913  1.00 27.70           C  
ANISOU  259  C   TRP A  33     2878   3930   3717     50    466   -611       C  
ATOM    260  O   TRP A  33      38.052 -45.266   7.039  1.00 25.31           O  
ANISOU  260  O   TRP A  33     2593   3660   3365     77    469   -570       O  
ATOM    261  CB  TRP A  33      37.739 -46.023  10.055  1.00 27.02           C  
ANISOU  261  CB  TRP A  33     2751   3849   3664     18    613   -554       C  
ATOM    262  CG  TRP A  33      37.227 -46.906  11.145  1.00 27.32           C  
ANISOU  262  CG  TRP A  33     2756   3855   3768      5    690   -582       C  
ATOM    263  CD1 TRP A  33      37.440 -48.251  11.282  1.00 28.91           C  
ANISOU  263  CD1 TRP A  33     2944   4052   3990     22    767   -575       C  
ATOM    264  CD2 TRP A  33      36.401 -46.516  12.243  1.00 28.69           C  
ANISOU  264  CD2 TRP A  33     2908   3995   3998    -26    698   -624       C  
ATOM    265  NE1 TRP A  33      36.798 -48.717  12.404  1.00 28.81           N  
ANISOU  265  NE1 TRP A  33     2902   4005   4041      2    822   -609       N  
ATOM    266  CE2 TRP A  33      36.150 -47.673  13.011  1.00 31.32           C  
ANISOU  266  CE2 TRP A  33     3214   4305   4383    -28    783   -639       C  
ATOM    267  CE3 TRP A  33      35.839 -45.301  12.650  1.00 27.14           C  
ANISOU  267  CE3 TRP A  33     2712   3786   3814    -52    642   -651       C  
ATOM    268  CZ2 TRP A  33      35.365 -47.649  14.163  1.00 37.21           C  
ANISOU  268  CZ2 TRP A  33     3932   5017   5190    -55    813   -680       C  
ATOM    269  CZ3 TRP A  33      35.060 -45.281  13.801  1.00 31.89           C  
ANISOU  269  CZ3 TRP A  33     3286   4354   4477    -78    673   -692       C  
ATOM    270  CH2 TRP A  33      34.834 -46.446  14.543  1.00 36.40           C  
ANISOU  270  CH2 TRP A  33     3830   4904   5097    -80    758   -705       C  
ATOM    271  N   GLY A  34      36.958 -43.557   8.018  1.00 19.32           N  
ANISOU  271  N   GLY A  34     1826   2865   2648     29    397   -623       N  
ATOM    272  CA  GLY A  34      37.572 -42.551   7.175  1.00 20.89           C  
ANISOU  272  CA  GLY A  34     2061   3102   2776     31    323   -580       C  
ATOM    273  C   GLY A  34      38.796 -41.952   7.849  1.00 20.68           C  
ANISOU  273  C   GLY A  34     2047   3134   2675      2    334   -470       C  
ATOM    274  O   GLY A  34      39.281 -42.471   8.855  1.00 19.71           O  
ANISOU  274  O   GLY A  34     1909   3027   2552    -13    406   -423       O  
ATOM    275  N   ASN A  35      39.285 -40.850   7.297  1.00 21.08           N  
ANISOU  275  N   ASN A  35     2129   3217   2665     -5    263   -430       N  
ATOM    276  CA  ASN A  35      40.481 -40.203   7.827  1.00 21.01           C  
ANISOU  276  CA  ASN A  35     2135   3266   2581    -31    266   -325       C  
ATOM    277  C   ASN A  35      40.111 -39.067   8.755  1.00 19.67           C  
ANISOU  277  C   ASN A  35     1964   3086   2425    -69    230   -329       C  
ATOM    278  O   ASN A  35      39.546 -38.064   8.329  1.00 19.55           O  
ANISOU  278  O   ASN A  35     1963   3053   2414    -74    150   -369       O  
ATOM    279  CB  ASN A  35      41.362 -39.685   6.696  1.00 31.70           C  
ANISOU  279  CB  ASN A  35     3524   4667   3853    -18    212   -268       C  
ATOM    280  CG  ASN A  35      41.922 -40.801   5.852  1.00 45.33           C  
ANISOU  280  CG  ASN A  35     5254   6415   5556     18    253   -249       C  
ATOM    281  OD1 ASN A  35      42.064 -41.930   6.320  1.00 43.96           O  
ANISOU  281  OD1 ASN A  35     5058   6237   5406     27    332   -243       O  
ATOM    282  ND2 ASN A  35      42.243 -40.498   4.598  1.00 56.99           N  
ANISOU  282  ND2 ASN A  35     6758   7913   6985     39    198   -239       N  
ATOM    283  N   GLN A  36      40.437 -39.226  10.032  1.00 19.13           N  
ANISOU  283  N   GLN A  36     1878   3028   2362    -95    289   -287       N  
ATOM    284  CA  GLN A  36      40.078 -38.230  11.033  1.00 15.71           C  
ANISOU  284  CA  GLN A  36     1441   2584   1945   -132    263   -292       C  
ATOM    285  C   GLN A  36      40.659 -36.855  10.698  1.00 19.46           C  
ANISOU  285  C   GLN A  36     1948   3095   2353   -149    183   -239       C  
ATOM    286  O   GLN A  36      40.077 -35.830  11.049  1.00 17.88           O  
ANISOU  286  O   GLN A  36     1750   2873   2170   -170    128   -270       O  
ATOM    287  CB  GLN A  36      40.530 -38.708  12.416  1.00 21.17           C  
ANISOU  287  CB  GLN A  36     2112   3289   2642   -155    345   -242       C  
ATOM    288  CG  GLN A  36      40.075 -37.832  13.577  1.00 21.47           C  
ANISOU  288  CG  GLN A  36     2141   3311   2706   -192    330   -253       C  
ATOM    289  CD  GLN A  36      41.051 -36.700  13.877  1.00 21.25           C  
ANISOU  289  CD  GLN A  36     2137   3332   2603   -219    291   -164       C  
ATOM    290  OE1 GLN A  36      42.212 -36.745  13.473  1.00 23.76           O  
ANISOU  290  OE1 GLN A  36     2475   3702   2851   -215    296    -80       O  
ATOM    291  NE2 GLN A  36      40.574 -35.676  14.584  1.00 19.55           N  
ANISOU  291  NE2 GLN A  36     1921   3102   2405   -247    250   -183       N  
ATOM    292  N   ASP A  37      41.806 -36.835  10.021  1.00 18.94           N  
ANISOU  292  N   ASP A  37     1906   3082   2209   -140    176   -159       N  
ATOM    293  CA  ASP A  37      42.446 -35.578   9.656  1.00 17.14           C  
ANISOU  293  CA  ASP A  37     1709   2891   1912   -156    102   -102       C  
ATOM    294  C   ASP A  37      41.708 -34.792   8.571  1.00 23.36           C  
ANISOU  294  C   ASP A  37     2517   3652   2707   -144      8   -166       C  
ATOM    295  O   ASP A  37      42.053 -33.642   8.309  1.00 24.20           O  
ANISOU  295  O   ASP A  37     2649   3780   2765   -160    -62   -130       O  
ATOM    296  CB  ASP A  37      43.906 -35.808   9.250  1.00 25.11           C  
ANISOU  296  CB  ASP A  37     2738   3967   2836   -151    125      4       C  
ATOM    297  CG  ASP A  37      44.052 -36.918   8.238  1.00 40.71           C  
ANISOU  297  CG  ASP A  37     4713   5946   4809   -111    155    -10       C  
ATOM    298  OD1 ASP A  37      43.788 -38.085   8.603  1.00 45.25           O  
ANISOU  298  OD1 ASP A  37     5263   6501   5430    -97    229    -38       O  
ATOM    299  OD2 ASP A  37      44.420 -36.624   7.078  1.00 50.04           O  
ANISOU  299  OD2 ASP A  37     5919   7151   5942    -94    106      6       O  
ATOM    300  N   ASP A  38      40.684 -35.392   7.957  1.00 18.40           N  
ANISOU  300  N   ASP A  38     1876   2975   2140   -116      4   -260       N  
ATOM    301  CA  ASP A  38      39.933 -34.694   6.916  1.00 17.82           C  
ANISOU  301  CA  ASP A  38     1821   2874   2077   -102    -85   -325       C  
ATOM    302  C   ASP A  38      39.051 -33.588   7.483  1.00 19.39           C  
ANISOU  302  C   ASP A  38     2017   3036   2313   -127   -144   -376       C  
ATOM    303  O   ASP A  38      38.601 -32.706   6.745  1.00 20.59           O  
ANISOU  303  O   ASP A  38     2190   3174   2461   -124   -229   -413       O  
ATOM    304  CB  ASP A  38      39.047 -35.657   6.124  1.00 21.36           C  
ANISOU  304  CB  ASP A  38     2255   3277   2582    -65    -72   -414       C  
ATOM    305  CG  ASP A  38      39.822 -36.499   5.148  1.00 20.81           C  
ANISOU  305  CG  ASP A  38     2198   3241   2468    -33    -46   -375       C  
ATOM    306  OD1 ASP A  38      41.054 -36.289   5.012  1.00 19.37           O  
ANISOU  306  OD1 ASP A  38     2035   3118   2207    -40    -41   -279       O  
ATOM    307  OD2 ASP A  38      39.193 -37.374   4.512  1.00 22.14           O  
ANISOU  307  OD2 ASP A  38     2356   3376   2680     -2    -29   -442       O  
ATOM    308  N   TYR A  39      38.792 -33.639   8.788  1.00 17.12           N  
ANISOU  308  N   TYR A  39     1705   2735   2064   -152    -99   -380       N  
ATOM    309  CA  TYR A  39      37.806 -32.746   9.401  1.00 21.33           C  
ANISOU  309  CA  TYR A  39     2230   3228   2646   -173   -145   -442       C  
ATOM    310  C   TYR A  39      38.407 -31.895  10.505  1.00 25.65           C  
ANISOU  310  C   TYR A  39     2783   3805   3160   -211   -147   -373       C  
ATOM    311  O   TYR A  39      39.029 -32.407  11.441  1.00 26.89           O  
ANISOU  311  O   TYR A  39     2925   3985   3306   -226    -73   -317       O  
ATOM    312  CB  TYR A  39      36.600 -33.553   9.906  1.00 17.99           C  
ANISOU  312  CB  TYR A  39     1769   2747   2318   -164    -99   -538       C  
ATOM    313  CG  TYR A  39      36.103 -34.481   8.839  1.00 22.60           C  
ANISOU  313  CG  TYR A  39     2349   3305   2933   -125    -91   -599       C  
ATOM    314  CD1 TYR A  39      35.264 -34.016   7.829  1.00 17.51           C  
ANISOU  314  CD1 TYR A  39     1715   2625   2311   -107   -169   -675       C  
ATOM    315  CD2 TYR A  39      36.515 -35.808   8.797  1.00 22.55           C  
ANISOU  315  CD2 TYR A  39     2329   3310   2931   -106    -10   -578       C  
ATOM    316  CE1 TYR A  39      34.838 -34.852   6.825  1.00 18.86           C  
ANISOU  316  CE1 TYR A  39     1884   2773   2508    -71   -164   -729       C  
ATOM    317  CE2 TYR A  39      36.089 -36.654   7.794  1.00 17.79           C  
ANISOU  317  CE2 TYR A  39     1723   2684   2354    -70     -5   -633       C  
ATOM    318  CZ  TYR A  39      35.244 -36.168   6.815  1.00 19.20           C  
ANISOU  318  CZ  TYR A  39     1912   2828   2555    -53    -82   -708       C  
ATOM    319  OH  TYR A  39      34.814 -37.000   5.816  1.00 19.34           O  
ANISOU  319  OH  TYR A  39     1927   2821   2599    -16    -78   -763       O  
ATOM    320  N   GLN A  40      38.242 -30.585  10.364  1.00 20.44           N  
ANISOU  320  N   GLN A  40     2144   3143   2480   -228   -233   -377       N  
ATOM    321  CA  GLN A  40      38.687 -29.645  11.379  1.00 23.33           C  
ANISOU  321  CA  GLN A  40     2516   3531   2818   -265   -246   -321       C  
ATOM    322  C   GLN A  40      37.490 -29.054  12.116  1.00 25.44           C  
ANISOU  322  C   GLN A  40     2765   3747   3153   -280   -275   -403       C  
ATOM    323  O   GLN A  40      36.630 -28.428  11.501  1.00 18.67           O  
ANISOU  323  O   GLN A  40     1916   2855   2322   -271   -349   -474       O  
ATOM    324  CB  GLN A  40      39.509 -28.527  10.738  1.00 34.83           C  
ANISOU  324  CB  GLN A  40     4012   5028   4194   -275   -324   -253       C  
ATOM    325  CG  GLN A  40      40.746 -29.031  10.015  1.00 50.56           C  
ANISOU  325  CG  GLN A  40     6023   7075   6114   -262   -298   -167       C  
ATOM    326  CD  GLN A  40      41.760 -27.934   9.734  1.00 59.10           C  
ANISOU  326  CD  GLN A  40     7140   8206   7111   -282   -358    -79       C  
ATOM    327  OE1 GLN A  40      42.964 -28.138   9.879  1.00 55.16           O  
ANISOU  327  OE1 GLN A  40     6648   7760   6550   -290   -321     16       O  
ATOM    328  NE2 GLN A  40      41.275 -26.766   9.325  1.00 65.49           N  
ANISOU  328  NE2 GLN A  40     7970   8997   7917   -291   -452   -111       N  
ATOM    329  N   LEU A  41      37.441 -29.246  13.431  1.00 23.57           N  
ANISOU  329  N   LEU A  41     2504   3507   2943   -301   -217   -393       N  
ATOM    330  CA  LEU A  41      36.349 -28.700  14.241  1.00 20.98           C  
ANISOU  330  CA  LEU A  41     2158   3135   2679   -317   -238   -466       C  
ATOM    331  C   LEU A  41      36.390 -27.164  14.297  1.00 19.58           C  
ANISOU  331  C   LEU A  41     2006   2964   2469   -340   -330   -451       C  
ATOM    332  O   LEU A  41      37.447 -26.569  14.485  1.00 19.99           O  
ANISOU  332  O   LEU A  41     2081   3062   2451   -359   -344   -359       O  
ATOM    333  CB  LEU A  41      36.379 -29.295  15.648  1.00 22.01           C  
ANISOU  333  CB  LEU A  41     2258   3265   2840   -336   -150   -451       C  
ATOM    334  CG  LEU A  41      36.328 -30.822  15.735  1.00 16.83           C  
ANISOU  334  CG  LEU A  41     1575   2601   2219   -317    -55   -465       C  
ATOM    335  CD1 LEU A  41      36.442 -31.290  17.182  1.00 21.71           C  
ANISOU  335  CD1 LEU A  41     2167   3222   2860   -340     27   -441       C  
ATOM    336  CD2 LEU A  41      35.065 -31.354  15.093  1.00 21.48           C  
ANISOU  336  CD2 LEU A  41     2145   3134   2882   -290    -64   -577       C  
ATOM    337  N   VAL A  42      35.236 -26.533  14.102  1.00 19.54           N  
ANISOU  337  N   VAL A  42     1998   2912   2514   -336   -394   -542       N  
ATOM    338  CA  VAL A  42      35.135 -25.075  14.052  1.00 20.83           C  
ANISOU  338  CA  VAL A  42     2187   3075   2654   -354   -489   -541       C  
ATOM    339  C   VAL A  42      34.472 -24.500  15.310  1.00 21.04           C  
ANISOU  339  C   VAL A  42     2194   3076   2725   -379   -490   -577       C  
ATOM    340  O   VAL A  42      34.941 -23.519  15.876  1.00 23.99           O  
ANISOU  340  O   VAL A  42     2584   3472   3060   -405   -525   -526       O  
ATOM    341  CB  VAL A  42      34.335 -24.623  12.808  1.00 23.88           C  
ANISOU  341  CB  VAL A  42     2589   3427   3058   -331   -575   -617       C  
ATOM    342  CG1 VAL A  42      34.177 -23.108  12.793  1.00 31.16           C  
ANISOU  342  CG1 VAL A  42     3537   4345   3959   -350   -675   -619       C  
ATOM    343  CG2 VAL A  42      35.024 -25.100  11.544  1.00 26.27           C  
ANISOU  343  CG2 VAL A  42     2913   3757   3311   -307   -580   -578       C  
ATOM    344  N   ARG A  43      33.359 -25.094  15.729  1.00 22.92           N  
ANISOU  344  N   ARG A  43     2396   3267   3044   -370   -453   -667       N  
ATOM    345  CA  ARG A  43      32.715 -24.661  16.959  1.00 24.76           C  
ANISOU  345  CA  ARG A  43     2608   3477   3322   -392   -445   -704       C  
ATOM    346  C   ARG A  43      31.737 -25.689  17.493  1.00 21.65           C  
ANISOU  346  C   ARG A  43     2171   3044   3012   -383   -373   -783       C  
ATOM    347  O   ARG A  43      31.151 -26.448  16.732  1.00 22.81           O  
ANISOU  347  O   ARG A  43     2306   3163   3198   -356   -362   -844       O  
ATOM    348  CB  ARG A  43      32.010 -23.318  16.766  1.00 27.32           C  
ANISOU  348  CB  ARG A  43     2947   3775   3657   -399   -548   -756       C  
ATOM    349  CG  ARG A  43      30.981 -23.300  15.662  1.00 34.69           C  
ANISOU  349  CG  ARG A  43     3881   4665   4635   -371   -606   -852       C  
ATOM    350  CD  ARG A  43      30.017 -22.147  15.890  1.00 42.48           C  
ANISOU  350  CD  ARG A  43     4868   5614   5657   -380   -687   -924       C  
ATOM    351  NE  ARG A  43      29.701 -21.445  14.653  1.00 56.71           N  
ANISOU  351  NE  ARG A  43     6699   7401   7447   -363   -784   -959       N  
ATOM    352  CZ  ARG A  43      28.484 -21.368  14.124  1.00 63.47           C  
ANISOU  352  CZ  ARG A  43     7544   8207   8366   -344   -828  -1066       C  
ATOM    353  NH1 ARG A  43      27.453 -21.950  14.728  1.00 58.93           N  
ANISOU  353  NH1 ARG A  43     6929   7593   7871   -339   -783  -1148       N  
ATOM    354  NH2 ARG A  43      28.296 -20.702  12.993  1.00 69.65           N  
ANISOU  354  NH2 ARG A  43     8356   8979   9130   -330   -918  -1090       N  
ATOM    355  N   LYS A  44      31.572 -25.709  18.812  1.00 17.42           N  
ANISOU  355  N   LYS A  44     1612   2504   2502   -405   -325   -782       N  
ATOM    356  CA  LYS A  44      30.643 -26.631  19.444  1.00 21.28           C  
ANISOU  356  CA  LYS A  44     2059   2956   3071   -400   -255   -855       C  
ATOM    357  C   LYS A  44      29.227 -26.110  19.235  1.00 21.78           C  
ANISOU  357  C   LYS A  44     2108   2964   3202   -392   -315   -971       C  
ATOM    358  O   LYS A  44      28.940 -24.967  19.552  1.00 23.47           O  
ANISOU  358  O   LYS A  44     2332   3172   3414   -407   -380   -986       O  
ATOM    359  CB  LYS A  44      30.944 -26.746  20.947  1.00 21.45           C  
ANISOU  359  CB  LYS A  44     2062   2992   3095   -429   -187   -813       C  
ATOM    360  CG  LYS A  44      30.318 -27.960  21.615  1.00 21.19           C  
ANISOU  360  CG  LYS A  44     1988   2934   3130   -425    -94   -861       C  
ATOM    361  CD  LYS A  44      30.501 -27.949  23.131  1.00 35.38           C  
ANISOU  361  CD  LYS A  44     3768   4742   4933   -454    -35   -828       C  
ATOM    362  CE  LYS A  44      31.946 -28.202  23.520  1.00 45.21           C  
ANISOU  362  CE  LYS A  44     5030   6042   6105   -468     13   -708       C  
ATOM    363  NZ  LYS A  44      32.201 -28.024  24.985  1.00 48.12           N  
ANISOU  363  NZ  LYS A  44     5387   6425   6471   -498     59   -669       N  
ATOM    364  N   LEU A  45      28.342 -26.939  18.695  1.00 18.06           N  
ANISOU  364  N   LEU A  45     1614   2454   2792   -367   -295  -1053       N  
ATOM    365  CA  LEU A  45      26.960 -26.503  18.506  1.00 21.60           C  
ANISOU  365  CA  LEU A  45     2047   2850   3311   -358   -349  -1166       C  
ATOM    366  C   LEU A  45      26.112 -26.868  19.720  1.00 23.72           C  
ANISOU  366  C   LEU A  45     2273   3091   3650   -371   -290  -1223       C  
ATOM    367  O   LEU A  45      25.174 -26.149  20.086  1.00 26.91           O  
ANISOU  367  O   LEU A  45     2664   3463   4097   -378   -334  -1294       O  
ATOM    368  CB  LEU A  45      26.374 -27.107  17.242  1.00 18.66           C  
ANISOU  368  CB  LEU A  45     1672   2448   2970   -324   -369  -1232       C  
ATOM    369  CG  LEU A  45      27.060 -26.735  15.927  1.00 21.04           C  
ANISOU  369  CG  LEU A  45     2015   2773   3208   -308   -434  -1189       C  
ATOM    370  CD1 LEU A  45      26.280 -27.303  14.759  1.00 25.65           C  
ANISOU  370  CD1 LEU A  45     2593   3319   3834   -274   -455  -1270       C  
ATOM    371  CD2 LEU A  45      27.182 -25.232  15.792  1.00 25.51           C  
ANISOU  371  CD2 LEU A  45     2612   3347   3734   -322   -533  -1174       C  
ATOM    372  N   GLY A  46      26.450 -27.981  20.357  1.00 25.86           N  
ANISOU  372  N   GLY A  46     2522   3373   3930   -376   -191  -1192       N  
ATOM    373  CA  GLY A  46      25.697 -28.415  21.512  1.00 29.67           C  
ANISOU  373  CA  GLY A  46     2964   3831   4477   -390   -128  -1240       C  
ATOM    374  C   GLY A  46      26.109 -29.772  22.036  1.00 27.87           C  
ANISOU  374  C   GLY A  46     2716   3615   4259   -391    -17  -1204       C  
ATOM    375  O   GLY A  46      26.994 -30.427  21.499  1.00 24.72           O  
ANISOU  375  O   GLY A  46     2332   3243   3816   -380     13  -1141       O  
ATOM    376  N   ARG A  47      25.423 -30.196  23.088  1.00 29.31           N  
ANISOU  376  N   ARG A  47     2862   3775   4501   -404     42  -1248       N  
ATOM    377  CA  ARG A  47      25.749 -31.420  23.783  1.00 33.06           C  
ANISOU  377  CA  ARG A  47     3314   4259   4987   -410    148  -1215       C  
ATOM    378  C   ARG A  47      24.461 -32.132  24.150  1.00 36.27           C  
ANISOU  378  C   ARG A  47     3677   4617   5486   -406    191  -1316       C  
ATOM    379  O   ARG A  47      23.528 -31.508  24.652  1.00 37.40           O  
ANISOU  379  O   ARG A  47     3802   4732   5675   -416    163  -1384       O  
ATOM    380  CB  ARG A  47      26.542 -31.090  25.050  1.00 32.66           C  
ANISOU  380  CB  ARG A  47     3268   4244   4896   -442    187  -1134       C  
ATOM    381  CG  ARG A  47      26.839 -32.287  25.915  1.00 41.28           C  
ANISOU  381  CG  ARG A  47     4337   5345   6004   -451    297  -1102       C  
ATOM    382  CD  ARG A  47      28.247 -32.213  26.464  1.00 50.96           C  
ANISOU  382  CD  ARG A  47     5586   6625   7152   -469    329   -982       C  
ATOM    383  NE  ARG A  47      28.286 -31.582  27.774  1.00 57.17           N  
ANISOU  383  NE  ARG A  47     6366   7422   7935   -499    342   -960       N  
ATOM    384  CZ  ARG A  47      29.381 -31.070  28.330  1.00 55.87           C  
ANISOU  384  CZ  ARG A  47     6225   7301   7703   -519    344   -864       C  
ATOM    385  NH1 ARG A  47      30.544 -31.094  27.688  1.00 47.52           N  
ANISOU  385  NH1 ARG A  47     5199   6283   6575   -512    332   -779       N  
ATOM    386  NH2 ARG A  47      29.307 -30.525  29.533  1.00 60.60           N  
ANISOU  386  NH2 ARG A  47     6816   7904   8304   -545    355   -854       N  
ATOM    387  N   GLY A  48      24.407 -33.430  23.879  1.00 36.61           N  
ANISOU  387  N   GLY A  48     3704   4649   5558   -391    258  -1327       N  
ATOM    388  CA  GLY A  48      23.269 -34.246  24.253  1.00 43.19           C  
ANISOU  388  CA  GLY A  48     4495   5439   6478   -388    309  -1414       C  
ATOM    389  C   GLY A  48      23.695 -35.271  25.280  1.00 43.23           C  
ANISOU  389  C   GLY A  48     4480   5458   6487   -404    417  -1368       C  
ATOM    390  O   GLY A  48      24.866 -35.337  25.638  1.00 43.65           O  
ANISOU  390  O   GLY A  48     4553   5554   6477   -415    448  -1269       O  
ATOM    391  N   LYS A  49      22.750 -36.074  25.756  1.00 47.80           N  
ANISOU  391  N   LYS A  49     5020   6000   7142   -406    473  -1438       N  
ATOM    392  CA  LYS A  49      23.079 -37.111  26.722  1.00 45.40           C  
ANISOU  392  CA  LYS A  49     4697   5706   6848   -421    577  -1399       C  
ATOM    393  C   LYS A  49      24.058 -38.100  26.109  1.00 35.92           C  
ANISOU  393  C   LYS A  49     3512   4528   5606   -404    619  -1331       C  
ATOM    394  O   LYS A  49      24.841 -38.728  26.817  1.00 41.93           O  
ANISOU  394  O   LYS A  49     4275   5316   6341   -418    692  -1260       O  
ATOM    395  CB  LYS A  49      21.813 -37.830  27.215  1.00 51.88           C  
ANISOU  395  CB  LYS A  49     5472   6480   7761   -424    626  -1493       C  
ATOM    396  CG  LYS A  49      20.568 -37.561  26.373  1.00 54.96           C  
ANISOU  396  CG  LYS A  49     5847   6824   8212   -404    563  -1604       C  
ATOM    397  CD  LYS A  49      19.284 -38.049  27.060  1.00 63.39           C  
ANISOU  397  CD  LYS A  49     6868   7849   9370   -413    606  -1697       C  
ATOM    398  CE  LYS A  49      19.201 -39.569  27.129  1.00 66.56           C  
ANISOU  398  CE  LYS A  49     7247   8235   9810   -407    696  -1702       C  
ATOM    399  NZ  LYS A  49      17.842 -40.044  27.535  1.00 67.59           N  
ANISOU  399  NZ  LYS A  49     7330   8317  10032   -411    727  -1804       N  
ATOM    400  N   TYR A  50      24.038 -38.206  24.784  1.00 34.83           N  
ANISOU  400  N   TYR A  50     3390   4382   5461   -375    572  -1352       N  
ATOM    401  CA  TYR A  50      24.788 -39.255  24.100  1.00 35.43           C  
ANISOU  401  CA  TYR A  50     3478   4473   5510   -355    613  -1304       C  
ATOM    402  C   TYR A  50      25.979 -38.786  23.272  1.00 28.57           C  
ANISOU  402  C   TYR A  50     2652   3648   4554   -343    566  -1221       C  
ATOM    403  O   TYR A  50      26.767 -39.608  22.816  1.00 28.32           O  
ANISOU  403  O   TYR A  50     2633   3638   4490   -329    604  -1168       O  
ATOM    404  CB  TYR A  50      23.855 -40.049  23.191  1.00 43.16           C  
ANISOU  404  CB  TYR A  50     4438   5407   6552   -327    611  -1393       C  
ATOM    405  CG  TYR A  50      22.747 -40.756  23.925  1.00 54.97           C  
ANISOU  405  CG  TYR A  50     5890   6861   8134   -336    668  -1470       C  
ATOM    406  CD1 TYR A  50      23.027 -41.750  24.852  1.00 56.71           C  
ANISOU  406  CD1 TYR A  50     6093   7087   8367   -351    765  -1436       C  
ATOM    407  CD2 TYR A  50      21.416 -40.437  23.682  1.00 61.84           C  
ANISOU  407  CD2 TYR A  50     6737   7684   9074   -330    626  -1579       C  
ATOM    408  CE1 TYR A  50      22.012 -42.403  25.522  1.00 64.71           C  
ANISOU  408  CE1 TYR A  50     7066   8062   9459   -361    818  -1506       C  
ATOM    409  CE2 TYR A  50      20.395 -41.085  24.347  1.00 66.52           C  
ANISOU  409  CE2 TYR A  50     7289   8240   9747   -339    679  -1650       C  
ATOM    410  CZ  TYR A  50      20.698 -42.068  25.265  1.00 69.94           C  
ANISOU  410  CZ  TYR A  50     7704   8680  10190   -355    775  -1613       C  
ATOM    411  OH  TYR A  50      19.681 -42.716  25.929  1.00 76.85           O  
ANISOU  411  OH  TYR A  50     8539   9518  11144   -365    829  -1682       O  
ATOM    412  N   SER A  51      26.097 -37.481  23.062  1.00 26.64           N  
ANISOU  412  N   SER A  51     2430   3417   4273   -349    484  -1212       N  
ATOM    413  CA  SER A  51      27.116 -36.963  22.159  1.00 21.41           C  
ANISOU  413  CA  SER A  51     1809   2793   3533   -338    430  -1142       C  
ATOM    414  C   SER A  51      27.318 -35.465  22.302  1.00 20.30           C  
ANISOU  414  C   SER A  51     1692   2671   3351   -354    351  -1120       C  
ATOM    415  O   SER A  51      26.550 -34.772  22.982  1.00 24.16           O  
ANISOU  415  O   SER A  51     2165   3138   3875   -371    328  -1170       O  
ATOM    416  CB  SER A  51      26.716 -37.240  20.715  1.00 32.43           C  
ANISOU  416  CB  SER A  51     3213   4167   4944   -303    385  -1195       C  
ATOM    417  OG  SER A  51      25.740 -36.300  20.289  1.00 34.14           O  
ANISOU  417  OG  SER A  51     3429   4351   5193   -299    301  -1276       O  
ATOM    418  N   GLU A  52      28.372 -34.982  21.655  1.00 16.13           N  
ANISOU  418  N   GLU A  52     1581   2569   1979    -40   -314   -497       N  
ATOM    419  CA  GLU A  52      28.588 -33.560  21.444  1.00 23.57           C  
ANISOU  419  CA  GLU A  52     2481   3477   2996    -23   -320   -459       C  
ATOM    420  C   GLU A  52      28.637 -33.333  19.949  1.00 20.74           C  
ANISOU  420  C   GLU A  52     2140   3135   2604    -51   -336   -394       C  
ATOM    421  O   GLU A  52      29.212 -34.133  19.223  1.00 18.50           O  
ANISOU  421  O   GLU A  52     1906   2875   2249    -74   -325   -391       O  
ATOM    422  CB  GLU A  52      29.909 -33.105  22.062  1.00 28.68           C  
ANISOU  422  CB  GLU A  52     3125   4090   3683      3   -285   -494       C  
ATOM    423  CG  GLU A  52      29.905 -33.045  23.568  1.00 38.23           C  
ANISOU  423  CG  GLU A  52     4307   5276   4942     36   -270   -555       C  
ATOM    424  CD  GLU A  52      31.054 -32.226  24.100  1.00 38.03           C  
ANISOU  424  CD  GLU A  52     4263   5210   4976     65   -242   -576       C  
ATOM    425  OE1 GLU A  52      32.138 -32.267  23.489  1.00 34.57           O  
ANISOU  425  OE1 GLU A  52     3854   4769   4512     56   -223   -568       O  
ATOM    426  OE2 GLU A  52      30.868 -31.529  25.113  1.00 41.69           O  
ANISOU  426  OE2 GLU A  52     4683   5645   5513     95   -241   -600       O  
ATOM    427  N   VAL A  53      28.049 -32.235  19.495  1.00 13.76           N  
ANISOU  427  N   VAL A  53     1217   2239   1773    -47   -362   -341       N  
ATOM    428  CA  VAL A  53      27.943 -31.958  18.074  1.00 13.64           C  
ANISOU  428  CA  VAL A  53     1213   2240   1730    -73   -381   -274       C  
ATOM    429  C   VAL A  53      28.707 -30.679  17.736  1.00 16.95           C  
ANISOU  429  C   VAL A  53     1607   2624   2210    -58   -373   -241       C  
ATOM    430  O   VAL A  53      28.517 -29.641  18.380  1.00 22.10           O  
ANISOU  430  O   VAL A  53     2210   3243   2944    -31   -377   -241       O  
ATOM    431  CB  VAL A  53      26.460 -31.816  17.660  1.00 18.78           C  
ANISOU  431  CB  VAL A  53     1842   2912   2382    -87   -421   -232       C  
ATOM    432  CG1 VAL A  53      26.342 -31.425  16.200  1.00 21.71           C  
ANISOU  432  CG1 VAL A  53     2220   3297   2730   -111   -442   -161       C  
ATOM    433  CG2 VAL A  53      25.710 -33.115  17.919  1.00 17.35           C  
ANISOU  433  CG2 VAL A  53     1688   2768   2138   -104   -429   -263       C  
ATOM    434  N   PHE A  54      29.553 -30.761  16.711  1.00 15.01           N  
ANISOU  434  N   PHE A  54     1395   2387   1923    -75   -363   -212       N  
ATOM    435  CA  PHE A  54      30.391 -29.648  16.297  1.00 17.97           C  
ANISOU  435  CA  PHE A  54     1751   2729   2346    -64   -354   -180       C  
ATOM    436  C   PHE A  54      30.131 -29.255  14.846  1.00 24.44           C  
ANISOU  436  C   PHE A  54     2576   3566   3145    -88   -377   -106       C  
ATOM    437  O   PHE A  54      29.832 -30.102  14.000  1.00 25.40           O  
ANISOU  437  O   PHE A  54     2735   3726   3189   -118   -388    -87       O  
ATOM    438  CB  PHE A  54      31.869 -30.031  16.448  1.00 18.44           C  
ANISOU  438  CB  PHE A  54     1845   2779   2382    -59   -315   -217       C  
ATOM    439  CG  PHE A  54      32.284 -30.353  17.857  1.00 19.95           C  
ANISOU  439  CG  PHE A  54     2031   2951   2597    -34   -289   -290       C  
ATOM    440  CD1 PHE A  54      32.931 -29.402  18.634  1.00 18.78           C  
ANISOU  440  CD1 PHE A  54     1848   2760   2528     -2   -271   -310       C  
ATOM    441  CD2 PHE A  54      32.055 -31.607  18.399  1.00 18.57           C  
ANISOU  441  CD2 PHE A  54     1887   2802   2366    -41   -281   -339       C  
ATOM    442  CE1 PHE A  54      33.339 -29.687  19.936  1.00 24.13           C  
ANISOU  442  CE1 PHE A  54     2521   3420   3227     23   -246   -378       C  
ATOM    443  CE2 PHE A  54      32.464 -31.908  19.707  1.00 17.56           C  
ANISOU  443  CE2 PHE A  54     1756   2657   2260    -16   -256   -406       C  
ATOM    444  CZ  PHE A  54      33.104 -30.942  20.475  1.00 23.65           C  
ANISOU  444  CZ  PHE A  54     2491   3386   3110     16   -239   -426       C  
ATOM    445  N   GLU A  55      30.227 -27.968  14.548  1.00 22.30           N  
ANISOU  445  N   GLU A  55     2266   3266   2939    -76   -385    -63       N  
ATOM    446  CA  GLU A  55      30.323 -27.556  13.158  1.00 20.33           C  
ANISOU  446  CA  GLU A  55     2027   3028   2669    -96   -398      4       C  
ATOM    447  C   GLU A  55      31.766 -27.797  12.768  1.00 22.63           C  
ANISOU  447  C   GLU A  55     2355   3314   2927   -101   -366     -5       C  
ATOM    448  O   GLU A  55      32.651 -27.626  13.588  1.00 19.13           O  
ANISOU  448  O   GLU A  55     1907   2843   2518    -79   -338    -48       O  
ATOM    449  CB  GLU A  55      29.979 -26.083  13.007  1.00 20.72           C  
ANISOU  449  CB  GLU A  55     2023   3046   2803    -80   -416     52       C  
ATOM    450  CG  GLU A  55      30.209 -25.530  11.613  1.00 27.79           C  
ANISOU  450  CG  GLU A  55     2925   3949   3686    -98   -427    122       C  
ATOM    451  CD  GLU A  55      29.842 -24.061  11.504  1.00 33.49           C  
ANISOU  451  CD  GLU A  55     3592   4638   4493    -80   -444    169       C  
ATOM    452  OE1 GLU A  55      28.641 -23.745  11.593  1.00 46.55           O  
ANISOU  452  OE1 GLU A  55     5216   6299   6174    -79   -474    189       O  
ATOM    453  OE2 GLU A  55      30.749 -23.229  11.322  1.00 43.53           O  
ANISOU  453  OE2 GLU A  55     4853   5880   5807    -68   -428    185       O  
ATOM    454  N   ALA A  56      32.013 -28.205  11.531  1.00 21.27           N  
ANISOU  454  N   ALA A  56     2221   3171   2690   -129   -370     34       N  
ATOM    455  CA  ALA A  56      33.384 -28.450  11.106  1.00 19.79           C  
ANISOU  455  CA  ALA A  56     2070   2981   2469   -134   -340     27       C  
ATOM    456  C   ALA A  56      33.534 -28.207   9.623  1.00 17.35           C  
ANISOU  456  C   ALA A  56     1778   2690   2125   -158   -352     94       C  
ATOM    457  O   ALA A  56      32.558 -27.981   8.923  1.00 19.31           O  
ANISOU  457  O   ALA A  56     2014   2956   2367   -172   -384    143       O  
ATOM    458  CB  ALA A  56      33.823 -29.867  11.462  1.00 17.19           C  
ANISOU  458  CB  ALA A  56     1792   2677   2065   -145   -319    -30       C  
ATOM    459  N   ILE A  57      34.773 -28.241   9.154  1.00 14.84           N  
ANISOU  459  N   ILE A  57     1488   2366   1784   -162   -327     97       N  
ATOM    460  CA  ILE A  57      35.046 -28.091   7.739  1.00 18.59           C  
ANISOU  460  CA  ILE A  57     1984   2860   2220   -184   -335    157       C  
ATOM    461  C   ILE A  57      35.735 -29.359   7.265  1.00 21.03           C  
ANISOU  461  C   ILE A  57     2354   3201   2434   -207   -317    136       C  
ATOM    462  O   ILE A  57      36.643 -29.877   7.920  1.00 20.95           O  
ANISOU  462  O   ILE A  57     2367   3183   2411   -198   -286     82       O  
ATOM    463  CB  ILE A  57      35.917 -26.844   7.456  1.00 25.09           C  
ANISOU  463  CB  ILE A  57     2781   3645   3105   -169   -322    190       C  
ATOM    464  CG1 ILE A  57      36.276 -26.768   5.974  1.00 30.10           C  
ANISOU  464  CG1 ILE A  57     3441   4301   3693   -193   -328    251       C  
ATOM    465  CG2 ILE A  57      37.184 -26.883   8.282  1.00 33.95           C  
ANISOU  465  CG2 ILE A  57     3912   4740   4248   -149   -283    136       C  
ATOM    466  CD1 ILE A  57      37.222 -25.638   5.630  1.00 39.51           C  
ANISOU  466  CD1 ILE A  57     4614   5459   4939   -180   -313    283       C  
ATOM    467  N   ASN A  58      35.261 -29.891   6.152  1.00 18.95           N  
ANISOU  467  N   ASN A  58     2119   2978   2104   -237   -337    176       N  
ATOM    468  CA  ASN A  58      35.931 -30.997   5.501  1.00 19.65           C  
ANISOU  468  CA  ASN A  58     2266   3099   2102   -260   -322    165       C  
ATOM    469  C   ASN A  58      37.007 -30.377   4.627  1.00 20.12           C  
ANISOU  469  C   ASN A  58     2334   3147   2163   -262   -308    204       C  
ATOM    470  O   ASN A  58      36.698 -29.790   3.598  1.00 24.45           O  
ANISOU  470  O   ASN A  58     2873   3704   2714   -274   -328    268       O  
ATOM    471  CB  ASN A  58      34.920 -31.765   4.643  1.00 20.67           C  
ANISOU  471  CB  ASN A  58     2418   3274   2160   -291   -352    195       C  
ATOM    472  CG  ASN A  58      35.549 -32.901   3.851  1.00 26.18           C  
ANISOU  472  CG  ASN A  58     3177   4008   2761   -317   -340    190       C  
ATOM    473  OD1 ASN A  58      36.765 -32.968   3.688  1.00 20.69           O  
ANISOU  473  OD1 ASN A  58     2506   3304   2050   -315   -312    179       O  
ATOM    474  ND2 ASN A  58      34.705 -33.791   3.333  1.00 25.62           N  
ANISOU  474  ND2 ASN A  58     3131   3980   2624   -343   -362    199       N  
ATOM    475  N   ILE A  59      38.267 -30.492   5.030  1.00 23.02           N  
ANISOU  475  N   ILE A  59     2718   3495   2532   -251   -272    168       N  
ATOM    476  CA  ILE A  59      39.337 -29.794   4.321  1.00 18.90           C  
ANISOU  476  CA  ILE A  59     2199   2957   2023   -249   -256    202       C  
ATOM    477  C   ILE A  59      39.719 -30.421   2.976  1.00 25.46           C  
ANISOU  477  C   ILE A  59     3078   3825   2769   -279   -258    238       C  
ATOM    478  O   ILE A  59      40.600 -29.913   2.289  1.00 28.14           O  
ANISOU  478  O   ILE A  59     3423   4155   3112   -280   -245    270       O  
ATOM    479  CB  ILE A  59      40.601 -29.638   5.194  1.00 19.71           C  
ANISOU  479  CB  ILE A  59     2304   3026   2160   -226   -218    152       C  
ATOM    480  CG1 ILE A  59      41.247 -30.989   5.474  1.00 23.83           C  
ANISOU  480  CG1 ILE A  59     2877   3569   2606   -235   -193     96       C  
ATOM    481  CG2 ILE A  59      40.274 -28.943   6.495  1.00 24.78           C  
ANISOU  481  CG2 ILE A  59     2896   3629   2889   -195   -216    118       C  
ATOM    482  CD1 ILE A  59      42.601 -30.869   6.181  1.00 27.74           C  
ANISOU  482  CD1 ILE A  59     3379   4035   3127   -215   -154     50       C  
ATOM    483  N   THR A  60      39.070 -31.520   2.602  1.00 23.15           N  
ANISOU  483  N   THR A  60     2820   3576   2402   -303   -272    233       N  
ATOM    484  CA  THR A  60      39.301 -32.108   1.281  1.00 28.27           C  
ANISOU  484  CA  THR A  60     3511   4262   2968   -333   -278    270       C  
ATOM    485  C   THR A  60      38.400 -31.484   0.206  1.00 33.71           C  
ANISOU  485  C   THR A  60     4180   4966   3661   -347   -313    345       C  
ATOM    486  O   THR A  60      38.637 -31.673  -0.991  1.00 35.69           O  
ANISOU  486  O   THR A  60     4458   5244   3858   -368   -318    387       O  
ATOM    487  CB  THR A  60      39.124 -33.643   1.272  1.00 28.82           C  
ANISOU  487  CB  THR A  60     3632   4373   2947   -354   -276    231       C  
ATOM    488  OG1 THR A  60      37.726 -33.972   1.282  1.00 33.21           O  
ANISOU  488  OG1 THR A  60     4177   4951   3490   -365   -308    240       O  
ATOM    489  CG2 THR A  60      39.824 -34.272   2.470  1.00 34.17           C  
ANISOU  489  CG2 THR A  60     4324   5033   3624   -338   -244    155       C  
ATOM    490  N   ASN A  61      37.372 -30.750   0.632  1.00 32.24           N  
ANISOU  490  N   ASN A  61     3946   4765   3538   -335   -337    360       N  
ATOM    491  CA  ASN A  61      36.517 -30.011  -0.301  1.00 23.44           C  
ANISOU  491  CA  ASN A  61     2807   3660   2439   -344   -370    431       C  
ATOM    492  C   ASN A  61      36.170 -28.609   0.202  1.00 26.12           C  
ANISOU  492  C   ASN A  61     3085   3958   2881   -318   -379    452       C  
ATOM    493  O   ASN A  61      35.462 -27.857  -0.460  1.00 32.10           O  
ANISOU  493  O   ASN A  61     3815   4717   3664   -322   -406    510       O  
ATOM    494  CB  ASN A  61      35.249 -30.802  -0.648  1.00 24.84           C  
ANISOU  494  CB  ASN A  61     2997   3880   2563   -367   -402    440       C  
ATOM    495  CG  ASN A  61      34.439 -31.177   0.578  1.00 24.36           C  
ANISOU  495  CG  ASN A  61     2918   3812   2525   -355   -408    388       C  
ATOM    496  OD1 ASN A  61      34.612 -30.603   1.655  1.00 21.81           O  
ANISOU  496  OD1 ASN A  61     2562   3452   2273   -328   -395    356       O  
ATOM    497  ND2 ASN A  61      33.533 -32.135   0.417  1.00 28.38           N  
ANISOU  497  ND2 ASN A  61     3447   4359   2976   -376   -428    380       N  
ATOM    498  N   ASN A  62      36.702 -28.257   1.367  1.00 28.34           N  
ANISOU  498  N   ASN A  62     3345   4200   3222   -292   -356    405       N  
ATOM    499  CA  ASN A  62      36.363 -27.004   2.041  1.00 21.69           C  
ANISOU  499  CA  ASN A  62     2444   3316   2479   -265   -363    414       C  
ATOM    500  C   ASN A  62      34.861 -26.833   2.269  1.00 26.87           C  
ANISOU  500  C   ASN A  62     3068   3981   3160   -265   -398    428       C  
ATOM    501  O   ASN A  62      34.375 -25.710   2.369  1.00 36.30           O  
ANISOU  501  O   ASN A  62     4214   5150   4427   -250   -414    461       O  
ATOM    502  CB  ASN A  62      36.946 -25.785   1.305  1.00 24.88           C  
ANISOU  502  CB  ASN A  62     2826   3696   2930   -258   -361    471       C  
ATOM    503  CG  ASN A  62      38.452 -25.672   1.464  1.00 36.50           C  
ANISOU  503  CG  ASN A  62     4315   5144   4409   -248   -323    448       C  
ATOM    504  OD1 ASN A  62      39.053 -26.363   2.291  1.00 36.83           O  
ANISOU  504  OD1 ASN A  62     4377   5181   4434   -240   -297    385       O  
ATOM    505  ND2 ASN A  62      39.071 -24.797   0.676  1.00 36.86           N  
ANISOU  505  ND2 ASN A  62     4352   5176   4479   -247   -318    498       N  
ATOM    506  N   GLU A  63      34.137 -27.947   2.364  1.00 20.47           N  
ANISOU  506  N   GLU A  63     2283   3206   2288   -282   -411    404       N  
ATOM    507  CA  GLU A  63      32.700 -27.902   2.646  1.00 27.40           C  
ANISOU  507  CA  GLU A  63     3132   4094   3184   -282   -443    412       C  
ATOM    508  C   GLU A  63      32.417 -27.958   4.145  1.00 26.20           C  
ANISOU  508  C   GLU A  63     2955   3918   3081   -258   -435    350       C  
ATOM    509  O   GLU A  63      33.075 -28.670   4.900  1.00 25.93           O  
ANISOU  509  O   GLU A  63     2945   3880   3027   -252   -408    290       O  
ATOM    510  CB  GLU A  63      31.973 -29.062   1.966  1.00 28.11           C  
ANISOU  510  CB  GLU A  63     3261   4236   3184   -313   -463    419       C  
ATOM    511  CG  GLU A  63      32.280 -29.215   0.497  1.00 42.84           C  
ANISOU  511  CG  GLU A  63     5158   6131   4989   -339   -470    473       C  
ATOM    512  CD  GLU A  63      31.424 -28.342  -0.383  1.00 58.90           C  
ANISOU  512  CD  GLU A  63     7160   8171   7047   -345   -503    545       C  
ATOM    513  OE1 GLU A  63      30.940 -27.294   0.099  1.00 64.41           O  
ANISOU  513  OE1 GLU A  63     7808   8839   7827   -325   -514    559       O  
ATOM    514  OE2 GLU A  63      31.233 -28.715  -1.561  1.00 60.51           O  
ANISOU  514  OE2 GLU A  63     7391   8411   7189   -371   -518    587       O  
ATOM    515  N   LYS A  64      31.414 -27.208   4.570  1.00 26.31           N  
ANISOU  515  N   LYS A  64     2921   3917   3158   -245   -459    365       N  
ATOM    516  CA  LYS A  64      30.963 -27.268   5.942  1.00 26.31           C  
ANISOU  516  CA  LYS A  64     2895   3898   3202   -223   -456    311       C  
ATOM    517  C   LYS A  64      30.304 -28.625   6.204  1.00 22.12           C  
ANISOU  517  C   LYS A  64     2397   3405   2602   -241   -463    273       C  
ATOM    518  O   LYS A  64      29.598 -29.153   5.355  1.00 20.96           O  
ANISOU  518  O   LYS A  64     2270   3297   2399   -266   -486    304       O  
ATOM    519  CB  LYS A  64      29.981 -26.130   6.190  1.00 37.02           C  
ANISOU  519  CB  LYS A  64     4194   5233   4639   -207   -482    343       C  
ATOM    520  CG  LYS A  64      29.812 -25.747   7.630  1.00 47.84           C  
ANISOU  520  CG  LYS A  64     5527   6570   6082   -176   -474    293       C  
ATOM    521  CD  LYS A  64      29.031 -24.452   7.729  1.00 54.69           C  
ANISOU  521  CD  LYS A  64     6336   7411   7033   -159   -498    333       C  
ATOM    522  CE  LYS A  64      29.715 -23.340   6.953  1.00 52.07           C  
ANISOU  522  CE  LYS A  64     5988   7055   6739   -154   -494    386       C  
ATOM    523  NZ  LYS A  64      28.918 -22.082   7.015  1.00 50.83           N  
ANISOU  523  NZ  LYS A  64     5775   6874   6663   -138   -519    427       N  
ATOM    524  N   VAL A  65      30.565 -29.195   7.373  1.00 18.69           N  
ANISOU  524  N   VAL A  65     1969   2961   2173   -226   -442    205       N  
ATOM    525  CA  VAL A  65      29.913 -30.418   7.802  1.00 21.64           C  
ANISOU  525  CA  VAL A  65     2366   3364   2490   -239   -448    164       C  
ATOM    526  C   VAL A  65      29.625 -30.341   9.292  1.00 17.68           C  
ANISOU  526  C   VAL A  65     1836   2838   2045   -212   -440    107       C  
ATOM    527  O   VAL A  65      29.958 -29.361   9.950  1.00 18.67           O  
ANISOU  527  O   VAL A  65     1923   2923   2248   -184   -430    100       O  
ATOM    528  CB  VAL A  65      30.784 -31.672   7.542  1.00 13.04           C  
ANISOU  528  CB  VAL A  65     1339   2301   1316   -257   -423    131       C  
ATOM    529  CG1 VAL A  65      31.057 -31.825   6.059  1.00 21.10           C  
ANISOU  529  CG1 VAL A  65     2391   3349   2276   -285   -431    185       C  
ATOM    530  CG2 VAL A  65      32.090 -31.603   8.344  1.00 15.99           C  
ANISOU  530  CG2 VAL A  65     1719   2643   1714   -235   -384     81       C  
ATOM    531  N   VAL A  66      29.005 -31.385   9.820  1.00 16.59           N  
ANISOU  531  N   VAL A  66     1715   2724   1866   -220   -444     67       N  
ATOM    532  CA AVAL A  66      28.745 -31.475  11.250  1.00 14.78           C  
ANISOU  532  CA AVAL A  66     1462   2475   1679   -196   -435      9       C  
ATOM    533  CA BVAL A  66      28.758 -31.463  11.250  0.00 18.02           C  
ANISOU  533  CA BVAL A  66     1872   2884   2089   -195   -435      9       C  
ATOM    534  C   VAL A  66      29.320 -32.773  11.792  1.00 20.05           C  
ANISOU  534  C   VAL A  66     2175   3158   2286   -201   -409    -54       C  
ATOM    535  O   VAL A  66      29.225 -33.822  11.148  1.00 20.95           O  
ANISOU  535  O   VAL A  66     2333   3308   2317   -229   -413    -52       O  
ATOM    536  CB AVAL A  66      27.225 -31.384  11.528  1.00 20.20           C  
ANISOU  536  CB AVAL A  66     2116   3173   2386   -197   -470     21       C  
ATOM    537  CB BVAL A  66      27.258 -31.332  11.580  0.00 20.85           C  
ANISOU  537  CB BVAL A  66     2197   3253   2474   -195   -469     19       C  
ATOM    538  CG1AVAL A  66      26.895 -31.928  12.903  1.00 25.84           C  
ANISOU  538  CG1AVAL A  66     2823   3881   3116   -180   -460    -45       C  
ATOM    539  CG1BVAL A  66      26.533 -32.634  11.299  0.00 20.48           C  
ANISOU  539  CG1BVAL A  66     2186   3251   2344   -222   -482      8       C  
ATOM    540  CG2AVAL A  66      26.771 -29.942  11.392  1.00 22.92           C  
ANISOU  540  CG2AVAL A  66     2406   3490   2812   -180   -489     69       C  
ATOM    541  CG2BVAL A  66      27.069 -30.918  13.024  0.00 23.51           C  
ANISOU  541  CG2BVAL A  66     2493   3557   2882   -162   -460    -28       C  
ATOM    542  N   VAL A  67      29.937 -32.703  12.969  1.00 16.83           N  
ANISOU  542  N   VAL A  67     1757   2720   1917   -174   -382   -109       N  
ATOM    543  CA  VAL A  67      30.561 -33.870  13.556  1.00 14.61           C  
ANISOU  543  CA  VAL A  67     1517   2450   1584   -176   -355   -171       C  
ATOM    544  C   VAL A  67      29.936 -34.202  14.892  1.00 14.30           C  
ANISOU  544  C   VAL A  67     1457   2404   1571   -158   -354   -225       C  
ATOM    545  O   VAL A  67      29.940 -33.386  15.812  1.00 15.49           O  
ANISOU  545  O   VAL A  67     1566   2521   1800   -129   -348   -243       O  
ATOM    546  CB  VAL A  67      32.074 -33.641  13.773  1.00 15.21           C  
ANISOU  546  CB  VAL A  67     1606   2499   1673   -161   -317   -195       C  
ATOM    547  CG1 VAL A  67      32.709 -34.844  14.458  1.00 21.55           C  
ANISOU  547  CG1 VAL A  67     2451   3313   2426   -161   -288   -262       C  
ATOM    548  CG2 VAL A  67      32.750 -33.332  12.450  1.00 16.51           C  
ANISOU  548  CG2 VAL A  67     1792   2671   1810   -179   -317   -142       C  
ATOM    549  N   LYS A  68      29.420 -35.421  15.000  1.00 12.79           N  
ANISOU  549  N   LYS A  68     1297   2246   1315   -176   -358   -252       N  
ATOM    550  CA  LYS A  68      28.808 -35.906  16.223  1.00 12.64           C  
ANISOU  550  CA  LYS A  68     1266   2226   1311   -162   -357   -304       C  
ATOM    551  C   LYS A  68      29.741 -36.897  16.913  1.00 15.60           C  
ANISOU  551  C   LYS A  68     1679   2602   1646   -157   -321   -369       C  
ATOM    552  O   LYS A  68      29.842 -38.066  16.509  1.00 15.67           O  
ANISOU  552  O   LYS A  68     1737   2644   1575   -181   -316   -382       O  
ATOM    553  CB  LYS A  68      27.469 -36.574  15.880  1.00 12.17           C  
ANISOU  553  CB  LYS A  68     1212   2203   1208   -186   -389   -288       C  
ATOM    554  CG  LYS A  68      26.699 -37.135  17.048  1.00 11.49           C  
ANISOU  554  CG  LYS A  68     1114   2121   1131   -175   -391   -337       C  
ATOM    555  CD  LYS A  68      25.333 -37.603  16.526  1.00 15.60           C  
ANISOU  555  CD  LYS A  68     1635   2677   1615   -200   -426   -308       C  
ATOM    556  CE  LYS A  68      24.525 -38.341  17.552  1.00 20.22           C  
ANISOU  556  CE  LYS A  68     2216   3273   2196   -194   -430   -355       C  
ATOM    557  NZ  LYS A  68      23.236 -38.802  16.909  1.00 15.69           N  
ANISOU  557  NZ  LYS A  68     1645   2735   1582   -222   -465   -323       N  
ATOM    558  N   ILE A  69      30.439 -36.419  17.942  1.00 14.89           N  
ANISOU  558  N   ILE A  69     1567   2476   1612   -126   -296   -410       N  
ATOM    559  CA  ILE A  69      31.349 -37.253  18.713  1.00 15.90           C  
ANISOU  559  CA  ILE A  69     1727   2602   1712   -117   -261   -474       C  
ATOM    560  C   ILE A  69      30.558 -37.973  19.790  1.00 21.50           C  
ANISOU  560  C   ILE A  69     2432   3321   2418   -109   -264   -522       C  
ATOM    561  O   ILE A  69      30.034 -37.349  20.720  1.00 21.01           O  
ANISOU  561  O   ILE A  69     2324   3236   2423    -84   -270   -538       O  
ATOM    562  CB  ILE A  69      32.492 -36.413  19.323  1.00 16.71           C  
ANISOU  562  CB  ILE A  69     1810   2663   1877    -86   -232   -495       C  
ATOM    563  CG1 ILE A  69      33.206 -35.654  18.198  1.00 19.76           C  
ANISOU  563  CG1 ILE A  69     2200   3040   2268    -95   -232   -442       C  
ATOM    564  CG2 ILE A  69      33.432 -37.300  20.123  1.00 20.64           C  
ANISOU  564  CG2 ILE A  69     2341   3159   2343    -76   -196   -562       C  
ATOM    565  CD1 ILE A  69      34.332 -34.779  18.649  1.00 24.56           C  
ANISOU  565  CD1 ILE A  69     2788   3608   2936    -68   -206   -456       C  
ATOM    566  N   LEU A  70      30.444 -39.289  19.641  1.00 20.37           N  
ANISOU  566  N   LEU A  70     2333   3211   2195   -131   -260   -545       N  
ATOM    567  CA  LEU A  70      29.596 -40.076  20.519  1.00 23.96           C  
ANISOU  567  CA  LEU A  70     2787   3680   2637   -129   -265   -586       C  
ATOM    568  C   LEU A  70      30.206 -40.202  21.906  1.00 30.96           C  
ANISOU  568  C   LEU A  70     3665   4542   3555    -98   -234   -653       C  
ATOM    569  O   LEU A  70      31.381 -40.549  22.052  1.00 33.58           O  
ANISOU  569  O   LEU A  70     4027   4867   3866    -93   -203   -684       O  
ATOM    570  CB  LEU A  70      29.350 -41.464  19.925  1.00 25.15           C  
ANISOU  570  CB  LEU A  70     2991   3874   2692   -162   -269   -591       C  
ATOM    571  CG  LEU A  70      28.742 -41.467  18.522  1.00 22.89           C  
ANISOU  571  CG  LEU A  70     2716   3615   2364   -195   -299   -527       C  
ATOM    572  CD1 LEU A  70      28.592 -42.887  17.996  1.00 31.22           C  
ANISOU  572  CD1 LEU A  70     3826   4711   3323   -227   -300   -538       C  
ATOM    573  CD2 LEU A  70      27.395 -40.752  18.544  1.00 29.44           C  
ANISOU  573  CD2 LEU A  70     3499   4445   3243   -193   -335   -492       C  
ATOM    574  N   LYS A  71      29.411 -39.913  22.930  1.00 37.86           N  
ANISOU  574  N   LYS A  71     4499   5404   4482    -77   -244   -675       N  
ATOM    575  CA  LYS A  71      29.855 -40.160  24.294  1.00 38.35           C  
ANISOU  575  CA  LYS A  71     4555   5448   4569    -48   -216   -742       C  
ATOM    576  C   LYS A  71      29.957 -41.665  24.456  1.00 43.80           C  
ANISOU  576  C   LYS A  71     5296   6168   5178    -65   -202   -783       C  
ATOM    577  O   LYS A  71      29.251 -42.411  23.770  1.00 43.64           O  
ANISOU  577  O   LYS A  71     5301   6181   5099    -95   -221   -762       O  
ATOM    578  CB  LYS A  71      28.876 -39.583  25.320  1.00 35.82           C  
ANISOU  578  CB  LYS A  71     4181   5111   4318    -24   -232   -755       C  
ATOM    579  CG  LYS A  71      28.901 -38.067  25.439  1.00 37.30           C  
ANISOU  579  CG  LYS A  71     4315   5262   4596      0   -240   -727       C  
ATOM    580  CD  LYS A  71      28.454 -37.637  26.827  1.00 44.12           C  
ANISOU  580  CD  LYS A  71     5132   6102   5528     34   -238   -767       C  
ATOM    581  CE  LYS A  71      28.532 -36.129  27.001  1.00 47.17           C  
ANISOU  581  CE  LYS A  71     5466   6451   6007     60   -245   -742       C  
ATOM    582  NZ  LYS A  71      27.389 -35.452  26.344  1.00 49.58           N  
ANISOU  582  NZ  LYS A  71     5740   6763   6337     48   -283   -684       N  
ATOM    583  N   PRO A  72      30.854 -42.122  25.342  1.00 59.77           N  
ANISOU  583  N   PRO A  72     7350   8035   7326    133   -514     86       N  
ATOM    584  CA  PRO A  72      31.000 -43.556  25.608  1.00 66.40           C  
ANISOU  584  CA  PRO A  72     8186   8830   8212    140   -541    130       C  
ATOM    585  C   PRO A  72      29.719 -44.126  26.201  1.00 74.42           C  
ANISOU  585  C   PRO A  72     9234   9848   9195    119   -528    172       C  
ATOM    586  O   PRO A  72      29.688 -45.283  26.621  1.00 77.36           O  
ANISOU  586  O   PRO A  72     9611  10188   9593    120   -551    217       O  
ATOM    587  CB  PRO A  72      32.137 -43.608  26.634  1.00 63.60           C  
ANISOU  587  CB  PRO A  72     7829   8481   7855    151   -594    160       C  
ATOM    588  CG  PRO A  72      32.902 -42.343  26.418  1.00 62.79           C  
ANISOU  588  CG  PRO A  72     7713   8412   7734    157   -592    115       C  
ATOM    589  CD  PRO A  72      31.867 -41.322  26.051  1.00 60.90           C  
ANISOU  589  CD  PRO A  72     7490   8208   7443    139   -544     83       C  
ATOM    590  N   VAL A  73      28.672 -43.308  26.235  1.00 80.09           N  
ANISOU  590  N   VAL A  73     9972  10603   9857     99   -492    158       N  
ATOM    591  CA  VAL A  73      27.368 -43.753  26.698  1.00 85.73           C  
ANISOU  591  CA  VAL A  73    10714  11321  10538     77   -473    190       C  
ATOM    592  C   VAL A  73      26.847 -44.868  25.792  1.00 85.27           C  
ANISOU  592  C   VAL A  73    10646  11216  10537     80   -454    190       C  
ATOM    593  O   VAL A  73      26.482 -44.634  24.636  1.00 81.60           O  
ANISOU  593  O   VAL A  73    10167  10743  10094     82   -419    147       O  
ATOM    594  CB  VAL A  73      26.351 -42.588  26.752  1.00 87.64           C  
ANISOU  594  CB  VAL A  73    10974  11609  10716     58   -433    165       C  
ATOM    595  CG1 VAL A  73      25.018 -43.066  27.310  1.00 88.21           C  
ANISOU  595  CG1 VAL A  73    11074  11687  10754     33   -414    198       C  
ATOM    596  CG2 VAL A  73      26.900 -41.440  27.590  1.00 86.39           C  
ANISOU  596  CG2 VAL A  73    10823  11497  10503     55   -450    160       C  
ATOM    597  N   LYS A  74      26.846 -46.084  26.328  1.00 85.27           N  
ANISOU  597  N   LYS A  74    10654  11185  10561     80   -478    239       N  
ATOM    598  CA  LYS A  74      26.312 -47.260  25.640  1.00 80.27           C  
ANISOU  598  CA  LYS A  74    10015  10505   9979     81   -463    247       C  
ATOM    599  C   LYS A  74      27.237 -47.829  24.560  1.00 74.78           C  
ANISOU  599  C   LYS A  74     9283   9764   9365    105   -471    219       C  
ATOM    600  O   LYS A  74      28.262 -47.236  24.224  1.00 69.76           O  
ANISOU  600  O   LYS A  74     8625   9134   8746    121   -484    188       O  
ATOM    601  CB  LYS A  74      24.892 -47.010  25.124  1.00 78.26           C  
ANISOU  601  CB  LYS A  74     9773  10265   9698     61   -413    227       C  
ATOM    602  CG  LYS A  74      23.899 -46.635  26.227  1.00 75.70           C  
ANISOU  602  CG  LYS A  74     9484   9980   9299     35   -403    256       C  
ATOM    603  CD  LYS A  74      23.861 -47.672  27.352  1.00 78.20           C  
ANISOU  603  CD  LYS A  74     9822  10280   9609     25   -435    321       C  
ATOM    604  CE  LYS A  74      24.887 -47.391  28.456  1.00 81.00           C  
ANISOU  604  CE  LYS A  74    10184  10652   9939     31   -482    350       C  
ATOM    605  NZ  LYS A  74      24.695 -46.065  29.108  1.00 80.63           N  
ANISOU  605  NZ  LYS A  74    10153  10664   9820     16   -473    336       N  
ATOM    606  N   LYS A  75      26.861 -48.990  24.032  1.00 72.99           N  
ANISOU  606  N   LYS A  75     9051   9494   9188    106   -462    231       N  
ATOM    607  CA  LYS A  75      27.791 -49.848  23.306  1.00 70.54           C  
