CNRS Nantes University UFIP UFIP
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***  LIGASE 11-FEB-17 5N4W  ***

elNémo ID: 22060310370630738

Job options:

ID        	=	 22060310370630738
JOBID     	=	 LIGASE 11-FEB-17 5N4W
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -400
DQMAX     	=	 400
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    LIGASE                                  11-FEB-17   5N4W              
TITLE     CRYSTAL STRUCTURE OF THE CUL2-RBX1-ELOBC-VHL UBIQUITIN LIGASE COMPLEX 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CULLIN-2;                                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CUL-2;                                                      
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: VON HIPPEL-LINDAU DISEASE TUMOR SUPPRESSOR;                
COMPND   8 CHAIN: V;                                                            
COMPND   9 SYNONYM: PROTEIN G7,PVHL;                                            
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE RBX1;                          
COMPND  13 CHAIN: R;                                                            
COMPND  14 SYNONYM: PROTEIN ZYP,RING FINGER PROTEIN 75,RING-BOX PROTEIN 1,RBX1, 
COMPND  15 REGULATOR OF CULLINS 1;                                              
COMPND  16 EC: 6.3.2.-;                                                         
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MOL_ID: 4;                                                           
COMPND  19 MOLECULE: ELONGIN-B;                                                 
COMPND  20 CHAIN: B;                                                            
COMPND  21 SYNONYM: ELOB,ELONGIN 18 KDA SUBUNIT,RNA POLYMERASE II TRANSCRIPTION 
COMPND  22 FACTOR SIII SUBUNIT B,SIII P18,TRANSCRIPTION ELONGATION FACTOR B     
COMPND  23 POLYPEPTIDE 2;                                                       
COMPND  24 ENGINEERED: YES;                                                     
COMPND  25 MOL_ID: 5;                                                           
COMPND  26 MOLECULE: ELONGIN-C;                                                 
COMPND  27 CHAIN: C;                                                            
COMPND  28 SYNONYM: ELOC,ELONGIN 15 KDA SUBUNIT,RNA POLYMERASE II TRANSCRIPTION 
COMPND  29 FACTOR SIII SUBUNIT C,SIII P15,TRANSCRIPTION ELONGATION FACTOR B     
COMPND  30 POLYPEPTIDE 1;                                                       
COMPND  31 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: CUL2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF21;                                   
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: VHL;                                                           
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 MOL_ID: 3;                                                           
SOURCE  19 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  20 ORGANISM_COMMON: HUMAN;                                              
SOURCE  21 ORGANISM_TAXID: 9606;                                                
SOURCE  22 GENE: RBX1, RNF75, ROC1;                                             
SOURCE  23 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  24 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  26 EXPRESSION_SYSTEM_CELL_LINE: SF21;                                   
SOURCE  27 MOL_ID: 4;                                                           
SOURCE  28 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  29 ORGANISM_COMMON: HUMAN;                                              
SOURCE  30 ORGANISM_TAXID: 9606;                                                
SOURCE  31 GENE: ELOB, TCEB2;                                                   
SOURCE  32 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  33 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  34 MOL_ID: 5;                                                           
SOURCE  35 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  36 ORGANISM_COMMON: HUMAN;                                              
SOURCE  37 ORGANISM_TAXID: 9606;                                                
SOURCE  38 GENE: ELOC, TCEB1;                                                   
SOURCE  39 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  40 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CULLIN RING, E3 UBIQUITIN LIGASE, VHL, LIGASE, CULLIN-2               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.A.F.CARDOTE,M.S.GADD,A.CIULLI                                       
REVDAT   4   24-APR-19 5N4W    1       SOURCE                                   
REVDAT   3   24-OCT-18 5N4W    1       REMARK LINK                              
REVDAT   2   21-JUN-17 5N4W    1       JRNL                                     
REVDAT   1   07-JUN-17 5N4W    0                                                
JRNL        AUTH   T.A.F.CARDOTE,M.S.GADD,A.CIULLI                              
JRNL        TITL   CRYSTAL STRUCTURE OF THE CUL2-RBX1-ELOBC-VHL UBIQUITIN       
JRNL        TITL 2 LIGASE COMPLEX.                                              
JRNL        REF    STRUCTURE                     V.  25   901 2017              
JRNL        REFN                   ISSN 1878-4186                               
JRNL        PMID   28591624                                                     
JRNL        DOI    10.1016/J.STR.2017.04.009                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11_2558: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 95.48                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 34407                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.304                           
REMARK   3   R VALUE            (WORKING SET) : 0.302                           
REMARK   3   FREE R VALUE                     : 0.346                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.240                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1802                            
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 95.5096 -  9.1678    0.99     2523   132  0.2378 0.2543        
REMARK   3     2  9.1678 -  7.2776    1.00     2510   144  0.2965 0.4164        
REMARK   3     3  7.2776 -  6.3579    1.00     2534   132  0.3463 0.3968        
REMARK   3     4  6.3579 -  5.7767    0.99     2479   139  0.3654 0.3823        
REMARK   3     5  5.7767 -  5.3627    0.99     2555   126  0.3389 0.3884        
REMARK   3     6  5.3627 -  5.0465    0.99     2513   129  0.3019 0.3205        
REMARK   3     7  5.0465 -  4.7938    1.00     2485   162  0.2974 0.3758        
REMARK   3     8  4.7938 -  4.5851    0.99     2493   159  0.3068 0.3149        
REMARK   3     9  4.5851 -  4.4086    1.00     2568   134  0.3103 0.3438        
REMARK   3    10  4.4086 -  4.2565    1.00     2506   142  0.3215 0.3607        
REMARK   3    11  4.2565 -  4.1234    0.98     2448   135  0.3410 0.3982        
REMARK   3    12  4.1234 -  4.0055    0.99     2509   133  0.3506 0.3771        
REMARK   3    13  4.0055 -  3.9001    0.99     2482   135  0.3973 0.4026        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.680            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 40.040           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 200.0                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 191.0                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           7855                                  
REMARK   3   ANGLE     :  0.692          10574                                  
REMARK   3   CHIRALITY :  0.043           1195                                  
REMARK   3   PLANARITY :  0.004           1346                                  
REMARK   3   DIHEDRAL  :  3.499           5127                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 163)                    
REMARK   3    ORIGIN FOR THE GROUP (A): -22.3345   3.0801 -61.2783              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0689 T22:   2.2287                                     
REMARK   3      T33:   1.4286 T12:  -0.3334                                     
REMARK   3      T13:  -0.6835 T23:   0.0869                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4416 L22:   2.6024                                     
REMARK   3      L33:   0.9859 L12:  -0.9161                                     
REMARK   3      L13:  -0.4704 L23:   0.0327                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.4110 S12:  -0.8893 S13:  -0.4805                       
REMARK   3      S21:  -0.5002 S22:  -0.4473 S23:   0.0407                       
REMARK   3      S31:   0.5873 S32:   0.2498 S33:   0.7896                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 164 THROUGH 277 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   1.7137  -6.9799 -34.8271              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8643 T22:   1.2219                                     
REMARK   3      T33:   0.3861 T12:  -0.2563                                     
REMARK   3      T13:  -0.1499 T23:  -0.4484                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6601 L22:   1.8008                                     
REMARK   3      L33:   4.4624 L12:   1.5957                                     
REMARK   3      L13:   1.5672 L23:  -0.7209                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5151 S12:   0.4970 S13:  -1.5810                       
REMARK   3      S21:  -0.3201 S22:  -0.4902 S23:  -0.6268                       
REMARK   3      S31:   1.9262 S32:  -0.1380 S33:  -1.9091                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 278 THROUGH 384 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  28.4750   3.9890 -10.4271              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0145 T22:   0.6923                                     
REMARK   3      T33:   0.6978 T12:  -0.1987                                     
REMARK   3      T13:  -0.0458 T23:   0.2188                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6025 L22:   4.3182                                     
REMARK   3      L33:   4.0187 L12:   2.2955                                     
REMARK   3      L13:   3.0674 L23:   3.5745                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5896 S12:   0.0704 S13:   1.0121                       
REMARK   3      S21:   0.5913 S22:  -0.6006 S23:  -0.5931                       
REMARK   3      S31:   1.1456 S32:  -0.2406 S33:  -0.1875                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 385 THROUGH 745 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  44.5049  34.3277   8.3282              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2817 T22:   0.9750                                     
REMARK   3      T33:   1.2739 T12:  -0.0270                                     
REMARK   3      T13:  -0.1324 T23:   0.0145                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3887 L22:   2.7737                                     
REMARK   3      L33:   1.1465 L12:   2.3656                                     
REMARK   3      L13:   1.2059 L23:  -0.6650                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4383 S12:  -0.4654 S13:  -0.5272                       
REMARK   3      S21:   0.7327 S22:  -0.1995 S23:  -0.2278                       
REMARK   3      S31:  -0.4248 S32:   0.0227 S33:  -0.2087                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'V' AND (RESID 157 THROUGH 169 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -27.4166  36.3384 -64.3799              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.7599 T22:   4.9135                                     
REMARK   3      T33:   1.7178 T12:   2.2711                                     
REMARK   3      T13:  -0.0416 T23:   0.5893                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8190 L22:   0.6587                                     
REMARK   3      L33:   2.3176 L12:   1.3946                                     
REMARK   3      L13:   1.6200 L23:   1.0974                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0845 S12:   0.0787 S13:   0.2800                       
REMARK   3      S21:  -0.5578 S22:  -0.0792 S23:   0.4548                       
REMARK   3      S31:  -0.2568 S32:   0.2531 S33:   0.2607                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'V' AND (RESID 170 THROUGH 174 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -41.6138  38.7758 -65.2808              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.9341 T22:   4.1075                                     
REMARK   3      T33:   4.4692 T12:   1.2560                                     
REMARK   3      T13:   1.6627 T23:  -0.1328                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2834 L22:   0.0010                                     
REMARK   3      L33:   1.6384 L12:  -0.0082                                     
REMARK   3      L13:  -0.6799 L23:   0.0144                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3704 S12:  -0.0463 S13:   0.1389                       
REMARK   3      S21:   0.2860 S22:   0.0839 S23:  -0.0599                       
REMARK   3      S31:   0.5034 S32:  -0.0416 S33:   0.1952                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'V' AND (RESID 175 THROUGH 184 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -38.6655  28.7954 -67.2672              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8979 T22:   3.7251                                     
REMARK   3      T33:   5.7989 T12:  -0.4477                                     
REMARK   3      T13:  -0.2185 T23:   0.4033                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0940 L22:   3.9026                                     
REMARK   3      L33:   1.9340 L12:  -1.1519                                     
REMARK   3      L13:   0.1177 L23:  -0.3047                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.4182 S12:  -3.7635 S13:   0.4264                       
REMARK   3      S21:  -0.5461 S22:   0.7130 S23:   0.0162                       
REMARK   3      S31:   0.6000 S32:  -0.9840 S33:  -2.0622                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'V' AND (RESID 185 THROUGH 193 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -34.7566  31.7704 -58.7414              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   3.3408 T22:   4.6010                                     
REMARK   3      T33:   1.8977 T12:   2.5002                                     
REMARK   3      T13:  -0.0999 T23:  -0.3595                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.8289 L22:   6.8594                                     
REMARK   3      L33:   3.6211 L12:  -6.4760                                     
REMARK   3      L13:  -1.9960 L23:   3.8285                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.3507 S12:   1.5725 S13:   1.1976                       
REMARK   3      S21:  -1.6292 S22:  -0.7883 S23:  -0.9787                       
REMARK   3      S31:   0.0909 S32:  -0.3411 S33:   0.5941                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'R' AND (RESID 17 THROUGH 39 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  60.0442  45.0616  12.0342              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0551 T22:   1.4693                                     
REMARK   3      T33:   1.9921 T12:  -0.2412                                     
REMARK   3      T13:  -0.2591 T23:   0.3776                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4695 L22:   5.0819                                     
REMARK   3      L33:   4.1034 L12:  -3.3631                                     
REMARK   3      L13:   1.5711 L23:   0.6260                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2816 S12:  -1.0039 S13:   1.1395                       
REMARK   3      S21:   0.1591 S22:  -0.7327 S23:  -1.4716                       
REMARK   3      S31:   0.7498 S32:   0.8090 S33:   0.2479                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'R' AND (RESID 40 THROUGH 102 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  26.0964  49.7187  15.3168              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.1877 T22:   1.7940                                     
REMARK   3      T33:   4.1069 T12:   0.1148                                     
REMARK   3      T13:  -0.3588 T23:  -1.1907                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9618 L22:   5.1236                                     
REMARK   3      L33:   6.0420 L12:   1.7897                                     
REMARK   3      L13:   1.6618 L23:   0.7178                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.2555 S12:  -0.6793 S13:   1.1224                       
REMARK   3      S21:  -0.4194 S22:  -1.2611 S23:   0.8705                       
REMARK   3      S31:   0.2689 S32:  -2.4303 S33:   1.5632                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 97 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.3664  36.4351 -85.7069              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.9877 T22:   3.2780                                     
REMARK   3      T33:   2.0168 T12:  -0.0367                                     
REMARK   3      T13:   0.2935 T23:   0.0999                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6330 L22:   3.5227                                     
REMARK   3      L33:   0.1523 L12:   2.8189                                     
REMARK   3      L13:   0.8571 L23:   0.6830                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.1701 S12:  -0.8976 S13:   1.7102                       
REMARK   3      S21:  -0.5568 S22:  -0.0118 S23:  -0.3669                       
REMARK   3      S31:  -2.0484 S32:  -1.7834 S33:  -0.1751                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 17 THROUGH 112 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -15.5196  27.7148 -72.2335              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9334 T22:   2.6424                                     
REMARK   3      T33:   1.0703 T12:  -0.3529                                     
REMARK   3      T13:  -0.3580 T23:   0.6579                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9764 L22:   2.6639                                     
REMARK   3      L33:   4.2153 L12:  -0.8038                                     
REMARK   3      L13:   1.4942 L23:   0.9370                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5457 S12:   1.5225 S13:   1.5369                       
REMARK   3      S21:  -1.0610 S22:   0.5154 S23:  -0.2467                       
REMARK   3      S31:  -2.1753 S32:   0.2148 S33:   0.5464                       
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 5N4W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003519.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-AUG-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.928                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DIALS                              
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34407                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 95.481                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : 0.11400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.73200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.200                              
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: HOMOLOGY MODEL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 7.6, 0.15 M AMMONIUM       
REMARK 280  SULPHATE, 15% POLYETHYLENEGLYCOL 4000 AND 3% 1,4-DIOXANE OR 4%      
REMARK 280  ACETONITRILE. THE SAMPLE WAS CRYSTALLISED IN THE PRESENCE OF A      
REMARK 280  19-MER PEPTIDE MIMICKING THE SUBSTRATE HIF-1ALPHA - RESIDUES 559-   
REMARK 280  577 (DEALAPYIPMDDDFQLRSF, WITH THE MUTATIONS L559D AND M561A AND    
REMARK 280  P564 IS HYDROXYPROLINE)., VAPOR DIFFUSION, HANGING DROP,            
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      119.44250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      119.44250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       43.01900            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       95.48100            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       43.01900            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       95.48100            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      119.44250            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       43.01900            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       95.48100            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      119.44250            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       43.01900            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       95.48100            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10350 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 56520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -174.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, V, R, B, C                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     LYS A   117                                                      
REMARK 465     LEU A   118                                                      
REMARK 465     THR A   119                                                      
REMARK 465     GLU A   120                                                      
REMARK 465     ALA A   121                                                      
REMARK 465     ASP A   122                                                      
REMARK 465     LEU A   123                                                      
REMARK 465     GLN A   124                                                      
REMARK 465     TYR A   125                                                      
REMARK 465     GLY A   126                                                      
REMARK 465     TYR A   127                                                      
REMARK 465     GLY A   128                                                      
REMARK 465     GLY A   129                                                      
REMARK 465     VAL A   130                                                      
REMARK 465     ASP A   131                                                      
REMARK 465     MET A   132                                                      
REMARK 465     ASN A   133                                                      
REMARK 465     GLU A   134                                                      
REMARK 465     TYR A   194                                                      
REMARK 465     LYS A   195                                                      
REMARK 465     LYS A   196                                                      
REMARK 465     LYS A   197                                                      
REMARK 465     LYS A   291                                                      
REMARK 465     LYS A   382                                                      
REMARK 465     LYS A   404                                                      
REMARK 465     ILE A   501                                                      
REMARK 465     ASP A   502                                                      
REMARK 465     LEU A   503                                                      
REMARK 465     GLY A   504                                                      
REMARK 465     ILE A   505                                                      
REMARK 465     SER A   524                                                      
REMARK 465     SER A   525                                                      
REMARK 465     THR A   526                                                      
REMARK 465     PHE A   527                                                      
REMARK 465     ALA A   528                                                      
REMARK 465     ILE A   529                                                      
REMARK 465     TYR A   568                                                      
REMARK 465     GLY A   570                                                      
REMARK 465     TYR A   573                                                      
REMARK 465     LEU A   585                                                      
REMARK 465     LEU A   586                                                      
REMARK 465     ALA A   587                                                      
REMARK 465     PHE A   588                                                      
REMARK 465     ASN A   589                                                      
REMARK 465     ASN A   590                                                      
REMARK 465     THR A   593                                                      
REMARK 465     LYS A   615                                                      
REMARK 465     HIS A   625                                                      
REMARK 465     ASP A   626                                                      
REMARK 465     SER A   627                                                      
REMARK 465     GLU A   628                                                      
REMARK 465     LYS A   629                                                      
REMARK 465     GLU A   630                                                      
REMARK 465     ASP A   631                                                      
REMARK 465     ILE A   632                                                      
REMARK 465     ASP A   633                                                      
REMARK 465     ALA A   634                                                      
REMARK 465     SER A   645                                                      
REMARK 465     SER A   646                                                      
REMARK 465     LYS A   647                                                      
REMARK 465     ARG A   648                                                      
REMARK 465     THR A   649                                                      
REMARK 465     LYS A   650                                                      
REMARK 465     PHE A   651                                                      
REMARK 465     LYS A   652                                                      
REMARK 465     ILE A   653                                                      
REMARK 465     THR A   654                                                      
REMARK 465     THR A   655                                                      
REMARK 465     SER A   656                                                      
REMARK 465     MET A   657                                                      
REMARK 465     GLN A   658                                                      
REMARK 465     LYS A   659                                                      
REMARK 465     ASP A   660                                                      
REMARK 465     GLN A   729                                                      
REMARK 465     MET V    54                                                      
REMARK 465     GLU V    55                                                      
REMARK 465     ALA V    56                                                      
REMARK 465     GLY V    57                                                      
REMARK 465     ARG V    58                                                      
REMARK 465     PRO V    59                                                      
REMARK 465     ARG V    60                                                      
REMARK 465     PRO V    61                                                      
REMARK 465     VAL V    62                                                      
REMARK 465     LEU V    63                                                      
REMARK 465     ARG V    64                                                      
REMARK 465     SER V    65                                                      
REMARK 465     VAL V    66                                                      
REMARK 465     ASN V    67                                                      
REMARK 465     SER V    68                                                      
REMARK 465     ARG V    69                                                      
REMARK 465     GLU V    70                                                      
REMARK 465     PRO V    71                                                      
REMARK 465     SER V    72                                                      
REMARK 465     GLN V    73                                                      
REMARK 465     VAL V    74                                                      
REMARK 465     ILE V    75                                                      
REMARK 465     PHE V    76                                                      
REMARK 465     CYS V    77                                                      
REMARK 465     ASN V    78                                                      
REMARK 465     ARG V    79                                                      
REMARK 465     SER V    80                                                      
REMARK 465     PRO V    81                                                      
REMARK 465     ARG V    82                                                      
REMARK 465     VAL V    83                                                      
REMARK 465     VAL V    84                                                      
REMARK 465     LEU V    85                                                      
REMARK 465     PRO V    86                                                      
REMARK 465     VAL V    87                                                      
REMARK 465     TRP V    88                                                      
REMARK 465     LEU V    89                                                      
REMARK 465     ASN V    90                                                      
REMARK 465     PHE V    91                                                      
REMARK 465     ASP V    92                                                      
REMARK 465     GLY V    93                                                      
REMARK 465     GLU V    94                                                      
REMARK 465     PRO V    95                                                      
REMARK 465     GLN V    96                                                      
REMARK 465     PRO V    97                                                      
REMARK 465     TYR V    98                                                      
REMARK 465     PRO V    99                                                      
REMARK 465     THR V   100                                                      
REMARK 465     LEU V   101                                                      
REMARK 465     PRO V   102                                                      
REMARK 465     PRO V   103                                                      
REMARK 465     GLY V   104                                                      
REMARK 465     THR V   105                                                      
REMARK 465     GLY V   106                                                      
REMARK 465     ARG V   107                                                      
REMARK 465     ARG V   108                                                      
REMARK 465     ILE V   109                                                      
REMARK 465     HIS V   110                                                      
REMARK 465     SER V   111                                                      
REMARK 465     TYR V   112                                                      
REMARK 465     ARG V   113                                                      
REMARK 465     GLY V   114                                                      
REMARK 465     HIS V   115                                                      
REMARK 465     LEU V   116                                                      
REMARK 465     TRP V   117                                                      
REMARK 465     LEU V   118                                                      
REMARK 465     PHE V   119                                                      
REMARK 465     ARG V   120                                                      
REMARK 465     ASP V   121                                                      
REMARK 465     ALA V   122                                                      
REMARK 465     GLY V   123                                                      
REMARK 465     THR V   124                                                      
REMARK 465     HIS V   125                                                      
REMARK 465     ASP V   126                                                      
REMARK 465     GLY V   127                                                      
REMARK 465     LEU V   128                                                      
REMARK 465     LEU V   129                                                      
REMARK 465     VAL V   130                                                      
REMARK 465     ASN V   131                                                      
REMARK 465     GLN V   132                                                      
REMARK 465     THR V   133                                                      
REMARK 465     GLU V   134                                                      
REMARK 465     LEU V   135                                                      
REMARK 465     PHE V   136                                                      
REMARK 465     VAL V   137                                                      
REMARK 465     PRO V   138                                                      
REMARK 465     SER V   139                                                      
REMARK 465     LEU V   140                                                      
REMARK 465     ASN V   141                                                      
REMARK 465     VAL V   142                                                      
REMARK 465     ASP V   143                                                      
REMARK 465     GLY V   144                                                      
REMARK 465     GLN V   145                                                      
REMARK 465     PRO V   146                                                      
REMARK 465     ILE V   147                                                      
REMARK 465     PHE V   148                                                      
REMARK 465     ALA V   149                                                      
REMARK 465     ASN V   150                                                      
REMARK 465     ILE V   151                                                      
REMARK 465     THR V   152                                                      
REMARK 465     LEU V   153                                                      
REMARK 465     PRO V   154                                                      
REMARK 465     VAL V   155                                                      
REMARK 465     TYR V   156                                                      
REMARK 465     VAL V   194                                                      
REMARK 465     GLN V   195                                                      
REMARK 465     LYS V   196                                                      
REMARK 465     ASP V   197                                                      
REMARK 465     LEU V   198                                                      
REMARK 465     GLU V   199                                                      
REMARK 465     ARG V   200                                                      
REMARK 465     LEU V   201                                                      
REMARK 465     THR V   202                                                      
REMARK 465     GLN V   203                                                      
REMARK 465     GLU V   204                                                      
REMARK 465     ARG V   205                                                      
REMARK 465     ILE V   206                                                      
REMARK 465     ALA V   207                                                      
REMARK 465     HIS V   208                                                      
REMARK 465     GLN V   209                                                      
REMARK 465     ARG V   210                                                      
REMARK 465     MET V   211                                                      
REMARK 465     GLY V   212                                                      
REMARK 465     ASP V   213                                                      
REMARK 465     MET R     1                                                      
REMARK 465     ALA R     2                                                      
REMARK 465     ALA R     3                                                      
REMARK 465     ALA R     4                                                      
REMARK 465     MET R     5                                                      
REMARK 465     ASP R     6                                                      
REMARK 465     VAL R     7                                                      
REMARK 465     ASP R     8                                                      
REMARK 465     THR R     9                                                      
REMARK 465     PRO R    10                                                      
REMARK 465     SER R    11                                                      
REMARK 465     GLY R    12                                                      
REMARK 465     THR R    13                                                      
REMARK 465     ASN R    14                                                      
REMARK 465     SER R    15                                                      
REMARK 465     GLY R    16                                                      
REMARK 465     HIS B    10                                                      
REMARK 465     LYS B    11                                                      
REMARK 465     ALA B    18                                                      
REMARK 465     LYS B    19                                                      
REMARK 465     GLU B    20                                                      
REMARK 465     SER B    21                                                      
REMARK 465     GLY B    61                                                      
REMARK 465     PHE B    62                                                      
REMARK 465     THR B    63                                                      
REMARK 465     VAL B    75                                                      
REMARK 465     GLY B    76                                                      
REMARK 465     LEU B    88                                                      
REMARK 465     CYS B    89                                                      
REMARK 465     ILE B    90                                                      
REMARK 465     GLU B    91                                                      
REMARK 465     GLU B    98                                                      
REMARK 465     LEU B    99                                                      
REMARK 465     PRO B   100                                                      
REMARK 465     ASP B   101                                                      
REMARK 465     VAL B   102                                                      
REMARK 465     MET B   103                                                      
REMARK 465     LYS B   104                                                      
REMARK 465     MET C    16                                                      
REMARK 465     PHE C    52                                                      
REMARK 465     GLU C    54                                                      
REMARK 465     ASN C    55                                                      
REMARK 465     GLU C    56                                                      
REMARK 465     THR C    57                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     TYR A  58    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     VAL A  76    CG1  CG2                                            
REMARK 470     TYR A  90    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 136    CG   CD1  CD2                                       
REMARK 470     MET A 137    CG   SD   CE                                        
REMARK 470     TRP A 147    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 147    CZ3  CH2                                            
REMARK 470     LYS A 238    CG   CD   CE   NZ                                   
REMARK 470     HIS A 255    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TYR A 378    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 398    CG   CD1  CD2                                       
REMARK 470     PHE A 422    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A 442    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A 449    CG   SD   CE                                        
REMARK 470     LYS A 462    CG   CD   CE   NZ                                   
REMARK 470     ILE A 494    CG1  CG2  CD1                                       
REMARK 470     PRO A 530    CG   CD                                             
REMARK 470     GLN A 531    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 532    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 533    CG   CD1  CD2                                       
REMARK 470     GLU A 534    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 535    CG   CD   CE   NZ                                   
REMARK 470     VAL A 537    CB   CG1  CG2                                       
REMARK 470     PHE A 540    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU A 542    CG   CD1  CD2                                       
REMARK 470     ARG A 710    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 720    CG   CD   CE   NZ                                   
REMARK 470     TYR A 741    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ALA R  17    CB                                                  
REMARK 470     GLN R  57    CG   CD   OE1  NE2                                  
REMARK 470     TRP R 101    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP R 101    CZ3  CH2                                            
REMARK 470     ARG B   8    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B  12    OG1  CG2                                            
REMARK 470     ASP B  52    CG   OD1  OD2                                       
REMARK 470     ARG B  80    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B  82    CG   OD1  OD2                                       
REMARK 470     PHE B  85    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     ARG C  63    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR C  83    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     THR C  88    CB   OG1  CG2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    LEU A   533     N    LYS A   535              1.22            
REMARK 500   NE   ARG A   475     OE2  GLU R    66              2.09            
REMARK 500   C    LEU A   533     N    LYS A   535              2.12            
REMARK 500   O    LEU A   533     CA   LYS A   535              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 530   N   -  CA  -  CB  ANGL. DEV. =   7.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A  47      -64.96   -122.95                                   
REMARK 500    PRO A  50       44.95    -82.04                                   
REMARK 500    GLU A  81       -2.80     67.60                                   
REMARK 500    GLU A 138       73.81     59.33                                   
REMARK 500    PRO A 154       -7.29    -55.55                                   
REMARK 500    HIS A 190      -21.54   -141.01                                   
REMARK 500    SER A 257       -7.44    -59.73                                   
REMARK 500    ALA A 272       -7.33     71.46                                   
REMARK 500    GLN A 332       -2.25     65.87                                   
REMARK 500    ASN A 334       57.48     35.62                                   
REMARK 500    ASN A 359       27.28     49.50                                   
REMARK 500    LYS A 386        1.68     58.33                                   
REMARK 500    ASN A 409       -0.98     66.12                                   
REMARK 500    ASN A 496       16.38   -140.40                                   
REMARK 500    GLN A 497     -148.15   -138.37                                   
REMARK 500    THR A 499     -163.04     54.43                                   
REMARK 500    ALA A 514       -0.85     67.14                                   
REMARK 500    LEU A 533     -169.34   -117.69                                   
REMARK 500    GLU A 534      -17.41     -5.83                                   
REMARK 500    LYS A 535     -148.79     73.23                                   
REMARK 500    SER A 536        6.32     92.74                                   
REMARK 500    LYS A 565       71.36     73.92                                   
REMARK 500    THR A 578      -51.22   -123.40                                   
REMARK 500    TYR A 580       62.12     66.18                                   
REMARK 500    SER A 595     -179.59    -68.82                                   
REMARK 500    VAL A 620      -69.54    -96.94                                   
REMARK 500    LYS A 621      -39.07   -135.03                                   
REMARK 500    GLN A 701      -16.85     75.58                                   
REMARK 500    SER A 707       30.02    -88.17                                   
REMARK 500    SER A 734      -61.25    -94.33                                   
REMARK 500    LYS R  26      130.45    -32.84                                   
REMARK 500    THR R  69      103.04   -161.28                                   
REMARK 500    ARG R  99     -168.47   -126.51                                   
REMARK 500    LYS B  46       74.83   -112.86                                   
REMARK 500    ASP B  47      -19.21     60.41                                   
REMARK 500    ASP B  48       -0.31   -149.06                                   
REMARK 500    ALA B  71       72.06   -161.08                                   
REMARK 500    ASP B  82      -67.53    -97.83                                   
REMARK 500    ASP B  83      -50.59   -126.52                                   
REMARK 500    ASP C 111       19.29     59.11                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN R 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS R  45   SG                                                     
REMARK 620 2 CYS R  83   SG   94.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN R 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS R  53   SG                                                     
REMARK 620 2 CYS R  56   SG  112.6                                              
REMARK 620 3 HIS R  82   NE2  65.9  86.0                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN R 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN R 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN R 203                  
DBREF  5N4W A    1   745  UNP    Q13617   CUL2_HUMAN       1    745             
DBREF  5N4W V   54   213  UNP    P40337   VHL_HUMAN       54    213             
DBREF  5N4W R    1   102  UNP    P62877   RBX1_HUMAN       1    102             
DBREF  5N4W B    1   104  UNP    Q15370   ELOB_HUMAN       1    104             
DBREF  5N4W C   17   112  UNP    Q15369   ELOC_HUMAN      17    112             
SEQADV 5N4W GLY A   -2  UNP  Q13617              EXPRESSION TAG                 
SEQADV 5N4W GLY A   -1  UNP  Q13617              EXPRESSION TAG                 
SEQADV 5N4W SER A    0  UNP  Q13617              EXPRESSION TAG                 
SEQADV 5N4W LYS R   18  UNP  P62877    GLY    18 CONFLICT                       
SEQADV 5N4W MET C   16  UNP  Q15369              INITIATING METHIONINE          
SEQRES   1 A  748  GLY GLY SER MET SER LEU LYS PRO ARG VAL VAL ASP PHE          
SEQRES   2 A  748  ASP GLU THR TRP ASN LYS LEU LEU THR THR ILE LYS ALA          
SEQRES   3 A  748  VAL VAL MET LEU GLU TYR VAL GLU ARG ALA THR TRP ASN          
SEQRES   4 A  748  ASP ARG PHE SER ASP ILE TYR ALA LEU CYS VAL ALA TYR          
SEQRES   5 A  748  PRO GLU PRO LEU GLY GLU ARG LEU TYR THR GLU THR LYS          
SEQRES   6 A  748  ILE PHE LEU GLU ASN HIS VAL ARG HIS LEU HIS LYS ARG          
SEQRES   7 A  748  VAL LEU GLU SER GLU GLU GLN VAL LEU VAL MET TYR HIS          
SEQRES   8 A  748  ARG TYR TRP GLU GLU TYR SER LYS GLY ALA ASP TYR MET          
SEQRES   9 A  748  ASP CYS LEU TYR ARG TYR LEU ASN THR GLN PHE ILE LYS          
SEQRES  10 A  748  LYS ASN LYS LEU THR GLU ALA ASP LEU GLN TYR GLY TYR          
SEQRES  11 A  748  GLY GLY VAL ASP MET ASN GLU PRO LEU MET GLU ILE GLY          
SEQRES  12 A  748  GLU LEU ALA LEU ASP MET TRP ARG LYS LEU MET VAL GLU          
SEQRES  13 A  748  PRO LEU GLN ALA ILE LEU ILE ARG MET LEU LEU ARG GLU          
SEQRES  14 A  748  ILE LYS ASN ASP ARG GLY GLY GLU ASP PRO ASN GLN LYS          
SEQRES  15 A  748  VAL ILE HIS GLY VAL ILE ASN SER PHE VAL HIS VAL GLU          
SEQRES  16 A  748  GLN TYR LYS LYS LYS PHE PRO LEU LYS PHE TYR GLN GLU          
SEQRES  17 A  748  ILE PHE GLU SER PRO PHE LEU THR GLU THR GLY GLU TYR          
SEQRES  18 A  748  TYR LYS GLN GLU ALA SER ASN LEU LEU GLN GLU SER ASN          
SEQRES  19 A  748  CYS SER GLN TYR MET GLU LYS VAL LEU GLY ARG LEU LYS          
SEQRES  20 A  748  ASP GLU GLU ILE ARG CYS ARG LYS TYR LEU HIS PRO SER          
SEQRES  21 A  748  SER TYR THR LYS VAL ILE HIS GLU CYS GLN GLN ARG MET          
SEQRES  22 A  748  VAL ALA ASP HIS LEU GLN PHE LEU HIS ALA GLU CYS HIS          
SEQRES  23 A  748  ASN ILE ILE ARG GLN GLU LYS LYS ASN ASP MET ALA ASN          
SEQRES  24 A  748  MET TYR VAL LEU LEU ARG ALA VAL SER THR GLY LEU PRO          
SEQRES  25 A  748  HIS MET ILE GLN GLU LEU GLN ASN HIS ILE HIS ASP GLU          
SEQRES  26 A  748  GLY LEU ARG ALA THR SER ASN LEU THR GLN GLU ASN MET          
SEQRES  27 A  748  PRO THR LEU PHE VAL GLU SER VAL LEU GLU VAL HIS GLY          
SEQRES  28 A  748  LYS PHE VAL GLN LEU ILE ASN THR VAL LEU ASN GLY ASP          
SEQRES  29 A  748  GLN HIS PHE MET SER ALA LEU ASP LYS ALA LEU THR SER          
SEQRES  30 A  748  VAL VAL ASN TYR ARG GLU PRO LYS SER VAL CYS LYS ALA          
SEQRES  31 A  748  PRO GLU LEU LEU ALA LYS TYR CYS ASP ASN LEU LEU LYS          
SEQRES  32 A  748  LYS SER ALA LYS GLY MET THR GLU ASN GLU VAL GLU ASP          
SEQRES  33 A  748  ARG LEU THR SER PHE ILE THR VAL PHE LYS TYR ILE ASP          
SEQRES  34 A  748  ASP LYS ASP VAL PHE GLN LYS PHE TYR ALA ARG MET LEU          
SEQRES  35 A  748  ALA LYS ARG LEU ILE HIS GLY LEU SER MET SER MET ASP          
SEQRES  36 A  748  SER GLU GLU ALA MET ILE ASN LYS LEU LYS GLN ALA CYS          
SEQRES  37 A  748  GLY TYR GLU PHE THR SER LYS LEU HIS ARG MET TYR THR          
SEQRES  38 A  748  ASP MET SER VAL SER ALA ASP LEU ASN ASN LYS PHE ASN          
SEQRES  39 A  748  ASN PHE ILE LYS ASN GLN ASP THR VAL ILE ASP LEU GLY          
SEQRES  40 A  748  ILE SER PHE GLN ILE TYR VAL LEU GLN ALA GLY ALA TRP          
SEQRES  41 A  748  PRO LEU THR GLN ALA PRO SER SER THR PHE ALA ILE PRO          
SEQRES  42 A  748  GLN GLU LEU GLU LYS SER VAL GLN MET PHE GLU LEU PHE          
SEQRES  43 A  748  TYR SER GLN HIS PHE SER GLY ARG LYS LEU THR TRP LEU          
SEQRES  44 A  748  HIS TYR LEU CYS THR GLY GLU VAL LYS MET ASN TYR LEU          
SEQRES  45 A  748  GLY LYS PRO TYR VAL ALA MET VAL THR THR TYR GLN MET          
SEQRES  46 A  748  ALA VAL LEU LEU ALA PHE ASN ASN SER GLU THR VAL SER          
SEQRES  47 A  748  TYR LYS GLU LEU GLN ASP SER THR GLN MET ASN GLU LYS          
SEQRES  48 A  748  GLU LEU THR LYS THR ILE LYS SER LEU LEU ASP VAL LYS          
SEQRES  49 A  748  MET ILE ASN HIS ASP SER GLU LYS GLU ASP ILE ASP ALA          
SEQRES  50 A  748  GLU SER SER PHE SER LEU ASN MET ASN PHE SER SER LYS          
SEQRES  51 A  748  ARG THR LYS PHE LYS ILE THR THR SER MET GLN LYS ASP          
SEQRES  52 A  748  THR PRO GLN GLU MET GLU GLN THR ARG SER ALA VAL ASP          
SEQRES  53 A  748  GLU ASP ARG LYS MET TYR LEU GLN ALA ALA ILE VAL ARG          
SEQRES  54 A  748  ILE MET LYS ALA ARG LYS VAL LEU ARG HIS ASN ALA LEU          
SEQRES  55 A  748  ILE GLN GLU VAL ILE SER GLN SER ARG ALA ARG PHE ASN          
SEQRES  56 A  748  PRO SER ILE SER MET ILE LYS LYS CYS ILE GLU VAL LEU          
SEQRES  57 A  748  ILE ASP LYS GLN TYR ILE GLU ARG SER GLN ALA SER ALA          
SEQRES  58 A  748  ASP GLU TYR SER TYR VAL ALA                                  
SEQRES   1 V  160  MET GLU ALA GLY ARG PRO ARG PRO VAL LEU ARG SER VAL          
SEQRES   2 V  160  ASN SER ARG GLU PRO SER GLN VAL ILE PHE CYS ASN ARG          
SEQRES   3 V  160  SER PRO ARG VAL VAL LEU PRO VAL TRP LEU ASN PHE ASP          
SEQRES   4 V  160  GLY GLU PRO GLN PRO TYR PRO THR LEU PRO PRO GLY THR          
SEQRES   5 V  160  GLY ARG ARG ILE HIS SER TYR ARG GLY HIS LEU TRP LEU          
SEQRES   6 V  160  PHE ARG ASP ALA GLY THR HIS ASP GLY LEU LEU VAL ASN          
SEQRES   7 V  160  GLN THR GLU LEU PHE VAL PRO SER LEU ASN VAL ASP GLY          
SEQRES   8 V  160  GLN PRO ILE PHE ALA ASN ILE THR LEU PRO VAL TYR THR          
SEQRES   9 V  160  LEU LYS GLU ARG CYS LEU GLN VAL VAL ARG SER LEU VAL          
SEQRES  10 V  160  LYS PRO GLU ASN TYR ARG ARG LEU ASP ILE VAL ARG SER          
SEQRES  11 V  160  LEU TYR GLU ASP LEU GLU ASP HIS PRO ASN VAL GLN LYS          
SEQRES  12 V  160  ASP LEU GLU ARG LEU THR GLN GLU ARG ILE ALA HIS GLN          
SEQRES  13 V  160  ARG MET GLY ASP                                              
SEQRES   1 R  102  MET ALA ALA ALA MET ASP VAL ASP THR PRO SER GLY THR          
SEQRES   2 R  102  ASN SER GLY ALA LYS LYS LYS ARG PHE GLU VAL LYS LYS          
SEQRES   3 R  102  TRP ASN ALA VAL ALA LEU TRP ALA TRP ASP ILE VAL VAL          
SEQRES   4 R  102  ASP ASN CYS ALA ILE CYS ARG ASN HIS ILE MET ASP LEU          
SEQRES   5 R  102  CYS ILE GLU CYS GLN ALA ASN GLN ALA SER ALA THR SER          
SEQRES   6 R  102  GLU GLU CYS THR VAL ALA TRP GLY VAL CYS ASN HIS ALA          
SEQRES   7 R  102  PHE HIS PHE HIS CYS ILE SER ARG TRP LEU LYS THR ARG          
SEQRES   8 R  102  GLN VAL CYS PRO LEU ASP ASN ARG GLU TRP GLU                  
SEQRES   1 B  104  MET ASP VAL PHE LEU MET ILE ARG ARG HIS LYS THR THR          
SEQRES   2 B  104  ILE PHE THR ASP ALA LYS GLU SER SER THR VAL PHE GLU          
SEQRES   3 B  104  LEU LYS ARG ILE VAL GLU GLY ILE LEU LYS ARG PRO PRO          
SEQRES   4 B  104  ASP GLU GLN ARG LEU TYR LYS ASP ASP GLN LEU LEU ASP          
SEQRES   5 B  104  ASP GLY LYS THR LEU GLY GLU CYS GLY PHE THR SER GLN          
SEQRES   6 B  104  THR ALA ARG PRO GLN ALA PRO ALA THR VAL GLY LEU ALA          
SEQRES   7 B  104  PHE ARG ALA ASP ASP THR PHE GLU ALA LEU CYS ILE GLU          
SEQRES   8 B  104  PRO PHE SER SER PRO PRO GLU LEU PRO ASP VAL MET LYS          
SEQRES   1 C   97  MET MET TYR VAL LYS LEU ILE SER SER ASP GLY HIS GLU          
SEQRES   2 C   97  PHE ILE VAL LYS ARG GLU HIS ALA LEU THR SER GLY THR          
SEQRES   3 C   97  ILE LYS ALA MET LEU SER GLY PRO GLY GLN PHE ALA GLU          
SEQRES   4 C   97  ASN GLU THR ASN GLU VAL ASN PHE ARG GLU ILE PRO SER          
SEQRES   5 C   97  HIS VAL LEU SER LYS VAL CYS MET TYR PHE THR TYR LYS          
SEQRES   6 C   97  VAL ARG TYR THR ASN SER SER THR GLU ILE PRO GLU PHE          
SEQRES   7 C   97  PRO ILE ALA PRO GLU ILE ALA LEU GLU LEU LEU MET ALA          
SEQRES   8 C   97  ALA ASN PHE LEU ASP CYS                                      
HET     ZN  R 201       1                                                       
HET     ZN  R 202       1                                                       
HET     ZN  R 203       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   6   ZN    3(ZN 2+)                                                     
HELIX    1 AA1 ASP A   11  VAL A   25  1                                  15    
HELIX    2 AA2 MET A   26  GLU A   28  5                                   3    
HELIX    3 AA3 ALA A   33  PHE A   39  1                                   7    
HELIX    4 AA4 PHE A   39  ALA A   44  1                                   6    
HELIX    5 AA5 LEU A   53  SER A   79  1                                  27    
HELIX    6 AA6 GLN A   82  GLU A   93  1                                  12    
HELIX    7 AA7 TYR A   94  TYR A  105  1                                  12    
HELIX    8 AA8 TYR A  105  GLN A  111  1                                   7    
HELIX    9 AA9 GLU A  138  VAL A  152  1                                  15    
HELIX   10 AB1 PRO A  154  ASN A  169  1                                  16    
HELIX   11 AB2 ASN A  177  SER A  187  1                                  11    
HELIX   12 AB3 LEU A  200  PHE A  207  1                                   8    
HELIX   13 AB4 PHE A  207  GLN A  228  1                                  22    
HELIX   14 AB5 ASN A  231  LEU A  254  1                                  24    
HELIX   15 AB6 HIS A  255  SER A  257  5                                   3    
HELIX   16 AB7 SER A  258  MET A  270  1                                  13    
HELIX   17 AB8 HIS A  274  ILE A  286  1                                  13    
HELIX   18 AB9 ASP A  293  ALA A  303  1                                  11    
HELIX   19 AC1 GLY A  307  THR A  327  1                                  21    
HELIX   20 AC2 MET A  335  LEU A  358  1                                  24    
HELIX   21 AC3 GLN A  362  VAL A  376  1                                  15    
HELIX   22 AC4 LYS A  386  LYS A  400  1                                  15    
HELIX   23 AC5 GLU A  410  TYR A  424  1                                  15    
HELIX   24 AC6 ASP A  427  HIS A  445  1                                  19    
HELIX   25 AC7 SER A  450  CYS A  465  1                                  16    
HELIX   26 AC8 THR A  470  LYS A  495  1                                  26    
HELIX   27 AC9 VAL A  537  PHE A  548  1                                  12    
HELIX   28 AD1 THR A  613  ILE A  614  5                                   2    
HELIX   29 AD2 SER A  616  ASP A  619  5                                   4    
HELIX   30 AD3 PRO A  662  ARG A  669  1                                   8    
HELIX   31 AD4 SER A  670  ARG A  691  1                                  22    
HELIX   32 AD5 ARG A  695  ILE A  700  1                                   6    
HELIX   33 AD6 GLN A  701  SER A  707  1                                   7    
HELIX   34 AD7 SER A  714  ILE A  726  1                                  13    
HELIX   35 AD8 LEU V  158  ARG V  167  1                                  10    
HELIX   36 AD9 CYS R   53  GLN R   60  1                                   8    
HELIX   37 AE1 PHE R   81  ARG R   91  1                                  11    
HELIX   38 AE2 THR B   23  LYS B   36  1                                  14    
HELIX   39 AE3 PRO B   38  ASP B   40  5                                   3    
HELIX   40 AE4 LYS C   32  LEU C   37  1                                   6    
HELIX   41 AE5 SER C   39  SER C   47  1                                   9    
HELIX   42 AE6 PRO C   66  TYR C   83  1                                  18    
HELIX   43 AE7 ILE C   99  LEU C  110  1                                  12    
SHEET    1 AA1 3 PHE A 507  LEU A 512  0                                        
SHEET    2 AA1 3 TRP R  27  ALA R  34  1  O  ALA R  31   N  TYR A 510           
SHEET    3 AA1 3 LYS A 552  LEU A 556 -1  N  LYS A 552   O  ALA R  34           
SHEET    1 AA2 2 ILE A 731  GLU A 732  0                                        
SHEET    2 AA2 2 SER A 742  TYR A 743 -1  O  SER A 742   N  GLU A 732           
SHEET    1 AA3 2 VAL R  70  ALA R  71  0                                        
SHEET    2 AA3 2 PHE R  79  HIS R  80 -1  O  PHE R  79   N  ALA R  71           
SHEET    1 AA4 2 GLN B  42  ARG B  43  0                                        
SHEET    2 AA4 2 ALA B  78  PHE B  79 -1  O  ALA B  78   N  ARG B  43           
SHEET    1 AA5 3 ILE C  30  VAL C  31  0                                        
SHEET    2 AA5 3 VAL C  19  LEU C  21 -1  N  VAL C  19   O  VAL C  31           
SHEET    3 AA5 3 GLU C  59  VAL C  60  1  O  VAL C  60   N  LYS C  20           
LINK         SG  CYS R  45                ZN    ZN R 201     1555   1555  2.68  
LINK         SG  CYS R  53                ZN    ZN R 202     1555   1555  2.45  
LINK         SG  CYS R  56                ZN    ZN R 202     1555   1555  2.36  
LINK         SG  CYS R  75                ZN    ZN R 203     1555   1555  2.52  
LINK         NE2 HIS R  82                ZN    ZN R 202     1555   1555  2.32  
LINK         SG  CYS R  83                ZN    ZN R 201     1555   1555  2.88  
CISPEP   1 TYR A   49    PRO A   50          0       -25.53                     
CISPEP   2 GLU A  174    ASP A  175          0         0.44                     
CISPEP   3 GLY A  360    ASP A  361          0        -5.10                     
CISPEP   4 SER A  383    VAL A  384          0        -1.48                     
CISPEP   5 VAL A  384    CYS A  385          0         3.51                     
CISPEP   6 VAL R   38    VAL R   39          0        10.13                     
SITE     1 AC1  4 CYS R  42  CYS R  45  HIS R  80  CYS R  83                    
SITE     1 AC2  4 CYS R  53  CYS R  56  CYS R  68  HIS R  82                    
SITE     1 AC3  4 CYS R  75  HIS R  77  CYS R  94  ASP R  97                    
CRYST1   86.038  190.962  238.885  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011623  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005237  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004186        0.00000                         
ATOM      1  N   MET A   1     -30.183  17.109 -80.688  1.00256.96           N  
ANISOU    1  N   MET A   1    32803  34676  30153   3333  -2020  -2136       N  
ATOM      2  CA  MET A   1     -30.425  18.417 -81.287  1.00258.45           C  
ANISOU    2  CA  MET A   1    33206  34796  30198   3603  -1429  -2328       C  
ATOM      3  C   MET A   1     -29.658  19.511 -80.553  1.00260.86           C  
ANISOU    3  C   MET A   1    33214  35440  30461   3317   -661  -2439       C  
ATOM      4  O   MET A   1     -28.550  19.286 -80.070  1.00261.63           O  
ANISOU    4  O   MET A   1    33137  35678  30594   3153   -504  -2438       O  
ATOM      5  CB  MET A   1     -31.921  18.736 -81.291  1.00256.17           C  
ANISOU    5  CB  MET A   1    32869  34526  29939   3528  -1635  -2284       C  
ATOM      6  CG  MET A   1     -32.741  17.840 -82.201  1.00253.14           C  
ANISOU    6  CG  MET A   1    32837  33758  29587   3889  -2342  -2222       C  
ATOM      7  SD  MET A   1     -32.227  17.972 -83.924  1.00254.38           S  
ANISOU    7  SD  MET A   1    33742  33375  29535   4726  -2219  -2420       S  
ATOM      8  CE  MET A   1     -32.752  19.642 -84.305  1.00254.53           C  
ANISOU    8  CE  MET A   1    33888  33429  29394   4913  -1505  -2614       C  
ATOM      9  N   SER A   2     -30.253  20.697 -80.479  1.00259.13           N  
ANISOU    9  N   SER A   2    32941  35346  30169   3261   -191  -2538       N  
ATOM     10  CA  SER A   2     -29.641  21.811 -79.774  1.00260.78           C  
ANISOU   10  CA  SER A   2    32871  35875  30338   2975    544  -2651       C  
ATOM     11  C   SER A   2     -29.770  21.621 -78.264  1.00261.54           C  
ANISOU   11  C   SER A   2    32384  36430  30561   2288    437  -2500       C  
ATOM     12  O   SER A   2     -30.433  20.702 -77.777  1.00259.32           O  
ANISOU   12  O   SER A   2    31916  36217  30398   2037   -173  -2304       O  
ATOM     13  CB  SER A   2     -30.279  23.131 -80.203  1.00259.61           C  
ANISOU   13  CB  SER A   2    32880  35698  30063   3152   1075  -2801       C  
ATOM     14  OG  SER A   2     -29.722  24.223 -79.491  1.00260.50           O  
ANISOU   14  OG  SER A   2    32717  36119  30141   2854   1787  -2913       O  
ATOM     15  N   LEU A   3     -29.121  22.514 -77.516  1.00260.35           N  
ANISOU   15  N   LEU A   3    31951  36587  30384   1985   1047  -2596       N  
ATOM     16  CA  LEU A   3     -29.224  22.478 -76.062  1.00260.17           C  
ANISOU   16  CA  LEU A   3    31395  37008  30449   1341   1017  -2473       C  
ATOM     17  C   LEU A   3     -30.573  22.964 -75.550  1.00258.85           C  
ANISOU   17  C   LEU A   3    31033  37023  30294   1062    996  -2390       C  
ATOM     18  O   LEU A   3     -30.774  22.986 -74.330  1.00257.72           O  
ANISOU   18  O   LEU A   3    30464  37244  30212    529    989  -2279       O  
ATOM     19  CB  LEU A   3     -28.089  23.294 -75.433  1.00261.47           C  
ANISOU   19  CB  LEU A   3    31330  37436  30582   1112   1667  -2616       C  
ATOM     20  CG  LEU A   3     -27.906  24.766 -75.811  1.00260.79           C  
ANISOU   20  CG  LEU A   3    31372  37342  30374   1275   2463  -2846       C  
ATOM     21  CD1 LEU A   3     -28.807  25.668 -75.004  1.00259.93           C  
ANISOU   21  CD1 LEU A   3    30986  37539  30235    888   2742  -2830       C  
ATOM     22  CD2 LEU A   3     -26.461  25.174 -75.609  1.00258.56           C  
ANISOU   22  CD2 LEU A   3    30994  37151  30097   1234   2965  -3000       C  
ATOM     23  N   LYS A   4     -31.486  23.361 -76.434  1.00265.79           N  
ANISOU   23  N   LYS A   4    32214  37661  31115   1412    993  -2441       N  
ATOM     24  CA  LYS A   4     -32.831  23.698 -76.004  1.00264.31           C  
ANISOU   24  CA  LYS A   4    31842  37619  30967   1173    899  -2344       C  
ATOM     25  C   LYS A   4     -33.503  22.464 -75.406  1.00261.63           C  
ANISOU   25  C   LYS A   4    31266  37342  30799    873    154  -2092       C  
ATOM     26  O   LYS A   4     -33.245  21.336 -75.837  1.00261.16           O  
ANISOU   26  O   LYS A   4    31366  37058  30803   1060   -384  -2014       O  
ATOM     27  CB  LYS A   4     -33.655  24.238 -77.173  1.00264.17           C  
ANISOU   27  CB  LYS A   4    32222  37288  30861   1662    963  -2447       C  
ATOM     28  CG  LYS A   4     -33.214  25.610 -77.658  1.00265.34           C  
ANISOU   28  CG  LYS A   4    32576  37403  30836   1913   1757  -2683       C  
ATOM     29  CD  LYS A   4     -34.052  26.079 -78.836  1.00264.25           C  
ANISOU   29  CD  LYS A   4    32862  36941  30600   2426   1777  -2776       C  
ATOM     30  CE  LYS A   4     -35.466  26.435 -78.400  1.00263.22           C  
ANISOU   30  CE  LYS A   4    32515  36967  30528   2189   1661  -2676       C  
ATOM     31  NZ  LYS A   4     -35.494  27.643 -77.529  1.00263.75           N  
ANISOU   31  NZ  LYS A   4    32283  37391  30541   1818   2332  -2734       N  
ATOM     32  N   PRO A   5     -34.363  22.646 -74.404  1.00264.82           N  
ANISOU   32  N   PRO A   5    31295  38042  31283    408    121  -1957       N  
ATOM     33  CA  PRO A   5     -34.927  21.488 -73.700  1.00262.33           C  
ANISOU   33  CA  PRO A   5    30718  37812  31144     72   -532  -1708       C  
ATOM     34  C   PRO A   5     -35.842  20.657 -74.584  1.00260.91           C  
ANISOU   34  C   PRO A   5    30787  37280  31067    391  -1176  -1623       C  
ATOM     35  O   PRO A   5     -36.930  21.102 -74.962  1.00260.57           O  
ANISOU   35  O   PRO A   5    30810  37149  31046    508  -1193  -1630       O  
ATOM     36  CB  PRO A   5     -35.701  22.129 -72.543  1.00260.80           C  
ANISOU   36  CB  PRO A   5    30114  37989  30989   -440   -287  -1612       C  
ATOM     37  CG  PRO A   5     -35.113  23.491 -72.385  1.00262.25           C  
ANISOU   37  CG  PRO A   5    30282  38353  31008   -465    509  -1813       C  
ATOM     38  CD  PRO A   5     -34.766  23.914 -73.776  1.00264.44           C  
ANISOU   38  CD  PRO A   5    31029  38279  31168    139    717  -2020       C  
ATOM     39  N   ARG A   6     -35.406  19.446 -74.915  1.00260.78           N  
ANISOU   39  N   ARG A   6    30908  37059  31118    534  -1717  -1545       N  
ATOM     40  CA  ARG A   6     -36.162  18.538 -75.762  1.00258.24           C  
ANISOU   40  CA  ARG A   6    30838  36381  30899    840  -2380  -1469       C  
ATOM     41  C   ARG A   6     -36.552  17.303 -74.963  1.00254.71           C  
ANISOU   41  C   ARG A   6    30100  36022  30655    455  -3008  -1217       C  
ATOM     42  O   ARG A   6     -35.734  16.748 -74.221  1.00254.95           O  
ANISOU   42  O   ARG A   6    29937  36229  30703    183  -3063  -1132       O  
ATOM     43  CB  ARG A   6     -35.352  18.127 -76.997  1.00259.19           C  
ANISOU   43  CB  ARG A   6    31449  36115  30917   1411  -2503  -1601       C  
ATOM     44  CG  ARG A   6     -34.926  19.289 -77.882  1.00261.38           C  
ANISOU   44  CG  ARG A   6    32066  36254  30991   1843  -1884  -1849       C  
ATOM     45  CD  ARG A   6     -36.117  19.929 -78.578  1.00259.90           C  
ANISOU   45  CD  ARG A   6    32069  35903  30779   2104  -1871  -1914       C  
ATOM     46  NE  ARG A   6     -35.715  21.046 -79.428  1.00260.75           N  
ANISOU   46  NE  ARG A   6    32525  35869  30680   2530  -1262  -2148       N  
ATOM     47  CZ  ARG A   6     -35.389  20.930 -80.711  1.00259.05           C  
ANISOU   47  CZ  ARG A   6    32830  35252  30345   3128  -1324  -2279       C  
ATOM     48  NH1 ARG A   6     -35.416  19.741 -81.299  1.00256.58           N  
ANISOU   48  NH1 ARG A   6    32752  34641  30097   3369  -1983  -2204       N  
ATOM     49  NH2 ARG A   6     -35.035  22.001 -81.407  1.00259.48           N  
ANISOU   49  NH2 ARG A   6    33187  35193  30211   3492   -719  -2484       N  
ATOM     50  N   VAL A   7     -37.805  16.878 -75.113  1.00249.62           N  
ANISOU   50  N   VAL A   7    29421  35252  30172    436  -3477  -1097       N  
ATOM     51  CA  VAL A   7     -38.290  15.655 -74.479  1.00250.76           C  
ANISOU   51  CA  VAL A   7    29324  35419  30533    112  -4110   -854       C  
ATOM     52  C   VAL A   7     -37.709  14.485 -75.269  1.00251.81           C  
ANISOU   52  C   VAL A   7    29786  35211  30680    453  -4640   -847       C  
ATOM     53  O   VAL A   7     -38.170  14.167 -76.366  1.00252.94           O  
ANISOU   53  O   VAL A   7    30276  34986  30844    879  -4998   -905       O  
ATOM     54  CB  VAL A   7     -39.818  15.602 -74.426  1.00251.83           C  
ANISOU   54  CB  VAL A   7    29310  35509  30865     -9  -4424   -738       C  
ATOM     55  CG1 VAL A   7     -40.283  14.282 -73.829  1.00253.21           C  
ANISOU   55  CG1 VAL A   7    29256  35670  31281   -324  -5082   -488       C  
ATOM     56  CG2 VAL A   7     -40.361  16.779 -73.627  1.00250.80           C  
ANISOU   56  CG2 VAL A   7    28861  35719  30713   -342  -3867   -741       C  
ATOM     57  N   VAL A   8     -36.689  13.840 -74.708  1.00246.95           N  
ANISOU   57  N   VAL A   8    29069  34715  30047    275  -4698   -777       N  
ATOM     58  CA  VAL A   8     -35.945  12.786 -75.389  1.00246.53           C  
ANISOU   58  CA  VAL A   8    29323  34366  29981    592  -5119   -775       C  
ATOM     59  C   VAL A   8     -36.444  11.437 -74.889  1.00247.85           C  
ANISOU   59  C   VAL A   8    29316  34493  30363    323  -5816   -532       C  
ATOM     60  O   VAL A   8     -36.977  11.320 -73.778  1.00247.86           O  
ANISOU   60  O   VAL A   8    28909  34772  30493   -176  -5865   -359       O  
ATOM     61  CB  VAL A   8     -34.426  12.965 -75.159  1.00249.39           C  
ANISOU   61  CB  VAL A   8    29699  34869  30188    608  -4711   -867       C  
ATOM     62  CG1 VAL A   8     -33.612  11.887 -75.870  1.00248.30           C  
ANISOU   62  CG1 VAL A   8    29885  34422  30035    952  -5117   -862       C  
ATOM     63  CG2 VAL A   8     -33.980  14.352 -75.605  1.00252.89           C  
ANISOU   63  CG2 VAL A   8    30289  35355  30443    843  -3984  -1106       C  
ATOM     64  N   ASP A   9     -36.287  10.410 -75.724  1.00249.92           N  
ANISOU   64  N   ASP A   9    29907  34391  30661    663  -6353   -516       N  
ATOM     65  CA  ASP A   9     -36.696   9.058 -75.369  1.00247.87           C  
ANISOU   65  CA  ASP A   9    29535  34041  30605    456  -7037   -295       C  
ATOM     66  C   ASP A   9     -35.991   8.589 -74.098  1.00247.23           C  
ANISOU   66  C   ASP A   9    29098  34292  30548    -13  -6990   -135       C  
ATOM     67  O   ASP A   9     -34.985   9.155 -73.663  1.00248.75           O  
ANISOU   67  O   ASP A   9    29199  34727  30588    -96  -6496   -214       O  
ATOM     68  CB  ASP A   9     -36.392   8.091 -76.515  1.00247.80           C  
ANISOU   68  CB  ASP A   9    29985  33584  30585    939  -7549   -334       C  
ATOM     69  CG  ASP A   9     -37.253   8.344 -77.737  1.00248.19           C  
ANISOU   69  CG  ASP A   9    30390  33273  30637   1386  -7745   -462       C  