ANISOU  607  CA  LYS A  75     8708   9132   8960    128   -479    220       C  
ATOM    608  C   LYS A  75      27.358 -50.162  21.875  1.00 62.81           C  
ANISOU  608  C   LYS A  75     7711   8127   8028    129   -438    177       C  
ATOM    609  O   LYS A  75      27.637 -49.396  20.953  1.00 63.31           O  
ANISOU  609  O   LYS A  75     7755   8201   8099    133   -416    125       O  
ATOM    610  CB  LYS A  75      27.980 -51.147  24.090  1.00 78.55           C  
ANISOU  610  CB  LYS A  75     9732  10110  10004    132   -516    280       C  
ATOM    611  CG  LYS A  75      26.970 -51.333  25.220  1.00 82.31           C  
ANISOU  611  CG  LYS A  75    10248  10606  10418    108   -517    331       C  
ATOM    612  CD  LYS A  75      27.632 -51.236  26.591  1.00 84.14           C  
ANISOU  612  CD  LYS A  75    10497  10855  10617    109   -567    377       C  
ATOM    613  CE  LYS A  75      28.239 -49.860  26.835  1.00 85.27           C  
ANISOU  613  CE  LYS A  75    10636  11046  10717    113   -573    349       C  
ATOM    614  NZ  LYS A  75      27.428 -49.015  27.763  1.00 83.83           N  
ANISOU  614  NZ  LYS A  75    10488  10918  10447     87   -561    363       N  
ATOM    615  N   LYS A  76      26.689 -51.299  21.695  1.00 55.57           N  
ANISOU  615  N   LYS A  76     6799   7174   7141    122   -428    201       N  
ATOM    616  CA  LYS A  76      26.199 -51.711  20.378  1.00 48.97           C  
ANISOU  616  CA  LYS A  76     5946   6311   6348    120   -389    164       C  
ATOM    617  C   LYS A  76      25.136 -50.752  19.843  1.00 37.27           C  
ANISOU  617  C   LYS A  76     4477   4868   4818    101   -343    129       C  
ATOM    618  O   LYS A  76      24.669 -50.886  18.709  1.00 35.16           O  
ANISOU  618  O   LYS A  76     4198   4586   4577     96   -309     94       O  
ATOM    619  CB  LYS A  76      25.621 -53.126  20.432  1.00 50.58           C  
ANISOU  619  CB  LYS A  76     6158   6472   6589    114   -388    201       C  
ATOM    620  CG  LYS A  76      24.477 -53.287  21.420  1.00 52.97           C  
ANISOU  620  CG  LYS A  76     6498   6795   6834     92   -382    247       C  
ATOM    621  CD  LYS A  76      23.565 -54.439  21.020  1.00 58.69           C  
ANISOU  621  CD  LYS A  76     7227   7483   7589     80   -359    262       C  
ATOM    622  CE  LYS A  76      22.619 -54.808  22.149  1.00 62.81           C  
ANISOU  622  CE  LYS A  76     7786   8017   8060     59   -363    315       C  
ATOM    623  NZ  LYS A  76      23.363 -55.336  23.330  1.00 64.57           N  
ANISOU  623  NZ  LYS A  76     8021   8227   8284     66   -414    370       N  
ATOM    624  N   LYS A  77      24.733 -49.800  20.673  1.00 33.14           N  
ANISOU  624  N   LYS A  77     3977   4393   4223     90   -344    140       N  
ATOM    625  CA  LYS A  77      23.899 -48.711  20.196  1.00 35.10           C  
ANISOU  625  CA  LYS A  77     4232   4679   4425     76   -306    103       C  
ATOM    626  C   LYS A  77      24.641 -47.953  19.092  1.00 28.18           C  
ANISOU  626  C   LYS A  77     3330   3804   3573     88   -296     45       C  
ATOM    627  O   LYS A  77      24.024 -47.397  18.181  1.00 23.31           O  
ANISOU  627  O   LYS A  77     2710   3198   2947     79   -260      5       O  
ATOM    628  CB  LYS A  77      23.535 -47.763  21.341  1.00 43.08           C  
ANISOU  628  CB  LYS A  77     5269   5741   5359     64   -312    122       C  
ATOM    629  CG  LYS A  77      23.018 -46.413  20.860  1.00 52.46           C  
ANISOU  629  CG  LYS A  77     6460   6969   6503     56   -281     77       C  
ATOM    630  CD  LYS A  77      22.330 -45.622  21.958  1.00 51.14           C  
ANISOU  630  CD  LYS A  77     6320   6849   6260     39   -278     96       C  
ATOM    631  CE  LYS A  77      21.900 -44.270  21.421  1.00 55.61           C  
ANISOU  631  CE  LYS A  77     6886   7453   6791     34   -249     49       C  
ATOM    632  NZ  LYS A  77      21.019 -43.540  22.368  1.00 60.18           N  
ANISOU  632  NZ  LYS A  77     7490   8075   7300     15   -238     63       N  
ATOM    633  N   ILE A  78      25.971 -47.935  19.174  1.00 21.48           N  
ANISOU  633  N   ILE A  78     2462   2945   2755    107   -327     39       N  
ATOM    634  CA  ILE A  78      26.763 -47.212  18.190  1.00 18.93           C  
ANISOU  634  CA  ILE A  78     2115   2624   2455    117   -318    -16       C  
ATOM    635  C   ILE A  78      26.637 -47.851  16.817  1.00 20.90           C  
ANISOU  635  C   ILE A  78     2344   2835   2763    116   -291    -49       C  
ATOM    636  O   ILE A  78      26.399 -47.163  15.826  1.00 19.77           O  
ANISOU  636  O   ILE A  78     2195   2703   2614    109   -261    -96       O  
ATOM    637  CB  ILE A  78      28.245 -47.140  18.591  1.00 25.23           C  
ANISOU  637  CB  ILE A  78     2895   3416   3277    137   -358    -14       C  
ATOM    638  CG1 ILE A  78      28.405 -46.317  19.867  1.00 31.47           C  
ANISOU  638  CG1 ILE A  78     3705   4250   4004    135   -382     12       C  
ATOM    639  CG2 ILE A  78      29.061 -46.532  17.467  1.00 31.51           C  
ANISOU  639  CG2 ILE A  78     3663   4207   4103    145   -345    -74       C  
ATOM    640  CD1 ILE A  78      29.842 -46.246  20.373  1.00 36.61           C  
ANISOU  640  CD1 ILE A  78     4338   4896   4675    155   -425     17       C  
ATOM    641  N   LYS A  79      26.811 -49.168  16.753  1.00 21.64           N  
ANISOU  641  N   LYS A  79     2427   2883   2913    123   -302    -26       N  
ATOM    642  CA  LYS A  79      26.642 -49.882  15.495  1.00 22.44           C  
ANISOU  642  CA  LYS A  79     2509   2945   3071    121   -275    -56       C  
ATOM    643  C   LYS A  79      25.212 -49.773  14.965  1.00 16.37           C  
ANISOU  643  C   LYS A  79     1757   2189   2274     99   -234    -65       C  
ATOM    644  O   LYS A  79      25.000 -49.703  13.758  1.00 17.17           O  
ANISOU  644  O   LYS A  79     1847   2280   2398     92   -204   -108       O  
ATOM    645  CB  LYS A  79      27.017 -51.352  15.654  1.00 21.41           C  
ANISOU  645  CB  LYS A  79     2367   2764   3006    131   -296    -25       C  
ATOM    646  CG  LYS A  79      28.496 -51.580  15.905  1.00 27.16           C  
ANISOU  646  CG  LYS A  79     3070   3470   3779    154   -334    -24       C  
ATOM    647  CD  LYS A  79      28.923 -52.933  15.393  1.00 33.52           C  
ANISOU  647  CD  LYS A  79     3851   4216   4668    164   -340    -22       C  
ATOM    648  CE  LYS A  79      30.415 -53.148  15.565  1.00 38.03           C  
ANISOU  648  CE  LYS A  79     4394   4765   5291    188   -378    -26       C  
ATOM    649  NZ  LYS A  79      30.792 -54.506  15.089  1.00 37.33           N  
ANISOU  649  NZ  LYS A  79     4281   4616   5287    199   -383    -23       N  
ATOM    650  N   ARG A  80      24.229 -49.789  15.859  1.00 17.21           N  
ANISOU  650  N   ARG A  80     1891   2316   2331     87   -233    -26       N  
ATOM    651  CA  ARG A  80      22.837 -49.686  15.435  1.00 20.64           C  
ANISOU  651  CA  ARG A  80     2340   2763   2737     67   -196    -34       C  
ATOM    652  C   ARG A  80      22.621 -48.387  14.681  1.00 19.09           C  
ANISOU  652  C   ARG A  80     2143   2600   2509     61   -171    -84       C  
ATOM    653  O   ARG A  80      22.065 -48.391  13.586  1.00 13.78           O  
ANISOU  653  O   ARG A  80     1464   1920   1851     51   -140   -116       O  
ATOM    654  CB  ARG A  80      21.897 -49.749  16.638  1.00 17.29           C  
ANISOU  654  CB  ARG A  80     1947   2363   2261     55   -199     13       C  
ATOM    655  CG  ARG A  80      20.432 -49.773  16.279  1.00 18.45           C  
ANISOU  655  CG  ARG A  80     2108   2519   2384     34   -162      8       C  
ATOM    656  CD  ARG A  80      19.594 -49.895  17.542  1.00 18.00           C  
ANISOU  656  CD  ARG A  80     2080   2484   2277     21   -167     55       C  
ATOM    657  NE  ARG A  80      19.612 -48.661  18.322  1.00 20.32           N  
ANISOU  657  NE  ARG A  80     2387   2826   2507     18   -175     54       N  
ATOM    658  CZ  ARG A  80      19.137 -48.553  19.562  1.00 27.70           C  
ANISOU  658  CZ  ARG A  80     3347   3786   3392      7   -184     93       C  
ATOM    659  NH1 ARG A  80      18.636 -49.614  20.177  1.00 28.92           N  
ANISOU  659  NH1 ARG A  80     3516   3922   3552     -3   -188    136       N  
ATOM    660  NH2 ARG A  80      19.174 -47.385  20.192  1.00 24.51           N  
ANISOU  660  NH2 ARG A  80     2954   3427   2932      4   -188     87       N  
ATOM    661  N   GLU A  81      23.067 -47.271  15.258  1.00 17.61           N  
ANISOU  661  N   GLU A  81     1963   2451   2278     65   -185    -89       N  
ATOM    662  CA  GLU A  81      22.856 -45.980  14.616  1.00 14.79           C  
ANISOU  662  CA  GLU A  81     1607   2126   1887     59   -164   -133       C  
ATOM    663  C   GLU A  81      23.611 -45.938  13.288  1.00 15.07           C  
ANISOU  663  C   GLU A  81     1617   2138   1970     64   -153   -182       C  
ATOM    664  O   GLU A  81      23.076 -45.504  12.277  1.00 12.64           O  
ANISOU  664  O   GLU A  81     1309   1835   1659     53   -125   -219       O  
ATOM    665  CB  GLU A  81      23.263 -44.819  15.530  1.00 13.15           C  
ANISOU  665  CB  GLU A  81     1411   1962   1625     63   -182   -129       C  
ATOM    666  CG  GLU A  81      23.170 -43.451  14.858  1.00 16.14           C  
ANISOU  666  CG  GLU A  81     1790   2370   1972     58   -162   -176       C  
ATOM    667  CD  GLU A  81      23.466 -42.292  15.800  1.00 15.49           C  
ANISOU  667  CD  GLU A  81     1720   2331   1833     61   -178   -172       C  
ATOM    668  OE1 GLU A  81      23.835 -42.538  16.966  1.00 17.69           O  
ANISOU  668  OE1 GLU A  81     2006   2617   2098     66   -205   -133       O  
ATOM    669  OE2 GLU A  81      23.326 -41.132  15.373  1.00 17.23           O  
ANISOU  669  OE2 GLU A  81     1944   2579   2024     56   -163   -207       O  
ATOM    670  N   ILE A  82      24.860 -46.399  13.293  1.00 14.70           N  
ANISOU  670  N   ILE A  82     1550   2066   1969     80   -177   -184       N  
ATOM    671  CA  ILE A  82      25.650 -46.429  12.065  1.00 16.94           C  
ANISOU  671  CA  ILE A  82     1809   2327   2303     83   -167   -232       C  
ATOM    672  C   ILE A  82      25.022 -47.246  10.945  1.00 14.45           C  
ANISOU  672  C   ILE A  82     1484   1978   2027     72   -137   -249       C  
ATOM    673  O   ILE A  82      24.960 -46.791   9.808  1.00 17.47           O  
ANISOU  673  O   ILE A  82     1861   2362   2416     62   -113   -295       O  
ATOM    674  CB  ILE A  82      27.076 -46.943  12.315  1.00 17.93           C  
ANISOU  674  CB  ILE A  82     1910   2425   2477    103   -199   -228       C  
ATOM    675  CG1 ILE A  82      27.860 -45.916  13.140  1.00 19.47           C  
ANISOU  675  CG1 ILE A  82     2109   2656   2634    113   -224   -226       C  
ATOM    676  CG2 ILE A  82      27.736 -47.211  10.986  1.00 18.58           C  
ANISOU  676  CG2 ILE A  82     1965   2476   2617    103   -182   -277       C  
ATOM    677  CD1 ILE A  82      29.275 -46.375  13.546  1.00 19.46           C  
ANISOU  677  CD1 ILE A  82     2085   2632   2678    134   -261   -219       C  
ATOM    678  N   LYS A  83      24.574 -48.461  11.257  1.00 16.91           N  
ANISOU  678  N   LYS A  83     1798   2261   2367     72   -140   -214       N  
ATOM    679  CA  LYS A  83      23.957 -49.340  10.267  1.00 15.88           C  
ANISOU  679  CA  LYS A  83     1660   2098   2277     60   -112   -227       C  
ATOM    680  C   LYS A  83      22.671 -48.732   9.705  1.00 15.01           C  
ANISOU  680  C   LYS A  83     1566   2012   2123     40    -79   -245       C  
ATOM    681  O   LYS A  83      22.418 -48.753   8.494  1.00 14.41           O  
ANISOU  681  O   LYS A  83     1482   1926   2069     28    -53   -283       O  
ATOM    682  CB  LYS A  83      23.666 -50.715  10.880  1.00 15.92           C  
ANISOU  682  CB  LYS A  83     1667   2069   2312     63   -124   -180       C  
ATOM    683  CG  LYS A  83      23.158 -51.746   9.891  1.00 20.59           C  
ANISOU  683  CG  LYS A  83     2248   2623   2953     53    -97   -193       C  
ATOM    684  CD  LYS A  83      24.091 -51.880   8.710  1.00 28.36           C  
ANISOU  684  CD  LYS A  83     3203   3579   3993     56    -88   -242       C  
ATOM    685  CE  LYS A  83      23.485 -52.752   7.630  1.00 29.59           C  
ANISOU  685  CE  LYS A  83     3350   3703   4190     41    -56   -261       C  
ATOM    686  NZ  LYS A  83      24.445 -52.981   6.521  1.00 31.14           N  
ANISOU  686  NZ  LYS A  83     3517   3870   4445     42    -47   -309       N  
ATOM    687  N   ILE A  84      21.862 -48.174  10.593  1.00 13.52           N  
ANISOU  687  N   ILE A  84     1402   1859   1876     35    -82   -218       N  
ATOM    688  CA  ILE A  84      20.628 -47.524  10.169  1.00 14.53           C  
ANISOU  688  CA  ILE A  84     1545   2013   1963     17    -53   -233       C  
ATOM    689  C   ILE A  84      20.924 -46.357   9.222  1.00 14.65           C  
ANISOU  689  C   ILE A  84     1556   2048   1964     13    -41   -285       C  
ATOM    690  O   ILE A  84      20.294 -46.227   8.174  1.00 17.01           O  
ANISOU  690  O   ILE A  84     1854   2344   2267     -1    -15   -314       O  
ATOM    691  CB  ILE A  84      19.787 -47.068  11.388  1.00 15.22           C  
ANISOU  691  CB  ILE A  84     1657   2136   1990     13    -59   -197       C  
ATOM    692  CG1 ILE A  84      19.137 -48.292  12.054  1.00 18.48           C  
ANISOU  692  CG1 ILE A  84     2078   2528   2415      9    -61   -151       C  
ATOM    693  CG2 ILE A  84      18.709 -46.077  10.968  1.00 16.82           C  
ANISOU  693  CG2 ILE A  84     1872   2371   2146     -1    -34   -220       C  
ATOM    694  CD1 ILE A  84      18.420 -47.998  13.358  1.00 20.30           C  
ANISOU  694  CD1 ILE A  84     2333   2791   2590      4    -68   -112       C  
ATOM    695  N   LEU A  85      21.880 -45.505   9.590  1.00 13.95           N  
ANISOU  695  N   LEU A  85     1464   1978   1858     24    -60   -295       N  
ATOM    696  CA  LEU A  85      22.262 -44.380   8.732  1.00 12.39           C  
ANISOU  696  CA  LEU A  85     1263   1798   1646     20    -50   -343       C  
ATOM    697  C   LEU A  85      22.742 -44.859   7.367  1.00 13.72           C  
ANISOU  697  C   LEU A  85     1412   1933   1868     14    -34   -383       C  
ATOM    698  O   LEU A  85      22.444 -44.247   6.344  1.00 15.24           O  
ANISOU  698  O   LEU A  85     1607   2133   2051      0    -12   -421       O  
ATOM    699  CB  LEU A  85      23.346 -43.523   9.403  1.00 11.31           C  
ANISOU  699  CB  LEU A  85     1125   1684   1489     34    -74   -346       C  
ATOM    700  CG  LEU A  85      22.857 -42.634  10.560  1.00 13.05           C  
ANISOU  700  CG  LEU A  85     1368   1947   1645     35    -85   -321       C  
ATOM    701  CD1 LEU A  85      24.032 -42.138  11.415  1.00 14.85           C  
ANISOU  701  CD1 LEU A  85     1591   2190   1861     51   -114   -313       C  
ATOM    702  CD2 LEU A  85      22.024 -41.465  10.033  1.00 13.00           C  
ANISOU  702  CD2 LEU A  85     1374   1970   1593     22    -62   -349       C  
ATOM    703  N   GLU A  86      23.509 -45.945   7.351  1.00 18.52           N  
ANISOU  703  N   GLU A  86     2001   2504   2533     23    -44   -375       N  
ATOM    704  CA  GLU A  86      23.985 -46.489   6.081  1.00 20.17           C  
ANISOU  704  CA  GLU A  86     2189   2679   2797     16    -27   -413       C  
ATOM    705  C   GLU A  86      22.861 -47.113   5.255  1.00 19.39           C  
ANISOU  705  C   GLU A  86     2094   2564   2710     -3      2   -419       C  
ATOM    706  O   GLU A  86      22.788 -46.897   4.047  1.00 16.08           O  
ANISOU  706  O   GLU A  86     1670   2139   2302    -18     24   -461       O  
ATOM    707  CB  GLU A  86      25.144 -47.460   6.291  1.00 16.99           C  
ANISOU  707  CB  GLU A  86     1761   2239   2455     32    -47   -406       C  
ATOM    708  CG  GLU A  86      26.458 -46.722   6.514  1.00 19.51           C  
ANISOU  708  CG  GLU A  86     2068   2570   2773     46    -68   -426       C  
ATOM    709  CD  GLU A  86      27.627 -47.636   6.802  1.00 28.89           C  
ANISOU  709  CD  GLU A  86     3230   3723   4023     64    -91   -417       C  
ATOM    710  OE1 GLU A  86      27.481 -48.876   6.684  1.00 29.59           O  
ANISOU  710  OE1 GLU A  86     3309   3773   4161     66    -89   -401       O  
ATOM    711  OE2 GLU A  86      28.694 -47.095   7.168  1.00 29.86           O  
ANISOU  711  OE2 GLU A  86     3343   3856   4146     77   -112   -427       O  
ATOM    712  N   ASN A  87      21.985 -47.874   5.905  1.00 19.41           N  
ANISOU  712  N   ASN A  87     2106   2560   2709     -3      1   -377       N  
ATOM    713  CA  ASN A  87      20.816 -48.424   5.213  1.00 20.98           C  
ANISOU  713  CA  ASN A  87     2310   2748   2914    -21     29   -380       C  
ATOM    714  C   ASN A  87      19.945 -47.357   4.556  1.00 19.21           C  
ANISOU  714  C   ASN A  87     2100   2554   2643    -38     49   -408       C  
ATOM    715  O   ASN A  87      19.450 -47.546   3.449  1.00 17.41           O  
ANISOU  715  O   ASN A  87     1870   2315   2431    -55     73   -435       O  
ATOM    716  CB  ASN A  87      19.955 -49.263   6.160  1.00 19.87           C  
ANISOU  716  CB  ASN A  87     2181   2602   2768    -19     24   -330       C  
ATOM    717  CG  ASN A  87      20.600 -50.577   6.524  1.00 21.93           C  
ANISOU  717  CG  ASN A  87     2427   2821   3085     -7     10   -304       C  
ATOM    718  OD1 ASN A  87      21.596 -50.980   5.920  1.00 21.18           O  
ANISOU  718  OD1 ASN A  87     2310   2697   3040     -2      7   -328       O  
ATOM    719  ND2 ASN A  87      20.030 -51.261   7.518  1.00 17.18           N  
ANISOU  719  ND2 ASN A  87     1838   2216   2476     -4      0   -255       N  
ATOM    720  N   LEU A  88      19.778 -46.228   5.233  1.00 15.95           N  
ANISOU  720  N   LEU A  88     1703   2181   2176    -33     39   -401       N  
ATOM    721  CA  LEU A  88      18.824 -45.208   4.808  1.00 12.77           C  
ANISOU  721  CA  LEU A  88     1317   1809   1727    -47     54   -420       C  
ATOM    722  C   LEU A  88      19.453 -44.119   3.939  1.00 15.70           C  
ANISOU  722  C   LEU A  88     1686   2193   2087    -52     58   -466       C  
ATOM    723  O   LEU A  88      18.756 -43.245   3.430  1.00 15.46           O  
ANISOU  723  O   LEU A  88     1668   2184   2022    -64     70   -486       O  
ATOM    724  CB  LEU A  88      18.159 -44.556   6.029  1.00 17.62           C  
ANISOU  724  CB  LEU A  88     1949   2459   2286    -41     44   -387       C  
ATOM    725  CG  LEU A  88      17.305 -45.438   6.947  1.00 18.61           C  
ANISOU  725  CG  LEU A  88     2082   2580   2408    -41     43   -342       C  
ATOM    726  CD1 LEU A  88      16.814 -44.645   8.155  1.00 19.32           C  
ANISOU  726  CD1 LEU A  88     2191   2709   2441    -37     33   -316       C  
ATOM    727  CD2 LEU A  88      16.123 -46.027   6.190  1.00 16.43           C  
ANISOU  727  CD2 LEU A  88     1808   2292   2145    -58     69   -347       C  
ATOM    728  N   ARG A  89      20.764 -44.185   3.750  1.00 14.49           N  
ANISOU  728  N   ARG A  89     1518   2025   1964    -44     47   -484       N  
ATOM    729  CA  ARG A  89      21.484 -43.102   3.091  1.00 17.92           C  
ANISOU  729  CA  ARG A  89     1951   2473   2383    -48     48   -525       C  
ATOM    730  C   ARG A  89      21.001 -42.898   1.665  1.00 20.43           C  
ANISOU  730  C   ARG A  89     2273   2785   2706    -72     74   -565       C  
ATOM    731  O   ARG A  89      20.855 -43.854   0.903  1.00 15.60           O  
ANISOU  731  O   ARG A  89     1649   2142   2135    -83     89   -575       O  
ATOM    732  CB  ARG A  89      22.997 -43.363   3.132  1.00 20.16           C  
ANISOU  732  CB  ARG A  89     2215   2738   2707    -36     34   -539       C  
ATOM    733  CG  ARG A  89      23.854 -42.207   2.630  1.00 24.12           C  
ANISOU  733  CG  ARG A  89     2717   3257   3192    -39     33   -580       C  
ATOM    734  CD  ARG A  89      25.283 -42.291   3.187  1.00 21.61           C  
ANISOU  734  CD  ARG A  89     2381   2932   2898    -21     11   -581       C  
ATOM    735  NE  ARG A  89      25.871 -43.608   2.952  1.00 17.86           N  
ANISOU  735  NE  ARG A  89     1882   2415   2489    -16     10   -579       N  
ATOM    736  CZ  ARG A  89      26.865 -44.131   3.664  1.00 29.70           C  
ANISOU  736  CZ  ARG A  89     3364   3900   4022      4    -13   -564       C  
ATOM    737  NH1 ARG A  89      27.404 -43.449   4.672  1.00 28.08           N  
ANISOU  737  NH1 ARG A  89     3163   3721   3787     20    -38   -547       N  
ATOM    738  NH2 ARG A  89      27.324 -45.343   3.365  1.00 27.34           N  
ANISOU  738  NH2 ARG A  89     3041   3560   3786      7    -12   -565       N  
ATOM    739  N   GLY A  90      20.750 -41.643   1.313  1.00 18.08           N  
ANISOU  739  N   GLY A  90     1990   2515   2365    -80     77   -587       N  
ATOM    740  CA  GLY A  90      20.262 -41.307  -0.013  1.00 15.39           C  
ANISOU  740  CA  GLY A  90     1655   2172   2021   -104     97   -623       C  
ATOM    741  C   GLY A  90      18.742 -41.294  -0.103  1.00 20.97           C  
ANISOU  741  C   GLY A  90     2376   2890   2703   -114    108   -608       C  
ATOM    742  O   GLY A  90      18.181 -40.884  -1.117  1.00 23.78           O  
ANISOU  742  O   GLY A  90     2740   3248   3048   -133    122   -634       O  
ATOM    743  N   GLY A  91      18.073 -41.754   0.950  1.00 18.29           N  
ANISOU  743  N   GLY A  91     2039   2556   2355   -102    102   -567       N  
ATOM    744  CA  GLY A  91      16.612 -41.768   0.975  1.00 15.75           C  
ANISOU  744  CA  GLY A  91     1728   2245   2010   -111    113   -552       C  
ATOM    745  C   GLY A  91      16.058 -40.359   1.088  1.00 16.34           C  
ANISOU  745  C   GLY A  91     1821   2355   2032   -112    109   -561       C  
ATOM    746  O   GLY A  91      16.758 -39.454   1.522  1.00 15.24           O  
ANISOU  746  O   GLY A  91     1686   2235   1869   -102     95   -567       O  
ATOM    747  N   PRO A  92      14.797 -40.152   0.677  1.00 13.63           N  
ANISOU  747  N   PRO A  92     1487   2021   1671   -125    120   -563       N  
ATOM    748  CA  PRO A  92      14.239 -38.790   0.685  1.00 10.85           C  
ANISOU  748  CA  PRO A  92     1150   1701   1273   -126    116   -575       C  
ATOM    749  C   PRO A  92      14.276 -38.131   2.061  1.00 12.49           C  
ANISOU  749  C   PRO A  92     1364   1936   1445   -108    102   -550       C  
ATOM    750  O   PRO A  92      13.742 -38.676   3.018  1.00 14.51           O  
ANISOU  750  O   PRO A  92     1619   2196   1697   -101    101   -517       O  
ATOM    751  CB  PRO A  92      12.789 -38.992   0.213  1.00 15.75           C  
ANISOU  751  CB  PRO A  92     1774   2321   1889   -140    130   -573       C  
ATOM    752  CG  PRO A  92      12.524 -40.431   0.318  1.00 22.20           C  
ANISOU  752  CG  PRO A  92     2580   3113   2742   -142    140   -552       C  
ATOM    753  CD  PRO A  92      13.825 -41.155   0.223  1.00 18.05           C  
ANISOU  753  CD  PRO A  92     2041   2562   2254   -137    136   -556       C  
ATOM    754  N   ASN A  93      14.931 -36.974   2.156  1.00 15.60           N  
ANISOU  754  N   ASN A  93     1766   2349   1813   -102     91   -567       N  
ATOM    755  CA  ASN A  93      14.928 -36.189   3.391  1.00 16.13           C  
ANISOU  755  CA  ASN A  93     1841   2447   1842    -88     79   -548       C  
ATOM    756  C   ASN A  93      15.581 -36.863   4.605  1.00 17.10           C  
ANISOU  756  C   ASN A  93     1957   2568   1973    -72     67   -515       C  
ATOM    757  O   ASN A  93      15.361 -36.460   5.735  1.00 15.52           O  
ANISOU  757  O   ASN A  93     1763   2391   1742    -63     59   -493       O  
ATOM    758  CB  ASN A  93      13.493 -35.719   3.694  1.00 16.21           C  
ANISOU  758  CB  ASN A  93     1860   2477   1822    -91     85   -539       C  
ATOM    759  CG  ASN A  93      12.975 -34.770   2.630  1.00 19.04           C  
ANISOU  759  CG  ASN A  93     2228   2842   2166   -103     90   -571       C  
ATOM    760  OD1 ASN A  93      13.764 -34.182   1.890  1.00 15.66           O  
ANISOU  760  OD1 ASN A  93     1802   2409   1737   -108     86   -599       O  
ATOM    761  ND2 ASN A  93      11.648 -34.609   2.550  1.00 15.29           N  
ANISOU  761  ND2 ASN A  93     1756   2375   1678   -110     98   -568       N  
ATOM    762  N   ILE A  94      16.389 -37.889   4.370  1.00 14.72           N  
ANISOU  762  N   ILE A  94     1642   2238   1713    -70     65   -513       N  
ATOM    763  CA  ILE A  94      17.151 -38.512   5.458  1.00 11.60           C  
ANISOU  763  CA  ILE A  94     1239   1838   1329    -55     50   -482       C  
ATOM    764  C   ILE A  94      18.513 -37.817   5.534  1.00 11.64           C  
ANISOU  764  C   ILE A  94     1241   1851   1331    -46     35   -501       C  
ATOM    765  O   ILE A  94      19.142 -37.618   4.517  1.00 11.72           O  
ANISOU  765  O   ILE A  94     1246   1848   1360    -52     40   -535       O  
ATOM    766  CB  ILE A  94      17.398 -40.017   5.164  1.00 17.52           C  
ANISOU  766  CB  ILE A  94     1974   2550   2132    -56     54   -470       C  
ATOM    767  CG1 ILE A  94      16.071 -40.746   4.877  1.00 15.03           C  
ANISOU  767  CG1 ILE A  94     1661   2225   1824    -68     72   -458       C  
ATOM    768  CG2 ILE A  94      18.211 -40.673   6.287  1.00 18.80           C  
ANISOU  768  CG2 ILE A  94     2130   2706   2309    -39     34   -437       C  
ATOM    769  CD1 ILE A  94      15.070 -40.683   6.012  1.00 15.09           C  
ANISOU  769  CD1 ILE A  94     1681   2256   1798    -65     71   -424       C  
ATOM    770  N   ILE A  95      18.963 -37.449   6.729  1.00 11.55           N  
ANISOU  770  N   ILE A  95     1234   1860   1296    -32     17   -479       N  
ATOM    771  CA  ILE A  95      20.273 -36.826   6.849  1.00 11.13           C  
ANISOU  771  CA  ILE A  95     1176   1814   1240    -23      2   -496       C  
ATOM    772  C   ILE A  95      21.332 -37.781   6.289  1.00 12.75           C  
ANISOU  772  C   ILE A  95     1361   1984   1500    -20     -1   -506       C  
ATOM    773  O   ILE A  95      21.238 -39.009   6.461  1.00 12.96           O  
ANISOU  773  O   ILE A  95     1378   1985   1561    -17     -2   -482       O  
ATOM    774  CB  ILE A  95      20.597 -36.440   8.316  1.00 11.01           C  
ANISOU  774  CB  ILE A  95     1166   1824   1192     -8    -18   -466       C  
ATOM    775  CG1 ILE A  95      21.732 -35.409   8.345  1.00 12.93           C  
ANISOU  775  CG1 ILE A  95     1408   2083   1420     -2    -29   -491       C  
ATOM    776  CG2 ILE A  95      20.946 -37.676   9.154  1.00 12.19           C  
ANISOU  776  CG2 ILE A  95     1306   1955   1369      2    -32   -427       C  
ATOM    777  CD1 ILE A  95      21.335 -34.035   7.849  1.00 14.05           C  
ANISOU  777  CD1 ILE A  95     1564   2249   1524    -11    -19   -522       C  
ATOM    778  N   THR A  96      22.320 -37.220   5.597  1.00 15.31           N  
ANISOU  778  N   THR A  96     1679   2304   1832    -22     -2   -543       N  
ATOM    779  CA  THR A  96      23.376 -38.007   4.991  1.00 11.90           C  
ANISOU  779  CA  THR A  96     1227   1841   1454    -21     -3   -560       C  
ATOM    780  C   THR A  96      24.583 -38.136   5.907  1.00 14.24           C  
ANISOU  780  C   THR A  96     1511   2138   1761     -2    -27   -546       C  
ATOM    781  O   THR A  96      25.209 -37.147   6.294  1.00 18.06           O  
ANISOU  781  O   THR A  96     1999   2646   2216      4    -39   -557       O  
ATOM    782  CB  THR A  96      23.843 -37.402   3.650  1.00 16.26           C  
ANISOU  782  CB  THR A  96     1777   2387   2013    -36     12   -612       C  
ATOM    783  OG1 THR A  96      22.788 -37.499   2.694  1.00 18.45           O  
ANISOU  783  OG1 THR A  96     2064   2658   2290    -55     33   -624       O  
ATOM    784  CG2 THR A  96      25.057 -38.150   3.111  1.00 21.88           C  
ANISOU  784  CG2 THR A  96     2466   3068   2780    -35     11   -633       C  
ATOM    785  N   LEU A  97      24.894 -39.373   6.244  1.00 14.79           N  
ANISOU  785  N   LEU A  97     1565   2180   1873      7    -36   -522       N  
ATOM    786  CA  LEU A  97      26.129 -39.680   6.941  1.00 16.95           C  
ANISOU  786  CA  LEU A  97     1823   2446   2171     25    -61   -512       C  
ATOM    787  C   LEU A  97      27.234 -39.676   5.910  1.00 15.10           C  
ANISOU  787  C   LEU A  97     1569   2192   1977     21    -55   -558       C  
ATOM    788  O   LEU A  97      27.267 -40.522   5.022  1.00 16.78           O  
ANISOU  788  O   LEU A  97     1768   2372   2236     13    -41   -574       O  
ATOM    789  CB  LEU A  97      26.042 -41.055   7.595  1.00 19.71           C  
ANISOU  789  CB  LEU A  97     2164   2770   2557     36    -74   -470       C  
ATOM    790  CG  LEU A  97      27.300 -41.519   8.340  1.00 15.61           C  
ANISOU  790  CG  LEU A  97     1626   2238   2068     55   -103   -455       C  
ATOM    791  CD1 LEU A  97      27.589 -40.640   9.545  1.00 14.71           C  
ANISOU  791  CD1 LEU A  97     1523   2160   1904     66   -127   -434       C  
ATOM    792  CD2 LEU A  97      27.125 -42.960   8.777  1.00 16.73           C  
ANISOU  792  CD2 LEU A  97     1760   2347   2251     63   -113   -416       C  
ATOM    793  N   ALA A  98      28.141 -38.717   6.022  1.00 13.74           N  
ANISOU  793  N   ALA A  98     1395   2038   1786     25    -65   -581       N  
ATOM    794  CA  ALA A  98      29.205 -38.567   5.038  1.00 17.45           C  
ANISOU  794  CA  ALA A  98     1848   2493   2289     19    -57   -630       C  
ATOM    795  C   ALA A  98      30.426 -39.427   5.344  1.00 16.81           C  
ANISOU  795  C   ALA A  98     1739   2386   2264     35    -76   -627       C  
ATOM    796  O   ALA A  98      31.154 -39.845   4.436  1.00 17.32           O  
ANISOU  796  O   ALA A  98     1781   2422   2375     29    -65   -663       O  
ATOM    797  CB  ALA A  98      29.607 -37.117   4.930  1.00 19.68           C  
ANISOU  797  CB  ALA A  98     2142   2808   2528     13    -56   -659       C  
ATOM    798  N   ASP A  99      30.661 -39.699   6.621  1.00 14.01           N  
ANISOU  798  N   ASP A  99     1381   2038   1904     55   -104   -585       N  
ATOM    799  CA  ASP A  99      31.871 -40.404   7.001  1.00 16.23           C  
ANISOU  799  CA  ASP A  99     1635   2296   2235     72   -128   -581       C  
ATOM    800  C   ASP A  99      31.774 -40.806   8.464  1.00 18.17           C  
ANISOU  800  C   ASP A  99     1886   2550   2469     91   -159   -524       C  
ATOM    801  O   ASP A  99      30.901 -40.337   9.193  1.00 15.16           O  
ANISOU  801  O   ASP A  99     1529   2197   2033     89   -162   -494       O  
ATOM    802  CB  ASP A  99      33.071 -39.476   6.802  1.00 18.00           C  
ANISOU  802  CB  ASP A  99     1848   2534   2456     74   -133   -622       C  
ATOM    803  CG  ASP A  99      34.365 -40.223   6.489  1.00 17.41           C  
ANISOU  803  CG  ASP A  99     1738   2426   2450     83   -143   -644       C  
ATOM    804  OD1 ASP A  99      34.409 -41.468   6.574  1.00 18.50           O  
ANISOU  804  OD1 ASP A  99     1860   2530   2641     93   -151   -624       O  
ATOM    805  OD2 ASP A  99      35.345 -39.540   6.140  1.00 19.56           O  
ANISOU  805  OD2 ASP A  99     1999   2706   2726     81   -143   -685       O  
ATOM    806  N   ILE A 100      32.673 -41.688   8.887  1.00 17.05           N  
ANISOU  806  N   ILE A 100     1720   2381   2377    108   -184   -510       N  
ATOM    807  CA  ILE A 100      32.795 -42.056  10.288  1.00 13.66           C  
ANISOU  807  CA  ILE A 100     1294   1958   1938    126   -219   -457       C  
ATOM    808  C   ILE A 100      34.291 -42.111  10.553  1.00 14.50           C  
ANISOU  808  C   ILE A 100     1373   2054   2082    143   -247   -470       C  
ATOM    809  O   ILE A 100      35.022 -42.741   9.793  1.00 18.43           O  
ANISOU  809  O   ILE A 100     1843   2518   2642    146   -242   -499       O  
ATOM    810  CB  ILE A 100      32.230 -43.455  10.560  1.00 17.79           C  
ANISOU  810  CB  ILE A 100     1815   2447   2496    131   -225   -415       C  
ATOM    811  CG1 ILE A 100      30.811 -43.592  10.009  1.00 21.92           C  
ANISOU  811  CG1 ILE A 100     2358   2970   2998    112   -192   -412       C  
ATOM    812  CG2 ILE A 100      32.272 -43.743  12.057  1.00 18.94           C  
ANISOU  812  CG2 ILE A 100     1971   2603   2623    146   -261   -358       C  
ATOM    813  CD1 ILE A 100      30.397 -45.041   9.730  1.00 22.93           C  
ANISOU  813  CD1 ILE A 100     2477   3055   3180    112   -186   -392       C  
ATOM    814  N   VAL A 101      34.743 -41.435  11.601  1.00 12.67           N  
ANISOU  814  N   VAL A 101     1148   1853   1812    154   -274   -451       N  
ATOM    815  CA  VAL A 101      36.164 -41.418  11.940  1.00 12.95           C  
ANISOU  815  CA  VAL A 101     1158   1883   1880    170   -303   -462       C  
ATOM    816  C   VAL A 101      36.305 -41.701  13.429  1.00 19.18           C  
ANISOU  816  C   VAL A 101     1954   2682   2652    186   -345   -405       C  
ATOM    817  O   VAL A 101      35.346 -41.553  14.190  1.00 19.93           O  
ANISOU  817  O   VAL A 101     2078   2800   2695    181   -346   -366       O  
ATOM    818  CB  VAL A 101      36.833 -40.062  11.632  1.00 17.75           C  
ANISOU  818  CB  VAL A 101     1765   2523   2457    164   -295   -509       C  
ATOM    819  CG1 VAL A 101      36.673 -39.683  10.143  1.00 17.91           C  
ANISOU  819  CG1 VAL A 101     1783   2536   2487    145   -254   -566       C  
ATOM    820  CG2 VAL A 101      36.281 -38.968  12.545  1.00 18.27           C  
ANISOU  820  CG2 VAL A 101     1861   2638   2442    160   -301   -486       C  
ATOM    821  N   LYS A 102      37.501 -42.114  13.840  1.00 16.87           N  
ANISOU  821  N   LYS A 102     1635   2373   2402    205   -378   -402       N  
ATOM    822  CA  LYS A 102      37.788 -42.335  15.250  1.00 16.94           C  
ANISOU  822  CA  LYS A 102     1650   2392   2395    220   -422   -349       C  
ATOM    823  C   LYS A 102      38.310 -41.036  15.830  1.00 21.09           C  
ANISOU  823  C   LYS A 102     2183   2964   2867    220   -434   -361       C  
ATOM    824  O   LYS A 102      39.368 -40.550  15.421  1.00 22.12           O  
ANISOU  824  O   LYS A 102     2290   3096   3018    225   -437   -404       O  
ATOM    825  CB  LYS A 102      38.858 -43.425  15.418  1.00 19.34           C  
ANISOU  825  CB  LYS A 102     1919   2654   2775    241   -457   -339       C  
ATOM    826  CG  LYS A 102      38.492 -44.754  14.770  1.00 29.98           C  
ANISOU  826  CG  LYS A 102     3254   3950   4186    242   -445   -333       C  
ATOM    827  CD  LYS A 102      39.469 -45.859  15.165  1.00 44.03           C  
ANISOU  827  CD  LYS A 102     5003   5688   6038    265   -485   -312       C  
ATOM    828  CE  LYS A 102      39.078 -47.185  14.531  1.00 45.45           C  
ANISOU  828  CE  LYS A 102     5171   5816   6281    266   -472   -306       C  
ATOM    829  NZ  LYS A 102      39.629 -48.348  15.281  1.00 50.62           N  
ANISOU  829  NZ  LYS A 102     5809   6433   6990    288   -517   -262       N  
ATOM    830  N   ASP A 103      37.599 -40.469  16.791  1.00 15.74           N  
ANISOU  830  N   ASP A 103     1638   1947   2394    -55   -449   -203       N  
ATOM    831  CA  ASP A 103      38.127 -39.275  17.428  1.00 16.68           C  
ANISOU  831  CA  ASP A 103     1733   2018   2587    -73   -484   -223       C  
ATOM    832  C   ASP A 103      39.247 -39.661  18.407  1.00 19.33           C  
ANISOU  832  C   ASP A 103     2059   2352   2932    -86   -522   -247       C  
ATOM    833  O   ASP A 103      39.066 -40.527  19.260  1.00 19.43           O  
ANISOU  833  O   ASP A 103     2103   2390   2888    -81   -538   -286       O  
ATOM    834  CB  ASP A 103      37.035 -38.463  18.117  1.00 13.90           C  
ANISOU  834  CB  ASP A 103     1406   1643   2234    -74   -499   -269       C  
ATOM    835  CG  ASP A 103      37.561 -37.160  18.663  1.00 22.96           C  
ANISOU  835  CG  ASP A 103     2529   2735   3459    -93   -532   -286       C  
ATOM    836  OD1 ASP A 103      37.670 -36.192  17.884  1.00 23.60           O  
ANISOU  836  OD1 ASP A 103     2582   2786   3598    -99   -519   -252       O  
ATOM    837  OD2 ASP A 103      37.881 -37.098  19.867  1.00 24.50           O  
ANISOU  837  OD2 ASP A 103     2735   2917   3657   -104   -572   -333       O  
ATOM    838  N   PRO A 104      40.417 -39.021  18.279  1.00 21.38           N  
ANISOU  838  N   PRO A 104     2275   2584   3264   -102   -538   -224       N  
ATOM    839  CA  PRO A 104      41.566 -39.448  19.084  1.00 20.53           C  
ANISOU  839  CA  PRO A 104     2154   2479   3166   -114   -571   -238       C  
ATOM    840  C   PRO A 104      41.509 -38.921  20.523  1.00 20.26           C  
ANISOU  840  C   PRO A 104     2137   2418   3145   -130   -620   -300       C  
ATOM    841  O   PRO A 104      42.218 -39.426  21.399  1.00 23.15           O  
ANISOU  841  O   PRO A 104     2502   2793   3500   -138   -650   -324       O  
ATOM    842  CB  PRO A 104      42.746 -38.820  18.338  1.00 22.97           C  
ANISOU  842  CB  PRO A 104     2409   2766   3551   -127   -569   -185       C  
ATOM    843  CG  PRO A 104      42.186 -37.543  17.813  1.00 21.03           C  
ANISOU  843  CG  PRO A 104     2152   2481   3356   -134   -560   -174       C  
ATOM    844  CD  PRO A 104      40.742 -37.862  17.425  1.00 16.97           C  
ANISOU  844  CD  PRO A 104     1677   1988   2781   -112   -527   -183       C  
ATOM    845  N   VAL A 105      40.686 -37.905  20.756  1.00 14.93           N  
ANISOU  845  N   VAL A 105     1474   1710   2490   -134   -627   -326       N  
ATOM    846  CA  VAL A 105      40.521 -37.351  22.096  1.00 14.93           C  
ANISOU  846  CA  VAL A 105     1493   1681   2499   -148   -671   -386       C  
ATOM    847  C   VAL A 105      39.449 -38.097  22.887  1.00 19.26           C  
ANISOU  847  C   VAL A 105     2093   2258   2968   -132   -673   -436       C  
ATOM    848  O   VAL A 105      39.673 -38.473  24.034  1.00 21.24           O  
ANISOU  848  O   VAL A 105     2360   2513   3196   -138   -707   -481       O  
ATOM    849  CB  VAL A 105      40.196 -35.831  22.062  1.00 18.21           C  
ANISOU  849  CB  VAL A 105     1899   2042   2978   -160   -681   -392       C  
ATOM    850  CG1 VAL A 105      39.957 -35.311  23.474  1.00 18.50           C  
ANISOU  850  CG1 VAL A 105     1963   2050   3017   -171   -725   -458       C  
ATOM    851  CG2 VAL A 105      41.335 -35.052  21.407  1.00 18.80           C  
ANISOU  851  CG2 VAL A 105     1924   2086   3135   -179   -684   -346       C  
ATOM    852  N   SER A 106      38.283 -38.316  22.279  1.00 20.03           N  
ANISOU  852  N   SER A 106     2214   2376   3022   -112   -638   -428       N  
ATOM    853  CA  SER A 106      37.201 -38.978  22.995  1.00 20.51           C  
ANISOU  853  CA  SER A 106     2322   2464   3007    -98   -639   -473       C  
ATOM    854  C   SER A 106      37.412 -40.488  23.038  1.00 26.82           C  
ANISOU  854  C   SER A 106     3137   3315   3739    -87   -630   -470       C  
ATOM    855  O   SER A 106      36.862 -41.174  23.908  1.00 27.67           O  
ANISOU  855  O   SER A 106     3280   3445   3786    -80   -643   -513       O  
ATOM    856  CB  SER A 106      35.854 -38.684  22.337  1.00 15.10           C  
ANISOU  856  CB  SER A 106     1655   1784   2297    -81   -606   -463       C  
ATOM    857  OG  SER A 106      35.819 -39.254  21.046  1.00 15.77           O  
ANISOU  857  OG  SER A 106     1729   1898   2365    -70   -563   -408       O  
ATOM    858  N   ARG A 107      38.199 -40.999  22.089  1.00 20.61           N  
ANISOU  858  N   ARG A 107     2323   2545   2962    -85   -607   -417       N  
ATOM    859  CA  ARG A 107      38.417 -42.435  21.952  1.00 22.22           C  
ANISOU  859  CA  ARG A 107     2543   2797   3102    -73   -593   -406       C  
ATOM    860  C   ARG A 107      37.098 -43.122  21.613  1.00 27.32           C  
ANISOU  860  C   ARG A 107     3229   3478   3672    -55   -562   -410       C  
ATOM    861  O   ARG A 107      36.841 -44.248  22.036  1.00 31.57           O  
ANISOU  861  O   ARG A 107     3799   4053   4141    -46   -563   -430       O  
ATOM    862  CB  ARG A 107      39.023 -43.010  23.240  1.00 27.91           C  
ANISOU  862  CB  ARG A 107     3274   3526   3803    -81   -632   -450       C  
ATOM    863  CG  ARG A 107      40.292 -42.276  23.706  1.00 33.68           C  
ANISOU  863  CG  ARG A 107     3967   4222   4609   -103   -668   -451       C  
ATOM    864  CD  ARG A 107      40.730 -42.707  25.107  1.00 35.10           C  
ANISOU  864  CD  ARG A 107     4161   4406   4769   -112   -710   -502       C  
ATOM    865  NE  ARG A 107      41.056 -44.130  25.149  1.00 27.37           N  
ANISOU  865  NE  ARG A 107     3196   3474   3730    -99   -701   -495       N  
ATOM    866  CZ  ARG A 107      42.144 -44.646  24.603  1.00 29.03           C  
ANISOU  866  CZ  ARG A 107     3377   3699   3954    -98   -691   -452       C  
ATOM    867  NH1 ARG A 107      43.000 -43.850  23.983  1.00 30.32           N  
ANISOU  867  NH1 ARG A 107     3493   3835   4190   -110   -690   -412       N  
ATOM    868  NH2 ARG A 107      42.375 -45.948  24.673  1.00 28.45           N  
ANISOU  868  NH2 ARG A 107     3320   3666   3822    -84   -681   -448       N  
ATOM    869  N   THR A 108      36.265 -42.426  20.844  1.00 22.72           N  
ANISOU  869  N   THR A 108     2646   2885   3104    -50   -537   -390       N  
ATOM    870  CA  THR A 108      34.984 -42.957  20.399  1.00 19.54           C  
ANISOU  870  CA  THR A 108     2276   2514   2633    -34   -506   -387       C  
ATOM    871  C   THR A 108      34.765 -42.583  18.938  1.00 20.95           C  
ANISOU  871  C   THR A 108     2435   2691   2835    -28   -465   -329       C  
ATOM    872  O   THR A 108      35.482 -41.740  18.393  1.00 17.29           O  
ANISOU  872  O   THR A 108     1932   2196   2443    -37   -463   -298       O  
ATOM    873  CB  THR A 108      33.813 -42.387  21.226  1.00 21.06           C  
ANISOU  873  CB  THR A 108     2498   2696   2810    -32   -522   -436       C  
ATOM    874  OG1 THR A 108      33.752 -40.969  21.050  1.00 19.03           O  
ANISOU  874  OG1 THR A 108     2217   2393   2623    -39   -526   -431       O  
ATOM    875  CG2 THR A 108      33.996 -42.696  22.701  1.00 26.62           C  
ANISOU  875  CG2 THR A 108     3222   3400   3491    -37   -564   -495       C  
ATOM    876  N   PRO A 109      33.764 -43.197  18.300  1.00 21.75           N  
ANISOU  876  N   PRO A 109     2562   2826   2876    -15   -432   -313       N  
ATOM    877  CA  PRO A 109      33.491 -42.855  16.903  1.00 18.62           C  
ANISOU  877  CA  PRO A 109     2148   2429   2497    -10   -393   -258       C  
ATOM    878  C   PRO A 109      32.887 -41.470  16.793  1.00 16.15           C  
ANISOU  878  C   PRO A 109     1821   2080   2236    -13   -393   -261       C  
ATOM    879  O   PRO A 109      32.127 -41.038  17.676  1.00 20.30           O  
ANISOU  879  O   PRO A 109     2367   2596   2751    -13   -413   -305       O  
ATOM    880  CB  PRO A 109      32.468 -43.915  16.470  1.00 18.07           C  
ANISOU  880  CB  PRO A 109     2118   2408   2341      3   -364   -250       C  
ATOM    881  CG  PRO A 109      32.593 -45.009  17.486  1.00 23.41           C  
ANISOU  881  CG  PRO A 109     2826   3111   2957      4   -386   -290       C  
ATOM    882  CD  PRO A 109      32.919 -44.307  18.769  1.00 17.86           C  
ANISOU  882  CD  PRO A 109     2116   2376   2293     -6   -430   -341       C  
ATOM    883  N   ALA A 110      33.225 -40.789  15.705  1.00 14.15           N  
ANISOU  883  N   ALA A 110     1533   1807   2037    -15   -370   -212       N  
ATOM    884  CA  ALA A 110      32.703 -39.468  15.404  1.00 13.72           C  
ANISOU  884  CA  ALA A 110     1462   1717   2034    -17   -365   -205       C  
ATOM    885  C   ALA A 110      31.998 -39.555  14.059  1.00 18.00           C  
ANISOU  885  C   ALA A 110     2002   2279   2557     -6   -319   -155       C  
ATOM    886  O   ALA A 110      32.630 -39.800  13.039  1.00 14.93           O  
ANISOU  886  O   ALA A 110     1591   1897   2184     -6   -295   -106       O  
ATOM    887  CB  ALA A 110      33.820 -38.443  15.352  1.00 15.53           C  
ANISOU  887  CB  ALA A 110     1648   1899   2354    -31   -382   -191       C  
ATOM    888  N   LEU A 111      30.683 -39.369  14.063  1.00 16.18           N  
ANISOU  888  N   LEU A 111     1797   2061   2291      3   -307   -167       N  
ATOM    889  CA  LEU A 111      29.911 -39.402  12.827  1.00 17.34           C  
ANISOU  889  CA  LEU A 111     1943   2228   2418     12   -264   -121       C  
ATOM    890  C   LEU A 111      29.906 -38.036  12.157  1.00 18.10           C  
ANISOU  890  C   LEU A 111     2005   2284   2589     10   -253    -93       C  
ATOM    891  O   LEU A 111      29.638 -37.012  12.804  1.00 17.83           O  
ANISOU  891  O   LEU A 111     1968   2214   2594      7   -273   -122       O  
ATOM    892  CB  LEU A 111      28.462 -39.835  13.092  1.00 16.33           C  
ANISOU  892  CB  LEU A 111     1855   2134   2215     22   -255   -142       C  
ATOM    893  CG  LEU A 111      28.202 -41.069  13.959  1.00 17.60           C  
ANISOU  893  CG  LEU A 111     2057   2334   2297     24   -270   -180       C  
ATOM    894  CD1 LEU A 111      26.707 -41.375  13.972  1.00 14.61           C  
ANISOU  894  CD1 LEU A 111     1713   1989   1850     33   -255   -189       C  
ATOM    895  CD2 LEU A 111      28.984 -42.265  13.487  1.00 19.53           C  
ANISOU  895  CD2 LEU A 111     2304   2606   2509     23   -259   -155       C  
ATOM    896  N   VAL A 112      30.169 -38.024  10.853  1.00 13.13           N  
ANISOU  896  N   VAL A 112     1352   1660   1978     11   -220    -35       N  
ATOM    897  CA  VAL A 112      30.215 -36.786  10.081  1.00 15.18           C  
ANISOU  897  CA  VAL A 112     1577   1883   2309      9   -205     -1       C  
ATOM    898  C   VAL A 112      28.989 -36.714   9.183  1.00 15.06           C  
ANISOU  898  C   VAL A 112     1571   1890   2260     20   -168     28       C  
ATOM    899  O   VAL A 112      28.768 -37.600   8.355  1.00 16.67           O  
ANISOU  899  O   VAL A 112     1785   2132   2415     25   -139     61       O  
ATOM    900  CB  VAL A 112      31.479 -36.734   9.217  1.00 14.05           C  
ANISOU  900  CB  VAL A 112     1394   1727   2218      2   -195     46       C  
ATOM    901  CG1 VAL A 112      31.563 -35.402   8.457  1.00 18.45           C  
ANISOU  901  CG1 VAL A 112     1914   2244   2852     -1   -182     80       C  
ATOM    902  CG2 VAL A 112      32.707 -36.953  10.085  1.00 12.94           C  
ANISOU  902  CG2 VAL A 112     1244   1572   2103     -9   -231     21       C  
ATOM    903  N   PHE A 113      28.193 -35.667   9.358  1.00 12.23           N  
ANISOU  903  N   PHE A 113     1213   1508   1927     24   -169     16       N  
ATOM    904  CA  PHE A 113      26.921 -35.514   8.624  1.00 13.54           C  
ANISOU  904  CA  PHE A 113     1388   1695   2060     35   -137     40       C  
ATOM    905  C   PHE A 113      26.944 -34.299   7.712  1.00 19.03           C  
ANISOU  905  C   PHE A 113     2048   2356   2825     36   -117     80       C  
ATOM    906  O   PHE A 113      27.703 -33.339   7.932  1.00 13.98           O  
ANISOU  906  O   PHE A 113     1382   1669   2261     28   -135     75       O  
ATOM    907  CB  PHE A 113      25.746 -35.309   9.586  1.00 13.58           C  
ANISOU  907  CB  PHE A 113     1425   1707   2028     44   -150     -7       C  
ATOM    908  CG  PHE A 113      25.487 -36.461  10.493  1.00 14.71           C  
ANISOU  908  CG  PHE A 113     1606   1886   2096     45   -168    -47       C  
ATOM    909  CD1 PHE A 113      24.661 -37.501  10.092  1.00 16.37           C  
ANISOU  909  CD1 PHE A 113     1845   2150   2227     51   -145    -33       C  
ATOM    910  CD2 PHE A 113      26.023 -36.485  11.769  1.00 16.63           C  
ANISOU  910  CD2 PHE A 113     1860   2111   2349     39   -207    -99       C  
ATOM    911  CE1 PHE A 113      24.390 -38.552  10.943  1.00 17.88           C  
ANISOU  911  CE1 PHE A 113     2071   2374   2347     51   -162    -71       C  
ATOM    912  CE2 PHE A 113      25.770 -37.542  12.622  1.00 12.89           C  
ANISOU  912  CE2 PHE A 113     1421   1671   1806     41   -224   -137       C  
ATOM    913  CZ  PHE A 113      24.953 -38.577  12.209  1.00 16.56           C  
ANISOU  913  CZ  PHE A 113     1913   2189   2191     47   -201   -122       C  
ATOM    914  N   GLU A 114      26.082 -34.324   6.704  1.00 13.90           N  
ANISOU  914  N   GLU A 114     1400   1731   2151     44    -81    119       N  
ATOM    915  CA  GLU A 114      25.899 -33.160   5.865  1.00 16.51           C  
ANISOU  915  CA  GLU A 114     1700   2032   2540     47    -60    155       C  
ATOM    916  C   GLU A 114      25.475 -31.998   6.758  1.00 18.96           C  
ANISOU  916  C   GLU A 114     2013   2302   2890     50    -83    116       C  
ATOM    917  O   GLU A 114      24.819 -32.187   7.791  1.00 18.28           O  
ANISOU  917  O   GLU A 114     1958   2225   2763     56   -102     69       O  
ATOM    918  CB  GLU A 114      24.819 -33.440   4.803  1.00 24.79           C  
ANISOU  918  CB  GLU A 114     2756   3120   3543     56    -19    197       C  
ATOM    919  CG  GLU A 114      23.413 -33.146   5.268  1.00 20.07           C  
ANISOU  919  CG  GLU A 114     2183   2535   2907     68    -17    173       C  
ATOM    920  CD  GLU A 114      22.336 -33.527   4.250  1.00 25.31           C  
ANISOU  920  CD  GLU A 114     2855   3243   3518     75     21    214       C  
ATOM    921  OE1 GLU A 114      21.939 -32.672   3.433  1.00 30.42           O  
ANISOU  921  OE1 GLU A 114     3480   3877   4201     81     45    250       O  
ATOM    922  OE2 GLU A 114      21.859 -34.678   4.296  1.00 18.47           O  
ANISOU  922  OE2 GLU A 114     2019   2425   2574     75     27    210       O  
ATOM    923  N   HIS A 115      25.849 -30.790   6.370  1.00 18.34           N  
ANISOU  923  N   HIS A 115     1902   2177   2888     47    -81    136       N  
ATOM    924  CA  HIS A 115      25.497 -29.610   7.140  1.00 20.92           C  
ANISOU  924  CA  HIS A 115     2232   2459   3256     51   -101    102       C  
ATOM    925  C   HIS A 115      24.212 -29.019   6.579  1.00 16.44           C  
ANISOU  925  C   HIS A 115     1668   1900   2677     67    -71    123       C  
ATOM    926  O   HIS A 115      24.087 -28.840   5.365  1.00 20.12           O  
ANISOU  926  O   HIS A 115     2112   2374   3157     69    -38    175       O  
ATOM    927  CB  HIS A 115      26.632 -28.588   7.052  1.00 24.21           C  
ANISOU  927  CB  HIS A 115     2614   2819   3766     37   -117    112       C  
ATOM    928  CG  HIS A 115      26.359 -27.307   7.776  1.00 25.64           C  
ANISOU  928  CG  HIS A 115     2798   2949   3995     40   -137     80       C  
ATOM    929  ND1 HIS A 115      25.636 -26.276   7.212  1.00 21.34           N  
ANISOU  929  ND1 HIS A 115     2245   2383   3480     51   -115    102       N  
ATOM    930  CD2 HIS A 115      26.727 -26.879   9.007  1.00 24.97           C  
ANISOU  930  CD2 HIS A 115     2727   2828   3933     33   -177     28       C  
ATOM    931  CE1 HIS A 115      25.561 -25.273   8.068  1.00 21.73           C  
ANISOU  931  CE1 HIS A 115     2303   2385   3568     51   -140     65       C  
ATOM    932  NE2 HIS A 115      26.204 -25.617   9.170  1.00 21.36           N  
ANISOU  932  NE2 HIS A 115     2271   2329   3518     40   -178     19       N  
ATOM    933  N   VAL A 116      23.257 -28.731   7.461  1.00 16.11           N  
ANISOU  933  N   VAL A 116     1654   1858   2608     79    -82     82       N  
ATOM    934  CA  VAL A 116      22.003 -28.097   7.069  1.00 18.56           C  
ANISOU  934  CA  VAL A 116     1970   2175   2908     97    -56     98       C  
ATOM    935  C   VAL A 116      21.928 -26.671   7.612  1.00 22.46           C  
ANISOU  935  C   VAL A 116     2460   2611   3465    103    -71     75       C  
ATOM    936  O   VAL A 116      21.982 -26.449   8.819  1.00 26.60           O  
ANISOU  936  O   VAL A 116     3005   3112   3991    103   -104     22       O  
ATOM    937  CB  VAL A 116      20.777 -28.902   7.567  1.00 21.44           C  
ANISOU  937  CB  VAL A 116     2371   2591   3183    110    -51     75       C  
ATOM    938  CG1 VAL A 116      19.478 -28.216   7.149  1.00 22.86           C  
ANISOU  938  CG1 VAL A 116     2553   2780   3353    129    -24     95       C  
ATOM    939  CG2 VAL A 116      20.815 -30.314   7.019  1.00 23.08           C  
ANISOU  939  CG2 VAL A 116     2587   2856   3326    103    -36     97       C  
ATOM    940  N   ASN A 117      21.828 -25.699   6.718  1.00 22.55           N  
ANISOU  940  N   ASN A 117     2445   2596   3529    107    -48    115       N  
ATOM    941  CA  ASN A 117      21.680 -24.314   7.146  1.00 19.94           C  
ANISOU  941  CA  ASN A 117     2112   2208   3256    114    -59     98       C  
ATOM    942  C   ASN A 117      20.259 -24.063   7.631  1.00 24.70           C  
ANISOU  942  C   ASN A 117     2744   2828   3815    138    -50     76       C  
ATOM    943  O   ASN A 117      19.460 -23.442   6.932  1.00 26.34           O  
ANISOU  943  O   ASN A 117     2942   3036   4029    153    -21    109       O  
ATOM    944  CB  ASN A 117      22.031 -23.366   6.001  1.00 28.30           C  
ANISOU  944  CB  ASN A 117     3133   3234   4385    110    -37    150       C  
ATOM    945  CG  ASN A 117      21.966 -21.913   6.414  1.00 36.42           C  
ANISOU  945  CG  ASN A 117     4160   4200   5477    116    -49    133       C  
ATOM    946  OD1 ASN A 117      22.095 -21.589   7.596  1.00 43.08           O  
ANISOU  946  OD1 ASN A 117     5026   5013   6329    116    -82     80       O  
ATOM    947  ND2 ASN A 117      21.762 -21.025   5.444  1.00 41.10           N  
ANISOU  947  ND2 ASN A 117     4729   4772   6115    122    -21    177       N  
ATOM    948  N   ASN A 118      19.935 -24.553   8.825  1.00 20.82           N  
ANISOU  948  N   ASN A 118     2285   2349   3275    143    -75     23       N  
ATOM    949  CA  ASN A 118      18.545 -24.502   9.284  1.00 30.46           C  
ANISOU  949  CA  ASN A 118     3534   3596   4443    167    -65      5       C  
ATOM    950  C   ASN A 118      18.199 -23.254  10.089  1.00 31.03           C  
ANISOU  950  C   ASN A 118     3620   3617   4553    182    -80    -29       C  
ATOM    951  O   ASN A 118      19.075 -22.466  10.452  1.00 30.53           O  
ANISOU  951  O   ASN A 118     3549   3494   4556    171   -104    -47       O  
ATOM    952  CB  ASN A 118      18.182 -25.756  10.090  1.00 23.22           C  
ANISOU  952  CB  ASN A 118     2648   2730   3444    167    -80    -30       C  
ATOM    953  CG  ASN A 118      18.701 -25.700  11.503  1.00 25.83           C  
ANISOU  953  CG  ASN A 118     3001   3030   3782    163   -123    -94       C  
ATOM    954  OD1 ASN A 118      19.862 -25.363  11.731  1.00 26.50           O  
ANISOU  954  OD1 ASN A 118     3074   3072   3924    145   -147   -106       O  
ATOM    955  ND2 ASN A 118      17.838 -26.003  12.468  1.00 26.57           N  
ANISOU  955  ND2 ASN A 118     3128   3147   3819    178   -133   -134       N  