ATOM     70  OD1 ASP A   9     -38.395   8.824 -77.575  1.00248.60           O  
ANISOU   70  OD1 ASP A   9    30260  33390  30805   1233  -7747   -440       O  
ATOM     71  OD2 ASP A   9     -36.787   8.061 -78.861  1.00248.49           O  
ANISOU   71  OD2 ASP A   9    30898  32958  30561   1900  -7898   -585       O  
ATOM     72  N   PHE A  10     -36.533   7.525 -73.505  1.00240.94           N  
ANISOU   72  N   PHE A  10    28103  33494  29951   -316  -7521     92       N  
ATOM     73  CA  PHE A  10     -36.025   7.000 -72.245  1.00240.79           C  
ANISOU   73  CA  PHE A  10    27744  33780  29966   -778  -7537    272       C  
ATOM     74  C   PHE A  10     -35.162   5.755 -72.412  1.00241.68           C  
ANISOU   74  C   PHE A  10    28030  33719  30078   -649  -7967    350       C  
ATOM     75  O   PHE A  10     -34.524   5.332 -71.442  1.00241.53           O  
ANISOU   75  O   PHE A  10    27776  33945  30049   -969  -7951    475       O  
ATOM     76  CB  PHE A  10     -37.190   6.697 -71.291  1.00241.63           C  
ANISOU   76  CB  PHE A  10    27473  34043  30293  -1259  -7768    495       C  
ATOM     77  CG  PHE A  10     -38.117   5.618 -71.778  1.00243.65           C  
ANISOU   77  CG  PHE A  10    27848  33954  30773  -1162  -8413    612       C  
ATOM     78  CD1 PHE A  10     -39.177   5.923 -72.616  1.00244.38           C  
ANISOU   78  CD1 PHE A  10    28079  33805  30970   -932  -8580    539       C  
ATOM     79  CD2 PHE A  10     -37.947   4.304 -71.374  1.00244.94           C  
ANISOU   79  CD2 PHE A  10    28045  34011  31010  -1241  -8532    732       C  
ATOM     80  CE1 PHE A  10     -40.036   4.935 -73.060  1.00246.43           C  
ANISOU   80  CE1 PHE A  10    28494  33733  31404   -812  -8850    596       C  
ATOM     81  CE2 PHE A  10     -38.804   3.313 -71.812  1.00246.92           C  
ANISOU   81  CE2 PHE A  10    28457  33928  31435  -1125  -8806    793       C  
ATOM     82  CZ  PHE A  10     -39.849   3.628 -72.656  1.00247.70           C  
ANISOU   82  CZ  PHE A  10    28678  33797  31640   -925  -8962    728       C  
ATOM     83  N   ASP A  11     -35.125   5.160 -73.604  1.00241.95           N  
ANISOU   83  N   ASP A  11    28478  33335  30115   -182  -8351    281       N  
ATOM     84  CA  ASP A  11     -34.260   4.020 -73.878  1.00242.12           C  
ANISOU   84  CA  ASP A  11    28714  33162  30118     -2  -8734    340       C  
ATOM     85  C   ASP A  11     -33.152   4.319 -74.874  1.00243.80           C  
ANISOU   85  C   ASP A  11    29322  33185  30127    508  -8480    131       C  
ATOM     86  O   ASP A  11     -32.114   3.655 -74.837  1.00244.37           O  
ANISOU   86  O   ASP A  11    29483  33225  30141    590  -8576    163       O  
ATOM     87  CB  ASP A  11     -35.080   2.832 -74.399  1.00243.98           C  
ANISOU   87  CB  ASP A  11    29159  33031  30510    112  -9026    440       C  
ATOM     88  CG  ASP A  11     -35.932   2.193 -73.322  1.00244.66           C  
ANISOU   88  CG  ASP A  11    28907  33267  30783   -356  -9021    636       C  
ATOM     89  OD1 ASP A  11     -35.545   2.260 -72.136  1.00244.23           O  
ANISOU   89  OD1 ASP A  11    28524  33560  30710   -733  -8823    724       O  
ATOM     90  OD2 ASP A  11     -36.984   1.611 -73.663  1.00246.08           O  
ANISOU   90  OD2 ASP A  11    29170  33198  31132   -330  -9213    689       O  
ATOM     91  N   GLU A  12     -33.352   5.295 -75.765  1.00239.72           N  
ANISOU   91  N   GLU A  12    29047  32532  29502    859  -8152    -76       N  
ATOM     92  CA  GLU A  12     -32.324   5.655 -76.737  1.00241.09           C  
ANISOU   92  CA  GLU A  12    29611  32510  29481   1360  -7855   -277       C  
ATOM     93  C   GLU A  12     -31.017   6.016 -76.044  1.00242.84           C  
ANISOU   93  C   GLU A  12    29636  33042  29592   1197  -7366   -313       C  
ATOM     94  O   GLU A  12     -29.968   5.418 -76.309  1.00243.56           O  
ANISOU   94  O   GLU A  12    29901  33017  29625   1402  -7444   -320       O  
ATOM     95  CB  GLU A  12     -32.812   6.817 -77.605  1.00242.57           C  
ANISOU   95  CB  GLU A  12    30028  32571  29566   1690  -7486   -486       C  
ATOM     96  CG  GLU A  12     -31.823   7.246 -78.675  1.00245.08           C  
ANISOU   96  CG  GLU A  12    30783  32654  29683   2238  -7145   -697       C  
ATOM     97  CD  GLU A  12     -32.342   8.388 -79.524  1.00246.90           C  
ANISOU   97  CD  GLU A  12    31258  32752  29802   2572  -6780   -896       C  
ATOM     98  OE1 GLU A  12     -33.471   8.857 -79.266  1.00246.94           O  
ANISOU   98  OE1 GLU A  12    31077  32860  29890   2372  -6797   -872       O  
ATOM     99  OE2 GLU A  12     -31.621   8.821 -80.448  1.00248.65           O  
ANISOU   99  OE2 GLU A  12    31862  32760  29855   3042  -6464  -1074       O  
ATOM    100  N   THR A  13     -31.062   7.001 -75.146  1.00237.37           N  
ANISOU  100  N   THR A  13    28575  32743  28873    828  -6859   -339       N  
ATOM    101  CA  THR A  13     -29.871   7.380 -74.398  1.00239.64           C  
ANISOU  101  CA  THR A  13    28634  33347  29071    630  -6407   -379       C  
ATOM    102  C   THR A  13     -29.498   6.346 -73.345  1.00237.51           C  
ANISOU  102  C   THR A  13    28079  33274  28890    245  -6754   -164       C  
ATOM    103  O   THR A  13     -28.338   6.302 -72.923  1.00238.76           O  
ANISOU  103  O   THR A  13    28135  33600  28982    184  -6543   -187       O  
ATOM    104  CB  THR A  13     -30.078   8.742 -73.733  1.00241.24           C  
ANISOU  104  CB  THR A  13    28537  33906  29215    340  -5778   -474       C  
ATOM    105  OG1 THR A  13     -31.168   8.662 -72.805  1.00238.33           O  
ANISOU  105  OG1 THR A  13    27827  33754  28971   -123  -5962   -303       O  
ATOM    106  CG2 THR A  13     -30.388   9.804 -74.778  1.00242.96           C  
ANISOU  106  CG2 THR A  13    29051  33931  29331    738  -5396   -691       C  
ATOM    107  N   TRP A  14     -30.447   5.507 -72.925  1.00235.99           N  
ANISOU  107  N   TRP A  14    27762  33053  28852     -6  -7283     42       N  
ATOM    108  CA  TRP A  14     -30.187   4.583 -71.829  1.00234.79           C  
ANISOU  108  CA  TRP A  14    27323  33108  28780   -405  -7583    259       C  
ATOM    109  C   TRP A  14     -29.462   3.323 -72.285  1.00234.19           C  
ANISOU  109  C   TRP A  14    27498  32766  28716   -150  -8049    332       C  
ATOM    110  O   TRP A  14     -28.772   2.689 -71.480  1.00234.35           O  
ANISOU  110  O   TRP A  14    27331  32968  28742   -384  -8162    458       O  
ATOM    111  CB  TRP A  14     -31.497   4.213 -71.132  1.00233.30           C  
ANISOU  111  CB  TRP A  14    26881  32999  28763   -799  -7919    462       C  
ATOM    112  CG  TRP A  14     -31.302   3.324 -69.947  1.00232.32           C  
ANISOU  112  CG  TRP A  14    26476  33086  28710  -1209  -8132    679       C  
ATOM    113  CD1 TRP A  14     -31.586   1.993 -69.863  1.00232.06           C  
ANISOU  113  CD1 TRP A  14    26565  32821  28785  -1163  -8338    783       C  
ATOM    114  CD2 TRP A  14     -30.749   3.698 -68.680  1.00232.17           C  
ANISOU  114  CD2 TRP A  14    26090  33499  28624  -1628  -7812    732       C  
ATOM    115  NE1 TRP A  14     -31.260   1.518 -68.616  1.00232.00           N  
ANISOU  115  NE1 TRP A  14    26314  33040  28795  -1497  -8207    887       N  
ATOM    116  CE2 TRP A  14     -30.742   2.544 -67.871  1.00231.03           C  
ANISOU  116  CE2 TRP A  14    25906  33304  28571  -1767  -7885    847       C  
ATOM    117  CE3 TRP A  14     -30.266   4.897 -68.149  1.00232.72           C  
ANISOU  117  CE3 TRP A  14    25946  33915  28560  -1800  -7216    605       C  
ATOM    118  CZ2 TRP A  14     -30.271   2.555 -66.561  1.00230.40           C  
ANISOU  118  CZ2 TRP A  14    25555  33521  28466  -2119  -7641    906       C  
ATOM    119  CZ3 TRP A  14     -29.799   4.906 -66.848  1.00231.45           C  
ANISOU  119  CZ3 TRP A  14    25447  34137  28358  -2226  -7067    703       C  
ATOM    120  CH2 TRP A  14     -29.804   3.743 -66.069  1.00230.34           C  
ANISOU  120  CH2 TRP A  14    25292  33896  28329  -2351  -7273    841       C  
ATOM    121  N   ASN A  15     -29.600   2.939 -73.555  1.00230.61           N  
ANISOU  121  N   ASN A  15    27479  31883  28261    333  -8326    258       N  
ATOM    122  CA  ASN A  15     -28.868   1.777 -74.049  1.00230.60           C  
ANISOU  122  CA  ASN A  15    27751  31610  28256    609  -8740    317       C  
ATOM    123  C   ASN A  15     -27.387   2.095 -74.211  1.00232.55           C  
ANISOU  123  C   ASN A  15    28077  31923  28357    826  -8327    183       C  
ATOM    124  O   ASN A  15     -26.528   1.455 -73.591  1.00232.79           O  
ANISOU  124  O   ASN A  15    27967  32093  28388    680  -8422    284       O  
ATOM    125  CB  ASN A  15     -29.470   1.295 -75.370  1.00230.07           C  
ANISOU  125  CB  ASN A  15    28147  31051  28219   1055  -9009    271       C  
ATOM    126  CG  ASN A  15     -30.811   0.615 -75.184  1.00230.10           C  
ANISOU  126  CG  ASN A  15    28075  30948  28404    808  -9148    425       C  
ATOM    127  OD1 ASN A  15     -31.002  -0.158 -74.245  1.00230.75           O  
ANISOU  127  OD1 ASN A  15    27904  31184  28586    436  -9164    599       O  
ATOM    128  ND2 ASN A  15     -31.749   0.896 -76.081  1.00230.97           N  
ANISOU  128  ND2 ASN A  15    28419  30782  28555   1048  -9248    339       N  
ATOM    129  N   LYS A  16     -27.068   3.091 -75.041  1.00223.69           N  
ANISOU  129  N   LYS A  16    27178  30698  27116   1180  -7857    -44       N  
ATOM    130  CA  LYS A  16     -25.673   3.473 -75.231  1.00226.54           C  
ANISOU  130  CA  LYS A  16    27603  31108  27363   1392  -7416   -183       C  
ATOM    131  C   LYS A  16     -25.078   4.030 -73.943  1.00227.53           C  
ANISOU  131  C   LYS A  16    27249  31722  27480    927  -7011   -171       C  
ATOM    132  O   LYS A  16     -23.900   3.800 -73.644  1.00228.64           O  
ANISOU  132  O   LYS A  16    27307  31973  27593    930  -6889   -179       O  
ATOM    133  CB  LYS A  16     -25.556   4.493 -76.364  1.00229.40           C  
ANISOU  133  CB  LYS A  16    28301  31253  27608   1851  -6961   -427       C  
ATOM    134  CG  LYS A  16     -24.125   4.864 -76.706  1.00232.64           C  
ANISOU  134  CG  LYS A  16    28819  31651  27924   2125  -6499   -576       C  
ATOM    135  CD  LYS A  16     -23.411   3.688 -77.353  1.00231.45           C  
ANISOU  135  CD  LYS A  16    28991  31173  27774   2482  -6900   -511       C  
ATOM    136  CE  LYS A  16     -22.006   4.059 -77.786  1.00234.67           C  
ANISOU  136  CE  LYS A  16    29525  31531  28109   2794  -6428   -661       C  
ATOM    137  NZ  LYS A  16     -21.135   4.318 -76.609  1.00237.04           N  
ANISOU  137  NZ  LYS A  16    29349  32267  28449   2384  -6124   -642       N  
ATOM    138  N   LEU A  17     -25.881   4.762 -73.165  1.00226.83           N  
ANISOU  138  N   LEU A  17    26842  31927  27415    530  -6806   -153       N  
ATOM    139  CA  LEU A  17     -25.406   5.276 -71.885  1.00226.86           C  
ANISOU  139  CA  LEU A  17    26398  32396  27402     67  -6455   -136       C  
ATOM    140  C   LEU A  17     -25.107   4.140 -70.916  1.00225.73           C  
ANISOU  140  C   LEU A  17    26029  32412  27327   -253  -6888     89       C  
ATOM    141  O   LEU A  17     -24.090   4.164 -70.215  1.00226.25           O  
ANISOU  141  O   LEU A  17    25877  32733  27356   -419  -6698     81       O  
ATOM    142  CB  LEU A  17     -26.437   6.242 -71.297  1.00225.87           C  
ANISOU  142  CB  LEU A  17    26018  32519  27285   -274  -6178   -148       C  
ATOM    143  CG  LEU A  17     -26.084   7.081 -70.065  1.00225.52           C  
ANISOU  143  CG  LEU A  17    25545  32948  27193   -729  -5708   -176       C  
ATOM    144  CD1 LEU A  17     -26.845   8.395 -70.102  1.00225.58           C  
ANISOU  144  CD1 LEU A  17    25484  33068  27157   -806  -5235   -305       C  
ATOM    145  CD2 LEU A  17     -26.393   6.339 -68.772  1.00223.54           C  
ANISOU  145  CD2 LEU A  17    24956  32965  27014  -1227  -6050     66       C  
ATOM    146  N   LEU A  18     -25.983   3.133 -70.865  1.00226.65           N  
ANISOU  146  N   LEU A  18    26196  32372  27549   -339  -7475    288       N  
ATOM    147  CA  LEU A  18     -25.768   2.002 -69.967  1.00225.39           C  
ANISOU  147  CA  LEU A  18    25849  32335  27453   -632  -7903    515       C  
ATOM    148  C   LEU A  18     -24.532   1.207 -70.371  1.00226.54           C  
ANISOU  148  C   LEU A  18    26189  32322  27564   -332  -8068    510       C  
ATOM    149  O   LEU A  18     -23.685   0.886 -69.528  1.00227.33           O  
ANISOU  149  O   LEU A  18    26061  32669  27643   -545  -8052    579       O  
ATOM    150  CB  LEU A  18     -27.011   1.108 -69.945  1.00223.33           C  
ANISOU  150  CB  LEU A  18    25651  31880  27326   -726  -8338    687       C  
ATOM    151  CG  LEU A  18     -27.068  -0.042 -68.932  1.00221.13           C  
ANISOU  151  CG  LEU A  18    25243  31663  27114   -973  -8365    838       C  
ATOM    152  CD1 LEU A  18     -28.503  -0.295 -68.510  1.00221.72           C  
ANISOU  152  CD1 LEU A  18    25241  31677  27325  -1195  -8387    927       C  
ATOM    153  CD2 LEU A  18     -26.466  -1.320 -69.502  1.00222.50           C  
ANISOU  153  CD2 LEU A  18    25710  31540  27291   -668  -8607    894       C  
ATOM    154  N   THR A  19     -24.415   0.872 -71.660  1.00225.49           N  
ANISOU  154  N   THR A  19    26486  31770  27420    173  -8233    430       N  
ATOM    155  CA  THR A  19     -23.225   0.166 -72.125  1.00226.98           C  
ANISOU  155  CA  THR A  19    26885  31784  27573    496  -8349    418       C  
ATOM    156  C   THR A  19     -21.965   0.992 -71.900  1.00230.19           C  
ANISOU  156  C   THR A  19    27138  32427  27897    525  -7768    251       C  
ATOM    157  O   THR A  19     -20.880   0.430 -71.711  1.00231.59           O  
ANISOU  157  O   THR A  19    27285  32638  28068    589  -7827    285       O  
ATOM    158  CB  THR A  19     -23.367  -0.199 -73.604  1.00227.22           C  
ANISOU  158  CB  THR A  19    27436  31309  27587   1058  -8569    342       C  
ATOM    159  OG1 THR A  19     -23.541   0.992 -74.381  1.00229.05           O  
ANISOU  159  OG1 THR A  19    27832  31454  27744   1317  -8093    118       O  
ATOM    160  CG2 THR A  19     -24.560  -1.122 -73.813  1.00224.31           C  
ANISOU  160  CG2 THR A  19    27212  30694  27321   1000  -8972    504       C  
ATOM    161  N   THR A  20     -22.088   2.322 -71.908  1.00224.00           N  
ANISOU  161  N   THR A  20    26246  31804  27060    476  -7204     70       N  
ATOM    162  CA  THR A  20     -20.944   3.164 -71.578  1.00227.79           C  
ANISOU  162  CA  THR A  20    26529  32536  27486    441  -6635    -92       C  
ATOM    163  C   THR A  20     -20.607   3.074 -70.093  1.00226.43           C  
ANISOU  163  C   THR A  20    25888  32814  27329    -82  -6628     17       C  
ATOM    164  O   THR A  20     -19.429   3.081 -69.719  1.00228.77           O  
ANISOU  164  O   THR A  20    26031  33275  27616   -102  -6446    -33       O  
ATOM    165  CB  THR A  20     -21.220   4.612 -71.986  1.00230.23           C  
ANISOU  165  CB  THR A  20    26861  32882  27734    524  -6034   -314       C  
ATOM    166  OG1 THR A  20     -21.492   4.669 -73.392  1.00230.26           O  
ANISOU  166  OG1 THR A  20    27332  32450  27704   1044  -6050   -417       O  
ATOM    167  CG2 THR A  20     -20.016   5.492 -71.679  1.00233.80           C  
ANISOU  167  CG2 THR A  20    27110  33573  28150    491  -5436   -494       C  
ATOM    168  N   ILE A  21     -21.627   2.985 -69.234  1.00225.65           N  
ANISOU  168  N   ILE A  21    25563  32914  27260   -502  -6826    168       N  
ATOM    169  CA  ILE A  21     -21.387   2.756 -67.809  1.00223.29           C  
ANISOU  169  CA  ILE A  21    24863  33014  26962   -988  -6889    301       C  
ATOM    170  C   ILE A  21     -20.632   1.449 -67.606  1.00222.20           C  
ANISOU  170  C   ILE A  21    24760  32812  26855   -932  -7347    458       C  
ATOM    171  O   ILE A  21     -19.591   1.405 -66.938  1.00223.23           O  
ANISOU  171  O   ILE A  21    24674  33184  26959  -1056  -7229    444       O  
ATOM    172  CB  ILE A  21     -22.715   2.758 -67.030  1.00220.21           C  
ANISOU  172  CB  ILE A  21    24282  32780  26608  -1404  -7065    462       C  
ATOM    173  CG1 ILE A  21     -23.420   4.108 -67.148  1.00220.77           C  
ANISOU  173  CG1 ILE A  21    24290  32948  26643  -1477  -6577    307       C  
ATOM    174  CG2 ILE A  21     -22.474   2.411 -65.568  1.00218.12           C  
ANISOU  174  CG2 ILE A  21    23649  32898  26329  -1881  -7166    620       C  
ATOM    175  CD1 ILE A  21     -22.655   5.244 -66.531  1.00222.25           C  
ANISOU  175  CD1 ILE A  21    24213  33486  26746  -1662  -5978    133       C  
ATOM    176  N   LYS A  22     -21.152   0.362 -68.183  1.00221.93           N  
ANISOU  176  N   LYS A  22    25000  32444  26880   -740  -7884    607       N  
ATOM    177  CA  LYS A  22     -20.501  -0.937 -68.048  1.00221.24           C  
ANISOU  177  CA  LYS A  22    24992  32252  26819   -650  -8283    751       C  
ATOM    178  C   LYS A  22     -19.106  -0.928 -68.662  1.00224.13           C  
ANISOU  178  C   LYS A  22    25484  32523  27154   -287  -8138    625       C  
ATOM    179  O   LYS A  22     -18.232  -1.689 -68.230  1.00224.34           O  
ANISOU  179  O   LYS A  22    25429  32624  27186   -307  -8338    718       O  
ATOM    180  CB  LYS A  22     -21.372  -2.017 -68.692  1.00220.36           C  
ANISOU  180  CB  LYS A  22    25231  31734  26763   -424  -8522    837       C  
ATOM    181  CG  LYS A  22     -20.877  -3.440 -68.503  1.00220.12           C  
ANISOU  181  CG  LYS A  22    25318  31570  26747   -333  -8687    959       C  
ATOM    182  CD  LYS A  22     -21.873  -4.439 -69.074  1.00219.43           C  
ANISOU  182  CD  LYS A  22    25528  31115  26732   -202  -8885   1061       C  
ATOM    183  CE  LYS A  22     -21.340  -5.860 -69.011  1.00220.63           C  
ANISOU  183  CE  LYS A  22    25824  31105  26899    -96  -9054   1184       C  
ATOM    184  NZ  LYS A  22     -21.198  -6.336 -67.607  1.00220.70           N  
ANISOU  184  NZ  LYS A  22    25558  31386  26910   -430  -8992   1261       N  
ATOM    185  N   ALA A  23     -18.875  -0.069 -69.659  1.00217.90           N  
ANISOU  185  N   ALA A  23    24901  31557  26335     64  -7728    403       N  
ATOM    186  CA  ALA A  23     -17.540   0.069 -70.228  1.00221.86           C  
ANISOU  186  CA  ALA A  23    25510  31965  26822    416  -7451    255       C  
ATOM    187  C   ALA A  23     -16.604   0.841 -69.306  1.00224.47           C  
ANISOU  187  C   ALA A  23    25436  32712  27140    143  -6999    146       C  
ATOM    188  O   ALA A  23     -15.395   0.581 -69.300  1.00227.44           O  
ANISOU  188  O   ALA A  23    25766  33113  27540    286  -6929    107       O  
ATOM    189  CB  ALA A  23     -17.618   0.757 -71.593  1.00224.75           C  
ANISOU  189  CB  ALA A  23    26246  31993  27157    887  -7133     56       C  
ATOM    190  N   VAL A  24     -17.133   1.788 -68.529  1.00220.53           N  
ANISOU  190  N   VAL A  24    24643  32537  26612   -243  -6693     92       N  
ATOM    191  CA  VAL A  24     -16.302   2.498 -67.563  1.00220.32           C  
ANISOU  191  CA  VAL A  24    24222  32920  26571   -540  -6303     -9       C  
ATOM    192  C   VAL A  24     -15.967   1.590 -66.386  1.00221.46           C  
ANISOU  192  C   VAL A  24    24101  33324  26721   -872  -6693    188       C  
ATOM    193  O   VAL A  24     -14.859   1.645 -65.837  1.00222.10           O  
ANISOU  193  O   VAL A  24    23952  33625  26810   -949  -6555    132       O  
ATOM    194  CB  VAL A  24     -16.998   3.795 -67.109  1.00218.88           C  
ANISOU  194  CB  VAL A  24    23835  32988  26342   -841  -5854   -128       C  
ATOM    195  CG1 VAL A  24     -16.214   4.461 -65.990  1.00218.85           C  
ANISOU  195  CG1 VAL A  24    23415  33421  26318  -1195  -5511   -219       C  
ATOM    196  CG2 VAL A  24     -17.149   4.751 -68.281  1.00217.88           C  
ANISOU  196  CG2 VAL A  24    23972  32612  26201   -480  -5414   -343       C  
ATOM    197  N   VAL A  25     -16.908   0.732 -65.988  1.00222.27           N  
ANISOU  197  N   VAL A  25    24234  33394  26824  -1066  -7189    421       N  
ATOM    198  CA  VAL A  25     -16.635  -0.241 -64.939  1.00220.34           C  
ANISOU  198  CA  VAL A  25    23793  33350  26576  -1343  -7594    630       C  
ATOM    199  C   VAL A  25     -15.630  -1.265 -65.454  1.00222.07           C  
ANISOU  199  C   VAL A  25    24194  33348  26833   -995  -7884    680       C  
ATOM    200  O   VAL A  25     -15.636  -1.626 -66.639  1.00222.94           O  
ANISOU  200  O   VAL A  25    24665  33064  26976   -568  -7995    653       O  
ATOM    201  CB  VAL A  25     -17.943  -0.908 -64.478  1.00217.41           C  
ANISOU  201  CB  VAL A  25    23569  32772  26264  -1476  -7760    744       C  
ATOM    202  CG1 VAL A  25     -17.673  -1.970 -63.421  1.00215.70           C  
ANISOU  202  CG1 VAL A  25    23336  32536  26085  -1582  -7859    826       C  
ATOM    203  CG2 VAL A  25     -18.909   0.141 -63.949  1.00215.72           C  
ANISOU  203  CG2 VAL A  25    23175  32756  26034  -1812  -7461    705       C  
ATOM    204  N   MET A  26     -14.746  -1.721 -64.563  1.00222.59           N  
ANISOU  204  N   MET A  26    24063  33608  26905  -1127  -7920    709       N  
ATOM    205  CA  MET A  26     -13.630  -2.623 -64.852  1.00224.97           C  
ANISOU  205  CA  MET A  26    24455  33788  27237   -846  -8149    753       C  
ATOM    206  C   MET A  26     -12.576  -1.987 -65.747  1.00228.47           C  
ANISOU  206  C   MET A  26    24946  34145  27718   -496  -7800    554       C  
ATOM    207  O   MET A  26     -11.692  -2.696 -66.246  1.00229.58           O  
ANISOU  207  O   MET A  26    25231  34095  27904   -173  -7954    576       O  
ATOM    208  CB  MET A  26     -14.092  -3.944 -65.479  1.00224.45           C  
ANISOU  208  CB  MET A  26    24798  33296  27185   -538  -8462    869       C  
ATOM    209  CG  MET A  26     -14.876  -4.848 -64.545  1.00221.86           C  
ANISOU  209  CG  MET A  26    24514  32935  26849   -739  -8505    962       C  
ATOM    210  SD  MET A  26     -15.415  -6.359 -65.368  1.00221.15           S  
ANISOU  210  SD  MET A  26    24850  32416  26761   -435  -8790   1127       S  
ATOM    211  CE  MET A  26     -13.848  -7.204 -65.576  1.00223.37           C  
ANISOU  211  CE  MET A  26    25174  32667  27028   -159  -8935   1175       C  
ATOM    212  N   LEU A  27     -12.642  -0.671 -65.962  1.00219.22           N  
ANISOU  212  N   LEU A  27    23691  33063  26541   -517  -7249    331       N  
ATOM    213  CA  LEU A  27     -11.693   0.053 -66.808  1.00223.96           C  
ANISOU  213  CA  LEU A  27    24365  33534  27196   -165  -6770     93       C  
ATOM    214  C   LEU A  27     -11.646  -0.512 -68.225  1.00226.40           C  
ANISOU  214  C   LEU A  27    25142  33345  27533    378  -6906     98       C  
ATOM    215  O   LEU A  27     -10.600  -0.488 -68.879  1.00230.83           O  
ANISOU  215  O   LEU A  27    25800  33749  28155    729  -6698    -13       O  
ATOM    216  CB  LEU A  27     -10.292   0.070 -66.190  1.00226.31           C  
ANISOU  216  CB  LEU A  27    24352  34084  27553   -226  -6629     22       C  
ATOM    217  CG  LEU A  27     -10.151   0.861 -64.889  1.00225.29           C  
ANISOU  217  CG  LEU A  27    23765  34441  27393   -716  -6386    -51       C  
ATOM    218  CD1 LEU A  27      -8.755   0.698 -64.306  1.00227.56           C  
ANISOU  218  CD1 LEU A  27    23763  34948  27750   -748  -6347   -106       C  
ATOM    219  CD2 LEU A  27     -10.474   2.329 -65.119  1.00227.26           C  
ANISOU  219  CD2 LEU A  27    23954  34763  27632   -780  -5785   -283       C  
ATOM    220  N   GLU A  28     -12.775  -1.027 -68.707  1.00217.68           N  
ANISOU  220  N   GLU A  28    24334  31984  26392    456  -7257    226       N  
ATOM    221  CA  GLU A  28     -12.857  -1.486 -70.084  1.00219.17           C  
ANISOU  221  CA  GLU A  28    25002  31685  26586    973  -7387    217       C  
ATOM    222  C   GLU A  28     -12.684  -0.309 -71.040  1.00222.63           C  
ANISOU  222  C   GLU A  28    25602  31967  27020   1277  -6798    -37       C  
ATOM    223  O   GLU A  28     -12.819   0.859 -70.664  1.00223.81           O  
ANISOU  223  O   GLU A  28    25518  32364  27157   1053  -6336   -188       O  
ATOM    224  CB  GLU A  28     -14.194  -2.184 -70.341  1.00214.97           C  
ANISOU  224  CB  GLU A  28    24723  30930  26025    952  -7883    389       C  
ATOM    225  CG  GLU A  28     -14.385  -3.488 -69.577  1.00211.29           C  
ANISOU  225  CG  GLU A  28    24179  30528  25573    723  -8494    655       C  
ATOM    226  CD  GLU A  28     -13.462  -4.591 -70.058  1.00212.32           C  
ANISOU  226  CD  GLU A  28    24529  30412  25730   1073  -8795    740       C  
ATOM    227  OE1 GLU A  28     -13.129  -4.607 -71.262  1.00214.01           O  
ANISOU  227  OE1 GLU A  28    25106  30262  25947   1555  -8696    641       O  
ATOM    228  OE2 GLU A  28     -13.073  -5.446 -69.234  1.00211.10           O  
ANISOU  228  OE2 GLU A  28    24205  30423  25579    872  -9024    902       O  
ATOM    229  N   TYR A  29     -12.378  -0.628 -72.294  1.00205.28           N  
ANISOU  229  N   TYR A  29    23829  29344  24826   1801  -6809    -82       N  
ATOM    230  CA  TYR A  29     -12.118   0.412 -73.279  1.00207.97           C  
ANISOU  230  CA  TYR A  29    24370  29491  25156   2148  -6243   -316       C  
ATOM    231  C   TYR A  29     -13.381   1.209 -73.579  1.00206.10           C  
ANISOU  231  C   TYR A  29    24254  29206  24848   2084  -6104   -387       C  
ATOM    232  O   TYR A  29     -14.419   0.643 -73.937  1.00203.37           O  
ANISOU  232  O   TYR A  29    24163  28647  24462   2140  -6529   -268       O  
ATOM    233  CB  TYR A  29     -11.559  -0.191 -74.565  1.00209.63           C  
ANISOU  233  CB  TYR A  29    25052  29228  25370   2745  -6318   -329       C  
ATOM    234  CG  TYR A  29     -11.340   0.839 -75.648  1.00213.58           C  
ANISOU  234  CG  TYR A  29    25817  29487  25847   3140  -5738   -558       C  
ATOM    235  CD1 TYR A  29     -10.314   1.769 -75.551  1.00218.80           C  
ANISOU  235  CD1 TYR A  29    26251  30305  26580   3157  -5121   -746       C  
ATOM    236  CD2 TYR A  29     -12.162   0.884 -76.767  1.00211.84           C  
ANISOU  236  CD2 TYR A  29    26078  28873  25538   3501  -5808   -590       C  
ATOM    237  CE1 TYR A  29     -10.115   2.718 -76.535  1.00221.86           C  
ANISOU  237  CE1 TYR A  29    26888  30461  26949   3519  -4564   -951       C  
ATOM    238  CE2 TYR A  29     -11.967   1.827 -77.759  1.00215.00           C  
ANISOU  238  CE2 TYR A  29    26747  29043  25900   3879  -5268   -796       C  
ATOM    239  CZ  TYR A  29     -10.941   2.741 -77.638  1.00219.84           C  
ANISOU  239  CZ  TYR A  29    27132  29814  26585   3887  -4635   -972       C  
ATOM    240  OH  TYR A  29     -10.743   3.682 -78.623  1.00222.13           O  
ANISOU  240  OH  TYR A  29    27698  29862  26841   4267  -4072  -1172       O  
ATOM    241  N   VAL A  30     -13.287   2.527 -73.429  1.00213.75           N  
ANISOU  241  N   VAL A  30    25032  30372  25810   1965  -5508   -583       N  
ATOM    242  CA  VAL A  30     -14.355   3.446 -73.794  1.00212.89           C  
ANISOU  242  CA  VAL A  30    25043  30214  25633   1953  -5270   -682       C  
ATOM    243  C   VAL A  30     -13.822   4.384 -74.869  1.00217.41           C  
ANISOU  243  C   VAL A  30    25870  30548  26188   2386  -4677   -917       C  
ATOM    244  O   VAL A  30     -12.641   4.746 -74.878  1.00221.27           O  
ANISOU  244  O   VAL A  30    26234  31097  26741   2485  -4281  -1038       O  
ATOM    245  CB  VAL A  30     -14.886   4.232 -72.572  1.00211.46           C  
ANISOU  245  CB  VAL A  30    24409  30494  25443   1383  -5081   -694       C  
ATOM    246  CG1 VAL A  30     -13.821   5.169 -72.025  1.00216.01           C  
ANISOU  246  CG1 VAL A  30    24639  31373  26063   1225  -4506   -871       C  
ATOM    247  CG2 VAL A  30     -16.157   4.992 -72.926  1.00209.98           C  
ANISOU  247  CG2 VAL A  30    24357  30237  25187   1362  -4947   -751       C  
ATOM    248  N   GLU A  31     -14.700   4.761 -75.793  1.00217.59           N  
ANISOU  248  N   GLU A  31    26259  30285  26130   2656  -4623   -979       N  
ATOM    249  CA  GLU A  31     -14.298   5.567 -76.935  1.00219.44           C  
ANISOU  249  CA  GLU A  31    26821  30230  26326   3127  -4097  -1186       C  
ATOM    250  C   GLU A  31     -14.098   7.022 -76.529  1.00221.73           C  
ANISOU  250  C   GLU A  31    26820  30803  26623   2910  -3401  -1386       C  
ATOM    251  O   GLU A  31     -14.717   7.518 -75.583  1.00220.56           O  
ANISOU  251  O   GLU A  31    26329  31007  26468   2443  -3359  -1371       O  
ATOM    252  CB  GLU A  31     -15.341   5.462 -78.048  1.00217.74           C  
ANISOU  252  CB  GLU A  31    27114  29612  26007   3498  -4305  -1185       C  
ATOM    253  CG  GLU A  31     -15.461   4.060 -78.628  1.00216.62           C  
ANISOU  253  CG  GLU A  31    27327  29123  25855   3787  -4957  -1016       C  
ATOM    254  CD  GLU A  31     -16.522   3.955 -79.704  1.00214.85           C  
ANISOU  254  CD  GLU A  31    27600  28502  25531   4144  -5200  -1026       C  
ATOM    255  OE1 GLU A  31     -17.244   4.948 -79.931  1.00214.37           O  
ANISOU  255  OE1 GLU A  31    27583  28459  25408   4139  -4893  -1148       O  
ATOM    256  OE2 GLU A  31     -16.639   2.874 -80.318  1.00215.37           O  
ANISOU  256  OE2 GLU A  31    28016  28236  25579   4433  -5709   -913       O  
ATOM    257  N   ARG A  32     -13.217   7.709 -77.261  1.00222.13           N  
ANISOU  257  N   ARG A  32    27022  30684  26692   3260  -2837  -1574       N  
ATOM    258  CA  ARG A  32     -12.885   9.091 -76.932  1.00221.25           C  
ANISOU  258  CA  ARG A  32    26647  30814  26605   3083  -2137  -1779       C  
ATOM    259  C   ARG A  32     -14.025  10.060 -77.223  1.00219.91           C  
ANISOU  259  C   ARG A  32    26613  30620  26322   3067  -1893  -1871       C  
ATOM    260  O   ARG A  32     -13.990  11.195 -76.737  1.00218.99           O  
ANISOU  260  O   ARG A  32    26229  30765  26213   2812  -1379  -2014       O  
ATOM    261  CB  ARG A  32     -11.634   9.535 -77.696  1.00222.15           C  
ANISOU  261  CB  ARG A  32    26903  30715  26789   3486  -1587  -1952       C  
ATOM    262  CG  ARG A  32     -10.339   8.879 -77.241  1.00223.48           C  
ANISOU  262  CG  ARG A  32    26814  30992  27105   3436  -1666  -1906       C  
ATOM    263  CD  ARG A  32      -9.156   9.419 -78.035  1.00224.45           C  
ANISOU  263  CD  ARG A  32    27070  30889  27321   3838  -1063  -2086       C  
ATOM    264  NE  ARG A  32      -7.885   8.838 -77.612  1.00225.88           N  
ANISOU  264  NE  ARG A  32    26981  31174  27667   3800  -1113  -2052       N  
ATOM    265  CZ  ARG A  32      -6.713   9.119 -78.173  1.00227.09           C  
ANISOU  265  CZ  ARG A  32    27181  31153  27949   4117   -649  -2179       C  
ATOM    266  NH1 ARG A  32      -6.648   9.975 -79.184  1.00227.03           N  
ANISOU  266  NH1 ARG A  32    27498  30850  27913   4500    -85  -2346       N  
ATOM    267  NH2 ARG A  32      -5.605   8.546 -77.724  1.00228.48           N  
ANISOU  267  NH2 ARG A  32    27079  31445  28289   4058   -742  -2136       N  
ATOM    268  N   ALA A  33     -15.027   9.647 -77.997  1.00230.68           N  
ANISOU  268  N   ALA A  33    28385  31677  27587   3332  -2252  -1796       N  
ATOM    269  CA  ALA A  33     -16.126  10.526 -78.384  1.00229.26           C  
ANISOU  269  CA  ALA A  33    28373  31436  27299   3376  -2047  -1883       C  
ATOM    270  C   ALA A  33     -17.417  10.245 -77.626  1.00225.78           C  
ANISOU  270  C   ALA A  33    27738  31211  26839   2960  -2510  -1728       C  
ATOM    271  O   ALA A  33     -18.137  11.185 -77.269  1.00225.25           O  
ANISOU  271  O   ALA A  33    27514  31339  26730   2720  -2231  -1797       O  
ATOM    272  CB  ALA A  33     -16.387  10.412 -79.890  1.00227.51           C  
ANISOU  272  CB  ALA A  33    28778  30692  26976   4013  -2069  -1939       C  
ATOM    273  N   THR A  34     -17.733   8.972 -77.379  1.00225.90           N  
ANISOU  273  N   THR A  34    27761  31181  26889   2874  -3201  -1517       N  
ATOM    274  CA  THR A  34     -18.939   8.645 -76.625  1.00224.84           C  
ANISOU  274  CA  THR A  34    27424  31241  26763   2467  -3643  -1356       C  
ATOM    275  C   THR A  34     -18.882   9.234 -75.221  1.00223.92           C  
ANISOU  275  C   THR A  34    26753  31639  26689   1871  -3404  -1349       C  
ATOM    276  O   THR A  34     -19.893   9.729 -74.704  1.00223.03           O  
ANISOU  276  O   THR A  34    26469  31719  26553   1560  -3387  -1321       O  
ATOM    277  CB  THR A  34     -19.127   7.130 -76.571  1.00225.99           C  
ANISOU  277  CB  THR A  34    27664  31244  26957   2476  -4398  -1131       C  
ATOM    278  OG1 THR A  34     -18.012   6.530 -75.901  1.00226.65           O  
ANISOU  278  OG1 THR A  34    27495  31507  27113   2319  -4471  -1061       O  
ATOM    279  CG2 THR A  34     -19.225   6.565 -77.979  1.00227.00           C  
ANISOU  279  CG2 THR A  34    28369  30849  27031   3074  -4645  -1146       C  
ATOM    280  N   TRP A  35     -17.704   9.196 -74.593  1.00225.23           N  
ANISOU  280  N   TRP A  35    26636  32026  26915   1713  -3217  -1375       N  
ATOM    281  CA  TRP A  35     -17.513   9.901 -73.330  1.00226.68           C  
ANISOU  281  CA  TRP A  35    26321  32685  27123   1190  -2912  -1412       C  
ATOM    282  C   TRP A  35     -17.819  11.385 -73.482  1.00229.09           C  
ANISOU  282  C   TRP A  35    26602  33073  27369   1168  -2263  -1616       C  
ATOM    283  O   TRP A  35     -18.370  12.011 -72.569  1.00228.96           O  
ANISOU  283  O   TRP A  35    26272  33391  27334    735  -2113  -1613       O  
ATOM    284  CB  TRP A  35     -16.084   9.700 -72.826  1.00230.21           C  
ANISOU  284  CB  TRP A  35    26516  33302  27651   1114  -2775  -1449       C  
ATOM    285  CG  TRP A  35     -15.816  10.369 -71.515  1.00231.00           C  
ANISOU  285  CG  TRP A  35    26114  33883  27772    586  -2499  -1494       C  
ATOM    286  CD1 TRP A  35     -15.173  11.556 -71.317  1.00233.92           C  
ANISOU  286  CD1 TRP A  35    26289  34432  28158    500  -1852  -1711       C  
ATOM    287  CD2 TRP A  35     -16.179   9.888 -70.215  1.00226.99           C  
ANISOU  287  CD2 TRP A  35    25251  33727  27267     77  -2863  -1320       C  
ATOM    288  NE1 TRP A  35     -15.118  11.846 -69.976  1.00231.97           N  
ANISOU  288  NE1 TRP A  35    25591  34630  27918    -31  -1806  -1689       N  
ATOM    289  CE2 TRP A  35     -15.727  10.838 -69.277  1.00227.73           C  
ANISOU  289  CE2 TRP A  35    24956  34207  27365   -292  -2416  -1448       C  
ATOM    290  CE3 TRP A  35     -16.843   8.748 -69.752  1.00221.66           C  
ANISOU  290  CE3 TRP A  35    24561  33068  26593    -98  -3514  -1069       C  
ATOM    291  CZ2 TRP A  35     -15.917  10.682 -67.906  1.00223.29           C  
ANISOU  291  CZ2 TRP A  35    24011  34042  26788   -814  -2605  -1333       C  
ATOM    292  CZ3 TRP A  35     -17.031   8.595 -68.390  1.00217.67           C  
ANISOU  292  CZ3 TRP A  35    23668  32955  26081   -618  -3681   -948       C  
ATOM    293  CH2 TRP A  35     -16.570   9.558 -67.483  1.00218.74           C  
ANISOU  293  CH2 TRP A  35    23440  33469  26203   -963  -3231  -1079       C  
ATOM    294  N   ASN A  36     -17.472  11.963 -74.633  1.00228.77           N  
ANISOU  294  N   ASN A  36    26906  32723  27294   1640  -1860  -1791       N  
ATOM    295  CA  ASN A  36     -17.820  13.349 -74.912  1.00229.98           C  
ANISOU  295  CA  ASN A  36    27100  32902  27380   1677  -1247  -1983       C  
ATOM    296  C   ASN A  36     -19.303  13.526 -75.214  1.00227.50           C  
ANISOU  296  C   ASN A  36    26971  32488  26982   1692  -1439  -1927       C  
ATOM    297  O   ASN A  36     -19.776  14.666 -75.258  1.00228.16           O  
ANISOU  297  O   ASN A  36    27037  32649  27003   1642   -978  -2058       O  
ATOM    298  CB  ASN A  36     -16.985  13.876 -76.082  1.00232.06           C  
ANISOU  298  CB  ASN A  36    27705  32837  27631   2204   -752  -2180       C  
ATOM    299  CG  ASN A  36     -15.507  13.970 -75.750  1.00234.01           C  
ANISOU  299  CG  ASN A  36    27713  33211  27989   2162   -428  -2274       C  
ATOM    300  OD1 ASN A  36     -15.128  14.379 -74.653  1.00234.38           O  
ANISOU  300  OD1 ASN A  36    27307  33652  28094   1712   -241  -2305       O  
ATOM    301  ND2 ASN A  36     -14.663  13.590 -76.702  1.00234.72           N  
ANISOU  301  ND2 ASN A  36    28111  32960  28114   2639   -362  -2320       N  
ATOM    302  N   ASP A  37     -20.041  12.433 -75.421  1.00232.20           N  
ANISOU  302  N   ASP A  37    27735  32908  27583   1761  -2105  -1738       N  
ATOM    303  CA  ASP A  37     -21.474  12.501 -75.679  1.00230.39           C  
ANISOU  303  CA  ASP A  37    27651  32579  27306   1762  -2353  -1673       C  
ATOM    304  C   ASP A  37     -22.330  12.250 -74.444  1.00228.22           C  
ANISOU  304  C   ASP A  37    26978  32654  27082   1193  -2669  -1496       C  
ATOM    305  O   ASP A  37     -23.485  12.694 -74.411  1.00227.20           O  
ANISOU  305  O   ASP A  37    26845  32553  26927   1086  -2680  -1477       O  
ATOM    306  CB  ASP A  37     -21.868  11.485 -76.759  1.00229.43           C  
ANISOU  306  CB  ASP A  37    27991  32009  27173   2211  -2899  -1586       C  
ATOM    307  CG  ASP A  37     -21.319  11.840 -78.125  1.00230.65           C  
ANISOU  307  CG  ASP A  37    28626  31764  27246   2827  -2577  -1762       C  
ATOM    308  OD1 ASP A  37     -21.135  13.044 -78.400  1.00231.83           O  
ANISOU  308  OD1 ASP A  37    28814  31939  27332   2933  -1940  -1952       O  
ATOM    309  OD2 ASP A  37     -21.072  10.912 -78.925  1.00230.24           O  
ANISOU  309  OD2 ASP A  37    28929  31364  27189   3213  -2952  -1707       O  
ATOM    310  N   ARG A  38     -21.798  11.558 -73.432  1.00233.45           N  
ANISOU  310  N   ARG A  38    27312  33574  27813    839  -2918  -1364       N  
ATOM    311  CA  ARG A  38     -22.635  11.129 -72.314  1.00229.70           C  
ANISOU  311  CA  ARG A  38    26512  33378  27384    338  -3289  -1165       C  
ATOM    312  C   ARG A  38     -23.141  12.310 -71.492  1.00229.92           C  
ANISOU  312  C   ARG A  38    26227  33758  27373    -57  -2833  -1233       C  
ATOM    313  O   ARG A  38     -24.275  12.285 -71.001  1.00226.79           O  
ANISOU  313  O   ARG A  38    25701  33473  26994   -333  -3038  -1107       O  
ATOM    314  CB  ARG A  38     -21.871  10.148 -71.427  1.00228.39           C  
ANISOU  314  CB  ARG A  38    26092  33403  27281     77  -3628  -1016       C  
ATOM    315  CG  ARG A  38     -21.481   8.848 -72.117  1.00227.50           C  
ANISOU  315  CG  ARG A  38    26270  32959  27213    419  -4151   -909       C  
ATOM    316  CD  ARG A  38     -22.675   7.917 -72.317  1.00224.14           C  
ANISOU  316  CD  ARG A  38    25999  32334  26831    423  -4785   -713       C  
ATOM    317  NE  ARG A  38     -23.513   8.302 -73.450  1.00224.84           N  
ANISOU  317  NE  ARG A  38    26455  32093  26883    790  -4757   -802       N  
ATOM    318  CZ  ARG A  38     -23.213   8.054 -74.721  1.00226.07           C  
ANISOU  318  CZ  ARG A  38    27057  31838  27000   1334  -4817   -888       C  
ATOM    319  NH1 ARG A  38     -22.092   7.416 -75.028  1.00227.44           N  
ANISOU  319  NH1 ARG A  38    27360  31877  27179   1571  -4894   -891       N  
ATOM    320  NH2 ARG A  38     -24.035   8.441 -75.687  1.00225.31           N  
ANISOU  320  NH2 ARG A  38    27289  31461  26858   1651  -4802   -970       N  
ATOM    321  N   PHE A  39     -22.317  13.347 -71.320  1.00231.44           N  
ANISOU  321  N   PHE A  39    26290  34124  27523    -94  -2209  -1429       N  
ATOM    322  CA  PHE A  39     -22.758  14.513 -70.557  1.00232.02           C  
ANISOU  322  CA  PHE A  39    26086  34522  27550   -459  -1747  -1507       C  
ATOM    323  C   PHE A  39     -23.967  15.174 -71.204  1.00231.72           C  
ANISOU  323  C   PHE A  39    26259  34323  27461   -301  -1621  -1549       C  
ATOM    324  O   PHE A  39     -24.900  15.597 -70.510  1.00229.94           O  
ANISOU  324  O   PHE A  39    25823  34319  27226   -646  -1581  -1482       O  
ATOM    325  CB  PHE A  39     -21.611  15.509 -70.403  1.00235.77           C  
ANISOU  325  CB  PHE A  39    26426  35158  27999   -475  -1094  -1733       C  
ATOM    326  CG  PHE A  39     -20.578  15.084 -69.405  1.00234.69           C  
ANISOU  326  CG  PHE A  39    25953  35305  27914   -782  -1170  -1693       C  
ATOM    327  CD1 PHE A  39     -20.857  14.081 -68.496  1.00230.85           C  
ANISOU  327  CD1 PHE A  39    25258  34993  27463  -1112  -1716  -1464       C  
ATOM    328  CD2 PHE A  39     -19.336  15.685 -69.368  1.00237.47           C  
ANISOU  328  CD2 PHE A  39    26195  35744  28287   -739   -698  -1886       C  
ATOM    329  CE1 PHE A  39     -19.917  13.689 -67.572  1.00229.89           C  
ANISOU  329  CE1 PHE A  39    24840  35133  27375  -1379  -1800  -1428       C  
ATOM    330  CE2 PHE A  39     -18.391  15.290 -68.441  1.00236.19           C  
ANISOU  330  CE2 PHE A  39    25713  35848  28180  -1018   -794  -1856       C  
ATOM    331  CZ  PHE A  39     -18.682  14.290 -67.546  1.00232.58           C  
ANISOU  331  CZ  PHE A  39    25067  35566  27736  -1330  -1353  -1627       C  
ATOM    332  N   SER A  40     -23.969  15.273 -72.534  1.00236.32           N  
ANISOU  332  N   SER A  40    27267  34517  28009    229  -1556  -1659       N  
ATOM    333  CA  SER A  40     -25.162  15.737 -73.229  1.00236.20           C  
ANISOU  333  CA  SER A  40    27489  34309  27948    427  -1540  -1683       C  
ATOM    334  C   SER A  40     -26.310  14.752 -73.052  1.00232.01           C  
ANISOU  334  C   SER A  40    26947  33714  27494    296  -2225  -1453       C  
ATOM    335  O   SER A  40     -27.459  15.155 -72.827  1.00230.01           O  
ANISOU  335  O   SER A  40    26607  33538  27247    124  -2237  -1403       O  
ATOM    336  CB  SER A  40     -24.854  15.944 -74.710  1.00238.87           C  
ANISOU  336  CB  SER A  40    28321  34220  28219   1055  -1371  -1843       C  
ATOM    337  OG  SER A  40     -23.889  16.965 -74.893  1.00242.93           O  
ANISOU  337  OG  SER A  40    28844  34781  28676   1172   -679  -2062       O  
ATOM    338  N   ASP A  41     -26.012  13.453 -73.131  1.00237.69           N  
ANISOU  338  N   ASP A  41    27740  34288  28284    368  -2793  -1307       N  
ATOM    339  CA  ASP A  41     -27.024  12.416 -72.963  1.00233.26           C  
ANISOU  339  CA  ASP A  41    27166  33643  27820    242  -3467  -1083       C  
ATOM    340  C   ASP A  41     -27.521  12.289 -71.527  1.00230.37           C  
ANISOU  340  C   ASP A  41    26340  33672  27520   -366  -3585   -908       C  
ATOM    341  O   ASP A  41     -28.356  11.418 -71.261  1.00227.32           O  
ANISOU  341  O   ASP A  41    25898  33239  27234   -523  -4125   -707       O  
ATOM    342  CB  ASP A  41     -26.477  11.071 -73.445  1.00232.37           C  
ANISOU  342  CB  ASP A  41    27274  33259  27756    496  -4011   -983       C  
ATOM    343  CG  ASP A  41     -26.298  11.024 -74.951  1.00233.67           C  
ANISOU  343  CG  ASP A  41    27956  32967  27860   1125  -4025  -1115       C  
ATOM    344  OD1 ASP A  41     -27.055  11.717 -75.662  1.00233.76           O  
ANISOU  344  OD1 ASP A  41    28183  32815  27818   1356  -3858  -1219       O  
ATOM    345  OD2 ASP A  41     -25.400  10.295 -75.423  1.00233.97           O  
ANISOU  345  OD2 ASP A  41    28197  32806  27895   1400  -4199  -1114       O  
ATOM    346  N   ILE A  42     -27.031  13.113 -70.604  1.00233.73           N  
ANISOU  346  N   ILE A  42    26446  34467  27893   -706  -3099   -978       N  
ATOM    347  CA  ILE A  42     -27.564  13.187 -69.252  1.00233.53           C  
ANISOU  347  CA  ILE A  42    26011  34818  27900  -1268  -3123   -832       C  
ATOM    348  C   ILE A  42     -28.234  14.531 -68.991  1.00232.44           C  
ANISOU  348  C   ILE A  42    25746  34869  27700  -1436  -2592   -938       C  
ATOM    349  O   ILE A  42     -29.319  14.584 -68.404  1.00232.43           O  
ANISOU  349  O   ILE A  42    25566  34999  27747  -1735  -2711   -803       O  
ATOM    350  CB  ILE A  42     -26.460  12.908 -68.208  1.00233.72           C  
ANISOU  350  CB  ILE A  42    25744  35149  27910  -1581  -3073   -798       C  
ATOM    351  CG1 ILE A  42     -25.931  11.481 -68.359  1.00234.93           C  
ANISOU  351  CG1 ILE A  42    25999  35130  28132  -1454  -3655   -654       C  
ATOM    352  CG2 ILE A  42     -26.984  13.132 -66.798  1.00233.54           C  
ANISOU  352  CG2 ILE A  42    25323  35523  27888  -2151  -3022   -667       C  
ATOM    353  CD1 ILE A  42     -24.680  11.205 -67.555  1.00235.28           C  
ANISOU  353  CD1 ILE A  42    25815  35421  28158  -1651  -3598   -653       C  
ATOM    354  N   TYR A  43     -27.604  15.626 -69.425  1.00239.96           N  
ANISOU  354  N   TYR A  43    26792  35828  28553  -1244  -1989  -1177       N  
ATOM    355  CA  TYR A  43     -28.239  16.936 -69.330  1.00240.78           C  
ANISOU  355  CA  TYR A  43    26831  36065  28588  -1341  -1463  -1294       C  
ATOM    356  C   TYR A  43     -29.568  16.958 -70.072  1.00239.75           C  
ANISOU  356  C   TYR A  43    26912  35688  28492  -1130  -1674  -1245       C  
ATOM    357  O   TYR A  43     -30.536  17.570 -69.607  1.00238.69           O  
ANISOU  357  O   TYR A  43    26615  35716  28362  -1375  -1520  -1204       O  
ATOM    358  CB  TYR A  43     -27.307  18.015 -69.878  1.00244.54           C  
ANISOU  358  CB  TYR A  43    27440  36510  28963  -1088   -808  -1565       C  
ATOM    359  CG  TYR A  43     -27.891  19.411 -69.837  1.00244.95           C  
ANISOU  359  CG  TYR A  43    27454  36682  28932  -1158   -226  -1701       C  
ATOM    360  CD1 TYR A  43     -27.948  20.128 -68.650  1.00242.75           C  
ANISOU  360  CD1 TYR A  43    26815  36801  28619  -1638    118  -1702       C  
ATOM    361  CD2 TYR A  43     -28.384  20.013 -70.988  1.00247.00           C  
ANISOU  361  CD2 TYR A  43    28057  36653  29139   -731    -20  -1828       C  
ATOM    362  CE1 TYR A  43     -28.480  21.404 -68.609  1.00242.45           C  
ANISOU  362  CE1 TYR A  43    26751  36868  28500  -1700    659  -1823       C  
ATOM    363  CE2 TYR A  43     -28.917  21.288 -70.958  1.00247.18           C  
ANISOU  363  CE2 TYR A  43    28054  36782  29081   -783    518  -1949       C  
ATOM    364  CZ  TYR A  43     -28.963  21.979 -69.766  1.00244.80           C  
ANISOU  364  CZ  TYR A  43    27384  36877  28752  -1272    860  -1945       C  
ATOM    365  OH  TYR A  43     -29.493  23.248 -69.730  1.00243.63           O  
ANISOU  365  OH  TYR A  43    27218  36830  28520  -1323   1404  -2063       O  
ATOM    366  N   ALA A  44     -29.633  16.299 -71.232  1.00242.46           N  
ANISOU  366  N   ALA A  44    27625  35635  28864   -668  -2032  -1253       N  
ATOM    367  CA  ALA A  44     -30.897  16.220 -71.957  1.00241.50           C  
ANISOU  367  CA  ALA A  44    27709  35260  28788   -455  -2309  -1207       C  
ATOM    368  C   ALA A  44     -31.951  15.462 -71.160  1.00237.39           C  
ANISOU  368  C   ALA A  44    26928  34855  28414   -839  -2817   -954       C  
ATOM    369  O   ALA A  44     -33.148  15.744 -71.288  1.00236.48           O  
ANISOU  369  O   ALA A  44    26802  34694  28354   -864  -2889   -909       O  
ATOM    370  CB  ALA A  44     -30.682  15.563 -73.320  1.00242.04           C  
ANISOU  370  CB  ALA A  44    28239  34873  28851    115  -2640  -1262       C  
ATOM    371  N   LEU A  45     -31.529  14.504 -70.333  1.00235.73           N  
ANISOU  371  N   LEU A  45    26503  34791  28273  -1137  -3162   -786       N  
ATOM    372  CA  LEU A  45     -32.478  13.738 -69.533  1.00236.53           C  
ANISOU  372  CA  LEU A  45    26357  34994  28521  -1512  -3628   -534       C  
ATOM    373  C   LEU A  45     -32.963  14.525 -68.322  1.00235.87           C  
ANISOU  373  C   LEU A  45    25888  35307  28423  -2011  -3262   -478       C  
ATOM    374  O   LEU A  45     -34.142  14.449 -67.962  1.00236.31           O  
ANISOU  374  O   LEU A  45    25795  35401  28590  -2228  -3443   -332       O  
ATOM    375  CB  LEU A  45     -31.846  12.422 -69.078  1.00237.47           C  
ANISOU  375  CB  LEU A  45    26407  35116  28706  -1638  -4117   -369       C  
ATOM    376  CG  LEU A  45     -31.502  11.390 -70.151  1.00238.45           C  
ANISOU  376  CG  LEU A  45    26894  34838  28869  -1196  -4601   -366       C  
ATOM    377  CD1 LEU A  45     -30.781  10.204 -69.529  1.00239.28           C  
ANISOU  377  CD1 LEU A  45    26886  35008  29022  -1373  -5000   -204       C  
ATOM    378  CD2 LEU A  45     -32.753  10.938 -70.884  1.00239.40           C  
ANISOU  378  CD2 LEU A  45    27200  34647  29116  -1007  -5058   -289       C  
ATOM    379  N   CYS A  46     -32.072  15.283 -67.685  1.00245.80           N  
ANISOU  379  N   CYS A  46    26982  36857  29555  -2197  -2747   -593       N  
ATOM    380  CA  CYS A  46     -32.379  15.933 -66.417  1.00244.92           C  
ANISOU  380  CA  CYS A  46    26506  37139  29411  -2696  -2422   -532       C  
ATOM    381  C   CYS A  46     -33.129  17.255 -66.570  1.00246.39           C  
ANISOU  381  C   CYS A  46    26685  37393  29540  -2691  -1910   -653       C  
ATOM    382  O   CYS A  46     -33.167  18.030 -65.606  1.00244.36           O  
ANISOU  382  O   CYS A  46    26167  37465  29214  -3056  -1502   -662       O  
ATOM    383  CB  CYS A  46     -31.091  16.164 -65.621  1.00245.40           C  
ANISOU  383  CB  CYS A  46    26388  37488  29363  -2911  -2116   -610       C  
ATOM    384  SG  CYS A  46     -30.261  14.655 -65.077  1.00243.89           S  
ANISOU  384  SG  CYS A  46    26114  37320  29233  -3037  -2690   -432       S  
ATOM    385  N   VAL A  47     -33.723  17.552 -67.727  1.00256.94           N  
ANISOU  385  N   VAL A  47    28306  38429  30891  -2289  -1915   -748       N  
ATOM    386  CA  VAL A  47     -34.368  18.851 -67.892  1.00259.13           C  
ANISOU  386  CA  VAL A  47    28588  38770  31098  -2260  -1398   -873       C  
ATOM    387  C   VAL A  47     -35.841  18.735 -68.268  1.00258.28           C  
ANISOU  387  C   VAL A  47    28517  38496  31120  -2196  -1688   -761       C  
ATOM    388  O   VAL A  47     -36.718  19.112 -67.484  1.00256.23           O  
ANISOU  388  O   VAL A  47    27995  38448  30913  -2543  -1574   -649       O  
ATOM    389  CB  VAL A  47     -33.618  19.703 -68.935  1.00262.62           C  
ANISOU  389  CB  VAL A  47    29343  39041  31398  -1814   -937  -1150       C  
ATOM    390  CG1 VAL A  47     -34.381  20.989 -69.216  1.00263.05           C  
ANISOU  390  CG1 VAL A  47    29445  39118  31382  -1738   -444  -1272       C  
ATOM    391  CG2 VAL A  47     -32.215  20.023 -68.447  1.00262.84           C  
ANISOU  391  CG2 VAL A  47    29271  39276  31321  -1933   -554  -1276       C  
ATOM    392  N   ALA A  48     -36.133  18.190 -69.446  1.00261.32           N  
ANISOU  392  N   ALA A  48    29222  38499  31567  -1758  -2078   -786       N  
ATOM    393  CA  ALA A  48     -37.393  18.473 -70.136  1.00261.87           C  
ANISOU  393  CA  ALA A  48    29415  38368  31716  -1552  -2193   -785       C  
ATOM    394  C   ALA A  48     -38.299  17.246 -70.217  1.00260.59           C  
ANISOU  394  C   ALA A  48    29219  38015  31778  -1591  -2934   -570       C  
ATOM    395  O   ALA A  48     -38.186  16.435 -71.138  1.00260.77           O  
ANISOU  395  O   ALA A  48    29530  37703  31847  -1232  -3391   -583       O  
ATOM    396  CB  ALA A  48     -37.109  19.019 -71.533  1.00263.92           C  
ANISOU  396  CB  ALA A  48    30110  38317  31850   -967  -1995  -1021       C  
ATOM    397  N   TYR A  49     -39.206  17.112 -69.244  1.00265.68           N  
ANISOU  397  N   TYR A  49    29515  38864  32567  -2030  -3043   -370       N  
ATOM    398  CA  TYR A  49     -40.406  16.316 -69.483  1.00262.96           C  
ANISOU  398  CA  TYR A  49    29139  38310  32462  -2026  -3630   -202       C  
ATOM    399  C   TYR A  49     -41.681  16.938 -68.895  1.00261.76           C  
ANISOU  399  C   TYR A  49    28701  38325  32431  -2318  -3459   -100       C  
ATOM    400  O   TYR A  49     -42.534  16.210 -68.376  1.00258.90           O  
ANISOU  400  O   TYR A  49    28110  37964  32295  -2590  -3863    121       O  
ATOM    401  CB  TYR A  49     -40.154  14.901 -68.934  1.00261.47           C  
ANISOU  401  CB  TYR A  49    28830  38106  32412  -2253  -4195      9       C  
ATOM    402  CG  TYR A  49     -41.296  13.908 -69.043  1.00257.79           C  
ANISOU  402  CG  TYR A  49    28295  37430  32225  -2311  -4842    206       C  
ATOM    403  CD1 TYR A  49     -41.722  13.432 -70.275  1.00256.59           C  
ANISOU  403  CD1 TYR A  49    28453  36875  32163  -1875  -5290    143       C  
ATOM    404  CD2 TYR A  49     -41.921  13.418 -67.899  1.00256.30           C  
ANISOU  404  CD2 TYR A  49    27735  37434  32213  -2803  -5011    456       C  
ATOM    405  CE1 TYR A  49     -42.761  12.524 -70.367  1.00254.53           C  
ANISOU  405  CE1 TYR A  49    28114  36416  32178  -1940  -5892    314       C  
ATOM    406  CE2 TYR A  49     -42.957  12.514 -67.981  1.00254.78           C  
ANISOU  406  CE2 TYR A  49    27461  37041  32301  -2871  -5584    637       C  
ATOM    407  CZ  TYR A  49     -43.372  12.067 -69.216  1.00254.10           C  
ANISOU  407  CZ  TYR A  49    27668  36560  32319  -2445  -6031    561       C  
ATOM    408  OH  TYR A  49     -44.403  11.160 -69.297  1.00253.75           O  
ANISOU  408  OH  TYR A  49    27530  36308  32577  -2522  -6616    731       O  
ATOM    409  N   PRO A  50     -41.882  18.272 -68.936  1.00263.50           N  
ANISOU  409  N   PRO A  50    28914  38682  32519  -2279  -2860   -243       N  
ATOM    410  CA  PRO A  50     -41.007  19.445 -69.006  1.00266.73           C  
ANISOU  410  CA  PRO A  50    29431  39246  32670  -2175  -2175   -466       C  
ATOM    411  C   PRO A  50     -40.543  19.717 -67.579  1.00265.56           C  
ANISOU  411  C   PRO A  50    28936  39512  32455  -2700  -1824   -379       C  
ATOM    412  O   PRO A  50     -40.598  20.837 -67.077  1.00265.25           O  
ANISOU  412  O   PRO A  50    28768  39718  32299  -2874  -1243   -453       O  
ATOM    413  CB  PRO A  50     -41.921  20.549 -69.534  1.00267.83           C  
ANISOU  413  CB  PRO A  50    29644  39333  32786  -1985  -1839   -575       C  
ATOM    414  CG  PRO A  50     -43.259  20.163 -69.049  1.00264.89           C  
ANISOU  414  CG  PRO A  50    28999  38986  32660  -2255  -2172   -355       C  
ATOM    415  CD  PRO A  50     -43.298  18.658 -69.080  1.00262.91           C  
ANISOU  415  CD  PRO A  50    28738  38553  32604  -2291  -2906   -183       C  
ATOM    416  N   GLU A  51     -40.158  18.633 -66.912  1.00267.08           N  
ANISOU  416  N   GLU A  51    28981  39770  32728  -2955  -2217   -208       N  
ATOM    417  CA  GLU A  51     -39.795  18.560 -65.508  1.00264.77           C  
ANISOU  417  CA  GLU A  51    28363  39837  32402  -3464  -2060    -76       C  
ATOM    418  C   GLU A  51     -38.499  17.776 -65.362  1.00264.70           C  
ANISOU  418  C   GLU A  51    28414  39839  32320  -3455  -2254    -87       C  
ATOM    419  O   GLU A  51     -38.180  16.940 -66.214  1.00264.87           O  
ANISOU  419  O   GLU A  51    28678  39569  32394  -3128  -2684   -105       O  
ATOM    420  CB  GLU A  51     -40.913  17.875 -64.707  1.00261.35           C  
ANISOU  420  CB  GLU A  51    27643  39466  32193  -3834  -2426    209       C  
ATOM    421  CG  GLU A  51     -42.231  18.635 -64.712  1.00260.06           C  
ANISOU  421  CG  GLU A  51    27363  39320  32129  -3892  -2226    245       C  
ATOM    422  CD  GLU A  51     -43.348  17.872 -64.028  1.00257.09           C  
ANISOU  422  CD  GLU A  51    26713  38954  32014  -4222  -2620    531       C  
ATOM    423  OE1 GLU A  51     -43.131  16.698 -63.663  1.00255.87           O  
ANISOU  423  OE1 GLU A  51    26496  38756  31968  -4368  -3088    697       O  
ATOM    424  OE2 GLU A  51     -44.446  18.444 -63.861  1.00256.64           O  
ANISOU  424  OE2 GLU A  51    26505  38943  32065  -4331  -2453    592       O  
ATOM    425  N   PRO A  52     -37.730  18.023 -64.301  1.00264.28           N  
ANISOU  425  N   PRO A  52    28155  40114  32144  -3797  -1953    -80       N  
ATOM    426  CA  PRO A  52     -36.483  17.271 -64.109  1.00263.92           C  
ANISOU  426  CA  PRO A  52    28144  40095  32038  -3798  -2145    -86       C  
ATOM    427  C   PRO A  52     -36.746  15.793 -63.858  1.00261.07           C  
ANISOU  427  C   PRO A  52    27727  39618  31849  -3909  -2832    160       C  
ATOM    428  O   PRO A  52     -37.815  15.398 -63.385  1.00259.31           O  
ANISOU  428  O   PRO A  52    27333  39408  31785  -4149  -3083    369       O  
ATOM    429  CB  PRO A  52     -35.846  17.943 -62.887  1.00262.51           C  
ANISOU  429  CB  PRO A  52    27711  40323  31708  -4198  -1675   -114       C  
ATOM    430  CG  PRO A  52     -36.989  18.565 -62.158  1.00260.81           C  
ANISOU  430  CG  PRO A  52    27272  40294  31530  -4521  -1446     -1       C  
ATOM    431  CD  PRO A  52     -37.958  18.999 -63.220  1.00262.83           C  
ANISOU  431  CD  PRO A  52    27704  40290  31869  -4195  -1431    -68       C  
ATOM    432  N   LEU A  53     -35.743  14.967 -64.186  1.00248.94           N  
ANISOU  432  N   LEU A  53    26338  37958  30289  -3728  -3125    137       N  
ATOM    433  CA  LEU A  53     -35.920  13.520 -64.144  1.00250.36           C  
ANISOU  433  CA  LEU A  53    26527  37970  30626  -3757  -3797    349       C  
ATOM    434  C   LEU A  53     -34.729  12.763 -63.561  1.00250.63           C  
ANISOU  434  C   LEU A  53    26510  38127  30593  -3877  -3960    399       C  
ATOM    435  O   LEU A  53     -34.703  11.529 -63.657  1.00251.79           O  
ANISOU  435  O   LEU A  53    26716  38102  30850  -3837  -4515    552       O  
ATOM    436  CB  LEU A  53     -36.211  12.977 -65.549  1.00250.91           C  
ANISOU  436  CB  LEU A  53    26933  37604  30795  -3273  -4200    294       C  
ATOM    437  CG  LEU A  53     -37.508  13.396 -66.241  1.00251.18           C  
ANISOU  437  CG  LEU A  53    27046  37444  30946  -3110  -4236    279       C  
ATOM    438  CD1 LEU A  53     -37.530  12.849 -67.658  1.00251.78           C  
ANISOU  438  CD1 LEU A  53    27502  37088  31074  -2590  -4630    190       C  
ATOM    439  CD2 LEU A  53     -38.723  12.925 -65.458  1.00252.38           C  
ANISOU  439  CD2 LEU A  53    26918  37667  31307  -3488  -4520    536       C  
ATOM    440  N   GLY A  54     -33.745  13.445 -62.970  1.00249.60           N  
ANISOU  440  N   GLY A  54    26270  38279  30288  -4016  -3509    273       N  
ATOM    441  CA  GLY A  54     -32.583  12.756 -62.425  1.00249.57           C  
ANISOU  441  CA  GLY A  54    26207  38396  30222  -4116  -3665    308       C  
ATOM    442  C   GLY A  54     -32.912  11.746 -61.344  1.00246.88           C  
ANISOU  442  C   GLY A  54    25659  38177  29964  -4493  -4068    590       C  
ATOM    443  O   GLY A  54     -32.120  10.821 -61.103  1.00246.99           O  
ANISOU  443  O   GLY A  54    25773  38075  29996  -4426  -4318    652       O  
ATOM    444  N   GLU A  55     -34.066  11.903 -60.687  1.00245.63           N  
ANISOU  444  N   GLU A  55    25439  37976  29914  -4699  -3964    736       N  
ATOM    445  CA  GLU A  55     -34.501  10.947 -59.674  1.00244.75           C  
ANISOU  445  CA  GLU A  55    25371  37683  29940  -4852  -4157    973       C  
ATOM    446  C   GLU A  55     -34.553   9.528 -60.227  1.00244.69           C  
ANISOU  446  C   GLU A  55    25554  37312  30104  -4621  -4743   1080       C  
ATOM    447  O   GLU A  55     -34.322   8.564 -59.488  1.00244.88           O  
ANISOU  447  O   GLU A  55    25635  37224  30183  -4685  -4918   1217       O  
ATOM    448  CB  GLU A  55     -35.868  11.367 -59.130  1.00245.07           C  
ANISOU  448  CB  GLU A  55    25313  37721  30081  -5058  -3980   1098       C  
ATOM    449  CG  GLU A  55     -36.400  10.515 -57.991  1.00246.29           C  
ANISOU  449  CG  GLU A  55    25479  37752  30349  -5247  -4101   1336       C  
ATOM    450  CD  GLU A  55     -37.731  11.021 -57.463  1.00247.01           C  
ANISOU  450  CD  GLU A  55    25461  37863  30529  -5444  -3889   1452       C  
ATOM    451  OE1 GLU A  55     -38.241  12.027 -58.000  1.00246.57           O  
ANISOU  451  OE1 GLU A  55    25324  37904  30458  -5427  -3654   1346       O  
ATOM    452  OE2 GLU A  55     -38.267  10.414 -56.512  1.00247.90           O  
ANISOU  452  OE2 GLU A  55    25564  37904  30724  -5613  -3950   1649       O  
ATOM    453  N   ARG A  56     -34.844   9.380 -61.521  1.00240.81           N  
ANISOU  453  N   ARG A  56    25181  36633  29684  -4338  -5046   1013       N  
ATOM    454  CA  ARG A  56     -34.812   8.063 -62.147  1.00241.34           C  
ANISOU  454  CA  ARG A  56    25475  36327  29896  -4071  -5587   1081       C  
ATOM    455  C   ARG A  56     -33.381   7.560 -62.299  1.00241.49           C  
ANISOU  455  C   ARG A  56    25601  36359  29796  -3913  -5695   1009       C  
ATOM    456  O   ARG A  56     -33.083   6.397 -61.996  1.00241.59           O  
ANISOU  456  O   ARG A  56    25732  36170  29890  -3856  -5973   1108       O  
ATOM    457  CB  ARG A  56     -35.509   8.118 -63.507  1.00240.95           C  
ANISOU  457  CB  ARG A  56    25560  36058  29933  -3783  -5879   1021       C  
ATOM    458  CG  ARG A  56     -35.558   6.790 -64.239  1.00241.19           C  
ANISOU  458  CG  ARG A  56    25864  35666  30110  -3472  -6421   1067       C  
ATOM    459  CD  ARG A  56     -36.310   6.923 -65.552  1.00241.24           C  
ANISOU  459  CD  ARG A  56    26032  35433  30195  -3173  -6703   1004       C  
ATOM    460  NE  ARG A  56     -36.315   5.677 -66.311  1.00241.92           N  
ANISOU  460  NE  ARG A  56    26417  35106  30397  -2844  -7182   1018       N  
ATOM    461  CZ  ARG A  56     -36.915   5.524 -67.487  1.00242.23           C  
ANISOU  461  CZ  ARG A  56    26678  34842  30516  -2519  -7495    962       C  
ATOM    462  NH1 ARG A  56     -37.561   6.542 -68.038  1.00242.60           N  
ANISOU  462  NH1 ARG A  56    26678  34945  30554  -2476  -7422    898       N  
ATOM    463  NH2 ARG A  56     -36.870   4.355 -68.111  1.00242.65           N  
ANISOU  463  NH2 ARG A  56    27010  34541  30645  -2234  -7860    971       N  
ATOM    464  N   LEU A  57     -32.480   8.430 -62.767  1.00239.93           N  
ANISOU  464  N   LEU A  57    25346  36417  29397  -3840  -5457    827       N  
ATOM    465  CA  LEU A  57     -31.101   8.019 -63.010  1.00241.40           C  
ANISOU  465  CA  LEU A  57    25616  36629  29475  -3669  -5555    747       C  
ATOM    466  C   LEU A  57     -30.416   7.577 -61.723  1.00240.14           C  
ANISOU  466  C   LEU A  57    25374  36564  29302  -3891  -5436    827       C  
ATOM    467  O   LEU A  57     -29.637   6.614 -61.726  1.00240.18           O  
ANISOU  467  O   LEU A  57    25503  36425  29330  -3749  -5701    862       O  
ATOM    468  CB  LEU A  57     -30.325   9.159 -63.672  1.00243.65           C  
ANISOU  468  CB  LEU A  57    25950  37031  29595  -3457  -5093    474       C  
ATOM    469  CG  LEU A  57     -28.866   8.882 -64.044  1.00245.97           C  
ANISOU  469  CG  LEU A  57    26375  37277  29805  -3199  -5074    346       C  
ATOM    470  CD1 LEU A  57     -28.774   7.740 -65.038  1.00245.84           C  
ANISOU  470  CD1 LEU A  57    26663  36864  29879  -2821  -5607    406       C  
ATOM    471  CD2 LEU A  57     -28.214  10.132 -64.612  1.00249.47           C  
ANISOU  471  CD2 LEU A  57    26904  37751  30133  -2972  -4471     57       C  
ATOM    472  N   TYR A  58     -30.696   8.263 -60.612  1.00238.71           N  
ANISOU  472  N   TYR A  58    25005  36623  29073  -4222  -5043    858       N  
ATOM    473  CA  TYR A  58     -30.104   7.865 -59.336  1.00238.30           C  
ANISOU  473  CA  TYR A  58    24898  36663  28982  -4424  -4946    946       C  
ATOM    474  C   TYR A  58     -30.528   6.451 -58.950  1.00238.56           C  
ANISOU  474  C   TYR A  58    25068  36398  29175  -4396  -5346   1150       C  
ATOM    475  O   TYR A  58     -29.686   5.598 -58.634  1.00239.20           O  
ANISOU  475  O   TYR A  58    25220  36419  29246  -4331  -5528   1186       O  
ATOM    476  CB  TYR A  58     -30.491   8.863 -58.245  1.00237.89           C  
ANISOU  476  CB  TYR A  58    24665  36887  28835  -4759  -4472    958       C  
ATOM    477  N   THR A  59     -31.835   6.181 -58.985  1.00238.44           N  
ANISOU  477  N   THR A  59    25081  36203  29312  -4442  -5477   1276       N  
ATOM    478  CA  THR A  59     -32.342   4.875 -58.571  1.00239.73           C  
ANISOU  478  CA  THR A  59    25347  36113  29626  -4448  -5804   1463       C  
ATOM    479  C   THR A  59     -31.837   3.768 -59.488  1.00240.25           C  
ANISOU  479  C   THR A  59    25627  35895  29762  -4115  -6235   1432       C  
ATOM    480  O   THR A  59     -31.353   2.732 -59.018  1.00240.55           O  
ANISOU  480  O   THR A  59    25742  35843  29812  -4096  -6421   1519       O  
ATOM    481  CB  THR A  59     -33.871   4.891 -58.539  1.00239.85           C  
ANISOU  481  CB  THR A  59    25326  36002  29805  -4557  -5840   1583       C  
ATOM    482  OG1 THR A  59     -34.376   5.185 -59.847  1.00239.74           O  
ANISOU  482  OG1 THR A  59    25386  35832  29873  -4323  -5991   1476       O  
ATOM    483  CG2 THR A  59     -34.373   5.937 -57.555  1.00239.83           C  
ANISOU  483  CG2 THR A  59    25126  36277  29722  -4883  -5400   1629       C  
ATOM    484  N   GLU A  60     -31.950   3.967 -60.806  1.00240.22           N  
ANISOU  484  N   GLU A  60    25737  35748  29788  -3838  -6395   1312       N  
ATOM    485  CA  GLU A  60     -31.461   2.963 -61.748  1.00240.64           C  
ANISOU  485  CA  GLU A  60    26028  35523  29880  -3489  -6788   1276       C  
ATOM    486  C   GLU A  60     -29.976   2.687 -61.538  1.00240.80           C  
ANISOU  486  C   GLU A  60    26068  35654  29770  -3413  -6775   1217       C  
ATOM    487  O   GLU A  60     -29.544   1.524 -61.522  1.00240.69           O  
ANISOU  487  O   GLU A  60    26195  35465  29792  -3276  -7040   1276       O  
ATOM    488  CB  GLU A  60     -31.723   3.422 -63.183  1.00239.93           C  
ANISOU  488  CB  GLU A  60    26070  35300  29793  -3196  -6923   1148       C  
ATOM    489  CG  GLU A  60     -33.195   3.524 -63.555  1.00239.66           C  
ANISOU  489  CG  GLU A  60    26049  35096  29914  -3205  -7021   1198       C  
ATOM    490  CD  GLU A  60     -33.880   2.173 -63.614  1.00240.49           C  
ANISOU  490  CD  GLU A  60    26306  34875  30194  -3122  -7367   1322       C  
ATOM    491  OE1 GLU A  60     -33.209   1.179 -63.963  1.00240.77           O  
ANISOU  491  OE1 GLU A  60    26531  34739  30212  -2906  -7611   1324       O  
ATOM    492  OE2 GLU A  60     -35.091   2.106 -63.317  1.00240.56           O  
ANISOU  492  OE2 GLU A  60    26237  34810  30356  -3280  -7380   1424       O  
ATOM    493  N   THR A  61     -29.181   3.748 -61.369  1.00237.40           N  
ANISOU  493  N   THR A  61    25484  35530  29187  -3507  -6450   1099       N  
ATOM    494  CA  THR A  61     -27.756   3.579 -61.105  1.00237.45           C  
ANISOU  494  CA  THR A  61    25466  35672  29081  -3461  -6408   1036       C  
ATOM    495  C   THR A  61     -27.527   2.733 -59.858  1.00238.76           C  
ANISOU  495  C   THR A  61    25601  35847  29270  -3640  -6446   1175       C  
ATOM    496  O   THR A  61     -26.695   1.817 -59.860  1.00239.67           O  
ANISOU  496  O   THR A  61    25817  35864  29382  -3488  -6663   1190       O  
ATOM    497  CB  THR A  61     -27.086   4.947 -60.962  1.00236.03           C  
ANISOU  497  CB  THR A  61    25076  35868  28738  -3600  -5978    882       C  
ATOM    498  OG1 THR A  61     -27.267   5.699 -62.168  1.00236.16           O  
ANISOU  498  OG1 THR A  61    25121  35906  28701  -3416  -5945    751       O  
ATOM    499  CG2 THR A  61     -25.597   4.787 -60.690  1.00236.28           C  
ANISOU  499  CG2 THR A  61    25055  36046  28673  -3555  -5933    807       C  
ATOM    500  N   LYS A  62     -28.272   3.015 -58.785  1.00234.33           N  
ANISOU  500  N   LYS A  62    24908  35407  28718  -3956  -6239   1287       N  
ATOM    501  CA  LYS A  62     -28.125   2.228 -57.563  1.00235.55           C  
ANISOU  501  CA  LYS A  62    25044  35585  28869  -4133  -6281   1439       C  
ATOM    502  C   LYS A  62     -28.502   0.768 -57.796  1.00235.95           C  
ANISOU  502  C   LYS A  62    25279  35318  29051  -3978  -6686   1568       C  
ATOM    503  O   LYS A  62     -27.892  -0.140 -57.216  1.00236.59           O  
ANISOU  503  O   LYS A  62    25408  35376  29111  -3975  -6825   1646       O  
ATOM    504  CB  LYS A  62     -28.970   2.837 -56.443  1.00236.10           C  
ANISOU  504  CB  LYS A  62    24960  35836  28910  -4486  -5989   1552       C  
ATOM    505  CG  LYS A  62     -28.773   2.183 -55.084  1.00236.89           C  
ANISOU  505  CG  LYS A  62    25031  36015  28960  -4694  -5994   1715       C  
ATOM    506  CD  LYS A  62     -29.515   2.942 -53.994  1.00237.01           C  
ANISOU  506  CD  LYS A  62    24903  36246  28906  -5033  -5668   1816       C  
ATOM    507  CE  LYS A  62     -29.292   2.313 -52.628  1.00238.25           C  
ANISOU  507  CE  LYS A  62    25043  36501  28981  -5235  -5684   1986       C  
ATOM    508  NZ  LYS A  62     -29.996   3.058 -51.547  1.00239.12           N  
ANISOU  508  NZ  LYS A  62    25032  36829  28994  -5556  -5368   2091       N  
ATOM    509  N   ILE A  63     -29.498   0.522 -58.652  1.00232.90           N  
ANISOU  509  N   ILE A  63    25001  34693  28798  -3847  -6874   1587       N  
ATOM    510  CA  ILE A  63     -29.884  -0.850 -58.976  1.00234.46           C  
ANISOU  510  CA  ILE A  63    25382  34586  29118  -3692  -7240   1695       C  
ATOM    511  C   ILE A  63     -28.731  -1.580 -59.654  1.00234.76           C  
ANISOU  511  C   ILE A  63    25584  34511  29101  -3381  -7463   1611       C  
ATOM    512  O   ILE A  63     -28.365  -2.700 -59.268  1.00236.16           O  
ANISOU  512  O   ILE A  63    25847  34596  29289  -3349  -7647   1710       O  
ATOM    513  CB  ILE A  63     -31.149  -0.861 -59.853  1.00234.54           C  
ANISOU  513  CB  ILE A  63    25471  34367  29277  -3597  -7385   1706       C  
ATOM    514  CG1 ILE A  63     -32.338  -0.278 -59.087  1.00234.59           C  
ANISOU  514  CG1 ILE A  63    25303  34474  29358  -3917  -7181   1820       C  
ATOM    515  CG2 ILE A  63     -31.458  -2.273 -60.327  1.00236.22           C  
ANISOU  515  CG2 ILE A  63    25889  34258  29605  -3415  -7754   1798       C  
ATOM    516  CD1 ILE A  63     -33.543   0.002 -59.957  1.00234.48           C  
ANISOU  516  CD1 ILE A  63    25320  34284  29487  -3835  -7272   1798       C  
ATOM    517  N   PHE A  64     -28.139  -0.954 -60.678  1.00233.04           N  
ANISOU  517  N   PHE A  64    25417  34307  28820  -3145  -7445   1437       N  
ATOM    518  CA  PHE A  64     -26.993  -1.569 -61.345  1.00233.45           C  
ANISOU  518  CA  PHE A  64    25621  34268  28810  -2840  -7636   1363       C  
ATOM    519  C   PHE A  64     -25.853  -1.817 -60.365  1.00233.69           C  
ANISOU  519  C   PHE A  64    25548  34492  28753  -2952  -7550   1380       C  
ATOM    520  O   PHE A  64     -25.181  -2.855 -60.430  1.00233.52           O  
ANISOU  520  O   PHE A  64    25648  34358  28721  -2787  -7761   1416       O  
ATOM    521  CB  PHE A  64     -26.523  -0.692 -62.505  1.00232.71           C  
ANISOU  521  CB  PHE A  64    25574  34200  28646  -2604  -7593   1190       C  
ATOM    522  CG  PHE A  64     -25.358  -1.265 -63.262  1.00233.06           C  
ANISOU  522  CG  PHE A  64    25782  34146  28625  -2274  -7783   1127       C  
ATOM    523  CD1 PHE A  64     -25.536  -2.325 -64.136  1.00233.61           C  
ANISOU  523  CD1 PHE A  64    26125  33899  28739  -1977  -8092   1174       C  
ATOM    524  CD2 PHE A  64     -24.085  -0.743 -63.102  1.00233.07           C  
ANISOU  524  CD2 PHE A  64    25660  34375  28522  -2269  -7634   1031       C  
ATOM    525  CE1 PHE A  64     -24.467  -2.855 -64.834  1.00234.06           C  
ANISOU  525  CE1 PHE A  64    26346  33858  28727  -1669  -8245   1138       C  
ATOM    526  CE2 PHE A  64     -23.012  -1.269 -63.797  1.00234.31           C  
ANISOU  526  CE2 PHE A  64    25958  34440  28629  -1961  -7811    988       C  
ATOM    527  CZ  PHE A  64     -23.204  -2.326 -64.664  1.00234.59           C  
ANISOU  527  CZ  PHE A  64    26283  34151  28699  -1653  -8114   1046       C  
ATOM    528  N   LEU A  65     -25.627  -0.875 -59.444  1.00234.75           N  
ANISOU  528  N   LEU A  65    25459  34919  28815  -3231  -7233   1357       N  