ATOM    956  N   THR A 119      16.904 -23.081  10.346  1.00 25.53           N  
ANISOU  956  N   THR A 119     2945   2943   3814    207    -65    -37       N  
ATOM    957  CA  THR A 119      16.417 -22.084  11.282  1.00 23.06           C  
ANISOU  957  CA  THR A 119     2654   2590   3520    226    -79    -76       C  
ATOM    958  C   THR A 119      15.829 -22.852  12.459  1.00 23.83           C  
ANISOU  958  C   THR A 119     2788   2722   3546    236    -98   -126       C  
ATOM    959  O   THR A 119      14.883 -23.628  12.279  1.00 30.50           O  
ANISOU  959  O   THR A 119     3642   3627   4321    247    -79   -114       O  
ATOM    960  CB  THR A 119      15.299 -21.213  10.648  1.00 37.02           C  
ANISOU  960  CB  THR A 119     4415   4357   5293    253    -43    -43       C  
ATOM    961  OG1 THR A 119      15.808 -20.513   9.502  1.00 31.49           O  
ANISOU  961  OG1 THR A 119     3680   3628   4658    244    -23      7       O  
ATOM    962  CG2 THR A 119      14.760 -20.211  11.660  1.00 34.55           C  
ANISOU  962  CG2 THR A 119     4129   4003   4994    276    -57    -85       C  
ATOM    963  N   ASP A 120      16.379 -22.658  13.655  1.00 23.65           N  
ANISOU  963  N   ASP A 120     2786   2662   3539    231   -137   -182       N  
ATOM    964  CA  ASP A 120      15.913 -23.410  14.820  1.00 26.93           C  
ANISOU  964  CA  ASP A 120     3236   3109   3889    238   -158   -231       C  
ATOM    965  C   ASP A 120      14.393 -23.348  14.945  1.00 26.22           C  
ANISOU  965  C   ASP A 120     3165   3056   3743    270   -134   -229       C  
ATOM    966  O   ASP A 120      13.772 -22.328  14.645  1.00 30.45           O  
ANISOU  966  O   ASP A 120     3696   3568   4304    290   -114   -212       O  
ATOM    967  CB  ASP A 120      16.557 -22.922  16.117  1.00 28.82           C  
ANISOU  967  CB  ASP A 120     3497   3295   4158    234   -201   -292       C  
ATOM    968  CG  ASP A 120      16.245 -23.838  17.296  1.00 33.04           C  
ANISOU  968  CG  ASP A 120     4064   3864   4624    237   -224   -343       C  
ATOM    969  OD1 ASP A 120      16.764 -24.977  17.315  1.00 33.53           O  
ANISOU  969  OD1 ASP A 120     4125   3962   4655    219   -235   -345       O  
ATOM    970  OD2 ASP A 120      15.483 -23.424  18.198  1.00 34.32           O  
ANISOU  970  OD2 ASP A 120     4256   4018   4766    260   -232   -379       O  
ATOM    971  N   PHE A 121      13.797 -24.444  15.399  1.00 24.15           N  
ANISOU  971  N   PHE A 121     2923   2852   3402    273   -136   -245       N  
ATOM    972  CA  PHE A 121      12.345 -24.525  15.436  1.00 21.75           C  
ANISOU  972  CA  PHE A 121     2633   2593   3038    301   -113   -237       C  
ATOM    973  C   PHE A 121      11.775 -23.470  16.378  1.00 23.66           C  
ANISOU  973  C   PHE A 121     2898   2797   3295    328   -122   -274       C  
ATOM    974  O   PHE A 121      10.662 -22.990  16.179  1.00 27.82           O  
ANISOU  974  O   PHE A 121     3428   3339   3804    355    -96   -256       O  
ATOM    975  CB  PHE A 121      11.876 -25.931  15.814  1.00 23.07           C  
ANISOU  975  CB  PHE A 121     2819   2829   3118    297   -117   -249       C  
ATOM    976  CG  PHE A 121      12.101 -26.289  17.254  1.00 25.13           C  
ANISOU  976  CG  PHE A 121     3111   3083   3355    296   -155   -314       C  
ATOM    977  CD1 PHE A 121      11.094 -26.106  18.194  1.00 23.30           C  
ANISOU  977  CD1 PHE A 121     2908   2864   3082    323   -160   -347       C  
ATOM    978  CD2 PHE A 121      13.311 -26.830  17.670  1.00 28.69           C  
ANISOU  978  CD2 PHE A 121     3563   3517   3822    270   -187   -341       C  
ATOM    979  CE1 PHE A 121      11.296 -26.439  19.526  1.00 23.90           C  
ANISOU  979  CE1 PHE A 121     3012   2934   3133    323   -195   -407       C  
ATOM    980  CE2 PHE A 121      13.513 -27.167  19.002  1.00 26.79           C  
ANISOU  980  CE2 PHE A 121     3351   3271   3558    270   -222   -400       C  
ATOM    981  CZ  PHE A 121      12.498 -26.967  19.927  1.00 25.78           C  
ANISOU  981  CZ  PHE A 121     3252   3155   3389    296   -226   -434       C  
ATOM    982  N   LYS A 122      12.555 -23.088  17.383  1.00 30.38           N  
ANISOU  982  N   LYS A 122     3766   3597   4181    321   -159   -325       N  
ATOM    983  CA  LYS A 122      12.132 -22.049  18.319  1.00 32.67           C  
ANISOU  983  CA  LYS A 122     4082   3843   4490    346   -170   -364       C  
ATOM    984  C   LYS A 122      11.921 -20.682  17.664  1.00 41.90           C  
ANISOU  984  C   LYS A 122     5236   4964   5719    362   -147   -334       C  
ATOM    985  O   LYS A 122      11.182 -19.851  18.194  1.00 45.71           O  
ANISOU  985  O   LYS A 122     5740   5424   6202    392   -143   -352       O  
ATOM    986  CB  LYS A 122      13.126 -21.926  19.467  1.00 37.99           C  
ANISOU  986  CB  LYS A 122     4775   4468   5191    331   -216   -423       C  
ATOM    987  CG  LYS A 122      13.076 -23.079  20.447  1.00 44.58           C  
ANISOU  987  CG  LYS A 122     5634   5345   5960    326   -241   -465       C  
ATOM    988  CD  LYS A 122      11.936 -22.923  21.438  1.00 55.39           C  
ANISOU  988  CD  LYS A 122     7038   6729   7279    359   -242   -500       C  
ATOM    989  CE  LYS A 122      12.174 -23.821  22.635  1.00 61.85           C  
ANISOU  989  CE  LYS A 122     7883   7568   8050    350   -276   -554       C  
ATOM    990  NZ  LYS A 122      13.628 -23.838  22.973  1.00 63.05           N  
ANISOU  990  NZ  LYS A 122     8030   7674   8252    319   -313   -580       N  
ATOM    991  N   GLN A 123      12.574 -20.442  16.528  1.00 40.19           N  
ANISOU  991  N   GLN A 123     4986   4732   5554    344   -133   -289       N  
ATOM    992  CA  GLN A 123      12.338 -19.217  15.756  1.00 42.13           C  
ANISOU  992  CA  GLN A 123     5215   4937   5855    358   -107   -253       C  
ATOM    993  C   GLN A 123      11.438 -19.467  14.549  1.00 34.13           C  
ANISOU  993  C   GLN A 123     4178   3978   4812    369    -62   -191       C  
ATOM    994  O   GLN A 123      10.647 -18.611  14.166  1.00 41.66           O  
ANISOU  994  O   GLN A 123     5129   4922   5778    395    -35   -167       O  
ATOM    995  CB  GLN A 123      13.657 -18.592  15.287  1.00 53.75           C  
ANISOU  995  CB  GLN A 123     6663   6348   7411    331   -120   -241       C  
ATOM    996  CG  GLN A 123      13.475 -17.520  14.203  1.00 64.11           C  
ANISOU  996  CG  GLN A 123     7950   7630   8778    340    -89   -191       C  
ATOM    997  CD  GLN A 123      14.786 -16.886  13.747  1.00 71.16           C  
ANISOU  997  CD  GLN A 123     8819   8462   9755    312   -103   -179       C  
ATOM    998  OE1 GLN A 123      15.835 -17.076  14.370  1.00 74.87           O  
ANISOU  998  OE1 GLN A 123     9294   8904  10248    288   -139   -212       O  
ATOM    999  NE2 GLN A 123      14.729 -16.127  12.653  1.00 65.45           N  
ANISOU  999  NE2 GLN A 123     8069   7720   9078    316    -74   -129       N  
ATOM   1000  N   LEU A 124      11.559 -20.650  13.953  1.00 26.63           N  
ANISOU 1000  N   LEU A 124     3213   3085   3821    350    -54   -165       N  
ATOM   1001  CA  LEU A 124      10.862 -20.961  12.710  1.00 22.62           C  
ANISOU 1001  CA  LEU A 124     2680   2626   3287    355    -13   -104       C  
ATOM   1002  C   LEU A 124       9.352 -21.164  12.855  1.00 24.56           C  
ANISOU 1002  C   LEU A 124     2942   2927   3464    384     10    -96       C  
ATOM   1003  O   LEU A 124       8.578 -20.676  12.037  1.00 25.63           O  
ANISOU 1003  O   LEU A 124     3062   3077   3601    401     45    -51       O  
ATOM   1004  CB  LEU A 124      11.475 -22.198  12.058  1.00 22.93           C  
ANISOU 1004  CB  LEU A 124     2704   2708   3301    325    -12    -80       C  
ATOM   1005  CG  LEU A 124      10.905 -22.567  10.690  1.00 25.19           C  
ANISOU 1005  CG  LEU A 124     2965   3044   3563    324     28    -15       C  
ATOM   1006  CD1 LEU A 124      11.267 -21.499   9.679  1.00 25.67           C  
ANISOU 1006  CD1 LEU A 124     2994   3060   3698    323     49     28       C  
ATOM   1007  CD2 LEU A 124      11.437 -23.922  10.244  1.00 27.28           C  
ANISOU 1007  CD2 LEU A 124     3222   3353   3789    296     25      0       C  
ATOM   1008  N   TYR A 125       8.931 -21.888  13.884  1.00 25.83           N  
ANISOU 1008  N   TYR A 125     3131   3120   3562    390     -8   -137       N  
ATOM   1009  CA  TYR A 125       7.527 -22.269  13.993  1.00 24.24           C  
ANISOU 1009  CA  TYR A 125     2942   2981   3288    415     13   -126       C  
ATOM   1010  C   TYR A 125       6.575 -21.076  14.050  1.00 28.43           C  
ANISOU 1010  C   TYR A 125     3477   3491   3835    452     34   -118       C  
ATOM   1011  O   TYR A 125       5.461 -21.146  13.539  1.00 26.99           O  
ANISOU 1011  O   TYR A 125     3286   3357   3611    470     65    -80       O  
ATOM   1012  CB  TYR A 125       7.299 -23.210  15.177  1.00 28.48           C  
ANISOU 1012  CB  TYR A 125     3511   3553   3759    414    -14   -176       C  
ATOM   1013  CG  TYR A 125       7.733 -24.638  14.914  1.00 24.19           C  
ANISOU 1013  CG  TYR A 125     2963   3057   3169    384    -22   -169       C  
ATOM   1014  CD1 TYR A 125       8.639 -24.937  13.905  1.00 29.65           C  
ANISOU 1014  CD1 TYR A 125     3629   3743   3894    356    -16   -135       C  
ATOM   1015  CD2 TYR A 125       7.214 -25.685  15.664  1.00 22.39           C  
ANISOU 1015  CD2 TYR A 125     2759   2883   2865    384    -35   -196       C  
ATOM   1016  CE1 TYR A 125       9.033 -26.246  13.663  1.00 26.87           C  
ANISOU 1016  CE1 TYR A 125     3276   3434   3498    330    -22   -128       C  
ATOM   1017  CE2 TYR A 125       7.593 -26.992  15.431  1.00 22.20           C  
ANISOU 1017  CE2 TYR A 125     2736   2903   2798    357    -42   -189       C  
ATOM   1018  CZ  TYR A 125       8.506 -27.268  14.431  1.00 21.99           C  
ANISOU 1018  CZ  TYR A 125     2684   2867   2804    331    -35   -156       C  
ATOM   1019  OH  TYR A 125       8.884 -28.571  14.196  1.00 26.49           O  
ANISOU 1019  OH  TYR A 125     3256   3478   3329    306    -41   -150       O  
ATOM   1020  N   GLN A 126       7.001 -19.974  14.651  1.00 26.10           N  
ANISOU 1020  N   GLN A 126     3194   3126   3599    463     18   -150       N  
ATOM   1021  CA  GLN A 126       6.097 -18.830  14.741  1.00 33.26           C  
ANISOU 1021  CA  GLN A 126     4108   4011   4520    502     39   -143       C  
ATOM   1022  C   GLN A 126       6.057 -17.980  13.469  1.00 29.17           C  
ANISOU 1022  C   GLN A 126     3557   3471   4054    505     73    -85       C  
ATOM   1023  O   GLN A 126       5.333 -16.989  13.401  1.00 29.39           O  
ANISOU 1023  O   GLN A 126     3588   3481   4098    537     94    -72       O  
ATOM   1024  CB  GLN A 126       6.431 -17.966  15.950  1.00 44.05           C  
ANISOU 1024  CB  GLN A 126     5505   5311   5921    516     11   -202       C  
ATOM   1025  CG  GLN A 126       7.863 -17.509  15.994  1.00 47.35           C  
ANISOU 1025  CG  GLN A 126     5919   5658   6415    488    -17   -221       C  
ATOM   1026  CD  GLN A 126       8.249 -17.032  17.371  1.00 53.71           C  
ANISOU 1026  CD  GLN A 126     6761   6410   7236    494    -54   -288       C  
ATOM   1027  OE1 GLN A 126       7.478 -17.178  18.322  1.00 58.27           O  
ANISOU 1027  OE1 GLN A 126     7368   7008   7764    519    -60   -322       O  
ATOM   1028  NE2 GLN A 126       9.439 -16.455  17.492  1.00 49.81           N  
ANISOU 1028  NE2 GLN A 126     6266   5849   6813    472    -80   -307       N  
ATOM   1029  N   THR A 127       6.831 -18.369  12.462  1.00 30.64           N  
ANISOU 1029  N   THR A 127     3714   3662   4267    474     78    -50       N  
ATOM   1030  CA  THR A 127       6.793 -17.687  11.174  1.00 34.89           C  
ANISOU 1030  CA  THR A 127     4219   4188   4850    475    111      9       C  
ATOM   1031  C   THR A 127       6.149 -18.541  10.069  1.00 33.67           C  
ANISOU 1031  C   THR A 127     4041   4108   4645    469    143     67       C  
ATOM   1032  O   THR A 127       5.854 -18.034   8.989  1.00 36.13           O  
ANISOU 1032  O   THR A 127     4326   4421   4981    474    175    119       O  
ATOM   1033  CB  THR A 127       8.199 -17.225  10.733  1.00 41.61           C  
ANISOU 1033  CB  THR A 127     5051   4975   5782    447     96     13       C  
ATOM   1034  OG1 THR A 127       8.992 -18.360  10.359  1.00 44.49           O  
ANISOU 1034  OG1 THR A 127     5402   5370   6131    412     85     20       O  
ATOM   1035  CG2 THR A 127       8.889 -16.482  11.867  1.00 40.35           C  
ANISOU 1035  CG2 THR A 127     4917   4744   5669    448     60    -46       C  
ATOM   1036  N   LEU A 128       5.910 -19.824  10.341  1.00 27.96           N  
ANISOU 1036  N   LEU A 128     3328   3446   3851    456    134     57       N  
ATOM   1037  CA  LEU A 128       5.367 -20.718   9.316  1.00 25.47           C  
ANISOU 1037  CA  LEU A 128     2993   3201   3484    445    161    109       C  
ATOM   1038  C   LEU A 128       3.936 -20.357   8.941  1.00 23.54           C  
ANISOU 1038  C   LEU A 128     2744   2998   3204    476    197    147       C  
ATOM   1039  O   LEU A 128       3.091 -20.105   9.799  1.00 18.72           O  
ANISOU 1039  O   LEU A 128     2154   2396   2561    504    195    121       O  
ATOM   1040  CB  LEU A 128       5.424 -22.184   9.746  1.00 25.58           C  
ANISOU 1040  CB  LEU A 128     3023   3270   3427    424    143     89       C  
ATOM   1041  CG  LEU A 128       6.786 -22.867   9.916  1.00 27.72           C  
ANISOU 1041  CG  LEU A 128     3295   3520   3718    390    113     63       C  
ATOM   1042  CD1 LEU A 128       6.568 -24.314  10.316  1.00 31.40           C  
ANISOU 1042  CD1 LEU A 128     3780   4048   4103    376    100     48       C  
ATOM   1043  CD2 LEU A 128       7.636 -22.779   8.646  1.00 22.75           C  
ANISOU 1043  CD2 LEU A 128     2632   2872   3139    367    128    109       C  
ATOM   1044  N   THR A 129       3.672 -20.329   7.642  1.00 20.65           N  
ANISOU 1044  N   THR A 129     2348   2656   2843    470    229    209       N  
ATOM   1045  CA  THR A 129       2.322 -20.082   7.171  1.00 19.47           C  
ANISOU 1045  CA  THR A 129     2190   2553   2656    496    264    251       C  
ATOM   1046  C   THR A 129       1.583 -21.408   7.075  1.00 14.21           C  
ANISOU 1046  C   THR A 129     1528   1971   1898    484    269    266       C  
ATOM   1047  O   THR A 129       2.178 -22.475   7.260  1.00 21.10           O  
ANISOU 1047  O   THR A 129     2411   2863   2742    456    247    247       O  
ATOM   1048  CB  THR A 129       2.327 -19.442   5.779  1.00 19.10           C  
ANISOU 1048  CB  THR A 129     2107   2496   2654    494    297    314       C  
ATOM   1049  OG1 THR A 129       2.928 -20.354   4.863  1.00 18.37           O  
ANISOU 1049  OG1 THR A 129     1997   2430   2551    459    301    344       O  
ATOM   1050  CG2 THR A 129       3.098 -18.121   5.779  1.00 18.42           C  
ANISOU 1050  CG2 THR A 129     2014   2324   2661    503    293    303       C  
ATOM   1051  N   ASP A 130       0.280 -21.333   6.805  1.00 15.32           N  
ANISOU 1051  N   ASP A 130     1665   2164   1993    506    296    301       N  
ATOM   1052  CA  ASP A 130      -0.526 -22.526   6.555  1.00 15.53           C  
ANISOU 1052  CA  ASP A 130     1693   2275   1933    494    305    326       C  
ATOM   1053  C   ASP A 130       0.128 -23.367   5.463  1.00 19.62           C  
ANISOU 1053  C   ASP A 130     2195   2814   2448    455    310    361       C  
ATOM   1054  O   ASP A 130       0.277 -24.588   5.598  1.00 17.26           O  
ANISOU 1054  O   ASP A 130     1909   2555   2094    431    295    351       O  
ATOM   1055  CB  ASP A 130      -1.955 -22.139   6.156  1.00 18.05           C  
ANISOU 1055  CB  ASP A 130     2000   2641   2216    522    339    371       C  
ATOM   1056  CG  ASP A 130      -2.829 -23.349   5.827  1.00 28.92           C  
ANISOU 1056  CG  ASP A 130     3379   4108   3503    507    348    402       C  
ATOM   1057  OD1 ASP A 130      -2.609 -24.435   6.409  1.00 22.80           O  
ANISOU 1057  OD1 ASP A 130     2624   3359   2678    486    323    371       O  
ATOM   1058  OD2 ASP A 130      -3.757 -23.205   4.997  1.00 27.70           O  
ANISOU 1058  OD2 ASP A 130     3204   3997   3325    515    380    458       O  
ATOM   1059  N   TYR A 131       0.535 -22.713   4.382  1.00 14.64           N  
ANISOU 1059  N   TYR A 131     1535   2153   1875    451    331    402       N  
ATOM   1060  CA  TYR A 131       1.156 -23.441   3.282  1.00 13.86           C  
ANISOU 1060  CA  TYR A 131     1419   2071   1775    417    339    439       C  
ATOM   1061  C   TYR A 131       2.455 -24.118   3.740  1.00 15.86           C  
ANISOU 1061  C   TYR A 131     1687   2297   2044    390    306    396       C  
ATOM   1062  O   TYR A 131       2.677 -25.311   3.472  1.00 14.57           O  
ANISOU 1062  O   TYR A 131     1531   2174   1833    363    300    403       O  
ATOM   1063  CB  TYR A 131       1.384 -22.536   2.071  1.00 15.37           C  
ANISOU 1063  CB  TYR A 131     1576   2233   2031    419    368    490       C  
ATOM   1064  CG  TYR A 131       1.843 -23.309   0.861  1.00 21.42           C  
ANISOU 1064  CG  TYR A 131     2325   3026   2787    387    380    534       C  
ATOM   1065  CD1 TYR A 131       0.934 -23.957   0.044  1.00 19.87           C  
ANISOU 1065  CD1 TYR A 131     2122   2900   2529    379    405    584       C  
ATOM   1066  CD2 TYR A 131       3.200 -23.422   0.557  1.00 22.65           C  
ANISOU 1066  CD2 TYR A 131     2474   3139   2995    363    367    526       C  
ATOM   1067  CE1 TYR A 131       1.356 -24.680  -1.065  1.00 24.62           C  
ANISOU 1067  CE1 TYR A 131     2710   3524   3119    350    417    624       C  
ATOM   1068  CE2 TYR A 131       3.631 -24.146  -0.538  1.00 26.18           C  
ANISOU 1068  CE2 TYR A 131     2906   3610   3430    336    380    566       C  
ATOM   1069  CZ  TYR A 131       2.704 -24.773  -1.345  1.00 28.95           C  
ANISOU 1069  CZ  TYR A 131     3253   4029   3719    329    405    615       C  
ATOM   1070  OH  TYR A 131       3.120 -25.493  -2.437  1.00 28.68           O  
ANISOU 1070  OH  TYR A 131     3208   4017   3672    303    418    654       O  
ATOM   1071  N   ASP A 132       3.310 -23.369   4.433  1.00 15.64           N  
ANISOU 1071  N   ASP A 132     1664   2199   2080    396    284    353       N  
ATOM   1072  CA  ASP A 132       4.568 -23.953   4.912  1.00 16.36           C  
ANISOU 1072  CA  ASP A 132     1766   2261   2188    371    251    313       C  
ATOM   1073  C   ASP A 132       4.327 -25.233   5.736  1.00 16.52           C  
ANISOU 1073  C   ASP A 132     1817   2331   2130    361    229    278       C  
ATOM   1074  O   ASP A 132       5.054 -26.225   5.588  1.00 17.77           O  
ANISOU 1074  O   ASP A 132     1980   2503   2270    333    216    274       O  
ATOM   1075  CB  ASP A 132       5.359 -22.964   5.774  1.00 16.16           C  
ANISOU 1075  CB  ASP A 132     1747   2158   2234    382    226    265       C  
ATOM   1076  CG  ASP A 132       5.853 -21.751   5.005  1.00 24.34           C  
ANISOU 1076  CG  ASP A 132     2756   3137   3356    387    242    294       C  
ATOM   1077  OD1 ASP A 132       6.131 -21.847   3.786  1.00 19.87           O  
ANISOU 1077  OD1 ASP A 132     2163   2580   2808    371    264    344       O  
ATOM   1078  OD2 ASP A 132       5.980 -20.686   5.651  1.00 32.84           O  
ANISOU 1078  OD2 ASP A 132     3839   4157   4482    406    232    265       O  
ATOM   1079  N   ILE A 133       3.324 -25.208   6.613  1.00 15.85           N  
ANISOU 1079  N   ILE A 133     1752   2272   1998    383    225    255       N  
ATOM   1080  CA  ILE A 133       3.093 -26.341   7.508  1.00 15.83           C  
ANISOU 1080  CA  ILE A 133     1778   2312   1923    375    202    218       C  
ATOM   1081  C   ILE A 133       2.749 -27.580   6.693  1.00 18.20           C  
ANISOU 1081  C   ILE A 133     2077   2682   2156    351    216    258       C  
ATOM   1082  O   ILE A 133       3.313 -28.648   6.906  1.00 16.34           O  
ANISOU 1082  O   ILE A 133     1858   2463   1889    327    197    239       O  
ATOM   1083  CB  ILE A 133       1.996 -26.064   8.554  1.00 18.98           C  
ANISOU 1083  CB  ILE A 133     2199   2731   2283    406    198    190       C  
ATOM   1084  CG1 ILE A 133       2.408 -24.933   9.494  1.00 19.17           C  
ANISOU 1084  CG1 ILE A 133     2232   2684   2368    428    180    143       C  
ATOM   1085  CG2 ILE A 133       1.692 -27.329   9.374  1.00 19.15           C  
ANISOU 1085  CG2 ILE A 133     2249   2805   2223    395    176    159       C  
ATOM   1086  CD1 ILE A 133       1.238 -24.411  10.344  1.00 19.40           C  
ANISOU 1086  CD1 ILE A 133     2278   2728   2367    466    184    126       C  
ATOM   1087  N   ARG A 134       1.842 -27.434   5.733  1.00 18.06           N  
ANISOU 1087  N   ARG A 134     2042   2703   2118    356    249    315       N  
ATOM   1088  CA  ARG A 134       1.459 -28.566   4.900  1.00 19.42           C  
ANISOU 1088  CA  ARG A 134     2213   2940   2225    332    263    356       C  
ATOM   1089  C   ARG A 134       2.666 -29.056   4.105  1.00 14.78           C  
ANISOU 1089  C   ARG A 134     1616   2332   1666    302    261    370       C  
ATOM   1090  O   ARG A 134       2.908 -30.260   3.988  1.00 13.62           O  
ANISOU 1090  O   ARG A 134     1486   2221   1470    277    252    369       O  
ATOM   1091  CB  ARG A 134       0.338 -28.158   3.955  1.00 18.51           C  
ANISOU 1091  CB  ARG A 134     2077   2864   2092    343    300    417       C  
ATOM   1092  CG  ARG A 134      -0.812 -27.440   4.653  1.00 11.47           C  
ANISOU 1092  CG  ARG A 134     1189   1985   1185    379    307    409       C  
ATOM   1093  CD  ARG A 134      -2.009 -27.410   3.747  1.00 17.63           C  
ANISOU 1093  CD  ARG A 134     1951   2823   1925    384    341    471       C  
ATOM   1094  NE  ARG A 134      -3.040 -26.491   4.228  1.00 14.71           N  
ANISOU 1094  NE  ARG A 134     1578   2457   1555    422    353    473       N  
ATOM   1095  CZ  ARG A 134      -4.331 -26.635   3.950  1.00 19.25           C  
ANISOU 1095  CZ  ARG A 134     2146   3096   2072    432    375    512       C  
ATOM   1096  NH1 ARG A 134      -4.736 -27.673   3.227  1.00 18.04           N  
ANISOU 1096  NH1 ARG A 134     1992   3006   1856    404    383    551       N  
ATOM   1097  NH2 ARG A 134      -5.207 -25.754   4.404  1.00 16.76           N  
ANISOU 1097  NH2 ARG A 134     1827   2781   1761    470    387    513       N  
ATOM   1098  N   PHE A 135       3.409 -28.112   3.540  1.00 17.70           N  
ANISOU 1098  N   PHE A 135     1962   2647   2118    305    270    384       N  
ATOM   1099  CA  PHE A 135       4.584 -28.444   2.737  1.00 14.43           C  
ANISOU 1099  CA  PHE A 135     1534   2210   1739    280    270    401       C  
ATOM   1100  C   PHE A 135       5.599 -29.274   3.531  1.00 13.48           C  
ANISOU 1100  C   PHE A 135     1436   2075   1612    262    236    352       C  
ATOM   1101  O   PHE A 135       6.045 -30.343   3.091  1.00 17.50           O  
ANISOU 1101  O   PHE A 135     1952   2610   2086    238    234    363       O  
ATOM   1102  CB  PHE A 135       5.235 -27.171   2.205  1.00 13.99           C  
ANISOU 1102  CB  PHE A 135     1449   2090   1778    289    281    417       C  
ATOM   1103  CG  PHE A 135       6.443 -27.427   1.347  1.00 23.47           C  
ANISOU 1103  CG  PHE A 135     2632   3267   3019    265    283    439       C  
ATOM   1104  CD1 PHE A 135       6.326 -27.524  -0.034  1.00 21.84           C  
ANISOU 1104  CD1 PHE A 135     2404   3083   2812    255    314    500       C  
ATOM   1105  CD2 PHE A 135       7.700 -27.584   1.925  1.00 22.43           C  
ANISOU 1105  CD2 PHE A 135     2507   3092   2924    253    254    398       C  
ATOM   1106  CE1 PHE A 135       7.454 -27.765  -0.823  1.00 20.28           C  
ANISOU 1106  CE1 PHE A 135     2191   2864   2652    235    317    520       C  
ATOM   1107  CE2 PHE A 135       8.813 -27.823   1.146  1.00 23.94           C  
ANISOU 1107  CE2 PHE A 135     2681   3264   3152    233    257    420       C  
ATOM   1108  CZ  PHE A 135       8.690 -27.914  -0.229  1.00 22.75           C  
ANISOU 1108  CZ  PHE A 135     2508   3134   3000    225    289    481       C  
ATOM   1109  N   TYR A 136       5.956 -28.785   4.710  1.00 13.25           N  
ANISOU 1109  N   TYR A 136     1419   2004   1612    275    209    297       N  
ATOM   1110  CA  TYR A 136       6.996 -29.432   5.496  1.00 14.94           C  
ANISOU 1110  CA  TYR A 136     1651   2197   1828    259    175    249       C  
ATOM   1111  C   TYR A 136       6.495 -30.735   6.113  1.00 15.14           C  
ANISOU 1111  C   TYR A 136     1708   2281   1764    250    161    227       C  
ATOM   1112  O   TYR A 136       7.247 -31.697   6.250  1.00 17.40           O  
ANISOU 1112  O   TYR A 136     2008   2575   2030    230    144    211       O  
ATOM   1113  CB  TYR A 136       7.576 -28.465   6.538  1.00 17.09           C  
ANISOU 1113  CB  TYR A 136     1926   2404   2163    274    149    198       C  
ATOM   1114  CG  TYR A 136       8.453 -27.364   5.957  1.00 16.63           C  
ANISOU 1114  CG  TYR A 136     1838   2281   2198    274    155    214       C  
ATOM   1115  CD1 TYR A 136       9.543 -27.667   5.139  1.00 19.48           C  
ANISOU 1115  CD1 TYR A 136     2180   2626   2593    251    158    238       C  
ATOM   1116  CD2 TYR A 136       8.193 -26.026   6.226  1.00 18.56           C  
ANISOU 1116  CD2 TYR A 136     2075   2481   2497    297    159    207       C  
ATOM   1117  CE1 TYR A 136      10.350 -26.666   4.622  1.00 21.51           C  
ANISOU 1117  CE1 TYR A 136     2411   2827   2936    250    162    255       C  
ATOM   1118  CE2 TYR A 136       8.990 -25.014   5.703  1.00 16.97           C  
ANISOU 1118  CE2 TYR A 136     1848   2220   2381    296    163    222       C  
ATOM   1119  CZ  TYR A 136      10.065 -25.337   4.903  1.00 14.72           C  
ANISOU 1119  CZ  TYR A 136     1543   1922   2128    272    165    247       C  
ATOM   1120  OH  TYR A 136      10.874 -24.355   4.378  1.00 22.04           O  
ANISOU 1120  OH  TYR A 136     2443   2791   3139    269    169    264       O  
ATOM   1121  N   MET A 137       5.215 -30.781   6.477  1.00 16.57           N  
ANISOU 1121  N   MET A 137     1901   2505   1890    266    168    228       N  
ATOM   1122  CA AMET A 137       4.618 -32.029   6.940  1.00 15.26           C  
ANISOU 1122  CA AMET A 137     1765   2401   1635    256    158    215       C  
ATOM   1123  CA BMET A 137       4.612 -32.026   6.941  0.00 15.30           C  
ANISOU 1123  CA BMET A 137     1769   2405   1639    256    158    215       C  
ATOM   1124  C   MET A 137       4.739 -33.107   5.868  1.00 15.98           C  
ANISOU 1124  C   MET A 137     1855   2533   1682    228    174    258       C  
ATOM   1125  O   MET A 137       5.108 -34.241   6.155  1.00 16.30           O  
ANISOU 1125  O   MET A 137     1919   2597   1678    209    157    239       O  
ATOM   1126  CB AMET A 137       3.148 -31.814   7.328  1.00 13.48           C  
ANISOU 1126  CB AMET A 137     1547   2218   1359    277    169    220       C  
ATOM   1127  CB BMET A 137       3.143 -31.811   7.320  0.00 14.47           C  
ANISOU 1127  CB BMET A 137     1671   2343   1484    277    169    221       C  
ATOM   1128  CG AMET A 137       2.971 -31.251   8.723  1.00 14.23           C  
ANISOU 1128  CG AMET A 137     1657   2286   1464    302    146    164       C  
ATOM   1129  CG BMET A 137       2.937 -31.528   8.800  0.00 14.00           C  
ANISOU 1129  CG BMET A 137     1633   2268   1420    298    143    161       C  
ATOM   1130  SD AMET A 137       3.362 -32.472  10.003  1.00 20.34           S  
ANISOU 1130  SD AMET A 137     2468   3077   2182    287    106    102       S  
ATOM   1131  SD BMET A 137       3.329 -32.976   9.799  0.00 21.63           S  
ANISOU 1131  SD BMET A 137     2635   3261   2321    277    107    111       S  
ATOM   1132  CE AMET A 137       1.836 -33.425  10.069  1.00 46.14           C  
ANISOU 1132  CE AMET A 137     5753   6435   5341    287    117    123       C  
ATOM   1133  CE BMET A 137       3.564 -32.239  11.415  0.00 20.62           C  
ANISOU 1133  CE BMET A 137     2524   3084   2225    302     75     39       C  
ATOM   1134  N   TYR A 138       4.445 -32.743   4.627  1.00 12.97           N  
ANISOU 1134  N   TYR A 138     1449   2162   1316    226    206    316       N  
ATOM   1135  CA  TYR A 138       4.554 -33.690   3.530  1.00 11.88           C  
ANISOU 1135  CA  TYR A 138     1311   2061   1140    201    222    360       C  
ATOM   1136  C   TYR A 138       6.006 -34.147   3.401  1.00 11.80           C  
ANISOU 1136  C   TYR A 138     1303   2016   1164    183    208    345       C  
ATOM   1137  O   TYR A 138       6.280 -35.316   3.161  1.00 15.91           O  
ANISOU 1137  O   TYR A 138     1842   2567   1635    162    204    350       O  
ATOM   1138  CB  TYR A 138       4.108 -33.040   2.234  1.00 15.92           C  
ANISOU 1138  CB  TYR A 138     1793   2579   1675    204    258    422       C  
ATOM   1139  CG  TYR A 138       3.774 -34.023   1.140  1.00 17.92           C  
ANISOU 1139  CG  TYR A 138     2052   2887   1870    181    278    472       C  
ATOM   1140  CD1 TYR A 138       2.588 -34.748   1.169  1.00 16.94           C  
ANISOU 1140  CD1 TYR A 138     1946   2830   1660    175    284    488       C  
ATOM   1141  CD2 TYR A 138       4.631 -34.205   0.068  1.00 22.10           C  
ANISOU 1141  CD2 TYR A 138     2567   3400   2429    164    292    505       C  
ATOM   1142  CE1 TYR A 138       2.277 -35.645   0.158  1.00 21.08           C  
ANISOU 1142  CE1 TYR A 138     2477   3403   2129    151    302    534       C  
ATOM   1143  CE2 TYR A 138       4.334 -35.086  -0.939  1.00 27.38           C  
ANISOU 1143  CE2 TYR A 138     3244   4116   3043    143    311    550       C  
ATOM   1144  CZ  TYR A 138       3.160 -35.807  -0.894  1.00 19.30           C  
ANISOU 1144  CZ  TYR A 138     2241   3158   1935    136    315    564       C  
ATOM   1145  OH  TYR A 138       2.881 -36.684  -1.920  1.00 22.96           O  
ANISOU 1145  OH  TYR A 138     2714   3667   2344    112    333    609       O  
ATOM   1146  N   GLU A 139       6.937 -33.223   3.573  1.00 14.75           N  
ANISOU 1146  N   GLU A 139     1658   2326   1621    191    199    327       N  
ATOM   1147  CA  GLU A 139       8.349 -33.573   3.478  1.00 16.15           C  
ANISOU 1147  CA  GLU A 139     1832   2469   1836    175    185    314       C  
ATOM   1148  C   GLU A 139       8.779 -34.534   4.591  1.00 13.10           C  
ANISOU 1148  C   GLU A 139     1478   2090   1409    167    152    261       C  
ATOM   1149  O   GLU A 139       9.571 -35.448   4.356  1.00 13.07           O  
ANISOU 1149  O   GLU A 139     1484   2093   1390    148    145    262       O  
ATOM   1150  CB  GLU A 139       9.216 -32.311   3.454  1.00 14.66           C  
ANISOU 1150  CB  GLU A 139     1615   2210   1747    185    182    308       C  
ATOM   1151  CG  GLU A 139       8.999 -31.461   2.196  1.00 13.28           C  
ANISOU 1151  CG  GLU A 139     1407   2024   1615    190    216    366       C  
ATOM   1152  CD  GLU A 139       9.424 -32.176   0.931  1.00 20.95           C  
ANISOU 1152  CD  GLU A 139     2369   3018   2573    170    237    415       C  
ATOM   1153  OE1 GLU A 139      10.524 -32.754   0.908  1.00 22.45           O  
ANISOU 1153  OE1 GLU A 139     2562   3192   2774    155    224    404       O  
ATOM   1154  OE2 GLU A 139       8.672 -32.160  -0.053  1.00 20.40           O  
ANISOU 1154  OE2 GLU A 139     2289   2981   2480    170    267    465       O  
ATOM   1155  N   ILE A 140       8.270 -34.331   5.806  1.00 12.25           N  
ANISOU 1155  N   ILE A 140     1393   1793   1470   -117     97      1       N  
ATOM   1156  CA  ILE A 140       8.551 -35.271   6.901  1.00 14.01           C  
ANISOU 1156  CA  ILE A 140     1643   1958   1720   -108     82    -41       C  
ATOM   1157  C   ILE A 140       7.971 -36.656   6.577  1.00 17.14           C  
ANISOU 1157  C   ILE A 140     2045   2381   2089   -128     89    -81       C  
ATOM   1158  O   ILE A 140       8.593 -37.693   6.817  1.00 12.90           O  
ANISOU 1158  O   ILE A 140     1515   1814   1571   -130     92   -126       O  
ATOM   1159  CB  ILE A 140       7.958 -34.780   8.242  1.00 13.59           C  
ANISOU 1159  CB  ILE A 140     1618   1858   1687    -85     62    -20       C  
ATOM   1160  CG1 ILE A 140       8.579 -33.438   8.639  1.00 18.92           C  
ANISOU 1160  CG1 ILE A 140     2293   2500   2394    -68     55     12       C  
ATOM   1161  CG2 ILE A 140       8.198 -35.806   9.345  1.00 14.03           C  
ANISOU 1161  CG2 ILE A 140     1702   1863   1767    -76     47    -59       C  
ATOM   1162  CD1 ILE A 140       7.880 -32.761   9.816  1.00 13.79           C  
ANISOU 1162  CD1 ILE A 140     1674   1811   1757    -47     41     36       C  
ATOM   1163  N   LEU A 141       6.765 -36.666   6.025  1.00 13.18           N  
ANISOU 1163  N   LEU A 141     1536   1930   1542   -143     91    -63       N  
ATOM   1164  CA  LEU A 141       6.122 -37.916   5.672  1.00 11.84           C  
ANISOU 1164  CA  LEU A 141     1370   1787   1343   -166     95   -101       C  
ATOM   1165  C   LEU A 141       6.939 -38.706   4.646  1.00 12.40           C  
ANISOU 1165  C   LEU A 141     1429   1882   1401   -189    118   -146       C  
ATOM   1166  O   LEU A 141       6.977 -39.930   4.705  1.00 14.53           O  
ANISOU 1166  O   LEU A 141     1708   2138   1674   -201    124   -195       O  
ATOM   1167  CB  LEU A 141       4.708 -37.647   5.158  1.00 12.23           C  
ANISOU 1167  CB  LEU A 141     1407   1893   1345   -182     92    -65       C  
ATOM   1168  CG  LEU A 141       3.670 -37.372   6.248  1.00 16.86           C  
ANISOU 1168  CG  LEU A 141     2010   2451   1944   -162     75    -33       C  
ATOM   1169  CD1 LEU A 141       2.324 -36.944   5.621  1.00 13.42           C  
ANISOU 1169  CD1 LEU A 141     1555   2078   1467   -178     73     14       C  
ATOM   1170  CD2 LEU A 141       3.480 -38.596   7.132  1.00 16.36           C  
ANISOU 1170  CD2 LEU A 141     1971   2345   1900   -159     67    -75       C  
ATOM   1171  N   LYS A 142       7.602 -38.016   3.718  1.00 17.86           N  
ANISOU 1171  N   LYS A 142     2098   2606   2080   -194    133   -131       N  
ATOM   1172  CA  LYS A 142       8.466 -38.709   2.757  1.00 13.81           C  
ANISOU 1172  CA  LYS A 142     1575   2114   1556   -213    160   -174       C  
ATOM   1173  C   LYS A 142       9.566 -39.452   3.502  1.00 20.53           C  
ANISOU 1173  C   LYS A 142     2440   2897   2466   -197    165   -213       C  
ATOM   1174  O   LYS A 142       9.814 -40.631   3.254  1.00 16.81           O  
ANISOU 1174  O   LYS A 142     1974   2418   1995   -210    182   -265       O  
ATOM   1175  CB  LYS A 142       9.093 -37.735   1.760  1.00 18.22           C  
ANISOU 1175  CB  LYS A 142     2108   2714   2099   -215    177   -142       C  
ATOM   1176  CG  LYS A 142       8.122 -37.187   0.729  1.00 24.39           C  
ANISOU 1176  CG  LYS A 142     2872   3578   2817   -237    178   -106       C  
ATOM   1177  CD  LYS A 142       8.860 -36.236  -0.209  1.00 26.64           C  
ANISOU 1177  CD  LYS A 142     3129   3899   3092   -236    198    -72       C  
ATOM   1178  CE  LYS A 142       7.892 -35.483  -1.100  1.00 28.97           C  
ANISOU 1178  CE  LYS A 142     3403   4275   3331   -253    195    -20       C  
ATOM   1179  NZ  LYS A 142       8.615 -34.486  -1.930  1.00 31.54           N  
ANISOU 1179  NZ  LYS A 142     3700   4633   3653   -247    215     21       N  
ATOM   1180  N   ALA A 143      10.214 -38.750   4.426  1.00 13.04           N  
ANISOU 1180  N   ALA A 143     1493   1895   1566   -169    149   -188       N  
ATOM   1181  CA  ALA A 143      11.256 -39.342   5.252  1.00 13.66           C  
ANISOU 1181  CA  ALA A 143     1580   1908   1703   -152    147   -215       C  
ATOM   1182  C   ALA A 143      10.717 -40.512   6.079  1.00 14.94           C  
ANISOU 1182  C   ALA A 143     1763   2037   1875   -152    137   -248       C  
ATOM   1183  O   ALA A 143      11.360 -41.556   6.172  1.00 10.45           O  
ANISOU 1183  O   ALA A 143     1196   1439   1335   -153    152   -287       O  
ATOM   1184  CB  ALA A 143      11.864 -38.281   6.165  1.00 11.33           C  
ANISOU 1184  CB  ALA A 143     1286   1568   1451   -127    124   -177       C  
ATOM   1185  N   LEU A 144       9.536 -40.350   6.681  1.00 12.32           N  
ANISOU 1185  N   LEU A 144     1448   1709   1525   -149    116   -228       N  
ATOM   1186  CA  LEU A 144       8.990 -41.416   7.518  1.00 11.38           C  
ANISOU 1186  CA  LEU A 144     1349   1558   1419   -146    107   -254       C  
ATOM   1187  C   LEU A 144       8.525 -42.629   6.704  1.00 16.13           C  
ANISOU 1187  C   LEU A 144     1946   2189   1993   -175    129   -298       C  
ATOM   1188  O   LEU A 144       8.819 -43.773   7.056  1.00 14.52           O  
ANISOU 1188  O   LEU A 144     1749   1949   1818   -175    138   -337       O  
ATOM   1189  CB  LEU A 144       7.879 -40.906   8.440  1.00 10.75           C  
ANISOU 1189  CB  LEU A 144     1286   1469   1329   -132     82   -218       C  
ATOM   1190  CG  LEU A 144       8.342 -39.991   9.582  1.00 11.83           C  
ANISOU 1190  CG  LEU A 144     1437   1559   1500   -103     60   -188       C  
ATOM   1191  CD1 LEU A 144       7.128 -39.512  10.385  1.00 14.17           C  
ANISOU 1191  CD1 LEU A 144     1754   1851   1781    -90     43   -155       C  
ATOM   1192  CD2 LEU A 144       9.362 -40.705  10.486  1.00 13.43           C  
ANISOU 1192  CD2 LEU A 144     1648   1702   1752    -88     52   -212       C  
ATOM   1193  N   ASP A 145       7.819 -42.406   5.606  1.00 13.85           N  
ANISOU 1193  N   ASP A 145     1647   1966   1650   -201    138   -294       N  
ATOM   1194  CA  ASP A 145       7.465 -43.553   4.785  1.00 18.17           C  
ANISOU 1194  CA  ASP A 145     2193   2541   2168   -233    158   -343       C  
ATOM   1195  C   ASP A 145       8.721 -44.283   4.316  1.00 19.38           C  
ANISOU 1195  C   ASP A 145     2343   2673   2349   -237    190   -390       C  
ATOM   1196  O   ASP A 145       8.752 -45.516   4.275  1.00 15.27           O  
ANISOU 1196  O   ASP A 145     1829   2132   1842   -249    208   -439       O  
ATOM   1197  CB  ASP A 145       6.656 -43.160   3.568  1.00 15.59           C  
ANISOU 1197  CB  ASP A 145     1854   2295   1774   -264    161   -331       C  
ATOM   1198  CG  ASP A 145       6.184 -44.376   2.800  1.00 27.73           C  
ANISOU 1198  CG  ASP A 145     3396   3861   3280   -303    177   -386       C  
ATOM   1199  OD1 ASP A 145       5.660 -45.311   3.449  1.00 22.16           O  
ANISOU 1199  OD1 ASP A 145     2703   3122   2595   -305    171   -410       O  
ATOM   1200  OD2 ASP A 145       6.373 -44.413   1.570  1.00 27.69           O  
ANISOU 1200  OD2 ASP A 145     3382   3909   3230   -330    198   -406       O  
ATOM   1201  N   TYR A 146       9.754 -43.528   3.944  1.00 16.75           N  
ANISOU 1201  N   TYR A 146     1996   2343   2027   -226    201   -373       N  
ATOM   1202  CA  TYR A 146      10.993 -44.173   3.526  1.00 15.93           C  
ANISOU 1202  CA  TYR A 146     1885   2215   1954   -225    236   -411       C  
ATOM   1203  C   TYR A 146      11.571 -45.081   4.617  1.00 15.23           C  
ANISOU 1203  C   TYR A 146     1804   2051   1933   -205    235   -433       C  
ATOM   1204  O   TYR A 146      11.769 -46.276   4.388  1.00 15.96           O  
ANISOU 1204  O   TYR A 146     1899   2125   2040   -217    263   -482       O  
ATOM   1205  CB  TYR A 146      12.038 -43.165   3.034  1.00 13.74           C  
ANISOU 1205  CB  TYR A 146     1587   1948   1685   -213    247   -382       C  
ATOM   1206  CG  TYR A 146      13.252 -43.866   2.464  1.00 13.07           C  
ANISOU 1206  CG  TYR A 146     1492   1844   1628   -215    289   -421       C  
ATOM   1207  CD1 TYR A 146      13.171 -44.535   1.243  1.00 19.16           C  
ANISOU 1207  CD1 TYR A 146     2265   2659   2356   -244    327   -465       C  
ATOM   1208  CD2 TYR A 146      14.465 -43.884   3.144  1.00 14.64           C  
ANISOU 1208  CD2 TYR A 146     1681   1983   1897   -188    291   -413       C  
ATOM   1209  CE1 TYR A 146      14.263 -45.194   0.711  1.00 21.98           C  
ANISOU 1209  CE1 TYR A 146     2615   2996   2740   -243    373   -501       C  
ATOM   1210  CE2 TYR A 146      15.573 -44.544   2.610  1.00 18.44           C  
ANISOU 1210  CE2 TYR A 146     2151   2445   2411   -187    334   -443       C  
ATOM   1211  CZ  TYR A 146      15.457 -45.195   1.390  1.00 22.28           C  
ANISOU 1211  CZ  TYR A 146     2641   2972   2854   -214    378   -488       C  
ATOM   1212  OH  TYR A 146      16.522 -45.857   0.828  1.00 22.86           O  
ANISOU 1212  OH  TYR A 146     2704   3025   2958   -212    428   -521       O  
ATOM   1213  N   CYS A 147      11.832 -44.546   5.808  1.00 16.57           N  
ANISOU 1213  N   CYS A 147     1977   2177   2144   -176    204   -397       N  
ATOM   1214  CA  CYS A 147      12.454 -45.388   6.826  1.00 15.40           C  
ANISOU 1214  CA  CYS A 147     1832   1961   2058   -157    202   -411       C  
ATOM   1215  C   CYS A 147      11.556 -46.558   7.244  1.00 15.69           C  
ANISOU 1215  C   CYS A 147     1884   1982   2095   -166    202   -441       C  
ATOM   1216  O   CYS A 147      12.034 -47.682   7.390  1.00 14.85           O  
ANISOU 1216  O   CYS A 147     1775   1838   2029   -165    225   -475       O  
ATOM   1217  CB  CYS A 147      13.008 -44.592   8.018  1.00 16.91           C  
ANISOU 1217  CB  CYS A 147     2025   2110   2290   -128    167   -368       C  
ATOM   1218  SG  CYS A 147      11.806 -43.821   9.129  1.00 14.85           S  
ANISOU 1218  SG  CYS A 147     1788   1848   2006   -115    122   -328       S  
ATOM   1219  N   HIS A 148      10.253 -46.313   7.380  1.00 11.14           N  
ANISOU 1219  N   HIS A 148     1321   1436   1477   -175    181   -427       N  
ATOM   1220  CA  HIS A 148       9.321 -47.409   7.652  1.00 12.23           C  
ANISOU 1220  CA  HIS A 148     1470   1565   1613   -187    182   -453       C  
ATOM   1221  C   HIS A 148       9.364 -48.475   6.543  1.00 12.35           C  
ANISOU 1221  C   HIS A 148     1480   1597   1615   -219    221   -512       C  
ATOM   1222  O   HIS A 148       9.404 -49.674   6.823  1.00 18.03           O  
ANISOU 1222  O   HIS A 148     2202   2278   2370   -222    238   -547       O  
ATOM   1223  CB  HIS A 148       7.896 -46.880   7.835  1.00 12.31           C  
ANISOU 1223  CB  HIS A 148     1490   1610   1579   -193    155   -423       C  
ATOM   1224  CG  HIS A 148       7.739 -45.949   8.997  1.00 12.14           C  
ANISOU 1224  CG  HIS A 148     1479   1565   1571   -162    122   -372       C  
ATOM   1225  ND1 HIS A 148       6.604 -45.192   9.194  1.00 12.53           N  
ANISOU 1225  ND1 HIS A 148     1535   1642   1584   -161    102   -334       N  
ATOM   1226  CD2 HIS A 148       8.572 -45.655  10.026  1.00 13.72           C  
ANISOU 1226  CD2 HIS A 148     1683   1715   1814   -133    108   -353       C  
ATOM   1227  CE1 HIS A 148       6.743 -44.475  10.296  1.00 17.68           C  
ANISOU 1227  CE1 HIS A 148     2200   2262   2258   -131     79   -298       C  
ATOM   1228  NE2 HIS A 148       7.933 -44.726  10.810  1.00 16.70           N  
ANISOU 1228  NE2 HIS A 148     2075   2092   2178   -115     80   -310       N  
ATOM   1229  N   SER A 149       9.385 -48.047   5.285  1.00 17.95           N  
ANISOU 1229  N   SER A 149     2182   2363   2274   -243    238   -522       N  
ATOM   1230  CA  SER A 149       9.414 -48.999   4.167  1.00 14.90           C  
ANISOU 1230  CA  SER A 149     1797   1999   1866   -277    277   -582       C  
ATOM   1231  C   SER A 149      10.722 -49.777   4.188  1.00 14.78           C  
ANISOU 1231  C   SER A 149     1775   1930   1910   -264    315   -616       C  
ATOM   1232  O   SER A 149      10.831 -50.864   3.608  1.00 14.99           O  
ANISOU 1232  O   SER A 149     1806   1947   1942   -285    353   -672       O  
ATOM   1233  CB  SER A 149       9.262 -48.279   2.821  1.00 19.65           C  
ANISOU 1233  CB  SER A 149     2392   2677   2396   -303    287   -580       C  
ATOM   1234  OG  SER A 149      10.431 -47.536   2.487  1.00 18.10           O  
ANISOU 1234  OG  SER A 149     2182   2482   2213   -286    302   -562       O  
ATOM   1235  N   MET A 150      11.709 -49.215   4.875  1.00 15.91           N  
ANISOU 1235  N   MET A 150     1908   2037   2101   -230    306   -581       N  
ATOM   1236  CA AMET A 150      13.019 -49.846   4.968  1.00 16.51           C  
ANISOU 1236  CA AMET A 150     1972   2060   2241   -214    340   -600       C  
ATOM   1237  CA BMET A 150      13.028 -49.828   4.985  0.00 17.16           C  
ANISOU 1237  CA BMET A 150     2054   2142   2324   -214    340   -599       C  
ATOM   1238  C   MET A 150      13.207 -50.571   6.303  1.00 20.08           C  
ANISOU 1238  C   MET A 150     2424   2442   2763   -189    327   -592       C  
ATOM   1239  O   MET A 150      14.330 -50.894   6.690  1.00 20.12           O  
ANISOU 1239  O   MET A 150     2415   2400   2831   -168    343   -588       O  
ATOM   1240  CB AMET A 150      14.111 -48.788   4.739  1.00 15.94           C  
ANISOU 1240  CB AMET A 150     1883   1995   2180   -197    341   -565       C  
ATOM   1241  CB BMET A 150      14.120 -48.767   4.829  0.00 16.51           C  
ANISOU 1241  CB BMET A 150     1955   2064   2255   -195    339   -562       C  
ATOM   1242  CG AMET A 150      14.020 -48.152   3.335  1.00 17.08           C  
ANISOU 1242  CG AMET A 150     2023   2208   2257   -220    362   -572       C  
ATOM   1243  CG BMET A 150      14.348 -48.356   3.385  0.00 16.72           C  
ANISOU 1243  CG BMET A 150     1974   2147   2230   -216    371   -578       C  
ATOM   1244  SD AMET A 150      14.813 -49.218   2.078  1.00 22.26           S  
ANISOU 1244  SD AMET A 150     2676   2865   2916   -240    435   -639       S  
ATOM   1245  SD BMET A 150      14.886 -49.761   2.393  0.00 22.35           S  
ANISOU 1245  SD BMET A 150     2690   2848   2954   -236    441   -652       S  
ATOM   1246  CE AMET A 150      16.541 -48.929   2.507  1.00 20.02           C  
ANISOU 1246  CE AMET A 150     2365   2525   2715   -202    451   -608       C  
ATOM   1247  CE BMET A 150      14.897 -49.055   0.749  0.00 22.77           C  
ANISOU 1247  CE BMET A 150     2742   2985   2926   -263    469   -662       C  
ATOM   1248  N   GLY A 151      12.099 -50.832   6.992  1.00 16.45           N  
ANISOU 1248  N   GLY A 151     1978   1980   2292   -192    299   -586       N  
ATOM   1249  CA  GLY A 151      12.109 -51.622   8.215  1.00 16.97           C  
ANISOU 1249  CA  GLY A 151     2045   1985   2416   -171    288   -579       C  
ATOM   1250  C   GLY A 151      12.600 -50.939   9.481  1.00 17.90           C  
ANISOU 1250  C   GLY A 151     2160   2071   2568   -136    249   -524       C  
ATOM   1251  O   GLY A 151      13.004 -51.595  10.436  1.00 15.22           O  
ANISOU 1251  O   GLY A 151     1817   1680   2287   -116    245   -516       O  
ATOM   1252  N   ILE A 152      12.548 -49.617   9.502  1.00 15.74           N  
ANISOU 1252  N   ILE A 152     1891   1830   2261   -130    220   -487       N  
ATOM   1253  CA  ILE A 152      13.138 -48.868  10.603  1.00  9.20           C  
ANISOU 1253  CA  ILE A 152     1062    972   1461   -102    183   -440       C  
ATOM   1254  C   ILE A 152      12.165 -47.861  11.186  1.00 15.13           C  
ANISOU 1254  C   ILE A 152     1833   1746   2170    -96    143   -404       C  
ATOM   1255  O   ILE A 152      11.490 -47.139  10.455  1.00 15.32           O  
ANISOU 1255  O   ILE A 152     1861   1819   2140   -111    142   -399       O  
ATOM   1256  CB  ILE A 152      14.417 -48.150  10.118  1.00 15.76           C  
ANISOU 1256  CB  ILE A 152     1873   1804   2310    -96    192   -428       C  
ATOM   1257  CG1 ILE A 152      15.510 -49.191   9.804  1.00 15.32           C  
ANISOU 1257  CG1 ILE A 152     1796   1713   2314    -94    233   -455       C  
ATOM   1258  CG2 ILE A 152      14.858 -47.078  11.129  1.00 12.81           C  
ANISOU 1258  CG2 ILE A 152     1502   1413   1951    -74    147   -378       C  
ATOM   1259  CD1 ILE A 152      16.546 -48.713   8.811  1.00 21.51           C  
ANISOU 1259  CD1 ILE A 152     2559   2511   3102    -98    261   -457       C  
ATOM   1260  N   MET A 153      12.094 -47.818  12.514  1.00 10.93           N  
ANISOU 1260  N   MET A 153     1313   1179   1661    -73    111   -376       N  
ATOM   1261  CA  MET A 153      11.347 -46.769  13.187  1.00 13.52           C  
ANISOU 1261  CA  MET A 153     1662   1520   1954    -63     76   -340       C  
ATOM   1262  C   MET A 153      12.308 -45.759  13.812  1.00 14.47           C  
ANISOU 1262  C   MET A 153     1782   1620   2094    -46     48   -308       C  
ATOM   1263  O   MET A 153      13.354 -46.128  14.353  1.00 13.67           O  
ANISOU 1263  O   MET A 153     1671   1482   2042    -34     43   -304       O  
ATOM   1264  CB  MET A 153      10.367 -47.338  14.220  1.00 22.03           C  
ANISOU 1264  CB  MET A 153     2760   2579   3032    -52     61   -331       C  
ATOM   1265  CG  MET A 153      10.887 -48.463  15.062  1.00 22.27           C  
ANISOU 1265  CG  MET A 153     2785   2560   3116    -38     63   -338       C  
ATOM   1266  SD  MET A 153       9.599 -49.211  16.102  1.00 19.07           S  
ANISOU 1266  SD  MET A 153     2399   2139   2707    -27     52   -328       S  
ATOM   1267  CE  MET A 153      10.502 -50.655  16.656  1.00 16.75           C  
ANISOU 1267  CE  MET A 153     2087   1791   2486    -16     67   -341       C  
ATOM   1268  N   HIS A 154      11.954 -44.482  13.720  1.00 11.92           N  
ANISOU 1268  N   HIS A 154     1470   1323   1736    -45     32   -282       N  
ATOM   1269  CA  HIS A 154      12.844 -43.426  14.182  1.00 12.51           C  
ANISOU 1269  CA  HIS A 154     1545   1381   1828    -34      7   -255       C  
ATOM   1270  C   HIS A 154      12.829 -43.338  15.711  1.00 17.35           C  
ANISOU 1270  C   HIS A 154     2182   1955   2455    -15    -30   -235       C  
ATOM   1271  O   HIS A 154      13.884 -43.313  16.342  1.00 14.50           O  
ANISOU 1271  O   HIS A 154     1815   1562   2132     -6    -49   -225       O  
ATOM   1272  CB  HIS A 154      12.468 -42.089  13.536  1.00 13.29           C  
ANISOU 1272  CB  HIS A 154     1645   1515   1888    -41      5   -235       C  
ATOM   1273  CG  HIS A 154      13.413 -40.975  13.865  1.00 13.72           C  
ANISOU 1273  CG  HIS A 154     1697   1553   1964    -33    -17   -210       C  
ATOM   1274  ND1 HIS A 154      13.393 -40.326  15.079  1.00 12.40           N  
ANISOU 1274  ND1 HIS A 154     1555   1355   1801    -19    -52   -189       N  
ATOM   1275  CD2 HIS A 154      14.407 -40.398  13.146  1.00 14.06           C  
ANISOU 1275  CD2 HIS A 154     1715   1601   2025    -39     -9   -204       C  
ATOM   1276  CE1 HIS A 154      14.334 -39.397  15.096  1.00 10.88           C  
ANISOU 1276  CE1 HIS A 154     1353   1150   1630    -19    -67   -172       C  
ATOM   1277  NE2 HIS A 154      14.963 -39.417  13.936  1.00  9.44           N  
ANISOU 1277  NE2 HIS A 154     1138    989   1459    -30    -41   -179       N  
ATOM   1278  N   ARG A 155      11.624 -43.304  16.285  1.00 14.40           N  
ANISOU 1278  N   ARG A 155     1835   1587   2050     -8    -38   -226       N  
ATOM   1279  CA  ARG A 155      11.394 -43.304  17.744  1.00 11.74           C  
ANISOU 1279  CA  ARG A 155     1526   1217   1715     11    -67   -208       C  
ATOM   1280  C   ARG A 155      11.813 -42.032  18.495  1.00 11.12           C  
ANISOU 1280  C   ARG A 155     1469   1124   1632     20   -100   -183       C  
ATOM   1281  O   ARG A 155      11.818 -42.007  19.724  1.00 14.32           O  
ANISOU 1281  O   ARG A 155     1899   1502   2038     34   -126   -171       O  
ATOM   1282  CB  ARG A 155      11.978 -44.553  18.438  1.00  9.72           C  
ANISOU 1282  CB  ARG A 155     1263    928   1503     20    -71   -216       C  
ATOM   1283  CG  ARG A 155      11.563 -45.892  17.800  1.00 12.71           C  
ANISOU 1283  CG  ARG A 155     1623   1312   1893     11    -37   -244       C  
ATOM   1284  CD  ARG A 155      11.858 -47.089  18.722  1.00 10.60           C  
ANISOU 1284  CD  ARG A 155     1353   1008   1669     24    -40   -243       C  
ATOM   1285  NE  ARG A 155      13.268 -47.150  19.119  1.00 12.13           N  
ANISOU 1285  NE  ARG A 155     1528   1172   1908     30    -56   -233       N  
ATOM   1286  CZ  ARG A 155      13.792 -48.056  19.948  1.00 16.69           C  
ANISOU 1286  CZ  ARG A 155     2096   1716   2529     42    -63   -223       C  
ATOM   1287  NH1 ARG A 155      13.029 -48.995  20.501  1.00 12.23           N  
ANISOU 1287  NH1 ARG A 155     1539   1140   1968     51    -56   -223       N  
ATOM   1288  NH2 ARG A 155      15.096 -48.012  20.239  1.00 13.85           N  
ANISOU 1288  NH2 ARG A 155     1716   1335   2212     46    -79   -208       N  
ATOM   1289  N   ASP A 156      12.134 -40.970  17.771  1.00 13.28           N  
ANISOU 1289  N   ASP A 156     1734   1415   1898     12    -97   -177       N  
ATOM   1290  CA  ASP A 156      12.465 -39.714  18.440  1.00  8.89           C  
ANISOU 1290  CA  ASP A 156     1198    841   1339     17   -125   -156       C  
ATOM   1291  C   ASP A 156      12.108 -38.554  17.536  1.00 11.31           C  
ANISOU 1291  C   ASP A 156     1499   1176   1623     10   -111   -144       C  
ATOM   1292  O   ASP A 156      12.850 -37.582  17.427  1.00 13.86           O  
ANISOU 1292  O   ASP A 156     1815   1490   1960      6   -122   -133       O  
ATOM   1293  CB  ASP A 156      13.953 -39.679  18.823  1.00 10.43           C  
ANISOU 1293  CB  ASP A 156     1378   1007   1578     15   -150   -154       C  
ATOM   1294  CG  ASP A 156      14.268 -38.609  19.858  1.00 16.50           C  
ANISOU 1294  CG  ASP A 156     2176   1749   2343     19   -188   -138       C  
ATOM   1295  OD1 ASP A 156      13.337 -38.125  20.552  1.00 13.46           O  
ANISOU 1295  OD1 ASP A 156     1830   1361   1923     29   -194   -131       O  
ATOM   1296  OD2 ASP A 156      15.461 -38.269  19.990  1.00 17.62           O  
ANISOU 1296  OD2 ASP A 156     2303   1873   2518     12   -211   -132       O  
ATOM   1297  N   VAL A 157      10.956 -38.668  16.877  1.00 12.85           N  
ANISOU 1297  N   VAL A 157     1693   1406   1785      7    -85   -143       N  
ATOM   1298  CA  VAL A 157      10.463 -37.579  16.050  1.00 11.54           C  
ANISOU 1298  CA  VAL A 157     1520   1271   1596      1    -71   -124       C  
ATOM   1299  C   VAL A 157      10.029 -36.429  16.970  1.00 16.56           C  
ANISOU 1299  C   VAL A 157     2189   1883   2220     15    -87   -101       C  
ATOM   1300  O   VAL A 157       9.233 -36.625  17.894  1.00 14.25           O  
ANISOU 1300  O   VAL A 157     1928   1575   1912     29    -92    -97       O  
ATOM   1301  CB  VAL A 157       9.280 -38.042  15.153  1.00 13.30           C  
ANISOU 1301  CB  VAL A 157     1731   1539   1784     -8    -43   -125       C  
ATOM   1302  CG1 VAL A 157       8.639 -36.848  14.452  1.00 12.02           C  
ANISOU 1302  CG1 VAL A 157     1562   1409   1597    -11    -31    -95       C  
ATOM   1303  CG2 VAL A 157       9.743 -39.081  14.133  1.00 14.95           C  
ANISOU 1303  CG2 VAL A 157     1908   1771   2000    -26    -24   -154       C  
ATOM   1304  N   LYS A 158      10.572 -35.242  16.722  1.00 10.05           N  