ATOM    529  CA  LEU A  65     -24.615  -1.070 -58.411  1.00234.55           C  
ANISOU  529  CA  LEU A  65    25328  35083  28705  -3359  -7147   1377       C  
ATOM    530  C   LEU A  65     -24.895  -2.330 -57.601  1.00235.06           C  
ANISOU  530  C   LEU A  65    25468  35031  28814  -3439  -7343   1562       C  
ATOM    531  O   LEU A  65     -24.005  -3.167 -57.405  1.00235.16           O  
ANISOU  531  O   LEU A  65    25541  35017  28793  -3325  -7500   1580       O  
ATOM    532  CB  LEU A  65     -24.555   0.157 -57.498  1.00233.91           C  
ANISOU  532  CB  LEU A  65    25013  35328  28533  -3673  -6753   1340       C  
ATOM    533  CG  LEU A  65     -24.054   1.463 -58.119  1.00232.86           C  
ANISOU  533  CG  LEU A  65    24762  35390  28324  -3642  -6490   1151       C  
ATOM    534  CD1 LEU A  65     -24.220   2.619 -57.145  1.00232.00           C  
ANISOU  534  CD1 LEU A  65    24436  35595  28117  -3979  -6069   1129       C  
ATOM    535  CD2 LEU A  65     -22.604   1.334 -58.558  1.00232.96           C  
ANISOU  535  CD2 LEU A  65    24774  35458  28282  -3432  -6557   1028       C  
ATOM    536  N   GLU A  66     -26.136  -2.488 -57.130  1.00233.10           N  
ANISOU  536  N   GLU A  66    25209  34716  28643  -3638  -7336   1710       N  
ATOM    537  CA  GLU A  66     -26.486  -3.666 -56.340  1.00235.14           C  
ANISOU  537  CA  GLU A  66    25528  34872  28945  -3745  -7513   1910       C  
ATOM    538  C   GLU A  66     -26.255  -4.950 -57.127  1.00235.94           C  
ANISOU  538  C   GLU A  66    25844  34695  29106  -3455  -7857   1935       C  
ATOM    539  O   GLU A  66     -25.636  -5.899 -56.625  1.00236.95           O  
ANISOU  539  O   GLU A  66    26025  34805  29199  -3430  -7997   2016       O  
ATOM    540  CB  GLU A  66     -27.942  -3.578 -55.879  1.00235.54           C  
ANISOU  540  CB  GLU A  66    25527  34877  29091  -3993  -7459   2069       C  
ATOM    541  CG  GLU A  66     -28.374  -4.742 -55.000  1.00237.48           C  
ANISOU  541  CG  GLU A  66    25817  35031  29384  -4145  -7627   2302       C  
ATOM    542  CD  GLU A  66     -29.809  -4.620 -54.529  1.00238.40           C  
ANISOU  542  CD  GLU A  66    25862  35113  29607  -4405  -7568   2472       C  
ATOM    543  OE1 GLU A  66     -30.478  -3.634 -54.903  1.00238.26           O  
ANISOU  543  OE1 GLU A  66    25763  35139  29628  -4454  -7395   2399       O  
ATOM    544  OE2 GLU A  66     -30.269  -5.513 -53.786  1.00239.82           O  
ANISOU  544  OE2 GLU A  66    26063  35223  29836  -4562  -7695   2686       O  
ATOM    545  N   ASN A  67     -26.750  -4.999 -58.367  1.00234.89           N  
ANISOU  545  N   ASN A  67    25846  34346  29054  -3229  -7992   1869       N  
ATOM    546  CA  ASN A  67     -26.604  -6.209 -59.171  1.00235.52           C  
ANISOU  546  CA  ASN A  67    26153  34151  29181  -2954  -8300   1902       C  
ATOM    547  C   ASN A  67     -25.136  -6.563 -59.383  1.00235.41           C  
ANISOU  547  C   ASN A  67    26196  34191  29056  -2731  -8364   1815       C  
ATOM    548  O   ASN A  67     -24.750  -7.735 -59.279  1.00236.21           O  
ANISOU  548  O   ASN A  67    26419  34173  29159  -2636  -8563   1908       O  
ATOM    549  CB  ASN A  67     -27.318  -6.035 -60.510  1.00234.84           C  
ANISOU  549  CB  ASN A  67    26210  33843  29175  -2737  -8409   1830       C  
ATOM    550  CG  ASN A  67     -28.826  -5.991 -60.363  1.00234.63           C  
ANISOU  550  CG  ASN A  67    26150  33705  29295  -2928  -8420   1940       C  
ATOM    551  OD1 ASN A  67     -29.410  -6.758 -59.596  1.00235.63           O  
ANISOU  551  OD1 ASN A  67    26259  33765  29503  -3122  -8502   2120       O  
ATOM    552  ND2 ASN A  67     -29.467  -5.089 -61.097  1.00233.29           N  
ANISOU  552  ND2 ASN A  67    25965  33512  29161  -2873  -8345   1839       N  
ATOM    553  N   HIS A  68     -24.300  -5.561 -59.668  1.00233.11           N  
ANISOU  553  N   HIS A  68    25811  34083  28676  -2655  -8196   1645       N  
ATOM    554  CA  HIS A  68     -22.877  -5.824 -59.863  1.00234.12           C  
ANISOU  554  CA  HIS A  68    25965  34278  28714  -2451  -8250   1562       C  
ATOM    555  C   HIS A  68     -22.233  -6.332 -58.577  1.00234.73           C  
ANISOU  555  C   HIS A  68    25937  34509  28740  -2626  -8232   1646       C  
ATOM    556  O   HIS A  68     -21.440  -7.286 -58.600  1.00235.53           O  
ANISOU  556  O   HIS A  68    26132  34547  28810  -2463  -8406   1680       O  
ATOM    557  CB  HIS A  68     -22.183  -4.553 -60.357  1.00233.52           C  
ANISOU  557  CB  HIS A  68    25773  34381  28573  -2383  -8057   1376       C  
ATOM    558  CG  HIS A  68     -20.760  -4.758 -60.773  1.00234.64           C  
ANISOU  558  CG  HIS A  68    25939  34567  28644  -2141  -8129   1288       C  
ATOM    559  ND1 HIS A  68     -20.413  -5.372 -61.957  1.00235.43           N  
ANISOU  559  ND1 HIS A  68    26261  34454  28739  -1785  -8343   1274       N  
ATOM    560  CD2 HIS A  68     -19.596  -4.419 -60.169  1.00235.08           C  
ANISOU  560  CD2 HIS A  68    25824  34856  28641  -2206  -8012   1218       C  
ATOM    561  CE1 HIS A  68     -19.097  -5.406 -62.064  1.00236.07           C  
ANISOU  561  CE1 HIS A  68    26298  34638  28760  -1637  -8357   1207       C  
ATOM    562  NE2 HIS A  68     -18.577  -4.836 -60.991  1.00235.82           N  
ANISOU  562  NE2 HIS A  68    26018  34877  28704  -1890  -8166   1164       N  
ATOM    563  N   VAL A  69     -22.578  -5.715 -57.442  1.00229.13           N  
ANISOU  563  N   VAL A  69    25045  34002  28013  -2956  -8021   1693       N  
ATOM    564  CA  VAL A  69     -22.039  -6.146 -56.153  1.00230.35           C  
ANISOU  564  CA  VAL A  69    25112  34309  28103  -3135  -8002   1786       C  
ATOM    565  C   VAL A  69     -22.397  -7.600 -55.874  1.00232.01           C  
ANISOU  565  C   VAL A  69    25474  34323  28356  -3113  -8262   1974       C  
ATOM    566  O   VAL A  69     -21.567  -8.374 -55.381  1.00233.35           O  
ANISOU  566  O   VAL A  69    25668  34525  28468  -3062  -8377   2019       O  
ATOM    567  CB  VAL A  69     -22.530  -5.214 -55.029  1.00230.08           C  
ANISOU  567  CB  VAL A  69    24886  34509  28027  -3498  -7722   1831       C  
ATOM    568  CG1 VAL A  69     -22.180  -5.788 -53.670  1.00231.63           C  
ANISOU  568  CG1 VAL A  69    25030  34832  28147  -3687  -7741   1967       C  
ATOM    569  CG2 VAL A  69     -21.911  -3.835 -55.180  1.00228.84           C  
ANISOU  569  CG2 VAL A  69    24565  34580  27804  -3532  -7445   1643       C  
ATOM    570  N   ARG A  70     -23.632  -8.002 -56.189  1.00232.74           N  
ANISOU  570  N   ARG A  70    25666  34207  28556  -3155  -8361   2090       N  
ATOM    571  CA  ARG A  70     -24.024  -9.385 -55.928  1.00234.19           C  
ANISOU  571  CA  ARG A  70    25988  34195  28798  -3163  -8603   2283       C  
ATOM    572  C   ARG A  70     -23.359 -10.353 -56.901  1.00235.18           C  
ANISOU  572  C   ARG A  70    26314  34118  28928  -2822  -8840   2247       C  
ATOM    573  O   ARG A  70     -23.012 -11.479 -56.521  1.00236.11           O  
ANISOU  573  O   ARG A  70    26519  34160  29033  -2793  -9013   2367       O  
ATOM    574  CB  ARG A  70     -25.544  -9.528 -55.970  1.00233.91           C  
ANISOU  574  CB  ARG A  70    25984  33991  28902  -3327  -8645   2423       C  
ATOM    575  CG  ARG A  70     -26.238  -8.910 -54.770  1.00233.65           C  
ANISOU  575  CG  ARG A  70    25770  34146  28860  -3697  -8444   2538       C  
ATOM    576  CD  ARG A  70     -27.730  -9.182 -54.783  1.00234.35           C  
ANISOU  576  CD  ARG A  70    25881  34055  29106  -3859  -8514   2701       C  
ATOM    577  NE  ARG A  70     -28.395  -8.577 -53.633  1.00233.95           N  
ANISOU  577  NE  ARG A  70    25658  34197  29036  -4214  -8309   2829       N  
ATOM    578  CZ  ARG A  70     -28.526  -9.173 -52.452  1.00235.25           C  
ANISOU  578  CZ  ARG A  70    25788  34428  29168  -4449  -8342   3042       C  
ATOM    579  NH1 ARG A  70     -28.035 -10.391 -52.264  1.00236.22           N  
ANISOU  579  NH1 ARG A  70    26032  34437  29282  -4367  -8574   3144       N  
ATOM    580  NH2 ARG A  70     -29.145  -8.552 -51.458  1.00235.08           N  
ANISOU  580  NH2 ARG A  70    25618  34592  29111  -4765  -8141   3163       N  
ATOM    581  N   HIS A  71     -23.172  -9.939 -58.159  1.00236.04           N  
ANISOU  581  N   HIS A  71    26505  34136  29043  -2563  -8850   2096       N  
ATOM    582  CA  HIS A  71     -22.434 -10.778 -59.100  1.00236.88           C  
ANISOU  582  CA  HIS A  71    26806  34068  29128  -2230  -9047   2069       C  
ATOM    583  C   HIS A  71     -21.023 -11.052 -58.595  1.00237.73           C  
ANISOU  583  C   HIS A  71    26854  34349  29124  -2152  -9049   2032       C  
ATOM    584  O   HIS A  71     -20.583 -12.208 -58.534  1.00238.92           O  
ANISOU  584  O   HIS A  71    27127  34391  29261  -2043  -9233   2129       O  
ATOM    585  CB  HIS A  71     -22.388 -10.123 -60.480  1.00235.27           C  
ANISOU  585  CB  HIS A  71    26695  33773  28925  -1971  -9029   1918       C  
ATOM    586  CG  HIS A  71     -21.701 -10.957 -61.517  1.00236.12           C  
ANISOU  586  CG  HIS A  71    27030  33678  29009  -1627  -9222   1915       C  
ATOM    587  ND1 HIS A  71     -20.337 -10.920 -61.715  1.00236.25           N  
ANISOU  587  ND1 HIS A  71    27030  33810  28924  -1432  -9210   1832       N  
ATOM    588  CD2 HIS A  71     -22.185 -11.857 -62.405  1.00237.05           C  
ANISOU  588  CD2 HIS A  71    27399  33469  29199  -1450  -9427   1994       C  
ATOM    589  CE1 HIS A  71     -20.012 -11.758 -62.684  1.00236.99           C  
ANISOU  589  CE1 HIS A  71    27364  33661  29022  -1145  -9390   1873       C  
ATOM    590  NE2 HIS A  71     -21.115 -12.339 -63.120  1.00237.66           N  
ANISOU  590  NE2 HIS A  71    27623  33468  29210  -1152  -9523   1967       N  
ATOM    591  N   LEU A  72     -20.298  -9.996 -58.218  1.00237.77           N  
ANISOU  591  N   LEU A  72    26666  34622  29055  -2215  -8849   1893       N  
ATOM    592  CA  LEU A  72     -18.963 -10.201 -57.670  1.00238.25           C  
ANISOU  592  CA  LEU A  72    26642  34857  29026  -2160  -8854   1851       C  
ATOM    593  C   LEU A  72     -18.989 -10.838 -56.287  1.00239.71           C  
ANISOU  593  C   LEU A  72    26766  35132  29182  -2393  -8887   1999       C  
ATOM    594  O   LEU A  72     -17.942 -11.296 -55.817  1.00240.66           O  
ANISOU  594  O   LEU A  72    26854  35354  29232  -2326  -8950   1994       O  
ATOM    595  CB  LEU A  72     -18.193  -8.879 -57.633  1.00236.19           C  
ANISOU  595  CB  LEU A  72    26179  34846  28717  -2188  -8634   1663       C  
ATOM    596  CG  LEU A  72     -17.512  -8.477 -58.947  1.00234.64           C  
ANISOU  596  CG  LEU A  72    26038  34601  28512  -1880  -8652   1519       C  
ATOM    597  CD1 LEU A  72     -18.520  -8.067 -60.008  1.00233.77           C  
ANISOU  597  CD1 LEU A  72    26054  34313  28456  -1797  -8646   1499       C  
ATOM    598  CD2 LEU A  72     -16.508  -7.362 -58.712  1.00233.10           C  
ANISOU  598  CD2 LEU A  72    25613  34672  28280  -1931  -8459   1356       C  
ATOM    599  N   HIS A  73     -20.150 -10.884 -55.630  1.00236.94           N  
ANISOU  599  N   HIS A  73    26400  34746  28882  -2660  -8853   2139       N  
ATOM    600  CA  HIS A  73     -20.278 -11.669 -54.409  1.00238.41           C  
ANISOU  600  CA  HIS A  73    26573  34972  29040  -2862  -8928   2322       C  
ATOM    601  C   HIS A  73     -20.403 -13.155 -54.705  1.00240.07           C  
ANISOU  601  C   HIS A  73    26990  34930  29295  -2724  -9201   2472       C  
ATOM    602  O   HIS A  73     -19.937 -13.981 -53.912  1.00241.74           O  
ANISOU  602  O   HIS A  73    27219  35182  29451  -2764  -9310   2584       O  
ATOM    603  CB  HIS A  73     -21.481 -11.203 -53.588  1.00237.81           C  
ANISOU  603  CB  HIS A  73    26406  34950  29002  -3208  -8796   2448       C  
ATOM    604  CG  HIS A  73     -21.699 -12.001 -52.340  1.00240.24           C  
ANISOU  604  CG  HIS A  73    26711  35294  29275  -3430  -8880   2666       C  
ATOM    605  ND1 HIS A  73     -20.890 -11.886 -51.230  1.00241.81           N  
ANISOU  605  ND1 HIS A  73    26799  35733  29345  -3545  -8814   2675       N  
ATOM    606  CD2 HIS A  73     -22.629 -12.936 -52.031  1.00241.76           C  
ANISOU  606  CD2 HIS A  73    27002  35309  29546  -3559  -9035   2891       C  
ATOM    607  CE1 HIS A  73     -21.314 -12.711 -50.289  1.00243.58           C  
ANISOU  607  CE1 HIS A  73    27063  35934  29553  -3728  -8925   2901       C  
ATOM    608  NE2 HIS A  73     -22.369 -13.359 -50.750  1.00243.80           N  
ANISOU  608  NE2 HIS A  73    27213  35709  29711  -3748  -9058   3040       N  
ATOM    609  N   LYS A  74     -21.031 -13.519 -55.825  1.00238.50           N  
ANISOU  609  N   LYS A  74    26956  34469  29194  -2565  -9316   2481       N  
ATOM    610  CA  LYS A  74     -21.073 -14.927 -56.200  1.00240.18           C  
ANISOU  610  CA  LYS A  74    27378  34425  29454  -2421  -9571   2614       C  
ATOM    611  C   LYS A  74     -19.750 -15.388 -56.798  1.00240.54           C  
ANISOU  611  C   LYS A  74    27508  34468  29417  -2104  -9661   2525       C  
ATOM    612  O   LYS A  74     -19.343 -16.535 -56.578  1.00242.29           O  
ANISOU  612  O   LYS A  74    27839  34601  29621  -2032  -9834   2639       O  
ATOM    613  CB  LYS A  74     -22.221 -15.186 -57.177  1.00239.95           C  
ANISOU  613  CB  LYS A  74    27507  34097  29569  -2372  -9674   2660       C  
ATOM    614  CG  LYS A  74     -22.415 -16.658 -57.514  1.00241.86           C  
ANISOU  614  CG  LYS A  74    27970  34042  29886  -2271  -9939   2813       C  
ATOM    615  CD  LYS A  74     -22.856 -17.440 -56.283  1.00243.75           C  
ANISOU  615  CD  LYS A  74    28176  34283  30154  -2544 -10026   3032       C  
ATOM    616  CE  LYS A  74     -23.028 -18.920 -56.587  1.00245.77           C  
ANISOU  616  CE  LYS A  74    28650  34238  30495  -2460 -10295   3187       C  
ATOM    617  NZ  LYS A  74     -24.160 -19.172 -57.519  1.00245.82           N  
ANISOU  617  NZ  LYS A  74    28799  33926  30677  -2438 -10414   3221       N  
ATOM    618  N   ARG A  75     -19.065 -14.518 -57.546  1.00240.88           N  
ANISOU  618  N   ARG A  75    27501  34609  29412  -1916  -9548   2335       N  
ATOM    619  CA  ARG A  75     -17.720 -14.851 -58.008  1.00241.49           C  
ANISOU  619  CA  ARG A  75    27621  34724  29409  -1634  -9613   2260       C  
ATOM    620  C   ARG A  75     -16.745 -14.934 -56.841  1.00242.89           C  
ANISOU  620  C   ARG A  75    27638  35157  29492  -1724  -9585   2257       C  
ATOM    621  O   ARG A  75     -15.934 -15.864 -56.761  1.00244.79           O  
ANISOU  621  O   ARG A  75    27950  35373  29684  -1574  -9728   2312       O  
ATOM    622  CB  ARG A  75     -17.239 -13.826 -59.034  1.00240.02           C  
ANISOU  622  CB  ARG A  75    27403  34592  29203  -1437  -9496   2074       C  
ATOM    623  CG  ARG A  75     -15.796 -14.043 -59.476  1.00241.09           C  
ANISOU  623  CG  ARG A  75    27546  34792  29264  -1160  -9547   2005       C  
ATOM    624  CD  ARG A  75     -15.616 -15.363 -60.210  1.00242.66           C  
ANISOU  624  CD  ARG A  75    28006  34717  29477   -917  -9764   2130       C  
ATOM    625  NE  ARG A  75     -16.370 -15.406 -61.459  1.00242.16           N  
ANISOU  625  NE  ARG A  75    28161  34363  29485   -769  -9820   2142       N  
ATOM    626  CZ  ARG A  75     -15.920 -14.927 -62.614  1.00241.39           C  
ANISOU  626  CZ  ARG A  75    28152  34189  29376   -512  -9796   2053       C  
ATOM    627  NH1 ARG A  75     -14.717 -14.372 -62.681  1.00241.13           N  
ANISOU  627  NH1 ARG A  75    27987  34357  29274   -385  -9717   1952       N  
ATOM    628  NH2 ARG A  75     -16.671 -15.006 -63.704  1.00240.94           N  
ANISOU  628  NH2 ARG A  75    28321  33838  29386   -381  -9861   2069       N  
ATOM    629  N   VAL A  76     -16.804 -13.963 -55.927  1.00239.49           N  
ANISOU  629  N   VAL A  76    26995  34966  29033  -1968  -9401   2194       N  
ATOM    630  CA  VAL A  76     -15.917 -13.976 -54.769  1.00240.61           C  
ANISOU  630  CA  VAL A  76    26987  35346  29087  -2070  -9375   2187       C  
ATOM    631  C   VAL A  76     -16.217 -15.177 -53.882  1.00242.73           C  
ANISOU  631  C   VAL A  76    27346  35543  29337  -2187  -9538   2399       C  
ATOM    632  O   VAL A  76     -15.305 -15.808 -53.337  1.00244.31           O  
ANISOU  632  O   VAL A  76    27535  35830  29462  -2116  -9639   2426       O  
ATOM    633  CB  VAL A  76     -16.034 -12.652 -53.994  1.00239.47           C  
ANISOU  633  CB  VAL A  76    26618  35448  28921  -2332  -9132   2091       C  
ATOM    634  N   LEU A  77     -17.499 -15.516 -53.728  1.00242.50           N  
ANISOU  634  N   LEU A  77    27403  35353  29384  -2368  -9575   2557       N  
ATOM    635  CA  LEU A  77     -17.865 -16.692 -52.946  1.00244.76           C  
ANISOU  635  CA  LEU A  77    27784  35543  29670  -2490  -9745   2780       C  
ATOM    636  C   LEU A  77     -17.435 -17.978 -53.640  1.00246.47           C  
ANISOU  636  C   LEU A  77    28204  35540  29902  -2227  -9972   2846       C  
ATOM    637  O   LEU A  77     -17.131 -18.971 -52.969  1.00248.92           O  
ANISOU  637  O   LEU A  77    28572  35837  30168  -2246 -10118   2984       O  
ATOM    638  CB  LEU A  77     -19.373 -16.698 -52.689  1.00245.10           C  
ANISOU  638  CB  LEU A  77    27856  35454  29818  -2757  -9733   2940       C  
ATOM    639  CG  LEU A  77     -19.931 -17.809 -51.797  1.00247.85           C  
ANISOU  639  CG  LEU A  77    28284  35702  30185  -2946  -9898   3200       C  
ATOM    640  CD1 LEU A  77     -19.358 -17.710 -50.391  1.00248.86           C  
ANISOU  640  CD1 LEU A  77    28284  36098  30174  -3121  -9846   3256       C  
ATOM    641  CD2 LEU A  77     -21.452 -17.760 -51.765  1.00247.58           C  
ANISOU  641  CD2 LEU A  77    28270  35510  30289  -3187  -9894   3349       C  
ATOM    642  N   GLU A  78     -17.403 -17.979 -54.976  1.00242.65           N  
ANISOU  642  N   GLU A  78    27840  34882  29474  -1981 -10005   2758       N  
ATOM    643  CA  GLU A  78     -16.919 -19.145 -55.709  1.00243.55           C  
ANISOU  643  CA  GLU A  78    28157  34786  29595  -1717 -10202   2818       C  
ATOM    644  C   GLU A  78     -15.453 -19.422 -55.400  1.00244.52           C  
ANISOU  644  C   GLU A  78    28220  35089  29596  -1544 -10234   2762       C  
ATOM    645  O   GLU A  78     -15.043 -20.583 -55.288  1.00246.53           O  
ANISOU  645  O   GLU A  78    28598  35246  29827  -1440 -10406   2879       O  
ATOM    646  CB  GLU A  78     -17.114 -18.941 -57.211  1.00241.61           C  
ANISOU  646  CB  GLU A  78    28051  34333  29416  -1485 -10209   2729       C  
ATOM    647  CG  GLU A  78     -16.657 -20.116 -58.059  1.00242.72           C  
ANISOU  647  CG  GLU A  78    28427  34226  29570  -1213 -10402   2798       C  
ATOM    648  CD  GLU A  78     -16.857 -19.877 -59.542  1.00241.55           C  
ANISOU  648  CD  GLU A  78    28440  33857  29482   -984 -10409   2719       C  
ATOM    649  OE1 GLU A  78     -17.342 -18.787 -59.910  1.00239.74           O  
ANISOU  649  OE1 GLU A  78    28132  33679  29277  -1030 -10267   2607       O  
ATOM    650  OE2 GLU A  78     -16.523 -20.778 -60.340  1.00242.53           O  
ANISOU  650  OE2 GLU A  78    28779  33746  29624   -756 -10557   2773       O  
ATOM    651  N   SER A  79     -14.649 -18.367 -55.266  1.00240.62           N  
ANISOU  651  N   SER A  79    27533  34857  29036  -1512 -10077   2584       N  
ATOM    652  CA  SER A  79     -13.232 -18.514 -54.963  1.00242.02           C  
ANISOU  652  CA  SER A  79    27619  35223  29115  -1354 -10107   2513       C  
ATOM    653  C   SER A  79     -13.041 -19.178 -53.606  1.00244.34           C  
ANISOU  653  C   SER A  79    27869  35630  29339  -1514 -10193   2635       C  
ATOM    654  O   SER A  79     -13.382 -18.598 -52.570  1.00244.00           O  
ANISOU  654  O   SER A  79    27686  35753  29269  -1779 -10092   2639       O  
ATOM    655  CB  SER A  79     -12.534 -17.152 -54.996  1.00240.92           C  
ANISOU  655  CB  SER A  79    27255  35333  28949  -1345  -9919   2296       C  
ATOM    656  OG  SER A  79     -12.583 -16.585 -56.294  1.00238.41           O  
ANISOU  656  OG  SER A  79    26989  34914  28682  -1166  -9857   2193       O  
ATOM    657  N   GLU A  80     -12.502 -20.396 -53.603  1.00241.27           N  
ANISOU  657  N   GLU A  80    27610  35149  28913  -1356 -10378   2746       N  
ATOM    658  CA  GLU A  80     -12.305 -21.153 -52.369  1.00243.40           C  
ANISOU  658  CA  GLU A  80    27868  35505  29106  -1478 -10488   2879       C  
ATOM    659  C   GLU A  80     -11.091 -20.582 -51.647  1.00243.43           C  
ANISOU  659  C   GLU A  80    27661  35824  29009  -1447 -10429   2738       C  
ATOM    660  O   GLU A  80      -9.946 -20.857 -52.014  1.00243.25           O  
ANISOU  660  O   GLU A  80    27618  35861  28944  -1195 -10494   2666       O  
ATOM    661  CB  GLU A  80     -12.133 -22.637 -52.672  1.00245.80           C  
ANISOU  661  CB  GLU A  80    28387  35595  29411  -1309 -10705   3041       C  
ATOM    662  CG  GLU A  80     -12.238 -23.545 -51.452  1.00248.93           C  
ANISOU  662  CG  GLU A  80    28819  36017  29744  -1463 -10840   3224       C  
ATOM    663  CD  GLU A  80     -10.929 -23.685 -50.699  1.00250.86           C  
ANISOU  663  CD  GLU A  80    28946  36514  29855  -1356 -10884   3169       C  
ATOM    664  OE1 GLU A  80      -9.859 -23.579 -51.334  1.00250.89           O  
ANISOU  664  OE1 GLU A  80    28906  36588  29833  -1093 -10881   3040       O  
ATOM    665  OE2 GLU A  80     -10.971 -23.901 -49.469  1.00252.92           O  
ANISOU  665  OE2 GLU A  80    29159  36901  30037  -1535 -10929   3263       O  
ATOM    666  N   GLU A  81     -11.346 -19.759 -50.630  1.00239.07           N  
ANISOU  666  N   GLU A  81    26946  35466  28422  -1710 -10306   2702       N  
ATOM    667  CA  GLU A  81     -10.358 -19.132 -49.755  1.00240.00           C  
ANISOU  667  CA  GLU A  81    26856  35877  28455  -1749 -10249   2572       C  
ATOM    668  C   GLU A  81      -9.493 -18.102 -50.471  1.00238.50           C  
ANISOU  668  C   GLU A  81    26505  35812  28302  -1595 -10126   2330       C  
ATOM    669  O   GLU A  81      -8.655 -17.464 -49.823  1.00239.88           O  
ANISOU  669  O   GLU A  81    26487  36220  28438  -1636 -10072   2198       O  
ATOM    670  CB  GLU A  81      -9.448 -20.161 -49.069  1.00242.89           C  
ANISOU  670  CB  GLU A  81    27251  36316  28720  -1631 -10439   2649       C  
ATOM    671  CG  GLU A  81     -10.174 -21.041 -48.066  1.00245.12           C  
ANISOU  671  CG  GLU A  81    27652  36535  28947  -1827 -10554   2885       C  
ATOM    672  CD  GLU A  81      -9.263 -22.061 -47.418  1.00248.29           C  
ANISOU  672  CD  GLU A  81    28091  37008  29238  -1693 -10747   2960       C  
ATOM    673  OE1 GLU A  81      -8.092 -22.165 -47.839  1.00248.78           O  
ANISOU  673  OE1 GLU A  81    28095  37150  29279  -1431 -10799   2835       O  
ATOM    674  OE2 GLU A  81      -9.718 -22.758 -46.487  1.00250.63           O  
ANISOU  674  OE2 GLU A  81    28473  37284  29470  -1850 -10850   3152       O  
ATOM    675  N   GLN A  82      -9.663 -17.914 -51.778  1.00237.78           N  
ANISOU  675  N   GLN A  82    26488  35569  28290  -1425 -10087   2273       N  
ATOM    676  CA  GLN A  82      -8.996 -16.845 -52.519  1.00235.11           C  
ANISOU  676  CA  GLN A  82    26001  35333  27999  -1306  -9957   2062       C  
ATOM    677  C   GLN A  82      -9.953 -15.703 -52.821  1.00232.03           C  
ANISOU  677  C   GLN A  82    25560  34923  27676  -1489  -9757   1991       C  
ATOM    678  O   GLN A  82      -9.897 -15.091 -53.892  1.00229.84           O  
ANISOU  678  O   GLN A  82    25278  34594  27458  -1355  -9678   1883       O  
ATOM    679  CB  GLN A  82      -8.378 -17.384 -53.805  1.00235.13           C  
ANISOU  679  CB  GLN A  82    26118  35197  28025   -963 -10054   2057       C  
ATOM    680  CG  GLN A  82      -7.193 -18.308 -53.586  1.00237.97           C  
ANISOU  680  CG  GLN A  82    26475  35622  28321   -756 -10222   2095       C  
ATOM    681  CD  GLN A  82      -6.583 -18.790 -54.887  1.00238.48           C  
ANISOU  681  CD  GLN A  82    26655  35546  28409   -424 -10297   2117       C  
ATOM    682  OE1 GLN A  82      -7.086 -18.490 -55.970  1.00237.42           O  
ANISOU  682  OE1 GLN A  82    26630  35245  28333   -342 -10238   2111       O  
ATOM    683  NE2 GLN A  82      -5.489 -19.536 -54.787  1.00239.65           N  
ANISOU  683  NE2 GLN A  82    26789  35758  28511   -226 -10430   2153       N  
ATOM    684  N   VAL A  83     -10.853 -15.407 -51.880  1.00230.68           N  
ANISOU  684  N   VAL A  83    25358  34797  27491  -1795  -9673   2065       N  
ATOM    685  CA  VAL A  83     -11.805 -14.317 -52.064  1.00229.42           C  
ANISOU  685  CA  VAL A  83    25142  34637  27390  -1991  -9471   2013       C  
ATOM    686  C   VAL A  83     -11.075 -12.983 -52.127  1.00228.65           C  
ANISOU  686  C   VAL A  83    24820  34746  27312  -2016  -9287   1795       C  
ATOM    687  O   VAL A  83     -11.565 -12.021 -52.731  1.00226.81           O  
ANISOU  687  O   VAL A  83    24543  34498  27139  -2068  -9122   1706       O  
ATOM    688  CB  VAL A  83     -12.851 -14.343 -50.930  1.00229.68           C  
ANISOU  688  CB  VAL A  83    25178  34697  27393  -2324  -9423   2171       C  
ATOM    689  CG1 VAL A  83     -13.919 -13.276 -51.143  1.00227.89           C  
ANISOU  689  CG1 VAL A  83    24899  34461  27226  -2525  -9213   2140       C  
ATOM    690  CG2 VAL A  83     -13.465 -15.729 -50.794  1.00231.31           C  
ANISOU  690  CG2 VAL A  83    25590  34701  27596  -2312  -9626   2398       C  
ATOM    691  N   LEU A  84      -9.886 -12.907 -51.525  1.00219.71           N  
ANISOU  691  N   LEU A  84    23538  33802  26140  -1980  -9317   1707       N  
ATOM    692  CA  LEU A  84      -9.110 -11.675 -51.505  1.00218.92           C  
ANISOU  692  CA  LEU A  84    23202  33897  26079  -2028  -9151   1506       C  
ATOM    693  C   LEU A  84      -8.344 -11.428 -52.800  1.00218.09           C  
ANISOU  693  C   LEU A  84    23067  33744  26054  -1746  -9167   1373       C  
ATOM    694  O   LEU A  84      -7.912 -10.295 -53.038  1.00217.02           O  
ANISOU  694  O   LEU A  84    22743  33730  25982  -1797  -9002   1216       O  
ATOM    695  CB  LEU A  84      -8.150 -11.694 -50.310  1.00220.91           C  
ANISOU  695  CB  LEU A  84    23298  34365  26273  -2113  -9192   1467       C  
ATOM    696  CG  LEU A  84      -7.177 -12.872 -50.167  1.00223.25           C  
ANISOU  696  CG  LEU A  84    23645  34653  26526  -1877  -9444   1508       C  
ATOM    697  CD1 LEU A  84      -5.880 -12.657 -50.935  1.00223.47           C  
ANISOU  697  CD1 LEU A  84    23540  34735  26632  -1623  -9487   1346       C  
ATOM    698  CD2 LEU A  84      -6.893 -13.150 -48.697  1.00225.38           C  
ANISOU  698  CD2 LEU A  84    23855  35086  26694  -2044  -9509   1564       C  
ATOM    699  N   VAL A  85      -8.166 -12.448 -53.638  1.00222.31           N  
ANISOU  699  N   VAL A  85    23780  34107  26581  -1459  -9351   1449       N  
ATOM    700  CA  VAL A  85      -7.484 -12.254 -54.916  1.00221.37           C  
ANISOU  700  CA  VAL A  85    23655  33937  26521  -1178  -9370   1359       C  
ATOM    701  C   VAL A  85      -8.439 -11.662 -55.946  1.00219.64           C  
ANISOU  701  C   VAL A  85    23539  33569  26345  -1167  -9258   1348       C  
ATOM    702  O   VAL A  85      -8.205 -10.573 -56.485  1.00217.93           O  
ANISOU  702  O   VAL A  85    23185  33425  26192  -1169  -9113   1211       O  
ATOM    703  CB  VAL A  85      -6.873 -13.578 -55.409  1.00222.24           C  
ANISOU  703  CB  VAL A  85    23925  33930  26587   -872  -9594   1470       C  
ATOM    704  CG1 VAL A  85      -6.254 -13.395 -56.786  1.00221.43           C  
ANISOU  704  CG1 VAL A  85    23842  33756  26534   -576  -9607   1421       C  
ATOM    705  CG2 VAL A  85      -5.839 -14.084 -54.417  1.00224.57           C  
ANISOU  705  CG2 VAL A  85    24095  34392  26838   -864  -9707   1462       C  
ATOM    706  N   MET A  86      -9.532 -12.375 -56.236  1.00225.59           N  
ANISOU  706  N   MET A  86    24530  34109  27074  -1161  -9329   1496       N  
ATOM    707  CA  MET A  86     -10.590 -11.808 -57.064  1.00223.93           C  
ANISOU  707  CA  MET A  86    24419  33757  26907  -1185  -9231   1490       C  
ATOM    708  C   MET A  86     -11.210 -10.574 -56.425  1.00222.26           C  
ANISOU  708  C   MET A  86    24034  33690  26722  -1503  -9002   1405       C  
ATOM    709  O   MET A  86     -11.805  -9.754 -57.133  1.00220.84           O  
ANISOU  709  O   MET A  86    23862  33464  26585  -1519  -8879   1343       O  
ATOM    710  CB  MET A  86     -11.672 -12.855 -57.338  1.00223.45           C  
ANISOU  710  CB  MET A  86    24625  33435  26840  -1160  -9362   1673       C  
ATOM    711  CG  MET A  86     -11.232 -13.982 -58.256  1.00224.32           C  
ANISOU  711  CG  MET A  86    24952  33343  26935   -841  -9556   1772       C  
ATOM    712  SD  MET A  86     -10.785 -13.388 -59.900  1.00222.85           S  
ANISOU  712  SD  MET A  86    24839  33052  26782   -530  -9526   1684       S  
ATOM    713  CE  MET A  86     -12.387 -12.882 -60.523  1.00220.76           C  
ANISOU  713  CE  MET A  86    24719  32589  26570   -635  -9450   1697       C  
ATOM    714  N   TYR A  87     -11.091 -10.430 -55.104  1.00217.78           N  
ANISOU  714  N   TYR A  87    23324  33298  26123  -1753  -8940   1415       N  
ATOM    715  CA  TYR A  87     -11.505  -9.202 -54.441  1.00216.63           C  
ANISOU  715  CA  TYR A  87    22999  33322  25988  -2061  -8692   1344       C  
ATOM    716  C   TYR A  87     -10.507  -8.076 -54.675  1.00215.94           C  
ANISOU  716  C   TYR A  87    22682  33423  25945  -2053  -8535   1153       C  
ATOM    717  O   TYR A  87     -10.902  -6.906 -54.740  1.00214.36           O  
ANISOU  717  O   TYR A  87    22363  33317  25768  -2229  -8298   1073       O  
ATOM    718  CB  TYR A  87     -11.687  -9.457 -52.943  1.00218.01           C  
ANISOU  718  CB  TYR A  87    23118  33622  26093  -2324  -8680   1443       C  
ATOM    719  CG  TYR A  87     -12.166  -8.260 -52.156  1.00217.04           C  
ANISOU  719  CG  TYR A  87    22831  33685  25951  -2657  -8410   1405       C  
ATOM    720  CD1 TYR A  87     -13.484  -7.833 -52.239  1.00215.65           C  
ANISOU  720  CD1 TYR A  87    22710  33439  25788  -2831  -8279   1476       C  
ATOM    721  CD2 TYR A  87     -11.305  -7.566 -51.316  1.00217.67           C  
ANISOU  721  CD2 TYR A  87    22697  34012  25994  -2799  -8283   1304       C  
ATOM    722  CE1 TYR A  87     -13.928  -6.742 -51.518  1.00214.82           C  
ANISOU  722  CE1 TYR A  87    22459  33517  25646  -3133  -8013   1454       C  
ATOM    723  CE2 TYR A  87     -11.740  -6.475 -50.590  1.00216.88           C  
ANISOU  723  CE2 TYR A  87    22458  34094  25852  -3104  -8015   1277       C  
ATOM    724  CZ  TYR A  87     -13.053  -6.068 -50.694  1.00215.42           C  
ANISOU  724  CZ  TYR A  87    22338  33846  25666  -3268  -7874   1357       C  
ATOM    725  OH  TYR A  87     -13.493  -4.982 -49.973  1.00214.68           O  
ANISOU  725  OH  TYR A  87    22112  33947  25511  -3565  -7590   1338       O  
ATOM    726  N   HIS A  88      -9.220  -8.407 -54.810  1.00212.84           N  
ANISOU  726  N   HIS A  88    22211  33091  25568  -1858  -8653   1088       N  
ATOM    727  CA  HIS A  88      -8.225  -7.395 -55.151  1.00212.97           C  
ANISOU  727  CA  HIS A  88    21989  33272  25657  -1839  -8516    920       C  
ATOM    728  C   HIS A  88      -8.398  -6.923 -56.588  1.00212.02           C  
ANISOU  728  C   HIS A  88    21924  33042  25592  -1651  -8475    869       C  
ATOM    729  O   HIS A  88      -8.385  -5.717 -56.862  1.00211.16           O  
ANISOU  729  O   HIS A  88    21644  33061  25524  -1773  -8241    762       O  
ATOM    730  CB  HIS A  88      -6.814  -7.943 -54.932  1.00214.82           C  
ANISOU  730  CB  HIS A  88    22115  33592  25916  -1671  -8676    879       C  
ATOM    731  CG  HIS A  88      -5.731  -6.974 -55.292  1.00215.21           C  
ANISOU  731  CG  HIS A  88    21887  33812  26069  -1654  -8543    722       C  
ATOM    732  ND1 HIS A  88      -5.428  -5.874 -54.519  1.00214.83           N  
ANISOU  732  ND1 HIS A  88    21572  34009  26045  -1939  -8293    611       N  
ATOM    733  CD2 HIS A  88      -4.882  -6.938 -56.347  1.00216.29           C  
ANISOU  733  CD2 HIS A  88    21959  33929  26294  -1391  -8605    670       C  
ATOM    734  CE1 HIS A  88      -4.438  -5.203 -55.080  1.00216.29           C  
ANISOU  734  CE1 HIS A  88    21517  34327  26334  -1867  -8190    488       C  
ATOM    735  NE2 HIS A  88      -4.089  -5.828 -56.191  1.00217.39           N  
ANISOU  735  NE2 HIS A  88    21766  34309  26522  -1535  -8383    530       N  
ATOM    736  N   ARG A  89      -8.553  -7.864 -57.524  1.00219.29           N  
ANISOU  736  N   ARG A  89    23087  33739  26496  -1350  -8686    956       N  
ATOM    737  CA  ARG A  89      -8.862  -7.478 -58.897  1.00218.30           C  
ANISOU  737  CA  ARG A  89    23067  33478  26397  -1155  -8670    935       C  
ATOM    738  C   ARG A  89     -10.210  -6.774 -58.977  1.00216.52           C  
ANISOU  738  C   ARG A  89    22901  33203  26164  -1354  -8508    938       C  
ATOM    739  O   ARG A  89     -10.419  -5.926 -59.852  1.00216.04           O  
ANISOU  739  O   ARG A  89    22822  33132  26130  -1304  -8398    871       O  
ATOM    740  CB  ARG A  89      -8.844  -8.705 -59.809  1.00218.84           C  
ANISOU  740  CB  ARG A  89    23422  33301  26424   -807  -8915   1062       C  
ATOM    741  CG  ARG A  89      -7.501  -9.419 -59.863  1.00221.11           C  
ANISOU  741  CG  ARG A  89    23661  33635  26716   -577  -9069   1080       C  
ATOM    742  CD  ARG A  89      -6.442  -8.569 -60.549  1.00223.84           C  
ANISOU  742  CD  ARG A  89    23801  34095  27155   -438  -9005    966       C  
ATOM    743  NE  ARG A  89      -5.161  -9.266 -60.645  1.00226.29           N  
ANISOU  743  NE  ARG A  89    24052  34439  27488   -202  -9157    999       N  
ATOM    744  CZ  ARG A  89      -4.047  -8.720 -61.122  1.00229.56           C  
ANISOU  744  CZ  ARG A  89    24245  34962  28016    -64  -9133    927       C  
ATOM    745  NH1 ARG A  89      -4.050  -7.465 -61.549  1.00230.50           N  
ANISOU  745  NH1 ARG A  89    24172  35182  28224   -152  -8947    824       N  
ATOM    746  NH2 ARG A  89      -2.927  -9.429 -61.170  1.00232.54           N  
ANISOU  746  NH2 ARG A  89    24569  35361  28425    154  -9280    977       N  
ATOM    747  N   TYR A  90     -11.127  -7.102 -58.065  1.00218.15           N  
ANISOU  747  N   TYR A  90    23169  33386  26334  -1580  -8492   1026       N  
ATOM    748  CA  TYR A  90     -12.428  -6.443 -58.034  1.00216.61           C  
ANISOU  748  CA  TYR A  90    23005  33156  26142  -1789  -8333   1043       C  
ATOM    749  C   TYR A  90     -12.289  -4.977 -57.641  1.00216.27           C  
ANISOU  749  C   TYR A  90    22697  33365  26111  -2048  -8022    917       C  
ATOM    750  O   TYR A  90     -12.747  -4.080 -58.360  1.00215.49           O  
ANISOU  750  O   TYR A  90    22575  33273  26026  -2061  -7870    852       O  
ATOM    751  CB  TYR A  90     -13.357  -7.177 -57.065  1.00216.09           C  
ANISOU  751  CB  TYR A  90    23036  33025  26044  -1980  -8390   1194       C  
ATOM    752  N   TRP A  91     -11.656  -4.714 -56.494  1.00214.54           N  
ANISOU  752  N   TRP A  91    22279  33367  25871  -2257  -7909    883       N  
ATOM    753  CA  TRP A  91     -11.513  -3.337 -56.031  1.00213.89           C  
ANISOU  753  CA  TRP A  91    21941  33551  25777  -2526  -7570    768       C  
ATOM    754  C   TRP A  91     -10.627  -2.523 -56.965  1.00214.59           C  
ANISOU  754  C   TRP A  91    21860  33764  25910  -2398  -7442    617       C  
ATOM    755  O   TRP A  91     -10.945  -1.370 -57.280  1.00213.87           O  
ANISOU  755  O   TRP A  91    21642  33817  25801  -2526  -7153    522       O  
ATOM    756  CB  TRP A  91     -10.950  -3.309 -54.611  1.00214.17           C  
ANISOU  756  CB  TRP A  91    21819  33789  25766  -2747  -7499    765       C  
ATOM    757  CG  TRP A  91     -10.794  -1.920 -54.078  1.00213.25           C  
ANISOU  757  CG  TRP A  91    21453  33958  25616  -3023  -7127    640       C  
ATOM    758  CD1 TRP A  91     -11.792  -1.036 -53.789  1.00211.17           C  
ANISOU  758  CD1 TRP A  91    21162  33777  25295  -3269  -6855    643       C  
ATOM    759  CD2 TRP A  91      -9.564  -1.243 -53.791  1.00214.96           C  
ANISOU  759  CD2 TRP A  91    21404  34422  25850  -3075  -6966    484       C  
ATOM    760  NE1 TRP A  91     -11.261   0.145 -53.329  1.00210.67           N  
ANISOU  760  NE1 TRP A  91    20852  33999  25194  -3466  -6522    493       N  
ATOM    761  CE2 TRP A  91      -9.894   0.043 -53.322  1.00213.82           C  
ANISOU  761  CE2 TRP A  91    21095  34503  25643  -3356  -6581    388       C  
ATOM    762  CE3 TRP A  91      -8.215  -1.603 -53.881  1.00217.50           C  
ANISOU  762  CE3 TRP A  91    21602  34799  26239  -2910  -7102    413       C  
ATOM    763  CZ2 TRP A  91      -8.925   0.972 -52.944  1.00215.81           C  
ANISOU  763  CZ2 TRP A  91    21073  35030  25897  -3476  -6322    209       C  
ATOM    764  CZ3 TRP A  91      -7.254  -0.680 -53.505  1.00218.27           C  
ANISOU  764  CZ3 TRP A  91    21405  35172  26357  -3036  -6856    244       C  
ATOM    765  CH2 TRP A  91      -7.615   0.592 -53.042  1.00217.69           C  
ANISOU  765  CH2 TRP A  91    21180  35314  26218  -3316  -6466    136       C  
ATOM    766  N   GLU A  92      -9.510  -3.099 -57.416  1.00215.15           N  
ANISOU  766  N   GLU A  92    21910  33806  26030  -2144  -7633    594       N  
ATOM    767  CA  GLU A  92      -8.620  -2.365 -58.308  1.00217.53           C  
ANISOU  767  CA  GLU A  92    22016  34258  26376  -2013  -7503    467       C  
ATOM    768  C   GLU A  92      -9.216  -2.217 -59.703  1.00218.48           C  
ANISOU  768  C   GLU A  92    22302  34222  26488  -1790  -7547    486       C  
ATOM    769  O   GLU A  92      -8.767  -1.358 -60.470  1.00220.51           O  
ANISOU  769  O   GLU A  92    22375  34670  26738  -1715  -7346    369       O  
ATOM    770  CB  GLU A  92      -7.251  -3.050 -58.357  1.00219.72           C  
ANISOU  770  CB  GLU A  92    22207  34555  26720  -1799  -7702    459       C  
ATOM    771  CG  GLU A  92      -6.167  -2.254 -59.072  1.00222.95           C  
ANISOU  771  CG  GLU A  92    22317  35208  27185  -1689  -7513    315       C  
ATOM    772  CD  GLU A  92      -4.795  -2.887 -58.944  1.00225.50           C  
ANISOU  772  CD  GLU A  92    22505  35579  27596  -1514  -7688    309       C  
ATOM    773  OE1 GLU A  92      -4.689  -3.960 -58.313  1.00225.07           O  
ANISOU  773  OE1 GLU A  92    22614  35359  27543  -1472  -7970    414       O  
ATOM    774  OE2 GLU A  92      -3.820  -2.307 -59.467  1.00228.17           O  
ANISOU  774  OE2 GLU A  92    22547  36155  27994  -1401  -7516    176       O  
ATOM    775  N   GLU A  93     -10.223  -3.024 -60.044  1.00222.23           N  
ANISOU  775  N   GLU A  93    23105  34386  26946  -1671  -7781    615       N  
ATOM    776  CA  GLU A  93     -11.038  -2.807 -61.231  1.00222.46           C  
ANISOU  776  CA  GLU A  93    23327  34241  26958  -1502  -7818    638       C  
ATOM    777  C   GLU A  93     -12.381  -2.160 -60.902  1.00220.14           C  
ANISOU  777  C   GLU A  93    23058  33955  26630  -1766  -7629    640       C  
ATOM    778  O   GLU A  93     -13.316  -2.252 -61.703  1.00220.55           O  
ANISOU  778  O   GLU A  93    23330  33792  26675  -1639  -7727    688       O  
ATOM    779  CB  GLU A  93     -11.266  -4.122 -61.980  1.00222.04           C  
ANISOU  779  CB  GLU A  93    23631  33825  26908  -1155  -8183    764       C  
ATOM    780  CG  GLU A  93     -10.045  -4.679 -62.695  1.00225.49           C  
ANISOU  780  CG  GLU A  93    24101  34200  27374   -812  -8372    783       C  
ATOM    781  CD  GLU A  93     -10.343  -5.985 -63.411  1.00225.25           C  
ANISOU  781  CD  GLU A  93    24453  33820  27314   -488  -8659    921       C  
ATOM    782  OE1 GLU A  93     -11.463  -6.514 -63.243  1.00222.58           O  
ANISOU  782  OE1 GLU A  93    24310  33326  26936   -562  -8707   1000       O  
ATOM    783  OE2 GLU A  93      -9.461  -6.481 -64.142  1.00228.01           O  
ANISOU  783  OE2 GLU A  93    24900  34045  27689   -169  -8811    968       O  
ATOM    784  N   TYR A  94     -12.502  -1.520 -59.738  1.00220.32           N  
ANISOU  784  N   TYR A  94    22870  34210  26631  -2118  -7365    596       N  
ATOM    785  CA  TYR A  94     -13.765  -0.898 -59.358  1.00217.56           C  
ANISOU  785  CA  TYR A  94    22532  33880  26250  -2373  -7170    615       C  
ATOM    786  C   TYR A  94     -13.595   0.550 -58.910  1.00217.49           C  
ANISOU  786  C   TYR A  94    22225  34225  26186  -2653  -6728    468       C  
ATOM    787  O   TYR A  94     -14.504   1.369 -59.089  1.00215.70           O  
ANISOU  787  O   TYR A  94    21982  34053  25920  -2786  -6511    436       O  
ATOM    788  CB  TYR A  94     -14.442  -1.709 -58.250  1.00215.89           C  
ANISOU  788  CB  TYR A  94    22427  33560  26041  -2536  -7285    755       C  
ATOM    789  CG  TYR A  94     -15.774  -1.143 -57.811  1.00214.77           C  
ANISOU  789  CG  TYR A  94    22291  33435  25879  -2797  -7098    806       C  
ATOM    790  CD1 TYR A  94     -16.907  -1.288 -58.601  1.00214.22           C  
ANISOU  790  CD1 TYR A  94    22407  33143  25842  -2699  -7200    863       C  
ATOM    791  CD2 TYR A  94     -15.898  -0.461 -56.607  1.00215.34           C  
ANISOU  791  CD2 TYR A  94    22183  33744  25894  -3131  -6822    800       C  
ATOM    792  CE1 TYR A  94     -18.126  -0.770 -58.204  1.00213.75           C  
ANISOU  792  CE1 TYR A  94    22332  33103  25780  -2935  -7033    915       C  
ATOM    793  CE2 TYR A  94     -17.113   0.059 -56.201  1.00214.55           C  
ANISOU  793  CE2 TYR A  94    22084  33665  25770  -3363  -6644    861       C  
ATOM    794  CZ  TYR A  94     -18.224  -0.098 -57.004  1.00213.24           C  
ANISOU  794  CZ  TYR A  94    22082  33283  25658  -3268  -6750    920       C  
ATOM    795  OH  TYR A  94     -19.436   0.418 -56.604  1.00210.86           O  
ANISOU  795  OH  TYR A  94    21763  33008  25348  -3498  -6577    986       O  
ATOM    796  N   SER A  95     -12.440   0.880 -58.330  1.00215.52           N  
ANISOU  796  N   SER A  95    21736  34222  25932  -2737  -6577    363       N  
ATOM    797  CA  SER A  95     -12.254   2.203 -57.740  1.00214.86           C  
ANISOU  797  CA  SER A  95    21373  34475  25790  -3017  -6129    202       C  
ATOM    798  C   SER A  95     -12.194   3.287 -58.811  1.00213.38           C  
ANISOU  798  C   SER A  95    21039  34469  25565  -2939  -5839     14       C  
ATOM    799  O   SER A  95     -12.959   4.261 -58.773  1.00212.00           O  
ANISOU  799  O   SER A  95    20805  34416  25328  -3120  -5527    -62       O  
ATOM    800  CB  SER A  95     -10.988   2.217 -56.880  1.00216.44           C  
ANISOU  800  CB  SER A  95    21360  34869  26009  -3098  -6067    120       C  
ATOM    801  OG  SER A  95      -9.829   2.032 -57.674  1.00217.12           O  
ANISOU  801  OG  SER A  95    21331  35007  26158  -2843  -6152     27       O  
ATOM    802  N   LYS A  96     -11.280   3.138 -59.776  1.00213.59           N  
ANISOU  802  N   LYS A  96    20994  34542  25618  -2651  -5918    -76       N  
ATOM    803  CA  LYS A  96     -11.142   4.141 -60.829  1.00217.06           C  
ANISOU  803  CA  LYS A  96    21489  34884  26101  -2414  -5453   -311       C  
ATOM    804  C   LYS A  96     -12.437   4.301 -61.613  1.00216.50           C  
ANISOU  804  C   LYS A  96    21716  34544  26000  -2300  -5436   -258       C  
ATOM    805  O   LYS A  96     -12.805   5.418 -61.998  1.00217.46           O  
ANISOU  805  O   LYS A  96    21860  34652  26114  -2289  -4970   -433       O  
ATOM    806  CB  LYS A  96      -9.991   3.767 -61.764  1.00221.41           C  
ANISOU  806  CB  LYS A  96    22165  35182  26780  -1966  -5426   -401       C  
ATOM    807  CG  LYS A  96      -8.615   3.810 -61.116  1.00222.58           C  
ANISOU  807  CG  LYS A  96    21991  35584  26996  -2042  -5349   -507       C  
ATOM    808  CD  LYS A  96      -7.525   3.456 -62.116  1.00226.64           C  
ANISOU  808  CD  LYS A  96    22638  35816  27657  -1576  -5292   -589       C  
ATOM    809  CE  LYS A  96      -6.141   3.581 -61.500  1.00227.19           C  
ANISOU  809  CE  LYS A  96    22356  36138  27827  -1648  -5185   -714       C  
ATOM    810  NZ  LYS A  96      -5.909   2.562 -60.440  1.00224.03           N  
ANISOU  810  NZ  LYS A  96    21790  35965  27367  -1870  -5718   -513       N  
ATOM    811  N   GLY A  97     -13.145   3.197 -61.858  1.00220.48           N  
ANISOU  811  N   GLY A  97    22450  34829  26493  -2212  -5946    -21       N  
ATOM    812  CA  GLY A  97     -14.432   3.290 -62.525  1.00219.04           C  
ANISOU  812  CA  GLY A  97    22527  34402  26294  -2130  -5987     39       C  
ATOM    813  C   GLY A  97     -15.471   4.005 -61.683  1.00215.43           C  
ANISOU  813  C   GLY A  97    21888  34208  25758  -2558  -5830     67       C  
ATOM    814  O   GLY A  97     -16.317   4.732 -62.211  1.00215.73           O  
ANISOU  814  O   GLY A  97    22047  34134  25788  -2512  -5578     -8       O  
ATOM    815  N   ALA A  98     -15.421   3.813 -60.363  1.00215.36           N  
ANISOU  815  N   ALA A  98    21718  34369  25740  -2890  -5866    157       N  
ATOM    816  CA  ALA A  98     -16.345   4.512 -59.477  1.00213.32           C  
ANISOU  816  CA  ALA A  98    21398  34206  25449  -3224  -5589    172       C  
ATOM    817  C   ALA A  98     -16.097   6.014 -59.503  1.00213.47           C  
ANISOU  817  C   ALA A  98    21142  34589  25379  -3382  -5068    -74       C  
ATOM    818  O   ALA A  98     -17.040   6.810 -59.602  1.00212.47           O  
ANISOU  818  O   ALA A  98    21002  34523  25203  -3512  -4829   -113       O  
ATOM    819  CB  ALA A  98     -16.223   3.967 -58.054  1.00212.96           C  
ANISOU  819  CB  ALA A  98    21347  34143  25425  -3436  -5648    294       C  
ATOM    820  N   ASP A  99     -14.828   6.423 -59.422  1.00213.12           N  
ANISOU  820  N   ASP A  99    20865  34784  25328  -3367  -4868   -260       N  
ATOM    821  CA  ASP A  99     -14.511   7.846 -59.487  1.00215.28           C  
ANISOU  821  CA  ASP A  99    20975  35237  25583  -3434  -4262   -536       C  
ATOM    822  C   ASP A  99     -14.880   8.432 -60.844  1.00218.92           C  
ANISOU  822  C   ASP A  99    21718  35363  26099  -3066  -3950   -672       C  
ATOM    823  O   ASP A  99     -15.391   9.556 -60.927  1.00219.53           O  
ANISOU  823  O   ASP A  99    21773  35500  26138  -3156  -3503   -811       O  
ATOM    824  CB  ASP A  99     -13.028   8.071 -59.190  1.00216.53           C  
ANISOU  824  CB  ASP A  99    20908  35568  25796  -3415  -4082   -713       C  
ATOM    825  CG  ASP A  99     -12.668   9.541 -59.110  1.00217.96           C  
ANISOU  825  CG  ASP A  99    20916  35920  25981  -3520  -3437   -999       C  
ATOM    826  OD1 ASP A  99     -13.023  10.189 -58.103  1.00215.04           O  
ANISOU  826  OD1 ASP A  99    20328  35867  25510  -3919  -3271  -1023       O  
ATOM    827  OD2 ASP A  99     -12.030  10.051 -60.056  1.00222.05           O  
ANISOU  827  OD2 ASP A  99    21525  36245  26601  -3200  -3084  -1199       O  
ATOM    828  N   TYR A 100     -14.629   7.683 -61.922  1.00215.06           N  
ANISOU  828  N   TYR A 100    21512  34511  25689  -2637  -4177   -633       N  
ATOM    829  CA  TYR A 100     -15.013   8.152 -63.250  1.00218.46           C  
ANISOU  829  CA  TYR A 100    22258  34594  26153  -2253  -3924   -748       C  
ATOM    830  C   TYR A 100     -16.524   8.292 -63.381  1.00216.17           C  
ANISOU  830  C   TYR A 100    22110  34217  25807  -2348  -4013   -638       C  
ATOM    831  O   TYR A 100     -17.003   9.194 -64.079  1.00218.76           O  
ANISOU  831  O   TYR A 100    22582  34416  26123  -2198  -3632   -780       O  
ATOM    832  CB  TYR A 100     -14.465   7.210 -64.322  1.00221.99           C  
ANISOU  832  CB  TYR A 100    23004  34662  26680  -1776  -4205   -705       C  
ATOM    833  CG  TYR A 100     -12.966   7.297 -64.510  1.00226.19           C  
ANISOU  833  CG  TYR A 100    23440  35204  27298  -1582  -3985   -863       C  
ATOM    834  CD1 TYR A 100     -12.243   8.370 -64.006  1.00227.02           C  
ANISOU  834  CD1 TYR A 100    23251  35582  27423  -1767  -3477  -1081       C  
ATOM    835  CD2 TYR A 100     -12.273   6.305 -65.194  1.00228.65           C  
ANISOU  835  CD2 TYR A 100    23950  35244  27683  -1214  -4282   -796       C  
ATOM    836  CE1 TYR A 100     -10.873   8.454 -64.176  1.00230.52           C  
ANISOU  836  CE1 TYR A 100    23581  36029  27978  -1596  -3273  -1229       C  
ATOM    837  CE2 TYR A 100     -10.904   6.380 -65.368  1.00232.44           C  
ANISOU  837  CE2 TYR A 100    24326  35727  28263  -1032  -4070   -935       C  
ATOM    838  CZ  TYR A 100     -10.209   7.457 -64.858  1.00233.65           C  
ANISOU  838  CZ  TYR A 100    24167  36156  28455  -1226  -3567  -1152       C  
ATOM    839  OH  TYR A 100      -8.846   7.535 -65.030  1.00237.46           O  
ANISOU  839  OH  TYR A 100    24521  36635  29068  -1051  -3355  -1293       O  
ATOM    840  N   MET A 101     -17.292   7.417 -62.726  1.00222.95           N  
ANISOU  840  N   MET A 101    22931  35140  26640  -2588  -4503   -385       N  
ATOM    841  CA  MET A 101     -18.742   7.581 -62.725  1.00220.13           C  
ANISOU  841  CA  MET A 101    22652  34733  26255  -2727  -4576   -276       C  
ATOM    842  C   MET A 101     -19.160   8.791 -61.900  1.00219.15           C  
ANISOU  842  C   MET A 101    22274  34941  26054  -3104  -4121   -372       C  
ATOM    843  O   MET A 101     -20.134   9.473 -62.240  1.00219.14           O  
ANISOU  843  O   MET A 101    22358  34871  26035  -3106  -3906   -409       O  
ATOM    844  CB  MET A 101     -19.428   6.318 -62.203  1.00216.20           C  
ANISOU  844  CB  MET A 101    22162  34210  25773  -2899  -5200     24       C  
ATOM    845  CG  MET A 101     -19.331   5.122 -63.132  1.00217.14           C  
ANISOU  845  CG  MET A 101    22590  33945  25968  -2518  -5678    137       C  
ATOM    846  SD  MET A 101     -20.289   3.715 -62.538  1.00213.87           S  
ANISOU  846  SD  MET A 101    22254  33385  25622  -2694  -6309    463       S  
ATOM    847  CE  MET A 101     -19.272   3.155 -61.176  1.00213.61           C  
ANISOU  847  CE  MET A 101    22087  33459  25617  -2874  -6283    504       C  
ATOM    848  N   ASP A 102     -18.441   9.071 -60.809  1.00221.39           N  
ANISOU  848  N   ASP A 102    22249  35584  26286  -3421  -3977   -416       N  
ATOM    849  CA  ASP A 102     -18.750  10.260 -60.020  1.00220.26           C  
ANISOU  849  CA  ASP A 102    21875  35756  26058  -3773  -3522   -526       C  
ATOM    850  C   ASP A 102     -18.489  11.527 -60.826  1.00223.67           C  
ANISOU  850  C   ASP A 102    22383  36102  26499  -3557  -2914   -809       C  
ATOM    851  O   ASP A 102     -19.256  12.494 -60.744  1.00222.76           O  
ANISOU  851  O   ASP A 102    22244  36065  26330  -3695  -2558   -878       O  
ATOM    852  CB  ASP A 102     -17.935  10.260 -58.726  1.00218.28           C  
ANISOU  852  CB  ASP A 102    21304  35886  25746  -4124  -3518   -531       C  
ATOM    853  CG  ASP A 102     -18.437  11.280 -57.718  1.00216.32           C  
ANISOU  853  CG  ASP A 102    20978  35789  25423  -4445  -3083   -566       C  
ATOM    854  OD1 ASP A 102     -19.421  11.990 -58.016  1.00216.38           O  
ANISOU  854  OD1 ASP A 102    21001  35819  25392  -4512  -2862   -597       O  
ATOM    855  OD2 ASP A 102     -17.847  11.371 -56.621  1.00214.99           O  
ANISOU  855  OD2 ASP A 102    20746  35715  25223  -4617  -2974   -562       O  
ATOM    856  N   CYS A 103     -17.413  11.538 -61.617  1.00225.33           N  
ANISOU  856  N   CYS A 103    22693  36141  26780  -3209  -2774   -969       N  
ATOM    857  CA  CYS A 103     -17.188  12.656 -62.527  1.00224.36           C  
ANISOU  857  CA  CYS A 103    22696  35873  26677  -2946  -2205  -1225       C  
ATOM    858  C   CYS A 103     -18.201  12.660 -63.665  1.00223.43           C  
ANISOU  858  C   CYS A 103    22930  35400  26563  -2625  -2243  -1191       C  
ATOM    859  O   CYS A 103     -18.478  13.716 -64.245  1.00223.68           O  
ANISOU  859  O   CYS A 103    23066  35351  26571  -2495  -1766  -1364       O  
ATOM    860  CB  CYS A 103     -15.767  12.607 -63.088  1.00225.15           C  
ANISOU  860  CB  CYS A 103    22816  35860  26870  -2644  -2047  -1391       C  
ATOM    861  SG  CYS A 103     -14.465  12.874 -61.864  1.00226.37           S  
ANISOU  861  SG  CYS A 103    22538  36427  27044  -2987  -1895  -1505       S  
ATOM    862  N   LEU A 104     -18.764  11.495 -63.993  1.00227.43           N  
ANISOU  862  N   LEU A 104    23626  35688  27100  -2492  -2809   -973       N  
ATOM    863  CA  LEU A 104     -19.739  11.398 -65.070  1.00228.50           C  
ANISOU  863  CA  LEU A 104    24099  35473  27246  -2181  -2920   -936       C  
ATOM    864  C   LEU A 104     -21.120  11.891 -64.654  1.00225.62           C  
ANISOU  864  C   LEU A 104    23670  35221  26835  -2457  -2873   -855       C  
ATOM    865  O   LEU A 104     -21.961  12.151 -65.522  1.00227.14           O  
ANISOU  865  O   LEU A 104    24108  35163  27030  -2219  -2834   -877       O  
ATOM    866  CB  LEU A 104     -19.817   9.949 -65.566  1.00227.57           C  
ANISOU  866  CB  LEU A 104    24205  35071  27191  -1944  -3561   -739       C  
ATOM    867  CG  LEU A 104     -20.677   9.601 -66.785  1.00228.28           C  
ANISOU  867  CG  LEU A 104    24687  34744  27307  -1560  -3792   -696       C  
ATOM    868  CD1 LEU A 104     -20.183  10.313 -68.030  1.00231.13           C  
ANISOU  868  CD1 LEU A 104    25333  34832  27656  -1090  -3369   -930       C  
ATOM    869  CD2 LEU A 104     -20.670   8.106 -67.007  1.00227.91           C  
ANISOU  869  CD2 LEU A 104    24799  34477  27321  -1417  -4454   -488       C  
ATOM    870  N   TYR A 105     -21.366  12.043 -63.356  1.00235.06           N  
ANISOU  870  N   TYR A 105    24546  36782  27986  -2939  -2866   -765       N  
ATOM    871  CA  TYR A 105     -22.652  12.483 -62.829  1.00232.26           C  
ANISOU  871  CA  TYR A 105    24096  36559  27593  -3237  -2813   -669       C  
ATOM    872  C   TYR A 105     -22.524  13.831 -62.129  1.00231.98           C  
ANISOU  872  C   TYR A 105    23827  36847  27469  -3525  -2212   -839       C  
ATOM    873  O   TYR A 105     -23.083  14.048 -61.052  1.00229.36           O  
ANISOU  873  O   TYR A 105    23266  36797  27082  -3941  -2187   -738       O  
ATOM    874  CB  TYR A 105     -23.235  11.439 -61.879  1.00228.11           C  
ANISOU  874  CB  TYR A 105    23425  36158  27087  -3565  -3344   -382       C  
ATOM    875  CG  TYR A 105     -23.684  10.166 -62.559  1.00228.04           C  
ANISOU  875  CG  TYR A 105    23655  35814  27175  -3319  -3942   -196       C  
ATOM    876  CD1 TYR A 105     -23.875  10.118 -63.934  1.00229.86           C  
ANISOU  876  CD1 TYR A 105    24221  35660  27455  -2858  -3981   -278       C  
ATOM    877  CD2 TYR A 105     -23.913   9.009 -61.826  1.00227.25           C  
ANISOU  877  CD2 TYR A 105    23460  35772  27111  -3543  -4467     60       C  
ATOM    878  CE1 TYR A 105     -24.284   8.957 -64.558  1.00229.89           C  
ANISOU  878  CE1 TYR A 105    24454  35347  27545  -2633  -4541   -118       C  
ATOM    879  CE2 TYR A 105     -24.322   7.843 -62.442  1.00228.03           C  
ANISOU  879  CE2 TYR A 105    23778  35556  27307  -3328  -5014    225       C  
ATOM    880  CZ  TYR A 105     -24.506   7.822 -63.808  1.00228.59           C  
ANISOU  880  CZ  TYR A 105    24176  35248  27429  -2876  -5056    132       C  
ATOM    881  OH  TYR A 105     -24.914   6.663 -64.425  1.00228.75           O  
ANISOU  881  OH  TYR A 105    24426  34945  27544  -2661  -5613    287       O  
ATOM    882  N   ARG A 106     -21.778  14.756 -62.736  1.00238.91           N  
ANISOU  882  N   ARG A 106    24770  37675  28332  -3302  -1707  -1100       N  
ATOM    883  CA  ARG A 106     -21.591  16.069 -62.127  1.00238.64           C  
ANISOU  883  CA  ARG A 106    24526  37926  28219  -3560  -1114  -1282       C  
ATOM    884  C   ARG A 106     -22.883  16.878 -62.155  1.00237.80           C  
ANISOU  884  C   ARG A 106    24458  37835  28061  -3665   -868  -1271       C  
ATOM    885  O   ARG A 106     -23.345  17.367 -61.117  1.00235.32           O  
ANISOU  885  O   ARG A 106    23914  37821  27676  -4073   -715  -1226       O  
ATOM    886  CB  ARG A 106     -20.464  16.821 -62.836  1.00242.54           C  
ANISOU  886  CB  ARG A 106    25090  38328  28736  -3276   -632  -1563       C  
ATOM    887  CG  ARG A 106     -20.146  18.173 -62.224  1.00241.10           C  
ANISOU  887  CG  ARG A 106    24689  38430  28488  -3537     -9  -1773       C  
ATOM    888  CD  ARG A 106     -19.623  18.020 -60.805  1.00237.83           C  
ANISOU  888  CD  ARG A 106    23923  38405  28035  -3992   -109  -1726       C  
ATOM    889  NE  ARG A 106     -18.410  17.209 -60.754  1.00238.47           N  
ANISOU  889  NE  ARG A 106    23934  38478  28194  -3894   -378  -1730       N  
ATOM    890  CZ  ARG A 106     -17.185  17.684 -60.950  1.00238.57           C  
ANISOU  890  CZ  ARG A 106    23867  38511  28269  -3781    -44  -1956       C  
ATOM    891  NH1 ARG A 106     -17.004  18.972 -61.208  1.00237.10           N  
ANISOU  891  NH1 ARG A 106    23666  38349  28072  -3759    582  -2199       N  
ATOM    892  NH2 ARG A 106     -16.139  16.871 -60.885  1.00239.64           N  
ANISOU  892  NH2 ARG A 106    23928  38636  28486  -3691   -329  -1937       N  
ATOM    893  N   TYR A 107     -23.484  17.029 -63.339  1.00247.55           N  
ANISOU  893  N   TYR A 107    25992  38743  29325  -3290   -830  -1310       N  
ATOM    894  CA  TYR A 107     -24.749  17.748 -63.431  1.00247.18           C  
ANISOU  894  CA  TYR A 107    25988  38688  29240  -3357   -630  -1292       C  
ATOM    895  C   TYR A 107     -25.883  17.001 -62.743  1.00243.94           C  
ANISOU  895  C   TYR A 107    25470  38355  28863  -3645  -1097  -1012       C  
ATOM    896  O   TYR A 107     -26.864  17.630 -62.333  1.00242.17           O  
ANISOU  896  O   TYR A 107    25153  38257  28605  -3867   -906   -970       O  
ATOM    897  CB  TYR A 107     -25.114  18.013 -64.893  1.00251.94           C  
ANISOU  897  CB  TYR A 107    26956  38906  29864  -2858   -528  -1398       C  
ATOM    898  CG  TYR A 107     -26.369  18.844 -65.053  1.00251.38           C  
ANISOU  898  CG  TYR A 107    26935  38822  29755  -2893   -285  -1404       C  
ATOM    899  CD1 TYR A 107     -26.346  20.216 -64.840  1.00250.07           C  
ANISOU  899  CD1 TYR A 107    26685  38831  29501  -3006    363  -1589       C  
ATOM    900  CD2 TYR A 107     -27.578  18.255 -65.401  1.00251.00           C  
ANISOU  900  CD2 TYR A 107    27008  38590  29771  -2818   -707  -1224       C  
ATOM    901  CE1 TYR A 107     -27.489  20.981 -64.977  1.00249.39           C  
ANISOU  901  CE1 TYR A 107    26642  38736  29377  -3031    592  -1590       C  
ATOM    902  CE2 TYR A 107     -28.727  19.012 -65.539  1.00250.42           C  
ANISOU  902  CE2 TYR A 107    26962  38508  29678  -2845   -493  -1228       C  
ATOM    903  CZ  TYR A 107     -28.676  20.374 -65.327  1.00250.25           C  
ANISOU  903  CZ  TYR A 107    26863  38665  29555  -2947    160  -1408       C  
ATOM    904  OH  TYR A 107     -29.816  21.132 -65.465  1.00250.96           O  
ANISOU  904  OH  TYR A 107    26982  38747  29624  -2964    380  -1407       O  
ATOM    905  N   LEU A 108     -25.769  15.677 -62.609  1.00244.77           N  
ANISOU  905  N   LEU A 108    25585  38378  29040  -3644  -1690   -818       N  
ATOM    906  CA  LEU A 108     -26.772  14.917 -61.872  1.00240.96           C  
ANISOU  906  CA  LEU A 108    24979  37971  28603  -3943  -2126   -543       C  
ATOM    907  C   LEU A 108     -26.845  15.352 -60.416  1.00237.20           C  
ANISOU  907  C   LEU A 108    24175  37909  28043  -4458  -1924   -483       C  
ATOM    908  O   LEU A 108     -27.891  15.202 -59.773  1.00234.86           O  
ANISOU  908  O   LEU A 108    23763  37708  27765  -4738  -2066   -293       O  
ATOM    909  CB  LEU A 108     -26.466  13.420 -61.965  1.00240.31           C  
ANISOU  909  CB  LEU A 108    24971  37730  28607  -3846  -2768   -360       C  
ATOM    910  CG  LEU A 108     -27.441  12.461 -61.277  1.00237.03           C  
ANISOU  910  CG  LEU A 108    24452  37342  28265  -4123  -3271    -61       C  
ATOM    911  CD1 LEU A 108     -28.823  12.549 -61.906  1.00237.54           C  
ANISOU  911  CD1 LEU A 108    24650  37184  28420  -4014  -3375     12       C  
ATOM    912  CD2 LEU A 108     -26.915  11.033 -61.313  1.00235.70           C  
ANISOU  912  CD2 LEU A 108    24353  37039  28164  -4029  -3852     94       C  
ATOM    913  N   ASN A 109     -25.755  15.907 -59.881  1.00243.70           N  
ANISOU  913  N   ASN A 109    24846  38971  28777  -4586  -1588   -645       N  
ATOM    914  CA  ASN A 109     -25.698  16.278 -58.476  1.00241.51           C  
ANISOU  914  CA  ASN A 109    24277  39086  28401  -5062  -1422   -602       C  
ATOM    915  C   ASN A 109     -25.587  17.775 -58.228  1.00241.02           C  
ANISOU  915  C   ASN A 109    24158  39184  28236  -5164   -741   -823       C  
ATOM    916  O   ASN A 109     -25.830  18.209 -57.097  1.00239.09           O  
ANISOU  916  O   ASN A 109    23982  38958  27902  -5358   -534   -751       O  
ATOM    917  CB  ASN A 109     -24.520  15.570 -57.789  1.00241.54           C  
ANISOU  917  CB  ASN A 109    24273  39108  28395  -5086  -1621   -564       C  
ATOM    918  CG  ASN A 109     -24.677  14.061 -57.773  1.00240.76           C  
ANISOU  918  CG  ASN A 109    24295  38787  28394  -4993  -2254   -307       C  
ATOM    919  OD1 ASN A 109     -23.898  13.338 -58.393  1.00242.72           O  
ANISOU  919  OD1 ASN A 109    24558  38973  28692  -4790  -2559   -338       O  
ATOM    920  ND2 ASN A 109     -25.692  13.580 -57.065  1.00238.27           N  
ANISOU  920  ND2 ASN A 109    24081  38334  28117  -5126  -2434    -56       N  
ATOM    921  N   THR A 110     -25.232  18.577 -59.238  1.00247.43           N  
ANISOU  921  N   THR A 110    25091  39869  29054  -4868   -352  -1066       N  
ATOM    922  CA  THR A 110     -25.180  20.020 -59.016  1.00246.30           C  
ANISOU  922  CA  THR A 110    24865  39903  28815  -4994    304  -1279       C  
ATOM    923  C   THR A 110     -26.579  20.617 -58.903  1.00245.73           C  
ANISOU  923  C   THR A 110    24831  39824  28710  -5107    475  -1191       C  
ATOM    924  O   THR A 110     -26.758  21.651 -58.249  1.00243.45           O  
ANISOU  924  O   THR A 110    24689  39492  28320  -5174    887  -1253       O  
ATOM    925  CB  THR A 110     -24.387  20.714 -60.126  1.00248.80           C  
ANISOU  925  CB  THR A 110    25359  40020  29154  -4604    707  -1556       C  
ATOM    926  OG1 THR A 110     -24.160  22.082 -59.765  1.00246.76           O  
ANISOU  926  OG1 THR A 110    24988  39965  28805  -4771   1348  -1770       O  
ATOM    927  CG2 THR A 110     -25.142  20.675 -61.443  1.00252.39           C  
ANISOU  927  CG2 THR A 110    26128  40103  29665  -4183    654  -1550       C  
ATOM    928  N   GLN A 111     -27.575  19.987 -59.527  1.00254.29           N  
ANISOU  928  N   GLN A 111    26047  40687  29886  -4945    118  -1026       N  
ATOM    929  CA  GLN A 111     -28.976  20.335 -59.338  1.00253.35           C  
ANISOU  929  CA  GLN A 111    25904  40585  29771  -5091    174   -897       C  
ATOM    930  C   GLN A 111     -29.656  19.416 -58.330  1.00250.85           C  
ANISOU  930  C   GLN A 111    25562  40255  29496  -5333   -264   -587       C  
ATOM    931  O   GLN A 111     -30.890  19.382 -58.257  1.00249.86           O  
ANISOU  931  O   GLN A 111    25466  40040  29429  -5388   -353   -427       O  
ATOM    932  CB  GLN A 111     -29.718  20.302 -60.675  1.00256.41           C  
ANISOU  932  CB  GLN A 111    26569  40607  30248  -4670     82   -913       C  
ATOM    933  CG  GLN A 111     -29.275  21.375 -61.656  1.00258.76           C  
ANISOU  933  CG  GLN A 111    27062  40767  30490  -4328    605  -1198       C  
ATOM    934  CD  GLN A 111     -29.548  22.778 -61.147  1.00256.23           C  
ANISOU  934  CD  GLN A 111    26621  40680  30054  -4552   1242  -1330       C  
ATOM    935  OE1 GLN A 111     -28.625  23.514 -60.797  1.00254.37           O  
ANISOU  935  OE1 GLN A 111    26295  40624  29731  -4653   1671  -1520       O  
ATOM    936  NE2 GLN A 111     -30.821  23.155 -61.104  1.00255.64           N  
ANISOU  936  NE2 GLN A 111    26541  40601  29990  -4629   1308  -1231       N  
ATOM    937  N   PHE A 112     -28.869  18.669 -57.557  1.00248.20           N  
ANISOU  937  N   PHE A 112    25236  39928  29139  -5415   -513   -497       N  
ATOM    938  CA  PHE A 112     -29.379  17.750 -56.555  1.00245.88           C  
ANISOU  938  CA  PHE A 112    25004  39538  28880  -5566   -875   -207       C  
ATOM    939  C   PHE A 112     -28.852  18.050 -55.159  1.00245.42           C  
ANISOU  939  C   PHE A 112    24995  39577  28677  -5748   -668   -193       C  
ATOM    940  O   PHE A 112     -29.393  17.517 -54.183  1.00245.68           O  
ANISOU  940  O   PHE A 112    25078  39565  28705  -5895   -847     30       O  
ATOM    941  CB  PHE A 112     -29.025  16.303 -56.943  1.00246.83           C  
ANISOU  941  CB  PHE A 112    25132  39527  29125  -5450  -1477    -70       C  
ATOM    942  CG  PHE A 112     -29.624  15.260 -56.045  1.00245.91           C  
ANISOU  942  CG  PHE A 112    25095  39260  29080  -5567  -1843    229       C  
ATOM    943  CD1 PHE A 112     -30.971  14.948 -56.127  1.00245.68           C  
ANISOU  943  CD1 PHE A 112    25103  39072  29174  -5596  -2021    415       C  
ATOM    944  CD2 PHE A 112     -28.837  14.575 -55.133  1.00246.00           C  
ANISOU  944  CD2 PHE A 112    25133  39287  29047  -5642  -2003    315       C  
ATOM    945  CE1 PHE A 112     -31.525  13.984 -55.308  1.00246.27           C  
ANISOU  945  CE1 PHE A 112    25238  39003  29330  -5702  -2321    677       C  
ATOM    946  CE2 PHE A 112     -29.385  13.609 -54.311  1.00246.66           C  
ANISOU  946  CE2 PHE A 112    25286  39242  29193  -5744  -2305    577       C  
ATOM    947  CZ  PHE A 112     -30.730  13.313 -54.399  1.00246.75           C  
ANISOU  947  CZ  PHE A 112    25330  39092  29330  -5776  -2452    756       C  
ATOM    948  N   ILE A 113     -27.827  18.898 -55.034  1.00247.58           N  
ANISOU  948  N   ILE A 113    25260  39975  28834  -5732   -300   -433       N  
ATOM    949  CA  ILE A 113     -27.299  19.254 -53.722  1.00247.45           C  
ANISOU  949  CA  ILE A 113    25300  40053  28668  -5889   -134   -446       C  
ATOM    950  C   ILE A 113     -28.321  20.054 -52.923  1.00248.12           C  
ANISOU  950  C   ILE A 113    25499  40119  28657  -6013    126   -385       C  
ATOM    951  O   ILE A 113     -28.333  20.002 -51.687  1.00250.25           O  
ANISOU  951  O   ILE A 113    25821  40449  28815  -6175    110   -287       O  
ATOM    952  CB  ILE A 113     -25.971  20.022 -53.878  1.00246.77           C  
ANISOU  952  CB  ILE A 113    25187  40062  28512  -5816    182   -738       C  
ATOM    953  CG1 ILE A 113     -25.292  20.220 -52.521  1.00246.99           C  
ANISOU  953  CG1 ILE A 113    25254  40194  28396  -5974    247   -752       C  
ATOM    954  CG2 ILE A 113     -26.185  21.357 -54.583  1.00245.70           C  
ANISOU  954  CG2 ILE A 113    25124  39874  28358  -5692    667   -970       C  
ATOM    955  CD1 ILE A 113     -23.857  20.692 -52.619  1.00246.63           C  
ANISOU  955  CD1 ILE A 113    25154  40227  28327  -5909    441  -1011       C  
ATOM    956  N   LYS A 114     -29.199  20.789 -53.601  1.00253.65           N  
ANISOU  956  N   LYS A 114    26243  40735  29398  -5929    358   -442       N  
ATOM    957  CA  LYS A 114     -30.205  21.595 -52.922  1.00252.60           C  
ANISOU  957  CA  LYS A 114    26230  40548  29198  -6007    598   -393       C  
ATOM    958  C   LYS A 114     -31.386  20.778 -52.394  1.00253.20           C  
ANISOU  958  C   LYS A 114    26289  40570  29347  -6136    305    -90       C  
ATOM    959  O   LYS A 114     -32.281  21.357 -51.773  1.00252.30           O  
ANISOU  959  O   LYS A 114    26258  40410  29194  -6205    479    -28       O  
ATOM    960  CB  LYS A 114     -30.721  22.689 -53.863  1.00250.03           C  
ANISOU  960  CB  LYS A 114    25972  40118  28910  -5840    952   -563       C  
ATOM    961  CG  LYS A 114     -31.496  22.165 -55.058  1.00249.71           C  
ANISOU  961  CG  LYS A 114    25829  40023  29026  -5740    769   -480       C  
ATOM    962  CD  LYS A 114     -31.965  23.283 -55.968  1.00248.43           C  
ANISOU  962  CD  LYS A 114    25743  39771  28879  -5562   1151   -657       C  
ATOM    963  CE  LYS A 114     -32.767  22.740 -57.139  1.00249.58           C  
ANISOU  963  CE  LYS A 114    25757  39901  29170  -5473    940   -579       C  
ATOM    964  NZ  LYS A 114     -33.234  23.823 -58.046  1.00250.81           N  
ANISOU  964  NZ  LYS A 114    25992  39980  29323  -5279   1335   -752       N  
ATOM    965  N   LYS A 115     -31.424  19.464 -52.629  1.00249.21           N  
ANISOU  965  N   LYS A 115    25692  40031  28967  -6151   -142     98       N  
ATOM    966  CA  LYS A 115     -32.545  18.617 -52.261  1.00249.89           C  
ANISOU  966  CA  LYS A 115    25767  40010  29169  -6245   -442    383       C  
ATOM    967  C   LYS A 115     -32.216  17.650 -51.135  1.00251.59           C  
ANISOU  967  C   LYS A 115    25991  40262  29338  -6394   -716    571       C  
ATOM    968  O   LYS A 115     -33.144  17.189 -50.472  1.00252.45           O  
ANISOU  968  O   LYS A 115    26117  40309  29495  -6512   -845    794       O  
ATOM    969  CB  LYS A 115     -33.028  17.823 -53.491  1.00249.09           C  
ANISOU  969  CB  LYS A 115    25592  39762  29288  -6110   -794    461       C  
ATOM    970  CG  LYS A 115     -33.663  18.644 -54.587  1.00247.43           C  
ANISOU  970  CG  LYS A 115    25356  39517  29141  -5981   -577    329       C  
ATOM    971  CD  LYS A 115     -34.022  17.777 -55.782  1.00247.38           C  
ANISOU  971  CD  LYS A 115    25280  39377  29336  -5837  -1005    393       C  
ATOM    972  CE  LYS A 115     -35.199  16.861 -55.464  1.00248.75           C  
ANISOU  972  CE  LYS A 115    25456  39365  29691  -5911  -1374    677       C  
ATOM    973  NZ  LYS A 115     -35.659  16.105 -56.662  1.00248.71           N  
ANISOU  973  NZ  LYS A 115    25426  39182  29892  -5737  -1816    724       N  
ATOM    974  N   ASN A 116     -30.942  17.297 -50.930  1.00248.72           N  
ANISOU  974  N   ASN A 116    25610  39993  28897  -6383   -812    491       N  
ATOM    975  CA  ASN A 116     -30.512  16.597 -49.709  1.00250.35           C  
ANISOU  975  CA  ASN A 116    25835  40277  29008  -6534   -989    635       C  
ATOM    976  C   ASN A 116     -30.175  17.688 -48.666  1.00251.44           C  
ANISOU  976  C   ASN A 116    26032  40595  28910  -6659   -604    502       C  
ATOM    977  O   ASN A 116     -29.017  17.879 -48.298  1.00252.41           O  
ANISOU  977  O   ASN A 116    26143  40850  28911  -6673   -537    360       O  
ATOM    978  CB  ASN A 116     -29.261  15.677 -49.889  1.00249.69           C  
ANISOU  978  CB  ASN A 116    25710  40204  28957  -6456  -1296    614       C  
ATOM    979  CG  ASN A 116     -29.455  14.349 -49.138  1.00250.11           C  
ANISOU  979  CG  ASN A 116    25786  40185  29059  -6545  -1695    886       C  
ATOM    980  OD1 ASN A 116     -28.486  13.645 -48.809  1.00251.23           O  
ANISOU  980  OD1 ASN A 116    25919  40360  29176  -6531  -1910    900       O  
ATOM    981  ND2 ASN A 116     -30.733  13.944 -49.026  1.00249.36           N  
ANISOU  981  ND2 ASN A 116    25717  39960  29071  -6607  -1816   1098       N  
ATOM    982  N   PRO A 135     -31.129  11.565 -47.433  1.00249.13           N  
ANISOU  982  N   PRO A 135    25746  39808  29103  -6807  -2463   1601       N  
ATOM    983  CA  PRO A 135     -30.390  10.330 -47.159  1.00250.49           C  
ANISOU  983  CA  PRO A 135    25948  39920  29308  -6770  -2834   1707       C  
ATOM    984  C   PRO A 135     -29.662   9.779 -48.385  1.00249.81           C  
ANISOU  984  C   PRO A 135    25873  39660  29382  -6505  -3100   1592       C  
ATOM    985  O   PRO A 135     -30.284   9.560 -49.426  1.00249.11           O  
ANISOU  985  O   PRO A 135    25802  39367  29482  -6361  -3245   1598       O  
ATOM    986  CB  PRO A 135     -31.486   9.364 -46.697  1.00251.98           C  
ANISOU  986  CB  PRO A 135    26169  39961  29610  -6876  -3077   1999       C  
ATOM    987  CG  PRO A 135     -32.730   9.873 -47.339  1.00251.06           C  
ANISOU  987  CG  PRO A 135    26030  39728  29635  -6859  -2955   2013       C  
ATOM    988  CD  PRO A 135     -32.588  11.367 -47.370  1.00249.56           C  
ANISOU  988  CD  PRO A 135    25805  39730  29287  -6886  -2502   1797       C  
ATOM    989  N   LEU A 136     -28.351   9.572 -48.246  1.00248.06           N  
ANISOU  989  N   LEU A 136    25644  39523  29083  -6438  -3168   1483       N  
ATOM    990  CA  LEU A 136     -27.528   8.881 -49.239  1.00247.82           C  
ANISOU  990  CA  LEU A 136    25640  39332  29189  -6183  -3460   1395       C  
ATOM    991  C   LEU A 136     -27.549   9.588 -50.599  1.00245.99           C  
ANISOU  991  C   LEU A 136    25379  39045  29043  -6005  -3341   1198       C  
ATOM    992  O   LEU A 136     -28.025   9.056 -51.604  1.00245.65           O  
ANISOU  992  O   LEU A 136    25389  38772  29174  -5832  -3594   1233       O  
ATOM    993  CB  LEU A 136     -27.958   7.416 -49.373  1.00249.08           C  
ANISOU  993  CB  LEU A 136    25896  39224  29518  -6097  -3915   1609       C  
ATOM    994  N   MET A 137     -27.020  10.809 -50.610  1.00243.55           N  
ANISOU  994  N   MET A 137    24989  38952  28598  -6047  -2948    983       N  
ATOM    995  CA  MET A 137     -26.704  11.512 -51.844  1.00241.99           C  
ANISOU  995  CA  MET A 137    24744  38757  28442  -5877  -2802    760       C  
ATOM    996  C   MET A 137     -25.259  11.186 -52.226  1.00242.22           C  
ANISOU  996  C   MET A 137    24740  38813  28477  -5717  -2929    615       C  
ATOM    997  O   MET A 137     -24.661  10.248 -51.692  1.00243.57           O  
ANISOU  997  O   MET A 137    24946  38937  28660  -5702  -3205    713       O  
ATOM    998  CB  MET A 137     -26.950  13.010 -51.680  1.00240.82           C  
ANISOU  998  CB  MET A 137    24534  38811  28155  -6001  -2283    596       C  
ATOM    999  N   GLU A 138     -24.678  11.949 -53.159  1.00240.19           N  
ANISOU  999  N   GLU A 138    24410  38637  28215  -5592  -2723    376       N  
ATOM   1000  CA  GLU A 138     -23.276  11.773 -53.552  1.00240.45           C  
ANISOU 1000  CA  GLU A 138    24381  38722  28257  -5443  -2790    215       C  
ATOM   1001  C   GLU A 138     -23.024  10.360 -54.091  1.00241.30           C  
ANISOU 1001  C   GLU A 138    24586  38588  28507  -5229  -3318    346       C  
ATOM   1002  O   GLU A 138     -22.450   9.503 -53.422  1.00242.68           O  
ANISOU 1002  O   GLU A 138    24797  38721  28690  -5232  -3559    447       O  
ATOM   1003  CB  GLU A 138     -22.313  12.103 -52.401  1.00241.40           C  
ANISOU 1003  CB  GLU A 138    24430  39045  28247  -5596  -2602    143       C  
ATOM   1004  CG  GLU A 138     -22.119  13.593 -52.138  1.00240.56           C  
ANISOU 1004  CG  GLU A 138    24234  39164  28003  -5726  -2064    -80       C  
ATOM   1005  CD  GLU A 138     -23.146  14.179 -51.192  1.00240.48           C  
ANISOU 1005  CD  GLU A 138    24284  39221  27867  -5949  -1833     22       C  
ATOM   1006  OE1 GLU A 138     -23.969  13.413 -50.652  1.00241.22           O  
ANISOU 1006  OE1 GLU A 138    24458  39215  27980  -6028  -2081    271       O  
ATOM   1007  OE2 GLU A 138     -23.124  15.411 -50.985  1.00239.77           O  
ANISOU 1007  OE2 GLU A 138    24169  39273  27659  -6036  -1398   -153       O  
ATOM   1008  N   ILE A 139     -23.517  10.141 -55.314  1.00231.37           N  
ANISOU 1008  N   ILE A 139    23390  37165  27355  -5032  -3496    340       N  
ATOM   1009  CA  ILE A 139     -23.487   8.854 -56.011  1.00232.14           C  
ANISOU 1009  CA  ILE A 139    23632  36983  27588  -4790  -4003    459       C  
ATOM   1010  C   ILE A 139     -22.201   8.080 -55.735  1.00233.32           C  
ANISOU 1010  C   ILE A 139    23784  37123  27745  -4690  -4215    449       C  
ATOM   1011  O   ILE A 139     -22.235   6.862 -55.519  1.00233.73           O  
ANISOU 1011  O   ILE A 139    23967  36962  27878  -4608  -4598    619       O  
ATOM   1012  CB  ILE A 139     -23.662   9.065 -57.527  1.00232.59           C  
ANISOU 1012  CB  ILE A 139    23723  36959  27693  -4544  -4080    341       C  
ATOM   1013  CG1 ILE A 139     -24.983   9.777 -57.823  1.00232.99           C  
ANISOU 1013  CG1 ILE A 139    23770  37005  27748  -4629  -3904    355       C  
ATOM   1014  CG2 ILE A 139     -23.586   7.740 -58.272  1.00233.22           C  
ANISOU 1014  CG2 ILE A 139    23994  36724  27895  -4262  -4613    457       C  
ATOM   1015  CD1 ILE A 139     -26.204   9.000 -57.392  1.00231.54           C  
ANISOU 1015  CD1 ILE A 139    23712  36584  27680  -4702  -4169    608       C  
ATOM   1016  N   GLY A 140     -21.060   8.773 -55.749  1.00225.21           N  
ANISOU 1016  N   GLY A 140    22604  36323  26642  -4690  -3957    241       N  
ATOM   1017  CA  GLY A 140     -19.813   8.129 -55.363  1.00226.26           C  
ANISOU 1017  CA  GLY A 140    22708  36476  26786  -4621  -4128    227       C  
ATOM   1018  C   GLY A 140     -19.869   7.551 -53.961  1.00227.34           C  
ANISOU 1018  C   GLY A 140    22883  36610  26886  -4805  -4227    398       C  
ATOM   1019  O   GLY A 140     -19.541   6.381 -53.741  1.00228.29           O  
ANISOU 1019  O   GLY A 140    23101  36571  27069  -4702  -4591    527       O  
ATOM   1020  N   GLU A 141     -20.289   8.368 -52.989  1.00224.66           N  
ANISOU 1020  N   GLU A 141    22475  36456  26429  -5072  -3898    397       N  
ATOM   1021  CA  GLU A 141     -20.496   7.876 -51.630  1.00226.33           C  
ANISOU 1021  CA  GLU A 141    22729  36695  26572  -5260  -3981    572       C  
ATOM   1022  C   GLU A 141     -21.539   6.765 -51.589  1.00226.09           C  
ANISOU 1022  C   GLU A 141    22861  36411  26633  -5231  -4324    824       C  
ATOM   1023  O   GLU A 141     -21.486   5.896 -50.712  1.00227.29           O  
ANISOU 1023  O   GLU A 141    23070  36521  26767  -5293  -4535    983       O  
ATOM   1024  CB  GLU A 141     -20.910   9.035 -50.717  1.00226.63           C  
ANISOU 1024  CB  GLU A 141    22688  36972  26448  -5534  -3556    527       C  
ATOM   1025  CG  GLU A 141     -21.184   8.655 -49.268  1.00228.20           C  
ANISOU 1025  CG  GLU A 141    22926  37245  26535  -5749  -3607    707       C  
ATOM   1026  CD  GLU A 141     -19.945   8.181 -48.537  1.00229.70           C  
ANISOU 1026  CD  GLU A 141    23072  37526  26677  -5741  -3748    676       C  
ATOM   1027  OE1 GLU A 141     -18.830   8.584 -48.928  1.00230.21           O  
ANISOU 1027  OE1 GLU A 141    23031  37679  26760  -5641  -3657    469       O  
ATOM   1028  OE2 GLU A 141     -20.088   7.406 -47.568  1.00230.47           O  
ANISOU 1028  OE2 GLU A 141    23231  37614  26723  -5837  -3947    858       O  
ATOM   1029  N   LEU A 142     -22.487   6.772 -52.528  1.00225.23           N  
ANISOU 1029  N   LEU A 142    22821  36133  26621  -5137  -4384    857       N  
ATOM   1030  CA  LEU A 142     -23.504   5.727 -52.563  1.00225.90           C  
ANISOU 1030  CA  LEU A 142    23053  35959  26818  -5102  -4707   1078       C  
ATOM   1031  C   LEU A 142     -22.962   4.443 -53.183  1.00226.77           C  
ANISOU 1031  C   LEU A 142    23292  35822  27050  -4832  -5143   1119       C  
ATOM   1032  O   LEU A 142     -23.309   3.343 -52.738  1.00228.11           O  
ANISOU 1032  O   LEU A 142    23570  35829  27273  -4831  -5420   1299       O  
ATOM   1033  CB  LEU A 142     -24.737   6.228 -53.320  1.00224.61           C  
ANISOU 1033  CB  LEU A 142    22914  35703  26727  -5098  -4621   1089       C  
ATOM   1034  CG  LEU A 142     -26.017   5.390 -53.291  1.00225.29           C  
ANISOU 1034  CG  LEU A 142    23116  35546  26940  -5115  -4877   1307       C  
ATOM   1035  CD1 LEU A 142     -27.234   6.295 -53.385  1.00224.28           C  
ANISOU 1035  CD1 LEU A 142    22933  35468  26816  -5259  -4621   1322       C  
ATOM   1036  CD2 LEU A 142     -26.034   4.380 -54.425  1.00225.52           C  
ANISOU 1036  CD2 LEU A 142    23297  35262  27128  -4815  -5289   1321       C  
ATOM   1037  N   ALA A 143     -22.118   4.560 -54.211  1.00219.25           N  
ANISOU 1037  N   ALA A 143    22331  34843  26130  -4600  -5197    955       N  
ATOM   1038  CA  ALA A 143     -21.490   3.374 -54.787  1.00220.16           C  
ANISOU 1038  CA  ALA A 143    22577  34737  26338  -4326  -5595    983       C  
ATOM   1039  C   ALA A 143     -20.543   2.723 -53.788  1.00221.80           C  
ANISOU 1039  C   ALA A 143    22759  35019  26498  -4372  -5697   1028       C  
ATOM   1040  O   ALA A 143     -20.554   1.498 -53.608  1.00223.14           O  
ANISOU 1040  O   ALA A 143    23060  34999  26723  -4274  -6022   1162       O  
ATOM   1041  CB  ALA A 143     -20.752   3.743 -56.074  1.00219.20           C  
ANISOU 1041  CB  ALA A 143    22439  34612  26237  -4076  -5602    801       C  
ATOM   1042  N   LEU A 144     -19.715   3.533 -53.123  1.00217.77           N  
ANISOU 1042  N   LEU A 144    22077  34788  25878  -4518  -5418    909       N  
ATOM   1043  CA  LEU A 144     -18.875   3.005 -52.055  1.00218.76           C  
ANISOU 1043  CA  LEU A 144    22168  35008  25944  -4586  -5506    951       C  
ATOM   1044  C   LEU A 144     -19.717   2.492 -50.894  1.00219.44           C  
ANISOU 1044  C   LEU A 144    22320  35083  25976  -4796  -5563   1164       C  
ATOM   1045  O   LEU A 144     -19.292   1.583 -50.172  1.00220.42           O  
ANISOU 1045  O   LEU A 144    22489  35182  26077  -4793  -5778   1266       O  
ATOM   1046  CB  LEU A 144     -17.895   4.077 -51.584  1.00218.48           C  
ANISOU 1046  CB  LEU A 144    21931  35276  25806  -4710  -5178    764       C  
ATOM   1047  CG  LEU A 144     -16.842   4.497 -52.611  1.00217.49           C  
ANISOU 1047  CG  LEU A 144    21702  35200  25735  -4511  -5121    552       C  
ATOM   1048  CD1 LEU A 144     -16.005   5.653 -52.087  1.00217.86           C  
ANISOU 1048  CD1 LEU A 144    21532  35556  25689  -4669  -4746    354       C  
ATOM   1049  CD2 LEU A 144     -15.960   3.316 -52.986  1.00217.87           C  
ANISOU 1049  CD2 LEU A 144    21823  35082  25874  -4253  -5508    584       C  
ATOM   1050  N   ASP A 145     -20.909   3.063 -50.698  1.00217.33           N  
ANISOU 1050  N   ASP A 145    22050  34845  25680  -4982  -5369   1239       N  
ATOM   1051  CA  ASP A 145     -21.859   2.492 -49.750  1.00218.44           C  
ANISOU 1051  CA  ASP A 145    22258  34949  25789  -5169  -5449   1470       C  
ATOM   1052  C   ASP A 145     -22.280   1.095 -50.189  1.00219.34           C  
ANISOU 1052  C   ASP A 145    22539  34757  26042  -4997  -5848   1623       C  
ATOM   1053  O   ASP A 145     -22.502   0.211 -49.353  1.00220.97           O  
ANISOU 1053  O   ASP A 145    22808  34927  26225  -5087  -6017   1805       O  
ATOM   1054  CB  ASP A 145     -23.076   3.411 -49.615  1.00217.32           C  
ANISOU 1054  CB  ASP A 145    22074  34886  25613  -5376  -5162   1512       C  
ATOM   1055  CG  ASP A 145     -23.985   3.027 -48.459  1.00218.60           C  
ANISOU 1055  CG  ASP A 145    22264  35084  25711  -5623  -5173   1749       C  
ATOM   1056  OD1 ASP A 145     -23.678   2.056 -47.737  1.00220.37           O  
ANISOU 1056  OD1 ASP A 145    22542  35282  25906  -5644  -5398   1883       O  
ATOM   1057  OD2 ASP A 145     -25.019   3.703 -48.275  1.00217.92           O  
ANISOU 1057  OD2 ASP A 145    22143  35059  25598  -5797  -4952   1805       O  
ATOM   1058  N   MET A 146     -22.384   0.874 -51.502  1.00222.66           N  
ANISOU 1058  N   MET A 146    23043  34961  26596  -4746  -6001   1549       N  
ATOM   1059  CA  MET A 146     -22.712  -0.460 -51.990  1.00223.88           C  
ANISOU 1059  CA  MET A 146    23373  34818  26875  -4556  -6379   1669       C  
ATOM   1060  C   MET A 146     -21.536  -1.416 -51.827  1.00224.64           C  
ANISOU 1060  C   MET A 146    23522  34877  26955  -4388  -6621   1658       C  
ATOM   1061  O   MET A 146     -21.740  -2.615 -51.604  1.00225.69           O  
ANISOU 1061  O   MET A 146    23778  34845  27128  -4335  -6889   1808       O  
ATOM   1062  CB  MET A 146     -23.154  -0.394 -53.452  1.00223.40           C  
ANISOU 1062  CB  MET A 146    23402  34540  26938  -4321  -6481   1585       C  
ATOM   1063  CG  MET A 146     -24.375   0.484 -53.680  1.00222.46           C  
ANISOU 1063  CG  MET A 146    23236  34437  26851  -4465  -6273   1598       C  
ATOM   1064  SD  MET A 146     -25.788   0.017 -52.663  1.00222.52           S  
ANISOU 1064  SD  MET A 146    23257  34398  26891  -4743  -6290   1862       S  
ATOM   1065  CE  MET A 146     -26.217  -1.564 -53.377  1.00222.02           C  
ANISOU 1065  CE  MET A 146    23404  33956  26996  -4507  -6745   1980       C  
ATOM   1066  N   TRP A 147     -20.304  -0.910 -51.939  1.00216.56           N  
ANISOU 1066  N   TRP A 147    22398  34008  25878  -4307  -6524   1484       N  
ATOM   1067  CA  TRP A 147     -19.147  -1.726 -51.581  1.00218.12           C  
ANISOU 1067  CA  TRP A 147    22612  34215  26050  -4184  -6725   1476       C  
ATOM   1068  C   TRP A 147     -19.181  -2.093 -50.102  1.00219.82           C  
ANISOU 1068  C   TRP A 147    22798  34567  26157  -4417  -6723   1624       C  
ATOM   1069  O   TRP A 147     -18.831  -3.219 -49.720  1.00221.52           O  
ANISOU 1069  O   TRP A 147    23101  34697  26369  -4337  -6980   1725       O  
ATOM   1070  CB  TRP A 147     -17.854  -0.987 -51.925  1.00217.61           C  
ANISOU 1070  CB  TRP A 147    22406  34316  25961  -4087  -6593   1260       C  
ATOM   1071  N   ARG A 148     -19.603  -1.151 -49.254  1.00215.01           N  
ANISOU 1071  N   ARG A 148    22072  34180  25442  -4703  -6430   1641       N  
ATOM   1072  CA  ARG A 148     -19.852  -1.482 -47.856  1.00217.11           C  
ANISOU 1072  CA  ARG A 148    22331  34574  25587  -4942  -6430   1813       C  
ATOM   1073  C   ARG A 148     -20.907  -2.574 -47.743  1.00218.42           C  
ANISOU 1073  C   ARG A 148    22643  34528  25817  -4969  -6658   2052       C  
ATOM   1074  O   ARG A 148     -20.803  -3.460 -46.891  1.00220.49           O  
ANISOU 1074  O   ARG A 148    22959  34796  26022  -5032  -6830   2207       O  
ATOM   1075  CB  ARG A 148     -20.286  -0.237 -47.083  1.00216.56           C  
ANISOU 1075  CB  ARG A 148    22133  34767  25383  -5238  -6063   1797       C  
ATOM   1076  CG  ARG A 148     -20.446  -0.462 -45.587  1.00218.40           C  
ANISOU 1076  CG  ARG A 148    22354  35176  25454  -5494  -6046   1965       C  
ATOM   1077  CD  ARG A 148     -20.841   0.822 -44.873  1.00218.47           C  
ANISOU 1077  CD  ARG A 148    22246  35452  25309  -5771  -5670   1933       C  
ATOM   1078  NE  ARG A 148     -21.037   0.614 -43.441  1.00220.53           N  
ANISOU 1078  NE  ARG A 148    22507  35891  25392  -6020  -5662   2106       N  
ATOM   1079  CZ  ARG A 148     -20.071   0.715 -42.534  1.00222.03           C  
ANISOU 1079  CZ  ARG A 148    22640  36289  25434  -6082  -5654   2048       C  
ATOM   1080  NH1 ARG A 148     -18.839   1.029 -42.910  1.00221.35           N  
ANISOU 1080  NH1 ARG A 148    22475  36253  25375  -5918  -5644   1819       N  
ATOM   1081  NH2 ARG A 148     -20.337   0.509 -41.252  1.00224.07           N  
ANISOU 1081  NH2 ARG A 148    22912  36709  25516  -6312  -5662   2220       N  
ATOM   1082  N   LYS A 149     -21.923  -2.535 -48.608  1.00219.47           N  
ANISOU 1082  N   LYS A 149    22840  34474  26075  -4921  -6669   2083       N  
ATOM   1083  CA  LYS A 149     -22.900  -3.616 -48.650  1.00219.93           C  
ANISOU 1083  CA  LYS A 149    23032  34301  26229  -4924  -6905   2295       C  
ATOM   1084  C   LYS A 149     -22.278  -4.920 -49.138  1.00220.77           C  
ANISOU 1084  C   LYS A 149    23281  34195  26406  -4655  -7248   2309       C  
ATOM   1085  O   LYS A 149     -22.831  -5.994 -48.879  1.00222.02           O  
ANISOU 1085  O   LYS A 149    23548  34198  26610  -4681  -7461   2504       O  
ATOM   1086  CB  LYS A 149     -24.083  -3.213 -49.534  1.00218.54           C  
ANISOU 1086  CB  LYS A 149    22881  33971  26184  -4916  -6843   2297       C  
ATOM   1087  CG  LYS A 149     -25.266  -4.166 -49.497  1.00219.46           C  
ANISOU 1087  CG  LYS A 149    23103  33866  26414  -4978  -7044   2524       C  
ATOM   1088  CD  LYS A 149     -26.436  -3.612 -50.293  1.00218.22           C  
ANISOU 1088  CD  LYS A 149    22940  33587  26386  -4989  -6961   2510       C  
ATOM   1089  CE  LYS A 149     -27.634  -4.546 -50.245  1.00219.29           C  
ANISOU 1089  CE  LYS A 149    23161  33499  26660  -5066  -7163   2736       C  
ATOM   1090  NZ  LYS A 149     -28.791  -4.003 -51.011  1.00218.23           N  
ANISOU 1090  NZ  LYS A 149    23009  33244  26665  -5072  -7096   2716       N  
ATOM   1091  N   LEU A 150     -21.136  -4.850 -49.826  1.00218.89           N  
ANISOU 1091  N   LEU A 150    23040  33953  26174  -4404  -7299   2115       N  
ATOM   1092  CA  LEU A 150     -20.393  -6.060 -50.155  1.00220.17           C  
ANISOU 1092  CA  LEU A 150    23326  33958  26369  -4152  -7603   2125       C  
ATOM   1093  C   LEU A 150     -19.587  -6.568 -48.967  1.00222.66           C  
ANISOU 1093  C   LEU A 150    23607  34430  26564  -4236  -7672   2195       C  
ATOM   1094  O   LEU A 150     -19.377  -7.780 -48.841  1.00223.74           O  
ANISOU 1094  O   LEU A 150    23862  34439  26709  -4126  -7929   2305       O  
ATOM   1095  CB  LEU A 150     -19.468  -5.808 -51.352  1.00218.63           C  
ANISOU 1095  CB  LEU A 150    23139  33707  26224  -3847  -7638   1905       C  
ATOM   1096  CG  LEU A 150     -18.744  -6.988 -52.014  1.00219.35           C  
ANISOU 1096  CG  LEU A 150    23375  33611  26355  -3530  -7940   1895       C  
ATOM   1097  CD1 LEU A 150     -18.527  -6.703 -53.490  1.00218.57           C  
ANISOU 1097  CD1 LEU A 150    23335  33379  26332  -3251  -7972   1738       C  
ATOM   1098  CD2 LEU A 150     -17.408  -7.286 -51.346  1.00220.23           C  
ANISOU 1098  CD2 LEU A 150    23417  33879  26383  -3479  -8000   1846       C  
ATOM   1099  N   MET A 151     -19.132  -5.673 -48.087  1.00216.87           N  
ANISOU 1099  N   MET A 151    22717  33973  25709  -4426  -7450   2133       N  
ATOM   1100  CA  MET A 151     -18.287  -6.104 -46.979  1.00218.17           C  
ANISOU 1100  CA  MET A 151    22848  34297  25751  -4487  -7530   2177       C  
ATOM   1101  C   MET A 151     -19.061  -6.470 -45.717  1.00219.18           C  
ANISOU 1101  C   MET A 151    22999  34505  25775  -4771  -7535   2421       C  
ATOM   1102  O   MET A 151     -18.568  -7.275 -44.919  1.00220.42           O  
ANISOU 1102  O   MET A 151    23195  34706  25849  -4778  -7706   2520       O  
ATOM   1103  CB  MET A 151     -17.253  -5.026 -46.646  1.00217.71           C  
ANISOU 1103  CB  MET A 151    22613  34500  25609  -4530  -7319   1976       C  
ATOM   1104  CG  MET A 151     -16.211  -4.838 -47.731  1.00216.75           C  
ANISOU 1104  CG  MET A 151    22452  34324  25580  -4247  -7359   1755       C  
ATOM   1105  SD  MET A 151     -15.393  -6.398 -48.118  1.00218.20           S  
ANISOU 1105  SD  MET A 151    22778  34309  25817  -3925  -7753   1791       S  
ATOM   1106  CE  MET A 151     -14.564  -6.743 -46.571  1.00219.93           C  
ANISOU 1106  CE  MET A 151    22927  34751  25885  -4056  -7822   1846       C  
ATOM   1107  N   VAL A 152     -20.257  -5.910 -45.510  1.00218.12           N  
ANISOU 1107  N   VAL A 152    22840  34397  25640  -5005  -7356   2528       N  
ATOM   1108  CA  VAL A 152     -21.066  -6.260 -44.344  1.00219.57           C  
ANISOU 1108  CA  VAL A 152    23042  34656  25727  -5289  -7362   2786       C  
ATOM   1109  C   VAL A 152     -21.478  -7.727 -44.382  1.00221.20           C  
ANISOU 1109  C   VAL A 152    23406  34627  26013  -5221  -7675   2996       C  
ATOM   1110  O   VAL A 152     -21.816  -8.308 -43.343  1.00223.85           O  
ANISOU 1110  O   VAL A 152    23773  35022  26259  -5415  -7757   3221       O  
ATOM   1111  CB  VAL A 152     -22.288  -5.312 -44.252  1.00218.27           C  
ANISOU 1111  CB  VAL A 152    22809  34560  25565  -5536  -7096   2850       C  
ATOM   1112  CG1 VAL A 152     -23.235  -5.721 -43.133  1.00219.96           C  
ANISOU 1112  CG1 VAL A 152    23044  34835  25696  -5836  -7113   3144       C  
ATOM   1113  CG2 VAL A 152     -21.828  -3.883 -44.024  1.00216.99           C  
ANISOU 1113  CG2 VAL A 152    22495  34665  25287  -5634  -6769   2657       C  
ATOM   1114  N   GLU A 153     -21.407  -8.356 -45.555  1.00220.64           N  
ANISOU 1114  N   GLU A 153    23440  34293  26098  -4946  -7856   2930       N  
ATOM   1115  CA  GLU A 153     -21.702  -9.767 -45.775  1.00222.16           C  
ANISOU 1115  CA  GLU A 153    23794  34237  26379  -4841  -8155   3098       C  
ATOM   1116  C   GLU A 153     -20.879 -10.630 -44.823  1.00223.87           C  
ANISOU 1116  C   GLU A 153    24049  34541  26469  -4838  -8328   3193       C  
ATOM   1117  O   GLU A 153     -19.898 -10.138 -44.250  1.00223.32           O  
ANISOU 1117  O   GLU A 153    23885  34700  26268  -4839  -8244   3071       O  
ATOM   1118  CB  GLU A 153     -21.399 -10.127 -47.232  1.00221.74           C  
ANISOU 1118  CB  GLU A 153    23839  33943  26469  -4499  -8293   2943       C  
ATOM   1119  CG  GLU A 153     -22.196  -9.323 -48.241  1.00220.62           C  
ANISOU 1119  CG  GLU A 153    23677  33701  26449  -4473  -8153   2843       C  
ATOM   1120  CD  GLU A 153     -23.685  -9.573 -48.144  1.00220.88           C  
ANISOU 1120  CD  GLU A 153    23749  33592  26583  -4672  -8173   3055       C  
ATOM   1121  OE1 GLU A 153     -24.081 -10.706 -47.799  1.00222.59           O  
ANISOU 1121  OE1 GLU A 153    24069  33666  26839  -4722  -8386   3265       O  
ATOM   1122  OE2 GLU A 153     -24.460  -8.630 -48.407  1.00220.06           O  
ANISOU 1122  OE2 GLU A 153    23565  33521  26525  -4785  -7977   3015       O  
ATOM   1123  N   PRO A 154     -21.217 -11.912 -44.630  1.00219.96           N  
ANISOU 1123  N   PRO A 154    23690  33874  26011  -4832  -8576   3405       N  
ATOM   1124  CA  PRO A 154     -20.378 -12.765 -43.767  1.00222.29           C  
ANISOU 1124  CA  PRO A 154    24031  34250  26178  -4803  -8753   3488       C  
ATOM   1125  C   PRO A 154     -18.918 -12.813 -44.190  1.00222.19           C  
ANISOU 1125  C   PRO A 154    24005  34284  26131  -4499  -8820   3251       C  
ATOM   1126  O   PRO A 154     -18.100 -13.392 -43.463  1.00224.10           O  
ANISOU 1126  O   PRO A 154    24264  34624  26259  -4457  -8953   3285       O  
ATOM   1127  CB  PRO A 154     -21.043 -14.145 -43.875  1.00223.89           C  
ANISOU 1127  CB  PRO A 154    24401  34191  26477  -4795  -9012   3729       C  
ATOM   1128  CG  PRO A 154     -21.832 -14.097 -45.140  1.00222.23           C  
ANISOU 1128  CG  PRO A 154    24244  33728  26464  -4690  -9014   3681       C  
ATOM   1129  CD  PRO A 154     -22.311 -12.680 -45.251  1.00220.13           C  
ANISOU 1129  CD  PRO A 154    23833  33605  26201  -4831  -8723   3566       C  
ATOM   1130  N   LEU A 155     -18.577 -12.228 -45.343  1.00219.61           N  
ANISOU 1130  N   LEU A 155    23646  33894  25901  -4288  -8739   3022       N  
ATOM   1131  CA  LEU A 155     -17.182 -12.013 -45.705  1.00219.39           C  
ANISOU 1131  CA  LEU A 155    23560  33956  25844  -4039  -8756   2787       C  
ATOM   1132  C   LEU A 155     -16.418 -11.321 -44.583  1.00220.19           C  
ANISOU 1132  C   LEU A 155    23509  34362  25790  -4184  -8633   2718       C  
ATOM   1133  O   LEU A 155     -15.286 -11.702 -44.268  1.00221.59           O  
ANISOU 1133  O   LEU A 155    23667  34623  25902  -4041  -8757   2644       O  
ATOM   1134  CB  LEU A 155     -17.108 -11.186 -46.989  1.00216.93           C  
ANISOU 1134  CB  LEU A 155    23205  33576  25644  -3873  -8626   2570       C  
ATOM   1135  CG  LEU A 155     -17.695 -11.807 -48.258  1.00216.14           C  
ANISOU 1135  CG  LEU A 155    23260  33176  25687  -3673  -8759   2592       C  
ATOM   1136  CD1 LEU A 155     -17.690 -10.796 -49.395  1.00213.73           C  
ANISOU 1136  CD1 LEU A 155    22900  32846  25463  -3551  -8602   2385       C  
ATOM   1137  CD2 LEU A 155     -16.934 -13.062 -48.650  1.00217.59           C  
ANISOU 1137  CD2 LEU A 155    23580  33219  25877  -3395  -9025   2611       C  
ATOM   1138  N   GLN A 156     -17.024 -10.306 -43.958  1.00218.54           N  
ANISOU 1138  N   GLN A 156    23194  34326  25518  -4468  -8392   2742       N  
ATOM   1139  CA  GLN A 156     -16.352  -9.604 -42.868  1.00219.40           C  
ANISOU 1139  CA  GLN A 156    23166  34730  25466  -4623  -8265   2677       C  
ATOM   1140  C   GLN A 156     -16.056 -10.521 -41.692  1.00222.22           C  
ANISOU 1140  C   GLN A 156    23586  35168  25682  -4693  -8460   2850       C  
ATOM   1141  O   GLN A 156     -15.170 -10.214 -40.889  1.00223.44           O  
ANISOU 1141  O   GLN A 156    23651  35540  25707  -4723  -8446   2765       O  
ATOM   1142  CB  GLN A 156     -17.187  -8.414 -42.392  1.00218.22           C  
ANISOU 1142  CB  GLN A 156    22913  34749  25251  -4929  -7964   2702       C  
ATOM   1143  CG  GLN A 156     -18.501  -8.788 -41.731  1.00218.99           C  
ANISOU 1143  CG  GLN A 156    23085  34815  25307  -5195  -7967   2990       C  
ATOM   1144  CD  GLN A 156     -19.310  -7.572 -41.326  1.00217.78           C  
ANISOU 1144  CD  GLN A 156    22824  34838  25085  -5484  -7654   3007       C  
ATOM   1145  OE1 GLN A 156     -18.866  -6.435 -41.486  1.00216.40           O  
ANISOU 1145  OE1 GLN A 156    22524  34817  24880  -5492  -7425   2799       O  
ATOM   1146  NE2 GLN A 156     -20.507  -7.806 -40.800  1.00218.39           N  
ANISOU 1146  NE2 GLN A 156    22945  34895  25138  -5729  -7638   3262       N  
ATOM   1147  N   ALA A 157     -16.785 -11.627 -41.561  1.00211.01           N  
ANISOU 1147  N   ALA A 157    22315  33577  24283  -4725  -8644   3091       N  
ATOM   1148  CA  ALA A 157     -16.403 -12.665 -40.616  1.00213.81           C  
ANISOU 1148  CA  ALA A 157    22752  33969  24516  -4733  -8870   3253       C  
ATOM   1149  C   ALA A 157     -15.424 -13.648 -41.243  1.00214.64           C  
ANISOU 1149  C   ALA A 157    22940  33930  24683  -4388  -9114   3166       C  
ATOM   1150  O   ALA A 157     -14.486 -14.096 -40.580  1.00216.64           O  
ANISOU 1150  O   ALA A 157    23192  34297  24824  -4304  -9255   3147       O  
ATOM   1151  CB  ALA A 157     -17.642 -13.406 -40.108  1.00214.96           C  
ANISOU 1151  CB  ALA A 157    23015  34008  24654  -4957  -8952   3577       C  
ATOM   1152  N   ILE A 158     -15.620 -13.974 -42.519  1.00217.11           N  
ANISOU 1152  N   ILE A 158    23328  34002  25162  -4181  -9166   3108       N  
ATOM   1153  CA  ILE A 158     -14.735 -14.909 -43.205  1.00217.84           C  
ANISOU 1153  CA  ILE A 158    23508  33955  25305  -3847  -9384   3034       C  
ATOM   1154  C   ILE A 158     -13.408 -14.245 -43.554  1.00217.26           C  
ANISOU 1154  C   ILE A 158    23296  34023  25228  -3644  -9330   2751       C  
ATOM   1155  O   ILE A 158     -12.341 -14.700 -43.127  1.00219.04           O  
ANISOU 1155  O   ILE A 158    23504  34344  25379  -3505  -9473   2700       O  
ATOM   1156  CB  ILE A 158     -15.425 -15.475 -44.461  1.00216.65           C  
ANISOU 1156  CB  ILE A 158    23495  33502  25319  -3700  -9459   3077       C  
ATOM   1157  CG1 ILE A 158     -16.665 -16.283 -44.075  1.00217.70           C  
ANISOU 1157  CG1 ILE A 158    23761  33477  25480  -3900  -9557   3372       C  
ATOM   1158  CG2 ILE A 158     -14.455 -16.328 -45.265  1.00217.23           C  
ANISOU 1158  CG2 ILE A 158    23655  33453  25430  -3343  -9652   2984       C  
ATOM   1159  CD1 ILE A 158     -17.540 -16.655 -45.253  1.00216.49           C  
ANISOU 1159  CD1 ILE A 158    23725  33027  25503  -3813  -9605   3413       C  
ATOM   1160  N   LEU A 159     -13.465 -13.150 -44.322  1.00217.36           N  
ANISOU 1160  N   LEU A 159    23205  34052  25329  -3632  -9126   2570       N  
ATOM   1161  CA  LEU A 159     -12.263 -12.585 -44.934  1.00216.66           C  
ANISOU 1161  CA  LEU A 159    22993  34043  25285  -3417  -9089   2310       C  
ATOM   1162  C   LEU A 159     -11.174 -12.301 -43.910  1.00218.38           C  
ANISOU 1162  C   LEU A 159    23073  34513  25391  -3457  -9103   2218       C  
ATOM   1163  O   LEU A 159     -10.026 -12.724 -44.082  1.00219.54           O  
ANISOU 1163  O   LEU A 159    23189  34680  25546  -3223  -9255   2111       O  
ATOM   1164  CB  LEU A 159     -12.603 -11.307 -45.704  1.00213.98           C  
ANISOU 1164  CB  LEU A 159    22548  33717  25036  -3471  -8835   2155       C  
ATOM   1165  CG  LEU A 159     -13.418 -11.494 -46.980  1.00212.20           C  
ANISOU 1165  CG  LEU A 159    22447  33240  24940  -3348  -8842   2176       C  
ATOM   1166  CD1 LEU A 159     -13.747 -10.152 -47.610  1.00209.72           C  
ANISOU 1166  CD1 LEU A 159    22020  32972  24693  -3421  -8582   2026       C  
ATOM   1167  CD2 LEU A 159     -12.640 -12.365 -47.939  1.00212.65           C  
ANISOU 1167  CD2 LEU A 159    22600  33143  25056  -2996  -9051   2116       C  
ATOM   1168  N   ILE A 160     -11.511 -11.577 -42.838  1.00210.73           N  
ANISOU 1168  N   ILE A 160    22016  33741  24311  -3749  -8949   2260       N  
ATOM   1169  CA  ILE A 160     -10.494 -11.246 -41.844  1.00212.50           C  
ANISOU 1169  CA  ILE A 160    22109  34209  24422  -3794  -8964   2162       C  
ATOM   1170  C   ILE A 160      -9.895 -12.519 -41.260  1.00215.29           C  
ANISOU 1170  C   ILE A 160    22562  34547  24692  -3653  -9259   2266       C  
ATOM   1171  O   ILE A 160      -8.673 -12.627 -41.107  1.00216.69           O  
ANISOU 1171  O   ILE A 160    22654  34820  24859  -3485  -9377   2124       O  
ATOM   1172  CB  ILE A 160     -11.066 -10.306 -40.761  1.00212.52           C  
ANISOU 1172  CB  ILE A 160    22029  34428  24289  -4143  -8749   2214       C  
ATOM   1173  CG1 ILE A 160     -12.272 -10.912 -40.034  1.00213.36           C  
ANISOU 1173  CG1 ILE A 160    22280  34492  24293  -4360  -8788   2507       C  
ATOM   1174  CG2 ILE A 160     -11.432  -8.957 -41.367  1.00209.84           C  
ANISOU 1174  CG2 ILE A 160    21568  34135  24029  -4253  -8441   2071       C  
ATOM   1175  CD1 ILE A 160     -11.936 -11.647 -38.746  1.00216.41           C  
ANISOU 1175  CD1 ILE A 160    22722  35004  24500  -4426  -8977   2648       C  
ATOM   1176  N   ARG A 161     -10.735 -13.523 -40.982  1.00220.80           N  
ANISOU 1176  N   ARG A 161    23439  35114  25342  -3709  -9387   2516       N  
ATOM   1177  CA  ARG A 161     -10.219 -14.808 -40.521  1.00223.44           C  
ANISOU 1177  CA  ARG A 161    23887  35412  25597  -3560  -9666   2630       C  
ATOM   1178  C   ARG A 161      -9.304 -15.429 -41.565  1.00223.41           C  
ANISOU 1178  C   ARG A 161    23907  35277  25703  -3197  -9820   2501       C  
ATOM   1179  O   ARG A 161      -8.260 -16.002 -41.230  1.00225.48           O  
ANISOU 1179  O   ARG A 161    24154  35611  25907  -3020 -10003   2451       O  
ATOM   1180  CB  ARG A 161     -11.371 -15.760 -40.195  1.00224.24           C  
ANISOU 1180  CB  ARG A 161    24178  35364  25660  -3695  -9762   2933       C  
ATOM   1181  CG  ARG A 161     -12.183 -15.389 -38.967  1.00225.06           C  
ANISOU 1181  CG  ARG A 161    24274  35620  25619  -4050  -9664   3111       C  
ATOM   1182  CD  ARG A 161     -13.324 -16.377 -38.772  1.00225.91           C  
ANISOU 1182  CD  ARG A 161    24559  35550  25725  -4180  -9773   3423       C  
ATOM   1183  NE  ARG A 161     -14.184 -16.027 -37.645  1.00226.71           N  
ANISOU 1183  NE  ARG A 161    24654  35795  25691  -4534  -9676   3622       N  
ATOM   1184  CZ  ARG A 161     -15.298 -16.680 -37.330  1.00227.49           C  
ANISOU 1184  CZ  ARG A 161    24875  35774  25789  -4727  -9736   3914       C  
ATOM   1185  NH1 ARG A 161     -15.693 -17.714 -38.060  1.00227.57           N  
ANISOU 1185  NH1 ARG A 161    25024  35507  25935  -4599  -9895   4031       N  
ATOM   1186  NH2 ARG A 161     -16.022 -16.295 -36.288  1.00228.32           N  
ANISOU 1186  NH2 ARG A 161    24958  36036  25756  -5055  -9639   4096       N  
ATOM   1187  N   MET A 162      -9.680 -15.323 -42.840  1.00222.59           N  
ANISOU 1187  N   MET A 162    23841  34987  25746  -3079  -9752   2448       N  
ATOM   1188  CA  MET A 162      -8.820 -15.786 -43.917  1.00222.41           C  
ANISOU 1188  CA  MET A 162    23834  34855  25816  -2739  -9869   2323       C  
ATOM   1189  C   MET A 162      -7.655 -14.838 -44.163  1.00221.95           C  
ANISOU 1189  C   MET A 162    23562  34958  25810  -2637  -9787   2055       C  
ATOM   1190  O   MET A 162      -6.650 -15.249 -44.754  1.00222.60           O  
ANISOU 1190  O   MET A 162    23619  35018  25940  -2359  -9916   1951       O  
ATOM   1191  CB  MET A 162      -9.633 -15.949 -45.204  1.00220.31           C  
ANISOU 1191  CB  MET A 162    23691  34341  25677  -2649  -9827   2359       C  
ATOM   1192  CG  MET A 162     -10.827 -16.891 -45.086  1.00220.78           C  
ANISOU 1192  CG  MET A 162    23953  34205  25729  -2755  -9917   2622       C  
ATOM   1193  SD  MET A 162     -10.422 -18.567 -44.560  1.00223.89           S  
ANISOU 1193  SD  MET A 162    24514  34525  26029  -2614 -10217   2815       S  
ATOM   1194  CE  MET A 162     -10.994 -18.535 -42.861  1.00225.69           C  
ANISOU 1194  CE  MET A 162    24729  34917  26107  -2967 -10210   3007       C  
ATOM   1195  N   LEU A 163      -7.766 -13.583 -43.718  1.00212.83           N  
ANISOU 1195  N   LEU A 163    22248  33968  24651  -2864  -9572   1952       N  
ATOM   1196  CA  LEU A 163      -6.710 -12.603 -43.949  1.00212.42           C  
ANISOU 1196  CA  LEU A 163    21975  34061  24672  -2806  -9476   1703       C  
ATOM   1197  C   LEU A 163      -5.630 -12.693 -42.879  1.00215.08           C  
ANISOU 1197  C   LEU A 163    22197  34602  24922  -2803  -9603   1637       C  
ATOM   1198  O   LEU A 163      -4.437 -12.769 -43.195  1.00216.03           O  
ANISOU 1198  O   LEU A 163    22203  34764  25114  -2591  -9712   1486       O  
ATOM   1199  CB  LEU A 163      -7.308 -11.197 -43.996  1.00210.21           C  
ANISOU 1199  CB  LEU A 163    21576  33866  24427  -3055  -9171   1621       C  
ATOM   1200  CG  LEU A 163      -6.369 -10.030 -44.296  1.00209.51           C  
ANISOU 1200  CG  LEU A 163    21249  33921  24434  -3046  -9020   1375       C  
ATOM   1201  CD1 LEU A 163      -5.750 -10.179 -45.675  1.00208.55           C  
ANISOU 1201  CD1 LEU A 163    21108  33663  24469  -2752  -9081   1259       C  
ATOM   1202  CD2 LEU A 163      -7.130  -8.721 -44.186  1.00207.50           C  
ANISOU 1202  CD2 LEU A 163    20905  33761  24173  -3326  -8700   1335       C  
ATOM   1203  N   LEU A 164      -6.033 -12.683 -41.605  1.00208.46           N  
ANISOU 1203  N   LEU A 164    28470  28018  22718  -2655  -1765  -4588       N  
ATOM   1204  CA  LEU A 164      -5.072 -12.841 -40.519  1.00208.15           C  
ANISOU 1204  CA  LEU A 164    28469  27847  22771  -2610  -1829  -4578       C  
ATOM   1205  C   LEU A 164      -4.322 -14.162 -40.624  1.00213.30           C  
ANISOU 1205  C   LEU A 164    29566  28064  23415  -2563  -2039  -4989       C  
ATOM   1206  O   LEU A 164      -3.192 -14.273 -40.136  1.00213.00           O  
ANISOU 1206  O   LEU A 164    29624  27883  23424  -2415  -2056  -5086       O  
ATOM   1207  CB  LEU A 164      -5.785 -12.728 -39.168  1.00207.34           C  
ANISOU 1207  CB  LEU A 164    28158  27846  22775  -2904  -1881  -4278       C  
ATOM   1208  CG  LEU A 164      -6.915 -13.720 -38.856  1.00212.13           C  
ANISOU 1208  CG  LEU A 164    28896  28328  23377  -3287  -2057  -4303       C  
ATOM   1209  CD1 LEU A 164      -6.419 -15.018 -38.225  1.00216.96           C  
ANISOU 1209  CD1 LEU A 164    29840  28538  24058  -3457  -2310  -4515       C  
ATOM   1210  CD2 LEU A 164      -7.989 -13.066 -37.992  1.00209.54           C  
ANISOU 1210  CD2 LEU A 164    28240  28301  23074  -3531  -1943  -3920       C  
ATOM   1211  N   ARG A 165      -4.934 -15.171 -41.251  1.00205.66           N  
ANISOU 1211  N   ARG A 165    28870  26867  22403  -2690  -2194  -5254       N  
ATOM   1212  CA  ARG A 165      -4.252 -16.446 -41.446  1.00211.75           C  
ANISOU 1212  CA  ARG A 165    30072  27169  23213  -2616  -2380  -5707       C  
ATOM   1213  C   ARG A 165      -2.999 -16.280 -42.296  1.00212.63           C  
ANISOU 1213  C   ARG A 165    30399  27175  23216  -2183  -2230  -5959       C  
ATOM   1214  O   ARG A 165      -2.036 -17.039 -42.139  1.00216.07           O  
ANISOU 1214  O   ARG A 165    31153  27224  23720  -2017  -2310  -6288       O  
ATOM   1215  CB  ARG A 165      -5.204 -17.457 -42.088  1.00216.71           C  
ANISOU 1215  CB  ARG A 165    30914  27612  23814  -2841  -2529  -5937       C  
ATOM   1216  CG  ARG A 165      -4.641 -18.865 -42.197  1.00223.04           C  
ANISOU 1216  CG  ARG A 165    32128  27887  24731  -2835  -2698  -6428       C  
ATOM   1217  CD  ARG A 165      -5.626 -19.808 -42.867  1.00227.39           C  
ANISOU 1217  CD  ARG A 165    32884  28276  25236  -3112  -2811  -6617       C  
ATOM   1218  NE  ARG A 165      -5.870 -19.440 -44.259  1.00227.00           N  
ANISOU 1218  NE  ARG A 165    32849  28410  24991  -2872  -2719  -6740       N  
ATOM   1219  CZ  ARG A 165      -5.082 -19.791 -45.270  1.00230.18           C  
ANISOU 1219  CZ  ARG A 165    33521  28606  25333  -2495  -2684  -7159       C  
ATOM   1220  NH1 ARG A 165      -3.998 -20.521 -45.047  1.00233.48           N  
ANISOU 1220  NH1 ARG A 165    34157  28639  25917  -2281  -2702  -7559       N  
ATOM   1221  NH2 ARG A 165      -5.378 -19.413 -46.506  1.00229.90           N  
ANISOU 1221  NH2 ARG A 165    33527  28747  25077  -2347  -2593  -7182       N  
ATOM   1222  N   GLU A 166      -2.989 -15.292 -43.193  1.00210.73           N  
ANISOU 1222  N   GLU A 166    29978  27266  22823  -2022  -1966  -5802       N  
ATOM   1223  CA  GLU A 166      -1.793 -14.996 -43.969  1.00211.36           C  
ANISOU 1223  CA  GLU A 166    30162  27358  22788  -1688  -1697  -5962       C  
ATOM   1224  C   GLU A 166      -0.827 -14.089 -43.218  1.00206.94           C  
ANISOU 1224  C   GLU A 166    29268  27052  22307  -1562  -1499  -5751       C  
ATOM   1225  O   GLU A 166       0.340 -13.987 -43.611  1.00207.74           O  
ANISOU 1225  O   GLU A 166    29365  27184  22384  -1281  -1260  -5938       O  
ATOM   1226  CB  GLU A 166      -2.181 -14.367 -45.309  1.00210.96           C  
ANISOU 1226  CB  GLU A 166    29978  27588  22589  -1611  -1496  -5909       C  
ATOM   1227  CG  GLU A 166      -2.911 -15.331 -46.236  1.00216.10           C  
ANISOU 1227  CG  GLU A 166    30991  27988  23127  -1680  -1666  -6197       C  
ATOM   1228  CD  GLU A 166      -3.323 -14.693 -47.548  1.00215.52           C  
ANISOU 1228  CD  GLU A 166    30778  28202  22907  -1640  -1486  -6133       C  
ATOM   1229  OE1 GLU A 166      -3.161 -13.464 -47.692  1.00210.78           O  
ANISOU 1229  OE1 GLU A 166    29765  27990  22333  -1582  -1258  -5841       O  
ATOM   1230  OE2 GLU A 166      -3.811 -15.423 -48.437  1.00220.44           O  
ANISOU 1230  OE2 GLU A 166    31691  28655  23410  -1670  -1596  -6387       O  
ATOM   1231  N   ILE A 167      -1.286 -13.434 -42.154  1.00205.75           N  
ANISOU 1231  N   ILE A 167    28784  27119  22273  -1747  -1571  -5386       N  
ATOM   1232  CA  ILE A 167      -0.383 -12.721 -41.259  1.00201.58           C  
ANISOU 1232  CA  ILE A 167    27974  26784  21835  -1652  -1460  -5206       C  
ATOM   1233  C   ILE A 167       0.053 -13.612 -40.098  1.00203.78           C  
ANISOU 1233  C   ILE A 167    28488  26720  22220  -1768  -1705  -5341       C  
ATOM   1234  O   ILE A 167       1.180 -13.482 -39.609  1.00202.89           O  
ANISOU 1234  O   ILE A 167    28299  26629  22161  -1607  -1625  -5413       O  
ATOM   1235  CB  ILE A 167      -1.040 -11.423 -40.755  1.00194.80           C  
ANISOU 1235  CB  ILE A 167    26637  26326  21052  -1763  -1371  -4730       C  
ATOM   1236  CG1 ILE A 167      -1.312 -10.475 -41.923  1.00192.35           C  
ANISOU 1236  CG1 ILE A 167    26088  26307  20691  -1637  -1140  -4618       C  
ATOM   1237  CG2 ILE A 167      -0.164 -10.727 -39.724  1.00191.22           C  
ANISOU 1237  CG2 ILE A 167    25912  26051  20693  -1690  -1304  -4532       C  
ATOM   1238  CD1 ILE A 167      -2.156  -9.277 -41.550  1.00186.90           C  
ANISOU 1238  CD1 ILE A 167    24993  25911  20110  -1749  -1060  -4207       C  
ATOM   1239  N   LYS A 168      -0.819 -14.528 -39.657  1.00198.37           N  
ANISOU 1239  N   LYS A 168    28022  25741  21608  -2045  -2008  -5395       N  
ATOM   1240  CA  LYS A 168      -0.444 -15.505 -38.639  1.00201.98           C  
ANISOU 1240  CA  LYS A 168    28704  25806  22234  -2197  -2277  -5558       C  
ATOM   1241  C   LYS A 168       0.840 -16.234 -39.007  1.00206.68           C  
ANISOU 1241  C   LYS A 168    29714  25974  22840  -1912  -2246  -6008       C  
ATOM   1242  O   LYS A 168       1.629 -16.593 -38.125  1.00207.95           O  
ANISOU 1242  O   LYS A 168    29971  25884  23157  -1933  -2353  -6099       O  
ATOM   1243  CB  LYS A 168      -1.580 -16.511 -38.434  1.00206.47           C  
ANISOU 1243  CB  LYS A 168    29393  26148  22910  -2563  -2511  -5619       C  
ATOM   1244  CG  LYS A 168      -1.310 -17.557 -37.363  1.00210.87           C  
ANISOU 1244  CG  LYS A 168    30182  26268  23671  -2885  -2720  -5678       C  
ATOM   1245  CD  LYS A 168      -2.513 -18.467 -37.168  1.00214.05           C  
ANISOU 1245  CD  LYS A 168    30748  26471  24112  -3345  -2884  -5580       C  
ATOM   1246  CE  LYS A 168      -2.667 -19.428 -38.338  1.00219.18           C  
ANISOU 1246  CE  LYS A 168    31742  26787  24747  -3264  -2909  -6036       C  
ATOM   1247  NZ  LYS A 168      -3.769 -20.405 -38.118  1.00223.12           N  
ANISOU 1247  NZ  LYS A 168    32476  27037  25264  -3744  -3096  -5920       N  
ATOM   1248  N   ASN A 169       1.075 -16.449 -40.301  1.00200.35           N  
ANISOU 1248  N   ASN A 169    29155  25082  21887  -1678  -2025  -6278       N  
ATOM   1249  CA  ASN A 169       2.349 -16.983 -40.760  1.00204.77           C  
ANISOU 1249  CA  ASN A 169    29863  25402  22539  -1330  -1760  -6731       C  
ATOM   1250  C   ASN A 169       3.405 -15.890 -40.672  1.00200.61           C  
ANISOU 1250  C   ASN A 169    28757  25390  22074   -888  -1514  -6644       C  
ATOM   1251  O   ASN A 169       3.935 -15.438 -41.691  1.00199.68           O  
ANISOU 1251  O   ASN A 169    28437  25553  21881   -519  -1209  -6748       O  
ATOM   1252  CB  ASN A 169       2.228 -17.512 -42.191  1.00208.65           C  
ANISOU 1252  CB  ASN A 169    30658  25729  22890  -1180  -1569  -7040       C  
ATOM   1253  CG  ASN A 169       1.348 -18.743 -42.285  1.00213.78           C  
ANISOU 1253  CG  ASN A 169    31850  25846  23531  -1601  -1776  -7157       C  
ATOM   1254  OD1 ASN A 169       1.416 -19.635 -41.440  1.00217.57           O  
ANISOU 1254  OD1 ASN A 169    32226  26059  24380  -1806  -1904  -7459       O  
ATOM   1255  ND2 ASN A 169       0.514 -18.797 -43.317  1.00214.73           N  
ANISOU 1255  ND2 ASN A 169    32117  25992  23477  -1496  -1928  -7111       N  
ATOM   1256  N   ASP A 170       3.706 -15.454 -39.449  1.00200.45           N  
ANISOU 1256  N   ASP A 170    28477  25509  22176   -959  -1667  -6423       N  
ATOM   1257  CA  ASP A 170       4.643 -14.362 -39.213  1.00197.14           C  
ANISOU 1257  CA  ASP A 170    27521  25603  21780   -611  -1486  -6273       C  
ATOM   1258  C   ASP A 170       6.079 -14.877 -39.173  1.00202.11           C  
ANISOU 1258  C   ASP A 170    28132  25948  22712     60  -1476  -6506       C  
ATOM   1259  O   ASP A 170       6.931 -14.427 -39.947  1.00202.84           O  
ANISOU 1259  O   ASP A 170    27954  26360  22756    552  -1198  -6683       O  
ATOM   1260  CB  ASP A 170       4.275 -13.641 -37.909  1.00192.47           C  
ANISOU 1260  CB  ASP A 170    26680  25274  21177  -1008  -1645  -5809       C  
ATOM   1261  CG  ASP A 170       5.041 -12.344 -37.713  1.00188.07           C  
ANISOU 1261  CG  ASP A 170    25581  25297  20581   -760  -1443  -5547       C  
ATOM   1262  OD1 ASP A 170       5.897 -12.011 -38.557  1.00189.31           O  
ANISOU 1262  OD1 ASP A 170    25534  25675  20722   -284  -1197  -5722       O  
ATOM   1263  OD2 ASP A 170       4.778 -11.650 -36.708  1.00183.74           O  
ANISOU 1263  OD2 ASP A 170    24816  24977  20018  -1056  -1528  -5127       O  
ATOM   1264  N   ARG A 171       6.357 -15.821 -38.278  1.00196.75           N  
ANISOU 1264  N   ARG A 171    27727  24629  22400     72  -1743  -6299       N  
ATOM   1265  CA  ARG A 171       7.685 -16.414 -38.168  1.00205.55           C  
ANISOU 1265  CA  ARG A 171    28840  25348  23911    710  -1728  -6282       C  
ATOM   1266  C   ARG A 171       7.877 -17.428 -39.293  1.00211.70           C  
ANISOU 1266  C   ARG A 171    30012  25684  24742   1103  -1653  -6858       C  
ATOM   1267  O   ARG A 171       7.222 -18.475 -39.324  1.00214.90           O  
ANISOU 1267  O   ARG A 171    30953  25491  25208    865  -1888  -7049       O  
ATOM   1268  CB  ARG A 171       7.872 -17.037 -36.785  1.00210.28           C  
ANISOU 1268  CB  ARG A 171    29599  25417  24882    553  -2074  -5827       C  
ATOM   1269  CG  ARG A 171       6.823 -18.072 -36.389  1.00212.01           C  
ANISOU 1269  CG  ARG A 171    30381  25038  25136     21  -2424  -5854       C  
ATOM   1270  CD  ARG A 171       7.059 -18.609 -34.985  1.00215.98           C  
ANISOU 1270  CD  ARG A 171    31007  25067  25987   -163  -2775  -5355       C  
ATOM   1271  NE  ARG A 171       8.270 -19.420 -34.896  1.00226.64           N  
ANISOU 1271  NE  ARG A 171    32470  25851  27792    468  -2851  -5354       N  
ATOM   1272  CZ  ARG A 171       8.844 -19.781 -33.753  1.00232.05           C  
ANISOU 1272  CZ  ARG A 171    33159  26172  28837    491  -3116  -4894       C  
ATOM   1273  NH1 ARG A 171       8.318 -19.405 -32.596  1.00225.82           N  
ANISOU 1273  NH1 ARG A 171    32283  25537  27983   -107  -3318  -4409       N  
ATOM   1274  NH2 ARG A 171       9.944 -20.521 -33.767  1.00243.05           N  
ANISOU 1274  NH2 ARG A 171    34639  27059  30651   1114  -3180  -4922       N  
ATOM   1275  N   GLY A 172       8.762 -17.105 -40.235  1.00211.51           N  
ANISOU 1275  N   GLY A 172    29726  25971  24666   1685  -1326  -7142       N  
ATOM   1276  CA  GLY A 172       9.057 -18.005 -41.334  1.00217.34           C  
ANISOU 1276  CA  GLY A 172    30799  26343  25438   2124  -1208  -7721       C  
ATOM   1277  C   GLY A 172       7.896 -18.293 -42.256  1.00214.55           C  
ANISOU 1277  C   GLY A 172    30828  25958  24731   1724  -1198  -8147       C  
ATOM   1278  O   GLY A 172       7.900 -19.322 -42.938  1.00220.66           O  
ANISOU 1278  O   GLY A 172    32018  26227  25595   1884  -1175  -8460       O  
ATOM   1279  N   GLY A 173       6.897 -17.416 -42.302  1.00215.51           N  
ANISOU 1279  N   GLY A 173    30748  26611  24526   1094  -1123  -7829       N  
ATOM   1280  CA  GLY A 173       5.749 -17.621 -43.164  1.00215.22           C  
ANISOU 1280  CA  GLY A 173    30987  26575  24214    584  -1030  -7825       C  
ATOM   1281  C   GLY A 173       5.610 -16.542 -44.218  1.00210.86           C  
ANISOU 1281  C   GLY A 173    30085  26676  23358    541   -682  -7627       C  
ATOM   1282  O   GLY A 173       4.504 -16.064 -44.490  1.00206.14           O  
ANISOU 1282  O   GLY A 173    29521  26288  22515     57   -705  -7337       O  
ATOM   1283  N   GLU A 174       6.730 -16.154 -44.819  1.00221.32           N  
ANISOU 1283  N   GLU A 174    31079  28288  24726   1084   -407  -7740       N  
ATOM   1284  CA  GLU A 174       6.789 -15.021 -45.727  1.00218.46           C  
ANISOU 1284  CA  GLU A 174    30324  28541  24142   1072   -130  -7496       C  
ATOM   1285  C   GLU A 174       7.298 -15.479 -47.090  1.00224.01           C  
ANISOU 1285  C   GLU A 174    31150  29187  24776   1401    134  -7822       C  
ATOM   1286  O   GLU A 174       8.088 -16.424 -47.182  1.00231.25           O  
ANISOU 1286  O   GLU A 174    32251  29728  25884   1853    178  -8208       O  
ATOM   1287  CB  GLU A 174       7.700 -13.929 -45.148  1.00214.73           C  
ANISOU 1287  CB  GLU A 174    29263  28578  23745   1327    -48  -7231       C  
ATOM   1288  CG  GLU A 174       7.255 -13.438 -43.780  1.00210.01           C  
ANISOU 1288  CG  GLU A 174    28537  28060  23195   1001   -292  -6908       C  
ATOM   1289  CD  GLU A 174       5.884 -12.793 -43.802  1.00205.95           C  
ANISOU 1289  CD  GLU A 174    28047  27704  22501    401   -371  -6515       C  
ATOM   1290  OE1 GLU A 174       5.532 -12.160 -44.819  1.00205.48           O  
ANISOU 1290  OE1 GLU A 174    27869  27907  22298    323   -213  -6362       O  
ATOM   1291  OE2 GLU A 174       5.153 -12.924 -42.796  1.00203.50           O  
ANISOU 1291  OE2 GLU A 174    27869  27233  22219     35   -616  -6344       O  
ATOM   1292  N   ASP A 175       6.846 -14.815 -48.157  1.00223.47           N  
ANISOU 1292  N   ASP A 175    30988  29461  24460   1200    288  -7656       N  
ATOM   1293  CA  ASP A 175       5.915 -13.689 -48.088  1.00216.22           C  
ANISOU 1293  CA  ASP A 175    29843  28913  23396    761    205  -7180       C  
ATOM   1294  C   ASP A 175       4.874 -13.707 -49.207  1.00216.68           C  
ANISOU 1294  C   ASP A 175    30161  28946  23220    465    201  -7145       C  
ATOM   1295  O   ASP A 175       5.191 -13.994 -50.361  1.00220.79           O  
ANISOU 1295  O   ASP A 175    30802  29464  23625    639    383  -7386       O  
ATOM   1296  CB  ASP A 175       6.683 -12.359 -48.118  1.00212.09           C  
ANISOU 1296  CB  ASP A 175    28710  28972  22903    931    357  -6870       C  
ATOM   1297  CG  ASP A 175       7.590 -12.224 -49.332  1.00215.91           C  
ANISOU 1297  CG  ASP A 175    29032  29686  23316   1271    628  -7041       C  
ATOM   1298  OD1 ASP A 175       7.724 -13.196 -50.104  1.00222.40           O  
ANISOU 1298  OD1 ASP A 175    30203  30217  24083   1438    731  -7430       O  
ATOM   1299  OD2 ASP A 175       8.171 -11.134 -49.516  1.00213.46           O  
ANISOU 1299  OD2 ASP A 175    28257  29844  23004   1353    729  -6778       O  
ATOM   1300  N   PRO A 176       3.629 -13.414 -48.861  1.00215.87           N  
ANISOU 1300  N   PRO A 176    30134  28831  23056     47    -22  -6847       N  
ATOM   1301  CA  PRO A 176       2.592 -13.207 -49.875  1.00215.73           C  
ANISOU 1301  CA  PRO A 176    30239  28878  22852   -186    -71  -6742       C  
ATOM   1302  C   PRO A 176       2.740 -11.823 -50.500  1.00211.56           C  
ANISOU 1302  C   PRO A 176    29202  28865  22315   -154     80  -6430       C  
ATOM   1303  O   PRO A 176       3.613 -11.037 -50.136  1.00208.89           O  
ANISOU 1303  O   PRO A 176    28447  28824  22096     21    201  -6278       O  
ATOM   1304  CB  PRO A 176       1.293 -13.335 -49.077  1.00212.88           C  
ANISOU 1304  CB  PRO A 176    30022  28355  22510   -561   -388  -6514       C  
ATOM   1305  CG  PRO A 176       1.672 -12.932 -47.694  1.00208.67           C  
ANISOU 1305  CG  PRO A 176    29218  27904  22164   -569   -442  -6307       C  
ATOM   1306  CD  PRO A 176       3.082 -13.396 -47.493  1.00211.94           C  
ANISOU 1306  CD  PRO A 176    29633  28221  22673   -206   -271  -6625       C  
ATOM   1307  N   ASN A 177       1.865 -11.533 -51.460  1.00211.64           N  
ANISOU 1307  N   ASN A 177    29255  28966  22193   -331     42  -6338       N  
ATOM   1308  CA  ASN A 177       1.888 -10.243 -52.140  1.00207.78           C  
ANISOU 1308  CA  ASN A 177    28329  28905  21715   -344    148  -6057       C  
ATOM   1309  C   ASN A 177       1.484  -9.142 -51.168  1.00201.01           C  
ANISOU 1309  C   ASN A 177    27024  28301  21051   -505     58  -5649       C  
ATOM   1310  O   ASN A 177       0.328  -9.076 -50.739  1.00199.25           O  
ANISOU 1310  O   ASN A 177    26777  28061  20866   -774   -102  -5513       O  
ATOM   1311  CB  ASN A 177       0.958 -10.260 -53.350  1.00210.20           C  
ANISOU 1311  CB  ASN A 177    28705  29308  21854   -530    115  -6153       C  
ATOM   1312  CG  ASN A 177       1.433 -11.197 -54.439  1.00216.49           C  
ANISOU 1312  CG  ASN A 177    29931  29886  22439   -351    232  -6537       C  
ATOM   1313  OD1 ASN A 177       0.784 -12.198 -54.738  1.00221.06           O  
ANISOU 1313  OD1 ASN A 177    30997  30116  22879   -438    103  -6752       O  
ATOM   1314  ND2 ASN A 177       2.569 -10.871 -55.045  1.00217.21           N  
ANISOU 1314  ND2 ASN A 177    29838  30190  22503    -97    469  -6630       N  
ATOM   1315  N   GLN A 178       2.437  -8.275 -50.814  1.00204.85           N  
ANISOU 1315  N   GLN A 178    27120  29053  21659   -344    170  -5478       N  
ATOM   1316  CA  GLN A 178       2.088  -7.063 -50.084  1.00199.65           C  
ANISOU 1316  CA  GLN A 178    25975  28707  21176   -494    114  -5125       C  
ATOM   1317  C   GLN A 178       1.160  -6.173 -50.896  1.00198.61           C  
ANISOU 1317  C   GLN A 178    25507  28923  21033   -721    117  -5022       C  
ATOM   1318  O   GLN A 178       0.466  -5.327 -50.324  1.00194.57           O  
ANISOU 1318  O   GLN A 178    24676  28595  20657   -904     65  -4764       O  
ATOM   1319  CB  GLN A 178       3.349  -6.283 -49.706  1.00197.41           C  
ANISOU 1319  CB  GLN A 178    25352  28654  21001   -273    213  -4979       C  
ATOM   1320  CG  GLN A 178       4.100  -5.711 -50.899  1.00199.65           C  
ANISOU 1320  CG  GLN A 178    25378  29272  21208   -134    356  -5056       C  
ATOM   1321  CD  GLN A 178       5.345  -4.948 -50.496  1.00197.83           C  
ANISOU 1321  CD  GLN A 178    24805  29285  21075     70    418  -4895       C  
ATOM   1322  OE1 GLN A 178       5.638  -4.796 -49.310  1.00195.46           O  
ANISOU 1322  OE1 GLN A 178    24452  28910  20905    105    361  -4716       O  
ATOM   1323  NE2 GLN A 178       6.085  -4.458 -51.486  1.00199.16           N  
ANISOU 1323  NE2 GLN A 178    24742  29763  21167    188    523  -4953       N  
ATOM   1324  N   LYS A 179       1.146  -6.344 -52.217  1.00202.47           N  
ANISOU 1324  N   LYS A 179    26068  29502  21359   -710    191  -5228       N  
ATOM   1325  CA  LYS A 179       0.226  -5.603 -53.071  1.00202.46           C  
ANISOU 1325  CA  LYS A 179    25797  29804  21324   -943    187  -5157       C  
ATOM   1326  C   LYS A 179      -1.212  -6.060 -52.853  1.00202.95           C  
ANISOU 1326  C   LYS A 179    26036  29711  21364  -1218     63  -5145       C  
ATOM   1327  O   LYS A 179      -2.124  -5.236 -52.712  1.00200.88           O  
ANISOU 1327  O   LYS A 179    25452  29680  21194  -1434     41  -4933       O  
ATOM   1328  CB  LYS A 179       0.650  -5.779 -54.529  1.00206.92           C  
ANISOU 1328  CB  LYS A 179    26439  30489  21692   -864    293  -5401       C  
ATOM   1329  CG  LYS A 179      -0.215  -5.100 -55.567  1.00207.38           C  
ANISOU 1329  CG  LYS A 179    26264  30851  21679  -1104    292  -5362       C  
ATOM   1330  CD  LYS A 179       0.446  -5.242 -56.927  1.00211.08           C  
ANISOU 1330  CD  LYS A 179    26796  31460  21946   -999    408  -5600       C  
ATOM   1331  CE  LYS A 179       0.420  -6.690 -57.393  1.00216.43           C  
ANISOU 1331  CE  LYS A 179    28050  31765  22418   -919    423  -5953       C  
ATOM   1332  NZ  LYS A 179       1.041  -6.862 -58.733  1.00220.74           N  
ANISOU 1332  NZ  LYS A 179    28674  32450  22747   -812    561  -6209       N  
ATOM   1333  N   VAL A 180      -1.429  -7.376 -52.803  1.00203.79           N  
ANISOU 1333  N   VAL A 180    26659  29423  21349  -1211    -22  -5372       N  
ATOM   1334  CA  VAL A 180      -2.782  -7.904 -52.654  1.00204.71           C  
ANISOU 1334  CA  VAL A 180    26958  29398  21423  -1485   -169  -5376       C  
ATOM   1335  C   VAL A 180      -3.311  -7.638 -51.249  1.00201.06           C  
ANISOU 1335  C   VAL A 180    26341  28909  21142  -1612   -260  -5115       C  
ATOM   1336  O   VAL A 180      -4.396  -7.071 -51.076  1.00199.32           O  
ANISOU 1336  O   VAL A 180    25853  28897  20981  -1859   -276  -4934       O  
ATOM   1337  CB  VAL A 180      -2.812  -9.405 -52.994  1.00209.51           C  
ANISOU 1337  CB  VAL A 180    28191  29563  21850  -1434   -279  -5704       C  
ATOM   1338  CG1 VAL A 180      -4.188  -9.980 -52.715  1.00210.51           C  
ANISOU 1338  CG1 VAL A 180    28487  29549  21950  -1731   -475  -5692       C  
ATOM   1339  CG2 VAL A 180      -2.429  -9.623 -54.449  1.00213.85           C  
ANISOU 1339  CG2 VAL A 180    28883  30172  22198  -1336   -166  -5970       C  
ATOM   1340  N   ILE A 181      -2.555  -8.043 -50.225  1.00204.72           N  
ANISOU 1340  N   ILE A 181    26973  29125  21685  -1447   -306  -5095       N  
ATOM   1341  CA  ILE A 181      -3.007  -7.845 -48.850  1.00200.90           C  
ANISOU 1341  CA  ILE A 181    26368  28610  21357  -1574   -396  -4857       C  
ATOM   1342  C   ILE A 181      -3.060  -6.361 -48.512  1.00196.41           C  
ANISOU 1342  C   ILE A 181    25222  28452  20952  -1613   -270  -4559       C  
ATOM   1343  O   ILE A 181      -3.970  -5.903 -47.810  1.00194.41           O  
ANISOU 1343  O   ILE A 181    24752  28322  20794  -1814   -288  -4357       O  
ATOM   1344  CB  ILE A 181      -2.108  -8.618 -47.869  1.00200.54           C  
ANISOU 1344  CB  ILE A 181    26653  28197  21347  -1391   -489  -4910       C  
ATOM   1345  CG1 ILE A 181      -2.209 -10.121 -48.126  1.00205.54           C  
ANISOU 1345  CG1 ILE A 181    27902  28360  21834  -1369   -658  -5211       C  
ATOM   1346  CG2 ILE A 181      -2.493  -8.314 -46.431  1.00196.70           C  
ANISOU 1346  CG2 ILE A 181    26001  27719  21016  -1527   -575  -4647       C  
ATOM   1347  CD1 ILE A 181      -1.206 -10.926 -47.344  1.00206.85           C  
ANISOU 1347  CD1 ILE A 181    28376  28200  22020  -1197   -713  -5369       C  
ATOM   1348  N   HIS A 182      -2.092  -5.584 -49.004  1.00200.45           N  
ANISOU 1348  N   HIS A 182    25481  29183  21498  -1421   -144  -4534       N  
ATOM   1349  CA  HIS A 182      -2.129  -4.142 -48.784  1.00196.73           C  
ANISOU 1349  CA  HIS A 182    24488  29078  21182  -1452    -58  -4270       C  
ATOM   1350  C   HIS A 182      -3.331  -3.508 -49.469  1.00196.94           C  
ANISOU 1350  C   HIS A 182    24274  29362  21192  -1682    -24  -4206       C  
ATOM   1351  O   HIS A 182      -3.863  -2.504 -48.984  1.00194.13           O  
ANISOU 1351  O   HIS A 182    23569  29225  20967  -1779     19  -3981       O  
ATOM   1352  CB  HIS A 182      -0.832  -3.498 -49.276  1.00195.97           C  
ANISOU 1352  CB  HIS A 182    24187  29165  21107  -1217     32  -4270       C  
ATOM   1353  CG  HIS A 182      -0.764  -2.022 -49.040  1.00192.48           C  
ANISOU 1353  CG  HIS A 182    23251  29058  20824  -1236     84  -4007       C  
ATOM   1354  ND1 HIS A 182      -0.560  -1.477 -47.791  1.00189.16           N  
ANISOU 1354  ND1 HIS A 182    22662  28644  20565  -1213     72  -3785       N  
ATOM   1355  CD2 HIS A 182      -0.874  -0.977 -49.893  1.00192.02           C  
ANISOU 1355  CD2 HIS A 182    22860  29320  20779  -1278    139  -3938       C  
ATOM   1356  CE1 HIS A 182      -0.546  -0.159 -47.885  1.00186.96           C  
ANISOU 1356  CE1 HIS A 182    21982  28658  20396  -1228    122  -3599       C  
ATOM   1357  NE2 HIS A 182      -0.734   0.170 -49.150  1.00188.49           N  
ANISOU 1357  NE2 HIS A 182    22071  29042  20504  -1267    156  -3684       N  
ATOM   1358  N   GLY A 183      -3.774  -4.077 -50.592  1.00200.88           N  
ANISOU 1358  N   GLY A 183    24971  29834  21521  -1765    -37  -4409       N  
ATOM   1359  CA  GLY A 183      -4.997  -3.602 -51.212  1.00202.11           C  
ANISOU 1359  CA  GLY A 183    24940  30214  21639  -2005    -18  -4354       C  
ATOM   1360  C   GLY A 183      -6.243  -4.000 -50.447  1.00202.03           C  
ANISOU 1360  C   GLY A 183    25004  30117  21642  -2240    -86  -4274       C  
ATOM   1361  O   GLY A 183      -7.215  -3.241 -50.404  1.00200.36           O  
ANISOU 1361  O   GLY A 183    24501  30150  21477  -2411    -37  -4117       O  
ATOM   1362  N   VAL A 184      -6.234  -5.184 -49.830  1.00200.30           N  
ANISOU 1362  N   VAL A 184    25176  29556  21374  -2250   -203  -4383       N  
ATOM   1363  CA  VAL A 184      -7.398  -5.641 -49.076  1.00200.23           C  
ANISOU 1363  CA  VAL A 184    25243  29472  21362  -2499   -285  -4307       C  
ATOM   1364  C   VAL A 184      -7.557  -4.828 -47.796  1.00196.23           C  
ANISOU 1364  C   VAL A 184    24421  29105  21033  -2522   -224  -4037       C  
ATOM   1365  O   VAL A 184      -8.647  -4.331 -47.490  1.00195.46           O  
ANISOU 1365  O   VAL A 184    24088  29217  20961  -2723   -172  -3889       O  
ATOM   1366  CB  VAL A 184      -7.291  -7.147 -48.778  1.00203.41           C  
ANISOU 1366  CB  VAL A 184    26172  29447  21667  -2506   -468  -4505       C  
ATOM   1367  CG1 VAL A 184      -8.425  -7.586 -47.863  1.00203.64           C  
ANISOU 1367  CG1 VAL A 184    26242  29423  21708  -2783   -567  -4396       C  
ATOM   1368  CG2 VAL A 184      -7.313  -7.947 -50.070  1.00208.14           C  
ANISOU 1368  CG2 VAL A 184    27102  29910  22073  -2504   -526  -4790       C  
ATOM   1369  N   ILE A 185      -6.475  -4.684 -47.028  1.00198.17           N  
ANISOU 1369  N   ILE A 185    24665  29242  21388  -2314   -220  -3976       N  
ATOM   1370  CA  ILE A 185      -6.547  -3.925 -45.784  1.00194.53           C  
ANISOU 1370  CA  ILE A 185    23932  28897  21083  -2330   -162  -3731       C  
ATOM   1371  C   ILE A 185      -6.699  -2.437 -46.074  1.00191.92           C  
ANISOU 1371  C   ILE A 185    23133  28933  20855  -2300    -12  -3569       C  
ATOM   1372  O   ILE A 185      -7.507  -1.747 -45.440  1.00190.08           O  
ANISOU 1372  O   ILE A 185    22647  28883  20690  -2419     61  -3400       O  
ATOM   1373  CB  ILE A 185      -5.311  -4.208 -44.911  1.00192.86           C  
ANISOU 1373  CB  ILE A 185    23869  28463  20946  -2126   -216  -3712       C  
ATOM   1374  CG1 ILE A 185      -5.263  -5.684 -44.515  1.00195.12           C  
ANISOU 1374  CG1 ILE A 185    24645  28354  21140  -2164   -400  -3869       C  
ATOM   1375  CG2 ILE A 185      -5.321  -3.333 -43.668  1.00189.35           C  
ANISOU 1375  CG2 ILE A 185    23135  28155  20653  -2143   -145  -3456       C  
ATOM   1376  CD1 ILE A 185      -3.964  -6.099 -43.863  1.00194.20           C  
ANISOU 1376  CD1 ILE A 185    24740  27983  21064  -1936   -474  -3899       C  
ATOM   1377  N   ASN A 186      -5.932  -1.920 -47.037  1.00197.87           N  
ANISOU 1377  N   ASN A 186    23774  29800  21608  -2138     31  -3628       N  
ATOM   1378  CA  ASN A 186      -6.045  -0.514 -47.406  1.00195.87           C  
ANISOU 1378  CA  ASN A 186    23109  29870  21444  -2109    136  -3486       C  
ATOM   1379  C   ASN A 186      -7.405  -0.196 -48.014  1.00197.03           C  
ANISOU 1379  C   ASN A 186    23121  30219  21521  -2316    175  -3475       C  
ATOM   1380  O   ASN A 186      -7.828   0.964 -47.991  1.00195.42           O  
ANISOU 1380  O   ASN A 186    22593  30262  21395  -2323    256  -3331       O  
ATOM   1381  CB  ASN A 186      -4.927  -0.142 -48.385  1.00196.44           C  
ANISOU 1381  CB  ASN A 186    23115  30023  21500  -1923    150  -3561       C  
ATOM   1382  CG  ASN A 186      -4.746   1.361 -48.530  1.00193.80           C  
ANISOU 1382  CG  ASN A 186    22378  29975  21282  -1860    225  -3387       C  
ATOM   1383  OD1 ASN A 186      -5.430   2.151 -47.882  1.00191.15           O  
ANISOU 1383  OD1 ASN A 186    21829  29759  21042  -1924    277  -3221       O  
ATOM   1384  ND2 ASN A 186      -3.815   1.760 -49.390  1.00194.82           N  
ANISOU 1384  ND2 ASN A 186    22421  30216  21388  -1731    232  -3431       N  
ATOM   1385  N   SER A 187      -8.103  -1.202 -48.544  1.00197.58           N  
ANISOU 1385  N   SER A 187    23453  30183  21437  -2481    111  -3627       N  
ATOM   1386  CA  SER A 187      -9.433  -0.993 -49.100  1.00199.53           C  
ANISOU 1386  CA  SER A 187    23589  30629  21596  -2699    138  -3614       C  
ATOM   1387  C   SER A 187     -10.461  -0.609 -48.044  1.00197.70           C  
ANISOU 1387  C   SER A 187    23176  30519  21423  -2835    192  -3445       C  
ATOM   1388  O   SER A 187     -11.548  -0.146 -48.405  1.00198.82           O  
ANISOU 1388  O   SER A 187    23141  30892  21508  -2980    240  -3398       O  
ATOM   1389  CB  SER A 187      -9.897  -2.252 -49.835  1.00203.73           C  
ANISOU 1389  CB  SER A 187    24479  30994  21937  -2860     38  -3819       C  
ATOM   1390  OG  SER A 187     -11.206  -2.090 -50.352  1.00206.95           O  
ANISOU 1390  OG  SER A 187    24781  31607  22245  -3095     56  -3796       O  
ATOM   1391  N   PHE A 188     -10.149  -0.784 -46.758  1.00192.63           N  
ANISOU 1391  N   PHE A 188    22574  29742  20875  -2793    188  -3356       N  
ATOM   1392  CA  PHE A 188     -11.125  -0.472 -45.722  1.00191.60           C  
ANISOU 1392  CA  PHE A 188    22283  29744  20773  -2931    253  -3209       C  
ATOM   1393  C   PHE A 188     -11.170   1.021 -45.422  1.00188.74           C  
ANISOU 1393  C   PHE A 188    21537  29639  20537  -2806    380  -3053       C  
ATOM   1394  O   PHE A 188     -12.256   1.582 -45.241  1.00188.76           O  
ANISOU 1394  O   PHE A 188    21336  29873  20511  -2908    458  -2981       O  
ATOM   1395  CB  PHE A 188     -10.824  -1.270 -44.452  1.00191.20           C  
ANISOU 1395  CB  PHE A 188    22444  29455  20749  -2965    194  -3174       C  
ATOM   1396  CG  PHE A 188     -11.069  -2.746 -44.594  1.00194.44           C  
ANISOU 1396  CG  PHE A 188    23250  29606  21020  -3129     46  -3318       C  
ATOM   1397  CD1 PHE A 188     -11.767  -3.244 -45.682  1.00197.49           C  
ANISOU 1397  CD1 PHE A 188    23754  30023  21260  -3278     -4  -3450       C  
ATOM   1398  CD2 PHE A 188     -10.611  -3.636 -43.636  1.00194.65           C  
ANISOU 1398  CD2 PHE A 188    23551  29349  21057  -3140    -61  -3322       C  
ATOM   1399  CE1 PHE A 188     -11.992  -4.596 -45.818  1.00200.76           C  
ANISOU 1399  CE1 PHE A 188    24557  30177  21546  -3429   -161  -3593       C  
ATOM   1400  CE2 PHE A 188     -10.838  -4.993 -43.766  1.00197.92           C  
ANISOU 1400  CE2 PHE A 188    24356  29496  21349  -3283   -231  -3465       C  
ATOM   1401  CZ  PHE A 188     -11.530  -5.473 -44.858  1.00201.02           C  
ANISOU 1401  CZ  PHE A 188    24868  29910  21601  -3426   -282  -3606       C  
ATOM   1402  N   VAL A 189     -10.018   1.683 -45.359  1.00201.44           N  
ANISOU 1402  N   VAL A 189    23053  31214  22272  -2581    395  -3005       N  
ATOM   1403  CA  VAL A 189      -9.990   3.143 -45.162  1.00199.72           C  
ANISOU 1403  CA  VAL A 189    22509  31209  22166  -2450    491  -2868       C  
ATOM   1404  C   VAL A 189     -10.009   3.753 -46.560  1.00200.82           C  
ANISOU 1404  C   VAL A 189    22534  31509  22261  -2406    492  -2919       C  
ATOM   1405  O   VAL A 189      -8.996   4.196 -47.107  1.00200.79           O  
ANISOU 1405  O   VAL A 189    22488  31497  22306  -2255    473  -2921       O  
ATOM   1406  CB  VAL A 189      -8.780   3.595 -44.337  1.00197.56           C  
ANISOU 1406  CB  VAL A 189    22197  30829  22039  -2263    497  -2770       C  
ATOM   1407  CG1 VAL A 189      -8.789   5.111 -44.149  1.00195.60           C  
ANISOU 1407  CG1 VAL A 189    21656  30774  21889  -2136    580  -2638       C  
ATOM   1408  CG2 VAL A 189      -8.750   2.887 -43.003  1.00197.51           C  
ANISOU 1408  CG2 VAL A 189    22341  30653  22050  -2332    484  -2723       C  
ATOM   1409  N   HIS A 190     -11.195   3.756 -47.162  1.00203.93           N  
ANISOU 1409  N   HIS A 190    22879  32066  22539  -2561    509  -2956       N  
ATOM   1410  CA  HIS A 190     -11.461   4.594 -48.326  1.00204.87           C  
ANISOU 1410  CA  HIS A 190    22843  32389  22607  -2536    524  -2961       C  
ATOM   1411  C   HIS A 190     -12.850   5.210 -48.327  1.00205.21           C  
ANISOU 1411  C   HIS A 190    22711  32676  22583  -2630    582  -2908       C  
ATOM   1412  O   HIS A 190     -13.050   6.228 -48.999  1.00205.44           O  
ANISOU 1412  O   HIS A 190    22580  32882  22596  -2559    603  -2867       O  
ATOM   1413  CB  HIS A 190     -11.265   3.801 -49.624  1.00207.32           C  
ANISOU 1413  CB  HIS A 190    23341  32646  22786  -2626    449  -3116       C  
ATOM   1414  CG  HIS A 190     -11.196   4.660 -50.848  1.00207.96           C  
ANISOU 1414  CG  HIS A 190    23284  32915  22816  -2589    455  -3114       C  
ATOM   1415  ND1 HIS A 190     -12.317   5.059 -51.544  1.00209.81           N  
ANISOU 1415  ND1 HIS A 190    23422  33360  22936  -2717    467  -3105       N  
ATOM   1416  CD2 HIS A 190     -10.138   5.205 -51.494  1.00207.10           C  
ANISOU 1416  CD2 HIS A 190    23120  32828  22740  -2451    444  -3112       C  
ATOM   1417  CE1 HIS A 190     -11.952   5.809 -52.570  1.00209.91           C  
ANISOU 1417  CE1 HIS A 190    23346  33499  22913  -2662    460  -3095       C  
ATOM   1418  NE2 HIS A 190     -10.635   5.913 -52.562  1.00208.72           N  
ANISOU 1418  NE2 HIS A 190    23213  33243  22848  -2508    450  -3099       N  
ATOM   1419  N   VAL A 191     -13.809   4.646 -47.596  1.00204.38           N  
ANISOU 1419  N   VAL A 191    22637  32597  22421  -2786    605  -2905       N  
ATOM   1420  CA  VAL A 191     -15.222   4.979 -47.724  1.00205.68           C  
ANISOU 1420  CA  VAL A 191    22663  33016  22470  -2909    648  -2887       C  
ATOM   1421  C   VAL A 191     -15.646   5.764 -46.492  1.00204.07           C  
ANISOU 1421  C   VAL A 191    22340  32846  22351  -2782    699  -2769       C  
ATOM   1422  O   VAL A 191     -15.634   5.233 -45.375  1.00203.60           O  
ANISOU 1422  O   VAL A 191    22353  32679  22328  -2830    715  -2739       O  
ATOM   1423  CB  VAL A 191     -16.079   3.714 -47.883  1.00208.09           C  
ANISOU 1423  CB  VAL A 191    23147  33304  22615  -3191    599  -2967       C  
ATOM   1424  CG1 VAL A 191     -17.555   4.075 -47.968  1.00210.38           C  
ANISOU 1424  CG1 VAL A 191    23267  33896  22770  -3324    643  -2936       C  
ATOM   1425  CG2 VAL A 191     -15.629   2.913 -49.097  1.00209.90           C  
ANISOU 1425  CG2 VAL A 191    23604  33390  22760  -3274    498  -3093       C  
ATOM   1426  N   GLU A 192     -16.026   7.024 -46.697  1.00212.17           N  
ANISOU 1426  N   GLU A 192    23313  33889  23413  -2581    652  -2685       N  
ATOM   1427  CA  GLU A 192     -16.584   7.843 -45.631  1.00211.85           C  
ANISOU 1427  CA  GLU A 192    23281  33766  23446  -2412    625  -2580       C  
ATOM   1428  C   GLU A 192     -17.240   9.073 -46.239  1.00212.55           C  
ANISOU 1428  C   GLU A 192    23274  33990  23494  -2273    589  -2552       C  
ATOM   1429  O   GLU A 192     -16.762   9.602 -47.246  1.00211.62           O  
ANISOU 1429  O   GLU A 192    23131  33907  23368  -2209    566  -2556       O  
ATOM   1430  CB  GLU A 192     -15.510   8.259 -44.614  1.00209.67           C  
ANISOU 1430  CB  GLU A 192    23121  33184  23359  -2204    593  -2480       C  
ATOM   1431  CG  GLU A 192     -16.038   9.126 -43.476  1.00209.71           C  
ANISOU 1431  CG  GLU A 192    23137  33110  23434  -2046    571  -2390       C  
ATOM   1432  CD  GLU A 192     -17.084   8.419 -42.629  1.00211.23           C  
ANISOU 1432  CD  GLU A 192    23303  33417  23539  -2215    611  -2414       C  
ATOM   1433  OE1 GLU A 192     -17.053   7.173 -42.549  1.00212.14           O  
ANISOU 1433  OE1 GLU A 192    23448  33574  23580  -2448    654  -2466       O  
ATOM   1434  OE2 GLU A 192     -17.945   9.114 -42.049  1.00211.95           O  
ANISOU 1434  OE2 GLU A 192    23338  33578  23615  -2127    602  -2389       O  
ATOM   1435  N   GLN A 193     -18.338   9.506 -45.624  1.00220.45           N  
ANISOU 1435  N   GLN A 193    24214  35096  24449  -2237    586  -2533       N  
ATOM   1436  CA  GLN A 193     -19.062  10.708 -46.026  1.00222.42           C  
ANISOU 1436  CA  GLN A 193    24360  35505  24644  -2092    550  -2523       C  
ATOM   1437  C   GLN A 193     -18.142  11.918 -46.148  1.00221.23           C  
ANISOU 1437  C   GLN A 193    24260  35180  24619  -1838    499  -2455       C  
ATOM   1438  O   GLN A 193     -17.352  12.202 -45.248  1.00219.04           O  
ANISOU 1438  O   GLN A 193    24090  34643  24493  -1700    483  -2386       O  
ATOM   1439  CB  GLN A 193     -20.177  11.003 -45.020  1.00222.90           C  
ANISOU 1439  CB  GLN A 193    24359  35666  24668  -2047    553  -2522       C  
ATOM   1440  CG  GLN A 193     -21.040  12.203 -45.365  1.00224.08           C  
ANISOU 1440  CG  GLN A 193    24377  36031  24733  -1894    516  -2543       C  
ATOM   1441  CD  GLN A 193     -22.137  12.436 -44.344  1.00224.66           C  
ANISOU 1441  CD  GLN A 193    24372  36235  24754  -1848    522  -2567       C  
ATOM   1442  OE1 GLN A 193     -22.237  11.717 -43.349  1.00224.24           O  
ANISOU 1442  OE1 GLN A 193    24368  36101  24732  -1941    557  -2552       O  
ATOM   1443  NE2 GLN A 193     -22.963  13.447 -44.583  1.00225.22           N  
ANISOU 1443  NE2 GLN A 193    24308  36535  24729  -1707    487  -2611       N  
ATOM   1444  N   PHE A 198     -15.053  10.739 -38.219  1.00193.99           N  
ANISOU 1444  N   PHE A 198    21424  30441  21845  -1640    526  -2065       N  
ATOM   1445  CA  PHE A 198     -14.852   9.338 -37.858  1.00194.71           C  
ANISOU 1445  CA  PHE A 198    21564  30523  21894  -1852    564  -2079       C  
ATOM   1446  C   PHE A 198     -14.626   8.411 -39.063  1.00195.86           C  