ANISOU 1304  N   LYS A 158     1359   1053   1406     12    -91    -85       N  
ATOM   1305  CA  LYS A 158      10.285 -34.036  17.497  1.00 11.22           C  
ANISOU 1305  CA  LYS A 158     1539   1175   1550     23   -102    -66       C  
ATOM   1306  C   LYS A 158      10.892 -32.866  16.729  1.00 15.25           C  
ANISOU 1306  C   LYS A 158     2026   1690   2077     14    -96    -49       C  
ATOM   1307  O   LYS A 158      11.758 -33.074  15.870  1.00 10.97           O  
ANISOU 1307  O   LYS A 158     1449   1164   1555      2    -92    -55       O  
ATOM   1308  CB  LYS A 158      10.896 -34.128  18.910  1.00 10.10           C  
ANISOU 1308  CB  LYS A 158     1432    986   1422     30   -136    -79       C  
ATOM   1309  CG  LYS A 158      12.418 -34.210  18.932  1.00 14.66           C  
ANISOU 1309  CG  LYS A 158     1989   1543   2038     19   -161    -89       C  
ATOM   1310  CD  LYS A 158      12.933 -34.388  20.350  1.00 13.63           C  
ANISOU 1310  CD  LYS A 158     1890   1372   1915     23   -199    -98       C  
ATOM   1311  CE  LYS A 158      14.451 -34.454  20.379  1.00 13.01           C  
ANISOU 1311  CE  LYS A 158     1788   1276   1880     10   -227   -103       C  
ATOM   1312  NZ  LYS A 158      14.956 -34.412  21.806  1.00 20.64           N  
ANISOU 1312  NZ  LYS A 158     2787   2205   2848     10   -270   -107       N  
ATOM   1313  N   PRO A 159      10.437 -31.633  17.014  1.00 14.30           N  
ANISOU 1313  N   PRO A 159     1926   1556   1953     22    -92    -27       N  
ATOM   1314  CA  PRO A 159      10.897 -30.457  16.271  1.00 14.87           C  
ANISOU 1314  CA  PRO A 159     1975   1632   2045     15    -83     -5       C  
ATOM   1315  C   PRO A 159      12.424 -30.373  16.146  1.00 15.21           C  
ANISOU 1315  C   PRO A 159     1996   1656   2127      2   -104    -16       C  
ATOM   1316  O   PRO A 159      12.932 -30.092  15.064  1.00 13.78           O  
ANISOU 1316  O   PRO A 159     1775   1500   1961     -7    -89     -4       O  
ATOM   1317  CB  PRO A 159      10.351 -29.296  17.099  1.00 17.02           C  
ANISOU 1317  CB  PRO A 159     2284   1869   2315     27    -83     10       C  
ATOM   1318  CG  PRO A 159       9.043 -29.840  17.639  1.00 14.16           C  
ANISOU 1318  CG  PRO A 159     1949   1513   1917     42    -71     11       C  
ATOM   1319  CD  PRO A 159       9.361 -31.287  17.972  1.00 15.38           C  
ANISOU 1319  CD  PRO A 159     2105   1672   2066     39    -89    -19       C  
ATOM   1320  N   HIS A 160      13.145 -30.617  17.232  1.00 15.98           N  
ANISOU 1320  N   HIS A 160     2117   1713   2242      2   -138    -36       N  
ATOM   1321  CA  HIS A 160      14.604 -30.509  17.168  1.00 15.65           C  
ANISOU 1321  CA  HIS A 160     2052   1652   2243    -11   -161    -41       C  
ATOM   1322  C   HIS A 160      15.214 -31.430  16.119  1.00 16.29           C  
ANISOU 1322  C   HIS A 160     2087   1765   2338    -19   -145    -46       C  
ATOM   1323  O   HIS A 160      16.220 -31.087  15.495  1.00 19.06           O  
ANISOU 1323  O   HIS A 160     2404   2116   2723    -28   -145    -37       O  
ATOM   1324  CB  HIS A 160      15.234 -30.779  18.525  1.00 12.87           C  
ANISOU 1324  CB  HIS A 160     1730   1256   1903    -13   -204    -59       C  
ATOM   1325  CG  HIS A 160      16.734 -30.748  18.499  1.00 21.38           C  
ANISOU 1325  CG  HIS A 160     2780   2315   3028    -27   -231    -59       C  
ATOM   1326  ND1 HIS A 160      17.465 -29.655  18.913  1.00 27.93           N  
ANISOU 1326  ND1 HIS A 160     3616   3111   3886    -38   -257    -52       N  
ATOM   1327  CD2 HIS A 160      17.636 -31.672  18.094  1.00 23.52           C  
ANISOU 1327  CD2 HIS A 160     3014   2595   3327    -33   -234    -64       C  
ATOM   1328  CE1 HIS A 160      18.754 -29.911  18.774  1.00 28.54           C  
ANISOU 1328  CE1 HIS A 160     3660   3179   4007    -51   -278    -50       C  
ATOM   1329  NE2 HIS A 160      18.886 -31.129  18.282  1.00 25.70           N  
ANISOU 1329  NE2 HIS A 160     3272   2843   3648    -46   -263    -56       N  
ATOM   1330  N   ASN A 161      14.605 -32.593  15.903  1.00 15.14           N  
ANISOU 1330  N   ASN A 161     1941   1646   2168    -15   -130    -61       N  
ATOM   1331  CA  ASN A 161      15.190 -33.579  14.979  1.00 13.20           C  
ANISOU 1331  CA  ASN A 161     1656   1425   1934    -22   -112    -73       C  
ATOM   1332  C   ASN A 161      14.753 -33.427  13.523  1.00 14.47           C  
ANISOU 1332  C   ASN A 161     1787   1637   2073    -29    -73    -63       C  
ATOM   1333  O   ASN A 161      15.113 -34.228  12.663  1.00 14.47           O  
ANISOU 1333  O   ASN A 161     1760   1663   2075    -36    -52    -77       O  
ATOM   1334  CB  ASN A 161      14.914 -34.997  15.473  1.00  9.02           C  
ANISOU 1334  CB  ASN A 161     1139    893   1397    -18   -114    -98       C  
ATOM   1335  CG  ASN A 161      15.740 -35.340  16.688  1.00 11.33           C  
ANISOU 1335  CG  ASN A 161     1446   1141   1720    -15   -151   -105       C  
ATOM   1336  OD1 ASN A 161      16.776 -34.708  16.932  1.00 14.17           O  
ANISOU 1336  OD1 ASN A 161     1796   1476   2113    -20   -175    -95       O  
ATOM   1337  ND2 ASN A 161      15.303 -36.329  17.455  1.00 12.48           N  
ANISOU 1337  ND2 ASN A 161     1611   1277   1854     -7   -159   -118       N  
ATOM   1338  N   VAL A 162      13.958 -32.406  13.244  1.00 12.18           N  
ANISOU 1338  N   VAL A 162     1503   1363   1761    -27    -62    -39       N  
ATOM   1339  CA  VAL A 162      13.563 -32.140  11.866  1.00 13.50           C  
ANISOU 1339  CA  VAL A 162     1640   1584   1906    -34    -29    -21       C  
ATOM   1340  C   VAL A 162      14.177 -30.822  11.454  1.00 20.08           C  
ANISOU 1340  C   VAL A 162     2453   2412   2765    -36    -26     10       C  
ATOM   1341  O   VAL A 162      13.610 -29.757  11.727  1.00 25.06           O  
ANISOU 1341  O   VAL A 162     3097   3032   3393    -29    -27     35       O  
ATOM   1342  CB  VAL A 162      12.022 -32.045  11.726  1.00 17.56           C  
ANISOU 1342  CB  VAL A 162     2168   2130   2373    -30    -14     -7       C  
ATOM   1343  CG1 VAL A 162      11.635 -31.684  10.289  1.00 15.46           C  
ANISOU 1343  CG1 VAL A 162     1868   1925   2082    -41     16     17       C  
ATOM   1344  CG2 VAL A 162      11.378 -33.355  12.126  1.00 15.58           C  
ANISOU 1344  CG2 VAL A 162     1935   1884   2100    -30    -16    -36       C  
ATOM   1345  N   MET A 163      15.332 -30.891  10.796  1.00 13.91           N  
ANISOU 1345  N   MET A 163     1637   1633   2013    -43    -20      9       N  
ATOM   1346  CA  MET A 163      16.071 -29.698  10.415  1.00 11.33           C  
ANISOU 1346  CA  MET A 163     1287   1298   1721    -45    -18     39       C  
ATOM   1347  C   MET A 163      15.541 -29.122   9.116  1.00 16.36           C  
ANISOU 1347  C   MET A 163     1894   1989   2331    -48     17     71       C  
ATOM   1348  O   MET A 163      15.379 -29.836   8.129  1.00 18.29           O  
ANISOU 1348  O   MET A 163     2120   2284   2546    -55     42     63       O  
ATOM   1349  CB  MET A 163      17.565 -29.991  10.292  1.00 15.54           C  
ANISOU 1349  CB  MET A 163     1793   1809   2302    -50    -26     31       C  
ATOM   1350  CG  MET A 163      18.112 -30.646  11.532  1.00 19.96           C  
ANISOU 1350  CG  MET A 163     2376   2320   2887    -49    -62      5       C  
ATOM   1351  SD  MET A 163      19.863 -30.348  11.670  1.00 25.32           S  
ANISOU 1351  SD  MET A 163     3024   2960   3638    -56    -83     15       S  
ATOM   1352  CE  MET A 163      19.861 -28.569  11.719  1.00 19.94           C  
ANISOU 1352  CE  MET A 163     2342   2259   2976    -58    -92     51       C  
ATOM   1353  N   ILE A 164      15.275 -27.821   9.125  1.00 17.72           N  
ANISOU 1353  N   ILE A 164     2065   2153   2515    -43     19    107       N  
ATOM   1354  CA  ILE A 164      14.683 -27.161   7.971  1.00 19.38           C  
ANISOU 1354  CA  ILE A 164     2246   2416   2701    -45     50    147       C  
ATOM   1355  C   ILE A 164      15.505 -25.963   7.518  1.00 23.77           C  
ANISOU 1355  C   ILE A 164     2770   2959   3301    -44     58    184       C  
ATOM   1356  O   ILE A 164      15.735 -25.021   8.284  1.00 23.42           O  
ANISOU 1356  O   ILE A 164     2739   2862   3296    -40     41    196       O  
ATOM   1357  CB  ILE A 164      13.259 -26.675   8.287  1.00 18.16           C  
ANISOU 1357  CB  ILE A 164     2113   2269   2516    -36     55    168       C  
ATOM   1358  CG1 ILE A 164      12.343 -27.858   8.580  1.00 17.33           C  
ANISOU 1358  CG1 ILE A 164     2034   2185   2367    -38     51    138       C  
ATOM   1359  CG2 ILE A 164      12.705 -25.841   7.146  1.00 23.44           C  
ANISOU 1359  CG2 ILE A 164     2747   2990   3168    -37     85    220       C  
ATOM   1360  CD1 ILE A 164      10.974 -27.438   9.130  1.00 23.01           C  
ANISOU 1360  CD1 ILE A 164     2778   2901   3064    -27     53    158       C  
ATOM   1361  N   ASP A 165      15.961 -26.022   6.273  1.00 17.35           N  
ANISOU 1361  N   ASP A 165     1917   2194   2483    -51     84    202       N  
ATOM   1362  CA  ASP A 165      16.530 -24.869   5.607  1.00 22.07           C  
ANISOU 1362  CA  ASP A 165     2477   2794   3114    -49    100    248       C  
ATOM   1363  C   ASP A 165      15.374 -24.153   4.926  1.00 25.66           C  
ANISOU 1363  C   ASP A 165     2920   3297   3535    -46    125    293       C  
ATOM   1364  O   ASP A 165      14.928 -24.542   3.851  1.00 25.26           O  
ANISOU 1364  O   ASP A 165     2847   3315   3435    -52    149    305       O  
ATOM   1365  CB  ASP A 165      17.592 -25.289   4.585  1.00 25.30           C  
ANISOU 1365  CB  ASP A 165     2847   3233   3532    -56    121    248       C  
ATOM   1366  CG  ASP A 165      18.216 -24.103   3.872  1.00 29.53           C  
ANISOU 1366  CG  ASP A 165     3340   3772   4106    -53    139    300       C  
ATOM   1367  OD1 ASP A 165      17.567 -23.037   3.798  1.00 31.11           O  
ANISOU 1367  OD1 ASP A 165     3535   3975   4309    -48    146    341       O  
ATOM   1368  OD2 ASP A 165      19.356 -24.237   3.389  1.00 31.96           O  
ANISOU 1368  OD2 ASP A 165     3619   4079   4445    -56    149    302       O  
ATOM   1369  N   HIS A 166      14.895 -23.104   5.574  1.00 23.93           N  
ANISOU 1369  N   HIS A 166     2714   3040   3340    -37    118    319       N  
ATOM   1370  CA  HIS A 166      13.725 -22.377   5.107  1.00 21.26           C  
ANISOU 1370  CA  HIS A 166     2364   2736   2977    -31    141    367       C  
ATOM   1371  C   HIS A 166      14.007 -21.559   3.843  1.00 26.37           C  
ANISOU 1371  C   HIS A 166     2958   3428   3633    -31    171    425       C  
ATOM   1372  O   HIS A 166      13.080 -21.183   3.127  1.00 29.81           O  
ANISOU 1372  O   HIS A 166     3374   3917   4037    -30    193    470       O  
ATOM   1373  CB  HIS A 166      13.202 -21.477   6.233  1.00 18.53           C  
ANISOU 1373  CB  HIS A 166     2051   2327   2663    -18    130    377       C  
ATOM   1374  CG  HIS A 166      11.777 -21.053   6.060  1.00 22.64           C  
ANISOU 1374  CG  HIS A 166     2571   2877   3153     -9    151    416       C  
ATOM   1375  ND1 HIS A 166      10.802 -21.896   5.571  1.00 23.89           N  
ANISOU 1375  ND1 HIS A 166     2729   3099   3251    -14    157    416       N  
ATOM   1376  CD2 HIS A 166      11.157 -19.880   6.334  1.00 25.06           C  
ANISOU 1376  CD2 HIS A 166     2878   3155   3487      4    166    460       C  
ATOM   1377  CE1 HIS A 166       9.645 -21.260   5.548  1.00 24.81           C  
ANISOU 1377  CE1 HIS A 166     2841   3227   3357     -4    174    461       C  
ATOM   1378  NE2 HIS A 166       9.832 -20.034   6.001  1.00 26.08           N  
ANISOU 1378  NE2 HIS A 166     3004   3333   3573      8    183    489       N  
ATOM   1379  N   GLU A 167      15.278 -21.282   3.567  1.00 25.68           N  
ANISOU 1379  N   GLU A 167     2846   3321   3590    -34    172    428       N  
ATOM   1380  CA  GLU A 167      15.637 -20.567   2.344  1.00 27.70           C  
ANISOU 1380  CA  GLU A 167     3049   3620   3854    -34    203    484       C  
ATOM   1381  C   GLU A 167      15.410 -21.417   1.098  1.00 31.17           C  
ANISOU 1381  C   GLU A 167     3466   4150   4226    -44    225    485       C  
ATOM   1382  O   GLU A 167      14.751 -20.984   0.152  1.00 31.17           O  
ANISOU 1382  O   GLU A 167     3437   4212   4193    -44    250    535       O  
ATOM   1383  CB  GLU A 167      17.088 -20.072   2.396  1.00 34.72           C  
ANISOU 1383  CB  GLU A 167     3915   4462   4813    -34    199    488       C  
ATOM   1384  CG  GLU A 167      17.542 -19.360   1.126  1.00 45.22           C  
ANISOU 1384  CG  GLU A 167     5189   5837   6156    -32    233    548       C  
ATOM   1385  CD  GLU A 167      18.980 -18.868   1.207  1.00 55.68           C  
ANISOU 1385  CD  GLU A 167     6489   7112   7556    -32    229    555       C  
ATOM   1386  OE1 GLU A 167      19.626 -19.064   2.259  1.00 55.80           O  
ANISOU 1386  OE1 GLU A 167     6530   7058   7613    -36    196    514       O  
ATOM   1387  OE2 GLU A 167      19.465 -18.282   0.216  1.00 61.72           O  
ANISOU 1387  OE2 GLU A 167     7206   7907   8339    -29    258    605       O  
ATOM   1388  N   HIS A 168      15.945 -22.633   1.099  1.00 32.98           N  
ANISOU 1388  N   HIS A 168     3709   4385   4435    -52    218    430       N  
ATOM   1389  CA  HIS A 168      15.806 -23.523  -0.051  1.00 31.81           C  
ANISOU 1389  CA  HIS A 168     3547   4318   4223    -64    241    419       C  
ATOM   1390  C   HIS A 168      14.678 -24.531   0.122  1.00 29.42           C  
ANISOU 1390  C   HIS A 168     3276   4047   3856    -74    231    383       C  
ATOM   1391  O   HIS A 168      14.554 -25.464  -0.668  1.00 28.61           O  
ANISOU 1391  O   HIS A 168     3171   4002   3698    -88    245    359       O  
ATOM   1392  CB  HIS A 168      17.111 -24.266  -0.307  1.00 31.94           C  
ANISOU 1392  CB  HIS A 168     3554   4323   4257    -68    248    383       C  
ATOM   1393  CG  HIS A 168      18.295 -23.362  -0.463  1.00 35.89           C  
ANISOU 1393  CG  HIS A 168     4020   4790   4826    -60    257    418       C  
ATOM   1394  ND1 HIS A 168      18.507 -22.604  -1.594  1.00 36.99           N  
ANISOU 1394  ND1 HIS A 168     4115   4977   4964    -58    289    475       N  
ATOM   1395  CD2 HIS A 168      19.326 -23.092   0.372  1.00 38.98           C  
ANISOU 1395  CD2 HIS A 168     4413   5106   5291    -55    236    408       C  
ATOM   1396  CE1 HIS A 168      19.622 -21.908  -1.451  1.00 42.46           C  
ANISOU 1396  CE1 HIS A 168     4783   5622   5729    -50    289    498       C  
ATOM   1397  NE2 HIS A 168      20.139 -22.186  -0.267  1.00 42.60           N  
ANISOU 1397  NE2 HIS A 168     4828   5565   5794    -50    256    457       N  
ATOM   1398  N   ARG A 169      13.870 -24.345   1.162  1.00 22.57           N  
ANISOU 1398  N   ARG A 169     2440   3140   2996    -67    208    379       N  
ATOM   1399  CA  ARG A 169      12.726 -25.212   1.413  1.00 24.39           C  
ANISOU 1399  CA  ARG A 169     2698   3395   3173    -74    198    351       C  
ATOM   1400  C   ARG A 169      13.147 -26.674   1.487  1.00 25.91           C  
ANISOU 1400  C   ARG A 169     2912   3589   3344    -86    192    283       C  
ATOM   1401  O   ARG A 169      12.495 -27.546   0.911  1.00 30.85           O  
ANISOU 1401  O   ARG A 169     3542   4270   3911   -101    199    263       O  
ATOM   1402  CB  ARG A 169      11.678 -25.043   0.307  1.00 28.73           C  
ANISOU 1402  CB  ARG A 169     3223   4032   3662    -85    217    395       C  
ATOM   1403  CG  ARG A 169      11.495 -23.610  -0.180  1.00 36.09           C  
ANISOU 1403  CG  ARG A 169     4118   4978   4615    -75    234    473       C  
ATOM   1404  CD  ARG A 169      10.464 -22.862   0.632  1.00 41.23           C  
ANISOU 1404  CD  ARG A 169     4782   5596   5285    -61    226    505       C  
ATOM   1405  NE  ARG A 169       9.157 -23.518   0.621  1.00 45.50           N  
ANISOU 1405  NE  ARG A 169     5338   6181   5770    -70    219    501       N  
ATOM   1406  CZ  ARG A 169       8.135 -23.140   1.385  1.00 42.51           C  
ANISOU 1406  CZ  ARG A 169     4976   5775   5401    -58    213    522       C  
ATOM   1407  NH1 ARG A 169       8.278 -22.109   2.209  1.00 43.44           N  
ANISOU 1407  NH1 ARG A 169     5104   5823   5580    -37    215    543       N  
ATOM   1408  NH2 ARG A 169       6.980 -23.787   1.337  1.00 35.17           N  
ANISOU 1408  NH2 ARG A 169     4055   4886   4422    -67    207    520       N  
ATOM   1409  N   LYS A 170      14.229 -26.933   2.213  1.00 22.91           N  
ANISOU 1409  N   LYS A 170     2544   3146   3014    -79    178    250       N  
ATOM   1410  CA  LYS A 170      14.824 -28.261   2.299  1.00 28.35           C  
ANISOU 1410  CA  LYS A 170     3247   3828   3698    -87    177    191       C  
ATOM   1411  C   LYS A 170      14.737 -28.810   3.729  1.00 24.85           C  
ANISOU 1411  C   LYS A 170     2844   3319   3279    -80    144    152       C  
ATOM   1412  O   LYS A 170      14.959 -28.085   4.699  1.00 22.26           O  
ANISOU 1412  O   LYS A 170     2529   2933   2995    -68    122    164       O  
ATOM   1413  CB  LYS A 170      16.286 -28.186   1.844  1.00 29.58           C  
ANISOU 1413  CB  LYS A 170     3375   3970   3896    -85    192    191       C  
ATOM   1414  CG  LYS A 170      17.041 -29.505   1.885  1.00 39.56           C  
ANISOU 1414  CG  LYS A 170     4647   5220   5165    -90    197    136       C  
ATOM   1415  CD  LYS A 170      18.475 -29.358   1.350  1.00 45.79           C  
ANISOU 1415  CD  LYS A 170     5403   5998   5998    -87    217    145       C  
ATOM   1416  CE  LYS A 170      19.434 -28.787   2.395  1.00 43.65           C  
ANISOU 1416  CE  LYS A 170     5129   5648   5805    -75    188    155       C  
ATOM   1417  NZ  LYS A 170      20.823 -28.675   1.862  1.00 45.77           N  
ANISOU 1417  NZ  LYS A 170     5362   5907   6122    -72    208    168       N  
ATOM   1418  N   LEU A 171      14.432 -30.095   3.857  1.00 16.14           N  
ANISOU 1418  N   LEU A 171     1760   2224   2146    -88    142    105       N  
ATOM   1419  CA  LEU A 171      14.193 -30.683   5.171  1.00 17.78           C  
ANISOU 1419  CA  LEU A 171     2006   2380   2370    -81    114     73       C  
ATOM   1420  C   LEU A 171      14.986 -31.973   5.361  1.00 19.01           C  
ANISOU 1420  C   LEU A 171     2168   2514   2542    -85    114     22       C  
ATOM   1421  O   LEU A 171      15.107 -32.769   4.428  1.00 17.55           O  
ANISOU 1421  O   LEU A 171     1969   2369   2329    -97    140      0       O  
ATOM   1422  CB  LEU A 171      12.689 -30.964   5.327  1.00 14.16           C  
ANISOU 1422  CB  LEU A 171     1568   1949   1862    -84    110     73       C  
ATOM   1423  CG  LEU A 171      12.188 -31.498   6.668  1.00 21.01           C  
ANISOU 1423  CG  LEU A 171     2476   2769   2738    -75     84     47       C  
ATOM   1424  CD1 LEU A 171      10.774 -30.977   6.939  1.00 18.92           C  
ANISOU 1424  CD1 LEU A 171     2225   2520   2445    -70     81     77       C  
ATOM   1425  CD2 LEU A 171      12.236 -33.022   6.671  1.00 17.94           C  
ANISOU 1425  CD2 LEU A 171     2097   2384   2334    -84     86     -4       C  
ATOM   1426  N   ARG A 172      15.530 -32.175   6.565  1.00 15.49           N  
ANISOU 1426  N   ARG A 172     1741   2005   2140    -75     86      5       N  
ATOM   1427  CA  ARG A 172      16.263 -33.398   6.882  1.00  8.69           C  
ANISOU 1427  CA  ARG A 172      884   1117   1301    -76     85    -36       C  
ATOM   1428  C   ARG A 172      15.857 -33.940   8.252  1.00  9.85           C  
ANISOU 1428  C   ARG A 172     1067   1219   1456    -68     53    -57       C  
ATOM   1429  O   ARG A 172      15.859 -33.202   9.249  1.00 14.38           O  
ANISOU 1429  O   ARG A 172     1659   1754   2052    -59     24    -40       O  
ATOM   1430  CB  ARG A 172      17.791 -33.164   6.859  1.00 12.87           C  
ANISOU 1430  CB  ARG A 172     1387   1613   1890    -72     85    -28       C  
ATOM   1431  CG  ARG A 172      18.349 -32.738   5.490  1.00 12.76           C  
ANISOU 1431  CG  ARG A 172     1335   1641   1872    -78    121     -8       C  
ATOM   1432  CD  ARG A 172      18.351 -33.886   4.507  1.00 16.06           C  
ANISOU 1432  CD  ARG A 172     1744   2100   2257    -88    159    -41       C  
ATOM   1433  NE  ARG A 172      18.917 -33.507   3.211  1.00 17.01           N  
ANISOU 1433  NE  ARG A 172     1831   2262   2370    -92    196    -22       N  
ATOM   1434  CZ  ARG A 172      18.201 -33.106   2.164  1.00 24.72           C  
ANISOU 1434  CZ  ARG A 172     2799   3304   3291   -102    218     -5       C  
ATOM   1435  NH1 ARG A 172      16.877 -33.016   2.241  1.00 20.57           N  
ANISOU 1435  NH1 ARG A 172     2293   2809   2715   -109    206     -2       N  
ATOM   1436  NH2 ARG A 172      18.808 -32.791   1.031  1.00 28.67           N  
ANISOU 1436  NH2 ARG A 172     3268   3841   3785   -105    253     13       N  
ATOM   1437  N   LEU A 173      15.525 -35.229   8.306  1.00 10.07           N  
ANISOU 1437  N   LEU A 173     1106   1253   1468    -72     61    -93       N  
ATOM   1438  CA  LEU A 173      15.258 -35.898   9.578  1.00 10.24           C  
ANISOU 1438  CA  LEU A 173     1157   1232   1501    -64     35   -112       C  
ATOM   1439  C   LEU A 173      16.592 -36.409  10.147  1.00 13.44           C  
ANISOU 1439  C   LEU A 173     1552   1590   1963    -58     22   -124       C  
ATOM   1440  O   LEU A 173      17.284 -37.206   9.507  1.00 15.81           O  
ANISOU 1440  O   LEU A 173     1831   1896   2280    -63     48   -143       O  
ATOM   1441  CB  LEU A 173      14.293 -37.065   9.377  1.00 10.25           C  
ANISOU 1441  CB  LEU A 173     1170   1258   1465    -71     49   -142       C  
ATOM   1442  CG  LEU A 173      13.771 -37.860  10.581  1.00 16.27           C  
ANISOU 1442  CG  LEU A 173     1963   1986   2232    -62     28   -159       C  
ATOM   1443  CD1 LEU A 173      13.079 -36.961  11.620  1.00 16.89           C  
ANISOU 1443  CD1 LEU A 173     2070   2045   2303    -49     -1   -132       C  
ATOM   1444  CD2 LEU A 173      12.817 -38.962  10.116  1.00 16.63           C  
ANISOU 1444  CD2 LEU A 173     2013   2063   2243    -74     48   -187       C  
ATOM   1445  N   ILE A 174      16.933 -35.962  11.350  1.00 13.88           N  
ANISOU 1445  N   ILE A 174     1625   1600   2048    -49    -15   -112       N  
ATOM   1446  CA  ILE A 174      18.231 -36.271  11.936  1.00 16.84           C  
ANISOU 1446  CA  ILE A 174     1987   1932   2479    -46    -34   -114       C  
ATOM   1447  C   ILE A 174      18.133 -37.093  13.221  1.00 16.21           C  
ANISOU 1447  C   ILE A 174     1933   1816   2410    -38    -62   -128       C  
ATOM   1448  O   ILE A 174      17.030 -37.453  13.662  1.00 15.92           O  
ANISOU 1448  O   ILE A 174     1925   1786   2338    -34    -65   -138       O  
ATOM   1449  CB  ILE A 174      18.991 -34.981  12.265  1.00 15.01           C  
ANISOU 1449  CB  ILE A 174     1748   1675   2279    -46    -60    -84       C  
ATOM   1450  CG1 ILE A 174      18.254 -34.179  13.346  1.00 13.87           C  
ANISOU 1450  CG1 ILE A 174     1644   1510   2116    -41    -94    -74       C  
ATOM   1451  CG2 ILE A 174      19.207 -34.142  10.997  1.00 14.38           C  
ANISOU 1451  CG2 ILE A 174     1638   1629   2196    -52    -31    -63       C  
ATOM   1452  CD1 ILE A 174      19.139 -33.101  14.005  1.00 17.54           C  
ANISOU 1452  CD1 ILE A 174     2109   1935   2620    -44   -129    -54       C  
ATOM   1453  N   ASP A 175      19.303 -37.373  13.799  1.00 13.87           N  
ANISOU 1453  N   ASP A 175     1621   1482   2165    -36    -83   -123       N  
ATOM   1454  CA  ASP A 175      19.466 -38.091  15.068  1.00 15.55           C  
ANISOU 1454  CA  ASP A 175     1851   1659   2397    -29   -115   -128       C  
ATOM   1455  C   ASP A 175      18.743 -39.432  15.112  1.00 11.90           C  
ANISOU 1455  C   ASP A 175     1399   1205   1918    -24    -94   -154       C  
ATOM   1456  O   ASP A 175      17.702 -39.577  15.760  1.00 14.24           O  
ANISOU 1456  O   ASP A 175     1728   1503   2179    -18   -104   -159       O  
ATOM   1457  CB  ASP A 175      19.065 -37.238  16.271  1.00 13.77           C  
ANISOU 1457  CB  ASP A 175     1665   1414   2155    -26   -159   -116       C  
ATOM   1458  CG  ASP A 175      19.668 -37.758  17.577  1.00 18.09           C  
ANISOU 1458  CG  ASP A 175     2222   1923   2729    -22   -200   -112       C  
ATOM   1459  OD1 ASP A 175      19.685 -37.009  18.566  1.00 25.06           O  
ANISOU 1459  OD1 ASP A 175     3132   2784   3604    -24   -240   -102       O  
ATOM   1460  OD2 ASP A 175      20.138 -38.913  17.612  1.00 17.02           O  
ANISOU 1460  OD2 ASP A 175     2066   1779   2624    -19   -191   -118       O  
ATOM   1461  N   TRP A 176      19.340 -40.404  14.436  1.00 10.44           N  
ANISOU 1461  N   TRP A 176     1183   1021   1762    -26    -62   -168       N  
ATOM   1462  CA  TRP A 176      18.835 -41.764  14.373  1.00 12.13           C  
ANISOU 1462  CA  TRP A 176     1400   1236   1972    -23    -36   -195       C  
ATOM   1463  C   TRP A 176      19.374 -42.616  15.510  1.00 14.74           C  
ANISOU 1463  C   TRP A 176     1729   1526   2347    -13    -59   -189       C  
ATOM   1464  O   TRP A 176      19.362 -43.848  15.441  1.00 16.33           O  
ANISOU 1464  O   TRP A 176     1920   1716   2568     -9    -34   -207       O  
ATOM   1465  CB  TRP A 176      19.167 -42.350  12.996  1.00  9.25           C  
ANISOU 1465  CB  TRP A 176     1006    893   1616    -31     17   -217       C  
ATOM   1466  CG  TRP A 176      18.482 -41.546  11.946  1.00 14.39           C  
ANISOU 1466  CG  TRP A 176     1661   1592   2215    -42     36   -220       C  
ATOM   1467  CD1 TRP A 176      18.866 -40.318  11.460  1.00 17.23           C  
ANISOU 1467  CD1 TRP A 176     2010   1968   2571    -46     31   -196       C  
ATOM   1468  CD2 TRP A 176      17.227 -41.849  11.323  1.00 15.90           C  
ANISOU 1468  CD2 TRP A 176     1868   1822   2350    -52     58   -242       C  
ATOM   1469  NE1 TRP A 176      17.936 -39.867  10.542  1.00 14.24           N  
ANISOU 1469  NE1 TRP A 176     1636   1637   2136    -56     52   -200       N  
ATOM   1470  CE2 TRP A 176      16.926 -40.788  10.441  1.00 14.83           C  
ANISOU 1470  CE2 TRP A 176     1728   1728   2178    -61     67   -228       C  
ATOM   1471  CE3 TRP A 176      16.346 -42.931  11.400  1.00 14.06           C  
ANISOU 1471  CE3 TRP A 176     1650   1594   2099    -56     72   -270       C  
ATOM   1472  CZ2 TRP A 176      15.770 -40.775   9.649  1.00 13.45           C  
ANISOU 1472  CZ2 TRP A 176     1562   1602   1944    -74     86   -239       C  
ATOM   1473  CZ3 TRP A 176      15.193 -42.915  10.614  1.00 18.70           C  
ANISOU 1473  CZ3 TRP A 176     2247   2227   2629    -70     89   -284       C  
ATOM   1474  CH2 TRP A 176      14.921 -41.848   9.750  1.00 17.10           C  
ANISOU 1474  CH2 TRP A 176     2039   2069   2388    -80     95   -268       C  
ATOM   1475  N   GLY A 177      19.826 -41.949  16.570  1.00 17.31           N  
ANISOU 1475  N   GLY A 177     2065   1827   2685     -9   -107   -163       N  
ATOM   1476  CA  GLY A 177      20.432 -42.618  17.708  1.00 16.98           C  
ANISOU 1476  CA  GLY A 177     2019   1750   2683     -1   -137   -148       C  
ATOM   1477  C   GLY A 177      19.475 -43.454  18.545  1.00 18.84           C  
ANISOU 1477  C   GLY A 177     2283   1980   2896      9   -143   -157       C  
ATOM   1478  O   GLY A 177      19.911 -44.324  19.301  1.00 18.10           O  
ANISOU 1478  O   GLY A 177     2179   1861   2837     18   -155   -147       O  
ATOM   1479  N   LEU A 178      18.176 -43.188  18.429  1.00 17.53           N  
ANISOU 1479  N   LEU A 178     2149   1837   2673      9   -134   -171       N  
ATOM   1480  CA  LEU A 178      17.176 -44.027  19.082  1.00 14.17           C  
ANISOU 1480  CA  LEU A 178     1747   1409   2228     19   -132   -178       C  
ATOM   1481  C   LEU A 178      16.451 -44.951  18.098  1.00 16.85           C  
ANISOU 1481  C   LEU A 178     2077   1767   2559     14    -83   -208       C  
ATOM   1482  O   LEU A 178      15.591 -45.722  18.500  1.00 16.89           O  
ANISOU 1482  O   LEU A 178     2096   1769   2551     20    -76   -216       O  
ATOM   1483  CB  LEU A 178      16.140 -43.183  19.843  1.00 12.31           C  
ANISOU 1483  CB  LEU A 178     1557   1181   1938     24   -158   -169       C  
ATOM   1484  CG  LEU A 178      16.645 -42.387  21.050  1.00 20.05           C  
ANISOU 1484  CG  LEU A 178     2560   2140   2918     28   -208   -146       C  
ATOM   1485  CD1 LEU A 178      15.481 -41.717  21.790  1.00 20.05           C  
ANISOU 1485  CD1 LEU A 178     2609   2146   2864     36   -222   -141       C  
ATOM   1486  CD2 LEU A 178      17.422 -43.291  21.978  1.00 26.37           C  
ANISOU 1486  CD2 LEU A 178     3347   2913   3759     35   -231   -132       C  
ATOM   1487  N   ALA A 179      16.798 -44.873  16.817  1.00 17.60           N  
ANISOU 1487  N   ALA A 179     2148   1882   2659      2    -49   -225       N  
ATOM   1488  CA  ALA A 179      16.089 -45.653  15.801  1.00 14.08           C  
ANISOU 1488  CA  ALA A 179     1696   1460   2196     -8     -4   -258       C  
ATOM   1489  C   ALA A 179      16.336 -47.147  15.967  1.00 18.29           C  
ANISOU 1489  C   ALA A 179     2213   1963   2773     -3     19   -275       C  
ATOM   1490  O   ALA A 179      17.405 -47.553  16.434  1.00 16.14           O  
ANISOU 1490  O   ALA A 179     1919   1658   2556      6     13   -261       O  
ATOM   1491  CB  ALA A 179      16.472 -45.189  14.394  1.00 12.10           C  
ANISOU 1491  CB  ALA A 179     1424   1238   1935    -23     26   -271       C  
ATOM   1492  N   GLU A 180      15.346 -47.962  15.602  1.00 12.77           N  
ANISOU 1492  N   GLU A 180     1522   1276   2054    -10     46   -303       N  
ATOM   1493  CA  GLU A 180      15.467 -49.428  15.702  1.00 16.10           C  
ANISOU 1493  CA  GLU A 180     1929   1668   2521     -7     74   -322       C  
ATOM   1494  C   GLU A 180      14.892 -50.126  14.483  1.00 16.88           C  
ANISOU 1494  C   GLU A 180     2023   1787   2602    -28    121   -368       C  
ATOM   1495  O   GLU A 180      14.079 -49.555  13.758  1.00 20.07           O  
ANISOU 1495  O   GLU A 180     2441   2235   2951    -44    124   -380       O  
ATOM   1496  CB  GLU A 180      14.714 -49.965  16.919  1.00 17.20           C  
ANISOU 1496  CB  GLU A 180     2087   1786   2661      7     51   -307       C  
ATOM   1497  CG  GLU A 180      15.579 -50.424  18.072  1.00 20.57           C  
ANISOU 1497  CG  GLU A 180     2502   2172   3143     26     30   -277       C  
ATOM   1498  CD  GLU A 180      16.343 -51.715  17.797  1.00 22.60           C  
ANISOU 1498  CD  GLU A 180     2724   2394   3468     29     68   -291       C  
ATOM   1499  OE1 GLU A 180      16.844 -52.301  18.774  1.00 27.51           O  
ANISOU 1499  OE1 GLU A 180     3334   2982   4137     45     54   -263       O  
ATOM   1500  OE2 GLU A 180      16.467 -52.142  16.629  1.00 21.15           O  
ANISOU 1500  OE2 GLU A 180     2526   2217   3293     14    114   -327       O  
ATOM   1501  N   PHE A 181      15.294 -51.378  14.284  1.00 15.58           N  
ANISOU 1501  N   PHE A 181     1840   1592   2487    -28    158   -392       N  
ATOM   1502  CA  PHE A 181      14.721 -52.217  13.242  1.00 14.19           C  
ANISOU 1502  CA  PHE A 181     1663   1429   2298    -50    203   -442       C  
ATOM   1503  C   PHE A 181      13.410 -52.827  13.748  1.00 14.12           C  
ANISOU 1503  C   PHE A 181     1673   1420   2271    -54    195   -449       C  
ATOM   1504  O   PHE A 181      13.343 -53.300  14.885  1.00 18.49           O  
ANISOU 1504  O   PHE A 181     2228   1939   2858    -34    177   -425       O  
ATOM   1505  CB  PHE A 181      15.702 -53.333  12.877  1.00 20.31           C  
ANISOU 1505  CB  PHE A 181     2412   2165   3141    -48    251   -467       C  
ATOM   1506  CG  PHE A 181      16.925 -52.851  12.149  1.00 15.72           C  
ANISOU 1506  CG  PHE A 181     1810   1587   2578    -48    271   -465       C  
ATOM   1507  CD1 PHE A 181      16.944 -52.809  10.760  1.00 14.82           C  
ANISOU 1507  CD1 PHE A 181     1694   1503   2432    -70    313   -505       C  
ATOM   1508  CD2 PHE A 181      18.051 -52.441  12.851  1.00 16.40           C  
ANISOU 1508  CD2 PHE A 181     1875   1645   2711    -27    248   -422       C  
ATOM   1509  CE1 PHE A 181      18.073 -52.365  10.077  1.00 18.59           C  
ANISOU 1509  CE1 PHE A 181     2151   1985   2928    -68    335   -501       C  
ATOM   1510  CE2 PHE A 181      19.184 -51.995  12.181  1.00 19.46           C  
ANISOU 1510  CE2 PHE A 181     2239   2034   3120    -26    267   -416       C  
ATOM   1511  CZ  PHE A 181      19.190 -51.964  10.783  1.00 17.85           C  
ANISOU 1511  CZ  PHE A 181     2034   1860   2886    -45    313   -455       C  
ATOM   1512  N   TYR A 182      12.377 -52.812  12.909  1.00 15.91           N  
ANISOU 1512  N   TYR A 182     1913   1686   2445    -79    207   -479       N  
ATOM   1513  CA  TYR A 182      11.121 -53.453  13.270  1.00 15.25           C  
ANISOU 1513  CA  TYR A 182     1844   1602   2349    -85    203   -486       C  
ATOM   1514  C   TYR A 182      11.122 -54.933  12.900  1.00 17.20           C  
ANISOU 1514  C   TYR A 182     2078   1817   2639    -98    247   -531       C  
ATOM   1515  O   TYR A 182      11.323 -55.307  11.737  1.00 16.00           O  
ANISOU 1515  O   TYR A 182     1921   1678   2480   -123    285   -577       O  
ATOM   1516  CB  TYR A 182       9.887 -52.753  12.672  1.00 18.00           C  
ANISOU 1516  CB  TYR A 182     2209   2007   2623   -107    189   -489       C  
ATOM   1517  CG  TYR A 182       8.618 -53.520  13.013  1.00 16.76           C  
ANISOU 1517  CG  TYR A 182     2061   1846   2461   -115    187   -496       C  
ATOM   1518  CD1 TYR A 182       8.076 -53.478  14.293  1.00 18.70           C  
ANISOU 1518  CD1 TYR A 182     2317   2071   2716    -90    158   -456       C  
ATOM   1519  CD2 TYR A 182       8.008 -54.340  12.076  1.00 19.91           C  
ANISOU 1519  CD2 TYR A 182     2457   2260   2847   -148    216   -543       C  
ATOM   1520  CE1 TYR A 182       6.926 -54.212  14.616  1.00 18.94           C  
ANISOU 1520  CE1 TYR A 182     2353   2096   2748    -96    159   -459       C  
ATOM   1521  CE2 TYR A 182       6.873 -55.068  12.388  1.00 19.00           C  
ANISOU 1521  CE2 TYR A 182     2347   2139   2734   -157    213   -549       C  
ATOM   1522  CZ  TYR A 182       6.342 -55.009  13.656  1.00 15.86           C  
ANISOU 1522  CZ  TYR A 182     1956   1719   2350   -130    186   -505       C  
ATOM   1523  OH  TYR A 182       5.210 -55.755  13.948  1.00 16.36           O  
ANISOU 1523  OH  TYR A 182     2022   1775   2420   -139    186   -507       O  
ATOM   1524  N   HIS A 183      10.895 -55.764  13.913  1.00 13.33           N  
ANISOU 1524  N   HIS A 183     1586   1284   2194    -81    242   -517       N  
ATOM   1525  CA  HIS A 183      10.777 -57.203  13.740  1.00 16.68           C  
ANISOU 1525  CA  HIS A 183     1999   1671   2668    -91    282   -554       C  
ATOM   1526  C   HIS A 183       9.438 -57.638  14.349  1.00 17.75           C  
ANISOU 1526  C   HIS A 183     2146   1805   2792    -93    266   -545       C  
ATOM   1527  O   HIS A 183       9.170 -57.366  15.526  1.00 19.91           O  
ANISOU 1527  O   HIS A 183     2427   2068   3070    -67    232   -497       O  
ATOM   1528  CB  HIS A 183      11.932 -57.925  14.429  1.00 19.80           C  
ANISOU 1528  CB  HIS A 183     2371   2007   3147    -64    299   -537       C  
ATOM   1529  CG  HIS A 183      13.278 -57.644  13.826  1.00 23.30           C  
ANISOU 1529  CG  HIS A 183     2796   2444   3612    -61    321   -544       C  
ATOM   1530  ND1 HIS A 183      13.671 -58.154  12.606  1.00 26.13           N  
ANISOU 1530  ND1 HIS A 183     3148   2802   3980    -83    374   -598       N  
ATOM   1531  CD2 HIS A 183      14.328 -56.924  14.288  1.00 23.44           C  
ANISOU 1531  CD2 HIS A 183     2802   2455   3648    -39    299   -503       C  
ATOM   1532  CE1 HIS A 183      14.900 -57.750  12.338  1.00 26.26           C  
ANISOU 1532  CE1 HIS A 183     3147   2811   4020    -72    386   -586       C  
ATOM   1533  NE2 HIS A 183      15.323 -57.004  13.343  1.00 23.62           N  
ANISOU 1533  NE2 HIS A 183     2807   2473   3693    -46    339   -529       N  
ATOM   1534  N   PRO A 184       8.596 -58.312  13.555  1.00 18.36           N  
ANISOU 1534  N   PRO A 184     2228   1894   2855   -126    290   -591       N  
ATOM   1535  CA  PRO A 184       7.261 -58.658  14.067  1.00 20.60           C  
ANISOU 1535  CA  PRO A 184     2519   2180   3127   -130    273   -579       C  
ATOM   1536  C   PRO A 184       7.382 -59.436  15.373  1.00 19.16           C  
ANISOU 1536  C   PRO A 184     2327   1942   3011    -98    270   -545       C  
ATOM   1537  O   PRO A 184       8.157 -60.394  15.429  1.00 17.53           O  
ANISOU 1537  O   PRO A 184     2102   1687   2872    -92    304   -562       O  
ATOM   1538  CB  PRO A 184       6.688 -59.564  12.972  1.00 21.55           C  
ANISOU 1538  CB  PRO A 184     2638   2306   3243   -173    308   -643       C  
ATOM   1539  CG  PRO A 184       7.460 -59.235  11.744  1.00 27.23           C  
ANISOU 1539  CG  PRO A 184     3358   3052   3937   -194    333   -683       C  
ATOM   1540  CD  PRO A 184       8.839 -58.861  12.209  1.00 20.53           C  
ANISOU 1540  CD  PRO A 184     2498   2176   3126   -160    335   -655       C  
ATOM   1541  N   GLY A 185       6.657 -59.016  16.406  1.00 20.23           N  
ANISOU 1541  N   GLY A 185     2474   2084   3130    -77    234   -496       N  
ATOM   1542  CA  GLY A 185       6.621 -59.738  17.664  1.00 22.19           C  
ANISOU 1542  CA  GLY A 185     2714   2285   3432    -47    230   -460       C  
ATOM   1543  C   GLY A 185       7.681 -59.319  18.661  1.00 23.51           C  
ANISOU 1543  C   GLY A 185     2877   2432   3622    -11    209   -414       C  
ATOM   1544  O   GLY A 185       7.686 -59.763  19.807  1.00 21.28           O  
ANISOU 1544  O   GLY A 185     2591   2120   3376     17    199   -374       O  
ATOM   1545  N   GLN A 186       8.587 -58.453  18.232  1.00 18.73           N  
ANISOU 1545  N   GLN A 186     2274   1846   2995    -11    201   -416       N  
ATOM   1546  CA  GLN A 186       9.681 -58.035  19.095  1.00 19.73           C  
ANISOU 1546  CA  GLN A 186     2395   1956   3145     18    178   -375       C  
ATOM   1547  C   GLN A 186       9.188 -57.026  20.131  1.00 21.94           C  
ANISOU 1547  C   GLN A 186     2701   2257   3376     38    130   -326       C  
ATOM   1548  O   GLN A 186       8.395 -56.136  19.816  1.00 21.24           O  
ANISOU 1548  O   GLN A 186     2635   2210   3226     28    114   -328       O  
ATOM   1549  CB  GLN A 186      10.816 -57.448  18.254  1.00 19.54           C  
ANISOU 1549  CB  GLN A 186     2361   1943   3119      8    186   -393       C  
ATOM   1550  CG  GLN A 186      12.121 -57.280  19.003  1.00 28.53           C  
ANISOU 1550  CG  GLN A 186     3484   3055   4300     33    170   -355       C  
ATOM   1551  CD  GLN A 186      13.309 -57.145  18.062  1.00 33.03           C  
ANISOU 1551  CD  GLN A 186     4033   3623   4894     24    196   -378       C  
ATOM   1552  OE1 GLN A 186      13.556 -58.021  17.227  1.00 36.94           O  
ANISOU 1552  OE1 GLN A 186     4511   4098   5426     10    244   -419       O  
ATOM   1553  NE2 GLN A 186      14.039 -56.042  18.182  1.00 31.62           N  
ANISOU 1553  NE2 GLN A 186     3858   3463   4695     30    165   -354       N  
ATOM   1554  N   GLU A 187       9.638 -57.182  21.371  1.00 18.90           N  
ANISOU 1554  N   GLU A 187     2313   1846   3020     67    108   -282       N  
ATOM   1555  CA  GLU A 187       9.313 -56.226  22.420  1.00 20.08           C  
ANISOU 1555  CA  GLU A 187     2492   2014   3124     86     64   -239       C  
ATOM   1556  C   GLU A 187      10.428 -55.194  22.529  1.00 21.68           C  
ANISOU 1556  C   GLU A 187     2698   2225   3313     91     36   -224       C  
ATOM   1557  O   GLU A 187      11.603 -55.555  22.590  1.00 23.77           O  
ANISOU 1557  O   GLU A 187     2937   2466   3627     95     39   -218       O  
ATOM   1558  CB  GLU A 187       9.109 -56.943  23.754  1.00 20.03           C  
ANISOU 1558  CB  GLU A 187     2484   1978   3147    113     54   -197       C  
ATOM   1559  CG  GLU A 187       7.947 -57.944  23.721  1.00 24.92           C  
ANISOU 1559  CG  GLU A 187     3099   2586   3784    110     81   -206       C  
ATOM   1560  CD  GLU A 187       7.559 -58.446  25.099  1.00 37.68           C  
ANISOU 1560  CD  GLU A 187     4719   4181   5415    139     68   -157       C  
ATOM   1561  OE1 GLU A 187       8.460 -58.672  25.935  1.00 39.16           O  
ANISOU 1561  OE1 GLU A 187     4895   4348   5634    159     54   -124       O  
ATOM   1562  OE2 GLU A 187       6.348 -58.617  25.345  1.00 41.74           O  
ANISOU 1562  OE2 GLU A 187     5246   4702   5910    142     73   -149       O  
ATOM   1563  N   TYR A 188      10.058 -53.914  22.539  1.00 15.11           N  
ANISOU 1563  N   TYR A 188     1895   1427   2419     88      9   -217       N  
ATOM   1564  CA  TYR A 188      11.038 -52.823  22.537  1.00 16.20           C  
ANISOU 1564  CA  TYR A 188     2038   1575   2543     88    -18   -207       C  
ATOM   1565  C   TYR A 188      11.037 -52.054  23.843  1.00 20.21           C  
ANISOU 1565  C   TYR A 188     2575   2083   3020    107    -62   -167       C  
ATOM   1566  O   TYR A 188      10.068 -52.094  24.586  1.00 20.21           O  
ANISOU 1566  O   TYR A 188     2599   2086   2993    120    -70   -149       O  
ATOM   1567  CB  TYR A 188      10.774 -51.860  21.379  1.00 20.55           C  
ANISOU 1567  CB  TYR A 188     2596   2163   3049     67    -11   -233       C  
ATOM   1568  CG  TYR A 188      10.938 -52.538  20.054  1.00 17.41           C  
ANISOU 1568  CG  TYR A 188     2172   1769   2675     45     31   -275       C  
ATOM   1569  CD1 TYR A 188      12.189 -52.652  19.486  1.00 20.03           C  
ANISOU 1569  CD1 TYR A 188     2478   2088   3045     39     45   -288       C  
ATOM   1570  CD2 TYR A 188       9.851 -53.117  19.397  1.00 14.15           C  
ANISOU 1570  CD2 TYR A 188     1760   1369   2247     29     58   -303       C  
ATOM   1571  CE1 TYR A 188      12.374 -53.289  18.296  1.00 22.63           C  
ANISOU 1571  CE1 TYR A 188     2786   2418   3393     20     88   -329       C  
ATOM   1572  CE2 TYR A 188      10.026 -53.767  18.182  1.00 16.03           C  
ANISOU 1572  CE2 TYR A 188     1978   1611   2503      5     97   -347       C  
ATOM   1573  CZ  TYR A 188      11.306 -53.845  17.646  1.00 16.47           C  
ANISOU 1573  CZ  TYR A 188     2011   1654   2593      2    114   -361       C  
ATOM   1574  OH  TYR A 188      11.541 -54.479  16.454  1.00 20.28           O  
ANISOU 1574  OH  TYR A 188     2477   2138   3091    -20    157   -407       O  
ATOM   1575  N   ASN A 189      12.133 -51.353  24.109  1.00 17.19           N  
ANISOU 1575  N   ASN A 189     2191   1699   2643    108    -91   -152       N  
ATOM   1576  CA  ASN A 189      12.237 -50.467  25.263  1.00 16.32           C  
ANISOU 1576  CA  ASN A 189     2113   1591   2498    121   -136   -121       C  
ATOM   1577  C   ASN A 189      11.219 -49.337  25.126  1.00 13.85           C  
ANISOU 1577  C   ASN A 189     1837   1305   2119    118   -141   -127       C  
ATOM   1578  O   ASN A 189      11.091 -48.747  24.054  1.00 19.45           O  
ANISOU 1578  O   ASN A 189     2543   2035   2813    102   -125   -150       O  
ATOM   1579  CB  ASN A 189      13.664 -49.901  25.305  1.00 21.42           C  
ANISOU 1579  CB  ASN A 189     2742   2229   3165    114   -163   -111       C  
ATOM   1580  CG  ASN A 189      13.932 -49.018  26.518  1.00 29.77           C  
ANISOU 1580  CG  ASN A 189     3833   3289   4191    122   -214    -82       C  
ATOM   1581  OD1 ASN A 189      13.101 -48.873  27.414  1.00 21.50           O  
ANISOU 1581  OD1 ASN A 189     2821   2244   3102    135   -227    -68       O  
ATOM   1582  ND2 ASN A 189      15.126 -48.436  26.556  1.00 36.70           N  
ANISOU 1582  ND2 ASN A 189     4697   4161   5085    112   -243    -73       N  
ATOM   1583  N   VAL A 190      10.485 -49.029  26.191  1.00 16.54           N  
ANISOU 1583  N   VAL A 190     2215   1647   2423    134   -159   -105       N  
ATOM   1584  CA  VAL A 190       9.501 -47.942  26.108  1.00 12.06           C  
ANISOU 1584  CA  VAL A 190     1684   1101   1799    135   -158   -106       C  
ATOM   1585  C   VAL A 190      10.115 -46.579  26.443  1.00 15.38           C  
ANISOU 1585  C   VAL A 190     2130   1524   2191    131   -191   -100       C  
ATOM   1586  O   VAL A 190       9.466 -45.544  26.304  1.00 20.86           O  
ANISOU 1586  O   VAL A 190     2851   2232   2844    131   -189   -102       O  
ATOM   1587  CB  VAL A 190       8.233 -48.208  26.976  1.00 15.67           C  
ANISOU 1587  CB  VAL A 190     2170   1557   2226    155   -152    -87       C  
ATOM   1588  CG1 VAL A 190       7.517 -49.486  26.524  1.00 17.61           C  
ANISOU 1588  CG1 VAL A 190     2390   1800   2502    154   -118    -95       C  
ATOM   1589  CG2 VAL A 190       8.596 -48.271  28.458  1.00 16.86           C  
ANISOU 1589  CG2 VAL A 190     2345   1691   2369    174   -183    -58       C  
ATOM   1590  N   ARG A 191      11.381 -46.586  26.864  1.00 16.73           N  
ANISOU 1590  N   ARG A 191     2288   1680   2389    128   -221    -92       N  
ATOM   1591  CA  ARG A 191      12.080 -45.351  27.209  1.00 22.31           C  
ANISOU 1591  CA  ARG A 191     3016   2386   3075    121   -256    -88       C  
ATOM   1592  C   ARG A 191      12.767 -44.729  25.995  1.00 21.88           C  
ANISOU 1592  C   ARG A 191     2934   2340   3039    101   -248   -106       C  
ATOM   1593  O   ARG A 191      14.004 -44.608  25.941  1.00 20.27           O  
ANISOU 1593  O   ARG A 191     2707   2126   2868     91   -269   -102       O  
ATOM   1594  CB  ARG A 191      13.085 -45.591  28.343  1.00 23.22           C  
ANISOU 1594  CB  ARG A 191     3132   2484   3206    124   -298    -65       C  
ATOM   1595  CG  ARG A 191      12.454 -46.138  29.620  1.00 29.76           C  
ANISOU 1595  CG  ARG A 191     3990   3307   4011    144   -308    -43       C  
ATOM   1596  CD  ARG A 191      13.455 -46.172  30.759  1.00 41.24           C  
ANISOU 1596  CD  ARG A 191     5450   4752   5470    144   -356    -18       C  
ATOM   1597  NE  ARG A 191      13.795 -44.826  31.209  1.00 51.04           N  
ANISOU 1597  NE  ARG A 191     6728   5994   6671    133   -392    -22       N  
ATOM   1598  CZ  ARG A 191      14.845 -44.533  31.970  1.00 59.55           C  
ANISOU 1598  CZ  ARG A 191     7809   7066   7751    122   -442     -7       C  
ATOM   1599  NH1 ARG A 191      15.671 -45.493  32.365  1.00 59.53           N  
ANISOU 1599  NH1 ARG A 191     7771   7058   7790    123   -460     19       N  
ATOM   1600  NH2 ARG A 191      15.075 -43.278  32.330  1.00 62.27           N  
ANISOU 1600  NH2 ARG A 191     8191   7410   8058    108   -472    -17       N  
ATOM   1601  N   VAL A 192      11.943 -44.335  25.029  1.00 17.93           N  
ANISOU 1601  N   VAL A 192     2435   1860   2518     95   -217   -121       N  
ATOM   1602  CA  VAL A 192      12.375 -43.648  23.830  1.00 17.11           C  
ANISOU 1602  CA  VAL A 192     2309   1770   2421     78   -205   -136       C  
ATOM   1603  C   VAL A 192      11.491 -42.413  23.645  1.00 19.79           C  
ANISOU 1603  C   VAL A 192     2679   2127   2714     78   -200   -134       C  
ATOM   1604  O   VAL A 192      10.457 -42.270  24.326  1.00 16.33           O  
ANISOU 1604  O   VAL A 192     2275   1688   2242     92   -198   -124       O  
ATOM   1605  CB  VAL A 192      12.229 -44.550  22.583  1.00 13.70           C  
ANISOU 1605  CB  VAL A 192     1839   1353   2012     69   -165   -156       C  
ATOM   1606  CG1 VAL A 192      13.139 -45.794  22.691  1.00 12.50           C  
ANISOU 1606  CG1 VAL A 192     1654   1179   1915     70   -162   -159       C  
ATOM   1607  CG2 VAL A 192      10.759 -44.966  22.400  1.00 16.11           C  
ANISOU 1607  CG2 VAL A 192     2158   1676   2289     73   -138   -162       C  
ATOM   1608  N   ALA A 193      11.899 -41.536  22.725  1.00 19.02           N  
ANISOU 1608  N   ALA A 193     2566   2041   2618     64   -195   -139       N  
ATOM   1609  CA  ALA A 193      11.188 -40.292  22.418  1.00 16.89           C  
ANISOU 1609  CA  ALA A 193     2317   1785   2313     63   -187   -133       C  
ATOM   1610  C   ALA A 193      11.255 -39.273  23.554  1.00 15.43           C  
ANISOU 1610  C   ALA A 193     2176   1578   2109     71   -217   -121       C  
ATOM   1611  O   ALA A 193      11.463 -39.619  24.724  1.00 19.31           O  
ANISOU 1611  O   ALA A 193     2691   2049   2597     80   -242   -117       O  
ATOM   1612  CB  ALA A 193       9.720 -40.582  22.037  1.00 18.06           C  
ANISOU 1612  CB  ALA A 193     2472   1957   2432     69   -155   -131       C  
ATOM   1613  N   SER A 194      11.107 -38.003  23.210  1.00 13.79           N  
ANISOU 1613  N   SER A 194     1979   1374   1886     66   -213   -117       N  
ATOM   1614  CA ASER A 194      11.015 -36.968  24.220  1.00 15.19           C  
ANISOU 1614  CA ASER A 194     2202   1528   2041     72   -234   -110       C  
ATOM   1615  CA BSER A 194      11.012 -36.959  24.217  0.00 17.17           C  
ANISOU 1615  CA BSER A 194     2453   1779   2293     72   -234   -110       C  
ATOM   1616  C   SER A 194       9.630 -37.015  24.851  1.00 17.31           C  
ANISOU 1616  C   SER A 194     2508   1797   2271     92   -215   -102       C  
ATOM   1617  O   SER A 194       8.655 -37.342  24.182  1.00 14.94           O  
ANISOU 1617  O   SER A 194     2194   1521   1962     97   -183    -96       O  
ATOM   1618  CB ASER A 194      11.242 -35.596  23.593  1.00 19.69           C  
ANISOU 1618  CB ASER A 194     2769   2098   2615     62   -229   -106       C  
ATOM   1619  CB BSER A 194      11.247 -35.583  23.594  0.00 19.96           C  
ANISOU 1619  CB BSER A 194     2803   2132   2649     62   -229   -106       C  
ATOM   1620  OG ASER A 194      10.557 -34.596  24.333  1.00 27.84           O  
ANISOU 1620  OG ASER A 194     3849   3112   3618     72   -228   -100       O  
ATOM   1621  OG BSER A 194      12.605 -35.405  23.235  0.00 19.92           O  
ANISOU 1621  OG BSER A 194     2768   2119   2681     45   -251   -111       O  
ATOM   1622  N   ARG A 195       9.553 -36.690  26.139  1.00 16.00           N  
ANISOU 1622  N   ARG A 195     2390   1608   2083    103   -235   -100       N  
ATOM   1623  CA  ARG A 195       8.296 -36.756  26.887  1.00 18.85           C  
ANISOU 1623  CA  ARG A 195     2790   1965   2407    125   -216    -90       C  
ATOM   1624  C   ARG A 195       7.057 -36.308  26.103  1.00 13.43           C  
ANISOU 1624  C   ARG A 195     2098   1297   1708    133   -174    -76       C  
ATOM   1625  O   ARG A 195       6.065 -37.027  26.056  1.00 13.56           O  
ANISOU 1625  O   ARG A 195     2110   1327   1714    145   -151    -66       O  
ATOM   1626  CB  ARG A 195       8.384 -35.945  28.184  1.00 19.55           C  
ANISOU 1626  CB  ARG A 195     2937   2025   2467    131   -237    -93       C  
ATOM   1627  CG  ARG A 195       7.106 -35.990  29.023  1.00 19.35           C  
ANISOU 1627  CG  ARG A 195     2955   1993   2403    157   -213    -81       C  
ATOM   1628  CD  ARG A 195       7.168 -34.972  30.155  1.00 23.67           C  
ANISOU 1628  CD  ARG A 195     3565   2512   2918    161   -226    -89       C  
ATOM   1629  NE  ARG A 195       8.430 -35.070  30.875  1.00 28.80           N  
ANISOU 1629  NE  ARG A 195     4224   3148   3569    145   -277   -103       N  
ATOM   1630  CZ  ARG A 195       9.040 -34.049  31.465  1.00 28.67           C  
ANISOU 1630  CZ  ARG A 195     4245   3108   3541    131   -302   -119       C  
ATOM   1631  NH1 ARG A 195       8.502 -32.833  31.440  1.00 23.38           N  
ANISOU 1631  NH1 ARG A 195     3608   2420   2856    135   -277   -124       N  
ATOM   1632  NH2 ARG A 195      10.188 -34.251  32.091  1.00 34.26           N  
ANISOU 1632  NH2 ARG A 195     4956   3809   4252    113   -353   -128       N  
ATOM   1633  N   TYR A 196       7.109 -35.119  25.508  1.00 16.27           N  
ANISOU 1633  N   TYR A 196     2455   1657   2071    125   -164    -73       N  
ATOM   1634  CA  TYR A 196       5.908 -34.519  24.903  1.00 15.08           C  
ANISOU 1634  CA  TYR A 196     2302   1522   1908    135   -125    -52       C  
ATOM   1635  C   TYR A 196       5.446 -35.275  23.656  1.00 14.31           C  
ANISOU 1635  C   TYR A 196     2154   1464   1819    126   -104    -44       C  
ATOM   1636  O   TYR A 196       4.301 -35.118  23.204  1.00 12.73           O  
ANISOU 1636  O   TYR A 196     1946   1284   1606    134    -74    -23       O  
ATOM   1637  CB  TYR A 196       6.151 -33.048  24.575  1.00 17.38           C  
ANISOU 1637  CB  TYR A 196     2599   1799   2204    129   -119    -46       C  
ATOM   1638  CG  TYR A 196       6.797 -32.313  25.717  1.00 21.19           C  
ANISOU 1638  CG  TYR A 196     3129   2240   2680    129   -144    -62       C  
ATOM   1639  CD1 TYR A 196       6.242 -32.350  26.990  1.00 20.98           C  
ANISOU 1639  CD1 TYR A 196     3157   2191   2623    147   -144    -64       C  
ATOM   1640  CD2 TYR A 196       7.989 -31.624  25.537  1.00 28.95           C  
ANISOU 1640  CD2 TYR A 196     4105   3209   3687    109   -170    -74       C  
ATOM   1641  CE1 TYR A 196       6.841 -31.693  28.048  1.00 24.20           C  
ANISOU 1641  CE1 TYR A 196     3613   2564   3019    143   -169    -82       C  
ATOM   1642  CE2 TYR A 196       8.600 -30.965  26.592  1.00 30.64           C  
ANISOU 1642  CE2 TYR A 196     4363   3385   3893    104   -198    -91       C  
ATOM   1643  CZ  TYR A 196       8.019 -31.003  27.843  1.00 30.86           C  
ANISOU 1643  CZ  TYR A 196     4447   3392   3885    120   -198    -97       C  
ATOM   1644  OH  TYR A 196       8.622 -30.349  28.895  1.00 32.91           O  
ANISOU 1644  OH  TYR A 196     4756   3618   4132    112   -227   -117       O  
ATOM   1645  N   PHE A 197       6.313 -36.145  23.150  1.00  9.74           N  
ANISOU 1645  N   PHE A 197     1541    897   1262    111   -119    -62       N  
ATOM   1646  CA  PHE A 197       6.071 -36.815  21.877  1.00 16.08           C  
ANISOU 1646  CA  PHE A 197     2298   1739   2073     97   -101    -64       C  
ATOM   1647  C   PHE A 197       5.928 -38.330  22.044  1.00 13.97           C  
ANISOU 1647  C   PHE A 197     2020   1477   1813     98   -101    -76       C  
ATOM   1648  O   PHE A 197       5.819 -39.057  21.064  1.00 11.77           O  
ANISOU 1648  O   PHE A 197     1705   1225   1543     84    -87    -85       O  
ATOM   1649  CB  PHE A 197       7.192 -36.445  20.897  1.00 15.93           C  
ANISOU 1649  CB  PHE A 197     2245   1731   2077     77   -107    -74       C  
ATOM   1650  CG  PHE A 197       7.339 -34.967  20.720  1.00 14.48           C  
ANISOU 1650  CG  PHE A 197     2069   1540   1893     76   -105    -59       C  
ATOM   1651  CD1 PHE A 197       6.569 -34.297  19.791  1.00 10.51           C  
ANISOU 1651  CD1 PHE A 197     1549   1066   1379     74    -78    -36       C  
ATOM   1652  CD2 PHE A 197       8.198 -34.234  21.536  1.00 14.96           C  
ANISOU 1652  CD2 PHE A 197     2156   1563   1964     77   -131    -65       C  
ATOM   1653  CE1 PHE A 197       6.665 -32.923  19.640  1.00 16.33           C  
ANISOU 1653  CE1 PHE A 197     2291   1793   2121     75    -72    -18       C  
ATOM   1654  CE2 PHE A 197       8.307 -32.865  21.398  1.00 14.59           C  
ANISOU 1654  CE2 PHE A 197     2117   1504   1922     75   -127    -53       C  
ATOM   1655  CZ  PHE A 197       7.528 -32.205  20.445  1.00 12.99           C  
ANISOU 1655  CZ  PHE A 197     1895   1328   1712     76    -95    -28       C  
ATOM   1656  N   LYS A 198       5.924 -38.797  23.296  1.00 13.64           N  
ANISOU 1656  N   LYS A 198     2008   1407   1768    114   -116    -77       N  
ATOM   1657  CA  LYS A 198       5.833 -40.229  23.578  1.00 13.40           C  
ANISOU 1657  CA  LYS A 198     1966   1375   1750    117   -117    -85       C  
ATOM   1658  C   LYS A 198       4.433 -40.683  23.244  1.00 16.42           C  
ANISOU 1658  C   LYS A 198     2343   1779   2118    122    -88    -72       C  
ATOM   1659  O   LYS A 198       3.488 -40.016  23.642  1.00 13.01           O  
ANISOU 1659  O   LYS A 198     1936   1346   1663    137    -76    -50       O  
ATOM   1660  CB  LYS A 198       6.083 -40.501  25.068  1.00 13.19           C  
ANISOU 1660  CB  LYS A 198     1976   1317   1718    134   -139    -81       C  
ATOM   1661  CG  LYS A 198       7.565 -40.506  25.478  1.00 10.01           C  
ANISOU 1661  CG  LYS A 198     1571    895   1339    126   -174    -93       C  
ATOM   1662  CD  LYS A 198       7.681 -40.482  26.992  1.00  8.55           C  
ANISOU 1662  CD  LYS A 198     1429    684   1135    142   -199    -84       C  
ATOM   1663  CE  LYS A 198       9.133 -40.252  27.434  1.00 10.62           C  
ANISOU 1663  CE  LYS A 198     1690    929   1415    129   -240    -92       C  
ATOM   1664  NZ  LYS A 198       9.975 -41.450  27.150  1.00 14.76           N  
ANISOU 1664  NZ  LYS A 198     2171   1454   1982    122   -248    -96       N  
ATOM   1665  N   GLY A 199       4.302 -41.803  22.530  1.00 12.98           N  
ANISOU 1665  N   GLY A 199     1873   1361   1699    109    -77    -86       N  
ATOM   1666  CA  GLY A 199       2.982 -42.349  22.208  1.00 11.79           C  
ANISOU 1666  CA  GLY A 199     1712   1230   1538    109    -54    -74       C  
ATOM   1667  C   GLY A 199       2.319 -42.946  23.440  1.00 14.45           C  
ANISOU 1667  C   GLY A 199     2075   1543   1872    133    -54    -58       C  
ATOM   1668  O   GLY A 199       2.987 -43.298  24.399  1.00 16.53           O  
ANISOU 1668  O   GLY A 199     2356   1780   2146    145    -71    -62       O  
ATOM   1669  N   PRO A 200       0.980 -43.048  23.433  1.00 10.74           N  
ANISOU 1669  N   PRO A 200     1606   1086   1388    141    -34    -35       N  
ATOM   1670  CA  PRO A 200       0.311 -43.720  24.549  1.00 12.28           C  
ANISOU 1670  CA  PRO A 200     1821   1260   1583    165    -29    -17       C  
ATOM   1671  C   PRO A 200       0.882 -45.125  24.802  1.00 13.89           C  
ANISOU 1671  C   PRO A 200     2009   1449   1821    161    -37    -36       C  
ATOM   1672  O   PRO A 200       0.897 -45.581  25.950  1.00 15.84           O  
ANISOU 1672  O   PRO A 200     2277   1672   2071    183    -43    -24       O  
ATOM   1673  CB  PRO A 200      -1.144 -43.797  24.074  1.00  8.24           C  
ANISOU 1673  CB  PRO A 200     1296    772   1064    164     -5      7       C  
ATOM   1674  CG  PRO A 200      -1.313 -42.571  23.242  1.00 14.32           C  
ANISOU 1674  CG  PRO A 200     2060   1567   1815    153      2     17       C  
ATOM   1675  CD  PRO A 200       0.028 -42.401  22.518  1.00 15.01           C  
ANISOU 1675  CD  PRO A 200     2132   1660   1912    131    -15    -17       C  
ATOM   1676  N   GLU A 201       1.371 -45.795  23.758  1.00 10.11           N  
ANISOU 1676  N   GLU A 201     1493    984   1366    135    -35    -65       N  
ATOM   1677  CA  GLU A 201       1.900 -47.140  23.944  1.00 12.28           C  
ANISOU 1677  CA  GLU A 201     1749   1239   1679    132    -36    -82       C  
ATOM   1678  C   GLU A 201       3.086 -47.133  24.921  1.00 14.93           C  
ANISOU 1678  C   GLU A 201     2101   1545   2026    146    -60    -82       C  
ATOM   1679  O   GLU A 201       3.215 -48.024  25.770  1.00 13.14           O  
ANISOU 1679  O   GLU A 201     1876   1296   1821    161    -64    -73       O  
ATOM   1680  CB  GLU A 201       2.281 -47.803  22.605  1.00 15.02           C  
ANISOU 1680  CB  GLU A 201     2056   1602   2048    100    -25   -118       C  
ATOM   1681  CG  GLU A 201       3.278 -47.031  21.735  1.00 12.17           C  
ANISOU 1681  CG  GLU A 201     1686   1257   1682     82    -31   -138       C  
ATOM   1682  CD  GLU A 201       2.589 -46.095  20.760  1.00 16.55           C  
ANISOU 1682  CD  GLU A 201     2235   1850   2202     67    -23   -132       C  
ATOM   1683  OE1 GLU A 201       1.789 -45.257  21.212  1.00 13.16           O  
ANISOU 1683  OE1 GLU A 201     1828   1427   1746     82    -23   -101       O  
ATOM   1684  OE2 GLU A 201       2.846 -46.196  19.545  1.00 13.80           O  
ANISOU 1684  OE2 GLU A 201     1861   1528   1854     41    -13   -156       O  
ATOM   1685  N   LEU A 202       3.943 -46.123  24.803  1.00 14.58           N  
ANISOU 1685  N   LEU A 202     2066   1503   1970    142    -77    -88       N  
ATOM   1686  CA  LEU A 202       5.064 -45.991  25.714  1.00 14.40           C  
ANISOU 1686  CA  LEU A 202     2059   1456   1955    151   -105    -86       C  
ATOM   1687  C   LEU A 202       4.571 -45.641  27.113  1.00 13.86           C  
ANISOU 1687  C   LEU A 202     2035   1373   1858    178   -116    -58       C  
ATOM   1688  O   LEU A 202       5.108 -46.120  28.111  1.00 14.22           O  
ANISOU 1688  O   LEU A 202     2091   1400   1912    190   -135    -49       O  
ATOM   1689  CB  LEU A 202       6.035 -44.909  25.226  1.00 14.75           C  
ANISOU 1689  CB  LEU A 202     2103   1506   1995    137   -122    -97       C  
ATOM   1690  CG  LEU A 202       6.452 -44.972  23.756  1.00 11.63           C  
ANISOU 1690  CG  LEU A 202     1670   1131   1619    112   -107   -122       C  
ATOM   1691  CD1 LEU A 202       7.373 -43.803  23.446  1.00 13.79           C  
ANISOU 1691  CD1 LEU A 202     1945   1407   1887    103   -124   -126       C  
ATOM   1692  CD2 LEU A 202       7.136 -46.309  23.442  1.00 14.66           C  
ANISOU 1692  CD2 LEU A 202     2018   1504   2048    103   -100   -140       C  
ATOM   1693  N   LEU A 203       3.552 -44.789  27.180  1.00 10.65           N  
ANISOU 1693  N   LEU A 203     1654    976   1415    187   -102    -44       N  
ATOM   1694  CA  LEU A 203       3.105 -44.252  28.458  1.00 11.46           C  
ANISOU 1694  CA  LEU A 203     1806   1065   1485    212   -107    -22       C  
ATOM   1695  C   LEU A 203       2.335 -45.294  29.267  1.00 14.34           C  
ANISOU 1695  C   LEU A 203     2175   1421   1853    233    -95      0       C  
ATOM   1696  O   LEU A 203       2.190 -45.172  30.482  1.00 13.07           O  
ANISOU 1696  O   LEU A 203     2052   1246   1668    256   -102     18       O  
ATOM   1697  CB  LEU A 203       2.260 -42.997  28.224  1.00 10.73           C  
ANISOU 1697  CB  LEU A 203     1737    982   1359    217    -90    -11       C  
ATOM   1698  CG  LEU A 203       3.019 -41.862  27.516  1.00 16.30           C  
ANISOU 1698  CG  LEU A 203     2439   1693   2061    199   -101    -27       C  
ATOM   1699  CD1 LEU A 203       2.074 -40.750  27.109  1.00 15.99           C  
ANISOU 1699  CD1 LEU A 203     2413   1665   2000    203    -76    -12       C  
ATOM   1700  CD2 LEU A 203       4.158 -41.327  28.381  1.00 16.19           C  
ANISOU 1700  CD2 LEU A 203     2455   1657   2040    199   -135    -37       C  
ATOM   1701  N   VAL A 204       1.835 -46.319  28.589  1.00 18.39           N  
ANISOU 1701  N   VAL A 204     2650   1942   2396    225    -76     -2       N  
ATOM   1702  CA  VAL A 204       1.150 -47.409  29.271  1.00 16.36           C  
ANISOU 1702  CA  VAL A 204     2389   1673   2152    243    -63     19       C  
ATOM   1703  C   VAL A 204       2.034 -48.646  29.348  1.00 18.17           C  
ANISOU 1703  C   VAL A 204     2588   1888   2427    237    -73      9       C  
ATOM   1704  O   VAL A 204       1.582 -49.712  29.772  1.00 17.81           O  
ANISOU 1704  O   VAL A 204     2530   1832   2405    249    -61     24       O  
ATOM   1705  CB  VAL A 204      -0.215 -47.756  28.610  1.00 10.98           C  
ANISOU 1705  CB  VAL A 204     1687   1007   1476    240    -32     29       C  
ATOM   1706  CG1 VAL A 204      -1.130 -46.542  28.617  1.00 16.54           C  
ANISOU 1706  CG1 VAL A 204     2420   1724   2142    250    -18     48       C  
ATOM   1707  CG2 VAL A 204      -0.022 -48.272  27.191  1.00 12.50           C  
ANISOU 1707  CG2 VAL A 204     1834   1216   1699    207    -25     -1       C  
ATOM   1708  N   ASP A 205       3.294 -48.494  28.938  1.00 14.79           N  
ANISOU 1708  N   ASP A 205     2145   1458   2015    220    -94    -14       N  
ATOM   1709  CA  ASP A 205       4.294 -49.546  29.095  1.00 15.82           C  
ANISOU 1709  CA  ASP A 205     2248   1572   2192    217   -104    -19       C  
ATOM   1710  C   ASP A 205       4.026 -50.758  28.190  1.00 22.82           C  
ANISOU 1710  C   ASP A 205     3089   2455   3125    202    -76    -37       C  
ATOM   1711  O   ASP A 205       4.309 -51.892  28.570  1.00 25.55           O  
ANISOU 1711  O   ASP A 205     3414   2781   3513    209    -72    -29       O  
ATOM   1712  CB  ASP A 205       4.357 -49.970  30.573  1.00 24.18           C  
ANISOU 1712  CB  ASP A 205     3328   2613   3245    243   -119     14       C  
ATOM   1713  CG  ASP A 205       5.636 -50.713  30.931  1.00 37.88           C  
ANISOU 1713  CG  ASP A 205     5039   4333   5022    242   -139     18       C  
ATOM   1714  OD1 ASP A 205       6.628 -50.624  30.171  1.00 36.53           O  
ANISOU 1714  OD1 ASP A 205     4842   4160   4876    221   -148     -5       O  
ATOM   1715  OD2 ASP A 205       5.647 -51.383  31.992  1.00 36.60           O  
ANISOU 1715  OD2 ASP A 205     4882   4159   4867    262   -147     48       O  
ATOM   1716  N   TYR A 206       3.491 -50.516  26.993  1.00 14.96           N  
ANISOU 1716  N   TYR A 206     2079   1480   2124    181    -58    -59       N  
ATOM   1717  CA  TYR A 206       3.277 -51.581  26.007  1.00 14.72           C  
ANISOU 1717  CA  TYR A 206     2011   1450   2134    161    -33    -85       C  
ATOM   1718  C   TYR A 206       4.460 -51.685  25.057  1.00 14.68           C  
ANISOU 1718  C   TYR A 206     1978   1444   2154    138    -32   -119       C  
ATOM   1719  O   TYR A 206       4.713 -50.761  24.293  1.00 15.31           O  
ANISOU 1719  O   TYR A 206     2061   1546   2209    123    -37   -135       O  
ATOM   1720  CB  TYR A 206       2.013 -51.320  25.182  1.00 15.52           C  
ANISOU 1720  CB  TYR A 206     2108   1577   2210    146    -14    -90       C  
ATOM   1721  CG  TYR A 206       1.659 -52.485  24.279  1.00 14.67           C  
ANISOU 1721  CG  TYR A 206     1965   1469   2139    122     10   -117       C  
ATOM   1722  CD1 TYR A 206       1.137 -53.666  24.806  1.00 18.65           C  
ANISOU 1722  CD1 TYR A 206     2457   1950   2680    132     24   -105       C  
ATOM   1723  CD2 TYR A 206       1.854 -52.412  22.905  1.00 15.70           C  
ANISOU 1723  CD2 TYR A 206     2075   1622   2267     89     20   -154       C  
ATOM   1724  CE1 TYR A 206       0.810 -54.738  23.983  1.00 16.60           C  
ANISOU 1724  CE1 TYR A 206     2166   1685   2456    107     47   -134       C  
ATOM   1725  CE2 TYR A 206       1.542 -53.477  22.078  1.00 13.49           C  
ANISOU 1725  CE2 TYR A 206     1767   1342   2018     64     42   -185       C  
ATOM   1726  CZ  TYR A 206       1.013 -54.634  22.621  1.00 15.11           C  
ANISOU 1726  CZ  TYR A 206     1962   1520   2261     72     55   -176       C  
ATOM   1727  OH  TYR A 206       0.697 -55.688  21.793  1.00 16.04           O  
ANISOU 1727  OH  TYR A 206     2052   1632   2410     44     78   -210       O  
ATOM   1728  N   GLN A 207       5.159 -52.820  25.077  1.00 15.08           N  
ANISOU 1728  N   GLN A 207     2001   1469   2259    136    -23   -129       N  
ATOM   1729  CA  GLN A 207       6.453 -52.926  24.396  1.00 18.49           C  
ANISOU 1729  CA  GLN A 207     2408   1894   2722    121    -22   -155       C  
ATOM   1730  C   GLN A 207       6.423 -53.393  22.943  1.00 18.69           C  
ANISOU 1730  C   GLN A 207     2407   1930   2764     91      9   -199       C  
ATOM   1731  O   GLN A 207       7.420 -53.232  22.225  1.00 16.10           O  
ANISOU 1731  O   GLN A 207     2063   1603   2451     78     13   -221       O  
ATOM   1732  CB  GLN A 207       7.391 -53.850  25.183  1.00 16.62           C  
ANISOU 1732  CB  GLN A 207     2154   1622   2540    136    -27   -139       C  
ATOM   1733  CG  GLN A 207       7.692 -53.387  26.591  1.00 18.90           C  
ANISOU 1733  CG  GLN A 207     2468   1904   2810    162    -62    -97       C  
ATOM   1734  CD  GLN A 207       8.671 -54.310  27.280  1.00 24.07           C  
ANISOU 1734  CD  GLN A 207     3097   2527   3520    174    -68    -76       C  
ATOM   1735  OE1 GLN A 207       8.278 -55.136  28.097  1.00 26.32           O  
ANISOU 1735  OE1 GLN A 207     3379   2795   3825    192    -63    -49       O  
ATOM   1736  NE2 GLN A 207       9.955 -54.196  26.928  1.00 20.65           N  
ANISOU 1736  NE2 GLN A 207     2642   2087   3116    165    -77    -84       N  
ATOM   1737  N   MET A 208       5.316 -53.989  22.503  1.00 15.20           N  
ANISOU 1737  N   MET A 208     1960   1496   2321     79     30   -212       N  
ATOM   1738  CA  MET A 208       5.269 -54.565  21.153  1.00 13.79           C  
ANISOU 1738  CA  MET A 208     1757   1326   2156     47     60   -258       C  
ATOM   1739  C   MET A 208       4.736 -53.552  20.140  1.00 14.19           C  
ANISOU 1739  C   MET A 208     1817   1425   2151     25     57   -272       C  
ATOM   1740  O   MET A 208       3.758 -53.813  19.417  1.00 15.06           O  
ANISOU 1740  O   MET A 208     1922   1557   2245      2     71   -289       O  
ATOM   1741  CB  MET A 208       4.452 -55.867  21.152  1.00 15.06           C  
ANISOU 1741  CB  MET A 208     1903   1467   2353     40     84   -269       C  
ATOM   1742  CG  MET A 208       4.778 -56.815  20.007  1.00 18.48           C  
ANISOU 1742  CG  MET A 208     2310   1891   2821     10    118   -321       C  
ATOM   1743  SD  MET A 208       3.933 -58.428  20.086  1.00 20.80           S  
ANISOU 1743  SD  MET A 208     2584   2150   3168      1    148   -337       S  
ATOM   1744  CE  MET A 208       4.650 -59.091  21.589  1.00 36.70           C  
ANISOU 1744  CE  MET A 208     4590   4111   5243     43    143   -292       C  
ATOM   1745  N   TYR A 209       5.378 -52.386  20.102  1.00 14.68           N  
ANISOU 1745  N   TYR A 209     1890   1502   2185     30     38   -262       N  
ATOM   1746  CA  TYR A 209       4.928 -51.287  19.249  1.00 15.47           C  
ANISOU 1746  CA  TYR A 209     1998   1647   2233     14     34   -265       C  
ATOM   1747  C   TYR A 209       5.668 -51.312  17.920  1.00 16.22           C  
ANISOU 1747  C   TYR A 209     2072   1760   2331    -14     52   -304       C  
ATOM   1748  O   TYR A 209       6.423 -52.245  17.657  1.00 13.40           O  
ANISOU 1748  O   TYR A 209     1696   1378   2017    -20     72   -331       O  
ATOM   1749  CB  TYR A 209       5.095 -49.934  19.959  1.00 11.07           C  
ANISOU 1749  CB  TYR A 209     1466   1095   1644     34      6   -230       C  
ATOM   1750  CG  TYR A 209       6.518 -49.567  20.373  1.00 13.55           C  
ANISOU 1750  CG  TYR A 209     1781   1388   1980     45    -10   -226       C  
ATOM   1751  CD1 TYR A 209       7.403 -49.025  19.461  1.00 14.76           C  
ANISOU 1751  CD1 TYR A 209     1920   1556   2132     30     -7   -244       C  
ATOM   1752  CD2 TYR A 209       6.945 -49.725  21.692  1.00 10.71           C  
ANISOU 1752  CD2 TYR A 209     1434    996   1638     71    -31   -201       C  
ATOM   1753  CE1 TYR A 209       8.693 -48.669  19.829  1.00 18.96           C  
ANISOU 1753  CE1 TYR A 209     2448   2067   2687     39    -24   -237       C  
ATOM   1754  CE2 TYR A 209       8.238 -49.362  22.079  1.00 16.38           C  
ANISOU 1754  CE2 TYR A 209     2150   1697   2375     77    -52   -195       C  
ATOM   1755  CZ  TYR A 209       9.109 -48.843  21.139  1.00 17.04           C  
ANISOU 1755  CZ  TYR A 209     2217   1793   2463     61    -48   -213       C  
ATOM   1756  OH  TYR A 209      10.390 -48.479  21.503  1.00 15.81           O  
ANISOU 1756  OH  TYR A 209     2056   1620   2331     66    -70   -203       O  
ATOM   1757  N   ASP A 210       5.446 -50.303  17.078  1.00 12.80           N  
ANISOU 1757  N   ASP A 210     1641   1368   1853    -29     49   -304       N  
ATOM   1758  CA  ASP A 210       5.954 -50.345  15.701  1.00 10.01           C  
ANISOU 1758  CA  ASP A 210     1270   1042   1493    -58     70   -341       C  
ATOM   1759  C   ASP A 210       6.120 -48.956  15.095  1.00 11.19           C  
ANISOU 1759  C   ASP A 210     1422   1229   1600    -63     60   -326       C  
ATOM   1760  O   ASP A 210       6.145 -47.958  15.816  1.00 12.61           O  
ANISOU 1760  O   ASP A 210     1619   1406   1768    -42     37   -291       O  
ATOM   1761  CB  ASP A 210       5.084 -51.258  14.813  1.00 10.75           C  
ANISOU 1761  CB  ASP A 210     1352   1155   1577    -89     93   -375       C  
ATOM   1762  CG  ASP A 210       3.615 -50.829  14.764  1.00 15.03           C  
ANISOU 1762  CG  ASP A 210     1902   1732   2075    -97     81   -351       C  
ATOM   1763  OD1 ASP A 210       3.333 -49.779  14.153  1.00 17.79           O  
ANISOU 1763  OD1 ASP A 210     2253   2126   2381   -106     73   -336       O  
ATOM   1764  OD2 ASP A 210       2.731 -51.551  15.298  1.00 15.69           O  
ANISOU 1764  OD2 ASP A 210     1988   1802   2173    -94     81   -344       O  
ATOM   1765  N   TYR A 211       6.242 -48.885  13.771  1.00 10.85           N  
ANISOU 1765  N   TYR A 211     1364   1223   1535    -91     78   -353       N  
ATOM   1766  CA  TYR A 211       6.354 -47.607  13.075  1.00 10.39           C  
ANISOU 1766  CA  TYR A 211     1304   1206   1437    -97     72   -337       C  
ATOM   1767  C   TYR A 211       5.315 -46.577  13.500  1.00 14.59           C  
ANISOU 1767  C   TYR A 211     1850   1758   1933    -86     51   -292       C  
ATOM   1768  O   TYR A 211       5.556 -45.372  13.441  1.00 10.36           O  
ANISOU 1768  O   TYR A 211     1319   1237   1381    -78     41   -266       O  
ATOM   1769  CB  TYR A 211       6.202 -47.816  11.562  1.00 11.86           C  
ANISOU 1769  CB  TYR A 211     1474   1440   1593   -133     96   -369       C  
ATOM   1770  CG  TYR A 211       6.921 -49.015  10.988  1.00  9.21           C  
ANISOU 1770  CG  TYR A 211     1126   1086   1287   -149    126   -421       C  
ATOM   1771  CD1 TYR A 211       8.311 -49.018  10.846  1.00 13.55           C  
ANISOU 1771  CD1 TYR A 211     1665   1612   1870   -140    140   -433       C  
ATOM   1772  CD2 TYR A 211       6.211 -50.139  10.560  1.00 11.36           C  
ANISOU 1772  CD2 TYR A 211     1396   1364   1557   -174    144   -457       C  
ATOM   1773  CE1 TYR A 211       8.967 -50.106  10.313  1.00 15.78           C  
ANISOU 1773  CE1 TYR A 211     1937   1875   2184   -152    175   -479       C  
ATOM   1774  CE2 TYR A 211       6.865 -51.238  10.017  1.00 14.27           C  
ANISOU 1774  CE2 TYR A 211     1755   1711   1955   -189    177   -508       C  
ATOM   1775  CZ  TYR A 211       8.247 -51.209   9.892  1.00 13.96           C  
ANISOU 1775  CZ  TYR A 211     1707   1648   1950   -177    195   -518       C  
ATOM   1776  OH  TYR A 211       8.917 -52.279   9.350  1.00 14.37           O  
ANISOU 1776  OH  TYR A 211     1749   1675   2035   -189    234   -567       O  
ATOM   1777  N   SER A 212       4.140 -47.054  13.888  1.00 11.20           N  
ANISOU 1777  N   SER A 212     1428   1331   1496    -87     49   -283       N  
ATOM   1778  CA  SER A 212       3.035 -46.160  14.224  1.00 12.21           C  
ANISOU 1778  CA  SER A 212     1567   1479   1592    -77     36   -240       C  
ATOM   1779  C   SER A 212       3.364 -45.212  15.393  1.00  8.63           C  
ANISOU 1779  C   SER A 212     1138    995   1147    -43     18   -205       C  
ATOM   1780  O   SER A 212       2.763 -44.149  15.512  1.00 11.13           O  
ANISOU 1780  O   SER A 212     1464   1327   1438    -33     11   -170       O  
ATOM   1781  CB  SER A 212       1.762 -46.964  14.481  1.00 12.26           C  
ANISOU 1781  CB  SER A 212     1574   1488   1597    -83     38   -235       C  
ATOM   1782  OG  SER A 212       1.961 -47.941  15.491  1.00 12.60           O  
ANISOU 1782  OG  SER A 212     1626   1482   1680    -65     38   -245       O  
ATOM   1783  N   LEU A 213       4.334 -45.573  16.233  1.00 11.37           N  
ANISOU 1783  N   LEU A 213     1494   1296   1529    -25     10   -215       N  
ATOM   1784  CA  LEU A 213       4.826 -44.625  17.252  1.00 10.76           C  
ANISOU 1784  CA  LEU A 213     1441   1192   1455      2    -11   -188       C  
ATOM   1785  C   LEU A 213       5.200 -43.272  16.632  1.00 14.81           C  
ANISOU 1785  C   LEU A 213     1951   1728   1948     -3    -14   -175       C  
ATOM   1786  O   LEU A 213       4.847 -42.213  17.162  1.00 11.80           O  
ANISOU 1786  O   LEU A 213     1590   1343   1551     12    -23   -144       O  
ATOM   1787  CB  LEU A 213       6.051 -45.190  17.975  1.00 11.77           C  
ANISOU 1787  CB  LEU A 213     1571   1278   1625     13    -22   -202       C  
ATOM   1788  CG  LEU A 213       6.723 -44.207  18.928  1.00 15.92           C  
ANISOU 1788  CG  LEU A 213     2119   1779   2152     33    -47   -180       C  
ATOM   1789  CD1 LEU A 213       5.835 -43.946  20.149  1.00 17.71           C  
ANISOU 1789  CD1 LEU A 213     2379   1988   2360     56    -58   -153       C  
ATOM   1790  CD2 LEU A 213       8.092 -44.747  19.354  1.00 14.74           C  
ANISOU 1790  CD2 LEU A 213     1960   1596   2044     37    -59   -193       C  
ATOM   1791  N   ASP A 214       5.927 -43.309  15.515  1.00 12.40           N  
ANISOU 1791  N   ASP A 214     1620   1445   1646    -24     -3   -196       N  
ATOM   1792  CA  ASP A 214       6.403 -42.087  14.861  1.00 13.58           C  
ANISOU 1792  CA  ASP A 214     1761   1616   1782    -29     -4   -182       C  
ATOM   1793  C   ASP A 214       5.228 -41.224  14.408  1.00 11.99           C  
ANISOU 1793  C   ASP A 214     1560   1453   1541    -33      2   -151       C  
ATOM   1794  O   ASP A 214       5.343 -40.003  14.304  1.00 11.26           O  
ANISOU 1794  O   ASP A 214     1470   1368   1441    -27     -2   -124       O  
ATOM   1795  CB  ASP A 214       7.278 -42.419  13.647  1.00 13.08           C  
ANISOU 1795  CB  ASP A 214     1670   1575   1726    -51     14   -211       C  
ATOM   1796  CG  ASP A 214       8.605 -43.068  14.031  1.00 15.36           C  
ANISOU 1796  CG  ASP A 214     1953   1823   2060    -45     11   -233       C  
ATOM   1797  OD1 ASP A 214       9.071 -42.892  15.179  1.00 14.00           O  
ANISOU 1797  OD1 ASP A 214     1797   1610   1912    -25    -11   -220       O  
ATOM   1798  OD2 ASP A 214       9.184 -43.755  13.163  1.00 14.88           O  
ANISOU 1798  OD2 ASP A 214     1871   1773   2012    -61     33   -263       O  
ATOM   1799  N   MET A 215       4.105 -41.866  14.120  1.00 11.39           N  
ANISOU 1799  N   MET A 215     1479   1402   1447    -44     11   -151       N  
ATOM   1800  CA  MET A 215       2.942 -41.139  13.630  1.00 10.59           C  
ANISOU 1800  CA  MET A 215     1371   1341   1311    -49     16   -116       C  
ATOM   1801  C   MET A 215       2.242 -40.373  14.764  1.00 11.69           C  
ANISOU 1801  C   MET A 215     1537   1454   1449    -20      9    -77       C  
ATOM   1802  O   MET A 215       1.737 -39.267  14.552  1.00 13.02           O  
ANISOU 1802  O   MET A 215     1704   1641   1602    -15     13    -40       O  
ATOM   1803  CB  MET A 215       1.988 -42.084  12.888  1.00 11.39           C  
ANISOU 1803  CB  MET A 215     1454   1481   1392    -76     26   -129       C  
ATOM   1804  CG  MET A 215       2.641 -42.790  11.694  1.00 16.78           C  
ANISOU 1804  CG  MET A 215     2114   2191   2068   -107     37   -172       C  
ATOM   1805  SD  MET A 215       3.507 -41.675  10.551  1.00 14.79           S  
ANISOU 1805  SD  MET A 215     1844   1978   1798   -118     45   -164       S  
ATOM   1806  CE  MET A 215       2.120 -40.845   9.765  1.00 15.01           C  
ANISOU 1806  CE  MET A 215     1854   2071   1778   -133     45   -115       C  
ATOM   1807  N   TRP A 216       2.221 -40.948  15.967  1.00 11.33           N  
ANISOU 1807  N   TRP A 216     1517   1366   1424      0      1    -83       N  
ATOM   1808  CA  TRP A 216       1.779 -40.193  17.130  1.00 11.21           C  
ANISOU 1808  CA  TRP A 216     1533   1319   1407     29     -4    -52       C  
ATOM   1809  C   TRP A 216       2.648 -38.945  17.312  1.00 12.59           C  
ANISOU 1809  C   TRP A 216     1720   1476   1586     39    -12    -43       C  
ATOM   1810  O   TRP A 216       2.144 -37.830  17.439  1.00 14.33           O  
ANISOU 1810  O   TRP A 216     1951   1699   1796     51     -5    -11       O  
ATOM   1811  CB  TRP A 216       1.812 -41.028  18.418  1.00  6.73           C  
ANISOU 1811  CB  TRP A 216      992    709    857     49    -13    -62       C  
ATOM   1812  CG  TRP A 216       1.405 -40.200  19.609  1.00 13.29           C  
ANISOU 1812  CG  TRP A 216     1860   1509   1679     79    -16    -33       C  
ATOM   1813  CD1 TRP A 216       2.226 -39.447  20.407  1.00  9.88           C  
ANISOU 1813  CD1 TRP A 216     1457   1044   1252     94    -30    -34       C  
ATOM   1814  CD2 TRP A 216       0.062 -39.969  20.087  1.00 13.28           C  
ANISOU 1814  CD2 TRP A 216     1873   1509   1663     96     -1      2       C  
ATOM   1815  NE1 TRP A 216       1.479 -38.794  21.368  1.00 14.93           N  
ANISOU 1815  NE1 TRP A 216     2131   1663   1877    119    -24     -7       N  
ATOM   1816  CE2 TRP A 216       0.153 -39.096  21.189  1.00 13.99           C  
ANISOU 1816  CE2 TRP A 216     2004   1564   1748    123     -4     17       C  
ATOM   1817  CE3 TRP A 216      -1.197 -40.434  19.701  1.00 11.54           C  
ANISOU 1817  CE3 TRP A 216     1634   1316   1434     91     14     23       C  
ATOM   1818  CZ2 TRP A 216      -0.972 -38.680  21.914  1.00 14.73           C  
ANISOU 1818  CZ2 TRP A 216     2122   1647   1829    147     14     52       C  
ATOM   1819  CZ3 TRP A 216      -2.320 -40.005  20.415  1.00 12.21           C  
ANISOU 1819  CZ3 TRP A 216     1739   1391   1510    115     29     62       C  
ATOM   1820  CH2 TRP A 216      -2.195 -39.146  21.511  1.00 16.29           C  
ANISOU 1820  CH2 TRP A 216     2298   1870   2022    145     31     76       C  
ATOM   1821  N   SER A 217       3.966 -39.147  17.330  1.00 10.21           N  
ANISOU 1821  N   SER A 217     1417   1157   1307     34    -25    -71       N  
ATOM   1822  CA  SER A 217       4.913 -38.038  17.478  1.00  8.02           C  
ANISOU 1822  CA  SER A 217     1147    861   1040     39    -36    -66       C  
ATOM   1823  C   SER A 217       4.679 -36.954  16.437  1.00 10.36           C  
ANISOU 1823  C   SER A 217     1423   1192   1322     29    -22    -42       C  
ATOM   1824  O   SER A 217       4.692 -35.769  16.758  1.00 10.59           O  
ANISOU 1824  O   SER A 217     1466   1205   1352     40    -22    -19       O  
ATOM   1825  CB  SER A 217       6.350 -38.561  17.383  1.00  7.89           C  
ANISOU 1825  CB  SER A 217     1118    829   1052     29    -49    -97       C  
ATOM   1826  OG  SER A 217       6.576 -39.521  18.396  1.00 12.32           O  
ANISOU 1826  OG  SER A 217     1695   1357   1628     40    -63   -112       O  
ATOM   1827  N   LEU A 218       4.455 -37.361  15.189  1.00 10.19           N  
ANISOU 1827  N   LEU A 218     1367   1218   1287      7     -8    -47       N  
ATOM   1828  CA  LEU A 218       4.193 -36.403  14.132  1.00  9.10           C  
ANISOU 1828  CA  LEU A 218     1204   1120   1132     -4      6    -19       C  
ATOM   1829  C   LEU A 218       2.903 -35.642  14.397  1.00 12.87           C  
ANISOU 1829  C   LEU A 218     1691   1606   1593     10     16     26       C  
ATOM   1830  O   LEU A 218       2.821 -34.441  14.126  1.00 12.97           O  
ANISOU 1830  O   LEU A 218     1698   1625   1607     15     24     59       O  
ATOM   1831  CB  LEU A 218       4.110 -37.091  12.767  1.00 11.20           C  
ANISOU 1831  CB  LEU A 218     1436   1442   1379    -32     17    -33       C  
ATOM   1832  CG  LEU A 218       3.924 -36.171  11.554  1.00 13.16           C  
ANISOU 1832  CG  LEU A 218     1654   1741   1606    -46     31     -3       C  
ATOM   1833  CD1 LEU A 218       5.199 -35.411  11.225  1.00 13.89           C  
ANISOU 1833  CD1 LEU A 218     1736   1823   1719    -46     30     -4       C  
ATOM   1834  CD2 LEU A 218       3.467 -36.973  10.342  1.00 11.86           C  
ANISOU 1834  CD2 LEU A 218     1462   1636   1409    -77     41    -16       C  
ATOM   1835  N   GLY A 219       1.898 -36.337  14.926  1.00 10.33           N  
ANISOU 1835  N   GLY A 219     1381   1282   1263     17     18     30       N  
ATOM   1836  CA  GLY A 219       0.635 -35.690  15.243  1.00 10.36           C  
ANISOU 1836  CA  GLY A 219     1392   1288   1254     32     31     75       C  
ATOM   1837  C   GLY A 219       0.850 -34.643  16.323  1.00 16.41           C  
ANISOU 1837  C   GLY A 219     2195   2004   2036     60     32     90       C  
ATOM   1838  O   GLY A 219       0.261 -33.563  16.273  1.00 15.04           O  
ANISOU 1838  O   GLY A 219     2021   1832   1861     72     48    130       O  
ATOM   1839  N   CYS A 220       1.695 -34.955  17.305  1.00 14.35           N  
ANISOU 1839  N   CYS A 220     1965   1698   1790     70     14     57       N  
ATOM   1840  CA  CYS A 220       2.011 -33.977  18.352  1.00 14.61           C  
ANISOU 1840  CA  CYS A 220     2037   1682   1832     92     11     63       C  
ATOM   1841  C   CYS A 220       2.660 -32.726  17.759  1.00 17.41           C  
ANISOU 1841  C   CYS A 220     2379   2038   2199     86     15     76       C  
ATOM   1842  O   CYS A 220       2.312 -31.603  18.148  1.00 12.24           O  
ANISOU 1842  O   CYS A 220     1742   1360   1548    101     28    102       O  
ATOM   1843  CB  CYS A 220       2.921 -34.577  19.430  1.00 12.75           C  
ANISOU 1843  CB  CYS A 220     1832   1405   1607     98    -14     27       C  
ATOM   1844  SG  CYS A 220       2.153 -35.883  20.408  1.00 14.03           S  
ANISOU 1844  SG  CYS A 220     2016   1555   1759    112    -16     20       S  
ATOM   1845  N   MET A 221       3.586 -32.925  16.816  1.00 11.13           N  
ANISOU 1845  N   MET A 221     1551   1267   1412     64      6     59       N  
ATOM   1846  CA  MET A 221       4.206 -31.805  16.102  1.00 12.81           C  
ANISOU 1846  CA  MET A 221     1743   1486   1638     57     11     75       C  
ATOM   1847  C   MET A 221       3.153 -30.992  15.338  1.00 15.26           C  
ANISOU 1847  C   MET A 221     2030   1830   1936     59     38    125       C  
ATOM   1848  O   MET A 221       3.132 -29.764  15.418  1.00 14.88           O  
ANISOU 1848  O   MET A 221     1986   1763   1903     69     50    152       O  
ATOM   1849  CB  MET A 221       5.305 -32.292  15.145  1.00 11.62           C  
ANISOU 1849  CB  MET A 221     1559   1360   1496     34      2     51       C  
ATOM   1850  CG  MET A 221       6.523 -32.873  15.863  1.00 12.35           C  
ANISOU 1850  CG  MET A 221     1668   1414   1611     33    -24     12       C  
ATOM   1851  SD  MET A 221       7.872 -33.232  14.701  1.00 18.58           S  
ANISOU 1851  SD  MET A 221     2414   2228   2419     11    -27     -9       S  
ATOM   1852  CE  MET A 221       8.013 -31.674  13.847  1.00 10.91           C  
ANISOU 1852  CE  MET A 221     1419   1273   1455      8    -11     30       C  
ATOM   1853  N   LEU A 222       2.299 -31.678  14.586  1.00 13.02           N  
ANISOU 1853  N   LEU A 222     1720   1598   1630     48     47    137       N  
ATOM   1854  CA  LEU A 222       1.253 -31.001  13.836  1.00 10.60           C  
ANISOU 1854  CA  LEU A 222     1386   1330   1310     47     70    190       C  
ATOM   1855  C   LEU A 222       0.375 -30.150  14.750  1.00 11.17           C  
ANISOU 1855  C   LEU A 222     1486   1366   1393     76     88    225       C  
ATOM   1856  O   LEU A 222       0.137 -28.973  14.469  1.00 14.19           O  
ANISOU 1856  O   LEU A 222     1857   1747   1788     84    107    267       O  
ATOM   1857  CB  LEU A 222       0.412 -31.998  13.039  1.00 13.21           C  
ANISOU 1857  CB  LEU A 222     1688   1719   1611     28     71    194       C  
ATOM   1858  CG  LEU A 222      -0.696 -31.382  12.184  1.00 10.03           C  
ANISOU 1858  CG  LEU A 222     1251   1368   1194     23     90    254       C  
ATOM   1859  CD1 LEU A 222      -0.140 -30.508  11.056  1.00 12.56           C  
ANISOU 1859  CD1 LEU A 222     1535   1723   1513     10     97    278       C  
ATOM   1860  CD2 LEU A 222      -1.555 -32.497  11.622  1.00 12.24           C  
ANISOU 1860  CD2 LEU A 222     1509   1698   1444      1     84    251       C  
ATOM   1861  N   ALA A 223      -0.100 -30.737  15.845  1.00 10.39           N  
ANISOU 1861  N   ALA A 223     1423   1235   1290     92     85    210       N  
ATOM   1862  CA  ALA A 223      -0.955 -30.004  16.772  1.00 11.50           C  
ANISOU 1862  CA  ALA A 223     1594   1337   1437    121    107    241       C  
ATOM   1863  C   ALA A 223      -0.255 -28.740  17.268  1.00 17.44           C  
ANISOU 1863  C   ALA A 223     2372   2040   2213    133    113    240       C  
ATOM   1864  O   ALA A 223      -0.869 -27.681  17.331  1.00 12.42           O  
ANISOU 1864  O   ALA A 223     1739   1391   1591    149    141    281       O  
ATOM   1865  CB  ALA A 223      -1.359 -30.880  17.938  1.00 11.81           C  
ANISOU 1865  CB  ALA A 223     1672   1347   1468    136    101    219       C  
ATOM   1866  N   SER A 224       1.032 -28.847  17.610  1.00 15.01           N  
ANISOU 1866  N   SER A 224     2082   1705   1915    124     87    195       N  
ATOM   1867  CA  SER A 224       1.777 -27.685  18.103  1.00 11.85           C  
ANISOU 1867  CA  SER A 224     1707   1256   1539    131     87    190       C  
ATOM   1868  C   SER A 224       1.906 -26.601  17.028  1.00 14.62           C  
ANISOU 1868  C   SER A 224     2017   1627   1909    124    105    227       C  
ATOM   1869  O   SER A 224       1.892 -25.410  17.334  1.00 19.99           O  
ANISOU 1869  O   SER A 224     2713   2271   2613    136    124    246       O  
ATOM   1870  CB  SER A 224       3.168 -28.090  18.637  1.00 14.67           C  
ANISOU 1870  CB  SER A 224     2085   1585   1904    119     50    137       C  
ATOM   1871  OG  SER A 224       4.081 -28.342  17.583  1.00 15.88           O  
ANISOU 1871  OG  SER A 224     2195   1771   2066     96     35    128       O  
ATOM   1872  N   MET A 225       2.008 -27.004  15.767  1.00 14.19           N  
ANISOU 1872  N   MET A 225     1905   1453   2035     42     41    352       N  
ATOM   1873  CA  MET A 225       2.169 -26.027  14.695  1.00 14.12           C  
ANISOU 1873  CA  MET A 225     1863   1430   2072     35     49    392       C  
ATOM   1874  C   MET A 225       0.835 -25.351  14.319  1.00 15.20           C  
ANISOU 1874  C   MET A 225     2014   1593   2167     58     70    385       C  
ATOM   1875  O   MET A 225       0.747 -24.119  14.290  1.00 17.67           O  
ANISOU 1875  O   MET A 225     2331   1871   2513     66     40    391       O  
ATOM   1876  CB  MET A 225       2.801 -26.675  13.457  1.00 14.89           C  
ANISOU 1876  CB  MET A 225     1910   1555   2193     10     95    437       C  
ATOM   1877  CG  MET A 225       4.240 -27.172  13.649  1.00 22.12           C  
ANISOU 1877  CG  MET A 225     2804   2439   3162    -15     74    454       C  
ATOM   1878  SD  MET A 225       4.731 -28.223  12.259  1.00 33.16           S  
ANISOU 1878  SD  MET A 225     4149   3886   4564    -39    138    498       S  
ATOM   1879  CE  MET A 225       6.376 -28.710  12.724  1.00 48.15           C  
ANISOU 1879  CE  MET A 225     6030   5742   6524    -65    103    510       C  
ATOM   1880  N   ILE A 226      -0.197 -26.141  14.042  1.00 15.33           N  
ANISOU 1880  N   ILE A 226     2040   1672   2113     67    120    372       N  
ATOM   1881  CA  ILE A 226      -1.472 -25.542  13.606  1.00 16.81           C  
ANISOU 1881  CA  ILE A 226     2238   1888   2259     88    144    367       C  
ATOM   1882  C   ILE A 226      -2.176 -24.755  14.713  1.00 16.32           C  
ANISOU 1882  C   ILE A 226     2224   1802   2175    116    100    326       C  
ATOM   1883  O   ILE A 226      -2.868 -23.782  14.427  1.00 20.69           O  
ANISOU 1883  O   ILE A 226     2784   2352   2725    131     98    328       O  
ATOM   1884  CB  ILE A 226      -2.440 -26.548  12.927  1.00 14.15           C  
ANISOU 1884  CB  ILE A 226     1897   1626   1853     92    211    366       C  
ATOM   1885  CG1 ILE A 226      -2.939 -27.603  13.922  1.00 14.27           C  
ANISOU 1885  CG1 ILE A 226     1948   1669   1806    102    214    324       C  
ATOM   1886  CG2 ILE A 226      -1.771 -27.188  11.710  1.00 15.37           C  
ANISOU 1886  CG2 ILE A 226     2002   1805   2033     67    255    409       C  
ATOM   1887  CD1 ILE A 226      -4.035 -28.491  13.350  1.00 13.53           C  
ANISOU 1887  CD1 ILE A 226     1854   1647   1641    109    276    319       C  
ATOM   1888  N   PHE A 227      -1.965 -25.153  15.966  1.00 13.74           N  
ANISOU 1888  N   PHE A 227     1930   1458   1834    123     65    290       N  
ATOM   1889  CA  PHE A 227      -2.565 -24.489  17.119  1.00 13.81           C  
ANISOU 1889  CA  PHE A 227     1985   1443   1820    150     20    248       C  
ATOM   1890  C   PHE A 227      -1.641 -23.462  17.771  1.00 19.51           C  
ANISOU 1890  C   PHE A 227     2713   2090   2611    149    -49    247       C  
ATOM   1891  O   PHE A 227      -2.064 -22.699  18.641  1.00 19.54           O  
ANISOU 1891  O   PHE A 227     2751   2067   2605    173    -91    216       O  
ATOM   1892  CB  PHE A 227      -2.999 -25.527  18.162  1.00 11.50           C  
ANISOU 1892  CB  PHE A 227     1726   1177   1464    162     22    207       C  
ATOM   1893  CG  PHE A 227      -4.121 -26.426  17.696  1.00 14.02           C  
ANISOU 1893  CG  PHE A 227     2048   1569   1709    170     83    202       C  
ATOM   1894  CD1 PHE A 227      -5.170 -25.916  16.952  1.00 13.31           C  
ANISOU 1894  CD1 PHE A 227     1958   1511   1590    183    116    209       C  
ATOM   1895  CD2 PHE A 227      -4.119 -27.778  18.001  1.00 12.26           C  
ANISOU 1895  CD2 PHE A 227     1830   1382   1446    163    108    189       C  
ATOM   1896  CE1 PHE A 227      -6.208 -26.746  16.519  1.00 14.19           C  
ANISOU 1896  CE1 PHE A 227     2071   1688   1634    189    172    204       C  
ATOM   1897  CE2 PHE A 227      -5.149 -28.608  17.578  1.00 14.53           C  
ANISOU 1897  CE2 PHE A 227     2120   1735   1668    169    163    184       C  
ATOM   1898  CZ  PHE A 227      -6.192 -28.086  16.837  1.00 16.01           C  
ANISOU 1898  CZ  PHE A 227     2305   1953   1826    182    195    192       C  
ATOM   1899  N   ARG A 228      -0.370 -23.464  17.385  1.00 20.12           N  
ANISOU 1899  N   ARG A 228     2755   2133   2755    122    -61    279       N  
ATOM   1900  CA  ARG A 228       0.575 -22.509  17.958  1.00 20.90           C  
ANISOU 1900  CA  ARG A 228     2857   2161   2925    119   -127    280       C  
ATOM   1901  C   ARG A 228       0.688 -22.704  19.461  1.00 17.92           C  
ANISOU 1901  C   ARG A 228     2522   1758   2530    134   -176    234       C  
ATOM   1902  O   ARG A 228       0.559 -21.758  20.242  1.00 21.09           O  
ANISOU 1902  O   ARG A 228     2951   2118   2944    153   -227    210       O  
ATOM   1903  CB  ARG A 228       0.147 -21.075  17.629  1.00 25.45           C  
ANISOU 1903  CB  ARG A 228     3434   2709   3526    132   -148    289       C  
ATOM   1904  CG  ARG A 228       0.269 -20.733  16.157  1.00 33.26           C  
ANISOU 1904  CG  ARG A 228     4377   3711   4548    115   -109    340       C  
ATOM   1905  CD  ARG A 228       1.722 -20.488  15.760  1.00 48.78           C  
ANISOU 1905  CD  ARG A 228     6304   5631   6601     86   -132    380       C  
ATOM   1906  NE  ARG A 228       1.849 -20.068  14.363  1.00 61.30           N  
ANISOU 1906  NE  ARG A 228     7845   7227   8220     72    -97    431       N  
ATOM   1907  CZ  ARG A 228       1.787 -18.804  13.947  1.00 62.73           C  
ANISOU 1907  CZ  ARG A 228     8015   7375   8443     76   -118    451       C  
ATOM   1908  NH1 ARG A 228       1.598 -17.820  14.819  1.00 64.73           N  
ANISOU 1908  NH1 ARG A 228     8301   7582   8710     95   -174    423       N  
ATOM   1909  NH2 ARG A 228       1.912 -18.521  12.656  1.00 57.33           N  
ANISOU 1909  NH2 ARG A 228     7289   6707   7788     62    -83    498       N  
ATOM   1910  N   LYS A 229       0.925 -23.947  19.862  1.00 17.11           N  
ANISOU 1910  N   LYS A 229     2423   1681   2397    125   -159    221       N  
ATOM   1911  CA  LYS A 229       1.167 -24.287  21.251  1.00 20.15           C  
ANISOU 1911  CA  LYS A 229     2843   2045   2768    136   -202    181       C  
ATOM   1912  C   LYS A 229       2.247 -25.366  21.267  1.00 22.32           C  
ANISOU 1912  C   LYS A 229     3096   2320   3065    109   -194    194       C  
ATOM   1913  O   LYS A 229       1.987 -26.513  20.920  1.00 18.46           O  
ANISOU 1913  O   LYS A 229     2598   1882   2534    101   -145    197       O  
ATOM   1914  CB  LYS A 229      -0.117 -24.779  21.925  1.00 20.49           C  
ANISOU 1914  CB  LYS A 229     2927   2135   2724    164   -184    139       C  
ATOM   1915  CG  LYS A 229       0.053 -25.099  23.410  1.00 21.54           C  
ANISOU 1915  CG  LYS A 229     3099   2249   2838    179   -229     95       C  
ATOM   1916  CD  LYS A 229      -1.237 -25.594  24.052  1.00 23.14           C  
ANISOU 1916  CD  LYS A 229     3340   2501   2953    208   -210     57       C  
ATOM   1917  CE  LYS A 229      -1.012 -25.933  25.523  1.00 27.67           C  
ANISOU 1917  CE  LYS A 229     3949   3055   3508    222   -254     16       C  
ATOM   1918  NZ  LYS A 229       0.195 -26.799  25.752  1.00 24.08           N  
ANISOU 1918  NZ  LYS A 229     3478   2584   3088    196   -262     25       N  
ATOM   1919  N   GLU A 230       3.467 -25.001  21.651  1.00 20.77           N  
ANISOU 1919  N   GLU A 230     2890   2066   2937     95   -242    202       N  
ATOM   1920  CA  GLU A 230       4.595 -25.935  21.553  1.00 23.03           C  
ANISOU 1920  CA  GLU A 230     3150   2347   3252     67   -236    221       C  
ATOM   1921  C   GLU A 230       5.279 -26.085  22.900  1.00 28.82           C  
ANISOU 1921  C   GLU A 230     3910   3040   4000     71   -291    189       C  
ATOM   1922  O   GLU A 230       5.840 -25.118  23.408  1.00 25.95           O  
ANISOU 1922  O   GLU A 230     3554   2617   3687     74   -348    185       O  
ATOM   1923  CB  GLU A 230       5.605 -25.452  20.496  1.00 30.20           C  
ANISOU 1923  CB  GLU A 230     4009   3227   4237     40   -234    272       C  
ATOM   1924  CG  GLU A 230       6.444 -26.562  19.819  1.00 30.77           C  
ANISOU 1924  CG  GLU A 230     4043   3322   4325     10   -196    303       C  
ATOM   1925  CD  GLU A 230       7.524 -27.142  20.731  1.00 30.89           C  
ANISOU 1925  CD  GLU A 230     4064   3306   4367     -2   -233    291       C  
ATOM   1926  OE1 GLU A 230       8.225 -26.363  21.408  1.00 33.35           O  
ANISOU 1926  OE1 GLU A 230     4385   3557   4730     -2   -292    284       O  
ATOM   1927  OE2 GLU A 230       7.673 -28.380  20.780  1.00 25.65           O  
ANISOU 1927  OE2 GLU A 230     3397   2677   3673    -12   -203    286       O  
ATOM   1928  N   PRO A 231       5.239 -27.302  23.481  1.00 27.48           N  
ANISOU 1928  N   PRO A 231     3754   2901   3785     70   -275    167       N  
ATOM   1929  CA  PRO A 231       4.599 -28.478  22.877  1.00 24.36           C  
ANISOU 1929  CA  PRO A 231     3350   2575   3332     65   -209    172       C  
ATOM   1930  C   PRO A 231       3.102 -28.487  23.165  1.00 20.10           C  
ANISOU 1930  C   PRO A 231     2844   2078   2714     95   -188    141       C  
ATOM   1931  O   PRO A 231       2.646 -27.744  24.036  1.00 20.97           O  
ANISOU 1931  O   PRO A 231     2990   2166   2812    120   -229    110       O  
ATOM   1932  CB  PRO A 231       5.279 -29.637  23.603  1.00 19.75           C  
ANISOU 1932  CB  PRO A 231     2770   1993   2739     54   -215    158       C  
ATOM   1933  CG  PRO A 231       5.509 -29.097  24.980  1.00 25.62           C  
ANISOU 1933  CG  PRO A 231     3551   2689   3492     72   -281    121       C  
ATOM   1934  CD  PRO A 231       5.831 -27.621  24.792  1.00 34.45           C  
ANISOU 1934  CD  PRO A 231     4663   3753   4672     74   -323    135       C  
ATOM   1935  N   PHE A 232       2.350 -29.324  22.453  1.00 14.29           N  
ANISOU 1935  N   PHE A 232     2099   1405   1927     93   -127    149       N  
ATOM   1936  CA  PHE A 232       0.908 -29.368  22.613  1.00 12.68           C  
ANISOU 1936  CA  PHE A 232     1924   1247   1649    120   -102    124       C  
ATOM   1937  C   PHE A 232       0.501 -30.085  23.912  1.00 16.65           C  
ANISOU 1937  C   PHE A 232     2466   1764   2096    138   -117     79       C  
ATOM   1938  O   PHE A 232      -0.226 -29.525  24.740  1.00 16.27           O  
ANISOU 1938  O   PHE A 232     2455   1710   2017    166   -144     47       O  
ATOM   1939  CB  PHE A 232       0.257 -30.016  21.377  1.00 14.34           C  
ANISOU 1939  CB  PHE A 232     2107   1517   1824    111    -31    149       C  
ATOM   1940  CG  PHE A 232      -1.254 -29.980  21.399  1.00 10.54           C  
ANISOU 1940  CG  PHE A 232     1651   1083   1270    137     -3    127       C  
ATOM   1941  CD1 PHE A 232      -1.927 -28.788  21.245  1.00 15.80           C  
ANISOU 1941  CD1 PHE A 232     2329   1737   1937    156    -15    125       C  
ATOM   1942  CD2 PHE A 232      -1.986 -31.137  21.582  1.00 15.46           C  
ANISOU 1942  CD2 PHE A 232     2287   1761   1826    143     36    110       C  
ATOM   1943  CE1 PHE A 232      -3.306 -28.746  21.277  1.00 14.01           C  
ANISOU 1943  CE1 PHE A 232     2126   1553   1644    181     10    105       C  
ATOM   1944  CE2 PHE A 232      -3.377 -31.101  21.613  1.00 21.47           C  
ANISOU 1944  CE2 PHE A 232     3072   2566   2521    167     61     91       C  
ATOM   1945  CZ  PHE A 232      -4.031 -29.904  21.464  1.00 20.03           C  
ANISOU 1945  CZ  PHE A 232     2900   2371   2338    186     48     88       C  
ATOM   1946  N   PHE A 233       0.969 -31.318  24.096  1.00 13.15           N  
ANISOU 1946  N   PHE A 233     2016   1340   1642    122   -100     79       N  
ATOM   1947  CA  PHE A 233       0.723 -32.031  25.340  1.00 10.24           C  
ANISOU 1947  CA  PHE A 233     1681    982   1226    137   -116     40       C  
ATOM   1948  C   PHE A 233       1.920 -31.792  26.249  1.00 17.59           C  
ANISOU 1948  C   PHE A 233     2619   1854   2210    131   -176     30       C  
ATOM   1949  O   PHE A 233       2.962 -32.425  26.099  1.00 15.32           O  
ANISOU 1949  O   PHE A 233     2308   1554   1959    105   -175     47       O  
ATOM   1950  CB  PHE A 233       0.546 -33.536  25.095  1.00  8.84           C  
ANISOU 1950  CB  PHE A 233     1494    859   1005    124    -66     43       C  
ATOM   1951  CG  PHE A 233      -0.637 -33.896  24.209  1.00 12.81           C  
ANISOU 1951  CG  PHE A 233     1990   1423   1454    130     -5     52       C  
ATOM   1952  CD1 PHE A 233      -1.951 -33.676  24.628  1.00 15.01           C  
ANISOU 1952  CD1 PHE A 233     2301   1732   1670    159      2     25       C  
ATOM   1953  CD2 PHE A 233      -0.426 -34.494  22.980  1.00  8.64           C  
ANISOU 1953  CD2 PHE A 233     1423    924    937    106     44     86       C  
ATOM   1954  CE1 PHE A 233      -3.034 -34.033  23.820  1.00 15.28           C  
ANISOU 1954  CE1 PHE A 233     2328   1823   1655    164     57     33       C  
ATOM   1955  CE2 PHE A 233      -1.495 -34.851  22.162  1.00 11.04           C  
ANISOU 1955  CE2 PHE A 233     1720   1285   1191    112     99     94       C  
ATOM   1956  CZ  PHE A 233      -2.807 -34.612  22.581  1.00 14.96           C  
ANISOU 1956  CZ  PHE A 233     2249   1810   1627    140    106     67       C  
ATOM   1957  N   HIS A 234       1.758 -30.871  27.191  1.00 19.36           N  
ANISOU 1957  N   HIS A 234     2876   2041   2438    154   -228      2       N  
ATOM   1958  CA  HIS A 234       2.869 -30.352  27.983  1.00 16.77           C  
ANISOU 1958  CA  HIS A 234     2554   1650   2168    150   -291     -6       C  
ATOM   1959  C   HIS A 234       2.868 -30.973  29.384  1.00 19.59           C  
ANISOU 1959  C   HIS A 234     2948   2008   2490    166   -320    -47       C  
ATOM   1960  O   HIS A 234       2.524 -30.311  30.368  1.00 20.42           O  
ANISOU 1960  O   HIS A 234     3088   2090   2581    194   -364    -80       O  
ATOM   1961  CB  HIS A 234       2.719 -28.831  28.068  1.00 25.39           C  
ANISOU 1961  CB  HIS A 234     3657   2697   3292    167   -334    -11       C  
ATOM   1962  CG  HIS A 234       3.993 -28.100  28.362  1.00 32.21           C  
ANISOU 1962  CG  HIS A 234     4512   3491   4237    155   -391     -2       C  
ATOM   1963  ND1 HIS A 234       5.040 -28.668  29.055  1.00 40.96           N  
ANISOU 1963  ND1 HIS A 234     5620   4572   5372    141   -420     -8       N  
ATOM   1964  CD2 HIS A 234       4.387 -26.841  28.053  1.00 35.70           C  
ANISOU 1964  CD2 HIS A 234     4943   3882   4738    153   -426     14       C  
ATOM   1965  CE1 HIS A 234       6.021 -27.789  29.167  1.00 38.12           C  
ANISOU 1965  CE1 HIS A 234     5250   4149   5084    132   -470      2       C  
ATOM   1966  NE2 HIS A 234       5.649 -26.672  28.568  1.00 36.86           N  
ANISOU 1966  NE2 HIS A 234     5084   3974   4947    139   -475     16       N  
ATOM   1967  N   GLY A 235       3.249 -32.246  29.476  1.00 16.45           N  
ANISOU 1967  N   GLY A 235     2540   1635   2076    150   -295    -44       N  
ATOM   1968  CA  GLY A 235       3.246 -32.942  30.750  1.00 14.75           C  
ANISOU 1968  CA  GLY A 235     2356   1425   1825    163   -317    -80       C  
ATOM   1969  C   GLY A 235       4.442 -32.601  31.621  1.00 16.45           C  
ANISOU 1969  C   GLY A 235     2577   1578   2095    158   -379    -90       C  
ATOM   1970  O   GLY A 235       5.509 -32.280  31.110  1.00 16.97           O  
ANISOU 1970  O   GLY A 235     2613   1604   2229    134   -394    -62       O  
ATOM   1971  N   HIS A 236       4.270 -32.701  32.934  1.00 15.67           N  
ANISOU 1971  N   HIS A 236     2516   1473   1966    181   -416   -130       N  
ATOM   1972  CA  HIS A 236       5.350 -32.390  33.873  1.00 22.36           C  
ANISOU 1972  CA  HIS A 236     3373   2263   2861    180   -478   -144       C  
ATOM   1973  C   HIS A 236       6.243 -33.596  34.155  1.00 22.53           C  
ANISOU 1973  C   HIS A 236     3381   2287   2890    157   -471   -139       C  
ATOM   1974  O   HIS A 236       7.393 -33.449  34.608  1.00 22.88           O  
ANISOU 1974  O   HIS A 236     3421   2283   2989    145   -514   -139       O  
ATOM   1975  CB  HIS A 236       4.771 -31.824  35.169  1.00 29.40           C  
ANISOU 1975  CB  HIS A 236     4311   3141   3718    218   -524   -189       C  
ATOM   1976  CG  HIS A 236       4.039 -30.531  34.974  1.00 51.58           C  
ANISOU 1976  CG  HIS A 236     7134   5937   6528    241   -541   -195       C  
ATOM   1977  ND1 HIS A 236       4.618 -29.435  34.370  1.00 62.08           N  
ANISOU 1977  ND1 HIS A 236     8444   7217   7925    230   -566   -173       N  
ATOM   1978  CD2 HIS A 236       2.774 -30.162  35.291  1.00 55.16           C  
ANISOU 1978  CD2 HIS A 236     7617   6419   6922    275   -535   -220       C  
ATOM   1979  CE1 HIS A 236       3.744 -28.444  34.328  1.00 61.33           C  
ANISOU 1979  CE1 HIS A 236     8368   7122   7814    255   -576   -185       C  
ATOM   1980  NE2 HIS A 236       2.618 -28.859  34.881  1.00 58.45           N  
ANISOU 1980  NE2 HIS A 236     8033   6804   7372    283   -557   -214       N  
ATOM   1981  N   ASP A 237       5.694 -34.782  33.894  1.00 17.22           N  
ANISOU 1981  N   ASP A 237     2705   1674   2165    152   -418   -137       N  
ATOM   1982  CA  ASP A 237       6.420 -36.047  33.944  1.00 20.94           C  
ANISOU 1982  CA  ASP A 237     3159   2158   2639    128   -399   -128       C  
ATOM   1983  C   ASP A 237       5.661 -37.052  33.071  1.00 16.97           C  
ANISOU 1983  C   ASP A 237     2640   1721   2088    119   -329   -111       C  
ATOM   1984  O   ASP A 237       4.667 -36.691  32.458  1.00 19.66           O  
ANISOU 1984  O   ASP A 237     2980   2090   2397    130   -299   -106       O  
ATOM   1985  CB  ASP A 237       6.572 -36.560  35.387  1.00 22.73           C  
ANISOU 1985  CB  ASP A 237     3418   2379   2839    144   -434   -165       C  
ATOM   1986  CG  ASP A 237       5.234 -36.767  36.090  1.00 28.60           C  
ANISOU 1986  CG  ASP A 237     4199   3167   3502    178   -423   -198       C  
ATOM   1987  OD1 ASP A 237       4.278 -37.248  35.447  1.00 22.27           O  
ANISOU 1987  OD1 ASP A 237     3391   2418   2652    180   -370   -189       O  
ATOM   1988  OD2 ASP A 237       5.143 -36.458  37.298  1.00 28.84           O  
ANISOU 1988  OD2 ASP A 237     4264   3179   3516    204   -468   -232       O  
ATOM   1989  N   ASN A 238       6.113 -38.303  33.021  1.00 13.50           N  
ANISOU 1989  N   ASN A 238     2185   1304   1640     99   -303   -103       N  
ATOM   1990  CA  ASN A 238       5.502 -39.277  32.106  1.00 16.39           C  
ANISOU 1990  CA  ASN A 238     2532   1730   1968     87   -237    -85       C  
ATOM   1991  C   ASN A 238       4.082 -39.683  32.496  1.00 14.78           C  
ANISOU 1991  C   ASN A 238     2356   1578   1681    113   -211   -110       C  
ATOM   1992  O   ASN A 238       3.308 -40.145  31.651  1.00 16.78           O  
ANISOU 1992  O   ASN A 238     2596   1880   1899    110   -158    -96       O  
ATOM   1993  CB  ASN A 238       6.392 -40.515  31.925  1.00 20.71           C  
ANISOU 1993  CB  ASN A 238     3055   2285   2530     59   -217    -69       C  
ATOM   1994  CG  ASN A 238       7.712 -40.188  31.236  1.00 18.83           C  
ANISOU 1994  CG  ASN A 238     2781   2004   2370     30   -230    -36       C  
ATOM   1995  OD1 ASN A 238       7.833 -39.172  30.551  1.00 20.39           O  
ANISOU 1995  OD1 ASN A 238     2963   2177   2606     27   -237    -17       O  
ATOM   1996  ND2 ASN A 238       8.710 -41.050  31.420  1.00 21.74           N  
ANISOU 1996  ND2 ASN A 238     3135   2363   2763      9   -234    -29       N  
ATOM   1997  N   TYR A 239       3.742 -39.518  33.770  1.00 17.18           N  
ANISOU 1997  N   TYR A 239     2698   1875   1955    140   -247   -146       N  
ATOM   1998  CA  TYR A 239       2.401 -39.842  34.241  1.00 16.32           C  
ANISOU 1998  CA  TYR A 239     2618   1815   1768    167   -227   -171       C  
ATOM   1999  C   TYR A 239       1.461 -38.710  33.863  1.00 15.05           C  
ANISOU 1999  C   TYR A 239     2468   1657   1593    189   -225   -173       C  
ATOM   2000  O   TYR A 239       0.414 -38.932  33.245  1.00 14.74           O  
ANISOU 2000  O   TYR A 239     2426   1666   1509    195   -180   -167       O  