ANISOU 1446  C   PHE A 198    21691  30761  21966  -1992    582  -2160       C  
ATOM   1447  O   PHE A 198     -15.353   7.437 -39.247  1.00199.08           O  
ANISOU 1447  O   PHE A 198    22056  31341  22243  -2212    624  -2235       O  
ATOM   1448  CB  PHE A 198     -16.043   8.853 -37.014  1.00196.85           C  
ANISOU 1448  CB  PHE A 198    21781  30952  22060  -2005    604  -2107       C  
ATOM   1449  CG  PHE A 198     -17.394   9.119 -37.638  1.00199.36           C  
ANISOU 1449  CG  PHE A 198    21958  31536  22254  -2032    616  -2186       C  
ATOM   1450  CD1 PHE A 198     -18.037  10.329 -37.424  1.00199.00           C  
ANISOU 1450  CD1 PHE A 198    21834  31557  22220  -1851    593  -2191       C  
ATOM   1451  CD2 PHE A 198     -18.037   8.156 -38.401  1.00201.57           C  
ANISOU 1451  CD2 PHE A 198    22179  32022  22385  -2253    651  -2264       C  
ATOM   1452  CE1 PHE A 198     -19.276  10.584 -37.981  1.00200.79           C  
ANISOU 1452  CE1 PHE A 198    21920  32055  22317  -1867    600  -2270       C  
ATOM   1453  CE2 PHE A 198     -19.278   8.406 -38.961  1.00203.17           C  
ANISOU 1453  CE2 PHE A 198    22245  32493  22456  -2289    660  -2329       C  
ATOM   1454  CZ  PHE A 198     -19.898   9.620 -38.749  1.00203.01           C  
ANISOU 1454  CZ  PHE A 198    22141  32543  22451  -2087    634  -2331       C  
ATOM   1455  N   PRO A 199     -13.593   8.690 -39.867  1.00196.42           N  
ANISOU 1455  N   PRO A 199    21793  30734  22104  -1886    552  -2151       N  
ATOM   1456  CA  PRO A 199     -13.359   7.844 -41.048  1.00197.24           C  
ANISOU 1456  CA  PRO A 199    21862  30953  22127  -2019    572  -2253       C  
ATOM   1457  C   PRO A 199     -12.780   6.482 -40.707  1.00197.05           C  
ANISOU 1457  C   PRO A 199    21899  30901  22071  -2205    606  -2304       C  
ATOM   1458  O   PRO A 199     -13.070   5.506 -41.410  1.00197.83           O  
ANISOU 1458  O   PRO A 199    21957  31164  22047  -2415    647  -2427       O  
ATOM   1459  CB  PRO A 199     -12.379   8.679 -41.883  1.00195.93           C  
ANISOU 1459  CB  PRO A 199    21705  30700  22040  -1835    528  -2219       C  
ATOM   1460  CG  PRO A 199     -11.622   9.461 -40.870  1.00194.06           C  
ANISOU 1460  CG  PRO A 199    21561  30235  21939  -1663    493  -2090       C  
ATOM   1461  CD  PRO A 199     -12.593   9.769 -39.760  1.00194.27           C  
ANISOU 1461  CD  PRO A 199    21581  30270  21962  -1665    504  -2056       C  
ATOM   1462  N   LEU A 200     -11.975   6.385 -39.650  1.00189.90           N  
ANISOU 1462  N   LEU A 200    21090  29809  21256  -2155    594  -2223       N  
ATOM   1463  CA  LEU A 200     -11.324   5.140 -39.262  1.00190.36           C  
ANISOU 1463  CA  LEU A 200    21211  29841  21274  -2325    624  -2273       C  
ATOM   1464  C   LEU A 200     -12.237   4.208 -38.473  1.00191.85           C  
ANISOU 1464  C   LEU A 200    21422  30134  21340  -2590    674  -2295       C  
ATOM   1465  O   LEU A 200     -11.740   3.261 -37.856  1.00191.82           O  
ANISOU 1465  O   LEU A 200    21498  30090  21296  -2750    698  -2307       O  
ATOM   1466  CB  LEU A 200     -10.067   5.443 -38.439  1.00188.25           C  
ANISOU 1466  CB  LEU A 200    21039  29353  21135  -2175    587  -2164       C  
ATOM   1467  CG  LEU A 200      -8.929   6.185 -39.144  1.00186.70           C  
ANISOU 1467  CG  LEU A 200    20841  29058  21039  -1957    538  -2132       C  
ATOM   1468  CD1 LEU A 200      -7.834   6.543 -38.153  1.00184.78           C  
ANISOU 1468  CD1 LEU A 200    20695  28610  20903  -1836    505  -2002       C  
ATOM   1469  CD2 LEU A 200      -8.366   5.357 -40.287  1.00188.82           C  
ANISOU 1469  CD2 LEU A 200    21053  29448  21242  -2030    554  -2287       C  
ATOM   1470  N   LYS A 201     -13.549   4.452 -38.480  1.00189.31           N  
ANISOU 1470  N   LYS A 201    21032  29960  20939  -2654    690  -2298       N  
ATOM   1471  CA  LYS A 201     -14.462   3.668 -37.653  1.00190.89           C  
ANISOU 1471  CA  LYS A 201    21251  30273  21006  -2910    733  -2294       C  
ATOM   1472  C   LYS A 201     -14.555   2.224 -38.139  1.00193.11           C  
ANISOU 1472  C   LYS A 201    21565  30694  21115  -3257    788  -2411       C  
ATOM   1473  O   LYS A 201     -14.366   1.282 -37.359  1.00192.96           O  
ANISOU 1473  O   LYS A 201    21675  30618  21024  -3469    797  -2392       O  
ATOM   1474  CB  LYS A 201     -15.841   4.328 -37.641  1.00192.01           C  
ANISOU 1474  CB  LYS A 201    21285  30579  21090  -2882    735  -2284       C  
ATOM   1475  CG  LYS A 201     -16.861   3.649 -36.746  1.00194.59           C  
ANISOU 1475  CG  LYS A 201    21613  31054  21268  -3135    774  -2267       C  
ATOM   1476  CD  LYS A 201     -18.162   4.435 -36.717  1.00196.42           C  
ANISOU 1476  CD  LYS A 201    21712  31471  21450  -3060    772  -2269       C  
ATOM   1477  CE  LYS A 201     -19.244   3.697 -35.946  1.00199.00           C  
ANISOU 1477  CE  LYS A 201    22019  31999  21594  -3339    811  -2259       C  
ATOM   1478  NZ  LYS A 201     -18.915   3.585 -34.498  1.00198.16           N  
ANISOU 1478  NZ  LYS A 201    22000  31765  21528  -3357    812  -2168       N  
ATOM   1479  N   PHE A 202     -14.851   2.033 -39.427  1.00190.03           N  
ANISOU 1479  N   PHE A 202    21111  30443  20648  -3327    799  -2527       N  
ATOM   1480  CA  PHE A 202     -14.974   0.686 -39.979  1.00193.21           C  
ANISOU 1480  CA  PHE A 202    21812  30661  20937  -3520    667  -2612       C  
ATOM   1481  C   PHE A 202     -13.662  -0.079 -39.844  1.00192.72           C  
ANISOU 1481  C   PHE A 202    22049  30222  20952  -3433    538  -2641       C  
ATOM   1482  O   PHE A 202     -13.647  -1.252 -39.450  1.00193.64           O  
ANISOU 1482  O   PHE A 202    22454  30130  20992  -3599    425  -2662       O  
ATOM   1483  CB  PHE A 202     -15.407   0.768 -41.444  1.00194.63           C  
ANISOU 1483  CB  PHE A 202    21957  30939  21053  -3523    636  -2717       C  
ATOM   1484  CG  PHE A 202     -15.678  -0.566 -42.080  1.00197.56           C  
ANISOU 1484  CG  PHE A 202    22635  31141  21286  -3738    497  -2821       C  
ATOM   1485  CD1 PHE A 202     -16.870  -1.232 -41.844  1.00200.00           C  
ANISOU 1485  CD1 PHE A 202    22991  31574  21424  -4038    485  -2809       C  
ATOM   1486  CD2 PHE A 202     -14.742  -1.155 -42.915  1.00197.78           C  
ANISOU 1486  CD2 PHE A 202    22913  30892  21340  -3642    372  -2940       C  
ATOM   1487  CE1 PHE A 202     -17.126  -2.456 -42.433  1.00202.73           C  
ANISOU 1487  CE1 PHE A 202    23643  31745  21640  -4249    335  -2906       C  
ATOM   1488  CE2 PHE A 202     -14.991  -2.382 -43.503  1.00200.41           C  
ANISOU 1488  CE2 PHE A 202    23561  31045  21539  -3825    230  -3062       C  
ATOM   1489  CZ  PHE A 202     -16.184  -3.033 -43.260  1.00202.93           C  
ANISOU 1489  CZ  PHE A 202    23939  31463  21701  -4134    203  -3042       C  
ATOM   1490  N   TYR A 203     -12.547   0.579 -40.170  1.00186.24           N  
ANISOU 1490  N   TYR A 203    21170  29318  20275  -3169    538  -2642       N  
ATOM   1491  CA  TYR A 203     -11.231  -0.034 -40.020  1.00185.04           C  
ANISOU 1491  CA  TYR A 203    21271  28844  20190  -3047    424  -2671       C  
ATOM   1492  C   TYR A 203     -10.965  -0.449 -38.580  1.00183.65           C  
ANISOU 1492  C   TYR A 203    21215  28534  20028  -3121    405  -2565       C  
ATOM   1493  O   TYR A 203     -10.445  -1.542 -38.326  1.00183.85           O  
ANISOU 1493  O   TYR A 203    21561  28274  20020  -3166    261  -2610       O  
ATOM   1494  CB  TYR A 203     -10.159   0.943 -40.499  1.00182.24           C  
ANISOU 1494  CB  TYR A 203    20762  28506  19975  -2769    454  -2655       C  
ATOM   1495  CG  TYR A 203      -8.734   0.482 -40.299  1.00181.27           C  
ANISOU 1495  CG  TYR A 203    20849  28108  19917  -2611    355  -2674       C  
ATOM   1496  CD1 TYR A 203      -8.164  -0.473 -41.131  1.00182.99           C  
ANISOU 1496  CD1 TYR A 203    21343  28113  20072  -2566    228  -2833       C  
ATOM   1497  CD2 TYR A 203      -7.952   1.017 -39.283  1.00179.20           C  
ANISOU 1497  CD2 TYR A 203    20515  27808  19764  -2499    388  -2541       C  
ATOM   1498  CE1 TYR A 203      -6.856  -0.887 -40.949  1.00181.91           C  
ANISOU 1498  CE1 TYR A 203    21396  27744  19977  -2394    139  -2866       C  
ATOM   1499  CE2 TYR A 203      -6.648   0.610 -39.094  1.00178.55           C  
ANISOU 1499  CE2 TYR A 203    20615  27500  19727  -2352    294  -2552       C  
ATOM   1500  CZ  TYR A 203      -6.104  -0.342 -39.928  1.00179.86           C  
ANISOU 1500  CZ  TYR A 203    21043  27469  19826  -2290    171  -2718       C  
ATOM   1501  OH  TYR A 203      -4.802  -0.746 -39.738  1.00179.29           O  
ANISOU 1501  OH  TYR A 203    21152  27189  19780  -2119     80  -2745       O  
ATOM   1502  N   GLN A 204     -11.314   0.411 -37.623  1.00186.54           N  
ANISOU 1502  N   GLN A 204    21344  29098  20435  -3133    539  -2432       N  
ATOM   1503  CA  GLN A 204     -11.018   0.124 -36.223  1.00186.25           C  
ANISOU 1503  CA  GLN A 204    21405  28959  20404  -3212    534  -2315       C  
ATOM   1504  C   GLN A 204     -11.870  -1.027 -35.703  1.00189.23           C  
ANISOU 1504  C   GLN A 204    21985  29292  20622  -3517    470  -2312       C  
ATOM   1505  O   GLN A 204     -11.356  -1.953 -35.064  1.00189.88           O  
ANISOU 1505  O   GLN A 204    22348  29115  20684  -3595    338  -2286       O  
ATOM   1506  CB  GLN A 204     -11.230   1.382 -35.381  1.00184.09           C  
ANISOU 1506  CB  GLN A 204    20827  28925  20195  -3152    699  -2194       C  
ATOM   1507  CG  GLN A 204     -10.857   1.237 -33.919  1.00183.51           C  
ANISOU 1507  CG  GLN A 204    20833  28769  20122  -3232    711  -2061       C  
ATOM   1508  CD  GLN A 204     -11.006   2.538 -33.157  1.00181.64           C  
ANISOU 1508  CD  GLN A 204    20546  28451  20019  -2987    690  -1931       C  
ATOM   1509  OE1 GLN A 204     -11.416   3.555 -33.717  1.00180.11           O  
ANISOU 1509  OE1 GLN A 204    20255  28270  19907  -2773    673  -1942       O  
ATOM   1510  NE2 GLN A 204     -10.674   2.514 -31.871  1.00181.17           N  
ANISOU 1510  NE2 GLN A 204    20579  28286  19972  -3028    677  -1810       N  
ATOM   1511  N   GLU A 205     -13.176  -0.992 -35.975  1.00185.59           N  
ANISOU 1511  N   GLU A 205    21390  29086  20040  -3700    544  -2333       N  
ATOM   1512  CA  GLU A 205     -14.068  -2.017 -35.441  1.00188.21           C  
ANISOU 1512  CA  GLU A 205    21885  29426  20202  -4027    490  -2306       C  
ATOM   1513  C   GLU A 205     -13.838  -3.362 -36.120  1.00190.21           C  
ANISOU 1513  C   GLU A 205    22512  29359  20400  -4119    268  -2423       C  
ATOM   1514  O   GLU A 205     -13.713  -4.394 -35.450  1.00191.45           O  
ANISOU 1514  O   GLU A 205    22949  29294  20501  -4289    123  -2391       O  
ATOM   1515  CB  GLU A 205     -15.524  -1.581 -35.601  1.00189.31           C  
ANISOU 1515  CB  GLU A 205    21760  29962  20207  -4191    631  -2301       C  
ATOM   1516  CG  GLU A 205     -15.916  -0.387 -34.748  1.00187.29           C  
ANISOU 1516  CG  GLU A 205    21163  30027  19971  -4126    833  -2211       C  
ATOM   1517  CD  GLU A 205     -17.365   0.011 -34.945  1.00189.92           C  
ANISOU 1517  CD  GLU A 205    21327  30635  20198  -4179    873  -2223       C  
ATOM   1518  OE1 GLU A 205     -18.024  -0.564 -35.837  1.00192.51           O  
ANISOU 1518  OE1 GLU A 205    21637  31135  20373  -4401    891  -2304       O  
ATOM   1519  OE2 GLU A 205     -17.844   0.898 -34.209  1.00189.80           O  
ANISOU 1519  OE2 GLU A 205    21232  30626  20257  -3982    855  -2155       O  
ATOM   1520  N   ILE A 206     -13.779  -3.371 -37.453  1.00186.05           N  
ANISOU 1520  N   ILE A 206    22008  28799  19884  -4012    224  -2565       N  
ATOM   1521  CA  ILE A 206     -13.734  -4.635 -38.179  1.00189.37           C  
ANISOU 1521  CA  ILE A 206    22786  28941  20226  -4114     16  -2709       C  
ATOM   1522  C   ILE A 206     -12.368  -5.299 -38.063  1.00188.60           C  
ANISOU 1522  C   ILE A 206    23005  28434  20221  -3928   -161  -2784       C  
ATOM   1523  O   ILE A 206     -12.275  -6.532 -37.994  1.00190.13           O  
ANISOU 1523  O   ILE A 206    23553  28329  20359  -4047   -372  -2868       O  
ATOM   1524  CB  ILE A 206     -14.125  -4.405 -39.651  1.00191.43           C  
ANISOU 1524  CB  ILE A 206    22973  29318  20444  -4069     36  -2842       C  
ATOM   1525  CG1 ILE A 206     -15.544  -3.843 -39.735  1.00193.36           C  
ANISOU 1525  CG1 ILE A 206    22922  29968  20578  -4265    182  -2773       C  
ATOM   1526  CG2 ILE A 206     -14.013  -5.694 -40.453  1.00195.42           C  
ANISOU 1526  CG2 ILE A 206    23873  29516  20862  -4155   -181  -3020       C  
ATOM   1527  CD1 ILE A 206     -16.601  -4.766 -39.169  1.00197.66           C  
ANISOU 1527  CD1 ILE A 206    23595  30560  20948  -4634    121  -2722       C  
ATOM   1528  N   PHE A 207     -11.300  -4.520 -38.022  1.00184.68           N  
ANISOU 1528  N   PHE A 207    22391  27915  19865  -3638    -97  -2760       N  
ATOM   1529  CA  PHE A 207      -9.984  -5.115 -38.228  1.00185.17           C  
ANISOU 1529  CA  PHE A 207    22740  27624  19992  -3421   -263  -2872       C  
ATOM   1530  C   PHE A 207      -8.991  -4.835 -37.109  1.00182.05           C  
ANISOU 1530  C   PHE A 207    22338  27126  19705  -3289   -268  -2744       C  
ATOM   1531  O   PHE A 207      -8.174  -5.704 -36.797  1.00181.62           O  
ANISOU 1531  O   PHE A 207    22594  26745  19670  -3222   -462  -2807       O  
ATOM   1532  CB  PHE A 207      -9.418  -4.614 -39.566  1.00184.60           C  
ANISOU 1532  CB  PHE A 207    22593  27593  19955  -3178   -218  -3005       C  
ATOM   1533  CG  PHE A 207      -8.110  -5.241 -39.947  1.00184.18           C  
ANISOU 1533  CG  PHE A 207    22836  27217  19928  -2941   -369  -3156       C  
ATOM   1534  CD1 PHE A 207      -8.068  -6.524 -40.463  1.00187.51           C  
ANISOU 1534  CD1 PHE A 207    23660  27332  20254  -2976   -571  -3363       C  
ATOM   1535  CD2 PHE A 207      -6.924  -4.547 -39.793  1.00180.96           C  
ANISOU 1535  CD2 PHE A 207    22312  26815  19630  -2679   -312  -3102       C  
ATOM   1536  CE1 PHE A 207      -6.866  -7.104 -40.818  1.00187.40           C  
ANISOU 1536  CE1 PHE A 207    23937  27021  20246  -2726   -702  -3532       C  
ATOM   1537  CE2 PHE A 207      -5.721  -5.122 -40.145  1.00181.58           C  
ANISOU 1537  CE2 PHE A 207    22656  26629  19706  -2453   -434  -3246       C  
ATOM   1538  CZ  PHE A 207      -5.690  -6.401 -40.658  1.00184.08           C  
ANISOU 1538  CZ  PHE A 207    23385  26638  19918  -2464   -622  -3471       C  
ATOM   1539  N   GLU A 208      -9.037  -3.651 -36.496  1.00181.38           N  
ANISOU 1539  N   GLU A 208    21921  27302  19693  -3247    -75  -2576       N  
ATOM   1540  CA  GLU A 208      -7.956  -3.257 -35.599  1.00178.75           C  
ANISOU 1540  CA  GLU A 208    21572  26881  19465  -3094    -73  -2459       C  
ATOM   1541  C   GLU A 208      -8.051  -3.953 -34.244  1.00179.28           C  
ANISOU 1541  C   GLU A 208    21815  26811  19492  -3294   -168  -2341       C  
ATOM   1542  O   GLU A 208      -7.022  -4.292 -33.648  1.00179.22           O  
ANISOU 1542  O   GLU A 208    21980  26573  19541  -3194   -295  -2307       O  
ATOM   1543  CB  GLU A 208      -7.944  -1.737 -35.430  1.00176.13           C  
ANISOU 1543  CB  GLU A 208    20846  26849  19225  -2979    145  -2335       C  
ATOM   1544  CG  GLU A 208      -6.754  -1.207 -34.645  1.00173.96           C  
ANISOU 1544  CG  GLU A 208    20539  26498  19059  -2812    152  -2215       C  
ATOM   1545  CD  GLU A 208      -6.692   0.309 -34.629  1.00171.36           C  
ANISOU 1545  CD  GLU A 208    19847  26429  18831  -2683    333  -2119       C  
ATOM   1546  OE1 GLU A 208      -7.594   0.950 -35.209  1.00171.82           O  
ANISOU 1546  OE1 GLU A 208    19677  26725  18880  -2710    445  -2152       O  
ATOM   1547  OE2 GLU A 208      -5.735   0.860 -34.046  1.00168.65           O  
ANISOU 1547  OE2 GLU A 208    19459  26046  18574  -2555    345  -2014       O  
ATOM   1548  N   SER A 209      -9.268  -4.181 -33.741  1.00169.27           N  
ANISOU 1548  N   SER A 209    20502  25699  18116  -3589   -114  -2270       N  
ATOM   1549  CA  SER A 209      -9.399  -4.900 -32.475  1.00170.37           C  
ANISOU 1549  CA  SER A 209    20812  25723  18198  -3822   -212  -2144       C  
ATOM   1550  C   SER A 209      -9.041  -6.377 -32.611  1.00172.91           C  
ANISOU 1550  C   SER A 209    21543  25647  18506  -3883   -518  -2263       C  
ATOM   1551  O   SER A 209      -8.256  -6.876 -31.786  1.00172.88           O  
ANISOU 1551  O   SER A 209    21725  25403  18560  -3870   -679  -2202       O  
ATOM   1552  CB  SER A 209     -10.806  -4.703 -31.901  1.00171.67           C  
ANISOU 1552  CB  SER A 209    20796  26209  18222  -4131    -54  -2031       C  
ATOM   1553  OG  SER A 209     -11.033  -3.347 -31.562  1.00170.25           O  
ANISOU 1553  OG  SER A 209    20256  26360  18073  -4048    200  -1937       O  
ATOM   1554  N   PRO A 210      -9.560  -7.127 -33.595  1.00173.46           N  
ANISOU 1554  N   PRO A 210    21775  25619  18512  -3950   -630  -2438       N  
ATOM   1555  CA  PRO A 210      -9.162  -8.546 -33.692  1.00176.95           C  
ANISOU 1555  CA  PRO A 210    22625  25641  18967  -3986   -950  -2585       C  
ATOM   1556  C   PRO A 210      -7.678  -8.733 -33.952  1.00176.18           C  
ANISOU 1556  C   PRO A 210    22707  25234  18998  -3635  -1109  -2722       C  
ATOM   1557  O   PRO A 210      -7.042  -9.585 -33.317  1.00178.26           O  
ANISOU 1557  O   PRO A 210    23216  25178  19334  -3634  -1353  -2750       O  
ATOM   1558  CB  PRO A 210     -10.020  -9.069 -34.853  1.00180.47           C  
ANISOU 1558  CB  PRO A 210    23165  26094  19311  -4096   -990  -2761       C  
ATOM   1559  CG  PRO A 210     -11.171  -8.134 -34.932  1.00180.28           C  
ANISOU 1559  CG  PRO A 210    22787  26523  19190  -4257   -714  -2632       C  
ATOM   1560  CD  PRO A 210     -10.606  -6.796 -34.580  1.00175.36           C  
ANISOU 1560  CD  PRO A 210    21849  26118  18663  -4031   -493  -2511       C  
ATOM   1561  N   PHE A 211      -7.108  -7.963 -34.881  1.00170.52           N  
ANISOU 1561  N   PHE A 211    21863  24617  18311  -3345   -981  -2811       N  
ATOM   1562  CA  PHE A 211      -5.671  -8.037 -35.123  1.00169.77           C  
ANISOU 1562  CA  PHE A 211    21916  24288  18300  -3008  -1095  -2922       C  
ATOM   1563  C   PHE A 211      -4.887  -7.642 -33.878  1.00167.18           C  
ANISOU 1563  C   PHE A 211    21508  23950  18063  -2961  -1101  -2723       C  
ATOM   1564  O   PHE A 211      -3.856  -8.249 -33.562  1.00167.06           O  
ANISOU 1564  O   PHE A 211    21721  23638  18118  -2808  -1323  -2795       O  
ATOM   1565  CB  PHE A 211      -5.292  -7.139 -36.300  1.00167.85           C  
ANISOU 1565  CB  PHE A 211    21489  24236  18048  -2761   -905  -2998       C  
ATOM   1566  CG  PHE A 211      -3.839  -7.200 -36.665  1.00166.62           C  
ANISOU 1566  CG  PHE A 211    21482  23893  17932  -2428   -983  -3112       C  
ATOM   1567  CD1 PHE A 211      -3.342  -8.256 -37.409  1.00169.64           C  
ANISOU 1567  CD1 PHE A 211    22251  23943  18260  -2282  -1181  -3384       C  
ATOM   1568  CD2 PHE A 211      -2.966  -6.208 -36.255  1.00163.24           C  
ANISOU 1568  CD2 PHE A 211    20820  23623  17582  -2262   -851  -2955       C  
ATOM   1569  CE1 PHE A 211      -2.004  -8.316 -37.745  1.00169.92           C  
ANISOU 1569  CE1 PHE A 211    22386  23908  18268  -2034  -1176  -3533       C  
ATOM   1570  CE2 PHE A 211      -1.627  -6.265 -36.585  1.00163.04           C  
ANISOU 1570  CE2 PHE A 211    20918  23466  17566  -1974   -903  -3045       C  
ATOM   1571  CZ  PHE A 211      -1.146  -7.319 -37.332  1.00166.57           C  
ANISOU 1571  CZ  PHE A 211    21702  23674  17914  -1875  -1038  -3348       C  
ATOM   1572  N   LEU A 212      -5.370  -6.631 -33.154  1.00169.14           N  
ANISOU 1572  N   LEU A 212    21438  24518  18310  -3091   -867  -2486       N  
ATOM   1573  CA  LEU A 212      -4.682  -6.157 -31.959  1.00166.53           C  
ANISOU 1573  CA  LEU A 212    21020  24207  18047  -3070   -844  -2280       C  
ATOM   1574  C   LEU A 212      -4.621  -7.246 -30.893  1.00168.69           C  
ANISOU 1574  C   LEU A 212    21542  24215  18336  -3268  -1093  -2222       C  
ATOM   1575  O   LEU A 212      -3.538  -7.625 -30.429  1.00168.81           O  
ANISOU 1575  O   LEU A 212    21703  23992  18444  -3133  -1289  -2225       O  
ATOM   1576  CB  LEU A 212      -5.386  -4.908 -31.424  1.00163.98           C  
ANISOU 1576  CB  LEU A 212    20334  24272  17701  -3190   -539  -2075       C  
ATOM   1577  CG  LEU A 212      -4.760  -4.182 -30.234  1.00161.92           C  
ANISOU 1577  CG  LEU A 212    19945  24085  17491  -3177   -457  -1854       C  
ATOM   1578  CD1 LEU A 212      -3.402  -3.612 -30.610  1.00159.47           C  
ANISOU 1578  CD1 LEU A 212    19592  23719  17282  -2853   -468  -1875       C  
ATOM   1579  CD2 LEU A 212      -5.686  -3.085 -29.731  1.00161.01           C  
ANISOU 1579  CD2 LEU A 212    19510  24333  17332  -3321   -172  -1707       C  
ATOM   1580  N   THR A 213      -5.785  -7.772 -30.499  1.00164.72           N  
ANISOU 1580  N   THR A 213    21077  23765  17746  -3604  -1097  -2163       N  
ATOM   1581  CA  THR A 213      -5.813  -8.783 -29.446  1.00167.01           C  
ANISOU 1581  CA  THR A 213    21573  23830  18053  -3851  -1320  -2071       C  
ATOM   1582  C   THR A 213      -5.183 -10.094 -29.901  1.00170.45           C  
ANISOU 1582  C   THR A 213    22344  23855  18565  -3803  -1658  -2321       C  
ATOM   1583  O   THR A 213      -4.635 -10.835 -29.075  1.00172.91           O  
ANISOU 1583  O   THR A 213    22825  23968  18905  -4002  -1853  -2266       O  
ATOM   1584  CB  THR A 213      -7.248  -9.024 -28.980  1.00168.83           C  
ANISOU 1584  CB  THR A 213    21761  24258  18127  -4260  -1222  -1937       C  
ATOM   1585  OG1 THR A 213      -8.038  -9.497 -30.079  1.00171.55           O  
ANISOU 1585  OG1 THR A 213    22181  24595  18405  -4314  -1251  -2129       O  
ATOM   1586  CG2 THR A 213      -7.856  -7.737 -28.439  1.00166.45           C  
ANISOU 1586  CG2 THR A 213    21121  24398  17724  -4342   -873  -1731       C  
ATOM   1587  N   GLU A 214      -5.240 -10.397 -31.200  1.00166.90           N  
ANISOU 1587  N   GLU A 214    22006  23321  18089  -3652  -1699  -2598       N  
ATOM   1588  CA  GLU A 214      -4.691 -11.660 -31.676  1.00171.53           C  
ANISOU 1588  CA  GLU A 214    22940  23560  18676  -3708  -1965  -2895       C  
ATOM   1589  C   GLU A 214      -3.169 -11.620 -31.746  1.00171.15           C  
ANISOU 1589  C   GLU A 214    22973  23382  18674  -3467  -2047  -3038       C  
ATOM   1590  O   GLU A 214      -2.508 -12.613 -31.423  1.00174.62           O  
ANISOU 1590  O   GLU A 214    23687  23501  19158  -3603  -2288  -3173       O  
ATOM   1591  CB  GLU A 214      -5.280 -12.018 -33.039  1.00173.83           C  
ANISOU 1591  CB  GLU A 214    23349  23802  18898  -3630  -1968  -3160       C  
ATOM   1592  CG  GLU A 214      -4.862 -13.393 -33.525  1.00179.57           C  
ANISOU 1592  CG  GLU A 214    24478  24123  19628  -3709  -2229  -3506       C  
ATOM   1593  CD  GLU A 214      -5.524 -13.774 -34.826  1.00181.98           C  
ANISOU 1593  CD  GLU A 214    24913  24382  19849  -3659  -2229  -3756       C  
ATOM   1594  OE1 GLU A 214      -6.277 -12.942 -35.371  1.00179.13           O  
ANISOU 1594  OE1 GLU A 214    24317  24316  19428  -3572  -2036  -3638       O  
ATOM   1595  OE2 GLU A 214      -5.298 -14.908 -35.294  1.00186.43           O  
ANISOU 1595  OE2 GLU A 214    25826  24591  20418  -3722  -2422  -4070       O  
ATOM   1596  N   THR A 215      -2.593 -10.491 -32.170  1.00165.55           N  
ANISOU 1596  N   THR A 215    22043  22902  17956  -3134  -1850  -2999       N  
ATOM   1597  CA  THR A 215      -1.147 -10.340 -32.042  1.00165.22           C  
ANISOU 1597  CA  THR A 215    22024  22823  17929  -2940  -1900  -3072       C  
ATOM   1598  C   THR A 215      -0.735 -10.231 -30.579  1.00163.72           C  
ANISOU 1598  C   THR A 215    21750  22646  17811  -3132  -1979  -2780       C  
ATOM   1599  O   THR A 215       0.386 -10.611 -30.221  1.00164.86           O  
ANISOU 1599  O   THR A 215    22011  22653  17977  -3129  -2148  -2842       O  
ATOM   1600  CB  THR A 215      -0.657  -9.124 -32.829  1.00161.24           C  
ANISOU 1600  CB  THR A 215    21285  22588  17392  -2580  -1646  -3046       C  
ATOM   1601  OG1 THR A 215      -1.318  -7.944 -32.356  1.00156.78           O  
ANISOU 1601  OG1 THR A 215    20406  22275  16887  -2585  -1429  -2711       O  
ATOM   1602  CG2 THR A 215      -0.923  -9.304 -34.318  1.00161.64           C  
ANISOU 1602  CG2 THR A 215    21448  22606  17359  -2412  -1574  -3316       C  
ATOM   1603  N   GLY A 216      -1.628  -9.727 -29.723  1.00158.36           N  
ANISOU 1603  N   GLY A 216    20885  22128  17155  -3310  -1853  -2463       N  
ATOM   1604  CA  GLY A 216      -1.361  -9.758 -28.293  1.00158.42           C  
ANISOU 1604  CA  GLY A 216    20863  22121  17210  -3542  -1925  -2168       C  
ATOM   1605  C   GLY A 216      -1.213 -11.173 -27.766  1.00163.51           C  
ANISOU 1605  C   GLY A 216    21834  22406  17888  -3887  -2245  -2199       C  
ATOM   1606  O   GLY A 216      -0.255 -11.489 -27.055  1.00165.08           O  
ANISOU 1606  O   GLY A 216    22135  22441  18148  -3987  -2436  -2086       O  
ATOM   1607  N   GLU A 217      -2.167 -12.046 -28.106  1.00159.97           N  
ANISOU 1607  N   GLU A 217    21573  21795  17411  -4099  -2327  -2317       N  
ATOM   1608  CA  GLU A 217      -2.036 -13.459 -27.759  1.00165.21           C  
ANISOU 1608  CA  GLU A 217    22623  22018  18132  -4432  -2650  -2354       C  
ATOM   1609  C   GLU A 217      -0.789 -14.067 -28.388  1.00167.88           C  
ANISOU 1609  C   GLU A 217    23251  21994  18544  -4272  -2872  -2671       C  
ATOM   1610  O   GLU A 217      -0.085 -14.860 -27.750  1.00171.84           O  
ANISOU 1610  O   GLU A 217    24054  22078  19159  -4471  -3170  -2571       O  
ATOM   1611  CB  GLU A 217      -3.283 -14.228 -28.199  1.00168.85           C  
ANISOU 1611  CB  GLU A 217    23238  22385  18534  -4655  -2679  -2451       C  
ATOM   1612  CG  GLU A 217      -4.523 -13.940 -27.372  1.00168.29           C  
ANISOU 1612  CG  GLU A 217    22985  22590  18368  -4923  -2528  -2120       C  
ATOM   1613  CD  GLU A 217      -4.426 -14.507 -25.969  1.00170.76           C  
ANISOU 1613  CD  GLU A 217    23440  22743  18697  -5303  -2696  -1772       C  
ATOM   1614  OE1 GLU A 217      -3.786 -15.566 -25.798  1.00175.50           O  
ANISOU 1614  OE1 GLU A 217    24397  22887  19400  -5477  -3014  -1794       O  
ATOM   1615  OE2 GLU A 217      -4.987 -13.895 -25.036  1.00168.27           O  
ANISOU 1615  OE2 GLU A 217    22913  22730  18292  -5424  -2517  -1468       O  
ATOM   1616  N   TYR A 218      -0.503 -13.706 -29.642  1.00155.69           N  
ANISOU 1616  N   TYR A 218    21658  20561  16936  -3903  -2739  -3033       N  
ATOM   1617  CA  TYR A 218       0.661 -14.246 -30.337  1.00159.10           C  
ANISOU 1617  CA  TYR A 218    22399  20663  17389  -3700  -2889  -3408       C  
ATOM   1618  C   TYR A 218       1.949 -13.945 -29.579  1.00158.74           C  
ANISOU 1618  C   TYR A 218    22345  20576  17393  -3662  -3023  -3230       C  
ATOM   1619  O   TYR A 218       2.787 -14.832 -29.379  1.00162.94           O  
ANISOU 1619  O   TYR A 218    23241  20537  18132  -3593  -3291  -3237       O  
ATOM   1620  CB  TYR A 218       0.723 -13.680 -31.756  1.00157.42           C  
ANISOU 1620  CB  TYR A 218    22058  20705  17051  -3274  -2643  -3769       C  
ATOM   1621  CG  TYR A 218       1.907 -14.158 -32.565  1.00160.95           C  
ANISOU 1621  CG  TYR A 218    22815  20873  17467  -2992  -2688  -4232       C  
ATOM   1622  CD1 TYR A 218       1.940 -15.440 -33.096  1.00167.31           C  
ANISOU 1622  CD1 TYR A 218    24163  21066  18341  -3019  -2870  -4588       C  
ATOM   1623  CD2 TYR A 218       2.990 -13.323 -32.804  1.00159.06           C  
ANISOU 1623  CD2 TYR A 218    22311  20954  17171  -2618  -2498  -4290       C  
ATOM   1624  CE1 TYR A 218       3.021 -15.878 -33.839  1.00171.46           C  
ANISOU 1624  CE1 TYR A 218    24813  21258  19077  -2402  -2775  -4851       C  
ATOM   1625  CE2 TYR A 218       4.074 -13.751 -33.545  1.00163.09           C  
ANISOU 1625  CE2 TYR A 218    22881  21178  17907  -1996  -2389  -4505       C  
ATOM   1626  CZ  TYR A 218       4.085 -15.029 -34.060  1.00169.20           C  
ANISOU 1626  CZ  TYR A 218    24114  21323  18852  -1871  -2517  -4798       C  
ATOM   1627  OH  TYR A 218       5.164 -15.459 -34.798  1.00174.30           O  
ANISOU 1627  OH  TYR A 218    24808  21699  19719  -1216  -2390  -5042       O  
ATOM   1628  N   TYR A 219       2.120 -12.698 -29.137  1.00155.91           N  
ANISOU 1628  N   TYR A 219    21529  20730  16979  -3534  -2807  -2960       N  
ATOM   1629  CA  TYR A 219       3.348 -12.324 -28.448  1.00154.84           C  
ANISOU 1629  CA  TYR A 219    21321  20643  16869  -3499  -2935  -2751       C  
ATOM   1630  C   TYR A 219       3.329 -12.639 -26.958  1.00155.62           C  
ANISOU 1630  C   TYR A 219    21472  20541  17115  -3876  -3172  -2259       C  
ATOM   1631  O   TYR A 219       4.390 -12.598 -26.325  1.00156.66           O  
ANISOU 1631  O   TYR A 219    21542  20537  17445  -3715  -3284  -1966       O  
ATOM   1632  CB  TYR A 219       3.649 -10.842 -28.678  1.00149.22           C  
ANISOU 1632  CB  TYR A 219    20112  20532  16053  -3156  -2594  -2664       C  
ATOM   1633  CG  TYR A 219       4.158 -10.567 -30.076  1.00149.06           C  
ANISOU 1633  CG  TYR A 219    20029  20702  15903  -2738  -2402  -3104       C  
ATOM   1634  CD1 TYR A 219       5.480 -10.828 -30.409  1.00151.88           C  
ANISOU 1634  CD1 TYR A 219    20345  20838  16523  -2180  -2348  -3112       C  
ATOM   1635  CD2 TYR A 219       3.322 -10.062 -31.062  1.00147.02           C  
ANISOU 1635  CD2 TYR A 219    19667  20596  15600  -2530  -2132  -3209       C  
ATOM   1636  CE1 TYR A 219       5.960 -10.587 -31.679  1.00151.92           C  
ANISOU 1636  CE1 TYR A 219    20239  21008  16476  -1698  -2104  -3460       C  
ATOM   1637  CE2 TYR A 219       3.794  -9.818 -32.340  1.00147.36           C  
ANISOU 1637  CE2 TYR A 219    19658  20785  15548  -2149  -1934  -3534       C  
ATOM   1638  CZ  TYR A 219       5.114 -10.083 -32.641  1.00149.36           C  
ANISOU 1638  CZ  TYR A 219    19870  21059  15820  -1806  -1938  -3807       C  
ATOM   1639  OH  TYR A 219       5.595  -9.845 -33.907  1.00149.29           O  
ANISOU 1639  OH  TYR A 219    19755  21234  15734  -1362  -1701  -4144       O  
ATOM   1640  N   LYS A 220       2.169 -12.952 -26.379  1.00155.62           N  
ANISOU 1640  N   LYS A 220    21479  20507  17144  -4169  -3120  -2068       N  
ATOM   1641  CA  LYS A 220       2.168 -13.588 -25.065  1.00158.11           C  
ANISOU 1641  CA  LYS A 220    21961  20528  17585  -4557  -3377  -1654       C  
ATOM   1642  C   LYS A 220       2.688 -15.016 -25.162  1.00164.54           C  
ANISOU 1642  C   LYS A 220    23332  20590  18596  -4706  -3856  -1746       C  
ATOM   1643  O   LYS A 220       3.624 -15.403 -24.447  1.00166.91           O  
ANISOU 1643  O   LYS A 220    23772  20513  19133  -4710  -4159  -1459       O  
ATOM   1644  CB  LYS A 220       0.764 -13.577 -24.462  1.00157.41           C  
ANISOU 1644  CB  LYS A 220    21765  20630  17413  -4821  -3181  -1448       C  
ATOM   1645  CG  LYS A 220       0.700 -14.229 -23.086  1.00160.00           C  
ANISOU 1645  CG  LYS A 220    22267  20715  17812  -5229  -3406  -1008       C  
ATOM   1646  CD  LYS A 220      -0.707 -14.224 -22.511  1.00159.72           C  
ANISOU 1646  CD  LYS A 220    22148  20916  17623  -5488  -3204   -830       C  
ATOM   1647  CE  LYS A 220      -0.745 -14.938 -21.166  1.00162.52           C  
ANISOU 1647  CE  LYS A 220    22707  21045  17998  -5897  -3434   -394       C  
ATOM   1648  NZ  LYS A 220      -2.116 -14.992 -20.584  1.00162.32           N  
ANISOU 1648  NZ  LYS A 220    22631  21277  17767  -6171  -3253   -226       N  
ATOM   1649  N   GLN A 221       2.093 -15.809 -26.058  1.00154.98           N  
ANISOU 1649  N   GLN A 221    22418  19094  17374  -4704  -3881  -2105       N  
ATOM   1650  CA  GLN A 221       2.496 -17.202 -26.218  1.00161.80           C  
ANISOU 1650  CA  GLN A 221    23878  19115  18485  -4743  -4307  -2222       C  
ATOM   1651  C   GLN A 221       3.961 -17.307 -26.622  1.00163.31           C  
ANISOU 1651  C   GLN A 221    23996  19005  19049  -3952  -4216  -2256       C  
ATOM   1652  O   GLN A 221       4.725 -18.080 -26.033  1.00168.66           O  
ANISOU 1652  O   GLN A 221    24869  19120  20094  -3806  -4474  -1995       O  
ATOM   1653  CB  GLN A 221       1.600 -17.889 -27.250  1.00165.33           C  
ANISOU 1653  CB  GLN A 221    24575  19401  18843  -4760  -4226  -2625       C  
ATOM   1654  CG  GLN A 221       0.134 -17.985 -26.846  1.00164.69           C  
ANISOU 1654  CG  GLN A 221    24302  19657  18615  -5138  -4046  -2410       C  
ATOM   1655  CD  GLN A 221      -0.083 -18.845 -25.616  1.00167.73           C  
ANISOU 1655  CD  GLN A 221    24926  19681  19122  -5569  -4349  -1963       C  
ATOM   1656  OE1 GLN A 221      -0.392 -18.339 -24.537  1.00164.66           O  
ANISOU 1656  OE1 GLN A 221    24249  19660  18654  -5782  -4247  -1550       O  
ATOM   1657  NE2 GLN A 221       0.067 -20.155 -25.776  1.00173.94           N  
ANISOU 1657  NE2 GLN A 221    26265  19727  20099  -5670  -4714  -2044       N  
ATOM   1658  N   GLU A 222       4.377 -16.525 -27.621  1.00152.45           N  
ANISOU 1658  N   GLU A 222    22322  18020  17582  -3439  -3857  -2562       N  
ATOM   1659  CA  GLU A 222       5.773 -16.557 -28.036  1.00158.78           C  
ANISOU 1659  CA  GLU A 222    22992  18634  18701  -2687  -3738  -2599       C  
ATOM   1660  C   GLU A 222       6.681 -15.805 -27.070  1.00156.30           C  
ANISOU 1660  C   GLU A 222    22294  18585  18508  -2574  -3722  -2118       C  
ATOM   1661  O   GLU A 222       7.894 -16.037 -27.072  1.00161.97           O  
ANISOU 1661  O   GLU A 222    22931  19053  19559  -2036  -3729  -2009       O  
ATOM   1662  CB  GLU A 222       5.921 -15.999 -29.456  1.00158.47           C  
ANISOU 1662  CB  GLU A 222    22767  18951  18493  -2213  -3367  -3082       C  
ATOM   1663  CG  GLU A 222       7.313 -16.185 -30.052  1.00165.74           C  
ANISOU 1663  CG  GLU A 222    23578  19672  19722  -1418  -3228  -3201       C  
ATOM   1664  CD  GLU A 222       7.401 -15.747 -31.498  1.00165.35           C  
ANISOU 1664  CD  GLU A 222    23389  19962  19475  -1003  -2875  -3702       C  
ATOM   1665  OE1 GLU A 222       6.381 -15.273 -32.040  1.00159.64           O  
ANISOU 1665  OE1 GLU A 222    22655  19617  18385  -1332  -2752  -3942       O  
ATOM   1666  OE2 GLU A 222       8.489 -15.883 -32.096  1.00171.36           O  
ANISOU 1666  OE2 GLU A 222    24038  20629  20441   -351  -2725  -3852       O  
ATOM   1667  N   ALA A 223       6.129 -14.920 -26.238  1.00150.96           N  
ANISOU 1667  N   ALA A 223    21380  18413  17564  -3067  -3704  -1831       N  
ATOM   1668  CA  ALA A 223       6.917 -14.351 -25.150  1.00148.67           C  
ANISOU 1668  CA  ALA A 223    20812  18291  17385  -3074  -3760  -1331       C  
ATOM   1669  C   ALA A 223       7.332 -15.437 -24.165  1.00155.36           C  
ANISOU 1669  C   ALA A 223    21952  18491  18587  -3217  -4153   -955       C  
ATOM   1670  O   ALA A 223       8.518 -15.581 -23.838  1.00160.12           O  
ANISOU 1670  O   ALA A 223    22448  18875  19516  -2817  -4227   -693       O  
ATOM   1671  CB  ALA A 223       6.125 -13.252 -24.443  1.00142.08           C  
ANISOU 1671  CB  ALA A 223    19725  18091  16167  -3612  -3675  -1143       C  
ATOM   1672  N   SER A 224       6.362 -16.229 -23.695  1.00151.18           N  
ANISOU 1672  N   SER A 224    21793  17652  17998  -3799  -4428   -909       N  
ATOM   1673  CA  SER A 224       6.687 -17.333 -22.796  1.00157.54           C  
ANISOU 1673  CA  SER A 224    22929  17795  19133  -3981  -4846   -549       C  
ATOM   1674  C   SER A 224       7.506 -18.411 -23.496  1.00168.08           C  
ANISOU 1674  C   SER A 224    24548  18417  20897  -3365  -4961   -752       C  
ATOM   1675  O   SER A 224       8.322 -19.081 -22.853  1.00173.92           O  
ANISOU 1675  O   SER A 224    25411  18652  22018  -3209  -5243   -419       O  
ATOM   1676  CB  SER A 224       5.407 -17.934 -22.214  1.00157.39           C  
ANISOU 1676  CB  SER A 224    23251  17638  18911  -4783  -5117   -470       C  
ATOM   1677  OG  SER A 224       4.736 -17.000 -21.386  1.00151.89           O  
ANISOU 1677  OG  SER A 224    22281  17580  17849  -5345  -5036   -234       O  
ATOM   1678  N   ASN A 225       7.306 -18.597 -24.804  1.00148.21           N  
ANISOU 1678  N   ASN A 225    22141  15847  18326  -3005  -4754  -1297       N  
ATOM   1679  CA  ASN A 225       8.086 -19.592 -25.534  1.00158.60           C  
ANISOU 1679  CA  ASN A 225    23725  16506  20029  -2371  -4826  -1553       C  
ATOM   1680  C   ASN A 225       9.545 -19.167 -25.663  1.00164.39           C  
ANISOU 1680  C   ASN A 225    24071  17350  21038  -1633  -4649  -1443       C  
ATOM   1681  O   ASN A 225      10.452 -19.998 -25.538  1.00174.70           O  
ANISOU 1681  O   ASN A 225    25527  18072  22779  -1197  -4847  -1341       O  
ATOM   1682  CB  ASN A 225       7.474 -19.835 -26.914  1.00159.22           C  
ANISOU 1682  CB  ASN A 225    24012  16559  19924  -2207  -4626  -2182       C  
ATOM   1683  CG  ASN A 225       6.155 -20.578 -26.844  1.00158.09           C  
ANISOU 1683  CG  ASN A 225    24343  16129  19594  -2883  -4879  -2293       C  
ATOM   1684  OD1 ASN A 225       5.999 -21.516 -26.063  1.00161.94           O  
ANISOU 1684  OD1 ASN A 225    25210  16043  20278  -3227  -5286  -2020       O  
ATOM   1685  ND2 ASN A 225       5.196 -20.162 -27.664  1.00152.85           N  
ANISOU 1685  ND2 ASN A 225    23658  15875  18543  -3097  -4656  -2674       N  
ATOM   1686  N   LEU A 226       9.791 -17.880 -25.918  1.00153.32           N  
ANISOU 1686  N   LEU A 226    22168  16695  19389  -1484  -4291  -1455       N  
ATOM   1687  CA  LEU A 226      11.164 -17.397 -26.014  1.00153.05           C  
ANISOU 1687  CA  LEU A 226    21729  16851  19573   -843  -4123  -1313       C  
ATOM   1688  C   LEU A 226      11.840 -17.372 -24.650  1.00153.32           C  
ANISOU 1688  C   LEU A 226    21633  16783  19841   -999  -4391   -674       C  
ATOM   1689  O   LEU A 226      13.021 -17.720 -24.532  1.00158.40           O  
ANISOU 1689  O   LEU A 226    22162  17158  20864   -474  -4466   -493       O  
ATOM   1690  CB  LEU A 226      11.197 -16.006 -26.646  1.00147.18           C  
ANISOU 1690  CB  LEU A 226    20516  16935  18471   -712  -3701  -1475       C  
ATOM   1691  CG  LEU A 226      10.858 -15.882 -28.131  1.00146.98           C  
ANISOU 1691  CG  LEU A 226    20510  17100  18235   -408  -3385  -2090       C  
ATOM   1692  CD1 LEU A 226      10.774 -14.419 -28.532  1.00140.80           C  
ANISOU 1692  CD1 LEU A 226    19274  17151  17072   -425  -3040  -2141       C  
ATOM   1693  CD2 LEU A 226      11.892 -16.608 -28.974  1.00153.80           C  
ANISOU 1693  CD2 LEU A 226    21420  17587  19431    366  -3307  -2371       C  
ATOM   1694  N   LEU A 227      11.110 -16.962 -23.607  1.00156.03           N  
ANISOU 1694  N   LEU A 227    21977  17356  19953  -1716  -4535   -324       N  
ATOM   1695  CA  LEU A 227      11.735 -16.809 -22.296  1.00155.63           C  
ANISOU 1695  CA  LEU A 227    21778  17293  20062  -1917  -4770    294       C  
ATOM   1696  C   LEU A 227      12.186 -18.149 -21.724  1.00165.39           C  
ANISOU 1696  C   LEU A 227    23376  17706  21760  -1855  -5204    549       C  
ATOM   1697  O   LEU A 227      13.141 -18.196 -20.939  1.00168.81           O  
ANISOU 1697  O   LEU A 227    23653  18018  22470  -1715  -5384   1012       O  
ATOM   1698  CB  LEU A 227      10.773 -16.105 -21.337  1.00143.62           C  
ANISOU 1698  CB  LEU A 227    20205  16210  18153  -2720  -4814    560       C  
ATOM   1699  CG  LEU A 227      11.314 -15.746 -19.951  1.00140.02           C  
ANISOU 1699  CG  LEU A 227    19573  15871  17759  -3024  -5016   1192       C  
ATOM   1700  CD1 LEU A 227      12.495 -14.794 -20.068  1.00138.84           C  
ANISOU 1700  CD1 LEU A 227    18945  16144  17663  -2529  -4788   1348       C  
ATOM   1701  CD2 LEU A 227      10.219 -15.134 -19.090  1.00130.51           C  
ANISOU 1701  CD2 LEU A 227    18365  15091  16132  -3828  -5038   1361       C  
ATOM   1702  N   GLN A 228      11.528 -19.245 -22.108  1.00143.90           N  
ANISOU 1702  N   GLN A 228    21148  14400  19128  -1959  -5396    267       N  
ATOM   1703  CA  GLN A 228      11.946 -20.571 -21.672  1.00154.26           C  
ANISOU 1703  CA  GLN A 228    22859  14857  20897  -1858  -5832    467       C  
ATOM   1704  C   GLN A 228      13.195 -21.056 -22.401  1.00165.65           C  
ANISOU 1704  C   GLN A 228    24229  15929  22780   -924  -5768    285       C  
ATOM   1705  O   GLN A 228      13.851 -21.994 -21.932  1.00173.79           O  
ANISOU 1705  O   GLN A 228    25472  16301  24258   -706  -6123    541       O  
ATOM   1706  CB  GLN A 228      10.797 -21.568 -21.879  1.00156.37           C  
ANISOU 1706  CB  GLN A 228    23711  14616  21088  -2306  -6072    212       C  
ATOM   1707  CG  GLN A 228      11.046 -22.973 -21.336  1.00167.33           C  
ANISOU 1707  CG  GLN A 228    25598  15068  22913  -2340  -6594    449       C  
ATOM   1708  CD  GLN A 228       9.870 -23.910 -21.553  1.00168.06           C  
ANISOU 1708  CD  GLN A 228    26284  14687  22885  -2847  -6843    207       C  
ATOM   1709  OE1 GLN A 228       8.864 -23.536 -22.156  1.00161.16           O  
ANISOU 1709  OE1 GLN A 228    25434  14197  21605  -3153  -6612   -155       O  
ATOM   1710  NE2 GLN A 228       9.994 -25.137 -21.060  1.00175.81           N  
ANISOU 1710  NE2 GLN A 228    27753  14827  24220  -2953  -7339    425       N  
ATOM   1711  N   GLU A 229      13.557 -20.420 -23.514  1.00152.55           N  
ANISOU 1711  N   GLU A 229    22257  14702  21003   -368  -5329   -135       N  
ATOM   1712  CA  GLU A 229      14.587 -20.925 -24.414  1.00164.03           C  
ANISOU 1712  CA  GLU A 229    23663  15851  22812    528  -5209   -439       C  
ATOM   1713  C   GLU A 229      15.961 -20.306 -24.186  1.00164.99           C  
ANISOU 1713  C   GLU A 229    23231  16321  23136   1060  -5076   -121       C  
ATOM   1714  O   GLU A 229      16.957 -21.030 -24.100  1.00174.10           O  
ANISOU 1714  O   GLU A 229    24392  17002  24755   1615  -5248     -1       O  
ATOM   1715  CB  GLU A 229      14.160 -20.688 -25.868  1.00164.42           C  
ANISOU 1715  CB  GLU A 229    23721  16164  22589    817  -4808  -1127       C  
ATOM   1716  CG  GLU A 229      15.156 -21.191 -26.900  1.00176.13           C  
ANISOU 1716  CG  GLU A 229    25154  17390  24377   1743  -4632  -1522       C  
ATOM   1717  CD  GLU A 229      14.698 -20.937 -28.324  1.00175.58           C  
ANISOU 1717  CD  GLU A 229    25104  17615  23992   1964  -4238  -2195       C  
ATOM   1718  OE1 GLU A 229      13.608 -20.353 -28.503  1.00165.52           O  
ANISOU 1718  OE1 GLU A 229    23870  16741  22279   1403  -4116  -2331       O  
ATOM   1719  OE2 GLU A 229      15.429 -21.317 -29.263  1.00183.86           O  
ANISOU 1719  OE2 GLU A 229    26118  18515  25227   2701  -4049  -2587       O  
ATOM   1720  N   SER A 230      16.040 -18.983 -24.087  1.00158.90           N  
ANISOU 1720  N   SER A 230    21982  16365  22029    904  -4786     24       N  
ATOM   1721  CA  SER A 230      17.293 -18.266 -24.274  1.00158.74           C  
ANISOU 1721  CA  SER A 230    21405  16804  22105   1470  -4550    172       C  
ATOM   1722  C   SER A 230      17.851 -17.740 -22.956  1.00152.46           C  
ANISOU 1722  C   SER A 230    20327  16225  21375   1166  -4754    878       C  
ATOM   1723  O   SER A 230      17.175 -17.701 -21.924  1.00146.35           O  
ANISOU 1723  O   SER A 230    19739  15390  20476    459  -5009   1226       O  
ATOM   1724  CB  SER A 230      17.098 -17.107 -25.258  1.00152.93           C  
ANISOU 1724  CB  SER A 230    20327  16845  20934   1574  -4067   -196       C  
ATOM   1725  OG  SER A 230      16.723 -17.584 -26.539  1.00158.65           O  
ANISOU 1725  OG  SER A 230    21277  17400  21603   1910  -3864   -846       O  
ATOM   1726  N   ASN A 231      19.121 -17.339 -23.017  1.00152.21           N  
ANISOU 1726  N   ASN A 231    19831  16474  21528   1706  -4634   1085       N  
ATOM   1727  CA  ASN A 231      19.774 -16.623 -21.934  1.00145.50           C  
ANISOU 1727  CA  ASN A 231    18625  15979  20680   1469  -4753   1728       C  
ATOM   1728  C   ASN A 231      19.258 -15.183 -21.887  1.00134.38           C  
ANISOU 1728  C   ASN A 231    16952  15375  18733   1004  -4475   1753       C  
ATOM   1729  O   ASN A 231      18.577 -14.710 -22.801  1.00133.40           O  
ANISOU 1729  O   ASN A 231    16841  15569  18276    990  -4165   1275       O  
ATOM   1730  CB  ASN A 231      21.292 -16.662 -22.124  1.00149.64           C  
ANISOU 1730  CB  ASN A 231    18717  16580  21558   2216  -4702   1914       C  
ATOM   1731  CG  ASN A 231      22.054 -16.212 -20.892  1.00145.12           C  
ANISOU 1731  CG  ASN A 231    17846  16207  21087   1980  -4933   2645       C  
ATOM   1732  OD1 ASN A 231      21.460 -15.842 -19.880  1.00138.60           O  
ANISOU 1732  OD1 ASN A 231    17143  15468  20050   1252  -5120   3004       O  
ATOM   1733  ND2 ASN A 231      23.380 -16.245 -20.972  1.00148.53           N  
ANISOU 1733  ND2 ASN A 231    17872  16734  21829   2591  -4918   2867       N  
ATOM   1734  N   CYS A 232      19.590 -14.480 -20.801  1.00136.44           N  
ANISOU 1734  N   CYS A 232    16983  15952  18907    619  -4603   2321       N  
ATOM   1735  CA  CYS A 232      19.055 -13.137 -20.586  1.00129.54           C  
ANISOU 1735  CA  CYS A 232    15917  15769  17531    125  -4396   2381       C  
ATOM   1736  C   CYS A 232      19.446 -12.194 -21.720  1.00126.72           C  
ANISOU 1736  C   CYS A 232    15179  16021  16946    559  -3968   2053       C  
ATOM   1737  O   CYS A 232      18.583 -11.620 -22.397  1.00122.88           O  
ANISOU 1737  O   CYS A 232    14744  15851  16093    393  -3716   1651       O  
ATOM   1738  CB  CYS A 232      19.532 -12.591 -19.239  1.00127.95           C  
ANISOU 1738  CB  CYS A 232    15534  15773  17309   -292  -4618   3057       C  
ATOM   1739  SG  CYS A 232      18.853 -10.967 -18.823  1.00120.04           S  
ANISOU 1739  SG  CYS A 232    14360  15550  15700   -927  -4409   3147       S  
ATOM   1740  N   SER A 233      20.753 -12.020 -21.939  1.00128.19           N  
ANISOU 1740  N   SER A 233    14967  16400  17340   1103  -3893   2238       N  
ATOM   1741  CA  SER A 233      21.214 -11.157 -23.022  1.00125.97           C  
ANISOU 1741  CA  SER A 233    14304  16719  16839   1510  -3502   1959       C  
ATOM   1742  C   SER A 233      20.735 -11.657 -24.377  1.00132.58           C  
ANISOU 1742  C   SER A 233    15317  17411  17647   1895  -3258   1271       C  
ATOM   1743  O   SER A 233      20.428 -10.852 -25.266  1.00127.52           O  
ANISOU 1743  O   SER A 233    14534  17265  16653   1929  -2939    931       O  
ATOM   1744  CB  SER A 233      22.738 -11.060 -23.000  1.00128.11           C  
ANISOU 1744  CB  SER A 233    14113  17189  17374   2042  -3493   2294       C  
ATOM   1745  OG  SER A 233      23.339 -12.309 -23.294  1.00140.21           O  
ANISOU 1745  OG  SER A 233    15720  18167  19386   2635  -3605   2179       O  
ATOM   1746  N   GLN A 234      20.662 -12.977 -24.549  1.00128.15           N  
ANISOU 1746  N   GLN A 234    15085  16161  17443   2169  -3421   1063       N  
ATOM   1747  CA  GLN A 234      20.136 -13.541 -25.786  1.00133.48           C  
ANISOU 1747  CA  GLN A 234    16002  16633  18083   2483  -3220    396       C  
ATOM   1748  C   GLN A 234      18.648 -13.247 -25.930  1.00128.01           C  
ANISOU 1748  C   GLN A 234    15634  16009  16997   1879  -3169    110       C  
ATOM   1749  O   GLN A 234      18.161 -12.999 -27.041  1.00126.66           O  
ANISOU 1749  O   GLN A 234    15487  16069  16569   2002  -2886   -398       O  
ATOM   1750  CB  GLN A 234      20.402 -15.045 -25.815  1.00144.98           C  
ANISOU 1750  CB  GLN A 234    17787  17271  20028   2882  -3458    276       C  
ATOM   1751  CG  GLN A 234      21.882 -15.395 -25.811  1.00149.88           C  
ANISOU 1751  CG  GLN A 234    18059  17825  21064   3583  -3484    494       C  
ATOM   1752  CD  GLN A 234      22.134 -16.887 -25.748  1.00160.65           C  
ANISOU 1752  CD  GLN A 234    19776  18321  22941   3984  -3764    400       C  
ATOM   1753  OE1 GLN A 234      21.201 -17.684 -25.649  1.00164.24           O  
ANISOU 1753  OE1 GLN A 234    20771  18194  23441   3685  -3971    206       O  
ATOM   1754  NE2 GLN A 234      23.404 -17.273 -25.797  1.00165.29           N  
ANISOU 1754  NE2 GLN A 234    20059  18819  23923   4662  -3788    549       N  
ATOM   1755  N   TYR A 235      17.913 -13.265 -24.815  1.00133.90           N  
ANISOU 1755  N   TYR A 235    16613  16585  17676   1215  -3443    437       N  
ATOM   1756  CA  TYR A 235      16.502 -12.894 -24.849  1.00129.66           C  
ANISOU 1756  CA  TYR A 235    16320  16199  16747    615  -3394    216       C  
ATOM   1757  C   TYR A 235      16.326 -11.442 -25.269  1.00123.62           C  
ANISOU 1757  C   TYR A 235    15212  16219  15540    497  -3075    135       C  
ATOM   1758  O   TYR A 235      15.479 -11.127 -26.112  1.00121.31           O  
ANISOU 1758  O   TYR A 235    15001  16142  14948    407  -2865   -301       O  
ATOM   1759  CB  TYR A 235      15.857 -13.138 -23.484  1.00128.95           C  
ANISOU 1759  CB  TYR A 235    16483  15852  16658    -74  -3740    630       C  
ATOM   1760  CG  TYR A 235      14.413 -12.694 -23.410  1.00124.70           C  
ANISOU 1760  CG  TYR A 235    16134  15543  15701   -711  -3687    443       C  
ATOM   1761  CD1 TYR A 235      13.406 -13.431 -24.018  1.00126.36           C  
ANISOU 1761  CD1 TYR A 235    16725  15432  15853   -837  -3702      8       C  
ATOM   1762  CD2 TYR A 235      14.058 -11.535 -22.734  1.00119.33           C  
ANISOU 1762  CD2 TYR A 235    15249  15410  14679  -1182  -3624    699       C  
ATOM   1763  CE1 TYR A 235      12.086 -13.025 -23.955  1.00122.77           C  
ANISOU 1763  CE1 TYR A 235    16402  15229  15015  -1413  -3654   -148       C  
ATOM   1764  CE2 TYR A 235      12.742 -11.121 -22.665  1.00115.83           C  
ANISOU 1764  CE2 TYR A 235    14944  15202  13863  -1722  -3566    518       C  
ATOM   1765  CZ  TYR A 235      11.760 -11.870 -23.277  1.00117.56           C  
ANISOU 1765  CZ  TYR A 235    15502  15129  14036  -1835  -3580    104       C  
ATOM   1766  OH  TYR A 235      10.447 -11.463 -23.211  1.00114.37           O  
ANISOU 1766  OH  TYR A 235    15196  14997  13261  -2368  -3524    -62       O  
ATOM   1767  N   MET A 236      17.122 -10.539 -24.691  1.00131.16           N  
ANISOU 1767  N   MET A 236    15791  17597  16445    484  -3055    567       N  
ATOM   1768  CA  MET A 236      16.984  -9.125 -25.026  1.00119.85           C  
ANISOU 1768  CA  MET A 236    14063  16877  14596    349  -2794    528       C  
ATOM   1769  C   MET A 236      17.367  -8.862 -26.477  1.00122.33           C  
ANISOU 1769  C   MET A 236    14169  17496  14816    889  -2461     88       C  
ATOM   1770  O   MET A 236      16.661  -8.140 -27.192  1.00116.05           O  
ANISOU 1770  O   MET A 236    13354  17079  13662    754  -2246   -230       O  
ATOM   1771  CB  MET A 236      17.828  -8.281 -24.071  1.00112.76           C  
ANISOU 1771  CB  MET A 236    12844  16321  13679    211  -2879   1106       C  
ATOM   1772  CG  MET A 236      17.354  -8.361 -22.628  1.00108.58           C  
ANISOU 1772  CG  MET A 236    12513  15595  13149   -407  -3181   1531       C  
ATOM   1773  SD  MET A 236      18.286  -7.309 -21.506  1.00103.59           S  
ANISOU 1773  SD  MET A 236    11540  15382  12438   -631  -3283   2195       S  
ATOM   1774  CE  MET A 236      19.827  -8.209 -21.390  1.00111.08           C  
ANISOU 1774  CE  MET A 236    12290  15998  13915    -49  -3447   2519       C  
ATOM   1775  N   GLU A 237      18.478  -9.449 -26.931  1.00123.85           N  
ANISOU 1775  N   GLU A 237    14197  17540  15322   1504  -2419     63       N  
ATOM   1776  CA  GLU A 237      18.864  -9.351 -28.335  1.00126.44           C  
ANISOU 1776  CA  GLU A 237    14341  18133  15566   2037  -2098   -388       C  
ATOM   1777  C   GLU A 237      17.730  -9.824 -29.238  1.00128.33           C  
ANISOU 1777  C   GLU A 237    14943  18164  15652   1967  -1991   -978       C  
ATOM   1778  O   GLU A 237      17.349  -9.144 -30.203  1.00123.74           O  
ANISOU 1778  O   GLU A 237    14266  18017  14732   1980  -1729  -1318       O  
ATOM   1779  CB  GLU A 237      20.126 -10.185 -28.572  1.00136.78           C  
ANISOU 1779  CB  GLU A 237    15484  19192  17295   2716  -2106   -355       C  
ATOM   1780  CG  GLU A 237      20.772 -10.018 -29.936  1.00139.19           C  
ANISOU 1780  CG  GLU A 237    15505  19868  17513   3309  -1757   -755       C  
ATOM   1781  CD  GLU A 237      21.492  -8.691 -30.079  1.00130.82           C  
ANISOU 1781  CD  GLU A 237    13937  19593  16178   3318  -1569   -496       C  
ATOM   1782  OE1 GLU A 237      21.937  -8.144 -29.047  1.00126.05           O  
ANISOU 1782  OE1 GLU A 237    13143  19147  15603   3063  -1740     60       O  
ATOM   1783  OE2 GLU A 237      21.622  -8.199 -31.220  1.00128.58           O  
ANISOU 1783  OE2 GLU A 237    13455  19765  15636   3556  -1266   -839       O  
ATOM   1784  N   LYS A 238      17.153 -10.983 -28.906  1.00137.51           N  
ANISOU 1784  N   LYS A 238    16539  18660  17047   1848  -2219  -1079       N  
ATOM   1785  CA  LYS A 238      16.121 -11.580 -29.747  1.00140.42           C  
ANISOU 1785  CA  LYS A 238    17286  18767  17298   1782  -2154  -1627       C  
ATOM   1786  C   LYS A 238      14.870 -10.711 -29.797  1.00128.91           C  
ANISOU 1786  C   LYS A 238    15891  17695  15395   1197  -2079  -1731       C  
ATOM   1787  O   LYS A 238      14.320 -10.463 -30.874  1.00125.87           O  
ANISOU 1787  O   LYS A 238    15539  17542  14744   1244  -1858  -2179       O  
ATOM   1788  CB  LYS A 238      15.784 -12.983 -29.242  1.00149.10           C  
ANISOU 1788  CB  LYS A 238    18857  19054  18740   1707  -2471  -1636       C  
ATOM   1789  N   VAL A 239      14.399 -10.239 -28.638  1.00137.97           N  
ANISOU 1789  N   VAL A 239    17051  18924  16449    645  -2264  -1328       N  
ATOM   1790  CA  VAL A 239      13.174  -9.444 -28.627  1.00129.96           C  
ANISOU 1790  CA  VAL A 239    16087  18264  15027    111  -2201  -1433       C  
ATOM   1791  C   VAL A 239      13.397  -8.103 -29.316  1.00125.84           C  
ANISOU 1791  C   VAL A 239    15193  18442  14179    231  -1916  -1511       C  
ATOM   1792  O   VAL A 239      12.481  -7.564 -29.953  1.00123.01           O  
ANISOU 1792  O   VAL A 239    14868  18377  13494     29  -1776  -1812       O  
ATOM   1793  CB  VAL A 239      12.648  -9.263 -27.189  1.00127.71           C  
ANISOU 1793  CB  VAL A 239    15893  17922  14709   -493  -2452   -996       C  
ATOM   1794  CG1 VAL A 239      12.347 -10.613 -26.556  1.00132.04           C  
ANISOU 1794  CG1 VAL A 239    16839  17778  15551   -670  -2759   -918       C  
ATOM   1795  CG2 VAL A 239      13.630  -8.481 -26.340  1.00125.88           C  
ANISOU 1795  CG2 VAL A 239    15328  17975  14523   -472  -2492   -483       C  
ATOM   1796  N   LEU A 240      14.608  -7.548 -29.217  1.00137.10           N  
ANISOU 1796  N   LEU A 240    16260  20149  15682    547  -1844  -1230       N  
ATOM   1797  CA  LEU A 240      14.903  -6.305 -29.922  1.00131.29           C  
ANISOU 1797  CA  LEU A 240    15183  20064  14636    663  -1596  -1289       C  
ATOM   1798  C   LEU A 240      14.830  -6.513 -31.431  1.00134.60           C  
ANISOU 1798  C   LEU A 240    15608  20589  14944   1033  -1345  -1830       C  
ATOM   1799  O   LEU A 240      14.204  -5.724 -32.152  1.00128.78           O  
ANISOU 1799  O   LEU A 240    14817  20255  13859    892  -1185  -2070       O  
ATOM   1800  CB  LEU A 240      16.279  -5.780 -29.507  1.00131.22           C  
ANISOU 1800  CB  LEU A 240    14796  20319  14743    915  -1594   -855       C  
ATOM   1801  CG  LEU A 240      16.681  -4.399 -30.028  1.00125.86           C  
ANISOU 1801  CG  LEU A 240    13759  20328  13736    954  -1395   -795       C  
ATOM   1802  CD1 LEU A 240      15.758  -3.328 -29.463  1.00119.91           C  
ANISOU 1802  CD1 LEU A 240    13057  19850  12654    397  -1452   -661       C  
ATOM   1803  CD2 LEU A 240      18.131  -4.095 -29.689  1.00127.50           C  
ANISOU 1803  CD2 LEU A 240    13597  20754  14092   1238  -1407   -375       C  
ATOM   1804  N   GLY A 241      15.454  -7.588 -31.925  1.00140.63           N  
ANISOU 1804  N   GLY A 241    16448  20984  16000   1509  -1317  -2037       N  
ATOM   1805  CA  GLY A 241      15.325  -7.911 -33.338  1.00144.67           C  
ANISOU 1805  CA  GLY A 241    17020  21548  16400   1840  -1084  -2592       C  
ATOM   1806  C   GLY A 241      13.884  -8.147 -33.754  1.00140.90           C  
ANISOU 1806  C   GLY A 241    16905  20922  15708   1465  -1100  -2970       C  
ATOM   1807  O   GLY A 241      13.462  -7.729 -34.838  1.00138.07           O  
ANISOU 1807  O   GLY A 241    16516  20893  15053   1491   -895  -3337       O  
ATOM   1808  N   ARG A 242      13.108  -8.812 -32.893  1.00151.86           N  
ANISOU 1808  N   ARG A 242    18630  21840  17229   1085  -1355  -2863       N  
ATOM   1809  CA  ARG A 242      11.701  -9.071 -33.189  1.00148.95           C  
ANISOU 1809  CA  ARG A 242    18595  21345  16656    676  -1399  -3175       C  
ATOM   1810  C   ARG A 242      10.912  -7.778 -33.336  1.00137.82           C  
ANISOU 1810  C   ARG A 242    17005  20530  14831    302  -1292  -3168       C  
ATOM   1811  O   ARG A 242      10.068  -7.659 -34.232  1.00136.46           O  
ANISOU 1811  O   ARG A 242    16935  20512  14401    188  -1181  -3547       O  
ATOM   1812  CB  ARG A 242      11.084  -9.948 -32.099  1.00151.21           C  
ANISOU 1812  CB  ARG A 242    19231  21076  17145    285  -1715  -2978       C  
ATOM   1813  CG  ARG A 242      11.574 -11.380 -32.097  1.00164.16           C  
ANISOU 1813  CG  ARG A 242    21171  22019  19183    604  -1865  -3077       C  
ATOM   1814  CD  ARG A 242      11.068 -12.104 -33.330  1.00167.82           C  
ANISOU 1814  CD  ARG A 242    21933  22259  19572    770  -1758  -3662       C  
ATOM   1815  NE  ARG A 242       9.610 -12.171 -33.341  1.00161.14           N  
ANISOU 1815  NE  ARG A 242    21367  21390  18469    190  -1851  -3822       N  
ATOM   1816  CZ  ARG A 242       8.880 -12.435 -34.419  1.00160.69           C  
ANISOU 1816  CZ  ARG A 242    21520  21333  18202    157  -1741  -4304       C  
ATOM   1817  NH1 ARG A 242       9.471 -12.660 -35.584  1.00165.98           N  
ANISOU 1817  NH1 ARG A 242    22171  22018  18877    671  -1523  -4697       N  
ATOM   1818  NH2 ARG A 242       7.557 -12.473 -34.332  1.00154.85           N  
ANISOU 1818  NH2 ARG A 242    20998  20607  17233   -402  -1848  -4391       N  
ATOM   1819  N   LEU A 243      11.154  -6.804 -32.456  1.00137.49           N  
ANISOU 1819  N   LEU A 243    16708  20812  14719    102  -1339  -2739       N  
ATOM   1820  CA  LEU A 243      10.458  -5.527 -32.582  1.00132.44           C  
ANISOU 1820  CA  LEU A 243    15901  20717  13702   -207  -1249  -2730       C  
ATOM   1821  C   LEU A 243      10.893  -4.785 -33.840  1.00131.65           C  
ANISOU 1821  C   LEU A 243    15553  21088  13380    115   -994  -2968       C  
ATOM   1822  O   LEU A 243      10.051  -4.257 -34.583  1.00129.60           O  
ANISOU 1822  O   LEU A 243    15319  20886  13036    -37   -834  -3064       O  
ATOM   1823  CB  LEU A 243      10.700  -4.676 -31.336  1.00129.08           C  
ANISOU 1823  CB  LEU A 243    15294  20493  13257   -470  -1366  -2227       C  
ATOM   1824  CG  LEU A 243      10.093  -5.241 -30.051  1.00129.32           C  
ANISOU 1824  CG  LEU A 243    15559  20160  13419   -899  -1615  -1983       C  
ATOM   1825  CD1 LEU A 243      10.500  -4.415 -28.844  1.00126.52           C  
ANISOU 1825  CD1 LEU A 243    15019  20011  13042  -1119  -1716  -1489       C  
ATOM   1826  CD2 LEU A 243       8.582  -5.308 -30.170  1.00128.02           C  
ANISOU 1826  CD2 LEU A 243    15615  19958  13068  -1308  -1624  -2217       C  
ATOM   1827  N   LYS A 244      12.205  -4.753 -34.106  1.00143.40           N  
ANISOU 1827  N   LYS A 244    16803  22678  15006    562   -891  -2863       N  
ATOM   1828  CA  LYS A 244      12.703  -4.064 -35.293  1.00143.25           C  
ANISOU 1828  CA  LYS A 244    16527  23144  14758    852   -649  -3063       C  
ATOM   1829  C   LYS A 244      12.108  -4.655 -36.566  1.00145.29           C  
ANISOU 1829  C   LYS A 244    16985  23325  14893    970   -509  -3621       C  
ATOM   1830  O   LYS A 244      11.838  -3.927 -37.529  1.00143.29           O  
ANISOU 1830  O   LYS A 244    16609  23193  14641    907   -335  -3572       O  
ATOM   1831  CB  LYS A 244      14.229  -4.119 -35.335  1.00146.49           C  
ANISOU 1831  CB  LYS A 244    16643  23657  15359   1322   -565  -2864       C  
ATOM   1832  CG  LYS A 244      14.838  -3.361 -36.504  1.00146.80           C  
ANISOU 1832  CG  LYS A 244    16376  24264  15137   1591   -317  -3020       C  
ATOM   1833  CD  LYS A 244      14.613  -1.861 -36.356  1.00141.62           C  
ANISOU 1833  CD  LYS A 244    15513  24018  14277   1244   -324  -2697       C  
ATOM   1834  CE  LYS A 244      15.337  -1.073 -37.439  1.00142.51           C  
ANISOU 1834  CE  LYS A 244    15308  24427  14413   1416   -162  -2621       C  
ATOM   1835  NZ  LYS A 244      14.767  -1.327 -38.792  1.00144.26           N  
ANISOU 1835  NZ  LYS A 244    15660  24455  14699   1426    -62  -2936       N  
ATOM   1836  N   ASP A 245      11.893  -5.974 -36.592  1.00151.31           N  
ANISOU 1836  N   ASP A 245    18072  23525  15895   1070   -580  -3853       N  
ATOM   1837  CA  ASP A 245      11.192  -6.576 -37.723  1.00153.97           C  
ANISOU 1837  CA  ASP A 245    18664  23742  16095   1103   -479  -4387       C  
ATOM   1838  C   ASP A 245       9.710  -6.215 -37.709  1.00150.21           C  
ANISOU 1838  C   ASP A 245    18360  23128  15586    541   -533  -4229       C  
ATOM   1839  O   ASP A 245       9.118  -5.936 -38.761  1.00149.66           O  
ANISOU 1839  O   ASP A 245    18313  23012  15538    454   -384  -4220       O  
ATOM   1840  CB  ASP A 245      11.367  -8.096 -37.706  1.00161.14           C  
ANISOU 1840  CB  ASP A 245    19914  23975  17338   1343   -565  -4599       C  
ATOM   1841  CG  ASP A 245      12.790  -8.525 -38.005  1.00169.92           C  
ANISOU 1841  CG  ASP A 245    20846  25022  18696   1966   -436  -4618       C  
ATOM   1842  OD1 ASP A 245      13.492  -7.791 -38.732  1.00168.93           O  
ANISOU 1842  OD1 ASP A 245    20375  25421  18390   2235   -205  -4665       O  
ATOM   1843  OD2 ASP A 245      13.205  -9.597 -37.516  1.00178.28           O  
ANISOU 1843  OD2 ASP A 245    22099  25513  20125   2184   -573  -4580       O  
ATOM   1844  N   GLU A 246       9.101  -6.209 -36.520  1.00156.26           N  
ANISOU 1844  N   GLU A 246    19235  23755  16384    163   -742  -3988       N  
ATOM   1845  CA  GLU A 246       7.660  -6.006 -36.409  1.00153.84           C  
ANISOU 1845  CA  GLU A 246    19106  23196  16150   -295   -762  -3758       C  
ATOM   1846  C   GLU A 246       7.247  -4.646 -36.952  1.00149.41           C  
ANISOU 1846  C   GLU A 246    18296  22802  15671   -364   -569  -3405       C  
ATOM   1847  O   GLU A 246       6.199  -4.520 -37.598  1.00148.97           O  
ANISOU 1847  O   GLU A 246    18344  22598  15660   -516   -512  -3378       O  
ATOM   1848  CB  GLU A 246       7.222  -6.160 -34.952  1.00153.01           C  
ANISOU 1848  CB  GLU A 246    19109  22940  16089   -653   -994  -3504       C  
ATOM   1849  CG  GLU A 246       5.720  -6.044 -34.724  1.00151.18           C  
ANISOU 1849  CG  GLU A 246    19049  22455  15938  -1037  -1011  -3281       C  
ATOM   1850  CD  GLU A 246       4.939  -7.190 -35.343  1.00154.99           C  
ANISOU 1850  CD  GLU A 246    19889  22620  16379  -1139  -1092  -3614       C  
ATOM   1851  OE1 GLU A 246       5.518  -8.282 -35.520  1.00159.88           O  
ANISOU 1851  OE1 GLU A 246    20719  23074  16955  -1007  -1209  -4029       O  
ATOM   1852  OE2 GLU A 246       3.741  -7.002 -35.646  1.00153.63           O  
ANISOU 1852  OE2 GLU A 246    19786  22345  16243  -1317  -1049  -3483       O  
ATOM   1853  N   GLU A 247       8.055  -3.612 -36.705  1.00161.53           N  
ANISOU 1853  N   GLU A 247    19506  24627  17241   -247   -497  -3140       N  
ATOM   1854  CA  GLU A 247       7.706  -2.296 -37.230  1.00158.12           C  
ANISOU 1854  CA  GLU A 247    18857  24279  16941   -306   -357  -2853       C  
ATOM   1855  C   GLU A 247       7.713  -2.293 -38.756  1.00159.79           C  
ANISOU 1855  C   GLU A 247    19030  24560  17121   -152   -241  -3059       C  
ATOM   1856  O   GLU A 247       6.788  -1.765 -39.387  1.00158.56           O  
ANISOU 1856  O   GLU A 247    18886  24308  17052   -290   -194  -2959       O  
ATOM   1857  CB  GLU A 247       8.655  -1.232 -36.680  1.00156.07           C  
ANISOU 1857  CB  GLU A 247    18295  24268  16737   -227   -324  -2550       C  
ATOM   1858  CG  GLU A 247       8.273   0.185 -37.080  1.00152.41           C  
ANISOU 1858  CG  GLU A 247    17647  23808  16453   -309   -217  -2275       C  
ATOM   1859  CD  GLU A 247       9.148   1.236 -36.427  1.00149.98           C  
ANISOU 1859  CD  GLU A 247    17106  23659  16221   -279   -189  -1975       C  
ATOM   1860  OE1 GLU A 247      10.070   0.861 -35.672  1.00151.01           O  
ANISOU 1860  OE1 GLU A 247    17190  23939  16246   -195   -251  -1939       O  
ATOM   1861  OE2 GLU A 247       8.908   2.439 -36.668  1.00147.23           O  
ANISOU 1861  OE2 GLU A 247    16549  23389  16004   -346   -103  -1811       O  
ATOM   1862  N   ILE A 248       8.739  -2.894 -39.365  1.00157.09           N  
ANISOU 1862  N   ILE A 248    18644  24388  16655    157   -195  -3354       N  
ATOM   1863  CA  ILE A 248       8.799  -2.971 -40.823  1.00159.20           C  
ANISOU 1863  CA  ILE A 248    18903  24707  16881    295    -79  -3554       C  
ATOM   1864  C   ILE A 248       7.600  -3.738 -41.365  1.00160.78           C  
ANISOU 1864  C   ILE A 248    19446  24586  17058    120    -93  -3746       C  
ATOM   1865  O   ILE A 248       7.040  -3.386 -42.412  1.00160.47           O  
ANISOU 1865  O   ILE A 248    19410  24537  17026     46    -32  -3726       O  
ATOM   1866  CB  ILE A 248      10.130  -3.606 -41.270  1.00163.33           C  
ANISOU 1866  CB  ILE A 248    19339  25431  17288    715      2  -3862       C  
ATOM   1867  CG1 ILE A 248      11.310  -2.731 -40.843  1.00162.24           C  
ANISOU 1867  CG1 ILE A 248    18820  25678  17146    882      8  -3608       C  
ATOM   1868  CG2 ILE A 248      10.147  -3.820 -42.777  1.00166.34           C  
ANISOU 1868  CG2 ILE A 248    19767  25818  17615    831    133  -4086       C  
ATOM   1869  CD1 ILE A 248      12.659  -3.393 -41.023  1.00167.01           C  
ANISOU 1869  CD1 ILE A 248    19307  26503  17648   1364     95  -3868       C  
ATOM   1870  N   ARG A 249       7.178  -4.788 -40.657  1.00165.84           N  
ANISOU 1870  N   ARG A 249    20388  24961  17663     30   -201  -3925       N  
ATOM   1871  CA  ARG A 249       5.998  -5.538 -41.079  1.00167.33           C  
ANISOU 1871  CA  ARG A 249    20924  24837  17819   -175   -250  -4074       C  
ATOM   1872  C   ARG A 249       4.746  -4.669 -41.046  1.00163.32           C  
ANISOU 1872  C   ARG A 249    20355  24294  17405   -466   -271  -3724       C  
ATOM   1873  O   ARG A 249       3.986  -4.612 -42.023  1.00163.89           O  
ANISOU 1873  O   ARG A 249    20501  24314  17457   -537   -232  -3753       O  
ATOM   1874  CB  ARG A 249       5.821  -6.770 -40.194  1.00169.68           C  
ANISOU 1874  CB  ARG A 249    21556  24833  18083   -262   -420  -4302       C  
ATOM   1875  CG  ARG A 249       4.637  -7.627 -40.576  1.00172.57           C  
ANISOU 1875  CG  ARG A 249    22308  24857  18403   -497   -510  -4450       C  
ATOM   1876  CD  ARG A 249       4.615  -8.899 -39.762  1.00176.41           C  
ANISOU 1876  CD  ARG A 249    23149  24996  18884   -590   -720  -4712       C  
ATOM   1877  NE  ARG A 249       5.791  -9.708 -40.058  1.00181.45           N  
ANISOU 1877  NE  ARG A 249    23872  25542  19530   -192   -678  -5165       N  
ATOM   1878  CZ  ARG A 249       5.900 -10.494 -41.124  1.00185.97           C  
ANISOU 1878  CZ  ARG A 249    24688  25903  20069      7   -584  -5543       C  
ATOM   1879  NH1 ARG A 249       4.902 -10.573 -41.993  1.00185.66           N  
ANISOU 1879  NH1 ARG A 249    24842  25766  19934   -216   -551  -5509       N  
ATOM   1880  NH2 ARG A 249       7.006 -11.197 -41.322  1.00190.68           N  
ANISOU 1880  NH2 ARG A 249    25332  26371  20746    478   -532  -5951       N  
ATOM   1881  N   CYS A 250       4.513  -3.987 -39.920  1.00164.89           N  
ANISOU 1881  N   CYS A 250    20416  24519  17715   -609   -327  -3404       N  
ATOM   1882  CA  CYS A 250       3.355  -3.108 -39.815  1.00161.44           C  
ANISOU 1882  CA  CYS A 250    19861  24076  17401   -808   -310  -3123       C  
ATOM   1883  C   CYS A 250       3.374  -2.031 -40.889  1.00160.95           C  
ANISOU 1883  C   CYS A 250    19417  24358  17380   -754   -170  -3100       C  
ATOM   1884  O   CYS A 250       2.314  -1.610 -41.366  1.00161.50           O  
ANISOU 1884  O   CYS A 250    19335  24552  17474   -911   -123  -3091       O  
ATOM   1885  CB  CYS A 250       3.301  -2.473 -38.427  1.00158.80           C  
ANISOU 1885  CB  CYS A 250    19369  23790  17177   -925   -336  -2843       C  
ATOM   1886  SG  CYS A 250       3.028  -3.653 -37.089  1.00162.20           S  
ANISOU 1886  SG  CYS A 250    20143  23929  17558  -1101   -537  -2869       S  
ATOM   1887  N   ARG A 251       4.563  -1.579 -41.289  1.00167.75           N  
ANISOU 1887  N   ARG A 251    20114  25384  18239   -542   -118  -3088       N  
ATOM   1888  CA  ARG A 251       4.657  -0.611 -42.372  1.00167.70           C  
ANISOU 1888  CA  ARG A 251    19768  25695  18256   -503    -34  -3075       C  
ATOM   1889  C   ARG A 251       4.462  -1.249 -43.741  1.00171.16           C  
ANISOU 1889  C   ARG A 251    20356  26112  18563   -458     -1  -3344       C  
ATOM   1890  O   ARG A 251       4.139  -0.538 -44.699  1.00171.09           O  
ANISOU 1890  O   ARG A 251    20106  26343  18558   -509     45  -3345       O  
ATOM   1891  CB  ARG A 251       6.002   0.112 -42.308  1.00166.28           C  
ANISOU 1891  CB  ARG A 251    19347  25726  18106   -319    -14  -2950       C  
ATOM   1892  CG  ARG A 251       6.168   0.931 -41.038  1.00163.74           C  
ANISOU 1892  CG  ARG A 251    18848  25453  17913   -387    -31  -2666       C  
ATOM   1893  CD  ARG A 251       7.484   1.679 -41.003  1.00163.05           C  
ANISOU 1893  CD  ARG A 251    18518  25590  17845   -227    -23  -2526       C  
ATOM   1894  NE  ARG A 251       7.704   2.319 -39.710  1.00160.76           N  
ANISOU 1894  NE  ARG A 251    18129  25297  17655   -296    -30  -2266       N  
ATOM   1895  CZ  ARG A 251       7.256   3.527 -39.386  1.00158.84           C  
ANISOU 1895  CZ  ARG A 251    17635  25184  17532   -431     27  -2075       C  
ATOM   1896  NH1 ARG A 251       6.553   4.233 -40.261  1.00159.11           N  
ANISOU 1896  NH1 ARG A 251    17483  25369  17604   -506     77  -2107       N  
ATOM   1897  NH2 ARG A 251       7.505   4.027 -38.183  1.00156.85           N  
ANISOU 1897  NH2 ARG A 251    17347  24899  17348   -493     45  -1858       N  
ATOM   1898  N   LYS A 252       4.644  -2.568 -43.854  1.00166.01           N  
ANISOU 1898  N   LYS A 252    20119  25165  17790   -369    -22  -3577       N  
ATOM   1899  CA  LYS A 252       4.356  -3.249 -45.112  1.00169.63           C  
ANISOU 1899  CA  LYS A 252    20778  25561  18113   -345     24  -3850       C  
ATOM   1900  C   LYS A 252       2.864  -3.496 -45.292  1.00170.11           C  
ANISOU 1900  C   LYS A 252    20944  25533  18156   -606    -29  -3884       C  
ATOM   1901  O   LYS A 252       2.344  -3.374 -46.407  1.00172.35           O  
ANISOU 1901  O   LYS A 252    21170  25944  18370   -674     14  -3992       O  
ATOM   1902  CB  LYS A 252       5.108  -4.578 -45.194  1.00173.42           C  
ANISOU 1902  CB  LYS A 252    21616  25809  18466   -140     50  -4172       C  
ATOM   1903  CG  LYS A 252       6.604  -4.467 -45.412  1.00175.03           C  
ANISOU 1903  CG  LYS A 252    21601  26262  18639    173    156  -4287       C  
ATOM   1904  CD  LYS A 252       7.214  -5.851 -45.560  1.00180.85           C  
ANISOU 1904  CD  LYS A 252    22604  26835  19274    424    215  -4735       C  
ATOM   1905  CE  LYS A 252       8.714  -5.786 -45.785  1.00183.91           C  