ATOM   2001  CB  TYR A 239       2.409 -40.089  35.747  1.00 15.78           C  
ANISOU 2001  CB  TYR A 239     2585   1739   1672    189   -266   -207       C  
ATOM   2002  CG  TYR A 239       3.456 -41.106  36.118  1.00 27.93           C  
ANISOU 2002  CG  TYR A 239     4112   3267   3232    167   -273   -204       C  
ATOM   2003  CD1 TYR A 239       3.340 -42.421  35.703  1.00 29.10           C  
ANISOU 2003  CD1 TYR A 239     4244   3460   3354    149   -225   -191       C  
ATOM   2004  CD2 TYR A 239       4.581 -40.744  36.839  1.00 31.18           C  
ANISOU 2004  CD2 TYR A 239     4529   3624   3694    163   -326   -213       C  
ATOM   2005  CE1 TYR A 239       4.306 -43.359  36.015  1.00 32.55           C  
ANISOU 2005  CE1 TYR A 239     4669   3888   3811    128   -230   -187       C  
ATOM   2006  CE2 TYR A 239       5.554 -41.674  37.155  1.00 36.96           C  
ANISOU 2006  CE2 TYR A 239     5250   4348   4447    142   -331   -208       C  
ATOM   2007  CZ  TYR A 239       5.408 -42.983  36.740  1.00 36.84           C  
ANISOU 2007  CZ  TYR A 239     5218   4378   4403    125   -282   -196       C  
ATOM   2008  OH  TYR A 239       6.367 -43.924  37.048  1.00 35.98           O  
ANISOU 2008  OH  TYR A 239     5097   4259   4313    104   -287   -192       O  
ATOM   2009  N   ASP A 240       1.868 -37.489  34.192  1.00 14.82           N  
ANISOU 2009  N   ASP A 240     2448   1576   1606    199   -275   -180       N  
ATOM   2010  CA  ASP A 240       1.081 -36.325  33.845  1.00 12.58           C  
ANISOU 2010  CA  ASP A 240     2174   1289   1316    219   -279   -182       C  
ATOM   2011  C   ASP A 240       0.957 -36.226  32.324  1.00 12.39           C  
ANISOU 2011  C   ASP A 240     2114   1282   1312    197   -232   -144       C  
ATOM   2012  O   ASP A 240      -0.039 -35.736  31.814  1.00 16.24           O  
ANISOU 2012  O   ASP A 240     2606   1795   1770    211   -209   -142       O  
ATOM   2013  CB  ASP A 240       1.707 -35.058  34.429  1.00 16.75           C  
ANISOU 2013  CB  ASP A 240     2717   1753   1896    230   -345   -195       C  
ATOM   2014  CG  ASP A 240       0.847 -33.831  34.232  1.00 19.21           C  
ANISOU 2014  CG  ASP A 240     3043   2058   2197    255   -355   -201       C  
ATOM   2015  OD1 ASP A 240      -0.329 -33.830  34.655  1.00 19.42           O  
ANISOU 2015  OD1 ASP A 240     3097   2122   2160    284   -343   -225       O  
ATOM   2016  OD2 ASP A 240       1.344 -32.856  33.644  1.00 20.11           O  
ANISOU 2016  OD2 ASP A 240     3141   2132   2369    245   -373   -183       O  
ATOM   2017  N   GLN A 241       1.957 -36.710  31.602  1.00  8.86           N  
ANISOU 2017  N   GLN A 241     1631    824    912    164   -217   -114       N  
ATOM   2018  CA  GLN A 241       1.888 -36.689  30.144  1.00 11.71           C  
ANISOU 2018  CA  GLN A 241     1956   1204   1291    144   -171    -76       C  
ATOM   2019  C   GLN A 241       0.636 -37.455  29.689  1.00 15.44           C  
ANISOU 2019  C   GLN A 241     2430   1745   1692    151   -112    -77       C  
ATOM   2020  O   GLN A 241      -0.116 -36.980  28.842  1.00 16.94           O  
ANISOU 2020  O   GLN A 241     2611   1956   1869    156    -83    -64       O  
ATOM   2021  CB  GLN A 241       3.156 -37.281  29.527  1.00 11.55           C  
ANISOU 2021  CB  GLN A 241     1897   1166   1325    108   -161    -45       C  
ATOM   2022  CG  GLN A 241       3.224 -37.165  27.999  1.00 10.08           C  
ANISOU 2022  CG  GLN A 241     1670    995   1164     87   -118     -4       C  
ATOM   2023  CD  GLN A 241       3.294 -35.719  27.517  1.00 15.13           C  
ANISOU 2023  CD  GLN A 241     2302   1596   1848     91   -141     10       C  
ATOM   2024  OE1 GLN A 241       3.742 -34.843  28.238  1.00 14.33           O  
ANISOU 2024  OE1 GLN A 241     2218   1445   1781    101   -195     -4       O  
ATOM   2025  NE2 GLN A 241       2.866 -35.477  26.283  1.00 15.43           N  
ANISOU 2025  NE2 GLN A 241     2315   1659   1888     85   -100     38       N  
ATOM   2026  N   LEU A 242       0.400 -38.633  30.263  1.00 10.57           N  
ANISOU 2026  N   LEU A 242     1825   1162   1030    153    -96    -93       N  
ATOM   2027  CA  LEU A 242      -0.772 -39.412  29.856  1.00 11.92           C  
ANISOU 2027  CA  LEU A 242     1998   1398   1135    159    -42    -94       C  
ATOM   2028  C   LEU A 242      -2.058 -38.715  30.280  1.00 14.50           C  
ANISOU 2028  C   LEU A 242     2356   1743   1409    194    -46   -118       C  
ATOM   2029  O   LEU A 242      -3.060 -38.769  29.557  1.00 13.00           O  
ANISOU 2029  O   LEU A 242     2162   1596   1182    199     -3   -110       O  
ATOM   2030  CB  LEU A 242      -0.719 -40.847  30.377  1.00 13.43           C  
ANISOU 2030  CB  LEU A 242     2193   1621   1291    152    -24   -104       C  
ATOM   2031  CG  LEU A 242      -1.835 -41.758  29.846  1.00  9.80           C  
ANISOU 2031  CG  LEU A 242     1728   1227    768    154     35   -100       C  
ATOM   2032  CD1 LEU A 242      -1.836 -41.826  28.313  1.00 11.99           C  
ANISOU 2032  CD1 LEU A 242     1968   1524   1065    133     81    -65       C  
ATOM   2033  CD2 LEU A 242      -1.733 -43.158  30.455  1.00 12.60           C  
ANISOU 2033  CD2 LEU A 242     2088   1608   1091    147     47   -111       C  
ATOM   2034  N   VAL A 243      -2.046 -38.061  31.443  1.00 12.11           N  
ANISOU 2034  N   VAL A 243     2087   1410   1105    217    -98   -147       N  
ATOM   2035  CA  VAL A 243      -3.229 -37.316  31.884  1.00 11.31           C  
ANISOU 2035  CA  VAL A 243     2017   1323    957    252   -106   -171       C  
ATOM   2036  C   VAL A 243      -3.546 -36.177  30.914  1.00 14.80           C  
ANISOU 2036  C   VAL A 243     2447   1754   1423    254    -99   -153       C  
ATOM   2037  O   VAL A 243      -4.704 -35.967  30.553  1.00 15.92           O  
ANISOU 2037  O   VAL A 243     2597   1933   1520    270    -70   -155       O  
ATOM   2038  CB  VAL A 243      -3.102 -36.776  33.329  1.00 11.56           C  
ANISOU 2038  CB  VAL A 243     2086   1321    984    279   -167   -207       C  
ATOM   2039  CG1 VAL A 243      -4.403 -36.048  33.741  1.00 12.86           C  
ANISOU 2039  CG1 VAL A 243     2284   1507   1095    317   -172   -231       C  
ATOM   2040  CG2 VAL A 243      -2.769 -37.915  34.315  1.00 16.59           C  
ANISOU 2040  CG2 VAL A 243     2736   1970   1597    278   -174   -225       C  
ATOM   2041  N   ARG A 244      -2.517 -35.458  30.476  1.00 13.14           N  
ANISOU 2041  N   ARG A 244     2215   1493   1285    236   -124   -133       N  
ATOM   2042  CA  ARG A 244      -2.696 -34.367  29.511  1.00 15.63           C  
ANISOU 2042  CA  ARG A 244     2516   1794   1631    235   -119   -112       C  
ATOM   2043  C   ARG A 244      -3.362 -34.881  28.252  1.00 15.75           C  
ANISOU 2043  C   ARG A 244     2504   1860   1620    223    -53    -85       C  
ATOM   2044  O   ARG A 244      -4.261 -34.246  27.707  1.00 12.85           O  
ANISOU 2044  O   ARG A 244     2139   1512   1232    236    -34    -82       O  
ATOM   2045  CB  ARG A 244      -1.350 -33.747  29.119  1.00 14.77           C  
ANISOU 2045  CB  ARG A 244     2380   1626   1607    212   -150    -88       C  
ATOM   2046  CG  ARG A 244      -0.552 -33.194  30.276  1.00 22.38           C  
ANISOU 2046  CG  ARG A 244     3366   2533   2606    221   -217   -111       C  
ATOM   2047  CD  ARG A 244      -1.248 -32.014  30.900  1.00 25.82           C  
ANISOU 2047  CD  ARG A 244     3835   2950   3027    255   -255   -137       C  
ATOM   2048  NE  ARG A 244      -0.450 -31.397  31.960  1.00 28.99           N  
ANISOU 2048  NE  ARG A 244     4256   3292   3467    264   -323   -159       N  
ATOM   2049  CZ  ARG A 244      -0.382 -30.084  32.165  1.00 36.40           C  
ANISOU 2049  CZ  ARG A 244     5207   4186   4439    279   -368   -167       C  
ATOM   2050  NH1 ARG A 244      -1.042 -29.255  31.362  1.00 37.52           N  
ANISOU 2050  NH1 ARG A 244     5342   4334   4582    286   -351   -153       N  
ATOM   2051  NH2 ARG A 244       0.350 -29.596  33.158  1.00 34.32           N  
ANISOU 2051  NH2 ARG A 244     4961   3869   4208    288   -430   -188       N  
ATOM   2052  N   ILE A 245      -2.894 -36.026  27.778  1.00 11.77           N  
ANISOU 2052  N   ILE A 245     1975   1379   1119    197    -19    -67       N  
ATOM   2053  CA  ILE A 245      -3.462 -36.637  26.580  1.00 12.87           C  
ANISOU 2053  CA  ILE A 245     2088   1569   1234    184     44    -43       C  
ATOM   2054  C   ILE A 245      -4.917 -37.034  26.838  1.00 14.62           C  
ANISOU 2054  C   ILE A 245     2335   1846   1375    208     74    -64       C  
ATOM   2055  O   ILE A 245      -5.809 -36.724  26.046  1.00 13.51           O  
ANISOU 2055  O   ILE A 245     2188   1735   1210    215    108    -53       O  
ATOM   2056  CB  ILE A 245      -2.660 -37.873  26.148  1.00 11.09           C  
ANISOU 2056  CB  ILE A 245     1833   1356   1024    154     71    -23       C  
ATOM   2057  CG1 ILE A 245      -1.258 -37.443  25.660  1.00 11.82           C  
ANISOU 2057  CG1 ILE A 245     1895   1398   1198    128     48      4       C  
ATOM   2058  CG2 ILE A 245      -3.423 -38.636  25.069  1.00 11.12           C  
ANISOU 2058  CG2 ILE A 245     1816   1419    990    146    136     -5       C  
ATOM   2059  CD1 ILE A 245      -0.274 -38.585  25.437  1.00 12.57           C  
ANISOU 2059  CD1 ILE A 245     1964   1497   1316    100     63     20       C  
ATOM   2060  N   ALA A 246      -5.154 -37.697  27.963  1.00 12.06           N  
ANISOU 2060  N   ALA A 246     2038   1534   1010    222     60    -92       N  
ATOM   2061  CA  ALA A 246      -6.508 -38.149  28.310  1.00 15.56           C  
ANISOU 2061  CA  ALA A 246     2504   2031   1376    245     87   -112       C  
ATOM   2062  C   ALA A 246      -7.532 -37.007  28.470  1.00 15.93           C  
ANISOU 2062  C   ALA A 246     2577   2081   1396    276     75   -127       C  
ATOM   2063  O   ALA A 246      -8.740 -37.196  28.245  1.00 13.93           O  
ANISOU 2063  O   ALA A 246     2333   1876   1086    291    110   -132       O  
ATOM   2064  CB  ALA A 246      -6.471 -39.007  29.552  1.00 11.17           C  
ANISOU 2064  CB  ALA A 246     1973   1484    786    254     69   -139       C  
ATOM   2065  N   LYS A 247      -7.062 -35.827  28.849  1.00 11.66           N  
ANISOU 2065  N   LYS A 247     2046   1487    896    286     26   -135       N  
ATOM   2066  CA  LYS A 247      -7.934 -34.645  28.914  1.00 12.20           C  
ANISOU 2066  CA  LYS A 247     2136   1552    947    314     12   -147       C  
ATOM   2067  C   LYS A 247      -8.454 -34.169  27.543  1.00 16.76           C  
ANISOU 2067  C   LYS A 247     2689   2148   1531    307     53   -119       C  
ATOM   2068  O   LYS A 247      -9.404 -33.388  27.463  1.00 17.83           O  
ANISOU 2068  O   LYS A 247     2841   2296   1639    330     55   -127       O  
ATOM   2069  CB  LYS A 247      -7.256 -33.496  29.671  1.00 17.22           C  
ANISOU 2069  CB  LYS A 247     2790   2125   1630    327    -54   -163       C  
ATOM   2070  CG  LYS A 247      -7.139 -33.748  31.176  1.00 16.66           C  
ANISOU 2070  CG  LYS A 247     2754   2042   1535    347    -96   -199       C  
ATOM   2071  CD  LYS A 247      -6.543 -32.566  31.918  1.00 21.58           C  
ANISOU 2071  CD  LYS A 247     3396   2603   2202    362   -163   -216       C  
ATOM   2072  CE  LYS A 247      -6.719 -32.738  33.424  1.00 30.61           C  
ANISOU 2072  CE  LYS A 247     4579   3744   3309    390   -201   -256       C  
ATOM   2073  NZ  LYS A 247      -5.992 -31.700  34.203  1.00 36.89           N  
ANISOU 2073  NZ  LYS A 247     5391   4476   4150    403   -269   -274       N  
ATOM   2074  N   VAL A 248      -7.840 -34.656  26.475  1.00 12.09           N  
ANISOU 2074  N   VAL A 248     1686   1563   1344     75    -38    181       N  
ATOM   2075  CA  VAL A 248      -8.200 -34.271  25.123  1.00 12.93           C  
ANISOU 2075  CA  VAL A 248     1765   1704   1445     66    -29    193       C  
ATOM   2076  C   VAL A 248      -8.879 -35.426  24.401  1.00 14.51           C  
ANISOU 2076  C   VAL A 248     1945   1939   1630     32    -27    192       C  
ATOM   2077  O   VAL A 248      -9.956 -35.253  23.824  1.00 15.30           O  
ANISOU 2077  O   VAL A 248     2019   2086   1709     28    -18    211       O  
ATOM   2078  CB  VAL A 248      -6.965 -33.818  24.318  1.00 14.10           C  
ANISOU 2078  CB  VAL A 248     1914   1829   1616     65    -34    179       C  
ATOM   2079  CG1 VAL A 248      -7.336 -33.536  22.865  1.00 11.84           C  
ANISOU 2079  CG1 VAL A 248     1599   1583   1319     57    -23    192       C  
ATOM   2080  CG2 VAL A 248      -6.328 -32.579  24.956  1.00 13.22           C  
ANISOU 2080  CG2 VAL A 248     1819   1683   1523     96    -34    177       C  
ATOM   2081  N   LEU A 249      -8.252 -36.598  24.427  1.00 10.40           N  
ANISOU 2081  N   LEU A 249     1435   1397   1120      7    -35    169       N  
ATOM   2082  CA  LEU A 249      -8.800 -37.773  23.752  1.00 11.45           C  
ANISOU 2082  CA  LEU A 249     1551   1557   1243    -29    -33    162       C  
ATOM   2083  C   LEU A 249      -9.828 -38.490  24.616  1.00 13.95           C  
ANISOU 2083  C   LEU A 249     1869   1883   1547    -37    -26    171       C  
ATOM   2084  O   LEU A 249     -10.607 -39.311  24.124  1.00 11.89           O  
ANISOU 2084  O   LEU A 249     1589   1652   1277    -67    -21    169       O  
ATOM   2085  CB  LEU A 249      -7.681 -38.755  23.370  1.00 14.12           C  
ANISOU 2085  CB  LEU A 249     1901   1864   1600    -52    -40    133       C  
ATOM   2086  CG  LEU A 249      -6.827 -38.430  22.142  1.00 15.35           C  
ANISOU 2086  CG  LEU A 249     2047   2021   1764    -56    -43    121       C  
ATOM   2087  CD1 LEU A 249      -6.036 -37.140  22.301  1.00 16.15           C  
ANISOU 2087  CD1 LEU A 249     2156   2100   1879    -25    -45    128       C  
ATOM   2088  CD2 LEU A 249      -5.871 -39.576  21.829  1.00 16.02           C  
ANISOU 2088  CD2 LEU A 249     2143   2078   1866    -80    -47     93       C  
ATOM   2089  N   GLY A 250      -9.820 -38.185  25.903  1.00 11.25           N  
ANISOU 2089  N   GLY A 250     1549   1518   1208    -11    -27    180       N  
ATOM   2090  CA  GLY A 250     -10.807 -38.741  26.815  1.00 12.99           C  
ANISOU 2090  CA  GLY A 250     1771   1747   1417    -13    -18    194       C  
ATOM   2091  C   GLY A 250     -10.363 -40.033  27.466  1.00 15.00           C  
ANISOU 2091  C   GLY A 250     2047   1968   1684    -29    -18    180       C  
ATOM   2092  O   GLY A 250      -9.541 -40.782  26.919  1.00 14.67           O  
ANISOU 2092  O   GLY A 250     2011   1906   1658    -50    -23    158       O  
ATOM   2093  N   THR A 251     -10.913 -40.307  28.643  1.00 14.90           N  
ANISOU 2093  N   THR A 251     2048   1949   1664    -16    -11    194       N  
ATOM   2094  CA  THR A 251     -10.521 -41.503  29.371  1.00 13.15           C  
ANISOU 2094  CA  THR A 251     1848   1695   1454    -25     -8    187       C  
ATOM   2095  C   THR A 251     -11.213 -42.780  28.884  1.00  8.74           C  
ANISOU 2095  C   THR A 251     1274   1147    899    -67      6    184       C  
ATOM   2096  O   THR A 251     -10.643 -43.864  28.999  1.00 14.97           O  
ANISOU 2096  O   THR A 251     2078   1904   1704    -84      9    170       O  
ATOM   2097  CB  THR A 251     -10.739 -41.352  30.888  1.00 14.93           C  
ANISOU 2097  CB  THR A 251     2097   1907   1670      9     -4    204       C  
ATOM   2098  OG1 THR A 251     -12.054 -40.846  31.128  1.00 12.69           O  
ANISOU 2098  OG1 THR A 251     1796   1660   1367     17      9    229       O  
ATOM   2099  CG2 THR A 251      -9.721 -40.383  31.483  1.00 16.79           C  
ANISOU 2099  CG2 THR A 251     2355   2118   1908     47    -20    196       C  
ATOM   2100  N   GLU A 252     -12.441 -42.687  28.371  1.00 12.44           N  
ANISOU 2100  N   GLU A 252     1712   1661   1354    -86     16    196       N  
ATOM   2101  CA  GLU A 252     -13.116 -43.925  27.956  1.00 12.07           C  
ANISOU 2101  CA  GLU A 252     1649   1624   1313   -130     29    189       C  
ATOM   2102  C   GLU A 252     -12.375 -44.625  26.814  1.00 14.45           C  
ANISOU 2102  C   GLU A 252     1946   1914   1629   -163     23    157       C  
ATOM   2103  O   GLU A 252     -12.242 -45.855  26.799  1.00 15.38           O  
ANISOU 2103  O   GLU A 252     2072   2007   1764   -192     33    142       O  
ATOM   2104  CB  GLU A 252     -14.589 -43.683  27.611  1.00 16.76           C  
ANISOU 2104  CB  GLU A 252     2206   2273   1889   -144     39    206       C  
ATOM   2105  CG  GLU A 252     -15.444 -43.419  28.844  1.00 24.41           C  
ANISOU 2105  CG  GLU A 252     3179   3248   2847   -119     52    237       C  
ATOM   2106  CD  GLU A 252     -15.562 -44.640  29.737  1.00 37.97           C  
ANISOU 2106  CD  GLU A 252     4915   4934   4579   -132     69    241       C  
ATOM   2107  OE1 GLU A 252     -16.125 -45.661  29.284  1.00 46.30           O  
ANISOU 2107  OE1 GLU A 252     5951   5996   5644   -175     81    232       O  
ATOM   2108  OE2 GLU A 252     -15.084 -44.585  30.890  1.00 37.25           O  
ANISOU 2108  OE2 GLU A 252     4855   4809   4488    -99     70    252       O  
ATOM   2109  N   ASP A 253     -11.865 -43.848  25.867  1.00 12.71           N  
ANISOU 2109  N   ASP A 253     1716   1709   1404   -158     10    147       N  
ATOM   2110  CA  ASP A 253     -11.094 -44.438  24.779  1.00 14.01           C  
ANISOU 2110  CA  ASP A 253     1878   1863   1580   -185      4    117       C  
ATOM   2111  C   ASP A 253      -9.712 -44.927  25.211  1.00 13.90           C  
ANISOU 2111  C   ASP A 253     1898   1792   1589   -174      0    102       C  
ATOM   2112  O   ASP A 253      -9.160 -45.855  24.610  1.00 15.55           O  
ANISOU 2112  O   ASP A 253     2112   1982   1813   -201      2     77       O  
ATOM   2113  CB  ASP A 253     -11.026 -43.498  23.582  1.00 12.33           C  
ANISOU 2113  CB  ASP A 253     1642   1689   1355   -182     -6    114       C  
ATOM   2114  CG  ASP A 253     -12.383 -43.335  22.908  1.00 17.70           C  
ANISOU 2114  CG  ASP A 253     2283   2431   2011   -201     -1    123       C  
ATOM   2115  OD1 ASP A 253     -13.127 -44.333  22.818  1.00 21.86           O  
ANISOU 2115  OD1 ASP A 253     2796   2970   2538   -237      8    114       O  
ATOM   2116  OD2 ASP A 253     -12.707 -42.208  22.503  1.00 18.37           O  
ANISOU 2116  OD2 ASP A 253     2350   2553   2078   -180     -5    140       O  
ATOM   2117  N   LEU A 254      -9.172 -44.327  26.266  1.00 14.24           N  
ANISOU 2117  N   LEU A 254     1965   1810   1635   -135     -7    115       N  
ATOM   2118  CA  LEU A 254      -7.936 -44.831  26.858  1.00 17.65           C  
ANISOU 2118  CA  LEU A 254     2428   2193   2086   -122    -11    104       C  
ATOM   2119  C   LEU A 254      -8.210 -46.203  27.447  1.00 17.43           C  
ANISOU 2119  C   LEU A 254     2413   2140   2069   -140      5    105       C  
ATOM   2120  O   LEU A 254      -7.431 -47.139  27.248  1.00 17.70           O  
ANISOU 2120  O   LEU A 254     2462   2141   2122   -153      9     87       O  
ATOM   2121  CB  LEU A 254      -7.403 -43.889  27.936  1.00 13.92           C  
ANISOU 2121  CB  LEU A 254     1975   1704   1610    -77    -23    117       C  
ATOM   2122  CG  LEU A 254      -6.195 -44.374  28.745  1.00 16.16           C  
ANISOU 2122  CG  LEU A 254     2289   1943   1910    -57    -30    109       C  
ATOM   2123  CD1 LEU A 254      -5.041 -44.737  27.821  1.00 17.48           C  
ANISOU 2123  CD1 LEU A 254     2456   2090   2096    -71    -37     83       C  
ATOM   2124  CD2 LEU A 254      -5.801 -43.286  29.707  1.00 15.23           C  
ANISOU 2124  CD2 LEU A 254     2183   1818   1784    -15    -44    117       C  
ATOM   2125  N   TYR A 255      -9.322 -46.337  28.165  1.00 15.47           N  
ANISOU 2125  N   TYR A 255     2161   1907   1810   -140     18    126       N  
ATOM   2126  CA  TYR A 255      -9.672 -47.645  28.704  1.00 14.01           C  
ANISOU 2126  CA  TYR A 255     1988   1699   1639   -159     39    130       C  
ATOM   2127  C   TYR A 255      -9.949 -48.666  27.596  1.00 15.80           C  
ANISOU 2127  C   TYR A 255     2198   1928   1878   -210     51    106       C  
ATOM   2128  O   TYR A 255      -9.550 -49.825  27.714  1.00 17.25           O  
ANISOU 2128  O   TYR A 255     2398   2073   2083   -226     65     96       O  
ATOM   2129  CB  TYR A 255     -10.823 -47.563  29.713  1.00 11.64           C  
ANISOU 2129  CB  TYR A 255     1684   1414   1324   -148     53    160       C  
ATOM   2130  CG  TYR A 255     -10.342 -47.244  31.116  1.00 14.69           C  
ANISOU 2130  CG  TYR A 255     2101   1777   1705   -100     50    180       C  
ATOM   2131  CD1 TYR A 255      -9.822 -48.239  31.925  1.00 19.00           C  
ANISOU 2131  CD1 TYR A 255     2674   2282   2264    -92     62    185       C  
ATOM   2132  CD2 TYR A 255     -10.398 -45.949  31.629  1.00 21.03           C  
ANISOU 2132  CD2 TYR A 255     2905   2599   2488    -62     36    193       C  
ATOM   2133  CE1 TYR A 255      -9.373 -47.966  33.202  1.00 21.87           C  
ANISOU 2133  CE1 TYR A 255     3064   2630   2618    -46     57    202       C  
ATOM   2134  CE2 TYR A 255      -9.951 -45.669  32.916  1.00 19.68           C  
ANISOU 2134  CE2 TYR A 255     2761   2409   2308    -20     32    206       C  
ATOM   2135  CZ  TYR A 255      -9.441 -46.687  33.694  1.00 23.45           C  
ANISOU 2135  CZ  TYR A 255     3263   2851   2796    -11     41    210       C  
ATOM   2136  OH  TYR A 255      -8.991 -46.440  34.979  1.00 28.51           O  
ANISOU 2136  OH  TYR A 255     3930   3478   3423     33     35    223       O  
ATOM   2137  N   ASP A 256     -10.613 -48.245  26.519  1.00 14.06           N  
ANISOU 2137  N   ASP A 256     1944   1752   1645   -234     46     97       N  
ATOM   2138  CA  ASP A 256     -10.837 -49.147  25.387  1.00 12.60           C  
ANISOU 2138  CA  ASP A 256     1743   1576   1470   -283     54     68       C  
ATOM   2139  C   ASP A 256      -9.503 -49.667  24.829  1.00 15.19           C  
ANISOU 2139  C   ASP A 256     2090   1866   1816   -287     49     41       C  
ATOM   2140  O   ASP A 256      -9.389 -50.829  24.451  1.00 16.15           O  
ANISOU 2140  O   ASP A 256     2217   1964   1957   -320     63     19       O  
ATOM   2141  CB  ASP A 256     -11.585 -48.454  24.254  1.00 15.74           C  
ANISOU 2141  CB  ASP A 256     2101   2034   1845   -301     44     62       C  
ATOM   2142  CG  ASP A 256     -13.069 -48.238  24.549  1.00 19.83           C  
ANISOU 2142  CG  ASP A 256     2592   2596   2348   -310     52     83       C  
ATOM   2143  OD1 ASP A 256     -13.626 -48.836  25.501  1.00 17.04           O  
ANISOU 2143  OD1 ASP A 256     2247   2225   2004   -314     69     99       O  
ATOM   2144  OD2 ASP A 256     -13.683 -47.461  23.788  1.00 24.75           O  
ANISOU 2144  OD2 ASP A 256     3183   3273   2948   -313     42     86       O  
ATOM   2145  N   TYR A 257      -8.517 -48.774  24.752  1.00 15.49           N  
ANISOU 2145  N   TYR A 257     2138   1898   1850   -254     31     42       N  
ATOM   2146  CA  TYR A 257      -7.181 -49.080  24.248  1.00 16.94           C  
ANISOU 2146  CA  TYR A 257     2337   2049   2050   -251     25     19       C  
ATOM   2147  C   TYR A 257      -6.490 -50.118  25.116  1.00 16.68           C  
ANISOU 2147  C   TYR A 257     2336   1960   2040   -243     37     20       C  
ATOM   2148  O   TYR A 257      -6.088 -51.176  24.634  1.00 17.14           O  
ANISOU 2148  O   TYR A 257     2403   1992   2117   -268     49     -2       O  
ATOM   2149  CB  TYR A 257      -6.340 -47.803  24.199  1.00 15.96           C  
ANISOU 2149  CB  TYR A 257     2215   1931   1919   -214      4     25       C  
ATOM   2150  CG  TYR A 257      -4.899 -47.994  23.768  1.00 19.32           C  
ANISOU 2150  CG  TYR A 257     2654   2323   2361   -207     -3      6       C  
ATOM   2151  CD1 TYR A 257      -4.584 -48.768  22.650  1.00 15.97           C  
ANISOU 2151  CD1 TYR A 257     2225   1896   1945   -238      4    -22       C  
ATOM   2152  CD2 TYR A 257      -3.855 -47.373  24.451  1.00 16.61           C  
ANISOU 2152  CD2 TYR A 257     2329   1957   2026   -168    -16     13       C  
ATOM   2153  CE1 TYR A 257      -3.263 -48.936  22.234  1.00 17.06           C  
ANISOU 2153  CE1 TYR A 257     2376   2007   2100   -229     -1    -39       C  
ATOM   2154  CE2 TYR A 257      -2.520 -47.542  24.039  1.00 19.24           C  
ANISOU 2154  CE2 TYR A 257     2672   2263   2377   -161    -22     -4       C  
ATOM   2155  CZ  TYR A 257      -2.245 -48.326  22.923  1.00 20.90           C  
ANISOU 2155  CZ  TYR A 257     2877   2470   2595   -191    -13    -29       C  
ATOM   2156  OH  TYR A 257      -0.956 -48.510  22.463  1.00 17.11           O  
ANISOU 2156  OH  TYR A 257     2405   1965   2132   -184    -17    -45       O  
ATOM   2157  N   ILE A 258      -6.349 -49.829  26.403  1.00 14.21           N  
ANISOU 2157  N   ILE A 258     2042   1631   1726   -207     35     45       N  
ATOM   2158  CA  ILE A 258      -5.643 -50.769  27.263  1.00 10.14           C  
ANISOU 2158  CA  ILE A 258     1557   1066   1229   -193     46     49       C  
ATOM   2159  C   ILE A 258      -6.434 -52.077  27.368  1.00 18.57           C  
ANISOU 2159  C   ILE A 258     2627   2117   2311   -227     75     49       C  
ATOM   2160  O   ILE A 258      -5.855 -53.152  27.504  1.00 17.83           O  
ANISOU 2160  O   ILE A 258     2554   1980   2239   -232     91     43       O  
ATOM   2161  CB  ILE A 258      -5.315 -50.188  28.660  1.00 17.19           C  
ANISOU 2161  CB  ILE A 258     2469   1949   2113   -144     37     76       C  
ATOM   2162  CG1 ILE A 258      -6.582 -49.899  29.460  1.00 18.49           C  
ANISOU 2162  CG1 ILE A 258     2627   2137   2260   -139     45    103       C  
ATOM   2163  CG2 ILE A 258      -4.441 -48.930  28.538  1.00 16.83           C  
ANISOU 2163  CG2 ILE A 258     2421   1914   2060   -114      9     71       C  
ATOM   2164  CD1 ILE A 258      -6.303 -49.615  30.911  1.00 21.81           C  
ANISOU 2164  CD1 ILE A 258     3071   2544   2671    -93     41    127       C  
ATOM   2165  N   ASP A 259      -7.759 -51.985  27.293  1.00 14.49           N  
ANISOU 2165  N   ASP A 259     2089   1634   1784   -250     84     58       N  
ATOM   2166  CA  ASP A 259      -8.585 -53.190  27.362  1.00 10.77           C  
ANISOU 2166  CA  ASP A 259     1616   1148   1329   -287    113     56       C  
ATOM   2167  C   ASP A 259      -8.388 -54.069  26.135  1.00 15.75           C  
ANISOU 2167  C   ASP A 259     2240   1767   1977   -333    122     18       C  
ATOM   2168  O   ASP A 259      -8.349 -55.295  26.241  1.00 16.39           O  
ANISOU 2168  O   ASP A 259     2336   1809   2084   -355    148     10       O  
ATOM   2169  CB  ASP A 259     -10.071 -52.841  27.510  1.00 13.74           C  
ANISOU 2169  CB  ASP A 259     1965   1567   1688   -304    119     72       C  
ATOM   2170  CG  ASP A 259     -10.432 -52.398  28.912  1.00 17.44           C  
ANISOU 2170  CG  ASP A 259     2446   2036   2146   -264    123    111       C  
ATOM   2171  OD1 ASP A 259      -9.578 -52.489  29.819  1.00 17.27           O  
ANISOU 2171  OD1 ASP A 259     2455   1979   2128   -227    122    125       O  
ATOM   2172  OD2 ASP A 259     -11.594 -51.989  29.114  1.00 20.10           O  
ANISOU 2172  OD2 ASP A 259     2761   2409   2467   -271    127    128       O  
ATOM   2173  N   LYS A 260      -8.288 -53.441  24.970  1.00 16.45           N  
ANISOU 2173  N   LYS A 260     2307   1893   2052   -346    103     -5       N  
ATOM   2174  CA  LYS A 260      -8.050 -54.174  23.730  1.00 18.59           C  
ANISOU 2174  CA  LYS A 260     2571   2159   2334   -386    109    -45       C  
ATOM   2175  C   LYS A 260      -6.789 -55.020  23.795  1.00 18.35           C  
ANISOU 2175  C   LYS A 260     2573   2070   2330   -377    119    -58       C  
ATOM   2176  O   LYS A 260      -6.776 -56.145  23.307  1.00 20.25           O  
ANISOU 2176  O   LYS A 260     2818   2283   2591   -411    140    -83       O  
ATOM   2177  CB  LYS A 260      -7.973 -53.228  22.528  1.00 22.54           C  
ANISOU 2177  CB  LYS A 260     3044   2709   2810   -391     85    -62       C  
ATOM   2178  CG  LYS A 260      -7.436 -53.912  21.284  1.00 18.05           C  
ANISOU 2178  CG  LYS A 260     2475   2133   2251   -422     89   -103       C  
ATOM   2179  CD  LYS A 260      -7.580 -53.048  20.041  1.00 24.81           C  
ANISOU 2179  CD  LYS A 260     3301   3047   3080   -429     69   -119       C  
ATOM   2180  CE  LYS A 260      -6.770 -53.635  18.886  1.00 24.53           C  
ANISOU 2180  CE  LYS A 260     3269   2999   3051   -449     71   -158       C  
ATOM   2181  NZ  LYS A 260      -6.780 -52.754  17.696  1.00 25.15           N  
ANISOU 2181  NZ  LYS A 260     3321   3134   3101   -449     53   -169       N  
ATOM   2182  N   TYR A 261      -5.734 -54.476  24.401  1.00 15.81           N  
ANISOU 2182  N   TYR A 261     2271   1730   2008   -330    105    -41       N  
ATOM   2183  CA  TYR A 261      -4.447 -55.171  24.486  1.00 16.61           C  
ANISOU 2183  CA  TYR A 261     2400   1780   2132   -314    112    -50       C  
ATOM   2184  C   TYR A 261      -4.249 -55.887  25.819  1.00 18.36           C  
ANISOU 2184  C   TYR A 261     2650   1956   2370   -289    131    -22       C  
ATOM   2185  O   TYR A 261      -3.162 -56.416  26.104  1.00 18.74           O  
ANISOU 2185  O   TYR A 261     2723   1963   2436   -266    137    -22       O  
ATOM   2186  CB  TYR A 261      -3.311 -54.191  24.198  1.00 13.37           C  
ANISOU 2186  CB  TYR A 261     1989   1378   1712   -280     85    -52       C  
ATOM   2187  CG  TYR A 261      -3.402 -53.696  22.780  1.00 12.86           C  
ANISOU 2187  CG  TYR A 261     1899   1353   1635   -305     73    -79       C  
ATOM   2188  CD1 TYR A 261      -2.903 -54.460  21.727  1.00 16.26           C  
ANISOU 2188  CD1 TYR A 261     2332   1769   2078   -331     83   -112       C  
ATOM   2189  CD2 TYR A 261      -4.033 -52.488  22.482  1.00 13.21           C  
ANISOU 2189  CD2 TYR A 261     1917   1449   1652   -302     55    -70       C  
ATOM   2190  CE1 TYR A 261      -3.015 -54.031  20.421  1.00 17.30           C  
ANISOU 2190  CE1 TYR A 261     2440   1940   2193   -353     74   -137       C  
ATOM   2191  CE2 TYR A 261      -4.139 -52.044  21.176  1.00 14.91           C  
ANISOU 2191  CE2 TYR A 261     2109   1704   1853   -321     46    -91       C  
ATOM   2192  CZ  TYR A 261      -3.628 -52.818  20.150  1.00 18.46           C  
ANISOU 2192  CZ  TYR A 261     2561   2141   2313   -347     54   -125       C  
ATOM   2193  OH  TYR A 261      -3.734 -52.382  18.848  1.00 16.58           O  
ANISOU 2193  OH  TYR A 261     2298   1945   2056   -364     46   -145       O  
ATOM   2194  N   ASN A 262      -5.318 -55.924  26.614  1.00 20.95           N  
ANISOU 2194  N   ASN A 262     2974   2293   2691   -292    142      2       N  
ATOM   2195  CA  ASN A 262      -5.294 -56.560  27.925  1.00 20.67           C  
ANISOU 2195  CA  ASN A 262     2965   2221   2668   -267    162     33       C  
ATOM   2196  C   ASN A 262      -4.110 -56.040  28.749  1.00 22.84           C  
ANISOU 2196  C   ASN A 262     3260   2482   2936   -210    144     51       C  
ATOM   2197  O   ASN A 262      -3.388 -56.816  29.369  1.00 24.99           O  
ANISOU 2197  O   ASN A 262     3559   2713   3225   -187    158     63       O  
ATOM   2198  CB  ASN A 262      -5.244 -58.090  27.790  1.00 19.62           C  
ANISOU 2198  CB  ASN A 262     2849   2036   2568   -295    199     22       C  
ATOM   2199  CG  ASN A 262      -6.526 -58.687  27.205  1.00 24.72           C  
ANISOU 2199  CG  ASN A 262     3475   2693   3224   -353    221      5       C  
ATOM   2200  OD1 ASN A 262      -7.435 -57.976  26.769  1.00 31.16           O  
ANISOU 2200  OD1 ASN A 262     4261   3560   4020   -374    207     -1       O  
ATOM   2201  ND2 ASN A 262      -6.593 -60.010  27.190  1.00 30.97           N  
ANISOU 2201  ND2 ASN A 262     4283   3437   4049   -379    257     -4       N  
ATOM   2202  N   ILE A 263      -3.931 -54.717  28.717  1.00 24.17           N  
ANISOU 2202  N   ILE A 263     3415   2688   3080   -187    112     53       N  
ATOM   2203  CA  ILE A 263      -2.900 -53.986  29.450  1.00 21.22           C  
ANISOU 2203  CA  ILE A 263     3054   2311   2696   -136     88     66       C  
ATOM   2204  C   ILE A 263      -3.539 -53.438  30.719  1.00 25.67           C  
ANISOU 2204  C   ILE A 263     3623   2892   3240   -106     85     98       C  
ATOM   2205  O   ILE A 263      -4.717 -53.070  30.720  1.00 29.14           O  
ANISOU 2205  O   ILE A 263     4046   3361   3666   -123     89    107       O  
ATOM   2206  CB  ILE A 263      -2.423 -52.744  28.657  1.00 25.79           C  
ANISOU 2206  CB  ILE A 263     3614   2923   3263   -132     57     48       C  
ATOM   2207  CG1 ILE A 263      -1.774 -53.120  27.324  1.00 28.90           C  
ANISOU 2207  CG1 ILE A 263     4000   3307   3672   -159     58     16       C  
ATOM   2208  CG2 ILE A 263      -1.459 -51.899  29.479  1.00 29.30           C  
ANISOU 2208  CG2 ILE A 263     4068   3366   3698    -83     32     59       C  
ATOM   2209  CD1 ILE A 263      -1.470 -51.903  26.465  1.00 27.83           C  
ANISOU 2209  CD1 ILE A 263     3843   3206   3524   -158     33      2       C  
ATOM   2210  N   GLU A 264      -2.765 -53.361  31.793  1.00 17.83           N  
ANISOU 2210  N   GLU A 264     2650   1883   2241    -60     77    116       N  
ATOM   2211  CA  GLU A 264      -3.236 -52.734  33.013  1.00 24.93           C  
ANISOU 2211  CA  GLU A 264     3555   2801   3116    -26     70    144       C  
ATOM   2212  C   GLU A 264      -2.507 -51.410  33.238  1.00 24.75           C  
ANISOU 2212  C   GLU A 264     3528   2800   3076      8     34    137       C  
ATOM   2213  O   GLU A 264      -1.284 -51.359  33.152  1.00 25.73           O  
ANISOU 2213  O   GLU A 264     3658   2909   3208     26     19    124       O  
ATOM   2214  CB  GLU A 264      -2.981 -53.680  34.180  1.00 29.60           C  
ANISOU 2214  CB  GLU A 264     4174   3361   3712      4     90    171       C  
ATOM   2215  CG  GLU A 264      -3.625 -53.267  35.462  1.00 34.03           C  
ANISOU 2215  CG  GLU A 264     4742   3940   4246     37     91    202       C  
ATOM   2216  CD  GLU A 264      -3.897 -54.454  36.355  1.00 37.05           C  
ANISOU 2216  CD  GLU A 264     5147   4293   4637     50    126    233       C  
ATOM   2217  OE1 GLU A 264      -3.001 -55.323  36.490  1.00 36.76           O  
ANISOU 2217  OE1 GLU A 264     5129   4222   4617     64    136    236       O  
ATOM   2218  OE2 GLU A 264      -5.017 -54.520  36.902  1.00 38.19           O  
ANISOU 2218  OE2 GLU A 264     5290   4450   4771     46    145    256       O  
ATOM   2219  N   LEU A 265      -3.252 -50.339  33.509  1.00 21.44           N  
ANISOU 2219  N   LEU A 265     3097   2415   2634     15     23    145       N  
ATOM   2220  CA  LEU A 265      -2.634 -49.062  33.845  1.00 23.13           C  
ANISOU 2220  CA  LEU A 265     3309   2646   2832     48     -8    138       C  
ATOM   2221  C   LEU A 265      -1.882 -49.174  35.170  1.00 22.61           C  
ANISOU 2221  C   LEU A 265     3266   2567   2756     95    -17    151       C  
ATOM   2222  O   LEU A 265      -2.321 -49.869  36.080  1.00 28.20           O  
ANISOU 2222  O   LEU A 265     3991   3268   3457    110      1    176       O  
ATOM   2223  CB  LEU A 265      -3.680 -47.945  33.981  1.00 25.27           C  
ANISOU 2223  CB  LEU A 265     3566   2953   3081     49    -14    146       C  
ATOM   2224  CG  LEU A 265      -4.121 -47.107  32.785  1.00 21.23           C  
ANISOU 2224  CG  LEU A 265     3028   2468   2570     21    -21    132       C  
ATOM   2225  CD1 LEU A 265      -4.877 -45.903  33.296  1.00 22.47           C  
ANISOU 2225  CD1 LEU A 265     3179   2656   2704     41    -28    144       C  
ATOM   2226  CD2 LEU A 265      -2.928 -46.678  31.935  1.00 24.36           C  
ANISOU 2226  CD2 LEU A 265     3418   2855   2981     19    -40    106       C  
ATOM   2227  N   ASP A 266      -0.755 -48.481  35.268  1.00 20.39           N  
ANISOU 2227  N   ASP A 266     2986   2286   2475    119    -45    135       N  
ATOM   2228  CA  ASP A 266      -0.071 -48.294  36.542  1.00 23.03           C  
ANISOU 2228  CA  ASP A 266     3337   2620   2793    167    -61    143       C  
ATOM   2229  C   ASP A 266      -1.109 -47.812  37.556  1.00 24.91           C  
ANISOU 2229  C   ASP A 266     3581   2880   3001    187    -57    164       C  
ATOM   2230  O   ASP A 266      -1.856 -46.870  37.277  1.00 22.29           O  
ANISOU 2230  O   ASP A 266     3237   2572   2661    176    -61    160       O  
ATOM   2231  CB  ASP A 266       1.025 -47.243  36.367  1.00 22.24           C  
ANISOU 2231  CB  ASP A 266     3228   2527   2696    181    -95    116       C  
ATOM   2232  CG  ASP A 266       1.930 -47.117  37.573  1.00 23.26           C  
ANISOU 2232  CG  ASP A 266     3371   2658   2811    227   -116    117       C  
ATOM   2233  OD1 ASP A 266       1.467 -47.301  38.716  1.00 23.74           O  
ANISOU 2233  OD1 ASP A 266     3447   2726   2846    256   -110    139       O  
ATOM   2234  OD2 ASP A 266       3.114 -46.797  37.376  1.00 27.48           O  
ANISOU 2234  OD2 ASP A 266     3898   3187   3356    236   -138     96       O  
ATOM   2235  N   PRO A 267      -1.178 -48.462  38.733  1.00 22.66           N  
ANISOU 2235  N   PRO A 267     3317   2591   2702    219    -46    189       N  
ATOM   2236  CA  PRO A 267      -2.197 -48.064  39.712  1.00 21.53           C  
ANISOU 2236  CA  PRO A 267     3182   2470   2529    239    -38    211       C  
ATOM   2237  C   PRO A 267      -2.005 -46.636  40.219  1.00 24.28           C  
ANISOU 2237  C   PRO A 267     3527   2843   2854    267    -68    196       C  
ATOM   2238  O   PRO A 267      -2.919 -46.071  40.826  1.00 24.50           O  
ANISOU 2238  O   PRO A 267     3558   2893   2859    280    -63    209       O  
ATOM   2239  CB  PRO A 267      -2.010 -49.076  40.855  1.00 20.50           C  
ANISOU 2239  CB  PRO A 267     3075   2328   2387    274    -23    240       C  
ATOM   2240  CG  PRO A 267      -0.622 -49.587  40.685  1.00 23.66           C  
ANISOU 2240  CG  PRO A 267     3480   2707   2804    285    -36    226       C  
ATOM   2241  CD  PRO A 267      -0.386 -49.610  39.198  1.00 21.88           C  
ANISOU 2241  CD  PRO A 267     3236   2467   2611    239    -37    201       C  
ATOM   2242  N   ARG A 268      -0.839 -46.047  39.979  1.00 20.69           N  
ANISOU 2242  N   ARG A 268     3067   2386   2407    274    -97    168       N  
ATOM   2243  CA  ARG A 268      -0.633 -44.675  40.429  1.00 25.72           C  
ANISOU 2243  CA  ARG A 268     3701   3042   3027    296   -124    149       C  
ATOM   2244  C   ARG A 268      -1.552 -43.691  39.690  1.00 26.54           C  
ANISOU 2244  C   ARG A 268     3789   3161   3134    271   -120    143       C  
ATOM   2245  O   ARG A 268      -1.749 -42.565  40.143  1.00 27.62           O  
ANISOU 2245  O   ARG A 268     3926   3313   3254    289   -132    135       O  
ATOM   2246  CB  ARG A 268       0.836 -44.256  40.327  1.00 34.61           C  
ANISOU 2246  CB  ARG A 268     4823   4162   4166    308   -156    118       C  
ATOM   2247  CG  ARG A 268       1.291 -43.847  38.947  1.00 40.62           C  
ANISOU 2247  CG  ARG A 268     5564   4913   4959    272   -162     95       C  
ATOM   2248  CD  ARG A 268       2.733 -43.367  38.992  1.00 44.75           C  
ANISOU 2248  CD  ARG A 268     6080   5430   5493    286   -193     66       C  
ATOM   2249  NE  ARG A 268       3.676 -44.479  39.065  1.00 46.97           N  
ANISOU 2249  NE  ARG A 268     6366   5695   5785    294   -194     69       N  
ATOM   2250  CZ  ARG A 268       4.838 -44.428  39.704  1.00 47.02           C  
ANISOU 2250  CZ  ARG A 268     6373   5704   5787    323   -219     56       C  
ATOM   2251  NH1 ARG A 268       5.200 -43.322  40.345  1.00 46.62           N  
ANISOU 2251  NH1 ARG A 268     6320   5670   5724    344   -246     34       N  
ATOM   2252  NH2 ARG A 268       5.635 -45.487  39.710  1.00 45.27           N  
ANISOU 2252  NH2 ARG A 268     6156   5469   5577    333   -216     63       N  
ATOM   2253  N   PHE A 269      -2.116 -44.126  38.564  1.00 23.57           N  
ANISOU 2253  N   PHE A 269     3398   2779   2777    230   -101    148       N  
ATOM   2254  CA  PHE A 269      -3.081 -43.310  37.827  1.00 16.00           C  
ANISOU 2254  CA  PHE A 269     2422   1838   1818    208    -93    148       C  
ATOM   2255  C   PHE A 269      -4.441 -43.243  38.515  1.00 24.46           C  
ANISOU 2255  C   PHE A 269     3498   2931   2866    217    -74    176       C  
ATOM   2256  O   PHE A 269      -5.276 -42.417  38.153  1.00 27.65           O  
ANISOU 2256  O   PHE A 269     3888   3354   3264    209    -69    179       O  
ATOM   2257  CB  PHE A 269      -3.252 -43.815  36.394  1.00 20.28           C  
ANISOU 2257  CB  PHE A 269     2946   2375   2386    162    -81    143       C  
ATOM   2258  CG  PHE A 269      -2.112 -43.453  35.480  1.00 21.32           C  
ANISOU 2258  CG  PHE A 269     3067   2494   2540    151    -99    116       C  
ATOM   2259  CD1 PHE A 269      -2.002 -42.175  34.964  1.00 20.05           C  
ANISOU 2259  CD1 PHE A 269     2892   2344   2382    149   -112    101       C  
ATOM   2260  CD2 PHE A 269      -1.173 -44.403  35.110  1.00 20.43           C  
ANISOU 2260  CD2 PHE A 269     2957   2358   2447    141   -100    107       C  
ATOM   2261  CE1 PHE A 269      -0.964 -41.835  34.107  1.00 19.32           C  
ANISOU 2261  CE1 PHE A 269     2789   2240   2312    138   -126     79       C  
ATOM   2262  CE2 PHE A 269      -0.128 -44.074  34.254  1.00 22.16           C  
ANISOU 2262  CE2 PHE A 269     3165   2566   2687    131   -115     83       C  
ATOM   2263  CZ  PHE A 269      -0.026 -42.781  33.753  1.00 18.43           C  
ANISOU 2263  CZ  PHE A 269     2679   2107   2218    129   -128     69       C  
ATOM   2264  N   ASN A 270      -4.663 -44.102  39.506  1.00 22.09           N  
ANISOU 2264  N   ASN A 270     3215   2626   2552    237    -60    198       N  
ATOM   2265  CA  ASN A 270      -5.940 -44.125  40.223  1.00 22.61           C  
ANISOU 2265  CA  ASN A 270     3286   2711   2595    248    -39    227       C  
ATOM   2266  C   ASN A 270      -6.310 -42.791  40.865  1.00 29.10           C  
ANISOU 2266  C   ASN A 270     4110   3556   3391    277    -50    224       C  
ATOM   2267  O   ASN A 270      -7.489 -42.437  40.933  1.00 28.26           O  
ANISOU 2267  O   ASN A 270     3995   3469   3272    275    -33    242       O  
ATOM   2268  CB  ASN A 270      -5.948 -45.221  41.296  1.00 31.94           C  
ANISOU 2268  CB  ASN A 270     4489   3883   3765    271    -22    252       C  
ATOM   2269  CG  ASN A 270      -6.036 -46.623  40.710  1.00 36.06           C  
ANISOU 2269  CG  ASN A 270     5008   4381   4313    238      2    263       C  
ATOM   2270  OD1 ASN A 270      -6.577 -46.824  39.624  1.00 34.58           O  
ANISOU 2270  OD1 ASN A 270     4801   4194   4145    195     14    259       O  
ATOM   2271  ND2 ASN A 270      -5.509 -47.602  41.441  1.00 39.76           N  
ANISOU 2271  ND2 ASN A 270     5496   4830   4780    260     11    278       N  
ATOM   2272  N   ASP A 271      -5.307 -42.057  41.344  1.00 23.41           N  
ANISOU 2272  N   ASP A 271     3399   2831   2663    305    -78    200       N  
ATOM   2273  CA  ASP A 271      -5.547 -40.795  42.042  1.00 31.26           C  
ANISOU 2273  CA  ASP A 271     4400   3843   3634    336    -89    192       C  
ATOM   2274  C   ASP A 271      -5.306 -39.549  41.195  1.00 30.11           C  
ANISOU 2274  C   ASP A 271     4239   3697   3504    322   -103    166       C  
ATOM   2275  O   ASP A 271      -5.473 -38.429  41.685  1.00 32.25           O  
ANISOU 2275  O   ASP A 271     4515   3978   3760    345   -111    156       O  
ATOM   2276  CB  ASP A 271      -4.685 -40.708  43.303  1.00 44.70           C  
ANISOU 2276  CB  ASP A 271     6125   5545   5314    379   -109    180       C  
ATOM   2277  CG  ASP A 271      -5.034 -41.774  44.321  1.00 57.48           C  
ANISOU 2277  CG  ASP A 271     7762   7169   6910    403    -92    211       C  
ATOM   2278  OD1 ASP A 271      -6.134 -42.362  44.220  1.00 57.84           O  
ANISOU 2278  OD1 ASP A 271     7804   7220   6955    389    -62    243       O  
ATOM   2279  OD2 ASP A 271      -4.206 -42.019  45.224  1.00 65.78           O  
ANISOU 2279  OD2 ASP A 271     8830   8220   7944    437   -108    206       O  
ATOM   2280  N   ILE A 272      -4.902 -39.729  39.939  1.00 25.96           N  
ANISOU 2280  N   ILE A 272     3695   3160   3009    286   -105    155       N  
ATOM   2281  CA  ILE A 272      -4.565 -38.577  39.100  1.00 17.07           C  
ANISOU 2281  CA  ILE A 272     2555   2031   1900    275   -117    132       C  
ATOM   2282  C   ILE A 272      -5.295 -38.494  37.754  1.00 20.17           C  
ANISOU 2282  C   ILE A 272     2923   2433   2308    239   -101    142       C  
ATOM   2283  O   ILE A 272      -5.351 -37.417  37.153  1.00 19.32           O  
ANISOU 2283  O   ILE A 272     2803   2329   2208    235   -104    134       O  
ATOM   2284  CB  ILE A 272      -3.029 -38.463  38.847  1.00 19.50           C  
ANISOU 2284  CB  ILE A 272     2862   2317   2229    274   -143    101       C  
ATOM   2285  CG1 ILE A 272      -2.500 -39.706  38.128  1.00 16.43           C  
ANISOU 2285  CG1 ILE A 272     2468   1915   1861    247   -140    103       C  
ATOM   2286  CG2 ILE A 272      -2.294 -38.231  40.142  1.00 23.80           C  
ANISOU 2286  CG2 ILE A 272     3427   2860   2756    311   -164     85       C  
ATOM   2287  CD1 ILE A 272      -1.009 -39.619  37.744  1.00 20.48           C  
ANISOU 2287  CD1 ILE A 272     2977   2408   2398    244   -163     74       C  
ATOM   2288  N   LEU A 273      -5.855 -39.609  37.284  1.00 16.40           N  
ANISOU 2288  N   LEU A 273     2438   1960   1835    213    -83    160       N  
ATOM   2289  CA  LEU A 273      -6.372 -39.661  35.915  1.00 16.26           C  
ANISOU 2289  CA  LEU A 273     2394   1952   1831    176    -72    164       C  
ATOM   2290  C   LEU A 273      -7.742 -39.003  35.733  1.00 24.10           C  
ANISOU 2290  C   LEU A 273     3371   2976   2809    175    -55    185       C  
ATOM   2291  O   LEU A 273      -7.988 -38.357  34.716  1.00 26.12           O  
ANISOU 2291  O   LEU A 273     3607   3245   3072    160    -54    183       O  
ATOM   2292  CB  LEU A 273      -6.406 -41.099  35.399  1.00 22.71           C  
ANISOU 2292  CB  LEU A 273     3207   2762   2661    144    -60    169       C  
ATOM   2293  CG  LEU A 273      -6.874 -41.316  33.961  1.00 23.94           C  
ANISOU 2293  CG  LEU A 273     3336   2931   2830    103    -50    167       C  
ATOM   2294  CD1 LEU A 273      -6.095 -40.435  32.990  1.00 23.68           C  
ANISOU 2294  CD1 LEU A 273     3290   2895   2811     98    -65    147       C  
ATOM   2295  CD2 LEU A 273      -6.763 -42.787  33.566  1.00 26.06           C  
ANISOU 2295  CD2 LEU A 273     3605   3185   3113     73    -39    166       C  
ATOM   2296  N   GLY A 274      -8.637 -39.192  36.695  1.00 19.27           N  
ANISOU 2296  N   GLY A 274     2769   2378   2176    193    -42    207       N  
ATOM   2297  CA  GLY A 274      -9.977 -38.625  36.611  1.00 19.77           C  
ANISOU 2297  CA  GLY A 274     2816   2471   2223    195    -24    230       C  
ATOM   2298  C   GLY A 274     -10.826 -39.215  35.499  1.00 18.33           C  
ANISOU 2298  C   GLY A 274     2605   2311   2049    155     -9    242       C  
ATOM   2299  O   GLY A 274     -10.466 -40.235  34.914  1.00 19.30           O  
ANISOU 2299  O   GLY A 274     2723   2423   2188    124     -8    233       O  
ATOM   2300  N   ARG A 275     -11.973 -38.583  35.234  1.00 16.23           N  
ANISOU 2300  N   ARG A 275     2319   2079   1770    156      5    261       N  
ATOM   2301  CA  ARG A 275     -12.822 -38.918  34.090  1.00 15.31           C  
ANISOU 2301  CA  ARG A 275     2168   1991   1656    120     16    270       C  
ATOM   2302  C   ARG A 275     -12.916 -37.718  33.164  1.00 15.98           C  
ANISOU 2302  C   ARG A 275     2234   2096   1742    124     11    269       C  
ATOM   2303  O   ARG A 275     -13.203 -36.606  33.607  1.00 21.43           O  
ANISOU 2303  O   ARG A 275     2928   2793   2420    156     14    278       O  
ATOM   2304  CB  ARG A 275     -14.229 -39.337  34.542  1.00 18.34           C  
ANISOU 2304  CB  ARG A 275     2538   2404   2025    116     39    299       C  
ATOM   2305  CG  ARG A 275     -14.277 -40.674  35.268  1.00 23.99           C  
ANISOU 2305  CG  ARG A 275     3268   3102   2745    105     50    305       C  
ATOM   2306  CD  ARG A 275     -15.717 -41.203  35.330  1.00 24.86           C  
ANISOU 2306  CD  ARG A 275     3355   3244   2847     87     75    332       C  
ATOM   2307  NE  ARG A 275     -16.572 -40.403  36.204  1.00 20.86           N  
ANISOU 2307  NE  ARG A 275     2849   2759   2317    123     86    358       N  
ATOM   2308  CZ  ARG A 275     -17.884 -40.590  36.326  1.00 24.59           C  
ANISOU 2308  CZ  ARG A 275     3299   3265   2781    115    108    384       C  
ATOM   2309  NH1 ARG A 275     -18.472 -41.552  35.632  1.00 24.74           N  
ANISOU 2309  NH1 ARG A 275     3290   3298   2812     70    119    386       N  
ATOM   2310  NH2 ARG A 275     -18.605 -39.829  37.144  1.00 17.81           N  
ANISOU 2310  NH2 ARG A 275     2442   2424   1899    152    119    408       N  
ATOM   2311  N   HIS A 276     -12.696 -37.953  31.873  1.00 11.87           N  
ANISOU 2311  N   HIS A 276     1692   1585   1233     92      7    257       N  
ATOM   2312  CA  HIS A 276     -12.668 -36.889  30.885  1.00 12.28           C  
ANISOU 2312  CA  HIS A 276     1725   1654   1285     96      4    257       C  
ATOM   2313  C   HIS A 276     -13.342 -37.310  29.598  1.00 15.62           C  
ANISOU 2313  C   HIS A 276     2113   2116   1706     61      9    262       C  
ATOM   2314  O   HIS A 276     -13.107 -38.402  29.073  1.00 11.30           O  
ANISOU 2314  O   HIS A 276     1560   1564   1168     26      7    247       O  
ATOM   2315  CB  HIS A 276     -11.224 -36.498  30.577  1.00 16.69           C  
ANISOU 2315  CB  HIS A 276     2300   2178   1864    101    -13    232       C  
ATOM   2316  CG  HIS A 276     -10.451 -36.093  31.785  1.00 18.23           C  
ANISOU 2316  CG  HIS A 276     2527   2337   2062    133    -23    221       C  
ATOM   2317  ND1 HIS A 276     -10.579 -34.848  32.361  1.00 15.88           N  
ANISOU 2317  ND1 HIS A 276     2240   2037   1758    168    -21    227       N  
ATOM   2318  CD2 HIS A 276      -9.541 -36.764  32.529  1.00 19.78           C  
ANISOU 2318  CD2 HIS A 276     2749   2501   2267    136    -35    204       C  
ATOM   2319  CE1 HIS A 276      -9.777 -34.768  33.407  1.00 18.06           C  
ANISOU 2319  CE1 HIS A 276     2543   2281   2036    189    -33    211       C  
ATOM   2320  NE2 HIS A 276      -9.137 -35.918  33.530  1.00 23.89           N  
ANISOU 2320  NE2 HIS A 276     3291   3003   2783    171    -42    198       N  
ATOM   2321  N   SER A 277     -14.192 -36.431  29.092  1.00 11.47           N  
ANISOU 2321  N   SER A 277     1563   1629   1165     72     18    282       N  
ATOM   2322  CA  SER A 277     -14.809 -36.653  27.795  1.00 12.21           C  
ANISOU 2322  CA  SER A 277     1620   1768   1253     43     21    286       C  
ATOM   2323  C   SER A 277     -13.795 -36.429  26.685  1.00 16.92           C  
ANISOU 2323  C   SER A 277     2213   2353   1861     33      9    266       C  
ATOM   2324  O   SER A 277     -12.798 -35.710  26.871  1.00 17.78           O  
ANISOU 2324  O   SER A 277     2344   2428   1983     55      2    258       O  
ATOM   2325  CB  SER A 277     -15.974 -35.677  27.622  1.00 16.67           C  
ANISOU 2325  CB  SER A 277     2159   2380   1797     65     33    317       C  
ATOM   2326  OG  SER A 277     -15.486 -34.357  27.784  1.00 21.24           O  
ANISOU 2326  OG  SER A 277     2753   2940   2379    104     33    323       O  
ATOM   2327  N   ARG A 278     -14.032 -37.035  25.523  1.00 12.32           N  
ANISOU 2327  N   ARG A 278     1604   1802   1274     -1      8    258       N  
ATOM   2328  CA  ARG A 278     -13.207 -36.729  24.361  1.00 12.55           C  
ANISOU 2328  CA  ARG A 278     1627   1832   1310     -7      0    244       C  
ATOM   2329  C   ARG A 278     -13.596 -35.337  23.892  1.00 16.68           C  
ANISOU 2329  C   ARG A 278     2134   2384   1821     24      7    270       C  
ATOM   2330  O   ARG A 278     -14.783 -35.001  23.876  1.00 15.61           O  
ANISOU 2330  O   ARG A 278     1973   2292   1664     33     17    295       O  
ATOM   2331  CB  ARG A 278     -13.429 -37.754  23.248  1.00 15.01           C  
ANISOU 2331  CB  ARG A 278     1913   2173   1616    -50     -3    228       C  
ATOM   2332  CG  ARG A 278     -12.469 -37.612  22.065  1.00 15.25           C  
ANISOU 2332  CG  ARG A 278     1940   2201   1653    -58    -10    210       C  
ATOM   2333  CD  ARG A 278     -12.190 -38.990  21.457  1.00 15.79           C  
ANISOU 2333  CD  ARG A 278     2005   2266   1727   -102    -15    179       C  
ATOM   2334  NE  ARG A 278     -10.979 -39.019  20.633  1.00 22.77           N  
ANISOU 2334  NE  ARG A 278     2897   3129   2624   -107    -22    158       N  
ATOM   2335  CZ  ARG A 278     -10.279 -40.124  20.394  1.00 19.51           C  
ANISOU 2335  CZ  ARG A 278     2496   2690   2226   -135    -25    129       C  
ATOM   2336  NH1 ARG A 278     -10.669 -41.274  20.929  1.00 17.53           N  
ANISOU 2336  NH1 ARG A 278     2252   2427   1981   -162    -22    117       N  
ATOM   2337  NH2 ARG A 278      -9.193 -40.087  19.630  1.00 16.75           N  
ANISOU 2337  NH2 ARG A 278     2153   2324   1887   -137    -30    112       N  
ATOM   2338  N   LYS A 279     -12.614 -34.520  23.527  1.00 15.90           N  
ANISOU 2338  N   LYS A 279     2046   2260   1736     42      4    265       N  
ATOM   2339  CA  LYS A 279     -12.898 -33.142  23.113  1.00 19.66           C  
ANISOU 2339  CA  LYS A 279     2509   2755   2204     75     15    292       C  
ATOM   2340  C   LYS A 279     -12.930 -33.009  21.592  1.00 25.53           C  
ANISOU 2340  C   LYS A 279     3224   3540   2937     65     17    296       C  
ATOM   2341  O   LYS A 279     -12.280 -33.774  20.887  1.00 25.94           O  
ANISOU 2341  O   LYS A 279     3273   3587   2994     36      7    273       O  
ATOM   2342  CB  LYS A 279     -11.838 -32.188  23.666  1.00 12.05           C  
ANISOU 2342  CB  LYS A 279     1576   1738   1266    104     15    286       C  
ATOM   2343  CG  LYS A 279     -11.649 -32.222  25.171  1.00 11.59           C  
ANISOU 2343  CG  LYS A 279     1549   1638   1216    119     11    277       C  
ATOM   2344  CD  LYS A 279     -12.963 -32.139  25.954  1.00 16.74           C  
ANISOU 2344  CD  LYS A 279     2195   2318   1846    133     22    301       C  
ATOM   2345  CE  LYS A 279     -12.727 -32.098  27.472  1.00 17.42           C  
ANISOU 2345  CE  LYS A 279     2315   2365   1939    153     19    293       C  
ATOM   2346  NZ  LYS A 279     -12.103 -33.344  28.060  1.00 11.69           N  
ANISOU 2346  NZ  LYS A 279     1609   1612   1222    130      5    268       N  
ATOM   2347  N   ARG A 280     -13.671 -32.030  21.082  1.00 18.34           N  
ANISOU 2347  N   ARG A 280     2290   2670   2009     90     29    328       N  
ATOM   2348  CA  ARG A 280     -13.604 -31.723  19.654  1.00 17.01           C  
ANISOU 2348  CA  ARG A 280     2095   2540   1828     89     33    337       C  
ATOM   2349  C   ARG A 280     -12.442 -30.759  19.408  1.00 19.11           C  
ANISOU 2349  C   ARG A 280     2380   2762   2118    112     39    338       C  
ATOM   2350  O   ARG A 280     -12.166 -29.882  20.228  1.00 17.85           O  
ANISOU 2350  O   ARG A 280     2243   2562   1977    141     47    346       O  
ATOM   2351  CB  ARG A 280     -14.918 -31.132  19.154  1.00 19.93           C  
ANISOU 2351  CB  ARG A 280     2429   2977   2166    108     45    374       C  
ATOM   2352  CG  ARG A 280     -16.122 -32.016  19.469  1.00 19.67           C  
ANISOU 2352  CG  ARG A 280     2374   2988   2111     85     40    374       C  
ATOM   2353  CD  ARG A 280     -17.388 -31.493  18.852  1.00 21.61           C  
ANISOU 2353  CD  ARG A 280     2578   3308   2324    101     50    409       C  
ATOM   2354  NE  ARG A 280     -18.544 -32.185  19.405  1.00 22.34           N  
ANISOU 2354  NE  ARG A 280     2651   3434   2401     84     48    412       N  
ATOM   2355  CZ  ARG A 280     -19.076 -33.297  18.904  1.00 21.65           C  
ANISOU 2355  CZ  ARG A 280     2537   3390   2300     41     37    394       C  
ATOM   2356  NH1 ARG A 280     -20.130 -33.844  19.500  1.00 24.34           N  
ANISOU 2356  NH1 ARG A 280     2861   3757   2632     26     39    399       N  
ATOM   2357  NH2 ARG A 280     -18.557 -33.859  17.817  1.00 20.23           N  
ANISOU 2357  NH2 ARG A 280     2346   3225   2114     13     26    369       N  
ATOM   2358  N   TRP A 281     -11.771 -30.915  18.275  1.00 14.12           N  
ANISOU 2358  N   TRP A 281     1739   2139   1488    100     36    328       N  
ATOM   2359  CA  TRP A 281     -10.521 -30.183  18.049  1.00 16.44           C  
ANISOU 2359  CA  TRP A 281     2050   2385   1810    115     42    324       C  
ATOM   2360  C   TRP A 281     -10.728 -28.682  17.919  1.00 18.79           C  
ANISOU 2360  C   TRP A 281     2345   2683   2111    158     64    361       C  
ATOM   2361  O   TRP A 281      -9.796 -27.897  18.115  1.00 17.10           O  
ANISOU 2361  O   TRP A 281     2150   2418   1928    175     72    359       O  
ATOM   2362  CB  TRP A 281      -9.802 -30.721  16.814  1.00 17.65           C  
ANISOU 2362  CB  TRP A 281     2193   2552   1962     93     37    308       C  
ATOM   2363  CG  TRP A 281      -9.271 -32.078  17.027  1.00 17.73           C  
ANISOU 2363  CG  TRP A 281     2215   2542   1980     55     19    269       C  
ATOM   2364  CD1 TRP A 281      -9.752 -33.240  16.498  1.00 16.72           C  
ANISOU 2364  CD1 TRP A 281     2070   2453   1830     22      9    252       C  
ATOM   2365  CD2 TRP A 281      -8.169 -32.438  17.865  1.00 15.93           C  
ANISOU 2365  CD2 TRP A 281     2018   2249   1784     47      9    242       C  
ATOM   2366  NE1 TRP A 281      -9.002 -34.304  16.945  1.00 21.00           N  
ANISOU 2366  NE1 TRP A 281     2634   2954   2392     -6     -3    217       N  
ATOM   2367  CE2 TRP A 281      -8.022 -33.835  17.784  1.00 17.81           C  
ANISOU 2367  CE2 TRP A 281     2259   2488   2020     11     -4    212       C  
ATOM   2368  CE3 TRP A 281      -7.283 -31.710  18.673  1.00 20.27           C  
ANISOU 2368  CE3 TRP A 281     2595   2742   2367     68     10    238       C  
ATOM   2369  CZ2 TRP A 281      -7.029 -34.520  18.475  1.00 14.31           C  
ANISOU 2369  CZ2 TRP A 281     1842   1992   1603     -2    -15    184       C  
ATOM   2370  CZ3 TRP A 281      -6.299 -32.394  19.362  1.00 20.78           C  
ANISOU 2370  CZ3 TRP A 281     2683   2757   2456     53     -4    207       C  
ATOM   2371  CH2 TRP A 281      -6.183 -33.788  19.261  1.00 20.51           C  
ANISOU 2371  CH2 TRP A 281     2650   2726   2416     21    -16    183       C  
ATOM   2372  N   GLU A 282     -11.950 -28.294  17.577  1.00 17.72           N  
ANISOU 2372  N   GLU A 282     2182   2605   1945    175     75    394       N  
ATOM   2373  CA  GLU A 282     -12.283 -26.891  17.372  1.00 22.08           C  
ANISOU 2373  CA  GLU A 282     2729   3163   2497    219    100    434       C  
ATOM   2374  C   GLU A 282     -12.059 -26.035  18.619  1.00 18.02           C  
ANISOU 2374  C   GLU A 282     2246   2590   2012    245    110    435       C  
ATOM   2375  O   GLU A 282     -11.806 -24.835  18.523  1.00 21.37           O  
ANISOU 2375  O   GLU A 282     2678   2989   2454    277    131    457       O  
ATOM   2376  CB  GLU A 282     -13.731 -26.749  16.868  1.00 23.89           C  
ANISOU 2376  CB  GLU A 282     2921   3470   2685    234    108    469       C  
ATOM   2377  CG  GLU A 282     -13.923 -27.113  15.393  1.00 24.12           C  
ANISOU 2377  CG  GLU A 282     2915   3564   2684    223    105    477       C  
ATOM   2378  CD  GLU A 282     -14.131 -28.611  15.143  1.00 32.25           C  
ANISOU 2378  CD  GLU A 282     3931   4627   3695    174     80    442       C  
ATOM   2379  OE1 GLU A 282     -14.075 -29.414  16.104  1.00 26.65           O  
ANISOU 2379  OE1 GLU A 282     3240   3886   2998    148     66    414       O  
ATOM   2380  OE2 GLU A 282     -14.355 -28.988  13.967  1.00 35.47           O  
ANISOU 2380  OE2 GLU A 282     4309   5092   4074    162     75    443       O  
ATOM   2381  N   ARG A 283     -12.135 -26.635  19.794  1.00 18.51           N  
ANISOU 2381  N   ARG A 283     2328   2627   2080    231     95    412       N  
ATOM   2382  CA  ARG A 283     -11.917 -25.849  21.007  1.00 23.86           C  
ANISOU 2382  CA  ARG A 283     3035   3250   2780    256    103    409       C  
ATOM   2383  C   ARG A 283     -10.508 -25.245  21.094  1.00 19.13           C  
ANISOU 2383  C   ARG A 283     2461   2585   2221    260    105    389       C  
ATOM   2384  O   ARG A 283     -10.306 -24.280  21.810  1.00 17.24           O  
ANISOU 2384  O   ARG A 283     2242   2305   2003    285    117    390       O  
ATOM   2385  CB  ARG A 283     -12.217 -26.658  22.273  1.00 24.15           C  
ANISOU 2385  CB  ARG A 283     3089   3274   2811    242     87    387       C  
ATOM   2386  CG  ARG A 283     -11.326 -27.869  22.474  1.00 23.06           C  
ANISOU 2386  CG  ARG A 283     2964   3112   2685    204     62    348       C  
ATOM   2387  CD  ARG A 283     -10.992 -28.066  23.958  1.00 33.52           C  
ANISOU 2387  CD  ARG A 283     4322   4390   4023    207     52    325       C  
ATOM   2388  NE  ARG A 283     -12.183 -28.252  24.784  1.00 44.40           N  
ANISOU 2388  NE  ARG A 283     5698   5794   5378    217     56    340       N  
ATOM   2389  CZ  ARG A 283     -12.171 -28.318  26.114  1.00 40.28           C  
ANISOU 2389  CZ  ARG A 283     5202   5243   4859    228     51    328       C  
ATOM   2390  NH1 ARG A 283     -11.033 -28.203  26.788  1.00 40.36           N  
ANISOU 2390  NH1 ARG A 283     5241   5200   4893    229     40    299       N  
ATOM   2391  NH2 ARG A 283     -13.303 -28.493  26.770  1.00 38.76           N  
ANISOU 2391  NH2 ARG A 283     5006   5079   4644    237     58    346       N  
ATOM   2392  N   PHE A 284      -9.545 -25.808  20.370  1.00 18.17           N  
ANISOU 2392  N   PHE A 284     2337   2454   2111    234     94    368       N  
ATOM   2393  CA  PHE A 284      -8.174 -25.305  20.427  1.00 14.05           C  
ANISOU 2393  CA  PHE A 284     1835   1874   1631    234     95    348       C  
ATOM   2394  C   PHE A 284      -7.924 -24.208  19.401  1.00 16.47           C  
ANISOU 2394  C   PHE A 284     2129   2179   1949    257    121    377       C  
ATOM   2395  O   PHE A 284      -6.839 -23.639  19.340  1.00 20.06           O  
ANISOU 2395  O   PHE A 284     2596   2585   2440    259    128    365       O  
ATOM   2396  CB  PHE A 284      -7.194 -26.453  20.236  1.00 12.75           C  
ANISOU 2396  CB  PHE A 284     1675   1695   1475    198     71    312       C  
ATOM   2397  CG  PHE A 284      -7.348 -27.514  21.273  1.00 15.57           C  
ANISOU 2397  CG  PHE A 284     2046   2045   1823    179     49    287       C  
ATOM   2398  CD1 PHE A 284      -6.951 -27.273  22.581  1.00 19.39           C  
ANISOU 2398  CD1 PHE A 284     2558   2484   2326    188     41    267       C  
ATOM   2399  CD2 PHE A 284      -7.938 -28.723  20.966  1.00 14.48           C  
ANISOU 2399  CD2 PHE A 284     1894   1949   1658    153     37    283       C  
ATOM   2400  CE1 PHE A 284      -7.109 -28.233  23.553  1.00 17.92           C  
ANISOU 2400  CE1 PHE A 284     2385   2294   2130    175     23    248       C  
ATOM   2401  CE2 PHE A 284      -8.094 -29.693  21.936  1.00 20.28           C  
ANISOU 2401  CE2 PHE A 284     2642   2675   2388    137     21    263       C  
ATOM   2402  CZ  PHE A 284      -7.686 -29.449  23.232  1.00 19.51           C  
ANISOU 2402  CZ  PHE A 284     2573   2533   2307    150     14    248       C  
ATOM   2403  N   VAL A 285      -8.939 -23.919  18.598  1.00 17.01           N  
ANISOU 2403  N   VAL A 285     2172   2304   1988    274    137    415       N  
ATOM   2404  CA  VAL A 285      -8.831 -22.883  17.575  1.00 15.13           C  
ANISOU 2404  CA  VAL A 285     1920   2073   1756    300    166    450       C  
ATOM   2405  C   VAL A 285      -9.205 -21.525  18.144  1.00 19.44           C  
ANISOU 2405  C   VAL A 285     2478   2590   2318    340    194    476       C  
ATOM   2406  O   VAL A 285     -10.203 -21.396  18.843  1.00 25.56           O  
ANISOU 2406  O   VAL A 285     3254   3382   3075    356    196    488       O  
ATOM   2407  CB  VAL A 285      -9.760 -23.184  16.392  1.00 17.36           C  
ANISOU 2407  CB  VAL A 285     2167   2436   1994    304    171    482       C  
ATOM   2408  CG1 VAL A 285      -9.635 -22.095  15.331  1.00 15.97           C  
ANISOU 2408  CG1 VAL A 285     1977   2269   1822    337    203    523       C  
ATOM   2409  CG2 VAL A 285      -9.456 -24.549  15.821  1.00 15.22           C  
ANISOU 2409  CG2 VAL A 285     1885   2194   1706    264    144    453       C  
ATOM   2410  N   HIS A 286      -8.400 -20.510  17.848  1.00 15.71           N  
ANISOU 2410  N   HIS A 286     2015   2072   1883    356    218    484       N  
ATOM   2411  CA  HIS A 286      -8.680 -19.159  18.321  1.00 16.81           C  
ANISOU 2411  CA  HIS A 286     2168   2177   2044    394    249    507       C  
ATOM   2412  C   HIS A 286      -8.181 -18.144  17.297  1.00 18.14           C  
ANISOU 2412  C   HIS A 286     2328   2328   2235    416    284    539       C  
ATOM   2413  O   HIS A 286      -7.607 -18.528  16.274  1.00 21.26           O  
ANISOU 2413  O   HIS A 286     2708   2741   2628    402    282    542       O  
ATOM   2414  CB  HIS A 286      -8.066 -18.927  19.704  1.00 19.10           C  
ANISOU 2414  CB  HIS A 286     2492   2398   2369    387    239    467       C  
ATOM   2415  CG  HIS A 286      -6.617 -19.291  19.790  1.00 19.90           C  
ANISOU 2415  CG  HIS A 286     2605   2450   2505    356    221    424       C  
ATOM   2416  ND1 HIS A 286      -5.653 -18.681  19.021  1.00 15.99           N  
ANISOU 2416  ND1 HIS A 286     2107   1923   2045    356    240    429       N  
ATOM   2417  CD2 HIS A 286      -5.969 -20.191  20.568  1.00 15.79           C  
ANISOU 2417  CD2 HIS A 286     2099   1909   1991    325    187    378       C  
ATOM   2418  CE1 HIS A 286      -4.471 -19.201  19.306  1.00 15.81           C  
ANISOU 2418  CE1 HIS A 286     2094   1863   2049    326    217    387       C  
ATOM   2419  NE2 HIS A 286      -4.636 -20.116  20.244  1.00 19.04           N  
ANISOU 2419  NE2 HIS A 286     2515   2280   2441    308    185    355       N  
ATOM   2420  N   SER A 287      -8.404 -16.857  17.552  1.00 16.89           N  
ANISOU 2420  N   SER A 287     2180   2136   2100    452    319    565       N  
ATOM   2421  CA  SER A 287      -8.170 -15.850  16.518  1.00 20.35           C  
ANISOU 2421  CA  SER A 287     2608   2567   2556    480    359    607       C  
ATOM   2422  C   SER A 287      -6.711 -15.770  16.066  1.00 21.62           C  
ANISOU 2422  C   SER A 287     2776   2678   2761    458    362    585       C  
ATOM   2423  O   SER A 287      -6.420 -15.305  14.962  1.00 21.89           O  
ANISOU 2423  O   SER A 287     2796   2721   2803    473    389    619       O  
ATOM   2424  CB  SER A 287      -8.684 -14.483  16.969  1.00 32.23           C  
ANISOU 2424  CB  SER A 287     4126   4037   4081    524    400    637       C  
ATOM   2425  OG  SER A 287      -8.160 -14.143  18.238  1.00 46.24           O  
ANISOU 2425  OG  SER A 287     5934   5740   5895    514    394    594       O  
ATOM   2426  N   GLU A 288      -5.804 -16.247  16.911  1.00 17.86           N  
ANISOU 2426  N   GLU A 288     2319   2155   2313    424    334    531       N  
ATOM   2427  CA  GLU A 288      -4.370 -16.171  16.624  1.00 20.78           C  
ANISOU 2427  CA  GLU A 288     2694   2473   2728    402    335    506       C  
ATOM   2428  C   GLU A 288      -3.795 -17.389  15.907  1.00 22.45           C  
ANISOU 2428  C   GLU A 288     2890   2720   2921    369    307    488       C  
ATOM   2429  O   GLU A 288      -2.641 -17.354  15.475  1.00 25.72           O  
ANISOU 2429  O   GLU A 288     3304   3101   3370    353    310    474       O  
ATOM   2430  CB  GLU A 288      -3.574 -15.896  17.896  1.00 19.55           C  
ANISOU 2430  CB  GLU A 288     2567   2245   2618    385    323    456       C  
ATOM   2431  CG  GLU A 288      -3.702 -14.474  18.401  1.00 25.22           C  
ANISOU 2431  CG  GLU A 288     3302   2909   3372    414    360    468       C  
ATOM   2432  CD  GLU A 288      -5.077 -14.186  18.980  1.00 28.04           C  
ANISOU 2432  CD  GLU A 288     3665   3294   3696    445    368    491       C  
ATOM   2433  OE1 GLU A 288      -5.539 -14.977  19.839  1.00 28.20           O  
ANISOU 2433  OE1 GLU A 288     3692   3335   3687    433    334    465       O  
ATOM   2434  OE2 GLU A 288      -5.690 -13.170  18.577  1.00 32.21           O  
ANISOU 2434  OE2 GLU A 288     4190   3821   4228    483    409    537       O  
ATOM   2435  N   ASN A 289      -4.574 -18.463  15.789  1.00 17.01           N  
ANISOU 2435  N   ASN A 289     2188   2093   2180    358    280    487       N  
ATOM   2436  CA  ASN A 289      -4.109 -19.631  15.040  1.00 14.65           C  
ANISOU 2436  CA  ASN A 289     1875   1829   1862    328    256    470       C  
ATOM   2437  C   ASN A 289      -5.053 -20.086  13.921  1.00 17.87           C  
ANISOU 2437  C   ASN A 289     2254   2320   2216    338    259    505       C  
ATOM   2438  O   ASN A 289      -4.719 -20.995  13.165  1.00 20.11           O  
ANISOU 2438  O   ASN A 289     2524   2636   2480    315    243    493       O  
ATOM   2439  CB  ASN A 289      -3.796 -20.808  15.983  1.00 13.48           C  
ANISOU 2439  CB  ASN A 289     1740   1670   1711    292    214    419       C  
ATOM   2440  CG  ASN A 289      -5.048 -21.359  16.686  1.00 13.63           C  
ANISOU 2440  CG  ASN A 289     1760   1730   1690    294    196    419       C  
ATOM   2441  OD1 ASN A 289      -6.176 -21.196  16.210  1.00 14.95           O  
ANISOU 2441  OD1 ASN A 289     1909   1951   1821    314    208    455       O  
ATOM   2442  ND2 ASN A 289      -4.841 -22.036  17.816  1.00 14.30           N  
ANISOU 2442  ND2 ASN A 289     1863   1790   1779    273    168    379       N  
ATOM   2443  N   GLN A 290      -6.217 -19.447  13.798  1.00 16.88           N  
ANISOU 2443  N   GLN A 290     2118   2232   2065    371    279    547       N  
ATOM   2444  CA  GLN A 290      -7.253 -19.927  12.870  1.00 17.56           C  
ANISOU 2444  CA  GLN A 290     2174   2405   2094    380    276    577       C  
ATOM   2445  C   GLN A 290      -6.783 -19.966  11.405  1.00 19.52           C  
ANISOU 2445  C   GLN A 290     2400   2685   2330    383    290    598       C  
ATOM   2446  O   GLN A 290      -7.243 -20.786  10.606  1.00 20.97           O  
ANISOU 2446  O   GLN A 290     2561   2939   2468    373    274    600       O  
ATOM   2447  CB  GLN A 290      -8.534 -19.091  13.006  1.00 18.94           C  
ANISOU 2447  CB  GLN A 290     2339   2612   2247    421    299    622       C  
ATOM   2448  CG  GLN A 290      -8.395 -17.681  12.463  1.00 28.56           C  
ANISOU 2448  CG  GLN A 290     3557   3806   3488    464    346    670       C  
ATOM   2449  CD  GLN A 290      -9.456 -16.725  12.985  1.00 44.27           C  
ANISOU 2449  CD  GLN A 290     5548   5799   5472    506    371    706       C  
ATOM   2450  OE1 GLN A 290     -10.498 -17.144  13.491  1.00 48.16           O  
ANISOU 2450  OE1 GLN A 290     6033   6333   5931    507    355    706       O  
ATOM   2451  NE2 GLN A 290      -9.186 -15.424  12.871  1.00 46.74           N  
ANISOU 2451  NE2 GLN A 290     5872   6066   5822    541    414    739       N  
ATOM   2452  N   HIS A 291      -5.878 -19.069  11.049  1.00 22.27           N  
ANISOU 2452  N   HIS A 291     2757   2986   2720    398    319    613       N  
ATOM   2453  CA  HIS A 291      -5.339 -19.049   9.692  1.00 21.04           C  
ANISOU 2453  CA  HIS A 291     2583   2855   2555    405    336    634       C  
ATOM   2454  C   HIS A 291      -4.492 -20.299   9.375  1.00 22.80           C  
ANISOU 2454  C   HIS A 291     2805   3084   2774    362    305    589       C  
ATOM   2455  O   HIS A 291      -4.117 -20.524   8.221  1.00 21.85           O  
ANISOU 2455  O   HIS A 291     2669   2996   2637    363    312    601       O  
ATOM   2456  CB  HIS A 291      -4.511 -17.780   9.473  1.00 22.46           C  
ANISOU 2456  CB  HIS A 291     2773   2972   2787    429    378    660       C  
ATOM   2457  CG  HIS A 291      -3.267 -17.723  10.303  1.00 18.36           C  
ANISOU 2457  CG  HIS A 291     2279   2367   2328    401    371    616       C  
ATOM   2458  ND1 HIS A 291      -3.288 -17.477  11.659  1.00 20.87           N  
ANISOU 2458  ND1 HIS A 291     2621   2633   2676    393    360    587       N  
ATOM   2459  CD2 HIS A 291      -1.967 -17.912   9.976  1.00 23.04           C  
ANISOU 2459  CD2 HIS A 291     2875   2922   2956    379    371    594       C  
ATOM   2460  CE1 HIS A 291      -2.054 -17.500  12.128  1.00 25.00           C  
ANISOU 2460  CE1 HIS A 291     3159   3090   3248    368    353    549       C  
ATOM   2461  NE2 HIS A 291      -1.232 -17.765  11.126  1.00 24.33           N  
ANISOU 2461  NE2 HIS A 291     3061   3013   3169    358    359    552       N  
ATOM   2462  N   LEU A 292      -4.186 -21.097  10.396  1.00 18.11           N  
ANISOU 2462  N   LEU A 292     2230   2458   2195    327    271    539       N  
ATOM   2463  CA  LEU A 292      -3.398 -22.322  10.213  1.00 20.91           C  
ANISOU 2463  CA  LEU A 292     2586   2812   2548    287    243    496       C  
ATOM   2464  C   LEU A 292      -4.297 -23.557  10.264  1.00 22.19           C  
ANISOU 2464  C   LEU A 292     2737   3034   2660    265    210    476       C  
ATOM   2465  O   LEU A 292      -3.842 -24.690  10.064  1.00 18.70           O  
ANISOU 2465  O   LEU A 292     2295   2600   2209    232    187    441       O  
ATOM   2466  CB  LEU A 292      -2.331 -22.431  11.299  1.00 18.13           C  
ANISOU 2466  CB  LEU A 292     2260   2382   2247    264    228    453       C  
ATOM   2467  CG  LEU A 292      -1.379 -21.236  11.400  1.00 20.31           C  
ANISOU 2467  CG  LEU A 292     2547   2592   2580    279    258    463       C  
ATOM   2468  CD1 LEU A 292      -0.432 -21.394  12.571  1.00 16.41           C  
ANISOU 2468  CD1 LEU A 292     2076   2029   2132    255    238    417       C  
ATOM   2469  CD2 LEU A 292      -0.606 -21.064  10.098  1.00 21.98           C  
ANISOU 2469  CD2 LEU A 292     2743   2811   2799    285    281    483       C  
ATOM   2470  N   VAL A 293      -5.577 -23.332  10.528  1.00 17.53           N  
ANISOU 2470  N   VAL A 293     2137   2484   2039    282    211    499       N  
ATOM   2471  CA  VAL A 293      -6.515 -24.428  10.739  1.00 15.85           C  
ANISOU 2471  CA  VAL A 293     1914   2324   1784    259    183    480       C  
ATOM   2472  C   VAL A 293      -7.551 -24.489   9.629  1.00 17.89           C  
ANISOU 2472  C   VAL A 293     2138   2671   1988    274    188    512       C  
ATOM   2473  O   VAL A 293      -8.038 -23.473   9.146  1.00 25.60           O  
ANISOU 2473  O   VAL A 293     3101   3672   2953    314    215    559       O  
ATOM   2474  CB  VAL A 293      -7.238 -24.317  12.112  1.00 18.48           C  
ANISOU 2474  CB  VAL A 293     2261   2636   2124    261    173    474       C  
ATOM   2475  CG1 VAL A 293      -8.172 -25.501  12.336  1.00 25.32           C  
ANISOU 2475  CG1 VAL A 293     3117   3554   2952    235    146    454       C  
ATOM   2476  CG2 VAL A 293      -6.238 -24.232  13.244  1.00 19.51           C  
ANISOU 2476  CG2 VAL A 293     2425   2684   2304    249    166    441       C  
ATOM   2477  N   SER A 294      -7.879 -25.702   9.231  1.00 20.35           N  
ANISOU 2477  N   SER A 294     2436   3032   2265    243    163    486       N  
ATOM   2478  CA  SER A 294      -8.859 -25.933   8.198  1.00 21.02           C  
ANISOU 2478  CA  SER A 294     2485   3208   2293    251    162    507       C  
ATOM   2479  C   SER A 294      -9.530 -27.226   8.589  1.00 20.12           C  
ANISOU 2479  C   SER A 294     2365   3125   2155    211    130    469       C  
ATOM   2480  O   SER A 294      -8.993 -27.968   9.403  1.00 17.73           O  
ANISOU 2480  O   SER A 294     2085   2772   1880    179    113    429       O  
ATOM   2481  CB  SER A 294      -8.160 -26.082   6.841  1.00 21.16           C  
ANISOU 2481  CB  SER A 294     2491   3253   2297    251    170    509       C  
ATOM   2482  OG  SER A 294      -7.153 -27.082   6.890  1.00 18.82           O  
ANISOU 2482  OG  SER A 294     2212   2920   2020    212    152    460       O  
ATOM   2483  N   PRO A 295     -10.704 -27.511   8.017  1.00 21.46           N  
ANISOU 2483  N   PRO A 295     2501   3379   2275    212    123    482       N  
ATOM   2484  CA  PRO A 295     -11.323 -28.808   8.297  1.00 18.83           C  
ANISOU 2484  CA  PRO A 295     2159   3076   1921    169     94    443       C  
ATOM   2485  C   PRO A 295     -10.376 -29.955   7.936  1.00 20.45           C  
ANISOU 2485  C   PRO A 295     2376   3259   2134    128     78    394       C  
ATOM   2486  O   PRO A 295     -10.314 -30.946   8.660  1.00 14.43           O  
ANISOU 2486  O   PRO A 295     1628   2469   1386     91     59    355       O  
ATOM   2487  CB  PRO A 295     -12.551 -28.812   7.380  1.00 22.58           C  
ANISOU 2487  CB  PRO A 295     2590   3652   2339    180     92    467       C  
ATOM   2488  CG  PRO A 295     -12.860 -27.352   7.173  1.00 26.98           C  
ANISOU 2488  CG  PRO A 295     3137   4221   2891    236    121    526       C  
ATOM   2489  CD  PRO A 295     -11.528 -26.673   7.123  1.00 23.95           C  
ANISOU 2489  CD  PRO A 295     2783   3765   2551    253    141    533       C  
ATOM   2490  N   GLU A 296      -9.656 -29.816   6.826  1.00 18.47           N  
ANISOU 2490  N   GLU A 296     2120   3023   1876    136     87    397       N  
ATOM   2491  CA  GLU A 296      -8.674 -30.821   6.409  1.00 15.13           C  
ANISOU 2491  CA  GLU A 296     1709   2577   1461    102     76    353       C  
ATOM   2492  C   GLU A 296      -7.577 -31.050   7.450  1.00 13.28           C  
ANISOU 2492  C   GLU A 296     1514   2250   1283     86     72    326       C  
ATOM   2493  O   GLU A 296      -7.228 -32.197   7.727  1.00 16.78           O  
ANISOU 2493  O   GLU A 296     1970   2672   1736     49     55    283       O  
ATOM   2494  CB  GLU A 296      -8.040 -30.457   5.067  1.00 19.47           C  
ANISOU 2494  CB  GLU A 296     2248   3155   1995    121     91    368       C  
ATOM   2495  CG  GLU A 296      -8.990 -30.591   3.886  1.00 19.29           C  
ANISOU 2495  CG  GLU A 296     2186   3235   1909    128     88    381       C  
ATOM   2496  CD  GLU A 296      -9.898 -29.395   3.724  1.00 31.25           C  
ANISOU 2496  CD  GLU A 296     3677   4794   3401    175    106    439       C  
ATOM   2497  OE1 GLU A 296      -9.616 -28.335   4.327  1.00 25.80           O  
ANISOU 2497  OE1 GLU A 296     3005   4052   2747    206    127    472       O  
ATOM   2498  OE2 GLU A 296     -10.900 -29.522   2.985  1.00 30.89           O  
ANISOU 2498  OE2 GLU A 296     3596   4837   3302    180     99    450       O  
ATOM   2499  N   ALA A 297      -7.042 -29.972   8.027  1.00 16.22           N  
ANISOU 2499  N   ALA A 297     1903   2566   1692    115     89    351       N  
ATOM   2500  CA  ALA A 297      -6.010 -30.101   9.067  1.00 15.01           C  
ANISOU 2500  CA  ALA A 297     1784   2328   1591    103     84    326       C  
ATOM   2501  C   ALA A 297      -6.546 -30.827  10.295  1.00 16.97           C  
ANISOU 2501  C   ALA A 297     2045   2558   1845     80     64    302       C  
ATOM   2502  O   ALA A 297      -5.874 -31.700  10.841  1.00 14.90           O  
ANISOU 2502  O   ALA A 297     1803   2253   1605     52     50    265       O  
ATOM   2503  CB  ALA A 297      -5.459 -28.741   9.470  1.00 10.57           C  
ANISOU 2503  CB  ALA A 297     1235   1715   1066    138    106    356       C  
ATOM   2504  N   LEU A 298      -7.753 -30.467  10.734  1.00 17.46           N  
ANISOU 2504  N   LEU A 298     2095   2652   1887     92     65    325       N  
ATOM   2505  CA  LEU A 298      -8.337 -31.094  11.918  1.00 15.81           C  
ANISOU 2505  CA  LEU A 298     1897   2428   1682     73     49    307       C  
ATOM   2506  C   LEU A 298      -8.621 -32.578  11.694  1.00 20.87           C  
ANISOU 2506  C   LEU A 298     2531   3096   2304     30     30    270       C  
ATOM   2507  O   LEU A 298      -8.366 -33.406  12.573  1.00 18.70           O  
ANISOU 2507  O   LEU A 298     2276   2780   2048      6     17    240       O  
ATOM   2508  CB  LEU A 298      -9.582 -30.348  12.392  1.00 15.69           C  
ANISOU 2508  CB  LEU A 298     1869   2444   1650     99     58    342       C  
ATOM   2509  CG  LEU A 298      -9.293 -28.912  12.841  1.00 17.81           C  
ANISOU 2509  CG  LEU A 298     2152   2673   1945    141     79    374       C  
ATOM   2510  CD1 LEU A 298     -10.552 -28.260  13.397  1.00 17.28           C  
ANISOU 2510  CD1 LEU A 298     2073   2633   1860    166     87    406       C  
ATOM   2511  CD2 LEU A 298      -8.190 -28.912  13.876  1.00 21.82           C  
ANISOU 2511  CD2 LEU A 298     2695   3098   2499    134     73    348       C  
ATOM   2512  N   ASP A 299      -9.107 -32.930  10.512  1.00 15.45           N  
ANISOU 2512  N   ASP A 299     1816   2476   1580     21     28    269       N  
ATOM   2513  CA  ASP A 299      -9.361 -34.332  10.236  1.00 17.28           C  
ANISOU 2513  CA  ASP A 299     2040   2732   1795    -23     12    230       C  
ATOM   2514  C   ASP A 299      -8.050 -35.116  10.185  1.00 20.94           C  
ANISOU 2514  C   ASP A 299     2530   3141   2287    -46      7    192       C  
ATOM   2515  O   ASP A 299      -7.965 -36.223  10.689  1.00 16.04           O  
ANISOU 2515  O   ASP A 299     1922   2495   1677    -78     -5    159       O  
ATOM   2516  CB  ASP A 299     -10.146 -34.524   8.940  1.00 20.75           C  
ANISOU 2516  CB  ASP A 299     2441   3258   2184    -29     10    233       C  
ATOM   2517  CG  ASP A 299     -10.443 -35.986   8.665  1.00 24.08           C  
ANISOU 2517  CG  ASP A 299     2856   3703   2592    -78     -7    187       C  
ATOM   2518  OD1 ASP A 299     -11.171 -36.611   9.464  1.00 24.36           O  
ANISOU 2518  OD1 ASP A 299     2890   3735   2631   -101    -15    175       O  
ATOM   2519  OD2 ASP A 299      -9.942 -36.520   7.664  1.00 18.58           O  
ANISOU 2519  OD2 ASP A 299     2153   3024   1881    -94     -9    163       O  
ATOM   2520  N   PHE A 300      -7.029 -34.531   9.572  1.00 13.76           N  
ANISOU 2520  N   PHE A 300     1626   2212   1390    -26     18    201       N  
ATOM   2521  CA  PHE A 300      -5.727 -35.197   9.463  1.00 12.88           C  
ANISOU 2521  CA  PHE A 300     1537   2051   1306    -43     15    168       C  
ATOM   2522  C   PHE A 300      -5.151 -35.408  10.852  1.00 13.21           C  
ANISOU 2522  C   PHE A 300     1610   2020   1390    -48      8    155       C  
ATOM   2523  O   PHE A 300      -4.756 -36.511  11.189  1.00 12.95           O  
ANISOU 2523  O   PHE A 300     1592   1958   1369    -76     -2    121       O  
ATOM   2524  CB  PHE A 300      -4.785 -34.367   8.607  1.00 13.01           C  
ANISOU 2524  CB  PHE A 300     1551   2061   1330    -18     31    186       C  
ATOM   2525  CG  PHE A 300      -3.400 -34.936   8.494  1.00 14.47           C  
ANISOU 2525  CG  PHE A 300     1757   2196   1546    -31     31    157       C  
ATOM   2526  CD1 PHE A 300      -3.216 -36.289   8.269  1.00 13.16           C  
ANISOU 2526  CD1 PHE A 300     1596   2030   1374    -66     19    116       C  
ATOM   2527  CD2 PHE A 300      -2.289 -34.116   8.604  1.00 16.21           C  
ANISOU 2527  CD2 PHE A 300     1990   2367   1802     -9     43    171       C  
ATOM   2528  CE1 PHE A 300      -1.939 -36.818   8.150  1.00 18.29           C  
ANISOU 2528  CE1 PHE A 300     2265   2635   2051    -75     20     91       C  
ATOM   2529  CE2 PHE A 300      -1.004 -34.645   8.491  1.00 16.16           C  
ANISOU 2529  CE2 PHE A 300     1999   2317   1824    -20     42    145       C  
ATOM   2530  CZ  PHE A 300      -0.837 -35.988   8.272  1.00 15.65           C  
ANISOU 2530  CZ  PHE A 300     1940   2256   1751    -51     31    107       C  
ATOM   2531  N   LEU A 301      -5.119 -34.352  11.659  1.00 13.73           N  
ANISOU 2531  N   LEU A 301     1686   2056   1477    -20     15    181       N  
ATOM   2532  CA  LEU A 301      -4.614 -34.454  13.029  1.00 12.83           C  
ANISOU 2532  CA  LEU A 301     1600   1878   1398    -21      7    169       C  
ATOM   2533  C   LEU A 301      -5.380 -35.517  13.809  1.00 14.49           C  
ANISOU 2533  C   LEU A 301     1816   2092   1599    -47     -6    150       C  
ATOM   2534  O   LEU A 301      -4.781 -36.352  14.497  1.00 13.42           O  
ANISOU 2534  O   LEU A 301     1701   1913   1485    -64    -15    124       O  
ATOM   2535  CB  LEU A 301      -4.721 -33.109  13.746  1.00 13.19           C  
ANISOU 2535  CB  LEU A 301     1651   1901   1459     14     16    199       C  
ATOM   2536  CG  LEU A 301      -4.337 -33.111  15.227  1.00 15.24           C  
ANISOU 2536  CG  LEU A 301     1938   2102   1749     16      7    187       C  
ATOM   2537  CD1 LEU A 301      -2.839 -33.453  15.417  1.00 11.44           C  
ANISOU 2537  CD1 LEU A 301     1477   1565   1304      8      1    160       C  
ATOM   2538  CD2 LEU A 301      -4.686 -31.755  15.867  1.00 16.30           C  
ANISOU 2538  CD2 LEU A 301     2077   2224   1893     50     18    216       C  
ATOM   2539  N   ASP A 302      -6.709 -35.476  13.696  1.00 11.08           N  
ANISOU 2539  N   ASP A 302     1361   1712   1135    -48     -6    166       N  
ATOM   2540  CA  ASP A 302      -7.570 -36.438  14.370  1.00 12.93           C  
ANISOU 2540  CA  ASP A 302     1596   1956   1360    -74    -15    152       C  
ATOM   2541  C   ASP A 302      -7.205 -37.876  14.023  1.00 14.36           C  
ANISOU 2541  C   ASP A 302     1783   2130   1543   -113    -22    112       C  
ATOM   2542  O   ASP A 302      -7.375 -38.778  14.838  1.00 14.26           O  
ANISOU 2542  O   ASP A 302     1784   2093   1541   -133    -28     95       O  
ATOM   2543  CB  ASP A 302      -9.031 -36.198  13.981  1.00 16.89           C  
ANISOU 2543  CB  ASP A 302     2065   2528   1824    -72    -12    173       C  
ATOM   2544  CG  ASP A 302      -9.992 -36.992  14.840  1.00 23.97           C  
ANISOU 2544  CG  ASP A 302     2961   3431   2715    -94    -18    166       C  
ATOM   2545  OD1 ASP A 302      -9.848 -36.948  16.076  1.00 18.24           O  
ANISOU 2545  OD1 ASP A 302     2259   2659   2011    -86    -19    168       O  
ATOM   2546  OD2 ASP A 302     -10.873 -37.676  14.276  1.00 22.53           O  
ANISOU 2546  OD2 ASP A 302     2753   3300   2507   -121    -22    156       O  
ATOM   2547  N   LYS A 303      -6.727 -38.090  12.798  1.00 13.25           N  
ANISOU 2547  N   LYS A 303     1631   2011   1392   -122    -20     99       N  
ATOM   2548  CA  LYS A 303      -6.422 -39.432  12.327  1.00  7.65           C  
ANISOU 2548  CA  LYS A 303      926   1298    682   -159    -25     60       C  
ATOM   2549  C   LYS A 303      -4.999 -39.873  12.681  1.00 10.87           C  
ANISOU 2549  C   LYS A 303     1364   1639   1127   -160    -26     39       C  
ATOM   2550  O   LYS A 303      -4.669 -41.047  12.555  1.00 12.84           O  
ANISOU 2550  O   LYS A 303     1624   1871   1383   -188    -28      7       O  
ATOM   2551  CB  LYS A 303      -6.667 -39.535  10.817  1.00  9.15           C  
ANISOU 2551  CB  LYS A 303     1089   1550    838   -169    -23     52       C  
ATOM   2552  CG  LYS A 303      -8.162 -39.570  10.453  1.00 15.23           C  
ANISOU 2552  CG  LYS A 303     1826   2394   1569   -180    -27     61       C  
ATOM   2553  CD  LYS A 303      -8.372 -39.403   8.956  1.00 24.26           C  
ANISOU 2553  CD  LYS A 303     2940   3605   2674   -180    -25     59       C  
ATOM   2554  CE  LYS A 303      -9.761 -39.859   8.543  1.00 23.95           C  
ANISOU 2554  CE  LYS A 303     2866   3638   2595   -204    -33     52       C  
ATOM   2555  NZ  LYS A 303     -10.780 -39.395   9.526  1.00 25.12           N  
ANISOU 2555  NZ  LYS A 303     3006   3794   2744   -193    -34     80       N  
ATOM   2556  N   LEU A 304      -4.166 -38.936  13.132  1.00 14.49           N  
ANISOU 2556  N   LEU A 304     1836   2059   1609   -130    -23     57       N  
ATOM   2557  CA  LEU A 304      -2.828 -39.277  13.625  1.00 14.62           C  
ANISOU 2557  CA  LEU A 304     1880   2014   1663   -128    -25     39       C  
ATOM   2558  C   LEU A 304      -2.880 -39.565  15.129  1.00 15.95           C  
ANISOU 2558  C   LEU A 304     2070   2139   1851   -126    -33     38       C  
ATOM   2559  O   LEU A 304      -2.313 -40.546  15.612  1.00 11.66           O  
ANISOU 2559  O   LEU A 304     1546   1558   1326   -140    -37     16       O  
ATOM   2560  CB  LEU A 304      -1.850 -38.131  13.367  1.00 11.76           C  
ANISOU 2560  CB  LEU A 304     1518   1631   1319    -99    -19     56       C  
ATOM   2561  CG  LEU A 304      -1.496 -37.772  11.918  1.00 12.22           C  
ANISOU 2561  CG  LEU A 304     1558   1723   1363    -94     -8     61       C  
ATOM   2562  CD1 LEU A 304      -0.530 -36.593  11.885  1.00 14.93           C  
ANISOU 2562  CD1 LEU A 304     1903   2035   1732    -64      1     81       C  
ATOM   2563  CD2 LEU A 304      -0.901 -38.969  11.197  1.00 16.97           C  
ANISOU 2563  CD2 LEU A 304     2164   2322   1963   -119     -9     27       C  
ATOM   2564  N   LEU A 305      -3.570 -38.698  15.863  1.00  9.26           N  
ANISOU 2564  N   LEU A 305     1220   1298    999   -106    -33     64       N  
ATOM   2565  CA  LEU A 305      -3.639 -38.809  17.314  1.00  8.11           C  
ANISOU 2565  CA  LEU A 305     1096   1117    869    -98    -40     65       C  
ATOM   2566  C   LEU A 305      -4.734 -39.772  17.778  1.00 13.02           C  
ANISOU 2566  C   LEU A 305     1717   1756   1475   -121    -41     61       C  
ATOM   2567  O   LEU A 305      -5.809 -39.345  18.230  1.00 14.69           O  
ANISOU 2567  O   LEU A 305     1918   1992   1670   -114    -39     81       O  
ATOM   2568  CB  LEU A 305      -3.798 -37.424  17.948  1.00 13.54           C  
ANISOU 2568  CB  LEU A 305     1785   1799   1561    -65    -38     92       C  
ATOM   2569  CG  LEU A 305      -2.624 -36.455  17.713  1.00 13.78           C  
ANISOU 2569  CG  LEU A 305     1820   1801   1616    -43    -36     95       C  
ATOM   2570  CD1 LEU A 305      -2.843 -35.123  18.411  1.00 14.01           C  
ANISOU 2570  CD1 LEU A 305     1852   1819   1651    -12    -32    118       C  
ATOM   2571  CD2 LEU A 305      -1.271 -37.086  18.148  1.00 11.71           C  
ANISOU 2571  CD2 LEU A 305     1578   1487   1383    -48    -45     69       C  
ATOM   2572  N   ARG A 306      -4.460 -41.066  17.633  1.00 11.77           N  
ANISOU 2572  N   ARG A 306     1567   1583   1324   -149    -41     34       N  
ATOM   2573  CA  ARG A 306      -5.316 -42.134  18.165  1.00 16.22           C  
ANISOU 2573  CA  ARG A 306     2132   2149   1880   -174    -39     26       C  
ATOM   2574  C   ARG A 306      -4.569 -42.875  19.267  1.00 15.18           C  
ANISOU 2574  C   ARG A 306     2032   1960   1776   -171    -41     16       C  
ATOM   2575  O   ARG A 306      -3.367 -43.138  19.130  1.00 12.13           O  
ANISOU 2575  O   ARG A 306     1660   1539   1409   -168    -43      1       O  
ATOM   2576  CB  ARG A 306      -5.685 -43.156  17.079  1.00 16.18           C  
ANISOU 2576  CB  ARG A 306     2113   2173   1863   -213    -34      1       C  
ATOM   2577  CG  ARG A 306      -5.997 -42.602  15.698  1.00 20.67           C  
ANISOU 2577  CG  ARG A 306     2652   2797   2405   -216    -34      3       C  
ATOM   2578  CD  ARG A 306      -7.187 -41.648  15.685  1.00 14.86           C  
ANISOU 2578  CD  ARG A 306     1891   2113   1643   -202    -34     33       C  
ATOM   2579  NE  ARG A 306      -8.367 -42.186  16.360  1.00 16.74           N  
ANISOU 2579  NE  ARG A 306     2121   2366   1873   -219    -32     36       N  
ATOM   2580  CZ  ARG A 306      -9.517 -41.524  16.470  1.00 23.86           C  
ANISOU 2580  CZ  ARG A 306     3001   3313   2753   -210    -31     62       C  
ATOM   2581  NH1 ARG A 306      -9.652 -40.307  15.949  1.00 19.50           N  
ANISOU 2581  NH1 ARG A 306     2431   2794   2183   -181    -31     87       N  
ATOM   2582  NH2 ARG A 306     -10.539 -42.074  17.105  1.00 23.47           N  
ANISOU 2582  NH2 ARG A 306     2945   3276   2699   -227    -28     65       N  
ATOM   2583  N   TYR A 307      -5.257 -43.228  20.356  1.00 15.70           N  
ANISOU 2583  N   TYR A 307     2107   2017   1841   -171    -38     26       N  
ATOM   2584  CA  TYR A 307      -4.615 -44.043  21.391  1.00 13.78           C  
ANISOU 2584  CA  TYR A 307     1893   1724   1619   -167    -38     19       C  
ATOM   2585  C   TYR A 307      -4.084 -45.320  20.743  1.00 16.10           C  
ANISOU 2585  C   TYR A 307     2193   1998   1926   -196    -31     -9       C  
ATOM   2586  O   TYR A 307      -2.914 -45.666  20.883  1.00 14.00           O  
ANISOU 2586  O   TYR A 307     1946   1694   1681   -188    -34    -21       O  
ATOM   2587  CB  TYR A 307      -5.608 -44.448  22.482  1.00 14.89           C  
ANISOU 2587  CB  TYR A 307     2040   1865   1754   -169    -32     34       C  
ATOM   2588  CG  TYR A 307      -5.969 -43.379  23.492  1.00  9.87           C  
ANISOU 2588  CG  TYR A 307     1407   1232   1109   -135    -37     60       C  
ATOM   2589  CD1 TYR A 307      -4.993 -42.796  24.299  1.00  9.86           C  
ANISOU 2589  CD1 TYR A 307     1427   1198   1121   -102    -47     63       C  
ATOM   2590  CD2 TYR A 307      -7.291 -42.988  23.670  1.00 11.28           C  
ANISOU 2590  CD2 TYR A 307     1570   1450   1268   -135    -31     80       C  
ATOM   2591  CE1 TYR A 307      -5.319 -41.839  25.243  1.00 10.50           C  
ANISOU 2591  CE1 TYR A 307     1514   1283   1194    -71    -52     82       C  
ATOM   2592  CE2 TYR A 307      -7.634 -42.031  24.620  1.00 12.82           C  
ANISOU 2592  CE2 TYR A 307     1770   1647   1454   -103    -34    103       C  
ATOM   2593  CZ  TYR A 307      -6.642 -41.463  25.399  1.00 11.41           C  
ANISOU 2593  CZ  TYR A 307     1614   1433   1287    -71    -44    102       C  
ATOM   2594  OH  TYR A 307      -6.962 -40.519  26.329  1.00 14.50           O  
ANISOU 2594  OH  TYR A 307     2013   1826   1670    -39    -46    121       O  
ATOM   2595  N   ASP A 308      -4.967 -46.017  20.031  1.00 11.03           N  
ANISOU 2595  N   ASP A 308     1534   1385   1271   -231    -22    -21       N  
ATOM   2596  CA  ASP A 308      -4.633 -47.309  19.425  1.00  9.46           C  
ANISOU 2596  CA  ASP A 308     1342   1168   1084   -263    -13    -51       C  
ATOM   2597  C   ASP A 308      -3.653 -47.133  18.271  1.00 10.89           C  
ANISOU 2597  C   ASP A 308     1519   1351   1267   -263    -16    -70       C  
ATOM   2598  O   ASP A 308      -4.006 -46.597  17.222  1.00 14.36           O  
ANISOU 2598  O   ASP A 308     1934   1836   1686   -270    -19    -73       O  
ATOM   2599  CB  ASP A 308      -5.909 -48.009  18.928  1.00 11.30           C  
ANISOU 2599  CB  ASP A 308     1554   1435   1303   -304     -3    -63       C  
ATOM   2600  CG  ASP A 308      -5.679 -49.471  18.592  1.00 19.77           C  
ANISOU 2600  CG  ASP A 308     2640   2479   2394   -339     11    -95       C  
ATOM   2601  OD1 ASP A 308      -4.509 -49.861  18.416  1.00 16.78           O  
ANISOU 2601  OD1 ASP A 308     2280   2063   2033   -331     13   -109       O  
ATOM   2602  OD2 ASP A 308      -6.665 -50.237  18.523  1.00 17.40           O  
ANISOU 2602  OD2 ASP A 308     2329   2193   2091   -373     22   -105       O  
ATOM   2603  N   HIS A 309      -2.412 -47.571  18.477  1.00 13.38           N  
ANISOU 2603  N   HIS A 309     1857   1620   1607   -252    -15    -81       N  
ATOM   2604  CA  HIS A 309      -1.360 -47.394  17.481  1.00 11.12           C  
ANISOU 2604  CA  HIS A 309     1568   1331   1326   -248    -17    -96       C  
ATOM   2605  C   HIS A 309      -1.730 -48.055  16.154  1.00 11.53           C  
ANISOU 2605  C   HIS A 309     1605   1412   1363   -283     -9   -124       C  
ATOM   2606  O   HIS A 309      -1.319 -47.593  15.094  1.00 16.33           O  
ANISOU 2606  O   HIS A 309     2200   2045   1961   -280    -10   -131       O  
ATOM   2607  CB  HIS A 309      -0.036 -47.950  17.998  1.00 10.39           C  
ANISOU 2607  CB  HIS A 309     1501   1184   1263   -232    -16   -104       C  
ATOM   2608  CG  HIS A 309      -0.130 -49.357  18.522  1.00 13.59           C  
ANISOU 2608  CG  HIS A 309     1927   1553   1683   -250     -2   -116       C  
ATOM   2609  ND1 HIS A 309      -0.571 -49.655  19.796  1.00 12.91           N  
ANISOU 2609  ND1 HIS A 309     1855   1447   1604   -242      0    -99       N  
ATOM   2610  CD2 HIS A 309       0.165 -50.547  17.944  1.00 12.13           C  
ANISOU 2610  CD2 HIS A 309     1751   1347   1510   -274     13   -143       C  
ATOM   2611  CE1 HIS A 309      -0.528 -50.961  19.983  1.00 15.80           C  
ANISOU 2611  CE1 HIS A 309     2238   1779   1985   -260     17   -113       C  
ATOM   2612  NE2 HIS A 309      -0.077 -51.526  18.875  1.00 12.85           N  
ANISOU 2612  NE2 HIS A 309     1863   1404   1617   -280     25   -141       N  
ATOM   2613  N   GLN A 310      -2.534 -49.116  16.221  1.00 12.00           N  
ANISOU 2613  N   GLN A 310     1666   1472   1422   -316      2   -140       N  
ATOM   2614  CA  GLN A 310      -2.998 -49.806  15.021  1.00 13.71           C  
ANISOU 2614  CA  GLN A 310     1868   1719   1624   -353      9   -171       C  
ATOM   2615  C   GLN A 310      -4.025 -48.983  14.230  1.00 17.52           C  
ANISOU 2615  C   GLN A 310     2316   2272   2070   -361      0   -164       C  
ATOM   2616  O   GLN A 310      -4.256 -49.246  13.056  1.00 21.80           O  
ANISOU 2616  O   GLN A 310     2840   2851   2592   -384      2   -189       O  
ATOM   2617  CB  GLN A 310      -3.604 -51.169  15.378  1.00 16.55           C  
ANISOU 2617  CB  GLN A 310     2238   2055   1997   -389     24   -192       C  
ATOM   2618  CG  GLN A 310      -2.585 -52.221  15.828  1.00 16.02           C  
ANISOU 2618  CG  GLN A 310     2204   1920   1964   -387     38   -205       C  
ATOM   2619  CD  GLN A 310      -3.238 -53.565  16.137  1.00 22.15           C  
ANISOU 2619  CD  GLN A 310     2990   2670   2755   -424     58   -224       C  
ATOM   2620  OE1 GLN A 310      -4.403 -53.792  15.807  1.00 23.71           O  
ANISOU 2620  OE1 GLN A 310     3168   2903   2939   -458     61   -235       O  
ATOM   2621  NE2 GLN A 310      -2.486 -54.464  16.768  1.00 20.70           N  
ANISOU 2621  NE2 GLN A 310     2837   2425   2603   -417     74   -227       N  
ATOM   2622  N   SER A 311      -4.638 -47.996  14.871  1.00 16.22           N  
ANISOU 2622  N   SER A 311     2141   2129   1895   -339     -8   -131       N  
ATOM   2623  CA  SER A 311      -5.673 -47.184  14.217  1.00 17.81           C  
ANISOU 2623  CA  SER A 311     2308   2398   2062   -341    -15   -118       C  
ATOM   2624  C   SER A 311      -5.134 -45.910  13.556  1.00 15.40           C  
ANISOU 2624  C   SER A 311     1991   2118   1743   -308    -22   -100       C  
ATOM   2625  O   SER A 311      -5.857 -45.220  12.819  1.00 16.17           O  
ANISOU 2625  O   SER A 311     2060   2275   1809   -306    -25    -88       O  
ATOM   2626  CB  SER A 311      -6.769 -46.814  15.222  1.00 19.97           C  
ANISOU 2626  CB  SER A 311     2574   2685   2330   -335    -17    -91       C  
ATOM   2627  OG  SER A 311      -7.411 -47.976  15.708  1.00 20.18           O  
ANISOU 2627  OG  SER A 311     2604   2695   2367   -369     -7   -106       O  
ATOM   2628  N   ARG A 312      -3.875 -45.584  13.820  1.00 11.53           N  
ANISOU 2628  N   ARG A 312     1521   1583   1275   -282    -22    -94       N  
ATOM   2629  CA  ARG A 312      -3.304 -44.364  13.260  1.00 17.36           C  
ANISOU 2629  CA  ARG A 312     2250   2338   2007   -252    -25    -75       C  
ATOM   2630  C   ARG A 312      -3.084 -44.494  11.766  1.00 12.80           C  
ANISOU 2630  C   ARG A 312     1657   1798   1410   -263    -21    -94       C  
ATOM   2631  O   ARG A 312      -2.858 -45.599  11.272  1.00 15.63           O  
ANISOU 2631  O   ARG A 312     2022   2148   1770   -290    -16   -128       O  
ATOM   2632  CB  ARG A 312      -1.983 -44.033  13.953  1.00 12.82           C  
ANISOU 2632  CB  ARG A 312     1700   1705   1466   -225    -27    -68       C  
ATOM   2633  CG  ARG A 312      -2.184 -43.790  15.439  1.00 12.41           C  
ANISOU 2633  CG  ARG A 312     1664   1622   1430   -209    -32    -49       C  
ATOM   2634  CD  ARG A 312      -0.857 -43.645  16.168  1.00 13.88           C  
ANISOU 2634  CD  ARG A 312     1873   1754   1649   -186    -36    -49       C  
ATOM   2635  NE  ARG A 312      -1.078 -43.857  17.599  1.00 12.13           N  
ANISOU 2635  NE  ARG A 312     1669   1501   1438   -177    -41    -40       N  
ATOM   2636  CZ  ARG A 312      -0.173 -44.318  18.446  1.00 11.88           C  
ANISOU 2636  CZ  ARG A 312     1660   1422   1431   -166    -44    -46       C  
ATOM   2637  NH1 ARG A 312       1.061 -44.602  18.028  1.00  9.98           N  
ANISOU 2637  NH1 ARG A 312     1427   1155   1210   -163    -43    -61       N  
ATOM   2638  NH2 ARG A 312      -0.504 -44.481  19.718  1.00 11.43           N  
ANISOU 2638  NH2 ARG A 312     1618   1346   1378   -156    -47    -35       N  
ATOM   2639  N   LEU A 313      -3.175 -43.369  11.050  1.00 14.10           N  
ANISOU 2639  N   LEU A 313     1800   2003   1553   -241    -22    -71       N  
ATOM   2640  CA  LEU A 313      -2.753 -43.316   9.651  1.00 13.97           C  
ANISOU 2640  CA  LEU A 313     1771   2020   1518   -242    -16    -83       C  
ATOM   2641  C   LEU A 313      -1.297 -43.773   9.547  1.00 14.85           C  
ANISOU 2641  C   LEU A 313     1905   2078   1659   -238    -11   -101       C  
ATOM   2642  O   LEU A 313      -0.465 -43.434  10.398  1.00 14.51           O  
ANISOU 2642  O   LEU A 313     1880   1984   1648   -218    -12    -89       O  
ATOM   2643  CB  LEU A 313      -2.831 -41.886   9.106  1.00 13.10           C  
ANISOU 2643  CB  LEU A 313     1641   1947   1390   -208    -14    -46       C  
ATOM   2644  CG  LEU A 313      -4.215 -41.294   8.842  1.00 17.71           C  
ANISOU 2644  CG  LEU A 313     2195   2597   1936   -205    -17    -24       C  
ATOM   2645  CD1 LEU A 313      -4.074 -39.872   8.380  1.00 17.18           C  
ANISOU 2645  CD1 LEU A 313     2115   2554   1860   -166    -10     15       C  
ATOM   2646  CD2 LEU A 313      -4.961 -42.117   7.817  1.00 18.11           C  
ANISOU 2646  CD2 LEU A 313     2224   2707   1950   -236    -20    -53       C  
ATOM   2647  N   THR A 314      -0.998 -44.537   8.503  1.00 12.49           N  
ANISOU 2647  N   THR A 314     1604   1794   1347   -257     -5   -132       N  
ATOM   2648  CA  THR A 314       0.385 -44.839   8.167  1.00 15.26           C  
ANISOU 2648  CA  THR A 314     1972   2106   1721   -249      3   -146       C  
ATOM   2649  C   THR A 314       0.949 -43.624   7.446  1.00 16.88           C  
ANISOU 2649  C   THR A 314     2163   2332   1919   -217      9   -119       C  
ATOM   2650  O   THR A 314       0.201 -42.717   7.059  1.00 11.64           O  
ANISOU 2650  O   THR A 314     1478   1718   1229   -204      8    -94       O  
ATOM   2651  CB  THR A 314       0.529 -46.097   7.268  1.00 16.89           C  
ANISOU 2651  CB  THR A 314     2182   2319   1915   -279     11   -191       C  
ATOM   2652  OG1 THR A 314      -0.054 -45.862   5.979  1.00 15.50           O  
ANISOU 2652  OG1 THR A 314     1980   2213   1695   -285     12   -197       O  
ATOM   2653  CG2 THR A 314      -0.121 -47.312   7.914  1.00 12.26           C  
ANISOU 2653  CG2 THR A 314     1608   1713   1338   -314      9   -218       C  
ATOM   2654  N   ALA A 315       2.263 -43.597   7.262  1.00 14.41           N  
ANISOU 2654  N   ALA A 315     1862   1982   1632   -203     17   -122       N  
ATOM   2655  CA  ALA A 315       2.883 -42.479   6.577  1.00 11.71           C  
ANISOU 2655  CA  ALA A 315     1507   1654   1288   -174     26    -96       C  
ATOM   2656  C   ALA A 315       2.349 -42.389   5.148  1.00 13.77           C  
ANISOU 2656  C   ALA A 315     1746   1985   1503   -176     33    -99       C  
ATOM   2657  O   ALA A 315       2.072 -41.307   4.662  1.00 14.51           O  
ANISOU 2657  O   ALA A 315     1820   2115   1578   -154     38    -67       O  
ATOM   2658  CB  ALA A 315       4.406 -42.618   6.578  1.00 10.32           C  
ANISOU 2658  CB  ALA A 315     1345   1428   1148   -162     34   -103       C  
ATOM   2659  N   ARG A 316       2.217 -43.531   4.478  1.00 14.39           N  
ANISOU 2659  N   ARG A 316     1826   2080   1561   -203     34   -138       N  
ATOM   2660  CA  ARG A 316       1.766 -43.531   3.102  1.00 18.76           C  
ANISOU 2660  CA  ARG A 316     2358   2702   2067   -207     39   -146       C  
ATOM   2661  C   ARG A 316       0.317 -43.045   3.017  1.00 17.86           C  
ANISOU 2661  C   ARG A 316     2220   2652   1915   -210     29   -129       C  
ATOM   2662  O   ARG A 316       0.001 -42.189   2.195  1.00 16.65           O  
ANISOU 2662  O   ARG A 316     2043   2553   1728   -188     33   -104       O  
ATOM   2663  CB  ARG A 316       1.921 -44.913   2.482  1.00 25.06           C  
ANISOU 2663  CB  ARG A 316     3167   3502   2854   -238     42   -197       C  
ATOM   2664  CG  ARG A 316       1.825 -44.912   0.976  1.00 32.68           C  
ANISOU 2664  CG  ARG A 316     4112   4532   3771   -236     49   -210       C  
ATOM   2665  CD  ARG A 316       3.045 -44.242   0.368  1.00 33.59           C  
ANISOU 2665  CD  ARG A 316     4229   4636   3897   -202     66   -188       C  
ATOM   2666  NE  ARG A 316       2.842 -43.924  -1.040  1.00 37.24           N  
ANISOU 2666  NE  ARG A 316     4671   5171   4309   -190     74   -186       N  
ATOM   2667  CZ  ARG A 316       3.233 -44.702  -2.043  1.00 39.95           C  
ANISOU 2667  CZ  ARG A 316     5017   5533   4629   -200     83   -222       C  
ATOM   2668  NH1 ARG A 316       3.857 -45.844  -1.792  1.00 36.37           N  
ANISOU 2668  NH1 ARG A 316     4588   5028   4202   -222     86   -263       N  
ATOM   2669  NH2 ARG A 316       3.009 -44.330  -3.295  1.00 46.64           N  
ANISOU 2669  NH2 ARG A 316     5843   6452   5426   -185     89   -217       N  
ATOM   2670  N   GLU A 317      -0.552 -43.563   3.883  1.00 20.72           N  
ANISOU 2670  N   GLU A 317     2586   3006   2282   -234     16   -140       N  
ATOM   2671  CA  GLU A 317      -1.939 -43.089   3.938  1.00 19.64           C  
ANISOU 2671  CA  GLU A 317     2423   2926   2113   -236      7   -122       C  
ATOM   2672  C   GLU A 317      -2.000 -41.611   4.239  1.00 15.69           C  
ANISOU 2672  C   GLU A 317     1914   2432   1617   -196     10    -69       C  
ATOM   2673  O   GLU A 317      -2.847 -40.895   3.708  1.00 19.26           O  
ANISOU 2673  O   GLU A 317     2339   2946   2032   -182     10    -44       O  
ATOM   2674  CB  GLU A 317      -2.733 -43.789   5.037  1.00 19.38           C  
ANISOU 2674  CB  GLU A 317     2398   2870   2094   -264     -4   -136       C  
ATOM   2675  CG  GLU A 317      -2.967 -45.256   4.850  1.00 18.62           C  
ANISOU 2675  CG  GLU A 317     2310   2770   1996   -308     -5   -187       C  
ATOM   2676  CD  GLU A 317      -3.789 -45.824   5.983  1.00 24.97           C  
ANISOU 2676  CD  GLU A 317     3119   3551   2817   -333    -12   -193       C  
ATOM   2677  OE1 GLU A 317      -3.367 -45.717   7.160  1.00 16.99           O  
ANISOU 2677  OE1 GLU A 317     2131   2480   1844   -321    -11   -176       O  
ATOM   2678  OE2 GLU A 317      -4.874 -46.364   5.698  1.00 21.41           O  
ANISOU 2678  OE2 GLU A 317     2649   3145   2341   -364    -18   -214       O  
ATOM   2679  N   ALA A 318      -1.136 -41.153   5.142  1.00 13.91           N  
ANISOU 2679  N   ALA A 318     1709   2140   1436   -178     14    -52       N  
ATOM   2680  CA  ALA A 318      -1.126 -39.745   5.506  1.00 12.13           C  
ANISOU 2680  CA  ALA A 318     1478   1911   1221   -141     19     -5       C  
ATOM   2681  C   ALA A 318      -0.857 -38.898   4.258  1.00 16.66           C  
ANISOU 2681  C   ALA A 318     2032   2528   1770   -114     34     20       C  
ATOM   2682  O   ALA A 318      -1.473 -37.841   4.053  1.00 18.18           O  
ANISOU 2682  O   ALA A 318     2206   2758   1944    -89     39     58       O  
ATOM   2683  CB  ALA A 318      -0.082 -39.474   6.606  1.00 13.18           C  
ANISOU 2683  CB  ALA A 318     1636   1965   1407   -129     20      2       C  
ATOM   2684  N   MET A 319       0.042 -39.376   3.402  1.00 13.28           N  
ANISOU 2684  N   MET A 319     1609   2097   1340   -118     42     -1       N  
ATOM   2685  CA  MET A 319       0.398 -38.630   2.205  1.00 15.25           C  
ANISOU 2685  CA  MET A 319     1842   2386   1568    -90     59     23       C  
ATOM   2686  C   MET A 319      -0.755 -38.553   1.207  1.00 16.72           C  
ANISOU 2686  C   MET A 319     1998   2662   1692    -89     57     28       C  
ATOM   2687  O   MET A 319      -0.764 -37.683   0.340  1.00 17.25           O  
ANISOU 2687  O   MET A 319     2048   2772   1735    -59     71     62       O  
ATOM   2688  CB  MET A 319       1.658 -39.205   1.554  1.00 16.77           C  
ANISOU 2688  CB  MET A 319     2046   2553   1773    -94     70     -1       C  
ATOM   2689  CG  MET A 319       2.863 -39.060   2.459  1.00 19.83           C  
ANISOU 2689  CG  MET A 319     2457   2859   2220    -87     74      1       C  
ATOM   2690  SD  MET A 319       4.299 -39.836   1.733  1.00 21.15           S  
ANISOU 2690  SD  MET A 319     2636   2997   2402    -92     87    -28       S  
ATOM   2691  CE  MET A 319       4.618 -38.655   0.434  1.00 20.13           C  
ANISOU 2691  CE  MET A 319     2485   2914   2251    -54    112     13       C  
ATOM   2692  N   GLU A 320      -1.739 -39.434   1.360  1.00 18.27           N  
ANISOU 2692  N   GLU A 320     2188   2888   1865   -122     39     -2       N  
ATOM   2693  CA  GLU A 320      -2.947 -39.395   0.526  1.00 21.93           C  
ANISOU 2693  CA  GLU A 320     2621   3443   2270   -124     32      0       C  
ATOM   2694  C   GLU A 320      -4.002 -38.417   1.050  1.00 20.65           C  
ANISOU 2694  C   GLU A 320     2439   3308   2097   -104     29     44       C  
ATOM   2695  O   GLU A 320      -5.022 -38.195   0.394  1.00 22.25           O  
ANISOU 2695  O   GLU A 320     2613   3591   2252    -98     24     55       O  
ATOM   2696  CB  GLU A 320      -3.581 -40.791   0.410  1.00 19.95           C  
ANISOU 2696  CB  GLU A 320     2367   3214   1999   -172     16    -55       C  
ATOM   2697  CG  GLU A 320      -2.645 -41.900  -0.076  1.00 21.28           C  