ANISOU 1905  CE  LYS A 252    22740  27493  19644    810    341  -4861       C  
ATOM   1906  NZ  LYS A 252       9.301  -7.147 -45.934  1.00190.32           N  
ANISOU 1906  NZ  LYS A 252    23806  28087  20421   1139    421  -5330       N  
ATOM   1907  N   TYR A 253       2.159  -3.852 -44.220  1.00167.78           N  
ANISOU 1907  N   TYR A 253    20797  25041  17911   -766   -125  -3791       N  
ATOM   1908  CA  TYR A 253       0.768  -4.274 -44.331  1.00169.22           C  
ANISOU 1908  CA  TYR A 253    21114  25126  18054  -1011   -185  -3837       C  
ATOM   1909  C   TYR A 253      -0.231  -3.226 -43.866  1.00166.47           C  
ANISOU 1909  C   TYR A 253    20396  25026  17830  -1222   -148  -3593       C  
ATOM   1910  O   TYR A 253      -1.150  -2.875 -44.613  1.00167.33           O  
ANISOU 1910  O   TYR A 253    20362  25300  17916  -1361   -101  -3610       O  
ATOM   1911  CB  TYR A 253       0.553  -5.574 -43.541  1.00170.98           C  
ANISOU 1911  CB  TYR A 253    21808  24935  18219  -1070   -343  -3938       C  
ATOM   1912  CG  TYR A 253       1.266  -6.771 -44.128  1.00175.44           C  
ANISOU 1912  CG  TYR A 253    22813  25204  18643   -889   -370  -4255       C  
ATOM   1913  CD1 TYR A 253       0.735  -7.457 -45.211  1.00179.54           C  
ANISOU 1913  CD1 TYR A 253    23603  25587  19026   -925   -381  -4484       C  
ATOM   1914  CD2 TYR A 253       2.470  -7.216 -43.598  1.00177.33           C  
ANISOU 1914  CD2 TYR A 253    23077  25427  18873   -703   -348  -4431       C  
ATOM   1915  CE1 TYR A 253       1.382  -8.552 -45.752  1.00185.29           C  
ANISOU 1915  CE1 TYR A 253    24650  26129  19622   -775   -352  -4884       C  
ATOM   1916  CE2 TYR A 253       3.126  -8.310 -44.132  1.00182.59           C  
ANISOU 1916  CE2 TYR A 253    24024  25921  19430   -521   -312  -4850       C  
ATOM   1917  CZ  TYR A 253       2.577  -8.974 -45.209  1.00186.72           C  
ANISOU 1917  CZ  TYR A 253    24845  26270  19829   -560   -304  -5077       C  
ATOM   1918  OH  TYR A 253       3.225 -10.063 -45.744  1.00193.41           O  
ANISOU 1918  OH  TYR A 253    26000  26897  20592   -355   -245  -5513       O  
ATOM   1919  N   LEU A 254      -0.077  -2.711 -42.650  1.00166.58           N  
ANISOU 1919  N   LEU A 254    20262  25068  17963  -1246   -153  -3374       N  
ATOM   1920  CA  LEU A 254      -1.143  -1.960 -42.005  1.00164.22           C  
ANISOU 1920  CA  LEU A 254    19711  24928  17759  -1453   -104  -3178       C  
ATOM   1921  C   LEU A 254      -1.140  -0.497 -42.444  1.00162.09           C  
ANISOU 1921  C   LEU A 254    19001  24998  17589  -1421     19  -3040       C  
ATOM   1922  O   LEU A 254      -0.275  -0.039 -43.197  1.00162.34           O  
ANISOU 1922  O   LEU A 254    18902  25156  17623  -1259     46  -3071       O  
ATOM   1923  CB  LEU A 254      -1.007  -2.053 -40.489  1.00163.02           C  
ANISOU 1923  CB  LEU A 254    19617  24650  17673  -1506   -154  -3013       C  
ATOM   1924  CG  LEU A 254      -1.100  -3.456 -39.895  1.00165.82           C  
ANISOU 1924  CG  LEU A 254    20410  24651  17942  -1575   -324  -3120       C  
ATOM   1925  CD1 LEU A 254      -0.863  -3.402 -38.397  1.00164.73           C  
ANISOU 1925  CD1 LEU A 254    20285  24431  17874  -1634   -380  -2927       C  
ATOM   1926  CD2 LEU A 254      -2.436  -4.092 -40.218  1.00168.51           C  
ANISOU 1926  CD2 LEU A 254    20887  24936  18204  -1803   -368  -3216       C  
ATOM   1927  N   HIS A 255      -2.137   0.244 -41.958  1.00165.83           N  
ANISOU 1927  N   HIS A 255    19252  25621  18134  -1579     90  -2891       N  
ATOM   1928  CA  HIS A 255      -2.206   1.686 -42.119  1.00164.14           C  
ANISOU 1928  CA  HIS A 255    18661  25682  18025  -1550    192  -2745       C  
ATOM   1929  C   HIS A 255      -1.413   2.371 -41.007  1.00161.64           C  
ANISOU 1929  C   HIS A 255    18227  25370  17820  -1465    213  -2555       C  
ATOM   1930  O   HIS A 255      -1.293   1.833 -39.902  1.00161.33           O  
ANISOU 1930  O   HIS A 255    18353  25163  17784  -1508    175  -2498       O  
ATOM   1931  CB  HIS A 255      -3.658   2.157 -42.091  1.00163.23           C  
ANISOU 1931  CB  HIS A 255    18391  25716  17913  -1733    268  -2695       C  
ATOM   1932  N   PRO A 256      -0.855   3.554 -41.274  1.00158.85           N  
ANISOU 1932  N   PRO A 256    17608  25202  17546  -1359    263  -2451       N  
ATOM   1933  CA  PRO A 256      -0.030   4.218 -40.251  1.00156.34           C  
ANISOU 1933  CA  PRO A 256    17201  24881  17319  -1286    279  -2270       C  
ATOM   1934  C   PRO A 256      -0.786   4.568 -38.982  1.00154.92           C  
ANISOU 1934  C   PRO A 256    16993  24679  17191  -1418    342  -2132       C  
ATOM   1935  O   PRO A 256      -0.161   4.671 -37.918  1.00153.47           O  
ANISOU 1935  O   PRO A 256    16851  24415  17046  -1401    337  -2006       O  
ATOM   1936  CB  PRO A 256       0.478   5.475 -40.971  1.00155.79           C  
ANISOU 1936  CB  PRO A 256    16884  25007  17301  -1181    314  -2194       C  
ATOM   1937  CG  PRO A 256      -0.522   5.724 -42.048  1.00157.69           C  
ANISOU 1937  CG  PRO A 256    17059  25355  17501  -1246    339  -2280       C  
ATOM   1938  CD  PRO A 256      -0.985   4.369 -42.494  1.00159.83           C  
ANISOU 1938  CD  PRO A 256    17519  25541  17667  -1325    299  -2481       C  
ATOM   1939  N   SER A 257      -2.111   4.716 -39.051  1.00153.64           N  
ANISOU 1939  N   SER A 257    16765  24599  17011  -1556    403  -2156       N  
ATOM   1940  CA  SER A 257      -2.906   5.098 -37.889  1.00152.65           C  
ANISOU 1940  CA  SER A 257    16715  24366  16920  -1636    425  -2013       C  
ATOM   1941  C   SER A 257      -2.794   4.113 -36.732  1.00152.83           C  
ANISOU 1941  C   SER A 257    16843  24330  16896  -1783    431  -2008       C  
ATOM   1942  O   SER A 257      -3.310   4.401 -35.647  1.00152.09           O  
ANISOU 1942  O   SER A 257    16789  24179  16818  -1865    457  -1885       O  
ATOM   1943  CB  SER A 257      -4.373   5.250 -38.296  1.00153.77           C  
ANISOU 1943  CB  SER A 257    16819  24584  17021  -1734    459  -2061       C  
ATOM   1944  OG  SER A 257      -4.918   4.009 -38.708  1.00155.95           O  
ANISOU 1944  OG  SER A 257    17098  24975  17182  -1921    486  -2241       O  
ATOM   1945  N   SER A 258      -2.140   2.969 -36.929  1.00151.80           N  
ANISOU 1945  N   SER A 258    16966  24005  16708  -1745    314  -2101       N  
ATOM   1946  CA  SER A 258      -1.968   1.981 -35.875  1.00152.93           C  
ANISOU 1946  CA  SER A 258    17374  23934  16800  -1837    231  -2070       C  
ATOM   1947  C   SER A 258      -0.511   1.715 -35.526  1.00152.24           C  
ANISOU 1947  C   SER A 258    17420  23697  16727  -1682    137  -2028       C  
ATOM   1948  O   SER A 258      -0.250   0.900 -34.631  1.00152.18           O  
ANISOU 1948  O   SER A 258    17651  23495  16678  -1744     36  -1994       O  
ATOM   1949  CB  SER A 258      -2.644   0.660 -36.270  1.00155.96           C  
ANISOU 1949  CB  SER A 258    18022  24164  17072  -1953    133  -2234       C  
ATOM   1950  OG  SER A 258      -4.046   0.823 -36.401  1.00157.03           O  
ANISOU 1950  OG  SER A 258    18042  24451  17172  -2134    219  -2248       O  
ATOM   1951  N   TYR A 259       0.443   2.377 -36.193  1.00152.41           N  
ANISOU 1951  N   TYR A 259    17291  23820  16798  -1491    154  -2023       N  
ATOM   1952  CA  TYR A 259       1.855   2.082 -35.953  1.00152.07           C  
ANISOU 1952  CA  TYR A 259    17361  23675  16746  -1331     68  -1993       C  
ATOM   1953  C   TYR A 259       2.219   2.250 -34.483  1.00149.78           C  
ANISOU 1953  C   TYR A 259    17119  23309  16483  -1406     58  -1794       C  
ATOM   1954  O   TYR A 259       2.918   1.408 -33.908  1.00149.69           O  
ANISOU 1954  O   TYR A 259    17344  23110  16419  -1374    -70  -1786       O  
ATOM   1955  CB  TYR A 259       2.749   2.974 -36.818  1.00151.90           C  
ANISOU 1955  CB  TYR A 259    17103  23844  16769  -1150    112  -1978       C  
ATOM   1956  CG  TYR A 259       2.703   2.678 -38.301  1.00153.40           C  
ANISOU 1956  CG  TYR A 259    17277  24102  16905  -1058     97  -2178       C  
ATOM   1957  CD1 TYR A 259       2.078   1.537 -38.786  1.00155.58           C  
ANISOU 1957  CD1 TYR A 259    17800  24226  17086  -1110     39  -2374       C  
ATOM   1958  CD2 TYR A 259       3.311   3.531 -39.215  1.00152.44           C  
ANISOU 1958  CD2 TYR A 259    16915  24194  16812   -937    133  -2168       C  
ATOM   1959  CE1 TYR A 259       2.040   1.266 -40.140  1.00157.15           C  
ANISOU 1959  CE1 TYR A 259    18010  24484  17218  -1041     37  -2561       C  
ATOM   1960  CE2 TYR A 259       3.282   3.265 -40.570  1.00154.10           C  
ANISOU 1960  CE2 TYR A 259    17115  24483  16954   -873    119  -2346       C  
ATOM   1961  CZ  TYR A 259       2.644   2.132 -41.027  1.00156.63           C  
ANISOU 1961  CZ  TYR A 259    17687  24647  17177   -924     80  -2546       C  
ATOM   1962  OH  TYR A 259       2.608   1.863 -42.375  1.00159.19           O  
ANISOU 1962  OH  TYR A 259    18025  25044  17415   -875     80  -2730       O  
ATOM   1963  N   THR A 260       1.751   3.331 -33.858  1.00149.14           N  
ANISOU 1963  N   THR A 260    16831  23363  16471  -1506    181  -1639       N  
ATOM   1964  CA  THR A 260       2.053   3.554 -32.449  1.00147.96           C  
ANISOU 1964  CA  THR A 260    16730  23154  16334  -1604    187  -1446       C  
ATOM   1965  C   THR A 260       1.320   2.560 -31.557  1.00149.13           C  
ANISOU 1965  C   THR A 260    17105  23147  16413  -1803    122  -1443       C  
ATOM   1966  O   THR A 260       1.823   2.201 -30.486  1.00149.06           O  
ANISOU 1966  O   THR A 260    17245  23011  16381  -1871     43  -1316       O  
ATOM   1967  CB  THR A 260       1.697   4.992 -32.062  1.00146.37           C  
ANISOU 1967  CB  THR A 260    16337  23060  16217  -1630    306  -1303       C  
ATOM   1968  OG1 THR A 260       2.424   5.904 -32.894  1.00146.23           O  
ANISOU 1968  OG1 THR A 260    16277  23014  16272  -1414    277  -1271       O  
ATOM   1969  CG2 THR A 260       2.047   5.270 -30.605  1.00144.88           C  
ANISOU 1969  CG2 THR A 260    16263  22743  16041  -1715    288  -1101       C  
ATOM   1970  N   LYS A 261       0.152   2.083 -31.988  1.00148.11           N  
ANISOU 1970  N   LYS A 261    17004  23029  16240  -1913    138  -1571       N  
ATOM   1971  CA  LYS A 261      -0.653   1.218 -31.132  1.00150.03           C  
ANISOU 1971  CA  LYS A 261    17434  23162  16409  -2140     85  -1551       C  
ATOM   1972  C   LYS A 261      -0.155  -0.223 -31.158  1.00151.96           C  
ANISOU 1972  C   LYS A 261    18023  23124  16591  -2120   -148  -1651       C  
ATOM   1973  O   LYS A 261       0.080  -0.824 -30.103  1.00152.72           O  
ANISOU 1973  O   LYS A 261    18301  23063  16662  -2234   -272  -1550       O  
ATOM   1974  CB  LYS A 261      -2.122   1.287 -31.553  1.00151.42           C  
ANISOU 1974  CB  LYS A 261    17497  23486  16548  -2284    190  -1636       C  
ATOM   1975  CG  LYS A 261      -2.767   2.646 -31.332  1.00150.53           C  
ANISOU 1975  CG  LYS A 261    17069  23635  16490  -2316    385  -1550       C  
ATOM   1976  CD  LYS A 261      -4.227   2.642 -31.756  1.00152.34           C  
ANISOU 1976  CD  LYS A 261    17186  24031  16666  -2447    472  -1642       C  
ATOM   1977  CE  LYS A 261      -4.900   3.971 -31.450  1.00151.20           C  
ANISOU 1977  CE  LYS A 261    16956  23880  16614  -2325    503  -1547       C  
ATOM   1978  NZ  LYS A 261      -4.350   5.081 -32.278  1.00149.80           N  
ANISOU 1978  NZ  LYS A 261    16720  23637  16559  -2049    468  -1535       N  
ATOM   1979  N   VAL A 262       0.020  -0.786 -32.358  1.00142.03           N  
ANISOU 1979  N   VAL A 262    16866  21791  15308  -1976   -226  -1857       N  
ATOM   1980  CA  VAL A 262       0.352  -2.205 -32.494  1.00144.47           C  
ANISOU 1980  CA  VAL A 262    17539  21800  15553  -1948   -470  -2009       C  
ATOM   1981  C   VAL A 262       1.624  -2.534 -31.722  1.00143.75           C  
ANISOU 1981  C   VAL A 262    17603  21536  15481  -1842   -642  -1922       C  
ATOM   1982  O   VAL A 262       1.640  -3.425 -30.864  1.00144.19           O  
ANISOU 1982  O   VAL A 262    17888  21365  15531  -1960   -852  -1892       O  
ATOM   1983  CB  VAL A 262       0.484  -2.586 -33.978  1.00146.12           C  
ANISOU 1983  CB  VAL A 262    17827  21976  15717  -1778   -489  -2255       C  
ATOM   1984  CG1 VAL A 262       0.928  -4.035 -34.115  1.00148.36           C  
ANISOU 1984  CG1 VAL A 262    18535  21905  15931  -1717   -753  -2446       C  
ATOM   1985  CG2 VAL A 262      -0.830  -2.352 -34.704  1.00147.31           C  
ANISOU 1985  CG2 VAL A 262    17836  22289  15847  -1914   -358  -2327       C  
ATOM   1986  N   ILE A 263       2.709  -1.812 -32.016  1.00140.49           N  
ANISOU 1986  N   ILE A 263    17043  21240  15098  -1629   -575  -1870       N  
ATOM   1987  CA  ILE A 263       3.969  -2.042 -31.316  1.00139.91           C  
ANISOU 1987  CA  ILE A 263    17047  21100  15014  -1546   -721  -1779       C  
ATOM   1988  C   ILE A 263       3.794  -1.860 -29.815  1.00138.64           C  
ANISOU 1988  C   ILE A 263    16896  20868  14913  -1739   -764  -1518       C  
ATOM   1989  O   ILE A 263       4.424  -2.569 -29.019  1.00140.63           O  
ANISOU 1989  O   ILE A 263    17239  21086  15106  -1852   -955  -1477       O  
ATOM   1990  CB  ILE A 263       5.067  -1.116 -31.878  1.00137.94           C  
ANISOU 1990  CB  ILE A 263    16575  21051  14785  -1306   -599  -1724       C  
ATOM   1991  CG1 ILE A 263       5.327  -1.438 -33.350  1.00139.78           C  
ANISOU 1991  CG1 ILE A 263    16786  21387  14935  -1117   -554  -2005       C  
ATOM   1992  CG2 ILE A 263       6.352  -1.249 -31.077  1.00138.66           C  
ANISOU 1992  CG2 ILE A 263    16616  21254  14814  -1275   -711  -1612       C  
ATOM   1993  CD1 ILE A 263       6.202  -0.423 -34.049  1.00138.89           C  
ANISOU 1993  CD1 ILE A 263    16412  21494  14867   -902   -416  -1937       C  
ATOM   1994  N   HIS A 264       2.917  -0.939 -29.401  1.00140.22           N  
ANISOU 1994  N   HIS A 264    16878  21264  15136  -1913   -535  -1387       N  
ATOM   1995  CA  HIS A 264       2.704  -0.721 -27.975  1.00140.03           C  
ANISOU 1995  CA  HIS A 264    16841  21244  15119  -2139   -513  -1156       C  
ATOM   1996  C   HIS A 264       2.182  -1.975 -27.288  1.00141.95           C  
ANISOU 1996  C   HIS A 264    17337  21268  15330  -2344   -721  -1170       C  
ATOM   1997  O   HIS A 264       2.432  -2.177 -26.094  1.00141.99           O  
ANISOU 1997  O   HIS A 264    17408  21198  15344  -2500   -809   -979       O  
ATOM   1998  CB  HIS A 264       1.742   0.445 -27.751  1.00138.96           C  
ANISOU 1998  CB  HIS A 264    16445  21363  14990  -2281   -228  -1067       C  
ATOM   1999  CG  HIS A 264       1.522   0.772 -26.307  1.00138.63           C  
ANISOU 1999  CG  HIS A 264    16390  21357  14926  -2517   -165   -839       C  
ATOM   2000  ND1 HIS A 264       2.475   1.400 -25.534  1.00137.17           N  
ANISOU 2000  ND1 HIS A 264    16160  21185  14775  -2503   -154   -640       N  
ATOM   2001  CD2 HIS A 264       0.462   0.553 -25.493  1.00139.87           C  
ANISOU 2001  CD2 HIS A 264    16575  21558  15012  -2792   -103   -772       C  
ATOM   2002  CE1 HIS A 264       2.010   1.557 -24.307  1.00138.07           C  
ANISOU 2002  CE1 HIS A 264    16285  21332  14842  -2760    -87   -466       C  
ATOM   2003  NE2 HIS A 264       0.791   1.051 -24.256  1.00139.64           N  
ANISOU 2003  NE2 HIS A 264    16524  21565  14970  -2935    -50   -544       N  
ATOM   2004  N   GLU A 265       1.457  -2.826 -28.016  1.00134.84           N  
ANISOU 2004  N   GLU A 265    16575  20260  14396  -2368   -807  -1382       N  
ATOM   2005  CA  GLU A 265       1.090  -4.127 -27.468  1.00137.54           C  
ANISOU 2005  CA  GLU A 265    17168  20361  14731  -2560  -1055  -1422       C  
ATOM   2006  C   GLU A 265       2.304  -5.044 -27.395  1.00140.05           C  
ANISOU 2006  C   GLU A 265    17627  20587  15001  -2582  -1330  -1511       C  
ATOM   2007  O   GLU A 265       2.552  -5.681 -26.363  1.00141.78           O  
ANISOU 2007  O   GLU A 265    17945  20700  15225  -2828  -1515  -1370       O  
ATOM   2008  CB  GLU A 265      -0.019  -4.760 -28.309  1.00140.03           C  
ANISOU 2008  CB  GLU A 265    17578  20629  14996  -2636  -1061  -1632       C  
ATOM   2009  CG  GLU A 265      -0.469  -6.139 -27.832  1.00144.12           C  
ANISOU 2009  CG  GLU A 265    18332  20951  15474  -2934  -1297  -1694       C  
ATOM   2010  CD  GLU A 265      -1.140  -6.113 -26.469  1.00143.94           C  
ANISOU 2010  CD  GLU A 265    18281  20961  15450  -3222  -1253  -1426       C  
ATOM   2011  OE1 GLU A 265      -1.698  -5.060 -26.094  1.00142.49           O  
ANISOU 2011  OE1 GLU A 265    17877  21069  15195  -3310   -960  -1263       O  
ATOM   2012  OE2 GLU A 265      -1.116  -7.151 -25.775  1.00146.40           O  
ANISOU 2012  OE2 GLU A 265    18775  21112  15738  -3512  -1465  -1376       O  
ATOM   2013  N   CYS A 266       3.081  -5.107 -28.479  1.00131.76           N  
ANISOU 2013  N   CYS A 266    16578  19588  13898  -2341  -1357  -1736       N  
ATOM   2014  CA  CYS A 266       4.242  -5.991 -28.531  1.00135.37           C  
ANISOU 2014  CA  CYS A 266    17150  19999  14283  -2332  -1620  -1888       C  
ATOM   2015  C   CYS A 266       5.189  -5.717 -27.371  1.00134.91           C  
ANISOU 2015  C   CYS A 266    16986  20011  14263  -2409  -1731  -1571       C  
ATOM   2016  O   CYS A 266       5.453  -6.598 -26.543  1.00137.64           O  
ANISOU 2016  O   CYS A 266    17477  20185  14634  -2676  -2014  -1469       O  
ATOM   2017  CB  CYS A 266       4.967  -5.821 -29.866  1.00135.73           C  
ANISOU 2017  CB  CYS A 266    17128  20209  14235  -1993  -1523  -2175       C  
ATOM   2018  SG  CYS A 266       4.005  -6.311 -31.308  1.00139.00           S  
ANISOU 2018  SG  CYS A 266    17714  20500  14600  -1916  -1422  -2541       S  
ATOM   2019  N   GLN A 267       5.691  -4.483 -27.281  1.00136.26           N  
ANISOU 2019  N   GLN A 267    16921  20386  14465  -2210  -1521  -1368       N  
ATOM   2020  CA  GLN A 267       6.604  -4.122 -26.204  1.00135.56           C  
ANISOU 2020  CA  GLN A 267    16726  20361  14419  -2267  -1602  -1032       C  
ATOM   2021  C   GLN A 267       5.971  -4.287 -24.831  1.00135.14           C  
ANISOU 2021  C   GLN A 267    16767  20141  14439  -2602  -1637   -763       C  
ATOM   2022  O   GLN A 267       6.691  -4.292 -23.829  1.00135.33           O  
ANISOU 2022  O   GLN A 267    16767  20150  14502  -2728  -1762   -466       O  
ATOM   2023  CB  GLN A 267       7.081  -2.677 -26.370  1.00131.81           C  
ANISOU 2023  CB  GLN A 267    16025  20070  13988  -2026  -1328   -876       C  
ATOM   2024  CG  GLN A 267       5.988  -1.641 -26.156  1.00128.12           C  
ANISOU 2024  CG  GLN A 267    15517  19543  13619  -2057  -1037   -793       C  
ATOM   2025  CD  GLN A 267       6.485  -0.219 -26.327  1.00124.74           C  
ANISOU 2025  CD  GLN A 267    14904  19218  13271  -1864   -813   -660       C  
ATOM   2026  OE1 GLN A 267       7.669   0.013 -26.577  1.00124.69           O  
ANISOU 2026  OE1 GLN A 267    14791  19346  13238  -1713   -848   -601       O  
ATOM   2027  NE2 GLN A 267       5.582   0.744 -26.180  1.00123.79           N  
ANISOU 2027  NE2 GLN A 267    14624  19262  13150  -2011   -542   -611       N  
ATOM   2028  N   GLN A 268       4.646  -4.413 -24.761  1.00130.52           N  
ANISOU 2028  N   GLN A 268    16269  19460  13863  -2747  -1518   -834       N  
ATOM   2029  CA  GLN A 268       3.974  -4.599 -23.485  1.00130.77           C  
ANISOU 2029  CA  GLN A 268    16374  19399  13913  -3067  -1511   -593       C  
ATOM   2030  C   GLN A 268       3.916  -6.061 -23.064  1.00135.48           C  
ANISOU 2030  C   GLN A 268    17207  19763  14506  -3391  -1841   -584       C  
ATOM   2031  O   GLN A 268       3.781  -6.344 -21.867  1.00137.55           O  
ANISOU 2031  O   GLN A 268    17549  19934  14778  -3687  -1909   -299       O  
ATOM   2032  CB  GLN A 268       2.555  -4.020 -23.550  1.00128.85           C  
ANISOU 2032  CB  GLN A 268    16077  19221  13661  -3079  -1229   -638       C  
ATOM   2033  CG  GLN A 268       1.844  -3.924 -22.210  1.00128.89           C  
ANISOU 2033  CG  GLN A 268    16106  19238  13630  -3372  -1136   -385       C  
ATOM   2034  CD  GLN A 268       2.459  -2.876 -21.303  1.00127.21           C  
ANISOU 2034  CD  GLN A 268    15770  19173  13392  -3416   -977   -111       C  
ATOM   2035  OE1 GLN A 268       2.797  -1.779 -21.745  1.00125.55           O  
ANISOU 2035  OE1 GLN A 268    15381  19129  13192  -3235   -785   -128       O  
ATOM   2036  NE2 GLN A 268       2.611  -3.212 -20.027  1.00128.20           N  
ANISOU 2036  NE2 GLN A 268    15996  19228  13484  -3678  -1061    155       N  
ATOM   2037  N   ARG A 269       4.038  -6.993 -24.009  1.00132.25           N  
ANISOU 2037  N   ARG A 269    16944  19221  14084  -3360  -2053   -882       N  
ATOM   2038  CA  ARG A 269       3.959  -8.421 -23.715  1.00137.09           C  
ANISOU 2038  CA  ARG A 269    17852  19499  14738  -3689  -2400   -898       C  
ATOM   2039  C   ARG A 269       5.306  -9.122 -23.741  1.00140.50           C  
ANISOU 2039  C   ARG A 269    18414  19733  15237  -3709  -2803   -866       C  
ATOM   2040  O   ARG A 269       5.533 -10.038 -22.948  1.00144.48           O  
ANISOU 2040  O   ARG A 269    19152  19879  15867  -4022  -3145   -631       O  
ATOM   2041  CB  ARG A 269       3.012  -9.110 -24.705  1.00138.64           C  
ANISOU 2041  CB  ARG A 269    18216  19565  14894  -3701  -2394  -1263       C  
ATOM   2042  CG  ARG A 269       1.581  -8.625 -24.603  1.00136.56           C  
ANISOU 2042  CG  ARG A 269    17847  19457  14585  -3747  -2096  -1221       C  
ATOM   2043  CD  ARG A 269       0.952  -9.063 -23.293  1.00138.59           C  
ANISOU 2043  CD  ARG A 269    18198  19623  14835  -4140  -2145   -907       C  
ATOM   2044  NE  ARG A 269      -0.448  -8.659 -23.202  1.00138.39           N  
ANISOU 2044  NE  ARG A 269    18073  19783  14726  -4202  -1878   -882       N  
ATOM   2045  CZ  ARG A 269      -0.862  -7.524 -22.650  1.00135.40           C  
ANISOU 2045  CZ  ARG A 269    17479  19664  14303  -4130  -1582   -708       C  
ATOM   2046  NH1 ARG A 269       0.017  -6.679 -22.129  1.00133.16           N  
ANISOU 2046  NH1 ARG A 269    17070  19471  14054  -3996  -1503   -540       N  
ATOM   2047  NH2 ARG A 269      -2.156  -7.235 -22.612  1.00134.89           N  
ANISOU 2047  NH2 ARG A 269    17335  19761  14157  -4206  -1374   -705       N  
ATOM   2048  N   MET A 270       6.208  -8.722 -24.639  1.00124.09           N  
ANISOU 2048  N   MET A 270    16199  17863  13088  -3377  -2797  -1064       N  
ATOM   2049  CA  MET A 270       7.552  -9.285 -24.636  1.00127.27           C  
ANISOU 2049  CA  MET A 270    16622  17936  13801  -3008  -2942   -907       C  
ATOM   2050  C   MET A 270       8.419  -8.643 -23.563  1.00125.60           C  
ANISOU 2050  C   MET A 270    16181  17888  13652  -3045  -3008   -411       C  
ATOM   2051  O   MET A 270       9.266  -9.318 -22.966  1.00128.48           O  
ANISOU 2051  O   MET A 270    16618  17862  14337  -2934  -3209    -99       O  
ATOM   2052  CB  MET A 270       8.191  -9.112 -26.013  1.00127.65           C  
ANISOU 2052  CB  MET A 270    16535  18071  13895  -2388  -2699  -1255       C  
ATOM   2053  CG  MET A 270       7.429  -9.814 -27.121  1.00129.63           C  
ANISOU 2053  CG  MET A 270    17039  18123  14090  -2331  -2641  -1754       C  
ATOM   2054  SD  MET A 270       8.112  -9.519 -28.761  1.00131.13           S  
ANISOU 2054  SD  MET A 270    17058  18506  14261  -1654  -2328  -2185       S  
ATOM   2055  CE  MET A 270       9.567 -10.556 -28.729  1.00139.08           C  
ANISOU 2055  CE  MET A 270    18135  18952  15756  -1087  -2433  -2063       C  
ATOM   2056  N   VAL A 271       8.220  -7.350 -23.311  1.00129.86           N  
ANISOU 2056  N   VAL A 271    16461  18974  13907  -3183  -2841   -328       N  
ATOM   2057  CA  VAL A 271       8.866  -6.627 -22.226  1.00127.98           C  
ANISOU 2057  CA  VAL A 271    16046  18832  13750  -3199  -2785    134       C  
ATOM   2058  C   VAL A 271       7.753  -6.064 -21.347  1.00125.37           C  
ANISOU 2058  C   VAL A 271    15765  18471  13398  -3408  -2452    240       C  
ATOM   2059  O   VAL A 271       6.597  -5.973 -21.764  1.00124.31           O  
ANISOU 2059  O   VAL A 271    15688  18346  13198  -3415  -2232    -17       O  
ATOM   2060  CB  VAL A 271       9.798  -5.509 -22.751  1.00125.29           C  
ANISOU 2060  CB  VAL A 271    15384  18866  13354  -2791  -2576    162       C  
ATOM   2061  CG1 VAL A 271      10.553  -4.825 -21.618  1.00123.84           C  
ANISOU 2061  CG1 VAL A 271    15072  18709  13271  -2830  -2528    633       C  
ATOM   2062  CG2 VAL A 271      10.768  -6.064 -23.782  1.00128.14           C  
ANISOU 2062  CG2 VAL A 271    15665  19161  13860  -2312  -2637      2       C  
ATOM   2063  N   ALA A 272       8.100  -5.758 -20.093  1.00132.16           N  
ANISOU 2063  N   ALA A 272    16608  19295  14313  -3587  -2445    648       N  
ATOM   2064  CA  ALA A 272       7.195  -5.137 -19.127  1.00130.09           C  
ANISOU 2064  CA  ALA A 272    16381  19062  13985  -3778  -2138    787       C  
ATOM   2065  C   ALA A 272       6.123  -6.115 -18.662  1.00132.63           C  
ANISOU 2065  C   ALA A 272    16935  19188  14269  -4123  -2236    787       C  
ATOM   2066  O   ALA A 272       5.354  -5.815 -17.742  1.00132.10           O  
ANISOU 2066  O   ALA A 272    16916  19168  14107  -4324  -2039    945       O  
ATOM   2067  CB  ALA A 272       6.542  -3.878 -19.706  1.00125.62           C  
ANISOU 2067  CB  ALA A 272    15661  18715  13356  -3513  -1715    556       C  
ATOM   2068  N   ASP A 273       6.071  -7.287 -19.288  1.00130.71           N  
ANISOU 2068  N   ASP A 273    16854  18724  14086  -4200  -2546    611       N  
ATOM   2069  CA  ASP A 273       5.205  -8.373 -18.863  1.00134.24           C  
ANISOU 2069  CA  ASP A 273    17563  18913  14528  -4554  -2705    645       C  
ATOM   2070  C   ASP A 273       5.967  -9.400 -18.038  1.00138.42           C  
ANISOU 2070  C   ASP A 273    18301  19076  15215  -4846  -3161   1006       C  
ATOM   2071  O   ASP A 273       5.349 -10.292 -17.448  1.00142.30           O  
ANISOU 2071  O   ASP A 273    19038  19321  15708  -5179  -3316   1139       O  
ATOM   2072  CB  ASP A 273       4.573  -9.043 -20.092  1.00135.93           C  
ANISOU 2072  CB  ASP A 273    17889  19019  14737  -4482  -2763    212       C  
ATOM   2073  CG  ASP A 273       3.343  -9.863 -19.755  1.00139.03           C  
ANISOU 2073  CG  ASP A 273    18497  19253  15077  -4803  -2778    209       C  
ATOM   2074  OD1 ASP A 273       2.946  -9.904 -18.573  1.00140.71           O  
ANISOU 2074  OD1 ASP A 273    18764  19477  15222  -5075  -2738    535       O  
ATOM   2075  OD2 ASP A 273       2.768 -10.467 -20.686  1.00140.40           O  
ANISOU 2075  OD2 ASP A 273    18791  19308  15247  -4783  -2825   -118       O  
ATOM   2076  N   HIS A 274       7.296  -9.278 -17.982  1.00128.82           N  
ANISOU 2076  N   HIS A 274    16981  17818  14146  -4714  -3397   1207       N  
ATOM   2077  CA  HIS A 274       8.158 -10.170 -17.218  1.00133.46           C  
ANISOU 2077  CA  HIS A 274    17723  18015  14969  -4934  -3889   1617       C  
ATOM   2078  C   HIS A 274       9.167  -9.375 -16.398  1.00131.52           C  
ANISOU 2078  C   HIS A 274    17257  17954  14760  -4861  -3841   2033       C  
ATOM   2079  O   HIS A 274      10.172  -9.935 -15.949  1.00135.39           O  
ANISOU 2079  O   HIS A 274    17764  18177  15502  -4913  -4271   2400       O  
ATOM   2080  CB  HIS A 274       8.899 -11.129 -18.153  1.00138.03           C  
ANISOU 2080  CB  HIS A 274    18423  18189  15834  -4712  -4324   1455       C  
ATOM   2081  CG  HIS A 274       8.004 -11.880 -19.088  1.00139.32           C  
ANISOU 2081  CG  HIS A 274    18849  18109  15977  -4698  -4297    991       C  
ATOM   2082  ND1 HIS A 274       7.219 -12.938 -18.686  1.00142.85           N  
ANISOU 2082  ND1 HIS A 274    19663  18157  16455  -5162  -4572   1022       N  
ATOM   2083  CD2 HIS A 274       7.773 -11.721 -20.413  1.00138.33           C  
ANISOU 2083  CD2 HIS A 274    18683  18093  15784  -4306  -4040    496       C  
ATOM   2084  CE1 HIS A 274       6.542 -13.399 -19.723  1.00144.52           C  
ANISOU 2084  CE1 HIS A 274    20055  18234  16622  -5055  -4487    563       C  
ATOM   2085  NE2 HIS A 274       6.860 -12.678 -20.783  1.00141.46           N  
ANISOU 2085  NE2 HIS A 274    19424  18150  16173  -4535  -4162    233       N  
ATOM   2086  N   LEU A 275       8.911  -8.079 -16.193  1.00132.83           N  
ANISOU 2086  N   LEU A 275    17229  18522  14717  -4730  -3344   1991       N  
ATOM   2087  CA  LEU A 275       9.964  -7.145 -15.805  1.00130.65           C  
ANISOU 2087  CA  LEU A 275    16725  18441  14476  -4561  -3236   2255       C  
ATOM   2088  C   LEU A 275      10.644  -7.505 -14.488  1.00132.96           C  
ANISOU 2088  C   LEU A 275    17104  18524  14890  -4847  -3484   2806       C  
ATOM   2089  O   LEU A 275      11.748  -7.012 -14.230  1.00133.00           O  
ANISOU 2089  O   LEU A 275    16918  18605  15011  -4713  -3511   3068       O  
ATOM   2090  CB  LEU A 275       9.403  -5.718 -15.759  1.00125.74           C  
ANISOU 2090  CB  LEU A 275    15971  18159  13646  -4426  -2678   2087       C  
ATOM   2091  CG  LEU A 275       8.198  -5.362 -14.882  1.00124.87           C  
ANISOU 2091  CG  LEU A 275    15998  18113  13332  -4675  -2374   2117       C  
ATOM   2092  CD1 LEU A 275       8.604  -5.037 -13.451  1.00125.17           C  
ANISOU 2092  CD1 LEU A 275    16107  18139  13313  -4930  -2348   2569       C  
ATOM   2093  CD2 LEU A 275       7.437  -4.196 -15.499  1.00120.38           C  
ANISOU 2093  CD2 LEU A 275    15280  17802  12657  -4422  -1930   1771       C  
ATOM   2094  N   GLN A 276      10.031  -8.351 -13.653  1.00124.48           N  
ANISOU 2094  N   GLN A 276    16312  17198  13786  -5227  -3660   3003       N  
ATOM   2095  CA  GLN A 276      10.752  -8.848 -12.484  1.00127.81           C  
ANISOU 2095  CA  GLN A 276    16843  17378  14342  -5491  -3981   3555       C  
ATOM   2096  C   GLN A 276      12.037  -9.554 -12.894  1.00131.08           C  
ANISOU 2096  C   GLN A 276    17134  17498  15173  -5331  -4506   3753       C  
ATOM   2097  O   GLN A 276      13.079  -9.389 -12.248  1.00132.10           O  
ANISOU 2097  O   GLN A 276    17128  17586  15478  -5327  -4638   4169       O  
ATOM   2098  CB  GLN A 276       9.878  -9.795 -11.660  1.00131.61           C  
ANISOU 2098  CB  GLN A 276    17673  17639  14694  -5867  -4160   3718       C  
ATOM   2099  CG  GLN A 276       8.767  -9.135 -10.868  1.00129.47           C  
ANISOU 2099  CG  GLN A 276    17502  17710  13979  -6005  -3736   3688       C  
ATOM   2100  CD  GLN A 276       8.035 -10.129  -9.981  1.00133.33           C  
ANISOU 2100  CD  GLN A 276    18302  18061  14298  -6340  -3979   3889       C  
ATOM   2101  OE1 GLN A 276       8.306 -11.331 -10.021  1.00137.57           O  
ANISOU 2101  OE1 GLN A 276    19003  18190  15079  -6480  -4448   4026       O  
ATOM   2102  NE2 GLN A 276       7.115  -9.629  -9.164  1.00131.77           N  
ANISOU 2102  NE2 GLN A 276    18062  18157  13849  -6331  -3631   3701       N  
ATOM   2103  N   PHE A 277      11.980 -10.342 -13.970  1.00115.98           N  
ANISOU 2103  N   PHE A 277    15263  15373  13433  -5157  -4821   3457       N  
ATOM   2104  CA  PHE A 277      13.155 -11.079 -14.425  1.00120.13           C  
ANISOU 2104  CA  PHE A 277    15727  15515  14400  -4693  -5143   3595       C  
ATOM   2105  C   PHE A 277      14.271 -10.130 -14.847  1.00118.29           C  
ANISOU 2105  C   PHE A 277    15097  15651  14198  -4176  -4923   3663       C  
ATOM   2106  O   PHE A 277      15.402 -10.219 -14.349  1.00120.86           O  
ANISOU 2106  O   PHE A 277    15276  15867  14779  -4000  -5093   4098       O  
ATOM   2107  CB  PHE A 277      12.758 -12.016 -15.568  1.00122.72           C  
ANISOU 2107  CB  PHE A 277    16279  15427  14921  -4327  -5101   3113       C  
ATOM   2108  CG  PHE A 277      13.892 -12.838 -16.105  1.00127.83           C  
ANISOU 2108  CG  PHE A 277    16919  15586  16066  -3653  -5210   3145       C  
ATOM   2109  CD1 PHE A 277      14.437 -13.867 -15.353  1.00133.42           C  
ANISOU 2109  CD1 PHE A 277    17818  15721  17155  -3705  -5613   3554       C  
ATOM   2110  CD2 PHE A 277      14.395 -12.603 -17.374  1.00127.24           C  
ANISOU 2110  CD2 PHE A 277    16647  15625  16074  -2963  -4916   2758       C  
ATOM   2111  CE1 PHE A 277      15.478 -14.631 -15.847  1.00139.26           C  
ANISOU 2111  CE1 PHE A 277    18540  16002  18372  -3036  -5715   3568       C  
ATOM   2112  CE2 PHE A 277      15.434 -13.366 -17.876  1.00136.00           C  
ANISOU 2112  CE2 PHE A 277    17727  16314  17632  -2312  -4994   2757       C  
ATOM   2113  CZ  PHE A 277      15.976 -14.382 -17.110  1.00142.70           C  
ANISOU 2113  CZ  PHE A 277    18758  16582  18880  -2326  -5392   3155       C  
ATOM   2114  N   LEU A 278      13.968  -9.206 -15.763  1.00110.64           N  
ANISOU 2114  N   LEU A 278    18900  14206   8932  -4744    142     12       N  
ATOM   2115  CA  LEU A 278      14.972  -8.246 -16.209  1.00110.35           C  
ANISOU 2115  CA  LEU A 278    18655  14258   9015  -4231    116    211       C  
ATOM   2116  C   LEU A 278      15.541  -7.467 -15.031  1.00109.44           C  
ANISOU 2116  C   LEU A 278    18550  14044   8990  -4409    107    277       C  
ATOM   2117  O   LEU A 278      16.764  -7.396 -14.853  1.00107.82           O  
ANISOU 2117  O   LEU A 278    18486  13628   8854  -4155    -67    507       O  
ATOM   2118  CB  LEU A 278      14.367  -7.301 -17.247  1.00112.02           C  
ANISOU 2118  CB  LEU A 278    18411  14893   9259  -3946    310    138       C  
ATOM   2119  CG  LEU A 278      13.990  -7.949 -18.579  1.00112.87           C  
ANISOU 2119  CG  LEU A 278    18470  15151   9262  -3658    294     99       C  
ATOM   2120  CD1 LEU A 278      13.265  -6.960 -19.475  1.00115.09           C  
ANISOU 2120  CD1 LEU A 278    18330  15854   9544  -3462    453     20       C  
ATOM   2121  CD2 LEU A 278      15.229  -8.495 -19.272  1.00111.88           C  
ANISOU 2121  CD2 LEU A 278    18516  14881   9111  -3212    111    344       C  
ATOM   2122  N   HIS A 279      14.663  -6.895 -14.198  1.00115.67           N  
ANISOU 2122  N   HIS A 279    19176  15004   9769  -4863    294     41       N  
ATOM   2123  CA  HIS A 279      15.118  -6.182 -13.007  1.00114.19           C  
ANISOU 2123  CA  HIS A 279    18997  14765   9627  -5094    297     46       C  
ATOM   2124  C   HIS A 279      16.008  -7.054 -12.131  1.00111.10           C  
ANISOU 2124  C   HIS A 279    19084  13951   9178  -5254     23    222       C  
ATOM   2125  O   HIS A 279      16.907  -6.541 -11.454  1.00109.73           O  
ANISOU 2125  O   HIS A 279    18966  13663   9061  -5198    -82    342       O  
ATOM   2126  CB  HIS A 279      13.921  -5.676 -12.197  1.00113.94           C  
ANISOU 2126  CB  HIS A 279    18726  15013   9552  -5651    557   -312       C  
ATOM   2127  CG  HIS A 279      13.166  -4.562 -12.854  1.00117.69           C  
ANISOU 2127  CG  HIS A 279    18708  15906  10103  -5509    785   -549       C  
ATOM   2128  ND1 HIS A 279      12.135  -4.781 -13.742  1.00120.09           N  
ANISOU 2128  ND1 HIS A 279    18809  16435  10386  -5464    897   -744       N  
ATOM   2129  CD2 HIS A 279      13.284  -3.218 -12.742  1.00119.83           C  
ANISOU 2129  CD2 HIS A 279    18664  16408  10459  -5424    897   -649       C  
ATOM   2130  CE1 HIS A 279      11.657  -3.620 -14.154  1.00123.13           C  
ANISOU 2130  CE1 HIS A 279    18777  17166  10841  -5344   1039   -967       C  
ATOM   2131  NE2 HIS A 279      12.336  -2.656 -13.560  1.00123.07           N  
ANISOU 2131  NE2 HIS A 279    18699  17166  10895  -5333   1048   -918       N  
ATOM   2132  N   ALA A 280      15.784  -8.371 -12.139  1.00107.58           N  
ANISOU 2132  N   ALA A 280    19009  13255   8612  -5466   -120    245       N  
ATOM   2133  CA  ALA A 280      16.607  -9.264 -11.330  1.00106.35           C  
ANISOU 2133  CA  ALA A 280    19375  12652   8381  -5649   -446    416       C  
ATOM   2134  C   ALA A 280      17.990  -9.454 -11.941  1.00106.13           C  
ANISOU 2134  C   ALA A 280    19485  12384   8454  -5050   -728    653       C  
ATOM   2135  O   ALA A 280      18.994  -9.466 -11.220  1.00105.04           O  
ANISOU 2135  O   ALA A 280    19580  11983   8347  -5019   -976    789       O  
ATOM   2136  CB  ALA A 280      15.905 -10.610 -11.153  1.00106.95           C  
ANISOU 2136  CB  ALA A 280    19857  12499   8281  -6123   -535    386       C  
ATOM   2137  N   GLU A 281      18.067  -9.607 -13.265  1.00109.54           N  
ANISOU 2137  N   GLU A 281    19763  12930   8926  -4583   -695    690       N  
ATOM   2138  CA  GLU A 281      19.370  -9.731 -13.911  1.00109.14           C  
ANISOU 2138  CA  GLU A 281    19783  12727   8959  -4029   -919    886       C  
ATOM   2139  C   GLU A 281      20.130  -8.411 -13.970  1.00107.98           C  
ANISOU 2139  C   GLU A 281    19265  12780   8983  -3682   -803   1014       C  
ATOM   2140  O   GLU A 281      21.333  -8.419 -14.266  1.00108.00           O  
ANISOU 2140  O   GLU A 281    19324  12642   9069  -3289   -989   1188       O  
ATOM   2141  CB  GLU A 281      19.207 -10.297 -15.322  1.00110.29           C  
ANISOU 2141  CB  GLU A 281    19869  12996   9042  -3677   -901    861       C  
ATOM   2142  CG  GLU A 281      18.714 -11.738 -15.363  1.00111.52           C  
ANISOU 2142  CG  GLU A 281    20475  12862   9036  -3953  -1100    775       C  
ATOM   2143  CD  GLU A 281      19.735 -12.729 -14.829  1.00112.15           C  
ANISOU 2143  CD  GLU A 281    21133  12387   9094  -3964  -1578    900       C  
ATOM   2144  OE1 GLU A 281      20.949 -12.480 -14.993  1.00112.25           O  
ANISOU 2144  OE1 GLU A 281    21140  12303   9205  -3537  -1771   1018       O  
ATOM   2145  OE2 GLU A 281      19.323 -13.758 -14.247  1.00112.88           O  
ANISOU 2145  OE2 GLU A 281    21700  12117   9072  -4413  -1789    889       O  
ATOM   2146  N   CYS A 282      19.462  -7.286 -13.695  1.00101.54           N  
ANISOU 2146  N   CYS A 282    18090  12271   8221  -3839   -518    926       N  
ATOM   2147  CA  CYS A 282      20.136  -5.990 -13.730  1.00100.79           C  
ANISOU 2147  CA  CYS A 282    17674  12325   8296  -3565   -416   1078       C  
ATOM   2148  C   CYS A 282      21.302  -5.937 -12.750  1.00 99.77           C  
ANISOU 2148  C   CYS A 282    17772  11900   8238  -3571   -658   1209       C  
ATOM   2149  O   CYS A 282      22.397  -5.491 -13.107  1.00 99.78           O  
ANISOU 2149  O   CYS A 282    17666  11854   8392  -3174   -729   1425       O  
ATOM   2150  CB  CYS A 282      19.139  -4.869 -13.443  1.00101.35           C  
ANISOU 2150  CB  CYS A 282    17407  12718   8384  -3829   -126    915       C  
ATOM   2151  SG  CYS A 282      17.956  -4.580 -14.769  1.00103.68           S  
ANISOU 2151  SG  CYS A 282    17351  13399   8645  -3694    123    806       S  
ATOM   2152  N   HIS A 283      21.084  -6.385 -11.506  1.00 97.34           N  
ANISOU 2152  N   HIS A 283    17774  11398   7813  -4042   -791   1087       N  
ATOM   2153  CA  HIS A 283      22.153  -6.383 -10.506  1.00 96.68           C  
ANISOU 2153  CA  HIS A 283    17941  11029   7764  -4076  -1069   1196       C  
ATOM   2154  C   HIS A 283      23.439  -6.991 -11.049  1.00 97.64           C  
ANISOU 2154  C   HIS A 283    18254  10855   7989  -3604  -1390   1394       C  
ATOM   2155  O   HIS A 283      24.534  -6.474 -10.802  1.00 97.94           O  
ANISOU 2155  O   HIS A 283    18249  10787   8178  -3354  -1529   1541       O  
ATOM   2156  CB  HIS A 283      21.714  -7.143  -9.255  1.00 96.22           C  
ANISOU 2156  CB  HIS A 283    18289  10762   7507  -4672  -1231   1070       C  
ATOM   2157  CG  HIS A 283      22.754  -7.174  -8.177  1.00 95.87           C  
ANISOU 2157  CG  HIS A 283    18532  10430   7464  -4742  -1556   1174       C  
ATOM   2158  ND1 HIS A 283      23.784  -8.091  -8.165  1.00 97.11           N  
ANISOU 2158  ND1 HIS A 283    19074  10162   7660  -4519  -1998   1319       N  
ATOM   2159  CD2 HIS A 283      22.917  -6.413  -7.070  1.00 95.29           C  
ANISOU 2159  CD2 HIS A 283    18427  10431   7348  -5018  -1533   1135       C  
ATOM   2160  CE1 HIS A 283      24.541  -7.887  -7.103  1.00 97.25           C  
ANISOU 2160  CE1 HIS A 283    19277   9999   7674  -4634  -2246   1376       C  
ATOM   2161  NE2 HIS A 283      24.036  -6.876  -6.420  1.00 96.49           N  
ANISOU 2161  NE2 HIS A 283    18940  10210   7514  -4946  -1958   1277       N  
ATOM   2162  N   ASN A 284      23.324  -8.098 -11.783  1.00105.93           N  
ANISOU 2162  N   ASN A 284    19526  11762   8961  -3490  -1530   1378       N  
ATOM   2163  CA  ASN A 284      24.493  -8.694 -12.418  1.00108.01           C  
ANISOU 2163  CA  ASN A 284    19963  11773   9302  -3024  -1850   1505       C  
ATOM   2164  C   ASN A 284      24.998  -7.823 -13.561  1.00109.70           C  
ANISOU 2164  C   ASN A 284    19735  12301   9645  -2523  -1623   1635       C  
ATOM   2165  O   ASN A 284      26.199  -7.543 -13.659  1.00111.68           O  
ANISOU 2165  O   ASN A 284    19957  12435  10042  -2176  -1798   1778       O  
ATOM   2166  CB  ASN A 284      24.154 -10.098 -12.923  1.00109.52           C  
ANISOU 2166  CB  ASN A 284    20535  11731   9346  -3064  -2075   1422       C  
ATOM   2167  CG  ASN A 284      25.373 -10.855 -13.422  1.00112.34           C  
ANISOU 2167  CG  ASN A 284    21166  11749   9768  -2609  -2530   1483       C  
ATOM   2168  OD1 ASN A 284      26.494 -10.351 -13.383  1.00113.45           O  
ANISOU 2168  OD1 ASN A 284    21197  11834  10075  -2261  -2674   1587       O  
ATOM   2169  ND2 ASN A 284      25.153 -12.071 -13.908  1.00113.99           N  
ANISOU 2169  ND2 ASN A 284    21735  11717   9859  -2598  -2793   1393       N  
ATOM   2170  N   ILE A 285      24.092  -7.376 -14.434  1.00102.65           N  
ANISOU 2170  N   ILE A 285    18496  11802   8703  -2497  -1251   1595       N  
ATOM   2171  CA  ILE A 285      24.536  -6.777 -15.690  1.00103.92           C  
ANISOU 2171  CA  ILE A 285    18304  12258   8923  -2053  -1070   1743       C  
ATOM   2172  C   ILE A 285      25.224  -5.432 -15.467  1.00103.75           C  
ANISOU 2172  C   ILE A 285    17938  12333   9151  -1917   -931   1946       C  
ATOM   2173  O   ILE A 285      26.180  -5.098 -16.178  1.00106.49           O  
ANISOU 2173  O   ILE A 285    17930  12771   9762  -1488   -896   2026       O  
ATOM   2174  CB  ILE A 285      23.353  -6.672 -16.668  1.00104.48           C  
ANISOU 2174  CB  ILE A 285    18107  12712   8879  -2073   -760   1652       C  
ATOM   2175  CG1 ILE A 285      22.856  -8.073 -17.016  1.00105.52           C  
ANISOU 2175  CG1 ILE A 285    18576  12718   8799  -2151   -927   1459       C  
ATOM   2176  CG2 ILE A 285      23.767  -5.966 -17.940  1.00106.59           C  
ANISOU 2176  CG2 ILE A 285    17979  13326   9193  -1671   -557   1830       C  
ATOM   2177  CD1 ILE A 285      21.585  -8.092 -17.812  1.00106.23           C  
ANISOU 2177  CD1 ILE A 285    18444  13143   8776  -2228   -668   1321       C  
ATOM   2178  N   ILE A 286      24.781  -4.643 -14.482  1.00 99.13           N  
ANISOU 2178  N   ILE A 286    17269  11752   8644  -2239   -822   1925       N  
ATOM   2179  CA  ILE A 286      25.435  -3.357 -14.238  1.00 99.52           C  
ANISOU 2179  CA  ILE A 286    16927  11849   9037  -2099   -709   2072       C  
ATOM   2180  C   ILE A 286      26.768  -3.506 -13.523  1.00100.21           C  
ANISOU 2180  C   ILE A 286    17153  11613   9307  -1950  -1011   2118       C  
ATOM   2181  O   ILE A 286      27.546  -2.545 -13.485  1.00102.23           O  
ANISOU 2181  O   ILE A 286    17011  11896   9937  -1734   -936   2214       O  
ATOM   2182  CB  ILE A 286      24.528  -2.383 -13.457  1.00 98.37           C  
ANISOU 2182  CB  ILE A 286    16616  11832   8930  -2476   -508   1984       C  
ATOM   2183  CG1 ILE A 286      24.058  -2.981 -12.127  1.00 97.12           C  
ANISOU 2183  CG1 ILE A 286    16899  11513   8491  -2976   -660   1777       C  
ATOM   2184  CG2 ILE A 286      23.338  -1.953 -14.304  1.00 99.40           C  
ANISOU 2184  CG2 ILE A 286    16439  12292   9035  -2505   -225   1925       C  
ATOM   2185  CD1 ILE A 286      24.943  -2.665 -10.942  1.00 96.17           C  
ANISOU 2185  CD1 ILE A 286    16936  11157   8448  -3087   -867   1828       C  
ATOM   2186  N   ARG A 287      27.058  -4.680 -12.957  1.00 93.65           N  
ANISOU 2186  N   ARG A 287    16879  10454   8251  -2060  -1387   2054       N  
ATOM   2187  CA  ARG A 287      28.368  -4.967 -12.390  1.00 95.63           C  
ANISOU 2187  CA  ARG A 287    17278  10360   8699  -1849  -1767   2070       C  
ATOM   2188  C   ARG A 287      29.246  -5.750 -13.359  1.00 98.26           C  
ANISOU 2188  C   ARG A 287    17546  10612   9177  -1359  -1956   2002       C  
ATOM   2189  O   ARG A 287      30.244  -6.351 -12.950  1.00100.44           O  
ANISOU 2189  O   ARG A 287    18035  10537   9590  -1169  -2381   1934       O  
ATOM   2190  CB  ARG A 287      28.218  -5.699 -11.057  1.00 95.80           C  
ANISOU 2190  CB  ARG A 287    17889  10040   8472  -2268  -2129   2007       C  
ATOM   2191  CG  ARG A 287      27.542  -4.829 -10.012  1.00 94.38           C  
ANISOU 2191  CG  ARG A 287    17602  10022   8236  -2715  -1910   1944       C  
ATOM   2192  CD  ARG A 287      27.425  -5.489  -8.655  1.00 95.14           C  
ANISOU 2192  CD  ARG A 287    18135   9873   8140  -3148  -2207   1810       C  
ATOM   2193  NE  ARG A 287      26.599  -4.688  -7.752  1.00 94.38           N  
ANISOU 2193  NE  ARG A 287    17934  10024   7904  -3627  -1949   1693       N  
ATOM   2194  CZ  ARG A 287      27.054  -3.697  -6.992  1.00 94.80           C  
ANISOU 2194  CZ  ARG A 287    17875  10116   8030  -3706  -1941   1739       C  
ATOM   2195  NH1 ARG A 287      28.340  -3.370  -7.021  1.00 95.76           N  
ANISOU 2195  NH1 ARG A 287    17954  10021   8410  -3323  -2178   1923       N  
ATOM   2196  NH2 ARG A 287      26.221  -3.028  -6.205  1.00 94.79           N  
ANISOU 2196  NH2 ARG A 287    17795  10371   7850  -4182  -1703   1578       N  
ATOM   2197  N   GLN A 288      28.870  -5.762 -14.634  1.00105.23           N  
ANISOU 2197  N   GLN A 288    18125  11828  10029  -1155  -1669   1979       N  
ATOM   2198  CA  GLN A 288      29.738  -6.135 -15.743  1.00111.89           C  
ANISOU 2198  CA  GLN A 288    18676  12786  11050   -667  -1692   1871       C  
ATOM   2199  C   GLN A 288      29.841  -4.948 -16.686  1.00113.54           C  
ANISOU 2199  C   GLN A 288    18236  13467  11439   -484  -1229   2010       C  
ATOM   2200  O   GLN A 288      28.821  -4.435 -17.157  1.00109.89           O  
ANISOU 2200  O   GLN A 288    17635  13295  10823   -651   -915   2125       O  
ATOM   2201  CB  GLN A 288      29.210  -7.368 -16.479  1.00114.71           C  
ANISOU 2201  CB  GLN A 288    19305  13140  11140   -620  -1811   1699       C  
ATOM   2202  CG  GLN A 288      29.837  -7.593 -17.858  1.00121.62           C  
ANISOU 2202  CG  GLN A 288    19753  14330  12128   -157  -1689   1534       C  
ATOM   2203  CD  GLN A 288      31.354  -7.628 -17.846  1.00127.79           C  
ANISOU 2203  CD  GLN A 288    20279  14992  13282    239  -1902   1377       C  
ATOM   2204  OE1 GLN A 288      32.010  -6.672 -18.268  1.00131.10           O  
ANISOU 2204  OE1 GLN A 288    20168  15725  13919    411  -1611   1456       O  
ATOM   2205  NE2 GLN A 288      31.921  -8.730 -17.368  1.00129.40           N  
ANISOU 2205  NE2 GLN A 288    20853  14728  13584    374  -2436   1144       N  
ATOM   2206  N   GLU A 289      31.072  -4.516 -16.960  1.00114.01           N  
ANISOU 2206  N   GLU A 289    17900  13589  11829   -162  -1213   1999       N  
ATOM   2207  CA  GLU A 289      31.290  -3.386 -17.852  1.00117.67           C  
ANISOU 2207  CA  GLU A 289    17774  14479  12457    -39   -801   2182       C  
ATOM   2208  C   GLU A 289      30.806  -3.668 -19.269  1.00119.55           C  
ANISOU 2208  C   GLU A 289    17835  15150  12437     74   -554   2173       C  
ATOM   2209  O   GLU A 289      30.701  -2.732 -20.071  1.00121.49           O  
ANISOU 2209  O   GLU A 289    17674  15773  12715     84   -217   2399       O  
ATOM   2210  CB  GLU A 289      32.776  -3.016 -17.864  1.00125.39           C  
ANISOU 2210  CB  GLU A 289    18375  15452  13816    244   -840   2120       C  
ATOM   2211  CG  GLU A 289      33.350  -2.640 -16.493  1.00122.87           C  
ANISOU 2211  CG  GLU A 289    18175  14731  13778    161  -1095   2122       C  
ATOM   2212  CD  GLU A 289      32.778  -1.354 -15.926  1.00117.44           C  
ANISOU 2212  CD  GLU A 289    17345  14065  13212   -122   -872   2380       C  
ATOM   2213  OE1 GLU A 289      32.450  -0.447 -16.718  1.00118.36           O  
ANISOU 2213  OE1 GLU A 289    17078  14505  13388   -144   -516   2596       O  
ATOM   2214  OE2 GLU A 289      32.661  -1.249 -14.685  1.00111.96           O  
ANISOU 2214  OE2 GLU A 289    16922  13061  12556   -330  -1083   2353       O  
ATOM   2215  N   LYS A 290      30.508  -4.923 -19.593  1.00116.38           N  
ANISOU 2215  N   LYS A 290    17743  14693  11783    144   -742   1927       N  
ATOM   2216  CA  LYS A 290      29.978  -5.292 -20.899  1.00117.42           C  
ANISOU 2216  CA  LYS A 290    17739  15245  11631    239   -536   1864       C  
ATOM   2217  C   LYS A 290      28.456  -5.408 -20.858  1.00111.59           C  
ANISOU 2217  C   LYS A 290    17288  14525  10588    -64   -465   1945       C  
ATOM   2218  O   LYS A 290      27.889  -5.931 -19.896  1.00107.31           O  
ANISOU 2218  O   LYS A 290    17201  13614   9960   -314   -691   1876       O  
ATOM   2219  CB  LYS A 290      30.595  -6.609 -21.371  1.00120.90           C  
ANISOU 2219  CB  LYS A 290    18273  15635  12029    534   -792   1463       C  
ATOM   2220  CG  LYS A 290      30.106  -7.074 -22.730  1.00120.87           C  
ANISOU 2220  CG  LYS A 290    18113  16098  11714    646   -594   1324       C  
ATOM   2221  CD  LYS A 290      30.623  -6.178 -23.835  1.00123.68           C  
ANISOU 2221  CD  LYS A 290    17882  17060  12053    771   -190   1463       C  
ATOM   2222  CE  LYS A 290      30.230  -6.715 -25.197  1.00125.11           C  
ANISOU 2222  CE  LYS A 290    17912  17753  11873    882    -20   1283       C  
ATOM   2223  NZ  LYS A 290      30.679  -5.818 -26.295  1.00128.00           N  
ANISOU 2223  NZ  LYS A 290    17748  18761  12126    915    381   1476       N  
ATOM   2224  N   ASN A 292      27.231  -3.921 -23.466  1.00111.26           N  
ANISOU 2224  N   ASN A 292    16490  15600  10184    -29    252   2375       N  
ATOM   2225  CA  ASN A 292      26.305  -4.127 -24.575  1.00109.68           C  
ANISOU 2225  CA  ASN A 292    16242  15796   9635    -31    387   2374       C  
ATOM   2226  C   ASN A 292      24.970  -4.638 -24.045  1.00106.26           C  
ANISOU 2226  C   ASN A 292    16181  15146   9046   -271    270   2233       C  
ATOM   2227  O   ASN A 292      23.906  -4.070 -24.329  1.00104.42           O  
ANISOU 2227  O   ASN A 292    15871  15079   8726   -415    381   2364       O  
ATOM   2228  CB  ASN A 292      26.894  -5.110 -25.590  1.00113.64           C  
ANISOU 2228  CB  ASN A 292    16661  16609   9907    231    389   2086       C  
ATOM   2229  CG  ASN A 292      26.107  -5.158 -26.888  1.00112.52           C  
ANISOU 2229  CG  ASN A 292    16385  16987   9381    246    561   2116       C  
ATOM   2230  OD1 ASN A 292      25.097  -4.472 -27.045  1.00108.65           O  
ANISOU 2230  OD1 ASN A 292    15877  16592   8812     78    644   2366       O  
ATOM   2231  ND2 ASN A 292      26.573  -5.969 -27.830  1.00116.17           N  
ANISOU 2231  ND2 ASN A 292    16729  17798   9614    459    590   1820       N  
ATOM   2232  N   ASP A 293      25.046  -5.721 -23.268  1.00118.45           N  
ANISOU 2232  N   ASP A 293    18129  16308  10567   -329     19   1954       N  
ATOM   2233  CA  ASP A 293      23.854  -6.269 -22.632  1.00115.50           C  
ANISOU 2233  CA  ASP A 293    18146  15711  10028   -645    -87   1811       C  
ATOM   2234  C   ASP A 293      23.151  -5.207 -21.797  1.00112.59           C  
ANISOU 2234  C   ASP A 293    17723  15253   9804   -943     18   1984       C  
ATOM   2235  O   ASP A 293      21.916  -5.163 -21.737  1.00111.07           O  
ANISOU 2235  O   ASP A 293    17596  15136   9469  -1188     85   1903       O  
ATOM   2236  CB  ASP A 293      24.239  -7.463 -21.760  1.00116.28           C  
ANISOU 2236  CB  ASP A 293    18725  15334  10122   -718   -425   1580       C  
ATOM   2237  CG  ASP A 293      24.911  -8.568 -22.551  1.00119.87           C  
ANISOU 2237  CG  ASP A 293    19210  15822  10514   -391   -593   1315       C  
ATOM   2238  OD1 ASP A 293      24.654  -8.670 -23.770  1.00121.65           O  
ANISOU 2238  OD1 ASP A 293    19182  16482  10557   -215   -421   1234       O  
ATOM   2239  OD2 ASP A 293      25.694  -9.337 -21.953  1.00121.40           O  
ANISOU 2239  OD2 ASP A 293    19671  15607  10849   -307   -927   1160       O  
ATOM   2240  N   MET A 294      23.930  -4.334 -21.156  1.00102.59           N  
ANISOU 2240  N   MET A 294    16292  13841   8848   -920     29   2169       N  
ATOM   2241  CA  MET A 294      23.363  -3.272 -20.335  1.00100.19           C  
ANISOU 2241  CA  MET A 294    15877  13447   8743  -1173    111   2273       C  
ATOM   2242  C   MET A 294      22.770  -2.162 -21.192  1.00100.49           C  
ANISOU 2242  C   MET A 294    15489  13808   8883  -1103    308   2476       C  
ATOM   2243  O   MET A 294      21.770  -1.545 -20.801  1.00100.38           O  
ANISOU 2243  O   MET A 294    15391  13790   8958  -1318    354   2426       O  
ATOM   2244  CB  MET A 294      24.445  -2.742 -19.393  1.00 99.27           C  
ANISOU 2244  CB  MET A 294    15717  13056   8945  -1150     25   2374       C  
ATOM   2245  CG  MET A 294      23.995  -1.703 -18.395  1.00 97.43           C  
ANISOU 2245  CG  MET A 294    15370  12701   8949  -1411     77   2404       C  
ATOM   2246  SD  MET A 294      25.311  -1.363 -17.212  1.00 96.46           S  
ANISOU 2246  SD  MET A 294    15282  12234   9135  -1392    -81   2452       S  
ATOM   2247  CE  MET A 294      26.509  -0.542 -18.258  1.00 99.18           C  
ANISOU 2247  CE  MET A 294    15117  12764   9801   -983     49   2741       C  
ATOM   2248  N   ALA A 295      23.359  -1.906 -22.363  1.00 94.86           N  
ANISOU 2248  N   ALA A 295    14502  13387   8154   -822    403   2687       N  
ATOM   2249  CA  ALA A 295      22.766  -0.960 -23.303  1.00 95.11           C  
ANISOU 2249  CA  ALA A 295    14201  13720   8216   -771    522   2934       C  
ATOM   2250  C   ALA A 295      21.390  -1.433 -23.754  1.00 95.36           C  
ANISOU 2250  C   ALA A 295    14342  13924   7967   -872    512   2738       C  
ATOM   2251  O   ALA A 295      20.415  -0.671 -23.723  1.00 95.73           O  
ANISOU 2251  O   ALA A 295    14227  13996   8150   -983    510   2766       O  
ATOM   2252  CB  ALA A 295      23.691  -0.763 -24.503  1.00 96.38           C  
ANISOU 2252  CB  ALA A 295    14110  14221   8290   -525    632   3194       C  
ATOM   2253  N   ASN A 296      21.291  -2.698 -24.175  1.00 97.26           N  
ANISOU 2253  N   ASN A 296    14831  14269   7853   -824    481   2496       N  
ATOM   2254  CA  ASN A 296      19.982  -3.251 -24.512  1.00 97.66           C  
ANISOU 2254  CA  ASN A 296    15003  14460   7645   -948    465   2255       C  
ATOM   2255  C   ASN A 296      19.046  -3.237 -23.309  1.00 97.02           C  
ANISOU 2255  C   ASN A 296    15092  14109   7661  -1302    426   2014       C  
ATOM   2256  O   ASN A 296      17.836  -3.026 -23.466  1.00 98.64           O  
ANISOU 2256  O   ASN A 296    15203  14447   7830  -1438    449   1865       O  
ATOM   2257  CB  ASN A 296      20.134  -4.671 -25.059  1.00 98.40           C  
ANISOU 2257  CB  ASN A 296    15347  14645   7397   -845    410   1996       C  
ATOM   2258  CG  ASN A 296      20.718  -4.699 -26.461  1.00 99.99           C  
ANISOU 2258  CG  ASN A 296    15311  15281   7399   -539    492   2128       C  
ATOM   2259  OD1 ASN A 296      20.335  -3.906 -27.321  1.00100.12           O  
ANISOU 2259  OD1 ASN A 296    15049  15545   7448   -450    573   2316       O  
ATOM   2260  ND2 ASN A 296      21.654  -5.611 -26.696  1.00101.26           N  
ANISOU 2260  ND2 ASN A 296    15568  15448   7458   -360    445   1956       N  
ATOM   2261  N   MET A 297      19.588  -3.449 -22.106  1.00 95.12           N  
ANISOU 2261  N   MET A 297    15084  13522   7533  -1472    362   1947       N  
ATOM   2262  CA  MET A 297      18.783  -3.359 -20.891  1.00 94.74           C  
ANISOU 2262  CA  MET A 297    15182  13282   7533  -1875    358   1717       C  
ATOM   2263  C   MET A 297      18.120  -1.992 -20.766  1.00 96.44           C  
ANISOU 2263  C   MET A 297    14983  13591   8068  -1923    442   1752       C  
ATOM   2264  O   MET A 297      16.909  -1.895 -20.526  1.00 98.92           O  
ANISOU 2264  O   MET A 297    15232  13996   8357  -2168    484   1466       O  
ATOM   2265  CB  MET A 297      19.654  -3.652 -19.670  1.00 93.43           C  
ANISOU 2265  CB  MET A 297    15272  12749   7477  -2001    246   1699       C  
ATOM   2266  CG  MET A 297      18.911  -3.589 -18.352  1.00 93.40           C  
ANISOU 2266  CG  MET A 297    15405  12592   7489  -2459    253   1443       C  
ATOM   2267  SD  MET A 297      17.610  -4.819 -18.216  1.00 94.28           S  
ANISOU 2267  SD  MET A 297    15739  12708   7374  -2789    241   1036       S  
ATOM   2268  CE  MET A 297      18.571  -6.298 -17.953  1.00 93.57           C  
ANISOU 2268  CE  MET A 297    16100  12242   7210  -2726    -24   1056       C  
ATOM   2269  N   TYR A 298      18.903  -0.920 -20.918  1.00 93.52           N  
ANISOU 2269  N   TYR A 298    14307  13187   8038  -1698    446   2067       N  
ATOM   2270  CA  TYR A 298      18.330   0.424 -20.935  1.00 98.16           C  
ANISOU 2270  CA  TYR A 298    14481  13808   9009  -1687    452   2127       C  
ATOM   2271  C   TYR A 298      17.282   0.566 -22.032  1.00102.76           C  
ANISOU 2271  C   TYR A 298    14872  14667   9504  -1584    430   2104       C  
ATOM   2272  O   TYR A 298      16.174   1.062 -21.787  1.00109.65           O  
ANISOU 2272  O   TYR A 298    15544  15566  10551  -1721    399   1843       O  
ATOM   2273  CB  TYR A 298      19.434   1.466 -21.121  1.00 96.08           C  
ANISOU 2273  CB  TYR A 298    13950  13447   9108  -1454    433   2538       C  
ATOM   2274  CG  TYR A 298      18.920   2.886 -21.260  1.00100.81           C  
ANISOU 2274  CG  TYR A 298    14126  14013  10166  -1405    364   2656       C  
ATOM   2275  CD1 TYR A 298      18.509   3.613 -20.150  1.00105.33           C  
ANISOU 2275  CD1 TYR A 298    14528  14379  11114  -1594    330   2395       C  
ATOM   2276  CD2 TYR A 298      18.837   3.494 -22.508  1.00101.13           C  
ANISOU 2276  CD2 TYR A 298    13938  14222  10264  -1181    298   3014       C  
ATOM   2277  CE1 TYR A 298      18.038   4.911 -20.279  1.00111.07           C  
ANISOU 2277  CE1 TYR A 298    14841  15019  12341  -1515    204   2451       C  
ATOM   2278  CE2 TYR A 298      18.364   4.789 -22.647  1.00105.72           C  
ANISOU 2278  CE2 TYR A 298    14162  14692  11313  -1128    144   3149       C  
ATOM   2279  CZ  TYR A 298      17.968   5.493 -21.530  1.00110.85           C  
ANISOU 2279  CZ  TYR A 298    14622  15086  12411  -1273     83   2848       C  
ATOM   2280  OH  TYR A 298      17.500   6.781 -21.665  1.00115.64           O  
ANISOU 2280  OH  TYR A 298    14848  15529  13561  -1188   -128   2932       O  
ATOM   2281  N   VAL A 299      17.622   0.142 -23.255  1.00 94.48           N  
ANISOU 2281  N   VAL A 299    13858  13851   8187  -1339    432   2337       N  
ATOM   2282  CA  VAL A 299      16.717   0.311 -24.392  1.00 97.84           C  
ANISOU 2282  CA  VAL A 299    14112  14566   8497  -1217    374   2368       C  
ATOM   2283  C   VAL A 299      15.348  -0.283 -24.085  1.00102.51           C  
ANISOU 2283  C   VAL A 299    14786  15217   8946  -1448    369   1875       C  
ATOM   2284  O   VAL A 299      14.309   0.346 -24.320  1.00108.76           O  
ANISOU 2284  O   VAL A 299    15311  16093   9921  -1452    278   1741       O  
ATOM   2285  CB  VAL A 299      17.324  -0.311 -25.662  1.00 94.71           C  
ANISOU 2285  CB  VAL A 299    13798  14475   7713   -981    409   2600       C  
ATOM   2286  CG1 VAL A 299      16.319  -0.277 -26.803  1.00 97.51           C  
ANISOU 2286  CG1 VAL A 299    14028  15156   7867   -885    326   2593       C  
ATOM   2287  CG2 VAL A 299      18.594   0.422 -26.056  1.00 92.86           C  
ANISOU 2287  CG2 VAL A 299    13402  14261   7622   -803    443   3075       C  
ATOM   2288  N   LEU A 300      15.326  -1.501 -23.542  1.00100.10           N  
ANISOU 2288  N   LEU A 300    14846  14852   8336  -1659    442   1583       N  
ATOM   2289  CA  LEU A 300      14.047  -2.165 -23.312  1.00101.84           C  
ANISOU 2289  CA  LEU A 300    15163  15160   8371  -1937    466   1117       C  
ATOM   2290  C   LEU A 300      13.335  -1.625 -22.077  1.00103.81           C  
ANISOU 2290  C   LEU A 300    15289  15277   8878  -2288    512    777       C  
ATOM   2291  O   LEU A 300      12.125  -1.383 -22.118  1.00107.58           O  
ANISOU 2291  O   LEU A 300    15535  15904   9436  -2416    509    425       O  
ATOM   2292  CB  LEU A 300      14.250  -3.674 -23.201  1.00 99.40           C  
ANISOU 2292  CB  LEU A 300    15313  14801   7651  -2082    491    949       C  
ATOM   2293  CG  LEU A 300      14.681  -4.347 -24.506  1.00 99.04           C  
ANISOU 2293  CG  LEU A 300    15326  14967   7339  -1747    450   1098       C  
ATOM   2294  CD1 LEU A 300      15.003  -5.811 -24.270  1.00 97.52           C  
ANISOU 2294  CD1 LEU A 300    15440  14536   7075  -1755    399    873       C  
ATOM   2295  CD2 LEU A 300      13.603  -4.192 -25.571  1.00101.98           C  
ANISOU 2295  CD2 LEU A 300    15463  15689   7597  -1642    422    987       C  
ATOM   2296  N   LEU A 301      14.058  -1.427 -20.972  1.00 98.17           N  
ANISOU 2296  N   LEU A 301    14693  14313   8293  -2451    551    826       N  
ATOM   2297  CA  LEU A 301      13.410  -0.925 -19.765  1.00 98.56           C  
ANISOU 2297  CA  LEU A 301    14607  14301   8540  -2822    618    450       C  
ATOM   2298  C   LEU A 301      12.868   0.488 -19.932  1.00 99.56           C  
ANISOU 2298  C   LEU A 301    14178  14474   9177  -2655    545    385       C  
ATOM   2299  O   LEU A 301      11.984   0.891 -19.168  1.00100.73           O  
ANISOU 2299  O   LEU A 301    14093  14675   9506  -2936    596    -87       O  
ATOM   2300  CB  LEU A 301      14.374  -0.954 -18.580  1.00 97.52           C  
ANISOU 2300  CB  LEU A 301    14715  13911   8425  -3011    643    542       C  
ATOM   2301  CG  LEU A 301      14.794  -2.306 -18.012  1.00 97.34           C  
ANISOU 2301  CG  LEU A 301    15280  13748   7957  -3292    640    522       C  
ATOM   2302  CD1 LEU A 301      15.842  -2.103 -16.935  1.00 96.65           C  
ANISOU 2302  CD1 LEU A 301    15367  13394   7961  -3390    592    673       C  
ATOM   2303  CD2 LEU A 301      13.590  -3.039 -17.452  1.00 98.91           C  
ANISOU 2303  CD2 LEU A 301    15665  14077   7839  -3825    743     57       C  
ATOM   2304  N   ARG A 302      13.374   1.250 -20.908  1.00107.34           N  
ANISOU 2304  N   ARG A 302    14937  15441  10405  -2228    408    826       N  
ATOM   2305  CA  ARG A 302      12.975   2.651 -21.024  1.00114.43           C  
ANISOU 2305  CA  ARG A 302    15342  16275  11862  -2060    251    830       C  
ATOM   2306  C   ARG A 302      11.541   2.791 -21.525  1.00119.62           C  
ANISOU 2306  C   ARG A 302    15718  17130  12603  -2057    146    440       C  
ATOM   2307  O   ARG A 302      10.798   3.661 -21.055  1.00119.37           O  
ANISOU 2307  O   ARG A 302    15285  17046  13025  -2111     49     70       O  
ATOM   2308  CB  ARG A 302      13.936   3.399 -21.945  1.00114.33           C  
ANISOU 2308  CB  ARG A 302    15222  16171  12045  -1672    110   1476       C  
ATOM   2309  CG  ARG A 302      13.666   4.891 -22.019  1.00121.25           C  
ANISOU 2309  CG  ARG A 302    15638  16872  13560  -1507   -122   1564       C  
ATOM   2310  CD  ARG A 302      14.658   5.589 -22.928  1.00116.90           C  
ANISOU 2310  CD  ARG A 302    15038  16234  13146  -1214   -252   2266       C  
ATOM   2311  NE  ARG A 302      14.492   5.193 -24.322  1.00113.60           N  
ANISOU 2311  NE  ARG A 302    14722  16089  12350  -1031   -324   2574       N  
ATOM   2312  CZ  ARG A 302      15.339   5.517 -25.293  1.00107.70           C  
ANISOU 2312  CZ  ARG A 302    14006  15409  11506   -847   -377   3187       C  
ATOM   2313  NH1 ARG A 302      16.416   6.243 -25.019  1.00104.54           N  
ANISOU 2313  NH1 ARG A 302    13534  14792  11396   -820   -363   3561       N  
ATOM   2314  NH2 ARG A 302      15.112   5.115 -26.537  1.00105.38           N  
ANISOU 2314  NH2 ARG A 302    13803  15433  10803   -722   -431   3406       N  
ATOM   2315  N   ALA A 303      11.128   1.944 -22.467  1.00112.75           N  
ANISOU 2315  N   ALA A 303    15019  16491  11330  -1985    145    458       N  
ATOM   2316  CA  ALA A 303       9.784   2.005 -23.030  1.00116.12           C  
ANISOU 2316  CA  ALA A 303    15181  17123  11815  -1956     19     82       C  
ATOM   2317  C   ALA A 303       8.743   1.329 -22.146  1.00112.80           C  
ANISOU 2317  C   ALA A 303    14770  16841  11249  -2404    205   -640       C  
ATOM   2318  O   ALA A 303       7.654   0.990 -22.625  1.00113.23           O  
ANISOU 2318  O   ALA A 303    14691  17118  11212  -2440    162  -1014       O  
ATOM   2319  CB  ALA A 303       9.769   1.382 -24.428  1.00115.36           C  
ANISOU 2319  CB  ALA A 303    15250  17255  11328  -1704    -63    375       C  
ATOM   2320  N   VAL A 304       9.064   1.135 -20.872  1.00123.83           N  
ANISOU 2320  N   VAL A 304    16319  18130  12599  -2774    407   -841       N  
ATOM   2321  CA  VAL A 304       8.208   0.452 -19.913  1.00119.14           C  
ANISOU 2321  CA  VAL A 304    15798  17693  11775  -3318    628  -1476       C  
ATOM   2322  C   VAL A 304       7.651   1.479 -18.940  1.00117.30           C  
ANISOU 2322  C   VAL A 304    15089  17466  12012  -3505    647  -1985       C  
ATOM   2323  O   VAL A 304       8.256   2.532 -18.710  1.00118.39           O  
ANISOU 2323  O   VAL A 304    14995  17391  12598  -3275    522  -1773       O  
ATOM   2324  CB  VAL A 304       9.008  -0.650 -19.182  1.00115.37           C  
ANISOU 2324  CB  VAL A 304    15921  17110  10805  -3662    814  -1308       C  
ATOM   2325  CG1 VAL A 304       8.203  -1.286 -18.055  1.00110.96           C  
ANISOU 2325  CG1 VAL A 304    15489  16703   9967  -4334   1043  -1897       C  
ATOM   2326  CG2 VAL A 304       9.467  -1.703 -20.174  1.00114.85           C  
ANISOU 2326  CG2 VAL A 304    16260  17042  10335  -3456    764   -933       C  
ATOM   2327  N   SER A 305       6.472   1.181 -18.389  1.00125.24           N  
ANISOU 2327  N   SER A 305    15911  18737  12937  -3934    805  -2708       N  
ATOM   2328  CA  SER A 305       5.911   2.003 -17.323  1.00121.42           C  
ANISOU 2328  CA  SER A 305    14964  18341  12827  -4209    885  -3339       C  
ATOM   2329  C   SER A 305       6.925   2.212 -16.202  1.00118.90           C  
ANISOU 2329  C   SER A 305    14860  17847  12468  -4422   1007  -3149       C  
ATOM   2330  O   SER A 305       7.283   3.348 -15.873  1.00119.33           O  
ANISOU 2330  O   SER A 305    14556  17733  13049  -4205    879  -3146       O  
ATOM   2331  CB  SER A 305       4.636   1.355 -16.781  1.00117.69           C  
ANISOU 2331  CB  SER A 305    14375  18256  12086  -4790   1138  -4145       C  
ATOM   2332  OG  SER A 305       4.933   0.141 -16.114  1.00114.72           O  
ANISOU 2332  OG  SER A 305    14610  17943  11036  -5348   1412  -4060       O  
ATOM   2333  N   THR A 306       7.401   1.117 -15.600  1.00117.07           N  
ANISOU 2333  N   THR A 306    15224  17626  11630  -4850   1215  -2990       N  
ATOM   2334  CA  THR A 306       8.414   1.168 -14.541  1.00114.41           C  
ANISOU 2334  CA  THR A 306    15176  17119  11176  -5067   1291  -2771       C  
ATOM   2335  C   THR A 306       9.522   0.173 -14.886  1.00115.99           C  
ANISOU 2335  C   THR A 306    16052  17074  10945  -4956   1233  -2081       C  
ATOM   2336  O   THR A 306       9.513  -0.966 -14.415  1.00112.77           O  
ANISOU 2336  O   THR A 306    16160  16699   9988  -5412   1349  -2098       O  
ATOM   2337  CB  THR A 306       7.796   0.867 -13.171  1.00110.16           C  
ANISOU 2337  CB  THR A 306    14669  16863  10322  -5828   1571  -3402       C  
ATOM   2338  OG1 THR A 306       7.232  -0.450 -13.181  1.00109.04           O  
ANISOU 2338  OG1 THR A 306    14831  16768   9830  -6059   1747  -3255       O  
ATOM   2339  CG2 THR A 306       6.709   1.876 -12.834  1.00109.41           C  
ANISOU 2339  CG2 THR A 306    13795  17013  10761  -5811   1646  -4099       C  
ATOM   2340  N   GLY A 307      10.475   0.606 -15.710  1.00108.01           N  
ANISOU 2340  N   GLY A 307    15026  15815  10197  -4369   1036  -1495       N  
ATOM   2341  CA  GLY A 307      11.608  -0.239 -16.039  1.00105.85           C  
ANISOU 2341  CA  GLY A 307    15294  15325   9598  -4213    967   -920       C  
ATOM   2342  C   GLY A 307      12.939   0.243 -15.498  1.00104.29           C  
ANISOU 2342  C   GLY A 307    15193  14852   9582  -4055    891   -536       C  
ATOM   2343  O   GLY A 307      13.761  -0.558 -15.042  1.00103.50           O  
ANISOU 2343  O   GLY A 307    15587  14582   9154  -4194    868   -303       O  
ATOM   2344  N   LEU A 308      13.152   1.556 -15.531  1.00 98.89           N  
ANISOU 2344  N   LEU A 308    14029  14092   9452  -3764    815   -487       N  
ATOM   2345  CA  LEU A 308      14.431   2.193 -15.218  1.00 97.09           C  
ANISOU 2345  CA  LEU A 308    13788  13599   9503  -3532    726   -102       C  
ATOM   2346  C   LEU A 308      14.808   2.307 -13.737  1.00 94.58           C  
ANISOU 2346  C   LEU A 308    13587  13208   9142  -3917    793   -322       C  
ATOM   2347  O   LEU A 308      16.004   2.220 -13.427  1.00 92.61           O  
ANISOU 2347  O   LEU A 308    13578  12733   8875  -3808    717     32       O  
ATOM   2348  CB  LEU A 308      14.462   3.584 -15.856  1.00 99.59           C  
ANISOU 2348  CB  LEU A 308    13549  13829  10462  -3105    585     49       C  
ATOM   2349  CG  LEU A 308      14.524   3.554 -17.386  1.00101.83           C  
ANISOU 2349  CG  LEU A 308    13793  14145  10753  -2677    467    478       C  
ATOM   2350  CD1 LEU A 308      14.362   4.940 -17.970  1.00105.79           C  
ANISOU 2350  CD1 LEU A 308    13779  14543  11874  -2344    271    620       C  
ATOM   2351  CD2 LEU A 308      15.834   2.940 -17.846  1.00 97.79           C  
ANISOU 2351  CD2 LEU A 308    13651  13527   9979  -2471    464   1019       C  
ATOM   2352  N   PRO A 309      13.869   2.519 -12.797  1.00102.66           N  
ANISOU 2352  N   PRO A 309    14425  14442  10141  -4370    929   -921       N  
ATOM   2353  CA  PRO A 309      14.303   2.867 -11.427  1.00 99.23           C  
ANISOU 2353  CA  PRO A 309    14014  13974   9715  -4698    978  -1124       C  
ATOM   2354  C   PRO A 309      15.226   1.847 -10.775  1.00 96.63           C  
ANISOU 2354  C   PRO A 309    14355  13493   8866  -4945    940   -820       C  
ATOM   2355  O   PRO A 309      16.221   2.241 -10.152  1.00 95.46           O  
ANISOU 2355  O   PRO A 309    14253  13152   8864  -4872    848   -639       O  
ATOM   2356  CB  PRO A 309      12.977   3.003 -10.664  1.00 97.62           C  
ANISOU 2356  CB  PRO A 309    13533  14138   9422  -5224   1177  -1888       C  
ATOM   2357  CG  PRO A 309      12.006   2.205 -11.437  1.00 99.11           C  
ANISOU 2357  CG  PRO A 309    13821  14519   9317  -5314   1250  -2012       C  
ATOM   2358  CD  PRO A 309      12.402   2.378 -12.865  1.00103.00           C  
ANISOU 2358  CD  PRO A 309    14234  14806  10093  -4658   1061  -1493       C  
ATOM   2359  N   HIS A 310      14.931   0.550 -10.891  1.00103.30           N  
ANISOU 2359  N   HIS A 310    15720  14387   9142  -5232    966   -768       N  
ATOM   2360  CA  HIS A 310      15.804  -0.456 -10.292  1.00100.90           C  
ANISOU 2360  CA  HIS A 310    16087  13863   8387  -5450    834   -465       C  
ATOM   2361  C   HIS A 310      17.197  -0.405 -10.909  1.00100.13           C  
ANISOU 2361  C   HIS A 310    16079  13425   8542  -4856    615     88       C  
ATOM   2362  O   HIS A 310      18.207  -0.434 -10.197  1.00 98.24           O  
ANISOU 2362  O   HIS A 310    16074  12966   8286  -4866    467    277       O  
ATOM   2363  CB  HIS A 310      15.188  -1.847 -10.451  1.00101.24           C  
ANISOU 2363  CB  HIS A 310    16465  13840   8163  -5676    797   -490       C  
ATOM   2364  CG  HIS A 310      15.908  -2.926  -9.699  1.00 98.52           C  