ANISOU 2697  CG  GLU A 320     2555   3354   2176   -196     20   -104       C  
ATOM   2698  CD  GLU A 320      -2.428 -41.879  -1.574  1.00 25.98           C  
ANISOU 2698  CD  GLU A 320     3135   4013   2725   -184     28   -112       C  
ATOM   2699  OE1 GLU A 320      -3.383 -42.179  -2.317  1.00 26.11           O  
ANISOU 2699  OE1 GLU A 320     3125   4106   2690   -198     17   -130       O  
ATOM   2700  OE2 GLU A 320      -1.300 -41.574  -2.018  1.00 25.28           O  
ANISOU 2700  OE2 GLU A 320     3057   3898   2650   -161     45   -101       O  
ATOM   2701  N   HIS A 321      -3.790 -37.843   2.231  1.00 16.18           N  
ANISOU 2701  N   HIS A 321     1891   2681   1576    -91     31     67       N  
ATOM   2702  CA  HIS A 321      -4.855 -37.050   2.866  1.00 16.84           C  
ANISOU 2702  CA  HIS A 321     1960   2786   1652    -75     28    103       C  
ATOM   2703  C   HIS A 321      -5.165 -35.716   2.170  1.00 15.40           C  
ANISOU 2703  C   HIS A 321     1755   2652   1444    -30     44    156       C  
ATOM   2704  O   HIS A 321      -4.260 -35.033   1.703  1.00 17.60           O  
ANISOU 2704  O   HIS A 321     2040   2912   1736     -2     63    179       O  
ATOM   2705  CB  HIS A 321      -4.550 -36.815   4.355  1.00 20.12           C  
ANISOU 2705  CB  HIS A 321     2402   3122   2120    -74     27    110       C  
ATOM   2706  CG  HIS A 321      -5.740 -36.367   5.147  1.00 22.62           C  
ANISOU 2706  CG  HIS A 321     2707   3457   2429    -68     20    134       C  
ATOM   2707  ND1 HIS A 321      -6.159 -35.056   5.184  1.00 20.36           N  
ANISOU 2707  ND1 HIS A 321     2408   3190   2136    -29     33    183       N  
ATOM   2708  CD2 HIS A 321      -6.608 -37.059   5.924  1.00 15.63           C  
ANISOU 2708  CD2 HIS A 321     1822   2575   1542    -95      6    116       C  
ATOM   2709  CE1 HIS A 321      -7.231 -34.957   5.951  1.00 17.67           C  
ANISOU 2709  CE1 HIS A 321     2060   2864   1789    -31     25    194       C  
ATOM   2710  NE2 HIS A 321      -7.526 -36.159   6.410  1.00 16.05           N  
ANISOU 2710  NE2 HIS A 321     1861   2651   1587    -72      8    154       N  
ATOM   2711  N   PRO A 322      -6.464 -35.339   2.099  1.00 15.12           N  
ANISOU 2711  N   PRO A 322     1692   2681   1372    -21     39    179       N  
ATOM   2712  CA  PRO A 322      -6.861 -34.059   1.493  1.00 17.97           C  
ANISOU 2712  CA  PRO A 322     2030   3091   1707     26     56    234       C  
ATOM   2713  C   PRO A 322      -6.088 -32.819   1.991  1.00 16.23           C  
ANISOU 2713  C   PRO A 322     1828   2806   1531     65     79    277       C  
ATOM   2714  O   PRO A 322      -5.974 -31.831   1.255  1.00 16.40           O  
ANISOU 2714  O   PRO A 322     1838   2855   1540    104    101    320       O  
ATOM   2715  CB  PRO A 322      -8.358 -33.961   1.843  1.00 17.98           C  
ANISOU 2715  CB  PRO A 322     2006   3148   1679     25     44    248       C  
ATOM   2716  CG  PRO A 322      -8.810 -35.382   1.890  1.00 19.75           C  
ANISOU 2716  CG  PRO A 322     2225   3391   1887    -27     20    192       C  
ATOM   2717  CD  PRO A 322      -7.634 -36.159   2.471  1.00 19.58           C  
ANISOU 2717  CD  PRO A 322     2242   3282   1915    -55     18    153       C  
ATOM   2718  N   TYR A 323      -5.571 -32.863   3.215  1.00 16.49           N  
ANISOU 2718  N   TYR A 323     1891   2758   1617     53     76    266       N  
ATOM   2719  CA  TYR A 323      -4.765 -31.771   3.760  1.00 19.60           C  
ANISOU 2719  CA  TYR A 323     2303   3086   2058     83     96    297       C  
ATOM   2720  C   TYR A 323      -3.636 -31.382   2.793  1.00 14.72           C  
ANISOU 2720  C   TYR A 323     1687   2458   1449    101    117    308       C  
ATOM   2721  O   TYR A 323      -3.253 -30.216   2.691  1.00 20.48           O  
ANISOU 2721  O   TYR A 323     2418   3167   2198    136    142    349       O  
ATOM   2722  CB  TYR A 323      -4.192 -32.201   5.125  1.00 20.93           C  
ANISOU 2722  CB  TYR A 323     2503   3172   2277     59     84    267       C  
ATOM   2723  CG  TYR A 323      -3.380 -31.170   5.892  1.00 15.71           C  
ANISOU 2723  CG  TYR A 323     1862   2438   1668     83     99    289       C  
ATOM   2724  CD1 TYR A 323      -3.919 -29.938   6.247  1.00 17.09           C  
ANISOU 2724  CD1 TYR A 323     2033   2613   1849    117    115    332       C  
ATOM   2725  CD2 TYR A 323      -2.086 -31.461   6.319  1.00 13.12           C  
ANISOU 2725  CD2 TYR A 323     1558   2042   1386     70     98    264       C  
ATOM   2726  CE1 TYR A 323      -3.190 -29.012   6.976  1.00 11.61           C  
ANISOU 2726  CE1 TYR A 323     1357   1849   1204    134    129    346       C  
ATOM   2727  CE2 TYR A 323      -1.345 -30.546   7.037  1.00 14.16           C  
ANISOU 2727  CE2 TYR A 323     1706   2110   1566     87    109    278       C  
ATOM   2728  CZ  TYR A 323      -1.894 -29.330   7.362  1.00 14.72           C  
ANISOU 2728  CZ  TYR A 323     1772   2179   1642    118    125    317       C  
ATOM   2729  OH  TYR A 323      -1.155 -28.436   8.087  1.00 20.27           O  
ANISOU 2729  OH  TYR A 323     2491   2815   2394    132    137    326       O  
ATOM   2730  N   PHE A 324      -3.130 -32.357   2.053  1.00 16.82           N  
ANISOU 2730  N   PHE A 324     1952   2739   1698     78    110    273       N  
ATOM   2731  CA  PHE A 324      -1.978 -32.112   1.191  1.00 15.81           C  
ANISOU 2731  CA  PHE A 324     1829   2599   1581     93    130    280       C  
ATOM   2732  C   PHE A 324      -2.346 -31.802  -0.260  1.00 18.98           C  
ANISOU 2732  C   PHE A 324     2203   3083   1927    118    144    305       C  
ATOM   2733  O   PHE A 324      -1.474 -31.587  -1.091  1.00 16.21           O  
ANISOU 2733  O   PHE A 324     1852   2730   1578    134    164    315       O  
ATOM   2734  CB  PHE A 324      -1.002 -33.283   1.274  1.00 16.75           C  
ANISOU 2734  CB  PHE A 324     1968   2676   1722     58    119    228       C  
ATOM   2735  CG  PHE A 324      -0.463 -33.499   2.651  1.00 20.78           C  
ANISOU 2735  CG  PHE A 324     2504   3104   2287     41    108    208       C  
ATOM   2736  CD1 PHE A 324       0.399 -32.571   3.222  1.00 16.26           C  
ANISOU 2736  CD1 PHE A 324     1945   2468   1765     61    123    231       C  
ATOM   2737  CD2 PHE A 324      -0.835 -34.611   3.389  1.00 17.22           C  
ANISOU 2737  CD2 PHE A 324     2065   2641   1838      5     84    168       C  
ATOM   2738  CE1 PHE A 324       0.892 -32.759   4.513  1.00 16.20           C  
ANISOU 2738  CE1 PHE A 324     1961   2390   1805     46    111    211       C  
ATOM   2739  CE2 PHE A 324      -0.345 -34.809   4.679  1.00 18.85           C  
ANISOU 2739  CE2 PHE A 324     2295   2775   2091     -8     74    152       C  
ATOM   2740  CZ  PHE A 324       0.518 -33.880   5.239  1.00 14.78           C  
ANISOU 2740  CZ  PHE A 324     1792   2201   1621     14     86    173       C  
ATOM   2741  N   TYR A 325      -3.640 -31.739  -0.563  1.00 17.95           N  
ANISOU 2741  N   TYR A 325     2046   3027   1746    125    136    319       N  
ATOM   2742  CA  TYR A 325      -4.043 -31.424  -1.931  1.00 15.72           C  
ANISOU 2742  CA  TYR A 325     1735   2831   1405    153    147    345       C  
ATOM   2743  C   TYR A 325      -3.513 -30.063  -2.388  1.00 12.87           C  
ANISOU 2743  C   TYR A 325     1373   2459   1059    203    184    405       C  
ATOM   2744  O   TYR A 325      -3.205 -29.881  -3.565  1.00 16.53           O  
ANISOU 2744  O   TYR A 325     1823   2967   1490    226    201    422       O  
ATOM   2745  CB  TYR A 325      -5.573 -31.458  -2.087  1.00 14.31           C  
ANISOU 2745  CB  TYR A 325     1526   2738   1173    155    131    354       C  
ATOM   2746  CG  TYR A 325      -6.212 -32.828  -2.011  1.00 20.03           C  
ANISOU 2746  CG  TYR A 325     2244   3497   1871    106     98    296       C  
ATOM   2747  CD1 TYR A 325      -5.448 -33.994  -2.001  1.00 19.25           C  
ANISOU 2747  CD1 TYR A 325     2165   3360   1788     65     86    239       C  
ATOM   2748  CD2 TYR A 325      -7.596 -32.953  -1.962  1.00 22.59           C  
ANISOU 2748  CD2 TYR A 325     2540   3890   2154    100     81    298       C  
ATOM   2749  CE1 TYR A 325      -6.046 -35.240  -1.933  1.00 20.90           C  
ANISOU 2749  CE1 TYR A 325     2369   3596   1976     19     60    186       C  
ATOM   2750  CE2 TYR A 325      -8.199 -34.184  -1.891  1.00 27.87           C  
ANISOU 2750  CE2 TYR A 325     3201   4588   2802     52     53    245       C  
ATOM   2751  CZ  TYR A 325      -7.429 -35.321  -1.881  1.00 26.19           C  
ANISOU 2751  CZ  TYR A 325     3010   4334   2608     12     44    188       C  
ATOM   2752  OH  TYR A 325      -8.061 -36.536  -1.807  1.00 27.33           O  
ANISOU 2752  OH  TYR A 325     3146   4503   2734    -37     19    135       O  
ATOM   2753  N   THR A 326      -3.391 -29.112  -1.460  1.00 15.82           N  
ANISOU 2753  N   THR A 326     1759   2771   1481    221    198    436       N  
ATOM   2754  CA  THR A 326      -2.988 -27.758  -1.836  1.00 16.96           C  
ANISOU 2754  CA  THR A 326     1901   2899   1642    269    237    495       C  
ATOM   2755  C   THR A 326      -1.467 -27.636  -2.033  1.00 18.62           C  
ANISOU 2755  C   THR A 326     2131   3045   1900    268    257    490       C  
ATOM   2756  O   THR A 326      -0.991 -26.698  -2.669  1.00 21.52           O  
ANISOU 2756  O   THR A 326     2492   3408   2275    305    292    536       O  
ATOM   2757  CB  THR A 326      -3.486 -26.697  -0.831  1.00 29.18           C  
ANISOU 2757  CB  THR A 326     3456   4409   3224    290    248    532       C  
ATOM   2758  OG1 THR A 326      -3.153 -25.386  -1.308  1.00 35.24           O  
ANISOU 2758  OG1 THR A 326     4219   5164   4006    338    289    591       O  
ATOM   2759  CG2 THR A 326      -2.859 -26.906   0.515  1.00 29.96           C  
ANISOU 2759  CG2 THR A 326     3584   4414   3386    261    236    498       C  
ATOM   2760  N   VAL A 327      -0.729 -28.608  -1.516  1.00 15.81           N  
ANISOU 2760  N   VAL A 327     1794   2639   1573    228    237    437       N  
ATOM   2761  CA  VAL A 327       0.736 -28.637  -1.653  1.00 15.17           C  
ANISOU 2761  CA  VAL A 327     1730   2498   1538    223    252    426       C  
ATOM   2762  C   VAL A 327       1.175 -28.987  -3.077  1.00 17.69           C  
ANISOU 2762  C   VAL A 327     2035   2869   1817    233    266    427       C  
ATOM   2763  O   VAL A 327       0.740 -29.990  -3.643  1.00 20.21           O  
ANISOU 2763  O   VAL A 327     2346   3246   2086    214    245    394       O  
ATOM   2764  CB  VAL A 327       1.344 -29.628  -0.666  1.00 17.41           C  
ANISOU 2764  CB  VAL A 327     2036   2718   1860    179    226    370       C  
ATOM   2765  CG1 VAL A 327       2.856 -29.734  -0.874  1.00 19.37           C  
ANISOU 2765  CG1 VAL A 327     2296   2912   2151    175    241    358       C  
ATOM   2766  CG2 VAL A 327       1.035 -29.193   0.754  1.00 19.91           C  
ANISOU 2766  CG2 VAL A 327     2366   2980   2217    174    216    372       C  
ATOM   2767  N   VAL A 328       2.033 -28.154  -3.662  1.00 15.51           N  
ANISOU 2767  N   VAL A 328     1758   2572   1563    263    302    465       N  
ATOM   2768  CA  VAL A 328       2.514 -28.395  -5.019  1.00 20.21           C  
ANISOU 2768  CA  VAL A 328     2342   3216   2122    278    319    471       C  
ATOM   2769  C   VAL A 328       3.404 -29.626  -5.074  1.00 24.03           C  
ANISOU 2769  C   VAL A 328     2840   3675   2617    242    303    413       C  
ATOM   2770  O   VAL A 328       4.365 -29.737  -4.311  1.00 19.02           O  
ANISOU 2770  O   VAL A 328     2223   2961   2042    223    302    393       O  
ATOM   2771  CB  VAL A 328       3.305 -27.190  -5.582  1.00 25.81           C  
ANISOU 2771  CB  VAL A 328     3047   3900   2860    319    367    528       C  
ATOM   2772  CG1 VAL A 328       4.060 -27.595  -6.842  1.00 29.17           C  
ANISOU 2772  CG1 VAL A 328     3465   4360   3257    329    384    526       C  
ATOM   2773  CG2 VAL A 328       2.381 -26.013  -5.863  1.00 23.63           C  
ANISOU 2773  CG2 VAL A 328     2754   3665   2560    364    390    591       C  
ATOM   2774  N   LYS A 329       3.092 -30.536  -5.991  1.00 24.47           N  
ANISOU 2774  N   LYS A 329     2886   3800   2612    233    290    385       N  
ATOM   2775  CA  LYS A 329       3.924 -31.719  -6.204  1.00 36.96           C  
ANISOU 2775  CA  LYS A 329     4481   5363   4199    202    279    332       C  
ATOM   2776  C   LYS A 329       4.956 -31.494  -7.318  1.00 37.65           C  
ANISOU 2776  C   LYS A 329     4564   5459   4282    228    313    351       C  
ATOM   2777  O   LYS A 329       6.148 -31.770  -7.146  1.00 41.50           O  
ANISOU 2777  O   LYS A 329     5066   5887   4816    217    322    333       O  
ATOM   2778  CB  LYS A 329       3.054 -32.936  -6.528  1.00 43.00           C  
ANISOU 2778  CB  LYS A 329     5240   6192   4905    173    248    282       C  
ATOM   2779  CG  LYS A 329       1.943 -33.186  -5.519  1.00 44.23           C  
ANISOU 2779  CG  LYS A 329     5397   6349   5060    148    217    265       C  
ATOM   2780  CD  LYS A 329       2.471 -33.174  -4.088  1.00 41.48           C  
ANISOU 2780  CD  LYS A 329     5072   5904   4783    128    208    253       C  
ATOM   2781  CE  LYS A 329       1.384 -33.590  -3.102  1.00 39.67           C  
ANISOU 2781  CE  LYS A 329     4845   5678   4551    101    178    232       C  
ATOM   2782  NZ  LYS A 329       0.137 -32.776  -3.236  1.00 36.68           N  
ANISOU 2782  NZ  LYS A 329     4443   5359   4134    126    179    273       N  
TER    2783      LYS A 329                                                      
HETATM 2784  N1  FU9 A 338      23.421 -29.478  10.420  1.00 19.97           N  
HETATM 2785  C2  FU9 A 338      23.434 -28.488  11.339  1.00 19.82           C  
HETATM 2786  N3  FU9 A 338      23.310 -28.750  12.649  1.00 16.65           N  
HETATM 2787  C4  FU9 A 338      23.185 -30.006  13.072  1.00 14.99           C  
HETATM 2788  C5  FU9 A 338      23.147 -31.045  12.151  1.00 13.79           C  
HETATM 2789  C6  FU9 A 338      23.287 -30.744  10.797  1.00 17.01           C  
HETATM 2790  OAA FU9 A 338      22.464 -36.547  15.342  1.00 13.61           O  
HETATM 2791  OAB FU9 A 338      22.086 -37.214  13.268  1.00 16.32           O  
HETATM 2792  FAC FU9 A 338      24.116 -31.123  20.289  1.00 37.04           F  
HETATM 2793  FAD FU9 A 338      22.009 -30.950  20.696  1.00 39.25           F  
HETATM 2794  FAE FU9 A 338      22.714 -32.258  19.128  1.00 40.80           F  
HETATM 2795  CAF FU9 A 338      22.594 -27.556  18.409  1.00 18.66           C  
HETATM 2796  CAG FU9 A 338      22.777 -27.761  17.049  1.00 19.72           C  
HETATM 2797  CAH FU9 A 338      22.658 -28.643  19.269  1.00 16.31           C  
HETATM 2798  CAI FU9 A 338      22.800 -34.725  12.202  1.00 10.51           C  
HETATM 2799  CAJ FU9 A 338      22.968 -33.433  11.721  1.00 13.22           C  
HETATM 2800  CAL FU9 A 338      22.973 -30.130  17.400  1.00 17.88           C  
HETATM 2801  CAM FU9 A 338      22.708 -33.870  14.448  1.00 13.89           C  
HETATM 2802  CAN FU9 A 338      23.500 -24.762  11.531  1.00 23.65           C  
HETATM 2803  CAO FU9 A 338      24.834 -25.307  12.063  1.00 31.24           C  
HETATM 2804  NAQ FU9 A 338      22.885 -31.520  14.849  1.00 14.98           N  
HETATM 2805  NAS FU9 A 338      22.985 -29.154  15.196  1.00 14.12           N  
HETATM 2806  NAT FU9 A 338      23.580 -27.216  10.980  1.00 21.94           N  
HETATM 2807  CAU FU9 A 338      22.486 -36.365  14.101  1.00 15.99           C  
HETATM 2808  CAV FU9 A 338      22.877 -29.044  16.527  1.00 14.02           C  
HETATM 2809  CAW FU9 A 338      22.708 -34.950  13.574  1.00 15.52           C  
HETATM 2810  CAX FU9 A 338      22.843 -29.925  18.771  1.00 18.91           C  
HETATM 2811  CAZ FU9 A 338      23.093 -30.247  14.432  1.00 14.63           C  
HETATM 2812  CBA FU9 A 338      22.874 -32.568  13.978  1.00 14.78           C  
HETATM 2813  CBB FU9 A 338      22.996 -32.352  12.609  1.00 12.09           C  
HETATM 2814  CBE FU9 A 338      23.598 -26.197  12.040  1.00 24.43           C  
HETATM 2815  CBF FU9 A 338      22.914 -31.103  19.747  1.00 33.36           C  
HETATM 2816  S   SO4 A 339      16.994 -48.427  23.467  1.00 56.37           S  
HETATM 2817  O1  SO4 A 339      18.081 -47.592  22.948  1.00 54.07           O  
HETATM 2818  O2  SO4 A 339      16.573 -49.386  22.452  1.00 44.10           O  
HETATM 2819  O3  SO4 A 339      17.449 -49.155  24.652  1.00 62.33           O  
HETATM 2820  O4  SO4 A 339      15.862 -47.573  23.827  1.00 55.64           O  
HETATM 2821  S   SO4 A 340      12.335 -41.463  29.821  1.00 55.41           S  
HETATM 2822  O1  SO4 A 340      12.524 -41.505  28.365  1.00 49.11           O  
HETATM 2823  O2  SO4 A 340      11.605 -42.648  30.264  1.00 51.42           O  
HETATM 2824  O3  SO4 A 340      13.642 -41.420  30.480  1.00 56.91           O  
HETATM 2825  O4  SO4 A 340      11.578 -40.268  30.194  1.00 53.41           O  
HETATM 2826  S   SO4 A 341      -8.673 -44.194  19.555  1.00 20.92           S  
HETATM 2827  O1  SO4 A 341      -8.890 -44.407  18.118  1.00 26.24           O  
HETATM 2828  O2  SO4 A 341      -9.987 -44.244  20.203  1.00 24.61           O  
HETATM 2829  O3  SO4 A 341      -7.781 -45.264  20.045  1.00 17.72           O  
HETATM 2830  O4  SO4 A 341      -8.117 -42.851  19.768  1.00 12.17           O  
HETATM 2831  S   SO4 A 342      16.660 -32.532  -1.544  1.00 60.53           S  
HETATM 2832  O1  SO4 A 342      18.092 -32.240  -1.608  1.00 60.37           O  
HETATM 2833  O2  SO4 A 342      16.008 -31.860  -2.665  1.00 66.82           O  
HETATM 2834  O3  SO4 A 342      16.445 -33.972  -1.635  1.00 60.76           O  
HETATM 2835  O4  SO4 A 342      16.083 -32.057  -0.290  1.00 56.69           O  
HETATM 2836  C1  PEG A 343      11.944 -32.966  28.991  1.00 56.31           C  
HETATM 2837  O1  PEG A 343      11.298 -31.707  29.225  1.00 56.67           O  
HETATM 2838  C2  PEG A 343      11.484 -33.531  27.650  1.00 53.96           C  
HETATM 2839  O2  PEG A 343      12.178 -34.752  27.413  1.00 55.88           O  
HETATM 2840  C3  PEG A 343      11.570 -35.803  28.154  1.00 52.84           C  
HETATM 2841  C4  PEG A 343      12.333 -37.112  28.003  1.00 49.96           C  
HETATM 2842  O4  PEG A 343      11.995 -37.950  29.120  1.00 53.07           O  
HETATM 2843  C1  EDO A 344      36.720 -34.839  14.137  1.00 36.42           C  
HETATM 2844  O1  EDO A 344      37.874 -34.042  13.843  1.00 41.78           O  
HETATM 2845  C2  EDO A 344      37.172 -36.201  14.636  1.00 35.03           C  
HETATM 2846  O2  EDO A 344      38.187 -36.015  15.626  1.00 42.78           O  
HETATM 2847  C1  EDO A 345      19.415 -27.579  15.641  1.00 36.05           C  
HETATM 2848  O1  EDO A 345      18.612 -26.416  15.884  1.00 36.30           O  
HETATM 2849  C2  EDO A 345      18.554 -28.838  15.673  1.00 30.48           C  
HETATM 2850  O2  EDO A 345      17.199 -28.530  15.316  1.00 26.54           O  
HETATM 2851  C1  EDO A 346      46.096 -32.820   6.362  1.00 34.89           C  
HETATM 2852  O1  EDO A 346      45.187 -33.876   6.713  1.00 41.33           O  
HETATM 2853  C2  EDO A 346      46.688 -33.074   4.975  1.00 39.51           C  
HETATM 2854  O2  EDO A 346      47.830 -33.946   5.050  1.00 29.68           O  
HETATM 2855  C1  EDO A 347      -3.512 -28.782  24.927  1.00 31.45           C  
HETATM 2856  O1  EDO A 347      -4.315 -28.235  25.980  1.00 34.75           O  
HETATM 2857  C2  EDO A 347      -3.161 -30.226  25.258  1.00 23.02           C  
HETATM 2858  O2  EDO A 347      -2.455 -30.258  26.501  1.00 28.27           O  
HETATM 2859  C1  EDO A 348      13.925 -26.745  12.537  1.00 30.67           C  
HETATM 2860  O1  EDO A 348      15.064 -26.455  11.710  1.00 27.06           O  
HETATM 2861  C2  EDO A 348      14.326 -27.670  13.686  1.00 28.04           C  
HETATM 2862  O2  EDO A 348      15.184 -26.970  14.593  1.00 34.93           O  
HETATM 2863  C1  EDO A 349      13.940 -31.689  22.311  1.00 39.56           C  
HETATM 2864  O1  EDO A 349      14.512 -30.521  21.707  1.00 45.99           O  
HETATM 2865  C2  EDO A 349      13.327 -31.365  23.668  1.00 44.54           C  
HETATM 2866  O2  EDO A 349      12.614 -32.504  24.166  1.00 44.84           O  
HETATM 2867  C1  EDO A 350      10.835 -28.583  23.200  1.00 32.95           C  
HETATM 2868  O1  EDO A 350       9.779 -27.664  23.502  1.00 33.08           O  
HETATM 2869  C2  EDO A 350      10.240 -29.859  22.616  1.00 31.46           C  
HETATM 2870  O2  EDO A 350       9.881 -29.645  21.243  1.00 32.80           O  
HETATM 2871  C1  EDO A 351      20.986 -23.426  13.465  1.00 52.38           C  
HETATM 2872  O1  EDO A 351      20.721 -22.062  13.812  1.00 57.95           O  
HETATM 2873  C2  EDO A 351      20.228 -24.368  14.395  1.00 49.78           C  
HETATM 2874  O2  EDO A 351      20.793 -24.356  15.712  1.00 46.66           O  
HETATM 2875  C1  EDO A 352     -13.220 -35.583  18.281  1.00 37.90           C  
HETATM 2876  O1  EDO A 352     -13.664 -35.017  17.031  1.00 39.89           O  
HETATM 2877  C2  EDO A 352     -11.932 -36.382  18.091  1.00 40.36           C  
HETATM 2878  O2  EDO A 352     -12.190 -37.673  17.506  1.00 34.29           O  
HETATM 2879  O   HOH A 353       8.987 -40.871  17.285  1.00 11.54           O  
HETATM 2880  O   HOH A 354      19.887 -46.447  16.454  1.00 14.49           O  
HETATM 2881  O   HOH A 355       2.911 -32.739  22.505  1.00 12.91           O  
HETATM 2882  O   HOH A 356      17.796 -55.912  14.153  1.00 18.39           O  
HETATM 2883  O   HOH A 357       3.501 -48.348  17.810  1.00 12.78           O  
HETATM 2884  O   HOH A 358       4.072 -45.639   8.010  1.00 15.13           O  
HETATM 2885  O   HOH A 359       5.129 -56.420  16.508  1.00 14.96           O  
HETATM 2886  O   HOH A 360       2.642 -49.571  11.395  1.00 16.54           O  
HETATM 2887  O   HOH A 361       6.648 -54.967  18.038  1.00 14.45           O  
HETATM 2888  O   HOH A 362       2.678 -37.208  23.829  1.00 13.76           O  
HETATM 2889  O   HOH A 363     -12.542 -41.011  25.190  1.00 13.06           O  
HETATM 2890  O   HOH A 364       3.806 -30.836  20.403  1.00 14.14           O  
HETATM 2891  O   HOH A 365       3.656 -45.923   5.361  1.00 14.29           O  
HETATM 2892  O   HOH A 366      22.685 -41.517   5.775  1.00 15.45           O  
HETATM 2893  O   HOH A 367      10.733 -37.427  20.575  1.00 19.09           O  
HETATM 2894  O   HOH A 368       2.780 -53.781  16.835  1.00 14.74           O  
HETATM 2895  O   HOH A 369      14.426 -50.921  22.150  1.00 20.60           O  
HETATM 2896  O   HOH A 370      21.855 -39.865  13.360  1.00 13.76           O  
HETATM 2897  O   HOH A 371      42.009 -38.747  25.405  1.00 17.57           O  
HETATM 2898  O   HOH A 372      -4.465 -31.544  28.119  1.00 19.13           O  
HETATM 2899  O   HOH A 373       4.265 -54.914  26.848  1.00 23.39           O  
HETATM 2900  O   HOH A 374      17.533 -39.711  18.780  1.00 16.97           O  
HETATM 2901  O   HOH A 375       0.699 -45.713  11.723  1.00 17.36           O  
HETATM 2902  O   HOH A 376       2.793 -46.915  10.393  1.00 16.79           O  
HETATM 2903  O   HOH A 377     -14.155 -40.349  27.563  1.00 15.62           O  
HETATM 2904  O   HOH A 378      20.975 -39.402   2.890  1.00 21.54           O  
HETATM 2905  O   HOH A 379       9.134 -41.397   0.598  1.00 19.48           O  
HETATM 2906  O   HOH A 380      -4.935 -25.756   7.552  1.00 18.32           O  
HETATM 2907  O   HOH A 381      21.984 -35.285  17.697  1.00 18.29           O  
HETATM 2908  O   HOH A 382       0.274 -51.267  14.343  1.00 18.60           O  
HETATM 2909  O   HOH A 383      -1.149 -47.631  12.399  1.00 21.52           O  
HETATM 2910  O   HOH A 384       0.018 -50.293  11.987  1.00 20.34           O  
HETATM 2911  O   HOH A 385      39.348 -42.611  11.751  1.00 16.81           O  
HETATM 2912  O   HOH A 386      -7.995 -37.924  17.848  1.00 14.71           O  
HETATM 2913  O   HOH A 387      37.834 -39.677   5.231  1.00 20.11           O  
HETATM 2914  O   HOH A 388      -6.813 -42.787  11.904  1.00 13.63           O  
HETATM 2915  O   HOH A 389      11.369 -28.600  13.194  1.00 21.39           O  
HETATM 2916  O   HOH A 390      -3.234 -56.930  17.914  1.00 24.53           O  
HETATM 2917  O   HOH A 391      -1.347 -35.492  36.694  1.00 18.42           O  
HETATM 2918  O   HOH A 392       1.543 -47.653   4.618  1.00 22.24           O  
HETATM 2919  O   HOH A 393      22.234 -57.364  15.694  1.00 32.79           O  
HETATM 2920  O   HOH A 394      16.303 -42.005  16.506  1.00 16.12           O  
HETATM 2921  O   HOH A 395      14.367 -37.035  22.773  1.00 24.20           O  
HETATM 2922  O   HOH A 396       5.423 -24.868  -3.326  1.00 20.38           O  
HETATM 2923  O   HOH A 397      -9.125 -46.712  21.995  1.00 19.61           O  
HETATM 2924  O   HOH A 398      -1.139 -18.620   6.435  1.00 21.33           O  
HETATM 2925  O   HOH A 399     -11.422 -52.354  23.775  1.00 22.96           O  
HETATM 2926  O   HOH A 400      -7.604 -26.782   3.277  1.00 21.94           O  
HETATM 2927  O   HOH A 401     -13.582 -42.892  31.940  1.00 19.54           O  
HETATM 2928  O   HOH A 402      21.093 -26.219   3.957  1.00 23.45           O  
HETATM 2929  O   HOH A 403      43.640 -41.818  21.066  1.00 21.26           O  
HETATM 2930  O   HOH A 404       6.222 -31.065   0.101  1.00 21.88           O  
HETATM 2931  O   HOH A 405       5.926 -29.808  19.127  1.00 25.17           O  
HETATM 2932  O   HOH A 406      10.860 -50.969  28.444  1.00 23.36           O  
HETATM 2933  O   HOH A 407      23.244 -54.092   4.147  1.00 23.70           O  
HETATM 2934  O   HOH A 408      26.114 -50.905   5.506  1.00 23.66           O  
HETATM 2935  O   HOH A 409      -2.706 -21.923  21.212  1.00 21.27           O  
HETATM 2936  O   HOH A 410       0.774 -42.278  -0.412  1.00 29.93           O  
HETATM 2937  O   HOH A 411      23.379 -41.136  19.237  1.00 27.98           O  
HETATM 2938  O   HOH A 412     -10.318 -16.170  19.802  1.00 21.17           O  
HETATM 2939  O   HOH A 413      -7.632 -14.724  21.421  1.00 24.65           O  
HETATM 2940  O   HOH A 414     -15.121 -30.129  22.991  1.00 31.12           O  
HETATM 2941  O   HOH A 415       5.720 -44.137  32.363  1.00 32.89           O  
HETATM 2942  O   HOH A 416      -1.666 -25.760   8.506  1.00 20.16           O  
HETATM 2943  O   HOH A 417      17.143 -26.886  19.125  1.00 29.81           O  
HETATM 2944  O   HOH A 418      -4.114 -29.928  30.383  1.00 26.31           O  
HETATM 2945  O   HOH A 419       4.413 -46.642  34.675  1.00 32.14           O  
HETATM 2946  O   HOH A 420      10.164 -56.549   9.469  1.00 21.53           O  
HETATM 2947  O   HOH A 421      41.959 -41.303  14.987  1.00 24.00           O  
HETATM 2948  O   HOH A 422      -5.506 -28.983   0.729  1.00 24.63           O  
HETATM 2949  O   HOH A 423      -4.991 -46.372   9.146  1.00 30.81           O  
HETATM 2950  O   HOH A 424      27.660 -30.729   4.215  1.00 29.30           O  
HETATM 2951  O   HOH A 425     -21.404 -41.199  36.611  1.00 27.34           O  
HETATM 2952  O   HOH A 426      -2.740 -35.777  -0.544  1.00 20.22           O  
HETATM 2953  O   HOH A 427      -8.719 -49.412  21.249  1.00 29.92           O  
HETATM 2954  O   HOH A 428      16.577 -35.947   0.068  1.00 21.27           O  
HETATM 2955  O   HOH A 429       3.162 -42.870  31.959  1.00 22.42           O  
HETATM 2956  O   HOH A 430      -8.147 -43.271   9.276  1.00 29.09           O  
HETATM 2957  O   HOH A 431      31.321 -36.279  22.820  1.00 34.85           O  
HETATM 2958  O   HOH A 432      23.663 -61.490   5.037  1.00 37.50           O  
HETATM 2959  O   HOH A 433       9.789 -37.458  31.225  1.00 36.24           O  
HETATM 2960  O   HOH A 434       2.995 -25.731  25.757  1.00 31.26           O  
HETATM 2961  O   HOH A 435      -7.586 -40.501   5.760  1.00 22.37           O  
HETATM 2962  O   HOH A 436     -13.460 -28.763   3.650  1.00 41.17           O  
HETATM 2963  O   HOH A 437     -14.286 -47.573  28.134  1.00 28.78           O  
HETATM 2964  O   HOH A 438       8.992 -23.871  21.291  1.00 31.83           O  
HETATM 2965  O   HOH A 439     -11.063 -51.070  21.222  1.00 32.01           O  
HETATM 2966  O   HOH A 440      40.192 -26.924  14.795  1.00 25.66           O  
HETATM 2967  O   HOH A 441       8.846 -52.049  29.945  1.00 35.68           O  
HETATM 2968  O   HOH A 442      -9.323 -46.912  17.430  1.00 22.12           O  
HETATM 2969  O   HOH A 443      24.442 -44.374  18.580  1.00 28.11           O  
HETATM 2970  O   HOH A 444      -4.785 -23.809  21.307  1.00 23.80           O  
HETATM 2971  O   HOH A 445       0.403 -42.968  -3.612  1.00 25.15           O  
HETATM 2972  O   HOH A 446      -7.421 -35.680  36.038  1.00 23.99           O  
HETATM 2973  O   HOH A 447      30.472 -48.622   8.290  1.00 27.71           O  
HETATM 2974  O   HOH A 448      24.588 -23.891  18.696  1.00 39.99           O  
HETATM 2975  O   HOH A 449      -4.227 -19.079   5.923  1.00 25.82           O  
HETATM 2976  O   HOH A 450     -16.376 -33.756  16.087  1.00 26.91           O  
HETATM 2977  O   HOH A 451      -5.542 -40.836   3.692  1.00 26.34           O  
HETATM 2978  O   HOH A 452     -13.062 -33.825  34.162  1.00 25.66           O  
HETATM 2979  O   HOH A 453       2.877 -40.653  -2.024  1.00 36.34           O  
HETATM 2980  O   HOH A 454       8.408 -43.660  28.127  1.00 26.95           O  
HETATM 2981  O   HOH A 455      23.336 -24.450  16.087  1.00 23.85           O  
HETATM 2982  O   HOH A 456      -6.877 -38.794  -1.320  1.00 29.85           O  
HETATM 2983  O   HOH A 457       6.574 -42.217   0.161  1.00 32.59           O  
HETATM 2984  O   HOH A 458       4.250 -56.808  24.850  1.00 29.79           O  
HETATM 2985  O   HOH A 459      18.670 -36.527   1.628  1.00 41.68           O  
HETATM 2986  O   HOH A 460       2.731 -37.384  38.612  1.00 40.20           O  
HETATM 2987  O   HOH A 461      -8.272 -42.805   6.840  1.00 21.73           O  
HETATM 2988  O   HOH A 462      29.512 -44.707   6.245  1.00 30.57           O  
HETATM 2989  O   HOH A 463      13.783 -31.554   1.480  1.00 26.91           O  
HETATM 2990  O   HOH A 464      19.473 -40.454  20.444  1.00 32.00           O  
HETATM 2991  O   HOH A 465     -12.156 -44.554  18.915  1.00 26.17           O  
HETATM 2992  O   HOH A 466      33.404 -34.346  22.535  1.00 40.28           O  
HETATM 2993  O   HOH A 467      24.614 -42.885  20.996  1.00 27.93           O  
HETATM 2994  O   HOH A 468       0.554 -47.234  33.162  1.00 31.37           O  
HETATM 2995  O   HOH A 469      -9.790 -34.492  20.818  1.00 32.61           O  
HETATM 2996  O   HOH A 470       2.873 -47.067  32.777  1.00 36.55           O  
HETATM 2997  O   HOH A 471      -5.167 -15.793  12.654  1.00 33.66           O  
HETATM 2998  O   HOH A 472      22.380 -51.519   3.454  1.00 30.05           O  
HETATM 2999  O   HOH A 473      -4.059 -51.031  37.829  1.00 36.69           O  
HETATM 3000  O   HOH A 474      -4.934 -46.758  37.318  1.00 29.20           O  
HETATM 3001  O   HOH A 475      -3.943 -35.056  37.565  1.00 26.44           O  
HETATM 3002  O   HOH A 476      42.444 -43.224  16.922  1.00 30.61           O  
HETATM 3003  O   HOH A 477      -1.280 -39.304  -3.392  1.00 28.50           O  
HETATM 3004  O   HOH A 478     -13.624 -53.509  28.381  1.00 31.89           O  
HETATM 3005  O   HOH A 479      36.688 -36.539   3.451  1.00 40.64           O  
HETATM 3006  O   HOH A 480     -11.940 -46.797  21.061  1.00 26.59           O  
HETATM 3007  O   HOH A 481      39.690 -30.436  14.892  1.00 22.81           O  
HETATM 3008  O   HOH A 482     -12.156 -35.922  36.712  1.00 31.35           O  
HETATM 3009  O   HOH A 483      11.129 -59.699  22.041  1.00 28.91           O  
HETATM 3010  O   HOH A 484     -12.156 -36.058  12.025  1.00 31.53           O  
HETATM 3011  O   HOH A 485       0.691 -35.685  38.432  1.00 29.26           O  
HETATM 3012  O   HOH A 486     -15.249 -28.824  25.276  1.00 33.35           O  
HETATM 3013  O   HOH A 487     -17.117 -32.681  26.885  1.00 29.66           O  
HETATM 3014  O   HOH A 488      16.588 -54.905  16.453  1.00 26.49           O  
HETATM 3015  O   HOH A 489      25.439 -56.069   9.491  1.00 29.14           O  
HETATM 3016  O   HOH A 490      45.408 -39.758   7.676  1.00 36.57           O  
HETATM 3017  O   HOH A 491      31.016 -52.455   6.147  1.00 49.61           O  
HETATM 3018  O   HOH A 492     -11.225 -39.951  12.195  1.00 30.54           O  
HETATM 3019  O   HOH A 493      -8.669 -30.348  26.891  1.00 32.98           O  
HETATM 3020  O   HOH A 494      -8.812 -56.960  28.616  1.00 38.66           O  
HETATM 3021  O   HOH A 495       5.944 -56.460  28.158  1.00 42.20           O  
HETATM 3022  O   HOH A 496      -6.596 -51.753   8.705  1.00 41.18           O  
HETATM 3023  O   HOH A 497     -11.037 -26.208   3.618  1.00 44.65           O  
HETATM 3024  O   HOH A 498      -3.234 -43.681  42.897  1.00 42.07           O  
HETATM 3025  O   HOH A 499      42.432 -41.227  10.656  1.00 32.84           O  
HETATM 3026  O   HOH A 500      31.718 -33.575   2.882  1.00 31.86           O  
HETATM 3027  O   HOH A 501      -9.625 -34.728  37.096  1.00 31.70           O  
HETATM 3028  O   HOH A 502       9.199 -52.110   1.314  1.00 40.53           O  
HETATM 3029  O   HOH A 503      20.046 -49.891   1.955  1.00 31.41           O  
HETATM 3030  O   HOH A 504      41.837 -42.981  12.600  1.00 27.78           O  
HETATM 3031  O   HOH A 505      -7.323 -50.590  14.907  1.00 28.55           O  
HETATM 3032  O   HOH A 506      -7.186 -53.302  30.877  1.00 26.87           O  
HETATM 3033  O   HOH A 507       9.388 -39.697  -1.489  1.00 30.55           O  
HETATM 3034  O   HOH A 508     -13.871 -42.218  18.577  1.00 29.56           O  
HETATM 3035  O   HOH A 509      -1.937 -55.736  13.465  1.00 31.56           O  
HETATM 3036  O   HOH A 510     -12.295 -43.120  34.267  1.00 42.79           O  
HETATM 3037  O   HOH A 511      15.669 -52.821  21.172  1.00 28.09           O  
HETATM 3038  O   HOH A 512      -3.645 -30.545  32.931  1.00 29.39           O  
HETATM 3039  O   HOH A 513      10.723 -61.471  14.569  1.00 35.50           O  
HETATM 3040  O   HOH A 514      43.133 -41.011  23.974  1.00 24.97           O  
HETATM 3041  O   HOH A 515      12.327 -58.376  -0.032  1.00 33.37           O  
HETATM 3042  O   HOH A 516      13.442 -35.011  -1.078  1.00 51.72           O  
HETATM 3043  O   HOH A 517     -11.705 -27.740   1.000  1.00 36.49           O  
HETATM 3044  O   HOH A 518      -5.860 -42.693  -1.803  1.00 34.88           O  
HETATM 3045  O   HOH A 519      17.950 -53.316  22.670  1.00 34.24           O  
HETATM 3046  O   HOH A 520      19.622 -57.566  15.677  1.00 37.57           O  
HETATM 3047  O   HOH A 521      -8.882 -41.271  44.550  1.00 47.56           O  
HETATM 3048  O   HOH A 522     -13.228 -50.239  28.060  1.00 33.31           O  
HETATM 3049  O   HOH A 523       0.028 -51.910  36.102  1.00 34.92           O  
HETATM 3050  O   HOH A 524      -1.579 -21.597  23.731  1.00 34.19           O  
HETATM 3051  O   HOH A 525      11.834 -60.657  -0.713  1.00 33.81           O  
HETATM 3052  O   HOH A 526      22.340 -29.992   3.535  1.00 33.35           O  
HETATM 3053  O   HOH A 527      -6.869 -48.041   6.855  1.00 44.06           O  
HETATM 3054  O   HOH A 528      25.428 -25.634   4.585  1.00 36.24           O  
HETATM 3055  O   HOH A 529       5.592 -46.281  30.843  1.00 37.42           O  
HETATM 3056  O   HOH A 530      34.118 -44.081   5.974  1.00 42.31           O  
HETATM 3057  O   HOH A 531      -9.727 -36.677  19.920  1.00 29.57           O  
HETATM 3058  O   HOH A 532      41.958 -44.391  20.994  1.00 32.80           O  
HETATM 3059  O   HOH A 533      29.946 -25.609   2.803  1.00 31.26           O  
HETATM 3060  O   HOH A 534     -16.297 -31.170  13.532  1.00 36.73           O  
HETATM 3061  O   HOH A 535      20.135 -21.628   3.369  1.00 36.24           O  
HETATM 3062  O   HOH A 536      -5.726 -12.160  15.693  1.00 35.86           O  
HETATM 3063  O   HOH A 537      15.438 -64.473   6.272  1.00 47.94           O  
HETATM 3064  O   HOH A 538      25.336 -60.721  15.449  1.00 44.65           O  
HETATM 3065  O   HOH A 539      36.246 -51.381  12.114  1.00 43.19           O  
HETATM 3066  O   HOH A 540     -10.406 -12.657  12.914  1.00 44.14           O  
HETATM 3067  O   HOH A 541      -4.024 -57.459  32.035  1.00 29.96           O  
HETATM 3068  O   HOH A 542      -9.628 -39.050   4.423  1.00 40.58           O  
HETATM 3069  O   HOH A 543     -11.825 -18.407  15.845  1.00 43.15           O  
HETATM 3070  O   HOH A 544      29.965 -49.690   5.661  1.00 36.88           O  
HETATM 3071  O   HOH A 545       1.589 -17.726  10.004  1.00 34.66           O  
HETATM 3072  O   HOH A 546      24.998 -45.095   0.252  1.00 45.15           O  
HETATM 3073  O   HOH A 547      40.331 -25.921   4.480  1.00 43.50           O  
HETATM 3074  O   HOH A 548      -9.017 -49.318  18.607  1.00 42.10           O  
HETATM 3075  O   HOH A 549     -17.098 -27.192  24.175  1.00 24.07           O  
HETATM 3076  O   HOH A 550     -11.582 -32.895  30.824  1.00 37.29           O  
HETATM 3077  O   HOH A 551     -13.016 -49.345  20.451  1.00 33.16           O  
HETATM 3078  O   HOH A 552      14.318 -55.182  21.070  1.00 30.29           O  
HETATM 3079  O   HOH A 553      -2.595 -32.555  34.139  1.00 32.88           O  
HETATM 3080  O   HOH A 554      11.397 -33.436  -1.627  1.00 36.25           O  
HETATM 3081  O   HOH A 555      18.931 -45.870   1.296  1.00 29.31           O  
HETATM 3082  O   HOH A 556      -8.316 -12.231  22.397  1.00 34.91           O  
HETATM 3083  O   HOH A 557       4.166 -56.597   4.985  1.00 33.50           O  
HETATM 3084  O   HOH A 558       0.796 -49.582  32.362  1.00 41.85           O  
HETATM 3085  O   HOH A 559     -11.599 -18.937  20.443  1.00 44.26           O  
HETATM 3086  O   HOH A 560       1.785 -52.390  30.681  1.00 27.95           O  
HETATM 3087  O   HOH A 561       4.156 -23.647  16.847  1.00 36.00           O  
HETATM 3088  O   HOH A 562      18.500 -51.548   0.573  1.00 33.29           O  
HETATM 3089  O   HOH A 563     -14.599 -49.080  30.299  1.00 37.03           O  
HETATM 3090  O   HOH A 564      33.863 -30.493  24.531  1.00 34.27           O  
HETATM 3091  O   HOH A 565      19.680 -40.421  -3.506  1.00 41.55           O  
HETATM 3092  O   HOH A 566      -7.157 -47.993  35.960  1.00 30.89           O  
HETATM 3093  O   HOH A 567      -5.034 -24.078  23.853  1.00 41.10           O  
HETATM 3094  O   HOH A 568      29.486 -55.523   7.750  1.00 38.26           O  
HETATM 3095  O   HOH A 569      -7.865 -50.118  38.360  1.00 46.08           O  
HETATM 3096  O   HOH A 570      25.449 -60.897   9.766  1.00 50.64           O  
HETATM 3097  O   HOH A 571       5.339 -41.809  -1.955  1.00 41.56           O  
HETATM 3098  O   HOH A 572      10.026 -51.195  32.720  1.00 36.14           O  
HETATM 3099  O   HOH A 573      -3.816 -27.684  28.935  1.00 48.98           O  
HETATM 3100  O   HOH A 574      -3.764 -62.391  26.213  1.00 54.21           O  
HETATM 3101  O   HOH A 575      18.609 -20.792  13.803  1.00 29.57           O  
HETATM 3102  O   HOH A 576      -5.911 -50.429  39.984  1.00 31.27           O  
HETATM 3103  O   HOH A 577      10.886 -54.346   1.006  1.00 27.43           O  
HETATM 3104  O   HOH A 578       7.886 -43.712  33.472  1.00 40.79           O  
HETATM 3105  O   HOH A 579      21.565 -56.109   3.123  1.00 31.07           O  
HETATM 3106  O   HOH A 580      26.921 -54.949   7.785  1.00 38.95           O  
HETATM 3107  O   HOH A 581       5.219 -37.752  -3.409  1.00 31.63           O  
HETATM 3108  O   HOH A 582      23.543 -26.288   2.871  1.00 38.05           O  
HETATM 3109  O   HOH A 583      -3.752 -37.691  -3.065  1.00 35.09           O  
HETATM 3110  O   HOH A 584      33.644 -52.199  13.564  1.00 32.43           O  
HETATM 3111  O   HOH A 585      12.975 -52.583  28.329  1.00 38.29           O  
HETATM 3112  O   HOH A 586      -7.329 -46.771   9.945  1.00 38.33           O  
HETATM 3113  O   HOH A 587      15.709 -24.026  20.958  1.00 37.85           O  
HETATM 3114  O   HOH A 588      -6.695 -29.987  28.212  1.00 41.24           O  
HETATM 3115  O   HOH A 589       2.114 -60.305  23.873  1.00 41.47           O  
HETATM 3116  O   HOH A 590     -12.107 -36.412  39.559  1.00 33.57           O  
HETATM 3117  O   HOH A 591       0.659 -37.607  -2.181  1.00 38.27           O  
HETATM 3118  O   HOH A 592      -7.474 -11.257  19.867  1.00 38.67           O  
HETATM 3119  O   HOH A 593      -0.958 -57.855  30.505  1.00 37.24           O  
HETATM 3120  O   HOH A 594       8.309 -39.434  34.616  1.00 28.39           O  
HETATM 3121  O   HOH A 595       7.165 -48.266  31.823  1.00 40.15           O  
HETATM 3122  O   HOH A 596       9.210 -44.839  30.298  1.00 42.43           O  
HETATM 3123  O   HOH A 597      38.333 -41.802   3.751  1.00 44.38           O  
HETATM 3124  O   HOH A 598      11.855 -49.430  30.513  1.00 44.09           O  
HETATM 3125  O   HOH A 599     -13.199 -49.022  17.846  1.00 43.38           O  
HETATM 3126  O   HOH A 600     -12.130 -33.036  13.150  1.00 41.24           O  
HETATM 3127  O   HOH A 601       2.030 -54.408  28.689  1.00 33.15           O  
HETATM 3128  O   HOH A 602      12.591 -52.701   2.190  1.00 31.39           O  
HETATM 3129  O   HOH A 603     -22.838 -42.228  38.659  1.00 41.52           O  
HETATM 3130  O   HOH A 604      43.553 -46.577  21.223  1.00 39.70           O  
HETATM 3131  O   HOH A 605      21.818 -33.439   0.661  1.00 34.62           O  
HETATM 3132  O   HOH A 606       6.823 -39.637  -2.417  1.00 38.12           O  
HETATM 3133  O   HOH A 607      -2.702 -45.750  44.276  1.00 48.77           O  
HETATM 3134  O   HOH A 608     -11.272 -31.729   1.446  1.00 39.82           O  
HETATM 3135  O   HOH A 609      32.326 -24.884   9.038  1.00 38.28           O  
HETATM 3136  O   HOH A 610      35.295 -25.089  -1.615  1.00 49.23           O  
HETATM 3137  O   HOH A 611       7.698 -50.635  34.147  1.00 44.01           O  
HETATM 3138  O   HOH A 612       9.908 -34.472  35.583  1.00 42.93           O  
HETATM 3139  O   HOH A 613      37.928 -49.254   7.995  1.00 33.32           O  
HETATM 3140  O   HOH A 614      23.152 -26.273  22.215  1.00 41.20           O  
HETATM 3141  O   HOH A 615      41.285 -28.672  16.660  1.00 35.58           O  
HETATM 3142  O   HOH A 616      20.942 -32.581  17.029  1.00 26.57           O  
HETATM 3143  O   HOH A 617      22.035 -38.838  19.645  1.00 32.26           O  
HETATM 3144  O   HOH A 618      12.202 -30.676  19.997  1.00 14.82           O  
HETATM 3145  O   HOH A 619      14.373 -33.985  25.464  1.00 38.59           O  
HETATM 3146  O   HOH A 620      43.061 -34.427   4.985  1.00 35.88           O  
HETATM 3147  O   HOH A 621      -0.776 -29.421  28.143  1.00 20.64           O  
HETATM 3148  O   HOH A 622       3.095 -22.818  13.914  1.00 27.75           O  
HETATM 3149  O   HOH A 623       9.209 -20.408  16.731  1.00 38.23           O  
HETATM 3150  O   HOH A 624       3.905 -62.107  18.929  1.00 27.78           O  
HETATM 3151  O   HOH A 625      -0.182 -59.831  16.492  1.00 25.49           O  
HETATM 3152  O   HOH A 626      19.234 -38.595   0.745  1.00 35.60           O  
HETATM 3153  O   HOH A 627       9.452 -30.821  34.123  1.00 45.46           O  
HETATM 3154  O   HOH A 628     -12.153 -25.558   0.203  1.00 36.58           O  
HETATM 3155  O   HOH A 629      12.513 -56.905   2.268  1.00 32.28           O  
HETATM 3156  O   HOH A 630      12.552 -43.701  -2.672  1.00 39.41           O  
HETATM 3157  O   HOH A 631      24.894 -50.854   2.690  1.00 47.58           O  
HETATM 3158  O   HOH A 632      16.843 -21.855   7.294  1.00 31.74           O  
HETATM 3159  O   HOH A 633       6.043 -30.978  -2.727  1.00 40.43           O  
HETATM 3160  O   HOH A 634      44.817 -28.772  11.400  1.00 34.20           O  
HETATM 3161  O   HOH A 635      23.360 -38.250  -0.120  1.00 35.95           O  
HETATM 3162  O   HOH A 636      23.070 -35.013  20.269  1.00 37.93           O  
HETATM 3163  O   HOH A 637      -1.905 -57.581  15.499  1.00 37.08           O  
HETATM 3164  O   HOH A 638      -7.143 -62.724  28.374  1.00 43.76           O  
HETATM 3165  O   HOH A 639      -6.909 -22.965   3.883  1.00 36.99           O  
HETATM 3166  O   HOH A 640      35.774 -34.414  23.348  1.00 45.32           O  
HETATM 3167  O   HOH A 641     -12.621 -31.610  10.278  1.00 33.08           O  
HETATM 3168  O   HOH A 642     -13.569 -36.962  14.949  1.00 39.45           O  
HETATM 3169  O   HOH A 643      40.843 -44.553  18.615  1.00 34.61           O  
HETATM 3170  O   HOH A 644      15.373 -14.592  15.843  1.00 43.78           O  
HETATM 3171  O   HOH A 645      -6.338 -22.228   6.340  1.00 37.51           O  
HETATM 3172  O   HOH A 646      -8.097 -20.886   7.364  1.00 46.49           O  
HETATM 3173  O   HOH A 647      -1.390 -14.623  14.431  1.00 40.72           O  
HETATM 3174  O   HOH A 648      12.668 -60.723  16.841  1.00 38.81           O  
HETATM 3175  O   HOH A 649      19.780 -34.799  -1.808  1.00 38.64           O  
HETATM 3176  O   HOH A 650       4.401 -40.543  40.978  1.00 43.07           O  
HETATM 3177  O   HOH A 651       9.323 -46.983  31.784  1.00 53.17           O  
HETATM 3178  O   HOH A 652     -17.525 -43.561  33.887  1.00 35.48           O  
HETATM 3179  O   HOH A 653      25.803 -54.363   3.372  1.00 35.60           O  
HETATM 3180  O   HOH A 654      42.827 -26.398   5.086  1.00 36.77           O  
HETATM 3181  O   HOH A 655      15.340 -43.345  -2.787  1.00 43.07           O  
HETATM 3182  O   HOH A 656      42.969 -31.562  10.198  1.00 36.97           O  
HETATM 3183  O   HOH A 657      33.204 -51.226  16.085  1.00 54.54           O  
HETATM 3184  O   HOH A 658      -5.037 -26.627  34.398  1.00 49.78           O  
HETATM 3185  O   HOH A 659      -1.910 -34.521  -2.811  1.00 41.69           O  
HETATM 3186  O   HOH A 660      32.752 -37.926  24.216  1.00 43.13           O  
HETATM 3187  O   HOH A 661      17.955 -18.788  10.146  1.00 40.71           O  
HETATM 3188  O   HOH A 662      41.125 -44.687   9.088  1.00 40.62           O  
HETATM 3189  O   HOH A 663      14.143 -18.449   8.697  1.00 44.61           O  
HETATM 3190  O   HOH A 664      32.632 -23.638   3.736  1.00 42.30           O  
HETATM 3191  O   HOH A 665      43.601 -34.187  12.677  1.00 38.07           O  
HETATM 3192  O   HOH A 666      44.029 -39.282  13.971  1.00 36.52           O  
HETATM 3193  O   HOH A 667       4.442 -61.705   9.312  1.00 43.23           O  
HETATM 3194  O   HOH A 668      -6.223 -27.476  27.565  1.00 57.32           O  
HETATM 3195  O   HOH A 669      25.591 -23.039   3.959  1.00 49.88           O  
HETATM 3196  O   HOH A 670      10.349 -47.112  -0.137  1.00 39.41           O  
HETATM 3197  O   HOH A 671      16.192 -62.081   7.266  1.00 49.49           O  
HETATM 3198  O   HOH A 672      11.988 -17.990  10.583  1.00 43.35           O  
HETATM 3199  O   HOH A 673      33.949 -53.866  15.617  1.00 53.72           O  
HETATM 3200  O   HOH A 674      -4.454 -28.624  36.023  1.00 55.78           O  
HETATM 3201  O   HOH A 675     -13.092 -20.997  17.495  1.00 45.73           O  
HETATM 3202  O   HOH A 676      38.424 -43.378  18.884  1.00 48.49           O  
HETATM 3203  O   HOH A 677      17.663 -51.580  24.458  1.00 49.03           O  
HETATM 3204  O   HOH A 678      -0.956 -26.433  28.785  1.00 40.13           O  
HETATM 3205  O   HOH A 679     -12.680 -40.260  17.294  1.00 35.21           O  
HETATM 3206  O   HOH A 680      11.973 -60.029  11.207  1.00 40.14           O  
HETATM 3207  O   HOH A 681      10.583 -20.475   2.116  1.00 36.94           O  
HETATM 3208  O   HOH A 682     -16.460 -32.838  24.455  1.00 31.74           O  
HETATM 3209  O   HOH A 683      11.946 -31.462  32.508  1.00 41.88           O  
HETATM 3210  O   HOH A 684      17.725 -33.871  21.326  1.00 31.82           O  
HETATM 3211  O   HOH A 685      17.274 -36.842  20.894  1.00 39.21           O  
HETATM 3212  O   HOH A 686      18.354 -35.010  19.012  1.00 27.88           O  
CONECT 2784 2785 2789                                                           
CONECT 2785 2784 2786 2806                                                      
CONECT 2786 2785 2787                                                           
CONECT 2787 2786 2788 2811                                                      
CONECT 2788 2787 2789 2813                                                      
CONECT 2789 2784 2788                                                           
CONECT 2790 2807                                                                
CONECT 2791 2807                                                                
CONECT 2792 2815                                                                
CONECT 2793 2815                                                                
CONECT 2794 2815                                                                
CONECT 2795 2796 2797                                                           
CONECT 2796 2795 2808                                                           
CONECT 2797 2795 2810                                                           
CONECT 2798 2799 2809                                                           
CONECT 2799 2798 2813                                                           
CONECT 2800 2808 2810                                                           
CONECT 2801 2809 2812                                                           
CONECT 2802 2803 2814                                                           
CONECT 2803 2802 2814                                                           
CONECT 2804 2811 2812                                                           
CONECT 2805 2808 2811                                                           
CONECT 2806 2785 2814                                                           
CONECT 2807 2790 2791 2809                                                      
CONECT 2808 2796 2800 2805                                                      
CONECT 2809 2798 2801 2807                                                      
CONECT 2810 2797 2800 2815                                                      
CONECT 2811 2787 2804 2805                                                      
CONECT 2812 2801 2804 2813                                                      
CONECT 2813 2788 2799 2812                                                      
CONECT 2814 2802 2803 2806                                                      
CONECT 2815 2792 2793 2794 2810                                                 
CONECT 2816 2817 2818 2819 2820                                                 
CONECT 2817 2816                                                                
CONECT 2818 2816                                                                
CONECT 2819 2816                                                                
CONECT 2820 2816                                                                
CONECT 2821 2822 2823 2824 2825                                                 
CONECT 2822 2821                                                                
CONECT 2823 2821                                                                
CONECT 2824 2821                                                                
CONECT 2825 2821                                                                
CONECT 2826 2827 2828 2829 2830                                                 
CONECT 2827 2826                                                                
CONECT 2828 2826                                                                
CONECT 2829 2826                                                                
CONECT 2830 2826                                                                
CONECT 2831 2832 2833 2834 2835                                                 
CONECT 2832 2831                                                                
CONECT 2833 2831                                                                
CONECT 2834 2831                                                                
CONECT 2835 2831                                                                
CONECT 2836 2837 2838                                                           
CONECT 2837 2836                                                                
CONECT 2838 2836 2839                                                           
CONECT 2839 2838 2840                                                           
CONECT 2840 2839 2841                                                           
CONECT 2841 2840 2842                                                           
CONECT 2842 2841                                                                
CONECT 2843 2844 2845                                                           
CONECT 2844 2843                                                                
CONECT 2845 2843 2846                                                           
CONECT 2846 2845                                                                
CONECT 2847 2848 2849                                                           
CONECT 2848 2847                                                                
CONECT 2849 2847 2850                                                           
CONECT 2850 2849                                                                
CONECT 2851 2852 2853                                                           
CONECT 2852 2851                                                                
CONECT 2853 2851 2854                                                           
CONECT 2854 2853                                                                
CONECT 2855 2856 2857                                                           
CONECT 2856 2855                                                                
CONECT 2857 2855 2858                                                           
CONECT 2858 2857                                                                
CONECT 2859 2860 2861                                                           
CONECT 2860 2859                                                                
CONECT 2861 2859 2862                                                           
CONECT 2862 2861                                                                
CONECT 2863 2864 2865                                                           
CONECT 2864 2863                                                                
CONECT 2865 2863 2866                                                           
CONECT 2866 2865                                                                
CONECT 2867 2868 2869                                                           
CONECT 2868 2867                                                                
CONECT 2869 2867 2870                                                           
CONECT 2870 2869                                                                
CONECT 2871 2872 2873                                                           
CONECT 2872 2871                                                                
CONECT 2873 2871 2874                                                           
CONECT 2874 2873                                                                
CONECT 2875 2876 2877                                                           
CONECT 2876 2875                                                                
CONECT 2877 2875 2878                                                           
CONECT 2878 2877                                                                
MASTER      473    0   15   20    9    0   32    6 3194    1   95   26          
END