ANISOU 2364  CG  HIS A 310    16592  13105   7736  -5812    553   -261       C  
ATOM   2365  ND1 HIS A 310      16.966  -3.632 -10.234  1.00 96.64           N  
ANISOU 2365  ND1 HIS A 310    16658  12518   7541  -5384    275    116       N  
ATOM   2366  CD2 HIS A 310      15.717  -3.423  -8.454  1.00 97.90           C  
ANISOU 2366  CD2 HIS A 310    16721  12946   7532  -6348    543   -364       C  
ATOM   2367  CE1 HIS A 310      17.398  -4.512  -9.349  1.00 95.07           C  
ANISOU 2367  CE1 HIS A 310    16862  12017   7241  -5642     62    193       C  
ATOM   2368  NE2 HIS A 310      16.656  -4.408  -8.261  1.00 95.70           N  
ANISOU 2368  NE2 HIS A 310    16918  12242   7202  -6243    214    -55       N  
ATOM   2369  N   MET A 311      17.265  -0.314 -12.238  1.00 88.79           N  
ANISOU 2369  N   MET A 311    14432  11974   7328  -4353    592    326       N  
ATOM   2370  CA  MET A 311      18.554  -0.256 -12.919  1.00 86.93           C  
ANISOU 2370  CA  MET A 311    14218  11503   7310  -3823    434    799       C  
ATOM   2371  C   MET A 311      19.366   0.946 -12.452  1.00 86.84           C  
ANISOU 2371  C   MET A 311    13851  11365   7781  -3625    400    896       C  
ATOM   2372  O   MET A 311      20.553   0.821 -12.122  1.00 85.42           O  
ANISOU 2372  O   MET A 311    13856  10955   7646  -3483    256   1140       O  
ATOM   2373  CB  MET A 311      18.334  -0.209 -14.430  1.00 87.38           C  
ANISOU 2373  CB  MET A 311    14038  11675   7487  -3394    462    985       C  
ATOM   2374  CG  MET A 311      19.599  -0.253 -15.258  1.00 85.63           C  
ANISOU 2374  CG  MET A 311    13818  11312   7406  -2903    351   1423       C  
ATOM   2375  SD  MET A 311      19.210  -0.272 -17.015  1.00 86.52           S  
ANISOU 2375  SD  MET A 311    13690  11665   7516  -2510    404   1607       S  
ATOM   2376  CE  MET A 311      20.847  -0.220 -17.732  1.00 84.90           C  
ANISOU 2376  CE  MET A 311    13442  11359   7457  -2044    327   2050       C  
ATOM   2377  N   ILE A 312      18.732   2.121 -12.406  1.00 94.19           N  
ANISOU 2377  N   ILE A 312    14249  12422   9118  -3608    502    672       N  
ATOM   2378  CA  ILE A 312      19.413   3.331 -11.946  1.00 94.99           C  
ANISOU 2378  CA  ILE A 312    13972  12380   9739  -3441    455    718       C  
ATOM   2379  C   ILE A 312      19.922   3.142 -10.523  1.00 91.84           C  
ANISOU 2379  C   ILE A 312    13843  11896   9156  -3792    411    557       C  
ATOM   2380  O   ILE A 312      21.077   3.463 -10.206  1.00 90.70           O  
ANISOU 2380  O   ILE A 312    13701  11534   9226  -3601    290    784       O  
ATOM   2381  CB  ILE A 312      18.469   4.543 -12.050  1.00100.22           C  
ANISOU 2381  CB  ILE A 312    14030  13162  10887  -3410    516    403       C  
ATOM   2382  CG1 ILE A 312      18.069   4.786 -13.506  1.00105.42           C  
ANISOU 2382  CG1 ILE A 312    14453  13867  11735  -3034    481    648       C  
ATOM   2383  CG2 ILE A 312      19.119   5.781 -11.457  1.00100.97           C  
ANISOU 2383  CG2 ILE A 312    13737  13075  11553  -3283    443    388       C  
ATOM   2384  CD1 ILE A 312      16.939   5.772 -13.668  1.00111.71           C  
ANISOU 2384  CD1 ILE A 312    14714  14762  12970  -3015    463    287       C  
ATOM   2385  N   GLN A 313      19.062   2.618  -9.645  1.00 89.31           N  
ANISOU 2385  N   GLN A 313    13751  11771   8410  -4342    507    154       N  
ATOM   2386  CA  GLN A 313      19.459   2.327  -8.271  1.00 87.35           C  
ANISOU 2386  CA  GLN A 313    13842  11494   7855  -4769    450     15       C  
ATOM   2387  C   GLN A 313      20.711   1.461  -8.235  1.00 85.62           C  
ANISOU 2387  C   GLN A 313    14157  10961   7412  -4612    201    460       C  
ATOM   2388  O   GLN A 313      21.660   1.738  -7.489  1.00 85.08           O  
ANISOU 2388  O   GLN A 313    14153  10721   7452  -4583     51    544       O  
ATOM   2389  CB  GLN A 313      18.304   1.635  -7.544  1.00 86.78           C  
ANISOU 2389  CB  GLN A 313    14040  11722   7212  -5453    603   -407       C  
ATOM   2390  CG  GLN A 313      18.545   1.349  -6.072  1.00 86.35           C  
ANISOU 2390  CG  GLN A 313    14357  11718   6732  -6020    559   -574       C  
ATOM   2391  CD  GLN A 313      18.652   2.606  -5.236  1.00 86.63           C  
ANISOU 2391  CD  GLN A 313    13884  11877   7154  -6065    630   -931       C  
ATOM   2392  OE1 GLN A 313      19.741   2.996  -4.819  1.00 86.58           O  
ANISOU 2392  OE1 GLN A 313    13890  11643   7364  -5852    454   -728       O  
ATOM   2393  NE2 GLN A 313      17.516   3.247  -4.982  1.00 87.07           N  
ANISOU 2393  NE2 GLN A 313    13456  12297   7330  -6335    875  -1521       N  
ATOM   2394  N   GLU A 314      20.739   0.416  -9.066  1.00 93.73           N  
ANISOU 2394  N   GLU A 314    15539  11903   8169  -4479    125    708       N  
ATOM   2395  CA  GLU A 314      21.876  -0.494  -9.060  1.00 92.28           C  
ANISOU 2395  CA  GLU A 314    15845  11404   7812  -4310   -161   1049       C  
ATOM   2396  C   GLU A 314      23.139   0.162  -9.599  1.00 92.49           C  
ANISOU 2396  C   GLU A 314    15549  11241   8351  -3720   -258   1339       C  
ATOM   2397  O   GLU A 314      24.238  -0.156  -9.133  1.00 92.19           O  
ANISOU 2397  O   GLU A 314    15763  10947   8317  -3614   -508   1494       O  
ATOM   2398  CB  GLU A 314      21.549  -1.760  -9.848  1.00 91.78           C  
ANISOU 2398  CB  GLU A 314    16114  11289   7470  -4250   -238   1125       C  
ATOM   2399  CG  GLU A 314      20.542  -2.648  -9.147  1.00 91.50           C  
ANISOU 2399  CG  GLU A 314    16320  11293   7153  -4757   -242    800       C  
ATOM   2400  CD  GLU A 314      21.062  -3.164  -7.815  1.00 90.64           C  
ANISOU 2400  CD  GLU A 314    16594  10944   6902  -5090   -494    776       C  
ATOM   2401  OE1 GLU A 314      22.290  -3.360  -7.687  1.00 90.34           O  
ANISOU 2401  OE1 GLU A 314    16752  10615   6957  -4801   -779   1014       O  
ATOM   2402  OE2 GLU A 314      20.243  -3.368  -6.893  1.00 91.49           O  
ANISOU 2402  OE2 GLU A 314    16790  11156   6817  -5659   -405    526       O  
ATOM   2403  N   LEU A 315      23.019   1.075 -10.566  1.00 85.13           N  
ANISOU 2403  N   LEU A 315    14068  10426   7850  -3354    -88   1416       N  
ATOM   2404  CA  LEU A 315      24.212   1.798 -10.995  1.00 85.14           C  
ANISOU 2404  CA  LEU A 315    13741  10280   8328  -2892   -146   1688       C  
ATOM   2405  C   LEU A 315      24.726   2.702  -9.882  1.00 86.01           C  
ANISOU 2405  C   LEU A 315    13654  10283   8741  -2994   -198   1567       C  
ATOM   2406  O   LEU A 315      25.942   2.811  -9.674  1.00 86.28           O  
ANISOU 2406  O   LEU A 315    13688  10115   8981  -2769   -355   1732       O  
ATOM   2407  CB  LEU A 315      23.936   2.604 -12.265  1.00 85.43           C  
ANISOU 2407  CB  LEU A 315    13280  10461   8718  -2557     20   1852       C  
ATOM   2408  CG  LEU A 315      25.187   3.295 -12.823  1.00 85.69           C  
ANISOU 2408  CG  LEU A 315    12991  10376   9190  -2143    -12   2177       C  
ATOM   2409  CD1 LEU A 315      26.252   2.272 -13.178  1.00 85.35           C  
ANISOU 2409  CD1 LEU A 315    13254  10233   8940  -1921   -150   2345       C  
ATOM   2410  CD2 LEU A 315      24.867   4.153 -14.032  1.00 86.24           C  
ANISOU 2410  CD2 LEU A 315    12614  10587   9565  -1901    123   2397       C  
ATOM   2411  N   GLN A 316      23.816   3.346  -9.145  1.00 84.19           N  
ANISOU 2411  N   GLN A 316    13226  10208   8554  -3333    -73   1223       N  
ATOM   2412  CA  GLN A 316      24.233   4.138  -7.992  1.00 84.76           C  
ANISOU 2412  CA  GLN A 316    13124  10217   8864  -3478   -126   1025       C  
ATOM   2413  C   GLN A 316      24.999   3.284  -6.989  1.00 83.91           C  
ANISOU 2413  C   GLN A 316    13567   9956   8360  -3692   -364   1057       C  
ATOM   2414  O   GLN A 316      26.071   3.676  -6.512  1.00 84.63           O  
ANISOU 2414  O   GLN A 316    13584   9860   8714  -3525   -524   1139       O  
ATOM   2415  CB  GLN A 316      23.021   4.792  -7.323  1.00 85.60           C  
ANISOU 2415  CB  GLN A 316    12946  10580   8999  -3864     51    534       C  
ATOM   2416  CG  GLN A 316      23.377   5.614  -6.085  1.00 86.00           C  
ANISOU 2416  CG  GLN A 316    12783  10621   9273  -4046      9    239       C  
ATOM   2417  CD  GLN A 316      22.171   6.265  -5.435  1.00 86.44           C  
ANISOU 2417  CD  GLN A 316    12483  10980   9379  -4425    195   -355       C  
ATOM   2418  OE1 GLN A 316      21.047   6.147  -5.923  1.00 86.82           O  
ANISOU 2418  OE1 GLN A 316    12414  11235   9337  -4537    351   -555       O  
ATOM   2419  NE2 GLN A 316      22.396   6.932  -4.309  1.00 86.44           N  
ANISOU 2419  NE2 GLN A 316    12288  11035   9521  -4630    173   -698       N  
ATOM   2420  N   ASN A 317      24.467   2.105  -6.661  1.00 85.66           N  
ANISOU 2420  N   ASN A 317    14359  10230   7959  -4072   -426   1004       N  
ATOM   2421  CA  ASN A 317      25.135   1.262  -5.674  1.00 85.58           C  
ANISOU 2421  CA  ASN A 317    14941  10029   7547  -4320   -732   1072       C  
ATOM   2422  C   ASN A 317      26.477   0.752  -6.194  1.00 85.73           C  
ANISOU 2422  C   ASN A 317    15126   9705   7745  -3827  -1029   1420       C  
ATOM   2423  O   ASN A 317      27.463   0.701  -5.445  1.00 86.95           O  
ANISOU 2423  O   ASN A 317    15454   9642   7942  -3785  -1314   1473       O  
ATOM   2424  CB  ASN A 317      24.221   0.104  -5.278  1.00 85.64           C  
ANISOU 2424  CB  ASN A 317    15549  10137   6854  -4884   -757    983       C  
ATOM   2425  CG  ASN A 317      22.946   0.577  -4.600  1.00 86.34           C  
ANISOU 2425  CG  ASN A 317    15457  10626   6723  -5452   -453    544       C  
ATOM   2426  OD1 ASN A 317      21.844   0.384  -5.115  1.00 85.86           O  
ANISOU 2426  OD1 ASN A 317    15311  10794   6517  -5621   -219    381       O  
ATOM   2427  ND2 ASN A 317      23.093   1.210  -3.441  1.00 87.69           N  
ANISOU 2427  ND2 ASN A 317    15527  10911   6878  -5747   -456    297       N  
ATOM   2428  N   HIS A 318      26.532   0.373  -7.474  1.00 81.61           N  
ANISOU 2428  N   HIS A 318    14522   9157   7328  -3450   -973   1614       N  
ATOM   2429  CA  HIS A 318      27.792  -0.019  -8.100  1.00 81.98           C  
ANISOU 2429  CA  HIS A 318    14590   8958   7602  -2951  -1197   1852       C  
ATOM   2430  C   HIS A 318      28.847   1.069  -7.948  1.00 83.17           C  
ANISOU 2430  C   HIS A 318    14261   9033   8306  -2638  -1202   1894       C  
ATOM   2431  O   HIS A 318      29.963   0.813  -7.479  1.00 84.71           O  
ANISOU 2431  O   HIS A 318    14603   8984   8600  -2478  -1506   1938       O  
ATOM   2432  CB  HIS A 318      27.558  -0.331  -9.581  1.00 80.97           C  
ANISOU 2432  CB  HIS A 318    14295   8949   7523  -2624  -1033   1983       C  
ATOM   2433  CG  HIS A 318      28.796  -0.728 -10.327  1.00 82.59           C  
ANISOU 2433  CG  HIS A 318    14436   8996   7950  -2128  -1206   2141       C  
ATOM   2434  ND1 HIS A 318      28.859  -0.741 -11.704  1.00 83.61           N  
ANISOU 2434  ND1 HIS A 318    14271   9300   8198  -1782  -1023   2253       N  
ATOM   2435  CD2 HIS A 318      30.016  -1.124  -9.892  1.00 84.90           C  
ANISOU 2435  CD2 HIS A 318    14889   9005   8364  -1927  -1548   2156       C  
ATOM   2436  CE1 HIS A 318      30.064  -1.124 -12.085  1.00 86.87           C  
ANISOU 2436  CE1 HIS A 318    14636   9582   8790  -1409  -1205   2295       C  
ATOM   2437  NE2 HIS A 318      30.786  -1.363 -11.005  1.00 87.76           N  
ANISOU 2437  NE2 HIS A 318    15009   9396   8941  -1467  -1540   2226       N  
ATOM   2438  N   ILE A 319      28.507   2.296  -8.346  1.00 77.07           N  
ANISOU 2438  N   ILE A 319    12908   8443   7933  -2546   -900   1873       N  
ATOM   2439  CA  ILE A 319      29.488   3.374  -8.319  1.00 76.93           C  
ANISOU 2439  CA  ILE A 319    12406   8336   8488  -2261   -890   1940       C  
ATOM   2440  C   ILE A 319      29.880   3.716  -6.890  1.00 78.28           C  
ANISOU 2440  C   ILE A 319    12659   8389   8694  -2490  -1073   1739       C  
ATOM   2441  O   ILE A 319      31.039   4.057  -6.624  1.00 78.88           O  
ANISOU 2441  O   ILE A 319    12575   8291   9105  -2257  -1234   1784       O  
ATOM   2442  CB  ILE A 319      28.940   4.593  -9.073  1.00 75.88           C  
ANISOU 2442  CB  ILE A 319    11682   8367   8782  -2152   -588   1994       C  
ATOM   2443  CG1 ILE A 319      28.669   4.211 -10.526  1.00 75.03           C  
ANISOU 2443  CG1 ILE A 319    11525   8398   8586  -1920   -445   2229       C  
ATOM   2444  CG2 ILE A 319      29.930   5.723  -9.010  1.00 76.21           C  
ANISOU 2444  CG2 ILE A 319    11242   8282   9433  -1918   -590   2080       C  
ATOM   2445  CD1 ILE A 319      27.877   5.226 -11.292  1.00 74.56           C  
ANISOU 2445  CD1 ILE A 319    11012   8492   8826  -1876   -218   2306       C  
ATOM   2446  N   HIS A 320      28.939   3.625  -5.948  1.00 74.21           N  
ANISOU 2446  N   HIS A 320    12378   8004   7816  -2971  -1048   1485       N  
ATOM   2447  CA  HIS A 320      29.294   3.754  -4.538  1.00 76.14           C  
ANISOU 2447  CA  HIS A 320    12803   8187   7940  -3257  -1251   1284       C  
ATOM   2448  C   HIS A 320      30.346   2.728  -4.142  1.00 77.65           C  
ANISOU 2448  C   HIS A 320    13521   8091   7893  -3165  -1679   1443       C  
ATOM   2449  O   HIS A 320      31.329   3.057  -3.466  1.00 78.82           O  
ANISOU 2449  O   HIS A 320    13606   8078   8264  -3052  -1911   1407       O  
ATOM   2450  CB  HIS A 320      28.052   3.601  -3.661  1.00 77.56           C  
ANISOU 2450  CB  HIS A 320    13220   8631   7619  -3872  -1134    975       C  
ATOM   2451  CG  HIS A 320      28.336   3.716  -2.196  1.00 80.15           C  
ANISOU 2451  CG  HIS A 320    13756   8979   7717  -4244  -1324    753       C  
ATOM   2452  ND1 HIS A 320      28.748   2.644  -1.433  1.00 82.48           N  
ANISOU 2452  ND1 HIS A 320    14751   9123   7464  -4505  -1690    868       N  
ATOM   2453  CD2 HIS A 320      28.271   4.773  -1.352  1.00 81.23           C  
ANISOU 2453  CD2 HIS A 320    13503   9271   8090  -4408  -1230    415       C  
ATOM   2454  CE1 HIS A 320      28.924   3.035  -0.184  1.00 84.89           C  
ANISOU 2454  CE1 HIS A 320    15107   9523   7623  -4835  -1803    637       C  
ATOM   2455  NE2 HIS A 320      28.640   4.322  -0.107  1.00 84.10           N  
ANISOU 2455  NE2 HIS A 320    14331   9628   7994  -4779  -1508    329       N  
ATOM   2456  N   ASP A 321      30.156   1.473  -4.561  1.00 87.83           N  
ANISOU 2456  N   ASP A 321    15319   9286   8767  -3195  -1830   1596       N  
ATOM   2457  CA  ASP A 321      31.071   0.405  -4.168  1.00 89.38           C  
ANISOU 2457  CA  ASP A 321    16059   9146   8755  -3112  -2327   1720       C  
ATOM   2458  C   ASP A 321      32.456   0.601  -4.777  1.00 90.55           C  
ANISOU 2458  C   ASP A 321    15865   9087   9455  -2499  -2479   1817       C  
ATOM   2459  O   ASP A 321      33.457   0.672  -4.057  1.00 92.86           O  
ANISOU 2459  O   ASP A 321    16207   9167   9908  -2387  -2814   1776       O  
ATOM   2460  CB  ASP A 321      30.492  -0.955  -4.564  1.00 88.31           C  
ANISOU 2460  CB  ASP A 321    16507   8922   8126  -3270  -2467   1835       C  
ATOM   2461  CG  ASP A 321      29.349  -1.382  -3.668  1.00 88.16           C  
ANISOU 2461  CG  ASP A 321    16981   9050   7466  -3979  -2442   1740       C  
ATOM   2462  OD1 ASP A 321      29.376  -1.039  -2.467  1.00 89.86           O  
ANISOU 2462  OD1 ASP A 321    17333   9321   7490  -4356  -2542   1620       O  
ATOM   2463  OD2 ASP A 321      28.419  -2.050  -4.167  1.00 86.73           O  
ANISOU 2463  OD2 ASP A 321    17032   8964   6957  -4188  -2307   1763       O  
ATOM   2464  N   GLU A 322      32.535   0.680  -6.109  1.00 91.72           N  
ANISOU 2464  N   GLU A 322    15650   9325   9875  -2120  -2237   1923       N  
ATOM   2465  CA  GLU A 322      33.838   0.819  -6.754  1.00 94.91           C  
ANISOU 2465  CA  GLU A 322    15696   9609  10758  -1592  -2331   1972       C  
ATOM   2466  C   GLU A 322      34.531   2.107  -6.327  1.00 97.25           C  
ANISOU 2466  C   GLU A 322    15462   9922  11566  -1487  -2235   1910       C  
ATOM   2467  O   GLU A 322      35.742   2.115  -6.073  1.00 99.55           O  
ANISOU 2467  O   GLU A 322    15644  10023  12157  -1215  -2502   1854       O  
ATOM   2468  CB  GLU A 322      33.685   0.762  -8.275  1.00 96.22           C  
ANISOU 2468  CB  GLU A 322    15543   9973  11043  -1298  -2020   2090       C  
ATOM   2469  CG  GLU A 322      35.003   0.879  -9.033  1.00102.21           C  
ANISOU 2469  CG  GLU A 322    15887  10704  12243   -809  -2051   2097       C  
ATOM   2470  CD  GLU A 322      34.842   0.718 -10.536  1.00105.36           C  
ANISOU 2470  CD  GLU A 322    16020  11366  12646   -579  -1749   2198       C  
ATOM   2471  OE1 GLU A 322      33.708   0.463 -10.994  1.00102.65           O  
ANISOU 2471  OE1 GLU A 322    15842  11185  11975   -761  -1559   2272       O  
ATOM   2472  OE2 GLU A 322      35.849   0.861 -11.262  1.00111.39           O  
ANISOU 2472  OE2 GLU A 322    16387  12211  13726   -236  -1691   2181       O  
ATOM   2473  N   GLY A 323      33.778   3.200  -6.228  1.00 89.24           N  
ANISOU 2473  N   GLY A 323    14097   9115  10696  -1693  -1887   1879       N  
ATOM   2474  CA  GLY A 323      34.333   4.467  -5.798  1.00 90.83           C  
ANISOU 2474  CA  GLY A 323    13788   9304  11419  -1626  -1806   1799       C  
ATOM   2475  C   GLY A 323      34.915   4.397  -4.403  1.00 92.00           C  
ANISOU 2475  C   GLY A 323    14181   9277  11498  -1774  -2171   1611       C  
ATOM   2476  O   GLY A 323      36.097   4.701  -4.200  1.00 94.60           O  
ANISOU 2476  O   GLY A 323    14277   9446  12219  -1506  -2356   1571       O  
ATOM   2477  N   LEU A 324      34.090   3.987  -3.434  1.00 78.59           N  
ANISOU 2477  N   LEU A 324    12951   7634   9274  -2232  -2278   1483       N  
ATOM   2478  CA  LEU A 324      34.570   3.836  -2.064  1.00 81.16           C  
ANISOU 2478  CA  LEU A 324    13599   7833   9407  -2447  -2657   1328       C  
ATOM   2479  C   LEU A 324      35.786   2.923  -2.025  1.00 83.11           C  
ANISOU 2479  C   LEU A 324    14162   7747   9669  -2129  -3156   1426       C  
ATOM   2480  O   LEU A 324      36.733   3.153  -1.260  1.00 85.07           O  
ANISOU 2480  O   LEU A 324    14370   7833  10119  -2026  -3474   1316       O  
ATOM   2481  CB  LEU A 324      33.446   3.289  -1.183  1.00 82.49           C  
ANISOU 2481  CB  LEU A 324    14322   8160   8862  -3058  -2690   1227       C  
ATOM   2482  CG  LEU A 324      33.586   3.346   0.340  1.00 85.59           C  
ANISOU 2482  CG  LEU A 324    15023   8571   8926  -3465  -2976   1032       C  
ATOM   2483  CD1 LEU A 324      32.205   3.378   0.974  1.00 86.43           C  
ANISOU 2483  CD1 LEU A 324    15327   9038   8476  -4118  -2721    829       C  
ATOM   2484  CD2 LEU A 324      34.397   2.186   0.894  1.00 88.62           C  
ANISOU 2484  CD2 LEU A 324    16091   8620   8962  -3457  -3594   1196       C  
ATOM   2485  N   ARG A 325      35.781   1.894  -2.874  1.00100.16           N  
ANISOU 2485  N   ARG A 325    16596   9799  11661  -1942  -3249   1587       N  
ATOM   2486  CA  ARG A 325      36.900   0.965  -2.949  1.00101.85           C  
ANISOU 2486  CA  ARG A 325    17067   9677  11957  -1588  -3756   1613       C  
ATOM   2487  C   ARG A 325      38.171   1.672  -3.399  1.00104.64           C  
ANISOU 2487  C   ARG A 325    16770   9985  13004  -1087  -3725   1523       C  
ATOM   2488  O   ARG A 325      39.259   1.407  -2.874  1.00106.29           O  
ANISOU 2488  O   ARG A 325    17047   9934  13405   -862  -4187   1408       O  
ATOM   2489  CB  ARG A 325      36.541  -0.178  -3.900  1.00100.76           C  
ANISOU 2489  CB  ARG A 325    17242   9473  11569  -1473  -3798   1737       C  
ATOM   2490  CG  ARG A 325      37.530  -1.321  -3.931  1.00102.12           C  
ANISOU 2490  CG  ARG A 325    17757   9252  11791  -1138  -4403   1705       C  
ATOM   2491  CD  ARG A 325      36.995  -2.480  -4.752  1.00101.00           C  
ANISOU 2491  CD  ARG A 325    17976   9038  11361  -1101  -4462   1786       C  
ATOM   2492  NE  ARG A 325      37.908  -3.615  -4.729  1.00103.12           N  
ANISOU 2492  NE  ARG A 325    18584   8872  11725   -773  -5120   1703       N  
ATOM   2493  CZ  ARG A 325      37.920  -4.527  -3.763  1.00104.29           C  
ANISOU 2493  CZ  ARG A 325    19478   8620  11526  -1012  -5760   1773       C  
ATOM   2494  NH1 ARG A 325      37.070  -4.426  -2.749  1.00103.59           N  
ANISOU 2494  NH1 ARG A 325    19862   8587  10910  -1629  -5758   1926       N  
ATOM   2495  NH2 ARG A 325      38.780  -5.536  -3.806  1.00106.58           N  
ANISOU 2495  NH2 ARG A 325    20039   8459  11998   -654  -6423   1673       N  
ATOM   2496  N   ALA A 326      38.052   2.583  -4.366  1.00 93.01           N  
ANISOU 2496  N   ALA A 326    14665   8760  11912   -930  -3204   1575       N  
ATOM   2497  CA  ALA A 326      39.218   3.338  -4.807  1.00 96.00           C  
ANISOU 2497  CA  ALA A 326    14402   9139  12934   -546  -3113   1508       C  
ATOM   2498  C   ALA A 326      39.711   4.274  -3.711  1.00 96.93           C  
ANISOU 2498  C   ALA A 326    14297   9184  13349   -639  -3229   1349       C  
ATOM   2499  O   ALA A 326      40.907   4.306  -3.401  1.00 98.60           O  
ANISOU 2499  O   ALA A 326    14334   9222  13907   -369  -3528   1197       O  
ATOM   2500  CB  ALA A 326      38.888   4.119  -6.079  1.00 97.57           C  
ANISOU 2500  CB  ALA A 326    14045   9621  13405   -454  -2546   1670       C  
ATOM   2501  N   THR A 327      38.801   5.030  -3.096  1.00 91.70           N  
ANISOU 2501  N   THR A 327    13609   8661  12571  -1014  -3012   1323       N  
ATOM   2502  CA  THR A 327      39.188   6.016  -2.093  1.00 92.85           C  
ANISOU 2502  CA  THR A 327    13476   8777  13027  -1113  -3080   1122       C  
ATOM   2503  C   THR A 327      39.445   5.404  -0.721  1.00 93.15           C  
ANISOU 2503  C   THR A 327    14063   8658  12672  -1312  -3606    964       C  
ATOM   2504  O   THR A 327      39.612   6.152   0.248  1.00 94.23           O  
ANISOU 2504  O   THR A 327    14042   8819  12942  -1469  -3677    759       O  
ATOM   2505  CB  THR A 327      38.118   7.103  -1.969  1.00 91.95           C  
ANISOU 2505  CB  THR A 327    13056   8883  12998  -1419  -2666   1070       C  
ATOM   2506  OG1 THR A 327      36.916   6.537  -1.434  1.00 89.64           O  
ANISOU 2506  OG1 THR A 327    13282   8729  12049  -1849  -2667   1027       O  
ATOM   2507  CG2 THR A 327      37.817   7.697  -3.332  1.00 91.44           C  
ANISOU 2507  CG2 THR A 327    12513   8936  13292  -1246  -2221   1285       C  
ATOM   2508  N   SER A 328      39.472   4.077  -0.612  1.00102.17           N  
ANISOU 2508  N   SER A 328    15855   9630  13334  -1326  -4003   1058       N  
ATOM   2509  CA  SER A 328      39.793   3.415   0.647  1.00105.59           C  
ANISOU 2509  CA  SER A 328    16886   9863  13371  -1522  -4597    981       C  
ATOM   2510  C   SER A 328      41.211   2.863   0.700  1.00108.45           C  
ANISOU 2510  C   SER A 328    17279   9878  14047  -1064  -5157    911       C  
ATOM   2511  O   SER A 328      41.776   2.740   1.792  1.00111.62           O  
ANISOU 2511  O   SER A 328    17952  10108  14352  -1132  -5661    795       O  
ATOM   2512  CB  SER A 328      38.809   2.270   0.903  1.00106.41           C  
ANISOU 2512  CB  SER A 328    17790   9948  12693  -1934  -4768   1150       C  
ATOM   2513  OG  SER A 328      38.972   1.233  -0.048  1.00106.29           O  
ANISOU 2513  OG  SER A 328    17993   9736  12655  -1641  -4913   1308       O  
ATOM   2514  N   ASN A 329      41.797   2.538  -0.452  1.00126.39           N  
ANISOU 2514  N   ASN A 329    19257  12072  16694   -604  -5091    937       N  
ATOM   2515  CA  ASN A 329      43.089   1.870  -0.634  1.00126.98           C  
ANISOU 2515  CA  ASN A 329    19299  11841  17105   -116  -5600    795       C  
ATOM   2516  C   ASN A 329      44.293   2.795  -0.327  1.00129.02           C  
ANISOU 2516  C   ASN A 329    18929  12076  18015    172  -5661    536       C  
ATOM   2517  O   ASN A 329      45.448   2.442  -0.607  1.00129.14           O  
ANISOU 2517  O   ASN A 329    18715  11904  18447    622  -5989    335       O  
ATOM   2518  CB  ASN A 329      43.158   1.334  -2.071  1.00126.52           C  
ANISOU 2518  CB  ASN A 329    19024  11840  17208    219  -5366    839       C  
ATOM   2519  CG  ASN A 329      44.230   0.264  -2.267  1.00125.44           C  
ANISOU 2519  CG  ASN A 329    19017  11366  17280    680  -5977    641       C  
ATOM   2520  OD1 ASN A 329      44.963  -0.087  -1.346  1.00125.18           O  
ANISOU 2520  OD1 ASN A 329    19248  11008  17306    782  -6627    497       O  
ATOM   2521  ND2 ASN A 329      44.309  -0.267  -3.482  1.00125.64           N  
ANISOU 2521  ND2 ASN A 329    18845  11471  17422    966  -5797    603       N  
ATOM   2522  N   LEU A 330      44.062   3.974   0.255  1.00125.91           N  
ANISOU 2522  N   LEU A 330    18217  11866  17756    -74  -5367    484       N  
ATOM   2523  CA  LEU A 330      45.099   4.990   0.399  1.00126.52           C  
ANISOU 2523  CA  LEU A 330    17611  11952  18510    167  -5313    249       C  
ATOM   2524  C   LEU A 330      45.415   5.296   1.860  1.00127.07           C  
ANISOU 2524  C   LEU A 330    17868  11911  18500     -8  -5746     56       C  
ATOM   2525  O   LEU A 330      46.013   6.336   2.155  1.00127.91           O  
ANISOU 2525  O   LEU A 330    17411  12068  19121     72  -5632   -149       O  
ATOM   2526  CB  LEU A 330      44.674   6.267  -0.326  1.00127.88           C  
ANISOU 2526  CB  LEU A 330    17113  12411  19066     80  -4583    329       C  
ATOM   2527  CG  LEU A 330      44.361   6.086  -1.814  1.00127.95           C  
ANISOU 2527  CG  LEU A 330    16902  12583  19131    220  -4129    545       C  
ATOM   2528  CD1 LEU A 330      43.851   7.384  -2.419  1.00129.43           C  
ANISOU 2528  CD1 LEU A 330    16517  13003  19657     73  -3499    684       C  
ATOM   2529  CD2 LEU A 330      45.563   5.555  -2.579  1.00128.70           C  
ANISOU 2529  CD2 LEU A 330    16712  12603  19586    681  -4285    406       C  
ATOM   2530  N   THR A 331      45.038   4.410   2.778  1.00149.25           N  
ANISOU 2530  N   THR A 331    21469  14577  20662   -272  -6255    124       N  
ATOM   2531  CA  THR A 331      45.195   4.684   4.201  1.00151.61           C  
ANISOU 2531  CA  THR A 331    22018  14846  20741   -534  -6651    -33       C  
ATOM   2532  C   THR A 331      46.666   4.713   4.597  1.00152.13           C  
ANISOU 2532  C   THR A 331    21835  14649  21319   -103  -7198   -304       C  
ATOM   2533  O   THR A 331      47.482   3.940   4.085  1.00150.60           O  
ANISOU 2533  O   THR A 331    21660  14187  21374    332  -7570   -347       O  
ATOM   2534  CB  THR A 331      44.455   3.633   5.029  1.00150.71           C  
ANISOU 2534  CB  THR A 331    22876  14651  19737   -981  -7093    163       C  
ATOM   2535  OG1 THR A 331      45.001   2.334   4.759  1.00148.98           O  
ANISOU 2535  OG1 THR A 331    23139  14038  19429   -687  -7702    280       O  
ATOM   2536  CG2 THR A 331      42.971   3.638   4.691  1.00149.73           C  
ANISOU 2536  CG2 THR A 331    22949  14828  19113  -1444  -6531    364       C  
ATOM   2537  N   GLN A 332      47.003   5.631   5.507  1.00158.84           N  
ANISOU 2537  N   GLN A 332    22403  15590  22361   -212  -7248   -545       N  
ATOM   2538  CA  GLN A 332      48.337   5.849   6.063  1.00158.49           C  
ANISOU 2538  CA  GLN A 332    22072  15343  22805    136  -7751   -859       C  
ATOM   2539  C   GLN A 332      49.317   6.347   5.003  1.00157.60           C  
ANISOU 2539  C   GLN A 332    21105  15201  23575    649  -7460  -1038       C  
ATOM   2540  O   GLN A 332      50.468   6.666   5.333  1.00158.61           O  
ANISOU 2540  O   GLN A 332    20834  15199  24231    959  -7778  -1357       O  
ATOM   2541  CB  GLN A 332      48.889   4.582   6.744  1.00156.98           C  
ANISOU 2541  CB  GLN A 332    22623  14778  22244    254  -8693   -837       C  
ATOM   2542  CG  GLN A 332      50.151   4.768   7.587  1.00157.15           C  
ANISOU 2542  CG  GLN A 332    22471  14591  22647    544  -9340  -1181       C  
ATOM   2543  CD  GLN A 332      50.585   3.489   8.277  1.00157.00           C  
ANISOU 2543  CD  GLN A 332    23271  14156  22226    632 -10354  -1109       C  
ATOM   2544  OE1 GLN A 332      49.970   2.439   8.102  1.00156.85           O  
ANISOU 2544  OE1 GLN A 332    23954  13974  21666    472 -10576   -790       O  
ATOM   2545  NE2 GLN A 332      51.650   3.573   9.068  1.00158.09           N  
ANISOU 2545  NE2 GLN A 332    23329  14089  22648    883 -11015  -1403       N  
ATOM   2546  N   GLU A 333      48.886   6.475   3.749  1.00142.05           N  
ANISOU 2546  N   GLU A 333    18819  13386  21767    707  -6845   -855       N  
ATOM   2547  CA  GLU A 333      49.774   6.806   2.644  1.00140.38           C  
ANISOU 2547  CA  GLU A 333    17861  13203  22273   1120  -6550   -986       C  
ATOM   2548  C   GLU A 333      49.993   8.310   2.501  1.00141.56           C  
ANISOU 2548  C   GLU A 333    17207  13541  23037   1055  -6011  -1097       C  
ATOM   2549  O   GLU A 333      50.658   8.728   1.550  1.00141.17           O  
ANISOU 2549  O   GLU A 333    16508  13571  23561   1292  -5671  -1161       O  
ATOM   2550  CB  GLU A 333      49.205   6.210   1.350  1.00138.81           C  
ANISOU 2550  CB  GLU A 333    17734  13112  21894   1174  -6165   -720       C  
ATOM   2551  CG  GLU A 333      50.163   6.163   0.168  1.00137.93           C  
ANISOU 2551  CG  GLU A 333    16992  13059  22355   1595  -5966   -880       C  
ATOM   2552  CD  GLU A 333      49.548   5.499  -1.041  1.00139.37           C  
ANISOU 2552  CD  GLU A 333    17306  13383  22266   1620  -5629   -642       C  
ATOM   2553  OE1 GLU A 333      48.357   5.134  -0.970  1.00140.63           O  
ANISOU 2553  OE1 GLU A 333    18024  13573  21834   1316  -5535   -341       O  
ATOM   2554  OE2 GLU A 333      50.257   5.329  -2.055  1.00139.89           O  
ANISOU 2554  OE2 GLU A 333    16898  13560  22692   1928  -5456   -794       O  
ATOM   2555  N   ASN A 334      49.431   9.107   3.410  1.00136.62           N  
ANISOU 2555  N   ASN A 334    16618  12998  22295    710  -5932  -1133       N  
ATOM   2556  CA  ASN A 334      49.593  10.565   3.509  1.00137.69           C  
ANISOU 2556  CA  ASN A 334    16045  13238  23033    619  -5538  -1283       C  
ATOM   2557  C   ASN A 334      49.703  11.245   2.140  1.00136.64           C  
ANISOU 2557  C   ASN A 334    15252  13217  23447    718  -4903  -1113       C  
ATOM   2558  O   ASN A 334      50.658  11.957   1.831  1.00134.50           O  
ANISOU 2558  O   ASN A 334    14315  12923  23864    895  -4774  -1282       O  
ATOM   2559  CB  ASN A 334      50.761  10.939   4.441  1.00138.20           C  
ANISOU 2559  CB  ASN A 334    15823  13160  23526    803  -5996  -1697       C  
ATOM   2560  CG  ASN A 334      52.141  10.501   3.937  1.00136.38           C  
ANISOU 2560  CG  ASN A 334    15247  12781  23789   1280  -6265  -1906       C  
ATOM   2561  OD1 ASN A 334      52.324  10.086   2.799  1.00133.59           O  
ANISOU 2561  OD1 ASN A 334    14728  12473  23557   1475  -6022  -1779       O  
ATOM   2562  ND2 ASN A 334      53.129  10.607   4.817  1.00137.42           N  
ANISOU 2562  ND2 ASN A 334    15236  12765  24210   1466  -6782  -2287       N  
ATOM   2563  N   MET A 335      48.671  11.030   1.321  1.00120.42           N  
ANISOU 2563  N   MET A 335    13404  11302  21049    557  -4504   -762       N  
ATOM   2564  CA  MET A 335      48.607  11.655   0.004  1.00120.32           C  
ANISOU 2564  CA  MET A 335    12863  11423  21431    577  -3913   -523       C  
ATOM   2565  C   MET A 335      47.202  12.146  -0.318  1.00120.59           C  
ANISOU 2565  C   MET A 335    13006  11586  21225    247  -3485   -225       C  
ATOM   2566  O   MET A 335      46.273  11.337  -0.452  1.00120.20           O  
ANISOU 2566  O   MET A 335    13507  11612  20551    129  -3488    -44       O  
ATOM   2567  CB  MET A 335      49.070  10.686  -1.085  1.00119.83           C  
ANISOU 2567  CB  MET A 335    12837  11424  21269    852  -3884   -425       C  
ATOM   2568  CG  MET A 335      50.549  10.366  -1.052  1.00118.52           C  
ANISOU 2568  CG  MET A 335    12343  11166  21522   1221  -4214   -780       C  
ATOM   2569  SD  MET A 335      51.562  11.828  -1.327  1.00117.47           S  
ANISOU 2569  SD  MET A 335    11239  11087  22306   1227  -3859   -937       S  
ATOM   2570  CE  MET A 335      53.188  11.177  -0.956  1.00117.97           C  
ANISOU 2570  CE  MET A 335    11064  11030  22731   1671  -4414  -1482       C  
ATOM   2571  N   PRO A 336      47.004  13.460  -0.446  1.00102.74           N  
ANISOU 2571  N   PRO A 336    10225   9330  19484     94  -3146   -188       N  
ATOM   2572  CA  PRO A 336      45.727  13.966  -0.963  1.00100.12           C  
ANISOU 2572  CA  PRO A 336     9907   9093  19042   -158  -2754     90       C  
ATOM   2573  C   PRO A 336      45.669  13.900  -2.481  1.00 99.10           C  
ANISOU 2573  C   PRO A 336     9597   9077  18978    -88  -2362    486       C  
ATOM   2574  O   PRO A 336      44.584  13.812  -3.068  1.00 96.83           O  
ANISOU 2574  O   PRO A 336     9512   8897  18383   -232  -2122    756       O  
ATOM   2575  CB  PRO A 336      45.694  15.411  -0.455  1.00101.16           C  
ANISOU 2575  CB  PRO A 336     9517   9110  19809   -305  -2653    -76       C  
ATOM   2576  CG  PRO A 336      47.126  15.787  -0.346  1.00104.05           C  
ANISOU 2576  CG  PRO A 336     9416   9355  20763   -103  -2781   -266       C  
ATOM   2577  CD  PRO A 336      47.862  14.543   0.064  1.00105.16           C  
ANISOU 2577  CD  PRO A 336     9947   9508  20501    128  -3193   -452       C  
ATOM   2578  N   THR A 337      46.840  13.937  -3.125  1.00 96.41           N  
ANISOU 2578  N   THR A 337     8859   8751  19021    115  -2296    492       N  
ATOM   2579  CA  THR A 337      46.890  13.868  -4.583  1.00 96.25           C  
ANISOU 2579  CA  THR A 337     8641   8914  19015    141  -1908    841       C  
ATOM   2580  C   THR A 337      46.304  12.559  -5.096  1.00 94.38           C  
ANISOU 2580  C   THR A 337     8950   8836  18073    222  -1937    967       C  
ATOM   2581  O   THR A 337      45.591  12.542  -6.106  1.00 92.90           O  
ANISOU 2581  O   THR A 337     8807   8813  17675    124  -1612   1308       O  
ATOM   2582  CB  THR A 337      48.331  14.030  -5.068  1.00 99.59           C  
ANISOU 2582  CB  THR A 337     8530   9394  19916    311  -1842    716       C  
ATOM   2583  OG1 THR A 337      49.139  12.973  -4.536  1.00101.04           O  
ANISOU 2583  OG1 THR A 337     8915   9547  19928    603  -2257    335       O  
ATOM   2584  CG2 THR A 337      48.897  15.366  -4.617  1.00101.71           C  
ANISOU 2584  CG2 THR A 337     8238   9487  20920    196  -1796    611       C  
ATOM   2585  N   LEU A 338      46.593  11.452  -4.410  1.00102.55           N  
ANISOU 2585  N   LEU A 338    10418   9799  18749    397  -2365    699       N  
ATOM   2586  CA  LEU A 338      46.042  10.164  -4.815  1.00102.88           C  
ANISOU 2586  CA  LEU A 338    11009   9927  18154    468  -2458    793       C  
ATOM   2587  C   LEU A 338      44.537  10.104  -4.594  1.00101.58           C  
ANISOU 2587  C   LEU A 338    11300   9791  17504    182  -2364    993       C  
ATOM   2588  O   LEU A 338      43.826   9.423  -5.343  1.00101.72           O  
ANISOU 2588  O   LEU A 338    11610   9944  17093    160  -2220   1199       O  
ATOM   2589  CB  LEU A 338      46.743   9.036  -4.058  1.00101.62           C  
ANISOU 2589  CB  LEU A 338    11223   9595  17792    709  -3032    469       C  
ATOM   2590  CG  LEU A 338      48.091   8.557  -4.606  1.00103.52           C  
ANISOU 2590  CG  LEU A 338    11115   9864  18355   1075  -3159    220       C  
ATOM   2591  CD1 LEU A 338      49.188   9.596  -4.439  1.00104.32           C  
ANISOU 2591  CD1 LEU A 338    10524   9952  19160   1137  -3075     15       C  
ATOM   2592  CD2 LEU A 338      48.492   7.261  -3.927  1.00104.39           C  
ANISOU 2592  CD2 LEU A 338    11738   9741  18184   1320  -3816    -53       C  
ATOM   2593  N   PHE A 339      44.036  10.814  -3.582  1.00 93.98           N  
ANISOU 2593  N   PHE A 339    10363   8730  16614    -43  -2436    884       N  
ATOM   2594  CA  PHE A 339      42.601  10.836  -3.319  1.00 91.99           C  
ANISOU 2594  CA  PHE A 339    10459   8551  15943   -341  -2325    978       C  
ATOM   2595  C   PHE A 339      41.857  11.655  -4.369  1.00 90.39           C  
ANISOU 2595  C   PHE A 339     9919   8464  15959   -444  -1865   1282       C  
ATOM   2596  O   PHE A 339      40.828  11.209  -4.901  1.00 88.48           O  
ANISOU 2596  O   PHE A 339     9968   8355  15294   -552  -1710   1466       O  
ATOM   2597  CB  PHE A 339      42.363  11.357  -1.899  1.00 92.09           C  
ANISOU 2597  CB  PHE A 339    10533   8479  15977   -557  -2541    675       C  
ATOM   2598  CG  PHE A 339      40.922  11.567  -1.548  1.00 90.19           C  
ANISOU 2598  CG  PHE A 339    10509   8364  15393   -899  -2389    655       C  
ATOM   2599  CD1 PHE A 339      40.024  10.516  -1.564  1.00 88.04           C  
ANISOU 2599  CD1 PHE A 339    10833   8209  14407  -1062  -2427    739       C  
ATOM   2600  CD2 PHE A 339      40.486  12.800  -1.108  1.00 90.67           C  
ANISOU 2600  CD2 PHE A 339    10162   8419  15869  -1069  -2243    481       C  
ATOM   2601  CE1 PHE A 339      38.700  10.713  -1.218  1.00 86.51           C  
ANISOU 2601  CE1 PHE A 339    10788   8175  13905  -1404  -2266    652       C  
ATOM   2602  CE2 PHE A 339      39.168  12.999  -0.750  1.00 89.60           C  
ANISOU 2602  CE2 PHE A 339    10158   8429  15457  -1374  -2114    356       C  
ATOM   2603  CZ  PHE A 339      38.274  11.954  -0.806  1.00 87.55           C  
ANISOU 2603  CZ  PHE A 339    10466   8334  14464  -1552  -2108    434       C  
ATOM   2604  N   VAL A 340      42.383  12.834  -4.712  1.00 93.28           N  
ANISOU 2604  N   VAL A 340     9686   8766  16992   -419  -1675   1354       N  
ATOM   2605  CA  VAL A 340      41.778  13.638  -5.772  1.00 91.89           C  
ANISOU 2605  CA  VAL A 340     9206   8648  17058   -518  -1311   1706       C  
ATOM   2606  C   VAL A 340      41.840  12.895  -7.101  1.00 92.65           C  
ANISOU 2606  C   VAL A 340     9405   8962  16836   -406  -1104   2019       C  
ATOM   2607  O   VAL A 340      40.829  12.747  -7.801  1.00 90.45           O  
ANISOU 2607  O   VAL A 340     9301   8810  16255   -500   -925   2263       O  
ATOM   2608  CB  VAL A 340      42.465  15.010  -5.870  1.00 92.02           C  
ANISOU 2608  CB  VAL A 340     8588   8502  17873   -543  -1204   1757       C  
ATOM   2609  CG1 VAL A 340      41.855  15.826  -6.998  1.00 89.52           C  
ANISOU 2609  CG1 VAL A 340     8017   8198  17800   -670   -902   2191       C  
ATOM   2610  CG2 VAL A 340      42.374  15.743  -4.554  1.00 91.44           C  
ANISOU 2610  CG2 VAL A 340     8384   8230  18129   -642  -1416   1384       C  
ATOM   2611  N   GLU A 341      43.034  12.423  -7.473  1.00 91.97           N  
ANISOU 2611  N   GLU A 341     9176   8945  16824   -199  -1133   1962       N  
ATOM   2612  CA  GLU A 341      43.183  11.712  -8.737  1.00 94.89           C  
ANISOU 2612  CA  GLU A 341     9578   9577  16898    -91   -927   2171       C  
ATOM   2613  C   GLU A 341      42.332  10.453  -8.776  1.00 94.32           C  
ANISOU 2613  C   GLU A 341    10110   9591  16138    -55  -1047   2146       C  
ATOM   2614  O   GLU A 341      41.890  10.037  -9.853  1.00 96.03           O  
ANISOU 2614  O   GLU A 341    10407  10034  16047    -50   -826   2375       O  
ATOM   2615  CB  GLU A 341      44.652  11.372  -8.982  1.00 97.61           C  
ANISOU 2615  CB  GLU A 341     9617  10002  17469    135   -973   1965       C  
ATOM   2616  CG  GLU A 341      45.512  12.580  -9.298  1.00 96.24           C  
ANISOU 2616  CG  GLU A 341     8796   9829  17941     45   -746   2059       C  
ATOM   2617  CD  GLU A 341      46.972  12.228  -9.493  1.00 97.97           C  
ANISOU 2617  CD  GLU A 341     8659  10171  18394    251   -779   1763       C  
ATOM   2618  OE1 GLU A 341      47.348  11.065  -9.233  1.00 98.99           O  
ANISOU 2618  OE1 GLU A 341     9047  10315  18248    515  -1065   1435       O  
ATOM   2619  OE2 GLU A 341      47.745  13.116  -9.913  1.00 98.86           O  
ANISOU 2619  OE2 GLU A 341     8219  10354  18989    139   -539   1841       O  
ATOM   2620  N   SER A 342      42.076   9.841  -7.617  1.00 95.18           N  
ANISOU 2620  N   SER A 342    10657   9529  15979    -66  -1402   1881       N  
ATOM   2621  CA  SER A 342      41.248   8.640  -7.584  1.00 94.10           C  
ANISOU 2621  CA  SER A 342    11129   9436  15190    -93  -1541   1873       C  
ATOM   2622  C   SER A 342      39.783   8.977  -7.837  1.00 90.12           C  
ANISOU 2622  C   SER A 342    10765   9031  14444   -353  -1302   2078       C  
ATOM   2623  O   SER A 342      39.123   8.337  -8.668  1.00 89.58           O  
ANISOU 2623  O   SER A 342    10919   9130  13987   -354  -1165   2242       O  
ATOM   2624  CB  SER A 342      41.420   7.919  -6.247  1.00 92.35           C  
ANISOU 2624  CB  SER A 342    11369   8996  14722   -105  -2017   1578       C  
ATOM   2625  OG  SER A 342      40.911   8.697  -5.179  1.00 90.52           O  
ANISOU 2625  OG  SER A 342    11140   8676  14577   -361  -2064   1468       O  
ATOM   2626  N   VAL A 343      39.255   9.984  -7.131  1.00 84.23           N  
ANISOU 2626  N   VAL A 343     9858   8191  13953   -561  -1267   2019       N  
ATOM   2627  CA  VAL A 343      37.861  10.371  -7.347  1.00 82.54           C  
ANISOU 2627  CA  VAL A 343     9701   8065  13594   -784  -1072   2131       C  
ATOM   2628  C   VAL A 343      37.650  10.823  -8.788  1.00 82.44           C  
ANISOU 2628  C   VAL A 343     9391   8193  13740   -724   -757   2511       C  
ATOM   2629  O   VAL A 343      36.662  10.451  -9.438  1.00 81.11           O  
ANISOU 2629  O   VAL A 343     9427   8177  13215   -791   -628   2659       O  
ATOM   2630  CB  VAL A 343      37.444  11.463  -6.345  1.00 82.89           C  
ANISOU 2630  CB  VAL A 343     9515   7983  13997   -982  -1111   1909       C  
ATOM   2631  CG1 VAL A 343      36.017  11.904  -6.612  1.00 81.74           C  
ANISOU 2631  CG1 VAL A 343     9345   7925  13787  -1177   -934   1948       C  
ATOM   2632  CG2 VAL A 343      37.591  10.966  -4.920  1.00 83.45           C  
ANISOU 2632  CG2 VAL A 343     9927   7989  13790  -1101  -1418   1541       C  
ATOM   2633  N   LEU A 344      38.582  11.626  -9.313  1.00 91.21           N  
ANISOU 2633  N   LEU A 344    10023   9269  15363   -629   -638   2680       N  
ATOM   2634  CA  LEU A 344      38.499  12.052 -10.707  1.00 91.02           C  
ANISOU 2634  CA  LEU A 344     9742   9405  15434   -628   -355   3093       C  
ATOM   2635  C   LEU A 344      38.575  10.859 -11.653  1.00 94.50           C  
ANISOU 2635  C   LEU A 344    10442  10132  15333   -498   -261   3187       C  
ATOM   2636  O   LEU A 344      37.916  10.841 -12.702  1.00 92.01           O  
ANISOU 2636  O   LEU A 344    10148  10013  14797   -547    -65   3479       O  
ATOM   2637  CB  LEU A 344      39.617  13.048 -11.008  1.00 93.93           C  
ANISOU 2637  CB  LEU A 344     9578   9702  16410   -616   -252   3243       C  
ATOM   2638  CG  LEU A 344      39.537  14.364 -10.235  1.00 90.67           C  
ANISOU 2638  CG  LEU A 344     8840   8978  16633   -743   -342   3177       C  
ATOM   2639  CD1 LEU A 344      40.788  15.195 -10.458  1.00 93.64           C  
ANISOU 2639  CD1 LEU A 344     8717   9268  17592   -745   -262   3288       C  
ATOM   2640  CD2 LEU A 344      38.295  15.138 -10.640  1.00 87.67           C  
ANISOU 2640  CD2 LEU A 344     8410   8518  16382   -897   -281   3417       C  
ATOM   2641  N   GLU A 345      39.379   9.854 -11.293  1.00 91.64           N  
ANISOU 2641  N   GLU A 345    10267   9780  14774   -319   -437   2916       N  
ATOM   2642  CA  GLU A 345      39.495   8.639 -12.095  1.00 96.82           C  
ANISOU 2642  CA  GLU A 345    11156  10669  14963   -162   -409   2900       C  
ATOM   2643  C   GLU A 345      38.158   7.914 -12.186  1.00 91.36           C  
ANISOU 2643  C   GLU A 345    10945  10035  13734   -258   -433   2934       C  
ATOM   2644  O   GLU A 345      37.726   7.507 -13.274  1.00 91.23           O  
ANISOU 2644  O   GLU A 345    10980  10272  13409   -234   -247   3111       O  
ATOM   2645  CB  GLU A 345      40.568   7.736 -11.487  1.00102.97           C  
ANISOU 2645  CB  GLU A 345    12054  11339  15731     69   -714   2533       C  
ATOM   2646  CG  GLU A 345      40.868   6.467 -12.248  1.00108.20           C  
ANISOU 2646  CG  GLU A 345    12890  12191  16029    286   -755   2410       C  
ATOM   2647  CD  GLU A 345      41.973   5.663 -11.587  1.00108.48           C  
ANISOU 2647  CD  GLU A 345    13004  12041  16175    548  -1149   2011       C  
ATOM   2648  OE1 GLU A 345      42.483   6.111 -10.536  1.00106.31           O  
ANISOU 2648  OE1 GLU A 345    12666  11512  16216    542  -1378   1863       O  
ATOM   2649  OE2 GLU A 345      42.330   4.585 -12.110  1.00110.54           O  
ANISOU 2649  OE2 GLU A 345    13376  12396  16227    774  -1267   1815       O  
ATOM   2650  N   VAL A 346      37.482   7.752 -11.045  1.00 95.18           N  
ANISOU 2650  N   VAL A 346    11770  10315  14078   -400   -649   2746       N  
ATOM   2651  CA  VAL A 346      36.164   7.120 -11.037  1.00 90.21           C  
ANISOU 2651  CA  VAL A 346    11573   9750  12954   -558   -653   2742       C  
ATOM   2652  C   VAL A 346      35.184   7.922 -11.884  1.00 86.31           C  
ANISOU 2652  C   VAL A 346    10852   9411  12530   -676   -371   3013       C  
ATOM   2653  O   VAL A 346      34.467   7.371 -12.734  1.00 85.29           O  
ANISOU 2653  O   VAL A 346    10895   9480  12031   -677   -255   3135       O  
ATOM   2654  CB  VAL A 346      35.654   6.962  -9.593  1.00 86.87           C  
ANISOU 2654  CB  VAL A 346    11495   9136  12376   -778   -896   2474       C  
ATOM   2655  CG1 VAL A 346      34.245   6.392  -9.586  1.00 82.53           C  
ANISOU 2655  CG1 VAL A 346    11339   8694  11327  -1010   -850   2445       C  
ATOM   2656  CG2 VAL A 346      36.597   6.086  -8.787  1.00 89.74           C  
ANISOU 2656  CG2 VAL A 346    12161   9316  12621   -666  -1261   2256       C  
ATOM   2657  N   HIS A 347      35.141   9.240 -11.663  1.00 93.11           N  
ANISOU 2657  N   HIS A 347    11323  10156  13897   -767   -301   3098       N  
ATOM   2658  CA  HIS A 347      34.201  10.081 -12.398  1.00 89.38           C  
ANISOU 2658  CA  HIS A 347    10637   9749  13574   -867   -132   3353       C  
ATOM   2659  C   HIS A 347      34.402   9.946 -13.903  1.00 90.04           C  
ANISOU 2659  C   HIS A 347    10609  10089  13512   -765     71   3727       C  
ATOM   2660  O   HIS A 347      33.431   9.799 -14.656  1.00 87.40           O  
ANISOU 2660  O   HIS A 347    10385   9915  12909   -809    157   3884       O  
ATOM   2661  CB  HIS A 347      34.350  11.537 -11.960  1.00 88.12           C  
ANISOU 2661  CB  HIS A 347    10039   9354  14090   -943   -155   3387       C  
ATOM   2662  CG  HIS A 347      33.260  12.431 -12.462  1.00 85.72           C  
ANISOU 2662  CG  HIS A 347     9544   9010  14015  -1043   -106   3567       C  
ATOM   2663  ND1 HIS A 347      33.300  13.033 -13.701  1.00 85.43           N  
ANISOU 2663  ND1 HIS A 347     9277   9031  14151  -1021      8   4032       N  
ATOM   2664  CD2 HIS A 347      32.099  12.826 -11.890  1.00 85.09           C  
ANISOU 2664  CD2 HIS A 347     9458   8841  14030  -1173   -189   3321       C  
ATOM   2665  CE1 HIS A 347      32.210  13.759 -13.871  1.00 85.38           C  
ANISOU 2665  CE1 HIS A 347     9156   8915  14369  -1099    -61   4091       C  
ATOM   2666  NE2 HIS A 347      31.464  13.650 -12.787  1.00 84.67           N  
ANISOU 2666  NE2 HIS A 347     9167   8743  14262  -1176   -170   3624       N  
ATOM   2667  N   GLY A 348      35.657   9.975 -14.358  1.00101.32           N  
ANISOU 2667  N   GLY A 348    11806  11599  15090   -645    153   3838       N  
ATOM   2668  CA  GLY A 348      35.920   9.772 -15.775  1.00103.78           C  
ANISOU 2668  CA  GLY A 348    12005  12245  15180   -595    375   4141       C  
ATOM   2669  C   GLY A 348      35.460   8.410 -16.261  1.00105.22           C  
ANISOU 2669  C   GLY A 348    12570  12671  14738   -494    381   4009       C  
ATOM   2670  O   GLY A 348      34.804   8.297 -17.302  1.00103.36           O  
ANISOU 2670  O   GLY A 348    12374  12691  14206   -528    525   4241       O  
ATOM   2671  N   LYS A 349      35.805   7.358 -15.511  1.00103.09           N  
ANISOU 2671  N   LYS A 349    12596  12302  14271   -373    186   3639       N  
ATOM   2672  CA  LYS A 349      35.335   6.010 -15.823  1.00104.13           C  
ANISOU 2672  CA  LYS A 349    13133  12572  13859   -288    121   3476       C  
ATOM   2673  C   LYS A 349      33.840   5.993 -16.127  1.00 96.59           C  
ANISOU 2673  C   LYS A 349    12396  11693  12610   -445    183   3595       C  
ATOM   2674  O   LYS A 349      33.415   5.608 -17.225  1.00 95.93           O  
ANISOU 2674  O   LYS A 349    12343  11900  12204   -409    327   3731       O  
ATOM   2675  CB  LYS A 349      35.657   5.072 -14.655  1.00107.33           C  
ANISOU 2675  CB  LYS A 349    13911  12705  14164   -221   -211   3105       C  
ATOM   2676  CG  LYS A 349      35.149   3.639 -14.807  1.00108.30           C  
ANISOU 2676  CG  LYS A 349    14515  12861  13771   -167   -360   2928       C  
ATOM   2677  CD  LYS A 349      35.912   2.850 -15.859  1.00117.57           C  
ANISOU 2677  CD  LYS A 349    15574  14283  14813     96   -308   2839       C  
ATOM   2678  CE  LYS A 349      35.359   1.430 -15.984  1.00116.43           C  
ANISOU 2678  CE  LYS A 349    15912  14111  14215    152   -502   2639       C  
ATOM   2679  NZ  LYS A 349      35.554   0.619 -14.745  1.00112.01           N  
ANISOU 2679  NZ  LYS A 349    15809  13134  13615    148   -944   2390       N  
ATOM   2680  N   PHE A 350      33.024   6.437 -15.168  1.00 96.11           N  
ANISOU 2680  N   PHE A 350    12449  11406  12662   -627     79   3502       N  
ATOM   2681  CA  PHE A 350      31.584   6.268 -15.321  1.00 91.86           C  
ANISOU 2681  CA  PHE A 350    12121  10943  11836   -778    109   3491       C  
ATOM   2682  C   PHE A 350      30.935   7.310 -16.222  1.00 90.14           C  
ANISOU 2682  C   PHE A 350    11587  10845  11818   -822    263   3813       C  
ATOM   2683  O   PHE A 350      29.816   7.079 -16.690  1.00 88.74           O  
ANISOU 2683  O   PHE A 350    11541  10802  11375   -886    295   3825       O  
ATOM   2684  CB  PHE A 350      30.900   6.263 -13.957  1.00 89.53           C  
ANISOU 2684  CB  PHE A 350    12052  10432  11532   -997    -45   3187       C  
ATOM   2685  CG  PHE A 350      31.166   5.024 -13.170  1.00 90.24           C  
ANISOU 2685  CG  PHE A 350    12615  10418  11255  -1030   -249   2925       C  
ATOM   2686  CD1 PHE A 350      30.508   3.848 -13.479  1.00 88.93           C  
ANISOU 2686  CD1 PHE A 350    12857  10353  10580  -1078   -284   2843       C  
ATOM   2687  CD2 PHE A 350      32.074   5.028 -12.128  1.00 92.24           C  
ANISOU 2687  CD2 PHE A 350    12920  10445  11682  -1020   -449   2772       C  
ATOM   2688  CE1 PHE A 350      30.751   2.700 -12.766  1.00 89.41           C  
ANISOU 2688  CE1 PHE A 350    13394  10252  10326  -1133   -537   2646       C  
ATOM   2689  CE2 PHE A 350      32.320   3.884 -11.407  1.00 92.65           C  
ANISOU 2689  CE2 PHE A 350    13453  10353  11396  -1061   -718   2577       C  
ATOM   2690  CZ  PHE A 350      31.657   2.717 -11.726  1.00 91.13           C  
ANISOU 2690  CZ  PHE A 350    13692  10224  10711  -1127   -773   2531       C  
ATOM   2691  N   VAL A 351      31.586   8.445 -16.477  1.00 96.58           N  
ANISOU 2691  N   VAL A 351    12001  11592  13104   -804    322   4078       N  
ATOM   2692  CA  VAL A 351      31.077   9.332 -17.519  1.00 97.59           C  
ANISOU 2692  CA  VAL A 351    11883  11820  13376   -846    410   4473       C  
ATOM   2693  C   VAL A 351      31.301   8.710 -18.893  1.00 98.91           C  
ANISOU 2693  C   VAL A 351    12098  12382  13100   -764    576   4717       C  
ATOM   2694  O   VAL A 351      30.417   8.753 -19.762  1.00 99.43           O  
ANISOU 2694  O   VAL A 351    12208  12629  12942   -795    606   4916       O  
ATOM   2695  CB  VAL A 351      31.714  10.727 -17.405  1.00 99.66           C  
ANISOU 2695  CB  VAL A 351    11732  11855  14278   -900    393   4726       C  
ATOM   2696  CG1 VAL A 351      31.367  11.560 -18.617  1.00102.25           C  
ANISOU 2696  CG1 VAL A 351    11863  12277  14711   -964    437   5231       C  
ATOM   2697  CG2 VAL A 351      31.212  11.418 -16.153  1.00 98.71           C  
ANISOU 2697  CG2 VAL A 351    11527  11380  14596   -985    217   4437       C  
ATOM   2698  N   GLN A 352      32.478   8.107 -19.103  1.00105.99           N  
ANISOU 2698  N   GLN A 352    12964  13441  13865   -652    671   4654       N  
ATOM   2699  CA  GLN A 352      32.697   7.291 -20.294  1.00109.02           C  
ANISOU 2699  CA  GLN A 352    13400  14255  13766   -564    832   4722       C  
ATOM   2700  C   GLN A 352      31.623   6.219 -20.422  1.00107.05           C  
ANISOU 2700  C   GLN A 352    13534  14106  13034   -523    765   4503       C  
ATOM   2701  O   GLN A 352      31.045   6.022 -21.498  1.00106.31           O  
ANISOU 2701  O   GLN A 352    13470  14327  12596   -530    864   4673       O  
ATOM   2702  CB  GLN A 352      34.082   6.641 -20.249  1.00116.44           C  
ANISOU 2702  CB  GLN A 352    14243  15311  14687   -414    887   4489       C  
ATOM   2703  CG  GLN A 352      35.251   7.594 -20.399  1.00121.35           C  
ANISOU 2703  CG  GLN A 352    14432  15961  15716   -476   1021   4696       C  
ATOM   2704  CD  GLN A 352      36.588   6.879 -20.305  1.00131.33           C  
ANISOU 2704  CD  GLN A 352    15559  17352  16987   -301   1051   4350       C  
ATOM   2705  OE1 GLN A 352      36.644   5.673 -20.058  1.00136.21           O  
ANISOU 2705  OE1 GLN A 352    16435  17970  17350   -108    911   3960       O  
ATOM   2706  NE2 GLN A 352      37.673   7.622 -20.501  1.00134.32           N  
ANISOU 2706  NE2 GLN A 352    15522  17822  17693   -373   1206   4473       N  
ATOM   2707  N   LEU A 353      31.339   5.517 -19.321  1.00102.62           N  
ANISOU 2707  N   LEU A 353    13281  13287  12423   -514    588   4130       N  
ATOM   2708  CA  LEU A 353      30.338   4.455 -19.351  1.00100.96           C  
ANISOU 2708  CA  LEU A 353    13455  13139  11765   -529    518   3907       C  
ATOM   2709  C   LEU A 353      28.967   4.994 -19.745  1.00 97.22           C  
ANISOU 2709  C   LEU A 353    12967  12734  11240   -662    548   4057       C  
ATOM   2710  O   LEU A 353      28.371   4.550 -20.733  1.00 97.49           O  
ANISOU 2710  O   LEU A 353    13073  13054  10915   -628    619   4127       O  
ATOM   2711  CB  LEU A 353      30.271   3.757 -17.992  1.00100.31           C  
ANISOU 2711  CB  LEU A 353    13726  12736  11652   -593    303   3544       C  
ATOM   2712  CG  LEU A 353      29.249   2.623 -17.901  1.00 98.00           C  
ANISOU 2712  CG  LEU A 353    13869  12465  10901   -683    217   3312       C  
ATOM   2713  CD1 LEU A 353      29.588   1.516 -18.882  1.00100.96           C  
ANISOU 2713  CD1 LEU A 353    14359  13077  10924   -486    236   3244       C  
ATOM   2714  CD2 LEU A 353      29.170   2.085 -16.484  1.00 96.87           C  
ANISOU 2714  CD2 LEU A 353    14096  12000  10711   -849     -7   3030       C  
ATOM   2715  N   ILE A 354      28.452   5.959 -18.979  1.00 93.98           N  
ANISOU 2715  N   ILE A 354    12431  12065  11211   -799    472   4060       N  
ATOM   2716  CA  ILE A 354      27.072   6.397 -19.167  1.00 93.45           C  
ANISOU 2716  CA  ILE A 354    12338  12013  11155   -907    436   4068       C  
ATOM   2717  C   ILE A 354      26.891   7.053 -20.530  1.00 94.52           C  
ANISOU 2717  C   ILE A 354    12244  12367  11301   -846    494   4503       C  
ATOM   2718  O   ILE A 354      25.881   6.829 -21.209  1.00 94.77           O  
ANISOU 2718  O   ILE A 354    12354  12579  11074   -851    475   4520       O  
ATOM   2719  CB  ILE A 354      26.644   7.331 -18.021  1.00 93.60           C  
ANISOU 2719  CB  ILE A 354    12201  11716  11647  -1050    324   3889       C  
ATOM   2720  CG1 ILE A 354      26.671   6.582 -16.690  1.00 92.87           C  
ANISOU 2720  CG1 ILE A 354    12403  11482  11400  -1184    263   3460       C  
ATOM   2721  CG2 ILE A 354      25.249   7.872 -18.265  1.00 94.81           C  
ANISOU 2721  CG2 ILE A 354    12236  11883  11904  -1127    256   3834       C  
ATOM   2722  CD1 ILE A 354      26.510   7.476 -15.485  1.00 93.47           C  
ANISOU 2722  CD1 ILE A 354    12295  11307  11913  -1335    179   3233       C  
ATOM   2723  N   ASN A 355      27.861   7.862 -20.964  1.00104.81           N  
ANISOU 2723  N   ASN A 355    13273  13669  12879   -817    551   4871       N  
ATOM   2724  CA  ASN A 355      27.725   8.472 -22.283  1.00105.32           C  
ANISOU 2724  CA  ASN A 355    13174  13962  12882   -828    587   5351       C  
ATOM   2725  C   ASN A 355      27.903   7.454 -23.401  1.00105.77           C  
ANISOU 2725  C   ASN A 355    13377  14497  12313   -753    749   5395       C  
ATOM   2726  O   ASN A 355      27.331   7.621 -24.484  1.00106.89           O  
ANISOU 2726  O   ASN A 355    13512  14858  12244   -756    726   5523       O  
ATOM   2727  CB  ASN A 355      28.721   9.619 -22.453  1.00106.18           C  
ANISOU 2727  CB  ASN A 355    12966  13952  13427   -897    615   5760       C  
ATOM   2728  CG  ASN A 355      28.308  10.864 -21.695  1.00106.63           C  
ANISOU 2728  CG  ASN A 355    12817  13545  14152   -969    400   5805       C  
ATOM   2729  OD1 ASN A 355      27.132  11.230 -21.670  1.00108.21           O  
ANISOU 2729  OD1 ASN A 355    13020  13608  14487   -978    212   5752       O  
ATOM   2730  ND2 ASN A 355      29.278  11.529 -21.083  1.00106.36           N  
ANISOU 2730  ND2 ASN A 355    12569  13268  14575  -1009    410   5854       N  
ATOM   2731  N   THR A 356      28.674   6.393 -23.162  1.00102.72           N  
ANISOU 2731  N   THR A 356    13125  14228  11678   -655    853   5090       N  
ATOM   2732  CA  THR A 356      29.005   5.469 -24.241  1.00105.42           C  
ANISOU 2732  CA  THR A 356    13527  15039  11490   -564   1009   5067       C  
ATOM   2733  C   THR A 356      27.829   4.565 -24.601  1.00104.63           C  
ANISOU 2733  C   THR A 356    13705  15092  10957   -525    950   4850       C  
ATOM   2734  O   THR A 356      27.466   4.448 -25.777  1.00105.59           O  
ANISOU 2734  O   THR A 356    13808  15551  10760   -512   1004   4929       O  
ATOM   2735  CB  THR A 356      30.223   4.624 -23.857  1.00109.73           C  
ANISOU 2735  CB  THR A 356    14083  15611  11998   -432   1074   4739       C  
ATOM   2736  OG1 THR A 356      31.346   5.481 -23.614  1.00112.31           O  
ANISOU 2736  OG1 THR A 356    14102  15844  12726   -476   1148   4923       O  
ATOM   2737  CG2 THR A 356      30.572   3.654 -24.976  1.00113.62           C  
ANISOU 2737  CG2 THR A 356    14577  16607  11986   -318   1225   4612       C  
ATOM   2738  N   VAL A 357      27.214   3.929 -23.605  1.00106.34           N  
ANISOU 2738  N   VAL A 357    14188  15026  11188   -531    818   4464       N  
ATOM   2739  CA  VAL A 357      26.336   2.798 -23.853  1.00106.32           C  
ANISOU 2739  CA  VAL A 357    14477  15164  10755   -506    781   4170       C  
ATOM   2740  C   VAL A 357      24.865   3.103 -23.587  1.00105.13           C  
ANISOU 2740  C   VAL A 357    14405  14893  10649   -637    672   4102       C  
ATOM   2741  O   VAL A 357      23.998   2.469 -24.200  1.00105.92           O  
ANISOU 2741  O   VAL A 357    14641  15209  10393   -628    664   3980       O  
ATOM   2742  CB  VAL A 357      26.792   1.579 -23.026  1.00107.56           C  
ANISOU 2742  CB  VAL A 357    14933  15132  10803   -453    700   3749       C  
ATOM   2743  CG1 VAL A 357      28.203   1.171 -23.418  1.00111.85           C  
ANISOU 2743  CG1 VAL A 357    15350  15833  11316   -270    774   3714       C  
ATOM   2744  CG2 VAL A 357      26.709   1.884 -21.537  1.00105.32           C  
ANISOU 2744  CG2 VAL A 357    14765  14401  10850   -597    567   3604       C  
ATOM   2745  N   LEU A 358      24.549   4.046 -22.703  1.00105.28           N  
ANISOU 2745  N   LEU A 358    14303  14590  11108   -753    583   4119       N  
ATOM   2746  CA  LEU A 358      23.190   4.192 -22.202  1.00105.84           C  
ANISOU 2746  CA  LEU A 358    14423  14537  11253   -891    480   3875       C  
ATOM   2747  C   LEU A 358      22.378   5.255 -22.934  1.00108.43           C  
ANISOU 2747  C   LEU A 358    14482  14922  11795   -872    381   4137       C  
ATOM   2748  O   LEU A 358      21.299   5.618 -22.455  1.00112.29           O  
ANISOU 2748  O   LEU A 358    14900  15275  12489   -967    268   3894       O  
ATOM   2749  CB  LEU A 358      23.220   4.512 -20.706  1.00105.44           C  
ANISOU 2749  CB  LEU A 358    14386  14132  11544  -1048    421   3609       C  
ATOM   2750  CG  LEU A 358      23.831   3.445 -19.798  1.00103.70           C  
ANISOU 2750  CG  LEU A 358    14505  13789  11108  -1116    425   3332       C  
ATOM   2751  CD1 LEU A 358      23.864   3.925 -18.353  1.00103.96           C  
ANISOU 2751  CD1 LEU A 358    14526  13522  11453  -1306    358   3112       C  
ATOM   2752  CD2 LEU A 358      23.075   2.137 -19.922  1.00104.54           C  
ANISOU 2752  CD2 LEU A 358    14974  14025  10722  -1203    421   3047       C  
ATOM   2753  N   ASN A 359      22.859   5.759 -24.078  1.00116.50           N  
ANISOU 2753  N   ASN A 359    15348  16144  12771   -773    399   4608       N  
ATOM   2754  CA  ASN A 359      22.234   6.909 -24.754  1.00118.47           C  
ANISOU 2754  CA  ASN A 359    15365  16363  13286   -766    218   4961       C  
ATOM   2755  C   ASN A 359      21.999   8.048 -23.767  1.00119.80           C  
ANISOU 2755  C   ASN A 359    15301  16084  14134   -829     46   4894       C  
ATOM   2756  O   ASN A 359      21.080   8.857 -23.916  1.00125.08           O  
ANISOU 2756  O   ASN A 359    15791  16604  15130   -819   -191   4928       O  
ATOM   2757  CB  ASN A 359      20.917   6.515 -25.435  1.00122.30           C  
ANISOU 2757  CB  ASN A 359    15929  17061  13478   -735    106   4818       C  
ATOM   2758  CG  ASN A 359      20.356   7.620 -26.332  1.00125.08           C  
ANISOU 2758  CG  ASN A 359    16079  17400  14048   -696   -153   5247       C  
ATOM   2759  OD1 ASN A 359      20.993   8.654 -26.544  1.00124.33           O  
ANISOU 2759  OD1 ASN A 359    15815  17145  14281   -718   -241   5713       O  
ATOM   2760  ND2 ASN A 359      19.137   7.420 -26.821  1.00129.07           N  
ANISOU 2760  ND2 ASN A 359    16606  18035  14402   -651   -316   5082       N  
ATOM   2761  N   GLY A 360      22.814   8.112 -22.723  1.00111.52           N  
ANISOU 2761  N   GLY A 360    14235  14809  13329   -879    133   4746       N  
ATOM   2762  CA  GLY A 360      22.405   8.813 -21.531  1.00112.89           C  
ANISOU 2762  CA  GLY A 360    14240  14620  14032   -962      8   4434       C  
ATOM   2763  C   GLY A 360      23.532   9.546 -20.843  1.00114.04           C  
ANISOU 2763  C   GLY A 360    14217  14491  14623   -981     22   4570       C  
ATOM   2764  O   GLY A 360      24.690   9.516 -21.267  1.00113.16           O  
ANISOU 2764  O   GLY A 360    14106  14463  14427   -939    142   4907       O  
ATOM   2765  N   ASP A 361      23.152  10.244 -19.777  1.00113.56           N  
ANISOU 2765  N   ASP A 361    13965  14124  15060  -1055   -100   4253       N  
ATOM   2766  CA  ASP A 361      21.737  10.364 -19.404  1.00119.43           C  
ANISOU 2766  CA  ASP A 361    14621  14830  15925  -1116   -232   3811       C  
ATOM   2767  C   ASP A 361      21.600  11.640 -18.611  1.00123.22           C  
ANISOU 2767  C   ASP A 361    14721  14939  17156  -1138   -426   3640       C  
ATOM   2768  O   ASP A 361      22.470  12.508 -18.664  1.00121.69           O  
ANISOU 2768  O   ASP A 361    14342  14507  17390  -1085   -501   3993       O  
ATOM   2769  CB  ASP A 361      21.236   9.178 -18.562  1.00120.48           C  
ANISOU 2769  CB  ASP A 361    15042  15134  15601  -1283    -75   3255       C  
ATOM   2770  CG  ASP A 361      19.721   9.041 -18.602  1.00129.93           C  
ANISOU 2770  CG  ASP A 361    16177  16453  16739  -1360   -148   2843       C  
ATOM   2771  OD1 ASP A 361      19.075   9.857 -19.291  1.00133.71           O  
ANISOU 2771  OD1 ASP A 361    16383  16862  17559  -1232   -359   2974       O  
ATOM   2772  OD2 ASP A 361      19.173   8.129 -17.952  1.00132.08           O  
ANISOU 2772  OD2 ASP A 361    16669  16879  16637  -1564    -19   2389       O  
ATOM   2773  N   GLN A 362      20.495  11.772 -17.904  1.00127.39           N  
ANISOU 2773  N   GLN A 362    15101  15434  17868  -1228   -508   3066       N  
ATOM   2774  CA  GLN A 362      20.474  12.681 -16.774  1.00128.80           C  
ANISOU 2774  CA  GLN A 362    14949  15329  18661  -1297   -614   2680       C  
ATOM   2775  C   GLN A 362      20.184  11.947 -15.478  1.00128.30           C  
ANISOU 2775  C   GLN A 362    15024  15433  18292  -1552   -417   2029       C  
ATOM   2776  O   GLN A 362      20.773  12.270 -14.442  1.00124.97           O  
ANISOU 2776  O   GLN A 362    14514  14875  18095  -1652   -385   1820       O  
ATOM   2777  CB  GLN A 362      19.442  13.800 -16.985  1.00134.83           C  
ANISOU 2777  CB  GLN A 362    15278  15864  20087  -1191   -949   2494       C  
ATOM   2778  CG  GLN A 362      19.817  15.091 -16.265  1.00134.28           C  
ANISOU 2778  CG  GLN A 362    14797  15380  20845  -1157  -1155   2374       C  
ATOM   2779  CD  GLN A 362      19.525  15.066 -14.780  1.00133.64           C  
ANISOU 2779  CD  GLN A 362    14551  15348  20880  -1353  -1040   1581       C  
ATOM   2780  OE1 GLN A 362      18.573  14.431 -14.328  1.00133.22           O  
ANISOU 2780  OE1 GLN A 362    14536  15585  20497  -1519   -915   1004       O  
ATOM   2781  NE2 GLN A 362      20.368  15.744 -14.006  1.00131.49           N  
ANISOU 2781  NE2 GLN A 362    14094  14824  21041  -1372  -1068   1542       N  
ATOM   2782  N   HIS A 363      19.313  10.937 -15.520  1.00119.33           N  
ANISOU 2782  N   HIS A 363    14126  14603  16610  -1694   -288   1724       N  
ATOM   2783  CA  HIS A 363      19.045  10.131 -14.335  1.00115.75           C  
ANISOU 2783  CA  HIS A 363    13887  14337  15754  -2024    -95   1178       C  
ATOM   2784  C   HIS A 363      20.312   9.437 -13.853  1.00110.11           C  
ANISOU 2784  C   HIS A 363    13558  13597  14683  -2087     30   1419       C  
ATOM   2785  O   HIS A 363      20.728   9.600 -12.700  1.00107.55           O  
ANISOU 2785  O   HIS A 363    13221  13197  14446  -2260     56   1151       O  
ATOM   2786  CB  HIS A 363      17.955   9.102 -14.634  1.00116.90           C  
ANISOU 2786  CB  HIS A 363    14263  14803  15350  -2187     17    905       C  
ATOM   2787  CG  HIS A 363      16.630   9.702 -14.984  1.00120.67           C  
ANISOU 2787  CG  HIS A 363    14340  15337  16173  -2142   -120    540       C  
ATOM   2788  ND1 HIS A 363      16.267   9.996 -16.280  1.00125.44           N  
ANISOU 2788  ND1 HIS A 363    14831  15909  16924  -1853   -307    891       N  
ATOM   2789  CD2 HIS A 363      15.579  10.059 -14.208  1.00118.61           C  
ANISOU 2789  CD2 HIS A 363    13744  15179  16144  -2351   -121   -186       C  
ATOM   2790  CE1 HIS A 363      15.050  10.509 -16.289  1.00125.94           C  
ANISOU 2790  CE1 HIS A 363    14514  16003  17334  -1849   -459    409       C  
ATOM   2791  NE2 HIS A 363      14.610  10.558 -15.044  1.00121.76           N  
ANISOU 2791  NE2 HIS A 363    13815  15568  16880  -2145   -334   -282       N  
ATOM   2792  N   PHE A 364      20.942   8.650 -14.733  1.00112.05           N  
ANISOU 2792  N   PHE A 364    14129  13913  14530  -1938     84   1886       N  
ATOM   2793  CA  PHE A 364      22.141   7.915 -14.340  1.00105.79           C  
ANISOU 2793  CA  PHE A 364    13684  13079  13432  -1953    149   2064       C  
ATOM   2794  C   PHE A 364      23.254   8.862 -13.917  1.00104.08           C  
ANISOU 2794  C   PHE A 364    13214  12602  13728  -1836     77   2242       C  
ATOM   2795  O   PHE A 364      23.991   8.577 -12.966  1.00101.55           O  
ANISOU 2795  O   PHE A 364    13059  12202  13324  -1942     79   2117       O  
ATOM   2796  CB  PHE A 364      22.620   7.011 -15.479  1.00101.86           C  
ANISOU 2796  CB  PHE A 364    13472  12717  12514  -1764    201   2468       C  
ATOM   2797  CG  PHE A 364      21.696   5.861 -15.783  1.00102.26           C  
ANISOU 2797  CG  PHE A 364    13847  13002  12006  -1895    267   2270       C  
ATOM   2798  CD1 PHE A 364      21.645   4.759 -14.951  1.00 99.11           C  
ANISOU 2798  CD1 PHE A 364    13873  12630  11153  -2156    300   1996       C  
ATOM   2799  CD2 PHE A 364      20.910   5.869 -16.919  1.00105.64           C  
ANISOU 2799  CD2 PHE A 364    14175  13607  12358  -1772    266   2383       C  
ATOM   2800  CE1 PHE A 364      20.812   3.700 -15.233  1.00 98.85           C  
ANISOU 2800  CE1 PHE A 364    14143  12780  10633  -2308    350   1826       C  
ATOM   2801  CE2 PHE A 364      20.072   4.813 -17.206  1.00106.17           C  
ANISOU 2801  CE2 PHE A 364    14518  13887  11936  -1893    324   2176       C  
ATOM   2802  CZ  PHE A 364      20.023   3.728 -16.362  1.00102.63           C  
ANISOU 2802  CZ  PHE A 364    14478  13448  11070  -2168    377   1893       C  
ATOM   2803  N   MET A 365      23.396   9.991 -14.616  1.00101.71           N  
ANISOU 2803  N   MET A 365    12527  12152  13966  -1634    -18   2548       N  
ATOM   2804  CA  MET A 365      24.381  10.988 -14.208  1.00100.44           C  
ANISOU 2804  CA  MET A 365    12082  11716  14363  -1555    -95   2695       C  
ATOM   2805  C   MET A 365      24.113  11.469 -12.788  1.00102.58           C  
ANISOU 2805  C   MET A 365    12181  11872  14922  -1748   -145   2146       C  
ATOM   2806  O   MET A 365      25.043  11.610 -11.983  1.00100.39           O  
ANISOU 2806  O   MET A 365    11902  11468  14774  -1780   -153   2093       O  
ATOM   2807  CB  MET A 365      24.370  12.165 -15.182  1.00102.30           C  
ANISOU 2807  CB  MET A 365    11949  11773  15145  -1375   -235   3111       C  
ATOM   2808  CG  MET A 365      24.839  11.826 -16.585  1.00 99.07           C  
ANISOU 2808  CG  MET A 365    11679  11523  14439  -1230   -169   3701       C  
ATOM   2809  SD  MET A 365      26.553  11.283 -16.631  1.00 92.91           S  
ANISOU 2809  SD  MET A 365    11059  10802  13441  -1167     -3   3990       S  
ATOM   2810  CE  MET A 365      27.393  12.803 -16.199  1.00 94.24           C  
ANISOU 2810  CE  MET A 365    10785  10583  14439  -1158   -126   4165       C  
ATOM   2811  N   SER A 366      22.843  11.715 -12.458  1.00108.09           N  
ANISOU 2811  N   SER A 366    12707  12648  15713  -1885   -178   1684       N  
ATOM   2812  CA  SER A 366      22.504  12.134 -11.104  1.00108.16           C  
ANISOU 2812  CA  SER A 366    12517  12642  15935  -2114   -190   1067       C  
ATOM   2813  C   SER A 366      22.779  11.030 -10.091  1.00104.61           C  
ANISOU 2813  C   SER A 366    12520  12392  14835  -2409    -52    818       C  
ATOM   2814  O   SER A 366      23.169  11.319  -8.954  1.00102.97           O  
ANISOU 2814  O   SER A 366    12243  12141  14739  -2570    -69    509       O  
ATOM   2815  CB  SER A 366      21.041  12.570 -11.038  1.00110.99           C  
ANISOU 2815  CB  SER A 366    12551  13105  16514  -2208   -240    547       C  
ATOM   2816  OG  SER A 366      20.692  12.991  -9.731  1.00107.81           O  
ANISOU 2816  OG  SER A 366    11899  12760  16302  -2456   -222   -134       O  
ATOM   2817  N   ALA A 367      22.585   9.766 -10.478  1.00102.09           N  
ANISOU 2817  N   ALA A 367    12675  12274  13840  -2495     51    951       N  
ATOM   2818  CA  ALA A 367      22.931   8.658  -9.591  1.00 98.07           C  
ANISOU 2818  CA  ALA A 367    12671  11875  12715  -2775    102    818       C  
ATOM   2819  C   ALA A 367      24.430   8.630  -9.315  1.00 95.77           C  
ANISOU 2819  C   ALA A 367    12508  11367  12514  -2612      3   1128       C  
ATOM   2820  O   ALA A 367      24.862   8.446  -8.171  1.00 94.21           O  
ANISOU 2820  O   ALA A 367    12483  11149  12165  -2825    -52    906       O  
ATOM   2821  CB  ALA A 367      22.466   7.335 -10.200  1.00 95.77           C  
ANISOU 2821  CB  ALA A 367    12850  11766  11773  -2858    177    941       C  
ATOM   2822  N   LEU A 368      25.238   8.798 -10.365  1.00 84.61           N  
ANISOU 2822  N   LEU A 368    11005   9819  11322  -2254    -25   1624       N  
ATOM   2823  CA  LEU A 368      26.679   8.964 -10.203  1.00 84.32           C  
ANISOU 2823  CA  LEU A 368    10952   9587  11500  -2069   -108   1874       C  
ATOM   2824  C   LEU A 368      26.996  10.080  -9.216  1.00 85.32           C  
ANISOU 2824  C   LEU A 368    10710   9545  12164  -2129   -185   1622       C  
ATOM   2825  O   LEU A 368      27.814   9.910  -8.302  1.00 85.66           O  
ANISOU 2825  O   LEU A 368    10886   9505  12155  -2194   -275   1510       O  
ATOM   2826  CB  LEU A 368      27.310   9.248 -11.569  1.00 83.82           C  
ANISOU 2826  CB  LEU A 368    10704   9478  11666  -1738    -73   2388       C  
ATOM   2827  CG  LEU A 368      28.796   9.582 -11.686  1.00 83.78           C  
ANISOU 2827  CG  LEU A 368    10550   9312  11971  -1530   -112   2668       C  
ATOM   2828  CD1 LEU A 368      29.657   8.464 -11.172  1.00 83.89           C  
ANISOU 2828  CD1 LEU A 368    10964   9324  11588  -1518   -192   2596       C  
ATOM   2829  CD2 LEU A 368      29.132   9.875 -13.136  1.00 83.66           C  
ANISOU 2829  CD2 LEU A 368    10341   9362  12083  -1313    -20   3149       C  
ATOM   2830  N   ASP A 369      26.335  11.230  -9.382  1.00 88.06           N  
ANISOU 2830  N   ASP A 369    10583   9824  13052  -2100   -190   1501       N  
ATOM   2831  CA  ASP A 369      26.603  12.378  -8.522  1.00 89.40           C  
ANISOU 2831  CA  ASP A 369    10335   9807  13827  -2128   -284   1223       C  
ATOM   2832  C   ASP A 369      26.251  12.083  -7.070  1.00 89.37           C  
ANISOU 2832  C   ASP A 369    10470   9965  13523  -2476   -278    636       C  
ATOM   2833  O   ASP A 369      26.981  12.480  -6.155  1.00 89.13           O  
ANISOU 2833  O   ASP A 369    10336   9830  13698  -2520   -362    461       O  
ATOM   2834  CB  ASP A 369      25.833  13.598  -9.028  1.00 92.26           C  
ANISOU 2834  CB  ASP A 369    10176  10026  14852  -2020   -356   1167       C  
ATOM   2835  CG  ASP A 369      26.380  14.127 -10.341  1.00 92.23           C  
ANISOU 2835  CG  ASP A 369    10012   9819  15213  -1732   -410   1808       C  
ATOM   2836  OD1 ASP A 369      27.602  14.004 -10.573  1.00 89.15           O  
ANISOU 2836  OD1 ASP A 369     9706   9344  14822  -1617   -385   2184       O  
ATOM   2837  OD2 ASP A 369      25.587  14.657 -11.146  1.00 95.44           O  
ANISOU 2837  OD2 ASP A 369    10208  10167  15889  -1643   -487   1928       O  
ATOM   2838  N   LYS A 370      25.135  11.392  -6.835  1.00 86.74           N  
ANISOU 2838  N   LYS A 370    10366   9914  12676  -2760   -175    316       N  
ATOM   2839  CA  LYS A 370      24.762  11.041  -5.469  1.00 85.31           C  
ANISOU 2839  CA  LYS A 370    10361   9963  12091  -3189   -139   -225       C  
ATOM   2840  C   LYS A 370      25.765  10.066  -4.867  1.00 84.25           C  
ANISOU 2840  C   LYS A 370    10781   9802  11429  -3292   -230    -28       C  
ATOM   2841  O   LYS A 370      26.205  10.232  -3.721  1.00 84.93           O  
ANISOU 2841  O   LYS A 370    10894   9906  11468  -3488   -313   -299       O  
ATOM   2842  CB  LYS A 370      23.357  10.442  -5.456  1.00 84.09           C  
ANISOU 2842  CB  LYS A 370    10346  10143  11461  -3518     18   -574       C  
ATOM   2843  CG  LYS A 370      22.253  11.396  -5.880  1.00 85.93           C  
ANISOU 2843  CG  LYS A 370     9999  10419  12232  -3439     55   -916       C  
ATOM   2844  CD  LYS A 370      20.915  10.675  -5.907  1.00 84.70           C  
ANISOU 2844  CD  LYS A 370     9993  10627  11564  -3771    223  -1277       C  
ATOM   2845  CE  LYS A 370      19.794  11.564  -6.412  1.00 86.85           C  
ANISOU 2845  CE  LYS A 370     9672  10927  12398  -3642    207  -1645       C  
ATOM   2846  NZ  LYS A 370      18.502  10.820  -6.477  1.00 85.62           N  
ANISOU 2846  NZ  LYS A 370     9637  11150  11746  -3967    382  -2028       N  
ATOM   2847  N   ALA A 371      26.141   9.040  -5.635  1.00 87.30           N  
ANISOU 2847  N   ALA A 371    11601  10139  11429  -3150   -253    420       N  
ATOM   2848  CA  ALA A 371      27.074   8.032  -5.143  1.00 86.11           C  
ANISOU 2848  CA  ALA A 371    11991   9905  10821  -3202   -419    599       C  
ATOM   2849  C   ALA A 371      28.400   8.667  -4.745  1.00 87.76           C  
ANISOU 2849  C   ALA A 371    11987   9873  11486  -2964   -582    693       C  
ATOM   2850  O   ALA A 371      28.832   8.568  -3.589  1.00 87.44           O  
ANISOU 2850  O   ALA A 371    12121   9827  11276  -3172   -731    475       O  
ATOM   2851  CB  ALA A 371      27.283   6.952  -6.207  1.00 84.42           C  
ANISOU 2851  CB  ALA A 371    12155   9643  10277  -2997   -439   1016       C  
ATOM   2852  N   LEU A 372      29.056   9.343  -5.693  1.00 80.35           N  
ANISOU 2852  N   LEU A 372    10664   8750  11116  -2558   -560   1014       N  
ATOM   2853  CA  LEU A 372      30.302  10.023  -5.366  1.00 81.62           C  
ANISOU 2853  CA  LEU A 372    10554   8688  11770  -2348   -689   1080       C  
ATOM   2854  C   LEU A 372      30.101  11.110  -4.319  1.00 82.74           C  
ANISOU 2854  C   LEU A 372    10309   8820  12310  -2520   -713    644       C  
ATOM   2855  O   LEU A 372      31.065  11.496  -3.651  1.00 83.89           O  
ANISOU 2855  O   LEU A 372    10332   8821  12721  -2455   -858    568       O  
ATOM   2856  CB  LEU A 372      30.928  10.605  -6.631  1.00 80.79           C  
ANISOU 2856  CB  LEU A 372    10083   8435  12178  -1971   -615   1506       C  
ATOM   2857  CG  LEU A 372      31.423   9.547  -7.615  1.00 80.35           C  
ANISOU 2857  CG  LEU A 372    10347   8420  11762  -1768   -602   1876       C  
ATOM   2858  CD1 LEU A 372      31.912  10.189  -8.899  1.00 79.81           C  
ANISOU 2858  CD1 LEU A 372     9891   8305  12126  -1489   -474   2278       C  
ATOM   2859  CD2 LEU A 372      32.522   8.723  -6.972  1.00 81.86           C  
ANISOU 2859  CD2 LEU A 372    10873   8510  11720  -1710   -825   1837       C  
ATOM   2860  N   THR A 373      28.870  11.605  -4.159  1.00 86.55           N  
ANISOU 2860  N   THR A 373    10562   9463  12859  -2729   -586    300       N  
ATOM   2861  CA  THR A 373      28.577  12.504  -3.048  1.00 87.08           C  
ANISOU 2861  CA  THR A 373    10272   9587  13227  -2939   -611   -251       C  
ATOM   2862  C   THR A 373      28.739  11.785  -1.717  1.00 87.92           C  
ANISOU 2862  C   THR A 373    10809   9892  12703  -3313   -700   -558       C  
ATOM   2863  O   THR A 373      29.270  12.354  -0.755  1.00 89.20           O  
ANISOU 2863  O   THR A 373    10783  10026  13083  -3382   -813   -851       O  
ATOM   2864  CB  THR A 373      27.162  13.070  -3.176  1.00 86.23           C  
ANISOU 2864  CB  THR A 373     9814   9649  13300  -3085   -470   -643       C  
ATOM   2865  OG1 THR A 373      27.048  13.817  -4.392  1.00 85.39           O  
ANISOU 2865  OG1 THR A 373     9324   9307  13815  -2736   -470   -316       O  
ATOM   2866  CG2 THR A 373      26.833  13.970  -1.994  1.00 86.69           C  
ANISOU 2866  CG2 THR A 373     9454   9814  13671  -3309   -492  -1327       C  
ATOM   2867  N   SER A 374      28.295  10.527  -1.646  1.00 84.78           N  
ANISOU 2867  N   SER A 374    11014   9687  11512  -3579   -678   -479       N  
ATOM   2868  CA  SER A 374      28.439   9.759  -0.414  1.00 85.66           C  
ANISOU 2868  CA  SER A 374    11636   9967  10946  -3995   -812   -680       C  
ATOM   2869  C   SER A 374      29.838   9.179  -0.237  1.00 86.92           C  
ANISOU 2869  C   SER A 374    12162   9855  11007  -3781  -1116   -324       C  
ATOM   2870  O   SER A 374      30.217   8.849   0.892  1.00 88.47           O  
ANISOU 2870  O   SER A 374    12682  10113  10821  -4057  -1321   -489       O  
ATOM   2871  CB  SER A 374      27.408   8.631  -0.370  1.00 84.45           C  
ANISOU 2871  CB  SER A 374    12014  10086   9987  -4422   -707   -718       C  
ATOM   2872  OG  SER A 374      27.535   7.879   0.824  1.00 85.69           O  
ANISOU 2872  OG  SER A 374    12724  10395   9440  -4896   -868   -850       O  
ATOM   2873  N   VAL A 375      30.609   9.054  -1.320  1.00 79.96           N  
ANISOU 2873  N   VAL A 375    11222   8703  10456  -3310  -1164    129       N  
ATOM   2874  CA  VAL A 375      31.954   8.491  -1.219  1.00 80.19           C  
ANISOU 2874  CA  VAL A 375    11528   8482  10459  -3064  -1465    393       C  
ATOM   2875  C   VAL A 375      32.890   9.436  -0.476  1.00 81.65           C  
ANISOU 2875  C   VAL A 375    11328   8539  11156  -2945  -1607    198       C  
ATOM   2876  O   VAL A 375      33.715   9.003   0.338  1.00 83.30           O  
ANISOU 2876  O   VAL A 375    11841   8653  11156  -2979  -1920    162       O  
ATOM   2877  CB  VAL A 375      32.496   8.162  -2.622  1.00 78.17           C  
ANISOU 2877  CB  VAL A 375    11214   8052  10436  -2615  -1424    835       C  
ATOM   2878  CG1 VAL A 375      33.955   7.732  -2.546  1.00 78.94           C  
ANISOU 2878  CG1 VAL A 375    11443   7901  10648  -2311  -1730   1000       C  
ATOM   2879  CG2 VAL A 375      31.657   7.085  -3.273  1.00 77.08           C  
ANISOU 2879  CG2 VAL A 375    11514   8030   9741  -2731  -1341    997       C  
ATOM   2880  N   VAL A 376      32.767  10.739  -0.727  1.00 80.26           N  
ANISOU 2880  N   VAL A 376    10487   8334  11675  -2808  -1423     60       N  
ATOM   2881  CA  VAL A 376      33.807  11.703  -0.380  1.00 81.38           C  
ANISOU 2881  CA  VAL A 376    10172   8275  12472  -2587  -1540    -33       C  
ATOM   2882  C   VAL A 376      33.665  12.143   1.074  1.00 83.93           C  
ANISOU 2882  C   VAL A 376    10439   8749  12703  -2913  -1650   -556       C  
ATOM   2883  O   VAL A 376      34.358  13.060   1.530  1.00 85.29           O  
ANISOU 2883  O   VAL A 376    10181   8790  13435  -2788  -1741   -753       O  
ATOM   2884  CB  VAL A 376      33.756  12.905  -1.341  1.00 80.67           C  
ANISOU 2884  CB  VAL A 376     9419   8031  13199  -2319  -1337     98       C  
ATOM   2885  CG1 VAL A 376      32.540  13.774  -1.045  1.00 81.54           C  
ANISOU 2885  CG1 VAL A 376     9169   8281  13533  -2542  -1181   -303       C  
ATOM   2886  CG2 VAL A 376      35.063  13.697  -1.322  1.00 81.69           C  
ANISOU 2886  CG2 VAL A 376     9131   7894  14014  -2038  -1455    168       C  
ATOM   2887  N   ASN A 377      32.783  11.486   1.821  1.00 96.09           N  
ANISOU 2887  N   ASN A 377    12407  10589  13513  -3367  -1638   -802       N  
ATOM   2888  CA  ASN A 377      32.552  11.818   3.224  1.00 97.56           C  
ANISOU 2888  CA  ASN A 377    12577  11028  13464  -3768  -1711  -1335       C  
ATOM   2889  C   ASN A 377      32.712  10.555   4.062  1.00 97.80           C  
ANISOU 2889  C   ASN A 377    13406  11185  12568  -4125  -1974  -1259       C  
ATOM   2890  O   ASN A 377      31.865   9.657   4.012  1.00 96.02           O  
ANISOU 2890  O   ASN A 377    13665  11155  11664  -4466  -1892  -1181       O  
ATOM   2891  CB  ASN A 377      31.172  12.448   3.414  1.00 95.26           C  
ANISOU 2891  CB  ASN A 377    11928  11064  13204  -4087  -1407  -1825       C  
ATOM   2892  CG  ASN A 377      31.050  13.795   2.722  1.00 94.98           C  
ANISOU 2892  CG  ASN A 377    11100  10828  14162  -3737  -1261  -1933       C  
ATOM   2893  OD1 ASN A 377      30.291  13.953   1.764  1.00 94.05           O  
ANISOU 2893  OD1 ASN A 377    10797  10682  14256  -3623  -1073  -1805       O  
ATOM   2894  ND2 ASN A 377      31.802  14.774   3.207  1.00 96.00           N  
ANISOU 2894  ND2 ASN A 377    10769  10791  14917  -3573  -1388  -2159       N  
ATOM   2895  N   TYR A 378      33.800  10.490   4.825  1.00108.34           N  
ANISOU 2895  N   TYR A 378    14887  12384  13892  -4058  -2323  -1270       N  
ATOM   2896  CA  TYR A 378      34.105   9.334   5.656  1.00110.77           C  
ANISOU 2896  CA  TYR A 378    15982  12728  13378  -4366  -2693  -1147       C  
ATOM   2897  C   TYR A 378      33.527   9.513   7.053  1.00114.67           C  
ANISOU 2897  C   TYR A 378    16609  13652  13310  -4991  -2698  -1635       C  
ATOM   2898  O   TYR A 378      33.561  10.609   7.617  1.00116.04           O  
ANISOU 2898  O   TYR A 378    16215  13978  13896  -5014  -2597  -2103       O  
ATOM   2899  CB  TYR A 378      35.617   9.123   5.744  1.00111.38           C  
ANISOU 2899  CB  TYR A 378    16159  12426  13734  -3947  -3136   -918       C  
ATOM   2900  N   ARG A 379      32.997   8.422   7.612  1.00133.15           N  
ANISOU 2900  N   ARG A 379    19701  16197  14691  -5530  -2823  -1535       N  
ATOM   2901  CA  ARG A 379      32.468   8.416   8.977  1.00133.56           C  
ANISOU 2901  CA  ARG A 379    19997  16727  14021  -6237  -2840  -1954       C  
ATOM   2902  C   ARG A 379      33.122   7.226   9.678  1.00132.39           C  
ANISOU 2902  C   ARG A 379    20694  16432  13176  -6353  -3320  -1528       C  
ATOM   2903  O   ARG A 379      32.506   6.167   9.823  1.00130.86           O  
ANISOU 2903  O   ARG A 379    21067  16343  12310  -6630  -3250  -1204       O  
ATOM   2904  CB  ARG A 379      30.938   8.288   8.954  1.00132.47           C  
ANISOU 2904  CB  ARG A 379    19776  17061  13495  -6584  -2295  -2138       C  
ATOM   2905  CG  ARG A 379      30.209   9.340   8.121  1.00132.48           C  
ANISOU 2905  CG  ARG A 379    18986  17140  14212  -6424  -1883  -2517       C  
ATOM   2906  CD  ARG A 379      28.711   9.044   8.068  1.00129.97           C  
ANISOU 2906  CD  ARG A 379    18644  17255  13483  -6697  -1407  -2658       C  
ATOM   2907  NE  ARG A 379      27.982   9.949   7.181  1.00127.30           N  
ANISOU 2907  NE  ARG A 379    17592  16933  13842  -6480  -1083  -2972       N  
ATOM   2908  CZ  ARG A 379      27.744   9.703   5.894  1.00122.69           C  
ANISOU 2908  CZ  ARG A 379    17020  16094  13501  -6324  -1030  -2693       C  
ATOM   2909  NH1 ARG A 379      28.178   8.579   5.341  1.00119.63           N  
ANISOU 2909  NH1 ARG A 379    17284  15418  12750  -6226  -1240  -2075       N  
ATOM   2910  NH2 ARG A 379      27.072  10.580   5.159  1.00120.46           N  
ANISOU 2910  NH2 ARG A 379    16060  15820  13888  -6093   -761  -2961       N  
ATOM   2911  N   GLU A 380      34.370   7.395  10.116  1.00110.37           N  
ANISOU 2911  N   GLU A 380    17952  13363  10619  -6115  -3812  -1506       N  
ATOM   2912  CA  GLU A 380      35.067   6.224  10.636  1.00113.53           C  
ANISOU 2912  CA  GLU A 380    19131  13513  10494  -6104  -4332  -1046       C  
ATOM   2913  C   GLU A 380      34.810   5.961  12.120  1.00119.58           C  
ANISOU 2913  C   GLU A 380    20196  14673  10566  -6545  -4313  -1112       C  
ATOM   2914  O   GLU A 380      34.449   4.834  12.481  1.00122.65           O  
ANISOU 2914  O   GLU A 380    21243  15047  10310  -6848  -4378   -699       O  
ATOM   2915  CB  GLU A 380      36.566   6.329  10.343  1.00112.63           C  
ANISOU 2915  CB  GLU A 380    18965  12856  10972  -5550  -4922   -927       C  
ATOM   2916  CG  GLU A 380      36.888   6.211   8.865  1.00107.78           C  
ANISOU 2916  CG  GLU A 380    18046  11847  11060  -4883  -4776   -618       C  
ATOM   2917  CD  GLU A 380      38.373   6.243   8.587  1.00107.62           C  
ANISOU 2917  CD  GLU A 380    17838  11364  11688  -4215  -5200   -491       C  
ATOM   2918  OE1 GLU A 380      39.152   6.496   9.531  1.00110.89           O  
ANISOU 2918  OE1 GLU A 380    18274  11746  12112  -4218  -5593   -675       O  
ATOM   2919  OE2 GLU A 380      38.761   6.001   7.424  1.00104.58           O  
ANISOU 2919  OE2 GLU A 380    17269  10679  11788  -3701  -5140   -240       O  
ATOM   2920  N   PRO A 381      34.974   6.948  13.019  1.00119.09           N  
ANISOU 2920  N   PRO A 381    19669  14940  10639  -6627  -4229  -1611       N  
ATOM   2921  CA  PRO A 381      34.758   6.505  14.397  1.00125.51           C  
ANISOU 2921  CA  PRO A 381    20882  16097  10710  -7078  -4260  -1578       C  
ATOM   2922  C   PRO A 381      33.468   7.044  14.999  1.00127.82           C  
ANISOU 2922  C   PRO A 381    20800  17058  10708  -7542  -3622  -2022       C  
ATOM   2923  O   PRO A 381      33.568   7.793  15.971  1.00131.32           O  
ANISOU 2923  O   PRO A 381    20908  17850  11138  -7657  -3569  -2473       O  
ATOM   2924  CB  PRO A 381      35.967   7.083  15.129  1.00127.83           C  
ANISOU 2924  CB  PRO A 381    21005  16289  11275  -6836  -4712  -1809       C  
ATOM   2925  CG  PRO A 381      36.187   8.378  14.429  1.00123.24           C  
ANISOU 2925  CG  PRO A 381    19576  15651  11599  -6475  -4543  -2297       C  
ATOM   2926  CD  PRO A 381      35.796   8.172  12.978  1.00117.53           C  
ANISOU 2926  CD  PRO A 381    18795  14636  11225  -6280  -4359  -2052       C  
ATOM   2927  N   SER A 383      38.260  11.443  10.157  1.00126.49           N  
ANISOU 2927  N   SER A 383    17396  14597  16066  -4223  -4147  -2351       N  
ATOM   2928  CA  SER A 383      37.652  11.590  11.475  1.00130.29           C  
ANISOU 2928  CA  SER A 383    18048  15568  15888  -4847  -4164  -2816       C  
ATOM   2929  C   SER A 383      37.721  13.028  11.990  1.00132.82           C  
ANISOU 2929  C   SER A 383    17538  16059  16868  -4803  -3983  -3450       C  
ATOM   2930  O   SER A 383      38.609  13.355  12.778  1.00135.56           O  
ANISOU 2930  O   SER A 383    17788  16370  17349  -4724  -4319  -3673       O  
ATOM   2931  CB  SER A 383      38.327  10.656  12.482  1.00131.38           C  
ANISOU 2931  CB  SER A 383    18964  15694  15261  -5086  -4773  -2663       C  
ATOM   2932  OG  SER A 383      37.811  10.864  13.785  1.00131.37           O  
ANISOU 2932  OG  SER A 383    19090  16227  14599  -5702  -4765  -3117       O  
ATOM   2933  N   VAL A 384      36.800  13.892  11.564  1.00126.12           N  
ANISOU 2933  N   VAL A 384    16079  15373  16467  -4838  -3497  -3771       N  
ATOM   2934  CA  VAL A 384      35.736  13.584  10.612  1.00123.86           C  
ANISOU 2934  CA  VAL A 384    15846  15131  16085  -4902  -3115  -3551       C  
ATOM   2935  C   VAL A 384      35.409  14.910   9.911  1.00123.58           C  
ANISOU 2935  C   VAL A 384    14892  14966  17096  -4576  -2767  -3828       C  
ATOM   2936  O   VAL A 384      35.280  15.939  10.575  1.00123.99           O  
ANISOU 2936  O   VAL A 384    14375  15192  17542  -4666  -2701  -4442       O  
ATOM   2937  CB  VAL A 384      34.493  12.937  11.321  1.00123.69           C  
ANISOU 2937  CB  VAL A 384    16308  15682  15007  -5649  -2949  -3792       C  
ATOM   2938  CG1 VAL A 384      33.869  13.884  12.339  1.00126.46           C  
ANISOU 2938  CG1 VAL A 384    16145  16501  15403  -5861  -2708  -4498       C  
ATOM   2939  CG2 VAL A 384      33.453  12.451  10.315  1.00119.67           C  
ANISOU 2939  CG2 VAL A 384    15929  15195  14348  -5706  -2605  -3525       C  
ATOM   2940  N   CYS A 385      35.309  14.917   8.581  1.00115.44           N  
ANISOU 2940  N   CYS A 385    12940  11671  19251   -177  -4213   2669       N  
ATOM   2941  CA  CYS A 385      35.419  13.724   7.750  1.00113.90           C  
ANISOU 2941  CA  CYS A 385    12515  11205  19557    -74  -4471   2597       C  
ATOM   2942  C   CYS A 385      36.664  13.722   6.868  1.00113.14           C  
ANISOU 2942  C   CYS A 385    12308  10901  19779     63  -4465   2228       C  
ATOM   2943  O   CYS A 385      36.646  13.137   5.787  1.00112.05           O  
ANISOU 2943  O   CYS A 385    12041  10586  19946    208  -4490   2011       O  
ATOM   2944  CB  CYS A 385      34.178  13.586   6.866  1.00112.77           C  
ANISOU 2944  CB  CYS A 385    12388  11091  19367     57  -4320   2564       C  
ATOM   2945  SG  CYS A 385      33.999  14.884   5.620  1.00111.83           S  
ANISOU 2945  SG  CYS A 385    12437  11079  18973    256  -3834   2182       S  
ATOM   2946  N   LYS A 386      37.704  14.445   7.296  1.00108.87           N  
ANISOU 2946  N   LYS A 386    11830  10402  19133      9  -4401   2141       N  
ATOM   2947  CA  LYS A 386      39.064  14.392   6.752  1.00108.56           C  
ANISOU 2947  CA  LYS A 386    11651  10174  19422     89  -4447   1852       C  
ATOM   2948  C   LYS A 386      39.138  14.721   5.262  1.00107.37           C  
ANISOU 2948  C   LYS A 386    11492   9987  19316    299  -4164   1435       C  
ATOM   2949  O   LYS A 386      40.223  14.680   4.675  1.00107.34           O  
ANISOU 2949  O   LYS A 386    11358   9847  19579    373  -4156   1152       O  
ATOM   2950  CB  LYS A 386      39.721  13.023   7.012  1.00108.66           C  
ANISOU 2950  CB  LYS A 386    11371   9887  20026     37  -4902   1963       C  
ATOM   2951  CG  LYS A 386      39.241  11.864   6.139  1.00107.66           C  
ANISOU 2951  CG  LYS A 386    11052   9538  20317    162  -5054   1870       C  
ATOM   2952  CD  LYS A 386      39.918  10.551   6.479  1.00110.26           C  
ANISOU 2952  CD  LYS A 386    11081   9541  21273    108  -5526   1988       C  
ATOM   2953  CE  LYS A 386      39.309   9.408   5.677  1.00111.10           C  
ANISOU 2953  CE  LYS A 386    11021   9425  21765    220  -5683   1908       C  
ATOM   2954  NZ  LYS A 386      39.545   9.547   4.213  1.00110.19           N  
ANISOU 2954  NZ  LYS A 386    10872   9234  21762    435  -5397   1409       N  
ATOM   2955  N   ALA A 387      38.006  15.045   4.640  1.00104.80           N  
ANISOU 2955  N   ALA A 387    11294   9789  18738    375  -3935   1401       N  
ATOM   2956  CA  ALA A 387      37.972  15.400   3.224  1.00103.92           C  
ANISOU 2956  CA  ALA A 387    11199   9674  18611    525  -3674   1041       C  
ATOM   2957  C   ALA A 387      38.352  16.859   2.968  1.00104.24           C  
ANISOU 2957  C   ALA A 387    11430   9904  18272    546  -3331    855       C  
ATOM   2958  O   ALA A 387      39.208  17.126   2.109  1.00104.21           O  
ANISOU 2958  O   ALA A 387    11373   9857  18365    612  -3211    531       O  
ATOM   2959  CB  ALA A 387      36.591  15.105   2.634  1.00103.03           C  
ANISOU 2959  CB  ALA A 387    11133   9600  18413    572  -3615   1117       C  
ATOM   2960  N   PRO A 388      37.759  17.833   3.676  1.00 96.84           N  
ANISOU 2960  N   PRO A 388    10709   9176  16911    487  -3163   1037       N  
ATOM   2961  CA  PRO A 388      38.039  19.234   3.319  1.00 97.21           C  
ANISOU 2961  CA  PRO A 388    10936   9376  16625    517  -2845    850       C  
ATOM   2962  C   PRO A 388      39.486  19.644   3.535  1.00 97.83           C  
ANISOU 2962  C   PRO A 388    10988   9422  16760    480  -2864    699       C  
ATOM   2963  O   PRO A 388      40.052  20.340   2.685  1.00 97.46           O  
ANISOU 2963  O   PRO A 388    10972   9412  16649    535  -2672    427       O  
ATOM   2964  CB  PRO A 388      37.079  20.020   4.222  1.00 98.13           C  
ANISOU 2964  CB  PRO A 388    11257   9683  16346    455  -2704   1095       C  
ATOM   2965  CG  PRO A 388      36.831  19.131   5.375  1.00 98.67           C  
ANISOU 2965  CG  PRO A 388    11255   9723  16511    336  -2974   1408       C  
ATOM   2966  CD  PRO A 388      36.829  17.748   4.819  1.00 97.54           C  
ANISOU 2966  CD  PRO A 388    10882   9376  16803    381  -3238   1401       C  
ATOM   2967  N   GLU A 389      40.103  19.237   4.647  1.00 99.21           N  
ANISOU 2967  N   GLU A 389    11104   9537  17054    367  -3106    889       N  
ATOM   2968  CA  GLU A 389      41.491  19.617   4.889  1.00 99.94           C  
ANISOU 2968  CA  GLU A 389    11161   9590  17223    319  -3148    778       C  
ATOM   2969  C   GLU A 389      42.410  19.073   3.804  1.00 99.22           C  
ANISOU 2969  C   GLU A 389    10837   9329  17532    424  -3181    464       C  
ATOM   2970  O   GLU A 389      43.287  19.790   3.308  1.00 99.48           O  
ANISOU 2970  O   GLU A 389    10882   9403  17514    448  -3025    231       O  
ATOM   2971  CB  GLU A 389      41.951  19.131   6.262  1.00101.09           C  
ANISOU 2971  CB  GLU A 389    11261   9679  17468    147  -3456   1076       C  
ATOM   2972  CG  GLU A 389      43.369  19.571   6.598  1.00101.75           C  
ANISOU 2972  CG  GLU A 389    11316   9722  17622     74  -3521   1007       C  
ATOM   2973  CD  GLU A 389      43.810  19.147   7.983  1.00103.14           C  
ANISOU 2973  CD  GLU A 389    11466   9851  17870   -139  -3848   1338       C  
ATOM   2974  OE1 GLU A 389      43.014  18.488   8.686  1.00103.77           O  
ANISOU 2974  OE1 GLU A 389    11548   9944  17938   -240  -4025   1620       O  
ATOM   2975  OE2 GLU A 389      44.953  19.474   8.368  1.00103.67           O  
ANISOU 2975  OE2 GLU A 389    11511   9879  18001   -228  -3940   1334       O  
ATOM   2976  N   LEU A 390      42.229  17.805   3.426  1.00105.14           N  
ANISOU 2976  N   LEU A 390    11369   9891  18690    480  -3380    444       N  
ATOM   2977  CA  LEU A 390      43.016  17.248   2.331  1.00104.91           C  
ANISOU 2977  CA  LEU A 390    11111   9701  19051    585  -3374     95       C  
ATOM   2978  C   LEU A 390      42.774  18.015   1.041  1.00104.59           C  
ANISOU 2978  C   LEU A 390    11179   9804  18754    663  -3025   -215       C  
ATOM   2979  O   LEU A 390      43.711  18.272   0.274  1.00105.00           O  
ANISOU 2979  O   LEU A 390    11139   9851  18904    699  -2895   -527       O  
ATOM   2980  CB  LEU A 390      42.689  15.768   2.142  1.00104.56           C  
ANISOU 2980  CB  LEU A 390    10838   9418  19471    632  -3640    122       C  
ATOM   2981  CG  LEU A 390      43.127  14.869   3.294  1.00105.17           C  
ANISOU 2981  CG  LEU A 390    10742   9304  19913    539  -4045    413       C  
ATOM   2982  CD1 LEU A 390      42.679  13.433   3.054  1.00106.30           C  
ANISOU 2982  CD1 LEU A 390    10670   9201  20518    586  -4318    448       C  
ATOM   2983  CD2 LEU A 390      44.635  14.954   3.482  1.00106.20           C  
ANISOU 2983  CD2 LEU A 390    10701   9317  20332    522  -4129    289       C  
ATOM   2984  N   LEU A 391      41.526  18.408   0.790  1.00 96.78           N  
ANISOU 2984  N   LEU A 391    10379   8954  17439    673  -2877   -120       N  
ATOM   2985  CA  LEU A 391      41.253  19.198  -0.400  1.00 95.40           C  
ANISOU 2985  CA  LEU A 391    10319   8921  17008    709  -2578   -364       C  
ATOM   2986  C   LEU A 391      41.734  20.639  -0.270  1.00 94.17           C  
ANISOU 2986  C   LEU A 391    10344   8946  16490    665  -2364   -404       C  
ATOM   2987  O   LEU A 391      41.674  21.384  -1.254  1.00 93.23           O  
ANISOU 2987  O   LEU A 391    10310   8947  16164    668  -2136   -600       O  
ATOM   2988  CB  LEU A 391      39.760  19.130  -0.715  1.00 94.35           C  
ANISOU 2988  CB  LEU A 391    10305   8851  16693    725  -2520   -219       C  
ATOM   2989  CG  LEU A 391      39.437  17.678  -1.081  1.00 95.77           C  
ANISOU 2989  CG  LEU A 391    10292   8835  17262    765  -2733   -246       C  
ATOM   2990  CD1 LEU A 391      37.960  17.416  -1.260  1.00 95.06           C  
ANISOU 2990  CD1 LEU A 391    10289   8778  17050    768  -2741    -47       C  
ATOM   2991  CD2 LEU A 391      40.192  17.296  -2.331  1.00 96.80           C  
ANISOU 2991  CD2 LEU A 391    10273   8884  17623    802  -2656   -658       C  
ATOM   2992  N   ALA A 392      42.223  21.040   0.904  1.00 94.35           N  
ANISOU 2992  N   ALA A 392    10429   8989  16432    603  -2450   -218       N  
ATOM   2993  CA  ALA A 392      42.904  22.320   1.061  1.00 93.59           C  
ANISOU 2993  CA  ALA A 392    10481   9025  16054    554  -2288   -279       C  
ATOM   2994  C   ALA A 392      44.408  22.187   0.861  1.00 94.84           C  
ANISOU 2994  C   ALA A 392    10460   9106  16470    542  -2346   -482       C  
ATOM   2995  O   ALA A 392      45.028  23.056   0.237  1.00 94.34           O  
ANISOU 2995  O   ALA A 392    10442   9147  16253    528  -2163   -681       O  
ATOM   2996  CB  ALA A 392      42.611  22.916   2.440  1.00 93.32           C  
ANISOU 2996  CB  ALA A 392    10638   9067  15751    469  -2329     16       C  
ATOM   2997  N   LYS A 393      45.009  21.111   1.381  1.00 96.68           N  
ANISOU 2997  N   LYS A 393    10470   9150  17112    538  -2611   -421       N  
ATOM   2998  CA  LYS A 393      46.424  20.852   1.144  1.00 98.27           C  
ANISOU 2998  CA  LYS A 393    10443   9245  17650    542  -2677   -621       C  
ATOM   2999  C   LYS A 393      46.707  20.387  -0.275  1.00 98.95           C  
ANISOU 2999  C   LYS A 393    10339   9290  17969    632  -2539  -1007       C  
ATOM   3000  O   LYS A 393      47.872  20.382  -0.682  1.00100.24           O  
ANISOU 3000  O   LYS A 393    10318   9413  18353    640  -2502  -1240       O  
ATOM   3001  CB  LYS A 393      46.962  19.818   2.134  1.00100.38           C  
ANISOU 3001  CB  LYS A 393    10504   9292  18342    503  -3032   -420       C  
ATOM   3002  CG  LYS A 393      47.017  20.298   3.573  1.00100.33           C  
ANISOU 3002  CG  LYS A 393    10669   9341  18113    358  -3184    -62       C  
ATOM   3003  CD  LYS A 393      47.915  21.525   3.703  1.00 99.79           C  
ANISOU 3003  CD  LYS A 393    10728   9403  17786    290  -3043   -126       C  
ATOM   3004  CE  LYS A 393      49.373  21.212   3.392  1.00101.62           C  
ANISOU 3004  CE  LYS A 393    10678   9497  18436    304  -3133   -305       C  
ATOM   3005  NZ  LYS A 393      49.982  20.293   4.390  1.00103.96           N  
ANISOU 3005  NZ  LYS A 393    10771   9577  19152    221  -3514    -63       N  
ATOM   3006  N   TYR A 394      45.686  19.983  -1.030  1.00 98.38           N  
ANISOU 3006  N   TYR A 394    10298   9229  17853    684  -2459  -1084       N  
ATOM   3007  CA  TYR A 394      45.901  19.733  -2.450  1.00 99.04           C  
ANISOU 3007  CA  TYR A 394    10259   9327  18045    726  -2279  -1474       C  
ATOM   3008  C   TYR A 394      46.107  21.040  -3.203  1.00 97.71           C  
ANISOU 3008  C   TYR A 394    10258   9407  17463    663  -1986  -1636       C  
ATOM   3009  O   TYR A 394      46.989  21.137  -4.064  1.00 98.78           O  
ANISOU 3009  O   TYR A 394    10259   9589  17685    648  -1843  -1958       O  
ATOM   3010  CB  TYR A 394      44.728  18.951  -3.034  1.00 98.93           C  
ANISOU 3010  CB  TYR A 394    10255   9257  18077    767  -2299  -1488       C  
ATOM   3011  CG  TYR A 394      44.899  18.606  -4.495  1.00 99.97           C  
ANISOU 3011  CG  TYR A 394    10275   9405  18306    777  -2123  -1901       C  
ATOM   3012  CD1 TYR A 394      45.778  17.609  -4.894  1.00102.57           C  
ANISOU 3012  CD1 TYR A 394    10305   9546  19123    834  -2185  -2201       C  
ATOM   3013  CD2 TYR A 394      44.179  19.274  -5.474  1.00 98.67           C  
ANISOU 3013  CD2 TYR A 394    10297   9439  17753    714  -1896  -1995       C  
ATOM   3014  CE1 TYR A 394      45.938  17.289  -6.228  1.00103.89           C  
ANISOU 3014  CE1 TYR A 394    10376   9744  19355    823  -1996  -2617       C  
ATOM   3015  CE2 TYR A 394      44.331  18.960  -6.811  1.00 99.90           C  
ANISOU 3015  CE2 TYR A 394    10370   9636  17953    677  -1735  -2372       C  
ATOM   3016  CZ  TYR A 394      45.211  17.967  -7.182  1.00102.54           C  
ANISOU 3016  CZ  TYR A 394    10419   9801  18740    730  -1770  -2698       C  
ATOM   3017  OH  TYR A 394      45.365  17.652  -8.512  1.00104.11           O  
ANISOU 3017  OH  TYR A 394    10542  10057  18959    674  -1581  -3111       O  
ATOM   3018  N   CYS A 395      45.305  22.059  -2.884  1.00 95.63           N  
ANISOU 3018  N   CYS A 395    10275   9301  16761    619  -1897  -1415       N  
ATOM   3019  CA  CYS A 395      45.472  23.374  -3.495  1.00 94.46           C  
ANISOU 3019  CA  CYS A 395    10293   9367  16231    546  -1662  -1516       C  
ATOM   3020  C   CYS A 395      46.760  24.031  -3.018  1.00 94.91           C  
ANISOU 3020  C   CYS A 395    10319   9459  16285    500  -1663  -1544       C  
ATOM   3021  O   CYS A 395      47.620  24.408  -3.825  1.00 95.56           O  
ANISOU 3021  O   CYS A 395    10317   9637  16355    454  -1522  -1800       O  
ATOM   3022  CB  CYS A 395      44.270  24.255  -3.159  1.00 92.47           C  
ANISOU 3022  CB  CYS A 395    10323   9224  15587    526  -1594  -1259       C  
ATOM   3023  SG  CYS A 395      42.698  23.621  -3.755  1.00 91.92           S  
ANISOU 3023  SG  CYS A 395    10297   9131  15497    562  -1590  -1186       S  
ATOM   3024  N   ASP A 396      46.900  24.182  -1.698  1.00 94.75           N  
ANISOU 3024  N   ASP A 396    10369   9374  16258    491  -1824  -1271       N  
ATOM   3025  CA  ASP A 396      48.115  24.753  -1.128  1.00 95.34           C  
ANISOU 3025  CA  ASP A 396    10421   9462  16343    431  -1867  -1254       C  
ATOM   3026  C   ASP A 396      49.356  24.020  -1.620  1.00 97.47           C  
ANISOU 3026  C   ASP A 396    10366   9630  17037    454  -1909  -1509       C  
ATOM   3027  O   ASP A 396      50.373  24.646  -1.933  1.00 97.96           O  
ANISOU 3027  O   ASP A 396    10376   9779  17064    402  -1815  -1652       O  
ATOM   3028  CB  ASP A 396      48.039  24.709   0.398  1.00 95.42           C  
ANISOU 3028  CB  ASP A 396    10526   9388  16340    391  -2082   -917       C  
ATOM   3029  CG  ASP A 396      49.212  25.401   1.060  1.00 95.99           C  
ANISOU 3029  CG  ASP A 396    10621   9481  16371    299  -2143   -857       C  
ATOM   3030  OD1 ASP A 396      49.233  26.651   1.090  1.00 94.83           O  
ANISOU 3030  OD1 ASP A 396    10701   9482  15848    238  -2002   -838       O  
ATOM   3031  OD2 ASP A 396      50.119  24.692   1.544  1.00 97.78           O  
ANISOU 3031  OD2 ASP A 396    10631   9557  16963    281  -2350   -819       O  
ATOM   3032  N   ASN A 397      49.285  22.691  -1.704  1.00 98.97           N  
ANISOU 3032  N   ASN A 397    10321   9629  17653    533  -2050  -1575       N  
ATOM   3033  CA  ASN A 397      50.420  21.917  -2.195  1.00101.42           C  
ANISOU 3033  CA  ASN A 397    10288   9810  18437    576  -2079  -1851       C  
ATOM   3034  C   ASN A 397      50.672  22.187  -3.674  1.00101.77           C  
ANISOU 3034  C   ASN A 397    10269  10013  18386    565  -1785  -2251       C  
ATOM   3035  O   ASN A 397      51.827  22.269  -4.110  1.00103.37           O  
ANISOU 3035  O   ASN A 397    10270  10241  18767    548  -1696  -2491       O  
ATOM   3036  CB  ASN A 397      50.174  20.427  -1.953  1.00103.11           C  
ANISOU 3036  CB  ASN A 397    10273   9756  19150    665  -2311  -1831       C  
ATOM   3037  CG  ASN A 397      51.419  19.584  -2.160  1.00106.11           C  
ANISOU 3037  CG  ASN A 397    10263   9936  20119    721  -2399  -2066       C  
ATOM   3038  OD1 ASN A 397      52.496  20.102  -2.458  1.00106.95           O  
ANISOU 3038  OD1 ASN A 397    10260  10118  20259    691  -2277  -2240       O  
ATOM   3039  ND2 ASN A 397      51.272  18.272  -2.010  1.00107.95           N  
ANISOU 3039  ND2 ASN A 397    10268   9901  20846    803  -2616  -2073       N  
ATOM   3040  N   LEU A 398      49.605  22.334  -4.459  1.00100.49           N  
ANISOU 3040  N   LEU A 398    10273   9971  17938    553  -1634  -2318       N  
ATOM   3041  CA  LEU A 398      49.725  22.529  -5.898  1.00101.05           C  
ANISOU 3041  CA  LEU A 398    10305  10210  17880    497  -1370  -2681       C  
ATOM   3042  C   LEU A 398      50.014  23.972  -6.285  1.00 99.81           C  
ANISOU 3042  C   LEU A 398    10335  10321  17268    368  -1179  -2687       C  
ATOM   3043  O   LEU A 398      50.171  24.252  -7.479  1.00100.41           O  
ANISOU 3043  O   LEU A 398    10390  10576  17186    274   -964  -2964       O  
ATOM   3044  CB  LEU A 398      48.449  22.058  -6.600  1.00100.45           C  
ANISOU 3044  CB  LEU A 398    10330  10143  17693    503  -1323  -2721       C  
ATOM   3045  N   LEU A 399      50.085  24.892  -5.321  1.00 98.33           N  
ANISOU 3045  N   LEU A 399    10333  10168  16860    341  -1259  -2392       N  
ATOM   3046  CA  LEU A 399      50.399  26.283  -5.617  1.00 97.32           C  
ANISOU 3046  CA  LEU A 399    10381  10264  16333    220  -1113  -2379       C  
ATOM   3047  C   LEU A 399      51.791  26.715  -5.180  1.00 98.34           C  
ANISOU 3047  C   LEU A 399    10393  10405  16565    179  -1147  -2397       C  
ATOM   3048  O   LEU A 399      52.259  27.764  -5.632  1.00 98.04           O  
ANISOU 3048  O   LEU A 399    10441  10560  16249     64  -1017  -2451       O  
ATOM   3049  CB  LEU A 399      49.367  27.214  -4.965  1.00 94.96           C  
ANISOU 3049  CB  LEU A 399    10415  10010  15655    203  -1146  -2055       C  
ATOM   3050  CG  LEU A 399      47.944  27.131  -5.516  1.00 93.80           C  
ANISOU 3050  CG  LEU A 399    10412   9898  15328    212  -1084  -2007       C  
ATOM   3051  CD1 LEU A 399      47.012  28.030  -4.719  1.00 91.89           C  
ANISOU 3051  CD1 LEU A 399    10455   9670  14787    217  -1116  -1691       C  
ATOM   3052  CD2 LEU A 399      47.917  27.490  -6.991  1.00 94.16           C  
ANISOU 3052  CD2 LEU A 399    10455  10136  15186     90   -887  -2253       C  
ATOM   3053  N   LYS A 400      52.463  25.943  -4.327  1.00103.68           N  
ANISOU 3053  N   LYS A 400    10872  10879  17644    254  -1337  -2331       N  
ATOM   3054  CA  LYS A 400      53.782  26.326  -3.847  1.00104.40           C  
ANISOU 3054  CA  LYS A 400    10843  10962  17863    206  -1400  -2307       C  
ATOM   3055  C   LYS A 400      54.805  26.290  -4.985  1.00105.53           C  
ANISOU 3055  C   LYS A 400    10727  11226  18144    163  -1202  -2680       C  
ATOM   3056  O   LYS A 400      54.535  25.819  -6.094  1.00105.88           O  
ANISOU 3056  O   LYS A 400    10667  11341  18223    168  -1026  -2979       O  
ATOM   3057  CB  LYS A 400      54.228  25.413  -2.705  1.00104.21           C  
ANISOU 3057  CB  LYS A 400    10640  10672  18283    276  -1684  -2128       C  
ATOM   3058  CG  LYS A 400      53.334  25.468  -1.477  1.00103.38           C  
ANISOU 3058  CG  LYS A 400    10784  10478  18018    276  -1883  -1748       C  
ATOM   3059  CD  LYS A 400      53.413  26.819  -0.785  1.00103.77           C  
ANISOU 3059  CD  LYS A 400    11136  10658  17633    164  -1881  -1521       C  
ATOM   3060  CE  LYS A 400      52.504  26.873   0.435  1.00103.32           C  
ANISOU 3060  CE  LYS A 400    11326  10536  17395    148  -2040  -1183       C  
ATOM   3061  NZ  LYS A 400      52.978  25.984   1.532  1.00103.37           N  
ANISOU 3061  NZ  LYS A 400    11176  10335  17763    130  -2341   -975       N  
ATOM   3062  N   LYS A 401      56.004  26.795  -4.687  1.00129.82           N  
ANISOU 3062  N   LYS A 401    13698  14337  21291    101  -1229  -2660       N  
ATOM   3063  CA  LYS A 401      57.040  26.914  -5.707  1.00130.76           C  
ANISOU 3063  CA  LYS A 401    13571  14610  21501     36  -1023  -2996       C  
ATOM   3064  C   LYS A 401      57.581  25.545  -6.107  1.00130.24           C  
ANISOU 3064  C   LYS A 401    13095  14372  22020    149  -1003  -3304       C  
ATOM   3065  O   LYS A 401      57.542  25.169  -7.285  1.00130.80           O  
ANISOU 3065  O   LYS A 401    13028  14553  22115    135   -769  -3674       O  
ATOM   3066  CB  LYS A 401      58.163  27.822  -5.202  1.00131.29           C  
ANISOU 3066  CB  LYS A 401    13631  14748  21505    -62  -1081  -2854       C  
ATOM   3067  CG  LYS A 401      59.213  28.154  -6.248  1.00132.24           C  
ANISOU 3067  CG  LYS A 401    13527  15083  21635   -163   -851  -3165       C  
ATOM   3068  CD  LYS A 401      60.283  29.077  -5.680  1.00133.41           C  
ANISOU 3068  CD  LYS A 401    13681  15292  21716   -267   -942  -2978       C  
ATOM   3069  CE  LYS A 401      59.992  30.539  -6.005  1.00135.22           C  
ANISOU 3069  CE  LYS A 401    14248  15787  21342   -434   -850  -2862       C  
ATOM   3070  NZ  LYS A 401      58.923  31.122  -5.143  1.00135.89           N  
ANISOU 3070  NZ  LYS A 401    14735  15797  21099   -421  -1003  -2527       N  
ATOM   3071  N   SER A 402      58.092  24.785  -5.133  1.00144.74           N  
ANISOU 3071  N   SER A 402    14726  15928  24342    248  -1255  -3158       N  
ATOM   3072  CA  SER A 402      58.618  23.431  -5.342  1.00143.50           C  
ANISOU 3072  CA  SER A 402    14151  15533  24841    376  -1294  -3414       C  
ATOM   3073  C   SER A 402      59.735  23.422  -6.391  1.00145.32           C  
ANISOU 3073  C   SER A 402    14055  15897  25262    345  -1025  -3841       C  
ATOM   3074  O   SER A 402      59.621  22.822  -7.462  1.00145.81           O  
ANISOU 3074  O   SER A 402    13954  16007  25439    374   -797  -4249       O  
ATOM   3075  CB  SER A 402      57.499  22.450  -5.717  1.00141.56           C  
ANISOU 3075  CB  SER A 402    13926  15166  24693    477  -1292  -3534       C  
ATOM   3076  OG  SER A 402      56.968  22.726  -7.003  1.00143.00           O  
ANISOU 3076  OG  SER A 402    14218  15597  24518    410   -985  -3838       O  
ATOM   3077  N   ALA A 403      60.826  24.105  -6.060  1.00145.96           N  
ANISOU 3077  N   ALA A 403    14045  16048  25366    269  -1049  -3744       N  
ATOM   3078  CA  ALA A 403      61.985  24.170  -6.943  1.00146.72           C  
ANISOU 3078  CA  ALA A 403    13809  16288  25649    224   -799  -4113       C  
ATOM   3079  C   ALA A 403      62.946  23.015  -6.673  1.00144.83           C  
ANISOU 3079  C   ALA A 403    13071  15735  26221    368   -910  -4266       C  
ATOM   3080  O   ALA A 403      64.164  23.172  -6.768  1.00143.59           O  
ANISOU 3080  O   ALA A 403    12615  15607  26337    340   -848  -4373       O  
ATOM   3081  CB  ALA A 403      62.701  25.503  -6.782  1.00148.07           C  
ANISOU 3081  CB  ALA A 403    14110  16698  25451     60   -770  -3930       C  
ATOM   3082  N   GLY A 405      60.545  20.489 -10.177  1.00175.12           N  
ANISOU 3082  N   GLY A 405    16801  19655  30081    505   -176  -5621       N  
ATOM   3083  CA  GLY A 405      59.155  20.588  -9.773  1.00170.86           C  
ANISOU 3083  CA  GLY A 405    16663  19083  29174    505   -355  -5288       C  
ATOM   3084  C   GLY A 405      58.180  20.391 -10.917  1.00171.92           C  
ANISOU 3084  C   GLY A 405    16967  19387  28968    428   -126  -5574       C  
ATOM   3085  O   GLY A 405      58.482  19.702 -11.891  1.00172.10           O  
ANISOU 3085  O   GLY A 405    16747  19426  29219    429    111  -6068       O  
ATOM   3086  N   MET A 406      57.003  21.000 -10.799  1.00170.10           N  
ANISOU 3086  N   MET A 406    17152  19279  28199    351   -195  -5268       N  
ATOM   3087  CA  MET A 406      55.980  20.900 -11.827  1.00170.66           C  
ANISOU 3087  CA  MET A 406    17422  19512  27910    249    -23  -5458       C  
ATOM   3088  C   MET A 406      56.132  22.038 -12.834  1.00172.15           C  
ANISOU 3088  C   MET A 406    17770  20130  27509     -2    266  -5593       C  
ATOM   3089  O   MET A 406      57.141  22.748 -12.865  1.00172.04           O  
ANISOU 3089  O   MET A 406    17651  20283  27432    -84    369  -5629       O  
ATOM   3090  CB  MET A 406      54.585  20.897 -11.208  1.00169.48           C  
ANISOU 3090  CB  MET A 406    17602  19254  27540    295   -257  -5050       C  
ATOM   3091  CG  MET A 406      54.239  19.643 -10.435  1.00167.33           C  
ANISOU 3091  CG  MET A 406    17186  18587  27804    499   -532  -4949       C  
ATOM   3092  SD  MET A 406      52.566  19.738  -9.779  1.00167.89           S  
ANISOU 3092  SD  MET A 406    17647  18597  27547    519   -766  -4471       S  
ATOM   3093  CE  MET A 406      51.613  19.618 -11.293  1.00167.51           C  
ANISOU 3093  CE  MET A 406    17754  18753  27138    379   -516  -4781       C  
ATOM   3094  N   THR A 407      55.115  22.216 -13.673  1.00164.01           N  
ANISOU 3094  N   THR A 407    16991  19281  26045   -148    377  -5646       N  
ATOM   3095  CA  THR A 407      55.131  23.211 -14.735  1.00166.80           C  
ANISOU 3095  CA  THR A 407    17503  20042  25831   -429    624  -5765       C  
ATOM   3096  C   THR A 407      53.776  23.899 -14.781  1.00167.21           C  
ANISOU 3096  C   THR A 407    17965  20193  25375   -535    520  -5411       C  
ATOM   3097  O   THR A 407      52.742  23.227 -14.737  1.00167.38           O  
ANISOU 3097  O   THR A 407    18091  20049  25457   -459    410  -5343       O  
ATOM   3098  CB  THR A 407      55.438  22.558 -16.089  1.00168.70           C  
ANISOU 3098  CB  THR A 407    17550  20441  26107   -567    936  -6342       C  
ATOM   3099  OG1 THR A 407      56.698  21.879 -16.020  1.00169.57           O  
ANISOU 3099  OG1 THR A 407    17239  20429  26761   -442   1044  -6693       O  
ATOM   3100  CG2 THR A 407      55.493  23.601 -17.192  1.00171.61           C  
ANISOU 3100  CG2 THR A 407    18080  21264  25861   -910   1176  -6443       C  
ATOM   3101  N   GLU A 408      53.777  25.229 -14.859  1.00159.55           N  
ANISOU 3101  N   GLU A 408    17212  19475  23936   -710    540  -5176       N  
ATOM   3102  CA  GLU A 408      52.528  25.949 -15.054  1.00160.30           C  
ANISOU 3102  CA  GLU A 408    17665  19674  23569   -835    464  -4872       C  
ATOM   3103  C   GLU A 408      52.056  25.787 -16.498  1.00161.55           C  
ANISOU 3103  C   GLU A 408    17878  20072  23432  -1090    663  -5159       C  
ATOM   3104  O   GLU A 408      52.679  25.098 -17.311  1.00162.81           O  
ANISOU 3104  O   GLU A 408    17812  20319  23730  -1166    875  -5616       O  
ATOM   3105  CB  GLU A 408      52.675  27.419 -14.666  1.00161.24           C  
ANISOU 3105  CB  GLU A 408    17987  19949  23328   -938    400  -4532       C  
ATOM   3106  CG  GLU A 408      52.777  27.641 -13.164  1.00160.94           C  
ANISOU 3106  CG  GLU A 408    17996  19664  23491   -712    168  -4176       C  
ATOM   3107  CD  GLU A 408      52.802  29.108 -12.786  1.00161.98           C  
ANISOU 3107  CD  GLU A 408    18361  19926  23257   -816     99  -3851       C  
ATOM   3108  OE1 GLU A 408      52.872  29.959 -13.698  1.00162.66           O  
ANISOU 3108  OE1 GLU A 408    18540  20293  22972  -1063    220  -3898       O  
ATOM   3109  OE2 GLU A 408      52.741  29.411 -11.575  1.00161.57           O  
ANISOU 3109  OE2 GLU A 408    18407  19694  23287   -668    -84  -3546       O  
ATOM   3110  N   ASN A 409      50.922  26.419 -16.809  1.00159.81           N  
ANISOU 3110  N   ASN A 409    17958  19950  22811  -1236    589  -4888       N  
ATOM   3111  CA  ASN A 409      50.062  26.109 -17.952  1.00160.45           C  
ANISOU 3111  CA  ASN A 409    18155  20167  22643  -1453    674  -5031       C  
ATOM   3112  C   ASN A 409      49.446  24.723 -17.772  1.00159.65           C  
ANISOU 3112  C   ASN A 409    17975  19779  22907  -1255    600  -5153       C  
ATOM   3113  O   ASN A 409      48.663  24.278 -18.618  1.00160.57           O  
ANISOU 3113  O   ASN A 409    18184  19949  22875  -1404    640  -5268       O  
ATOM   3114  CB  ASN A 409      50.804  26.194 -19.296  1.00161.35           C  
ANISOU 3114  CB  ASN A 409    18157  20630  22517  -1773    958  -5461       C  
ATOM   3115  CG  ASN A 409      49.866  26.285 -20.489  1.00161.33           C  
ANISOU 3115  CG  ASN A 409    18358  20842  22100  -2098   1011  -5496       C  
ATOM   3116  OD1 ASN A 409      48.646  26.324 -20.340  1.00161.13           O  
ANISOU 3116  OD1 ASN A 409    18548  20695  21978  -2078    829  -5182       O  
ATOM   3117  ND2 ASN A 409      50.441  26.317 -21.687  1.00162.55           N  
ANISOU 3117  ND2 ASN A 409    18434  21325  22003  -2419   1262  -5877       N  
ATOM   3118  N   GLU A 410      49.778  24.036 -16.681  1.00150.53           N  
ANISOU 3118  N   GLU A 410    16654  18314  22226   -942    469  -5107       N  
ATOM   3119  CA  GLU A 410      49.254  22.740 -16.288  1.00149.18           C  
ANISOU 3119  CA  GLU A 410    16392  17827  22464   -726    339  -5155       C  
ATOM   3120  C   GLU A 410      48.578  22.771 -14.930  1.00147.12           C  
ANISOU 3120  C   GLU A 410    16243  17305  22350   -492     56  -4681       C  
ATOM   3121  O   GLU A 410      47.595  22.054 -14.724  1.00146.85           O  
ANISOU 3121  O   GLU A 410    16274  17083  22437   -398    -89  -4555       O  
ATOM   3122  CB  GLU A 410      50.397  21.708 -16.252  1.00150.05           C  
ANISOU 3122  CB  GLU A 410    16133  17782  23096   -582    433  -5581       C  
ATOM   3123  CG  GLU A 410      49.998  20.295 -15.875  1.00149.26           C  
ANISOU 3123  CG  GLU A 410    15894  17326  23492   -363    281  -5666       C  
ATOM   3124  CD  GLU A 410      51.199  19.370 -15.800  1.00148.50           C  
ANISOU 3124  CD  GLU A 410    15404  17050  23969   -214    358  -6073       C  
ATOM   3125  OE1 GLU A 410      52.335  19.853 -16.004  1.00148.66           O  
ANISOU 3125  OE1 GLU A 410    15259  17236  23991   -276    539  -6273       O  
ATOM   3126  OE2 GLU A 410      51.009  18.164 -15.535  1.00147.06           O  
ANISOU 3126  OE2 GLU A 410    15063  16551  24260    -38    227  -6183       O  
ATOM   3127  N   VAL A 411      49.075  23.597 -14.004  1.00129.81           N  
ANISOU 3127  N   VAL A 411    14082  15110  20130   -417    -23  -4417       N  
ATOM   3128  CA  VAL A 411      48.470  23.710 -12.681  1.00127.43           C  
ANISOU 3128  CA  VAL A 411    13901  14597  19917   -229   -268  -3979       C  
ATOM   3129  C   VAL A 411      47.028  24.186 -12.795  1.00126.65           C  
ANISOU 3129  C   VAL A 411    14096  14547  19479   -297   -337  -3669       C  
ATOM   3130  O   VAL A 411      46.147  23.730 -12.055  1.00125.18           O  
ANISOU 3130  O   VAL A 411    13978  14164  19421   -153   -514  -3411       O  
ATOM   3131  CB  VAL A 411      49.310  24.647 -11.792  1.00126.64           C  
ANISOU 3131  CB  VAL A 411    13811  14529  19775   -192   -312  -3785       C  
ATOM   3132  CG1 VAL A 411      48.650  24.836 -10.434  1.00124.60           C  
ANISOU 3132  CG1 VAL A 411    13709  14088  19545    -39   -541  -3348       C  
ATOM   3133  CG2 VAL A 411      50.720  24.104 -11.634  1.00127.45           C  
ANISOU 3133  CG2 VAL A 411    13593  14555  20275   -117   -270  -4060       C  
ATOM   3134  N   GLU A 412      46.759  25.098 -13.732  1.00122.79           N  
ANISOU 3134  N   GLU A 412    13768  14319  18567   -531   -209  -3677       N  
ATOM   3135  CA  GLU A 412      45.392  25.566 -13.919  1.00123.08           C  
ANISOU 3135  CA  GLU A 412    14055  14388  18321   -609   -283  -3378       C  
ATOM   3136  C   GLU A 412      44.510  24.467 -14.498  1.00123.40           C  
ANISOU 3136  C   GLU A 412    14082  14333  18470   -618   -317  -3479       C  
ATOM   3137  O   GLU A 412      43.307  24.424 -14.213  1.00123.87           O  
ANISOU 3137  O   GLU A 412    14287  14295  18484   -571   -449  -3180       O  
ATOM   3138  CB  GLU A 412      45.380  26.807 -14.814  1.00124.01           C  
ANISOU 3138  CB  GLU A 412    14328  14795  17995   -885   -174  -3345       C  
ATOM   3139  CG  GLU A 412      44.093  27.621 -14.755  1.00124.40           C  
ANISOU 3139  CG  GLU A 412    14626  14850  17788   -944   -282  -2951       C  
ATOM   3140  CD  GLU A 412      43.020  27.106 -15.690  1.00125.47           C  
ANISOU 3140  CD  GLU A 412    14835  15011  17826  -1088   -297  -2958       C  
ATOM   3141  OE1 GLU A 412      43.371  26.506 -16.728  1.00126.15           O  
ANISOU 3141  OE1 GLU A 412    14834  15221  17876  -1259   -178  -3301       O  
ATOM   3142  OE2 GLU A 412      41.824  27.307 -15.389  1.00125.57           O  
ANISOU 3142  OE2 GLU A 412    14991  14923  17798  -1040   -424  -2626       O  
ATOM   3143  N   ASP A 413      45.083  23.567 -15.301  1.00134.19           N  
ANISOU 3143  N   ASP A 413    15270  15722  19994   -681   -195  -3905       N  
ATOM   3144  CA  ASP A 413      44.336  22.395 -15.747  1.00134.40           C  
ANISOU 3144  CA  ASP A 413    15270  15613  20184   -668   -247  -4029       C  
ATOM   3145  C   ASP A 413      44.003  21.486 -14.571  1.00132.66           C  
ANISOU 3145  C   ASP A 413    14960  15062  20381   -378   -464  -3844       C  
ATOM   3146  O   ASP A 413      42.859  21.037 -14.422  1.00132.61           O  
ANISOU 3146  O   ASP A 413    15055  14931  20398   -335   -610  -3624       O  
ATOM   3147  CB  ASP A 413      45.132  21.630 -16.807  1.00135.71           C  
ANISOU 3147  CB  ASP A 413    15247  15859  20456   -789    -49  -4578       C  
ATOM   3148  CG  ASP A 413      45.211  22.368 -18.130  1.00137.24           C  
ANISOU 3148  CG  ASP A 413    15556  16407  20183  -1145    154  -4754       C  
ATOM   3149  OD1 ASP A 413      44.270  23.125 -18.449  1.00138.10           O  
ANISOU 3149  OD1 ASP A 413    15906  16641  19927  -1315     89  -4449       O  
ATOM   3150  OD2 ASP A 413      46.214  22.185 -18.853  1.00137.93           O  
ANISOU 3150  OD2 ASP A 413    15481  16648  20277  -1268    374  -5194       O  
ATOM   3151  N   ARG A 414      44.996  21.206 -13.721  1.00131.84           N  
ANISOU 3151  N   ARG A 414    14661  14819  20613   -197   -504  -3909       N  
ATOM   3152  CA  ARG A 414      44.769  20.332 -12.574  1.00129.87           C  
ANISOU 3152  CA  ARG A 414    14312  14263  20767     42   -738  -3717       C  
ATOM   3153  C   ARG A 414      43.722  20.919 -11.636  1.00128.51           C  
ANISOU 3153  C   ARG A 414    14359  14059  20410    106   -899  -3209       C  
ATOM   3154  O   ARG A 414      42.915  20.184 -11.054  1.00127.12           O  
ANISOU 3154  O   ARG A 414    14188  13692  20420    220  -1087  -2999       O  
ATOM   3155  CB  ARG A 414      46.086  20.086 -11.834  1.00128.87           C  
ANISOU 3155  CB  ARG A 414    13941  14013  21012    182   -769  -3836       C  
ATOM   3156  CG  ARG A 414      47.181  19.460 -12.694  1.00129.89           C  
ANISOU 3156  CG  ARG A 414    13802  14151  21398    146   -591  -4364       C  
ATOM   3157  CD  ARG A 414      46.841  18.030 -13.090  1.00130.03           C  
ANISOU 3157  CD  ARG A 414    13671  13942  21792    216   -658  -4611       C  
ATOM   3158  NE  ARG A 414      47.858  17.439 -13.957  1.00130.86           N  
ANISOU 3158  NE  ARG A 414    13513  14054  22153    181   -452  -5166       N  
ATOM   3159  CZ  ARG A 414      48.914  16.759 -13.519  1.00129.50           C  
ANISOU 3159  CZ  ARG A 414    13018  13667  22518    340   -493  -5370       C  
ATOM   3160  NH1 ARG A 414      49.099  16.580 -12.218  1.00126.88           N  
ANISOU 3160  NH1 ARG A 414    12602  13102  22503    520   -759  -5037       N  
ATOM   3161  NH2 ARG A 414      49.787  16.257 -14.383  1.00130.52           N  
ANISOU 3161  NH2 ARG A 414    12899  13815  22877    305   -267  -5909       N  
ATOM   3162  N   LEU A 415      43.717  22.246 -11.479  1.00112.38           N  
ANISOU 3162  N   LEU A 415    12489  12199  18010     28   -826  -3013       N  
ATOM   3163  CA  LEU A 415      42.670  22.891 -10.693  1.00109.93           C  
ANISOU 3163  CA  LEU A 415    12387  11871  17510     76   -935  -2574       C  
ATOM   3164  C   LEU A 415      41.318  22.779 -11.389  1.00109.47           C  
ANISOU 3164  C   LEU A 415    12470  11845  17279    -15   -952  -2452       C  
ATOM   3165  O   LEU A 415      40.294  22.524 -10.739  1.00108.33           O  
ANISOU 3165  O   LEU A 415    12396  11580  17184     82  -1091  -2149       O  
ATOM   3166  CB  LEU A 415      43.033  24.354 -10.441  1.00108.56           C  
ANISOU 3166  CB  LEU A 415    12355  11866  17026      9   -848  -2437       C  
ATOM   3167  CG  LEU A 415      44.268  24.612  -9.573  1.00108.73           C  
ANISOU 3167  CG  LEU A 415    12275  11853  17186     91   -864  -2468       C  
ATOM   3168  CD1 LEU A 415      44.625  26.086  -9.571  1.00107.68           C  
ANISOU 3168  CD1 LEU A 415    12294  11902  16716    -13   -768  -2376       C  
ATOM   3169  CD2 LEU A 415      44.046  24.117  -8.154  1.00108.03           C  
ANISOU 3169  CD2 LEU A 415    12164  11554  17328    268  -1060  -2205       C  
ATOM   3170  N   THR A 416      41.299  22.962 -12.714  1.00114.84           N  
ANISOU 3170  N   THR A 416    13189  12695  17749   -222   -815  -2675       N  
ATOM   3171  CA  THR A 416      40.072  22.769 -13.480  1.00116.61           C  
ANISOU 3171  CA  THR A 416    13536  12945  17825   -344   -851  -2570       C  
ATOM   3172  C   THR A 416      39.488  21.382 -13.248  1.00115.50           C  
ANISOU 3172  C   THR A 416    13303  12578  18003   -220  -1003  -2569       C  
ATOM   3173  O   THR A 416      38.262  21.220 -13.205  1.00115.37           O  
ANISOU 3173  O   THR A 416    13391  12502  17942   -221  -1117  -2295       O  
ATOM   3174  CB  THR A 416      40.342  23.002 -14.969  1.00118.99           C  
ANISOU 3174  CB  THR A 416    13869  13471  17871   -627   -689  -2867       C  
ATOM   3175  OG1 THR A 416      40.814  24.340 -15.165  1.00119.79           O  
ANISOU 3175  OG1 THR A 416    14061  13784  17668   -762   -581  -2815       O  
ATOM   3176  CG2 THR A 416      39.077  22.793 -15.793  1.00120.43           C  
ANISOU 3176  CG2 THR A 416    14187  13678  17892   -792   -751  -2740       C  
ATOM   3177  N   SER A 417      40.345  20.372 -13.080  1.00110.20           N  
ANISOU 3177  N   SER A 417    12423  11765  17684   -112  -1023  -2857       N  
ATOM   3178  CA  SER A 417      39.857  19.067 -12.648  1.00108.68           C  
ANISOU 3178  CA  SER A 417    12127  11317  17852     29  -1215  -2812       C  
ATOM   3179  C   SER A 417      39.375  19.117 -11.203  1.00106.16           C  
ANISOU 3179  C   SER A 417    11830  10860  17646    211  -1403  -2387       C  
ATOM   3180  O   SER A 417      38.319  18.562 -10.875  1.00105.40           O  
ANISOU 3180  O   SER A 417    11773  10645  17627    262  -1565  -2133       O  
ATOM   3181  CB  SER A 417      40.952  18.012 -12.814  1.00109.17           C  
ANISOU 3181  CB  SER A 417    11932  11232  18316    102  -1201  -3232       C  
ATOM   3182  OG  SER A 417      41.298  17.834 -14.177  1.00111.91           O  
ANISOU 3182  OG  SER A 417    12254  11708  18557    -79  -1010  -3661       O  
ATOM   3183  N   PHE A 418      40.132  19.791 -10.330  1.00 97.13           N  
ANISOU 3183  N   PHE A 418    10667   9745  16493    289  -1381  -2301       N  
ATOM   3184  CA  PHE A 418      39.793  19.868  -8.912  1.00 95.71           C  
ANISOU 3184  CA  PHE A 418    10514   9461  16389    427  -1541  -1928       C  
ATOM   3185  C   PHE A 418      38.406  20.443  -8.664  1.00 93.86           C  
ANISOU 3185  C   PHE A 418    10480   9290  15893    408  -1564  -1552       C  
ATOM   3186  O   PHE A 418      37.807  20.150  -7.621  1.00 93.19           O  
ANISOU 3186  O   PHE A 418    10402   9104  15901    507  -1713  -1250       O  
ATOM   3187  CB  PHE A 418      40.836  20.706  -8.175  1.00 95.15           C  
ANISOU 3187  CB  PHE A 418    10436   9454  16263    458  -1483  -1916       C  
ATOM   3188  CG  PHE A 418      40.514  20.941  -6.731  1.00 93.87           C  
ANISOU 3188  CG  PHE A 418    10339   9227  16099    553  -1619  -1546       C  
ATOM   3189  CD1 PHE A 418      40.697  19.944  -5.793  1.00 94.73           C  
ANISOU 3189  CD1 PHE A 418    10302   9140  16552    650  -1837  -1439       C  
ATOM   3190  CD2 PHE A 418      40.019  22.165  -6.313  1.00 92.08           C  
ANISOU 3190  CD2 PHE A 418    10318   9137  15531    526  -1531  -1308       C  
ATOM   3191  CE1 PHE A 418      40.397  20.163  -4.464  1.00 93.85           C  
ANISOU 3191  CE1 PHE A 418    10262   9001  16394    691  -1957  -1097       C  
ATOM   3192  CE2 PHE A 418      39.716  22.390  -4.988  1.00 91.24           C  
ANISOU 3192  CE2 PHE A 418    10281   8991  15396    591  -1626  -1003       C  
ATOM   3193  CZ  PHE A 418      39.906  21.387  -4.061  1.00 92.13           C  
ANISOU 3193  CZ  PHE A 418    10260   8941  15804    660  -1834   -896       C  
ATOM   3194  N   ILE A 419      37.886  21.248  -9.596  1.00100.53           N  
ANISOU 3194  N   ILE A 419    11472  10301  16425    271  -1427  -1555       N  
ATOM   3195  CA  ILE A 419      36.576  21.879  -9.419  1.00 99.86           C  
ANISOU 3195  CA  ILE A 419    11551  10263  16129    254  -1442  -1200       C  
ATOM   3196  C   ILE A 419      35.498  20.854  -9.087  1.00 98.86           C  
ANISOU 3196  C   ILE A 419    11388   9987  16189    324  -1619   -984       C  
ATOM   3197  O   ILE A 419      34.570  21.141  -8.321  1.00 97.61           O  
ANISOU 3197  O   ILE A 419    11299   9815  15974    388  -1670   -642       O  
ATOM   3198  CB  ILE A 419      36.207  22.695 -10.678  1.00102.86           C  
ANISOU 3198  CB  ILE A 419    12057  10814  16213     59  -1314  -1254       C  
ATOM   3199  CG1 ILE A 419      37.223  23.813 -10.910  1.00105.27           C  
ANISOU 3199  CG1 ILE A 419    12405  11279  16315    -23  -1158  -1412       C  
ATOM   3200  CG2 ILE A 419      34.812  23.289 -10.553  1.00103.05           C  
ANISOU 3200  CG2 ILE A 419    12214  10850  16090     46  -1347   -879       C  
ATOM   3201  CD1 ILE A 419      37.077  24.497 -12.253  1.00109.22           C  
ANISOU 3201  CD1 ILE A 419    13001  11960  16538   -264  -1054  -1507       C  
ATOM   3202  N   THR A 420      35.604  19.644  -9.639  1.00 93.52           N  
ANISOU 3202  N   THR A 420    10593   9195  15744    310  -1713  -1185       N  
ATOM   3203  CA  THR A 420      34.575  18.633  -9.415  1.00 93.84           C  
ANISOU 3203  CA  THR A 420    10600   9089  15967    356  -1906   -978       C  
ATOM   3204  C   THR A 420      34.656  18.066  -8.000  1.00 93.69           C  
ANISOU 3204  C   THR A 420    10481   8929  16189    511  -2078   -767       C  
ATOM   3205  O   THR A 420      33.672  18.087  -7.247  1.00 92.84           O  
ANISOU 3205  O   THR A 420    10420   8808  16045    556  -2167   -407       O  
ATOM   3206  CB  THR A 420      34.713  17.522 -10.457  1.00 95.85           C  
ANISOU 3206  CB  THR A 420    10767   9247  16407    283  -1961  -1286       C  
ATOM   3207  OG1 THR A 420      34.581  18.081 -11.769  1.00 96.20           O  
ANISOU 3207  OG1 THR A 420    10925   9455  16173     88  -1804  -1459       O  
ATOM   3208  CG2 THR A 420      33.641  16.475 -10.261  1.00 96.29           C  
ANISOU 3208  CG2 THR A 420    10792   9140  16652    317  -2184  -1060       C  
ATOM   3209  N   VAL A 421      35.828  17.548  -7.622  1.00 94.77           N  
ANISOU 3209  N   VAL A 421    10466   8963  16581    576  -2133   -979       N  
ATOM   3210  CA  VAL A 421      36.010  17.017  -6.273  1.00 94.94           C  
ANISOU 3210  CA  VAL A 421    10387   8852  16833    680  -2328   -764       C  
ATOM   3211  C   VAL A 421      35.637  18.064  -5.235  1.00 93.21           C  
ANISOU 3211  C   VAL A 421    10308   8766  16343    698  -2263   -443       C  
ATOM   3212  O   VAL A 421      35.088  17.736  -4.175  1.00 93.08           O  
ANISOU 3212  O   VAL A 421    10281   8703  16382    736  -2411   -133       O  
ATOM   3213  CB  VAL A 421      37.457  16.511  -6.087  1.00 96.49           C  
ANISOU 3213  CB  VAL A 421    10393   8924  17344    729  -2383  -1043       C  
ATOM   3214  CG1 VAL A 421      37.678  16.022  -4.665  1.00 96.84           C  
ANISOU 3214  CG1 VAL A 421    10339   8839  17616    795  -2617   -780       C  
ATOM   3215  CG2 VAL A 421      37.763  15.406  -7.080  1.00 98.63           C  
ANISOU 3215  CG2 VAL A 421    10507   9040  17926    724  -2436  -1390       C  
ATOM   3216  N   PHE A 422      35.901  19.340  -5.525  1.00 92.09           N  
ANISOU 3216  N   PHE A 422    10298   8795  15898    657  -2041   -514       N  
ATOM   3217  CA  PHE A 422      35.370  20.396  -4.670  1.00 90.66           C  
ANISOU 3217  CA  PHE A 422    10265   8729  15450    672  -1954   -234       C  
ATOM   3218  C   PHE A 422      33.848  20.423  -4.725  1.00 90.05           C  
ANISOU 3218  C   PHE A 422    10266   8679  15270    667  -1963     49       C  
ATOM   3219  O   PHE A 422      33.183  20.605  -3.698  1.00 89.62           O  
ANISOU 3219  O   PHE A 422    10254   8647  15151    708  -1987    338       O  
ATOM   3220  CB  PHE A 422      35.946  21.753  -5.079  1.00 89.80           C  
ANISOU 3220  CB  PHE A 422    10277   8773  15072    622  -1736   -379       C  
ATOM   3221  N   LYS A 423      33.281  20.231  -5.918  1.00 90.24           N  
ANISOU 3221  N   LYS A 423    10305   8707  15276    602  -1942    -29       N  
ATOM   3222  CA  LYS A 423      31.833  20.291  -6.080  1.00 89.81           C  
ANISOU 3222  CA  LYS A 423    10312   8671  15141    584  -1959    252       C  
ATOM   3223  C   LYS A 423      31.129  19.300  -5.166  1.00 90.28           C  
ANISOU 3223  C   LYS A 423    10286   8630  15386    648  -2153    523       C  
ATOM   3224  O   LYS A 423      30.079  19.613  -4.593  1.00 89.80           O  
ANISOU 3224  O   LYS A 423    10267   8618  15233    672  -2135    832       O  
ATOM   3225  CB  LYS A 423      31.468  20.032  -7.541  1.00 90.36           C  
ANISOU 3225  CB  LYS A 423    10399   8742  15193    468  -1957    113       C  
ATOM   3226  CG  LYS A 423      29.990  19.976  -7.845  1.00 90.20           C  
ANISOU 3226  CG  LYS A 423    10422   8719  15130    427  -2010    409       C  
ATOM   3227  CD  LYS A 423      29.783  19.737  -9.332  1.00 91.00           C  
ANISOU 3227  CD  LYS A 423    10559   8831  15186    267  -2020    247       C  
ATOM   3228  CE  LYS A 423      30.190  18.317  -9.712  1.00 92.51           C  
ANISOU 3228  CE  LYS A 423    10644   8884  15621    255  -2175     20       C  
ATOM   3229  NZ  LYS A 423      29.924  18.007 -11.144  1.00 93.64           N  
ANISOU 3229  NZ  LYS A 423    10838   9042  15699     71  -2183   -151       N  
ATOM   3230  N   TYR A 424      31.698  18.105  -4.998  1.00 91.45           N  
ANISOU 3230  N   TYR A 424    10298   8636  15814    670  -2345    418       N  
ATOM   3231  CA  TYR A 424      31.004  17.079  -4.225  1.00 92.15           C  
ANISOU 3231  CA  TYR A 424    10296   8622  16094    699  -2573    694       C  
ATOM   3232  C   TYR A 424      31.150  17.228  -2.714  1.00 92.06           C  
ANISOU 3232  C   TYR A 424    10273   8649  16058    735  -2620    923       C  
ATOM   3233  O   TYR A 424      30.464  16.506  -1.983  1.00 92.68           O  
ANISOU 3233  O   TYR A 424    10289   8686  16240    730  -2797   1205       O  
ATOM   3234  CB  TYR A 424      31.477  15.677  -4.623  1.00 93.79           C  
ANISOU 3234  CB  TYR A 424    10349   8628  16658    699  -2802    516       C  
ATOM   3235  CG  TYR A 424      31.018  15.229  -5.989  1.00 94.37           C  
ANISOU 3235  CG  TYR A 424    10436   8650  16771    635  -2810    354       C  
ATOM   3236  CD1 TYR A 424      29.701  14.857  -6.207  1.00 94.38           C  
ANISOU 3236  CD1 TYR A 424    10468   8637  16755    597  -2909    622       C  
ATOM   3237  CD2 TYR A 424      31.907  15.139  -7.048  1.00 95.19           C  
ANISOU 3237  CD2 TYR A 424    10517   8724  16926    595  -2722    -66       C  
ATOM   3238  CE1 TYR A 424      29.275  14.441  -7.449  1.00 95.10           C  
ANISOU 3238  CE1 TYR A 424    10588   8681  16865    508  -2935    488       C  
ATOM   3239  CE2 TYR A 424      31.489  14.718  -8.292  1.00 96.04           C  
ANISOU 3239  CE2 TYR A 424    10655   8801  17035    499  -2725   -228       C  
ATOM   3240  CZ  TYR A 424      30.174  14.371  -8.488  1.00 95.97           C  
ANISOU 3240  CZ  TYR A 424    10696   8771  16996    451  -2841     55       C  
ATOM   3241  OH  TYR A 424      29.755  13.952  -9.728  1.00 96.98           O  
ANISOU 3241  OH  TYR A 424    10872   8869  17108    327  -2860    -95       O  
ATOM   3242  N   ILE A 425      32.011  18.125  -2.223  1.00 91.50           N  
ANISOU 3242  N   ILE A 425    10266   8663  15838    746  -2478    821       N  
ATOM   3243  CA  ILE A 425      32.260  18.188  -0.786  1.00 91.79           C  
ANISOU 3243  CA  ILE A 425    10300   8734  15843    741  -2543   1016       C  
ATOM   3244  C   ILE A 425      30.976  18.535  -0.043  1.00 91.48           C  
ANISOU 3244  C   ILE A 425    10333   8813  15611    732  -2481   1357       C  
ATOM   3245  O   ILE A 425      30.214  19.422  -0.449  1.00 90.57           O  
ANISOU 3245  O   ILE A 425    10318   8798  15294    752  -2274   1395       O  
ATOM   3246  CB  ILE A 425      33.361  19.208  -0.459  1.00 91.27           C  
ANISOU 3246  CB  ILE A 425    10316   8746  15616    739  -2387    845       C  
ATOM   3247  CG1 ILE A 425      34.653  18.862  -1.186  1.00 91.83           C  
ANISOU 3247  CG1 ILE A 425    10286   8711  15895    746  -2432    506       C  
ATOM   3248  CG2 ILE A 425      33.632  19.232   1.038  1.00 91.86           C  
ANISOU 3248  CG2 ILE A 425    10404   8859  15638    694  -2474   1052       C  
ATOM   3249  CD1 ILE A 425      35.673  19.968  -1.109  1.00 91.22           C  
ANISOU 3249  CD1 ILE A 425    10295   8726  15639    736  -2258    329       C  
ATOM   3250  N   ASP A 426      30.730  17.820   1.056  1.00102.87           N  
ANISOU 3250  N   ASP A 426    11707  10246  17134    688  -2667   1613       N  
ATOM   3251  CA  ASP A 426      29.563  18.105   1.885  1.00103.71           C  
ANISOU 3251  CA  ASP A 426    11862  10492  17051    662  -2592   1929       C  
ATOM   3252  C   ASP A 426      29.769  19.384   2.689  1.00106.86           C  
ANISOU 3252  C   ASP A 426    12408  11053  17142    652  -2343   1918       C  
ATOM   3253  O   ASP A 426      28.907  20.271   2.699  1.00108.62           O  
ANISOU 3253  O   ASP A 426    12716  11388  17165    687  -2108   1989       O  
ATOM   3254  CB  ASP A 426      29.282  16.917   2.810  1.00103.82           C  
ANISOU 3254  CB  ASP A 426    11756  10466  17227    579  -2883   2212       C  
ATOM   3255  CG  ASP A 426      27.920  16.997   3.481  1.00104.52           C  
ANISOU 3255  CG  ASP A 426    11856  10704  17152    540  -2818   2545       C  
ATOM   3256  OD1 ASP A 426      27.174  17.968   3.223  1.00105.54           O  
ANISOU 3256  OD1 ASP A 426    12074  10947  17081    597  -2541   2548       O  
ATOM   3257  OD2 ASP A 426      27.601  16.084   4.272  1.00105.01           O  
ANISOU 3257  OD2 ASP A 426    11824  10770  17306    444  -3050   2811       O  
ATOM   3258  N   ASP A 427      30.912  19.495   3.367  1.00 98.10           N  
ANISOU 3258  N   ASP A 427    11322   9940  16013    600  -2397   1827       N  
ATOM   3259  CA  ASP A 427      31.249  20.665   4.178  1.00 99.81           C  
ANISOU 3259  CA  ASP A 427    11692  10294  15936    569  -2187   1796       C  
ATOM   3260  C   ASP A 427      32.218  21.535   3.388  1.00 99.23           C  
ANISOU 3260  C   ASP A 427    11694  10188  15820    625  -2045   1482       C  
ATOM   3261  O   ASP A 427      33.434  21.361   3.461  1.00 98.97           O  
ANISOU 3261  O   ASP A 427    11631  10088  15886    594  -2156   1338       O  
ATOM   3262  CB  ASP A 427      31.849  20.252   5.516  1.00101.39           C  
ANISOU 3262  CB  ASP A 427    11885  10528  16109    431  -2361   1943       C  
ATOM   3263  CG  ASP A 427      30.822  19.675   6.463  1.00102.65           C  
ANISOU 3263  CG  ASP A 427    12006  10790  16205    333  -2445   2274       C  
ATOM   3264  OD1 ASP A 427      29.644  20.085   6.380  1.00103.14           O  
ANISOU 3264  OD1 ASP A 427    12102  10956  16130    381  -2248   2371       O  
ATOM   3265  OD2 ASP A 427      31.192  18.815   7.290  1.00103.29           O  
ANISOU 3265  OD2 ASP A 427    12011  10850  16385    196  -2717   2451       O  
ATOM   3266  N   LYS A 428      31.669  22.482   2.622  1.00 90.23           N  
ANISOU 3266  N   LYS A 428    10640   9095  14547    697  -1811   1392       N  
ATOM   3267  CA  LYS A 428      32.498  23.520   2.021  1.00 89.31           C  
ANISOU 3267  CA  LYS A 428    10621   8988  14326    722  -1656   1135       C  
ATOM   3268  C   LYS A 428      32.964  24.525   3.062  1.00 89.52           C  
ANISOU 3268  C   LYS A 428    10795   9108  14112    682  -1521   1126       C  
ATOM   3269  O   LYS A 428      33.940  25.245   2.826  1.00 89.06           O  
ANISOU 3269  O   LYS A 428    10809   9048  13982    674  -1456    930       O  
ATOM   3270  CB  LYS A 428      31.726  24.229   0.911  1.00 88.39           C  
ANISOU 3270  CB  LYS A 428    10547   8886  14153    779  -1486   1085       C  
ATOM   3271  CG  LYS A 428      31.341  23.319  -0.236  1.00 88.30           C  
ANISOU 3271  CG  LYS A 428    10419   8789  14344    786  -1613   1064       C  
ATOM   3272  CD  LYS A 428      30.556  24.067  -1.295  1.00 87.63           C  
ANISOU 3272  CD  LYS A 428    10384   8726  14186    799  -1469   1056       C  
ATOM   3273  CE  LYS A 428      30.191  23.159  -2.458  1.00 87.76           C  
ANISOU 3273  CE  LYS A 428    10308   8667  14370    769  -1603   1029       C  
ATOM   3274  NZ  LYS A 428      29.206  22.113  -2.062  1.00 88.42           N  
ANISOU 3274  NZ  LYS A 428    10295   8705  14594    782  -1753   1281       N  
ATOM   3275  N   ASP A 429      32.278  24.570   4.205  1.00 91.74           N  
ANISOU 3275  N   ASP A 429    11123   9479  14257    640  -1477   1331       N  
ATOM   3276  CA  ASP A 429      32.636  25.445   5.315  1.00 94.09           C  
ANISOU 3276  CA  ASP A 429    11575   9875  14300    572  -1349   1324       C  
ATOM   3277  C   ASP A 429      34.104  25.293   5.708  1.00 94.44           C  
ANISOU 3277  C   ASP A 429    11636   9880  14367    482  -1508   1225       C  
ATOM   3278  O   ASP A 429      34.902  26.235   5.597  1.00 95.08           O  
ANISOU 3278  O   ASP A 429    11829   9967  14330    480  -1404   1050       O  
ATOM   3279  CB  ASP A 429      31.722  25.113   6.496  1.00 95.78           C  
ANISOU 3279  CB  ASP A 429    11793  10202  14395    497  -1332   1570       C  
ATOM   3280  CG  ASP A 429      31.855  26.086   7.641  1.00 98.80           C  
ANISOU 3280  CG  ASP A 429    12356  10711  14473    412  -1147   1549       C  
ATOM   3281  OD1 ASP A 429      32.628  27.060   7.526  1.00 99.46           O  
ANISOU 3281  OD1 ASP A 429    12569  10776  14446    424  -1040   1354       O  
ATOM   3282  OD2 ASP A 429      31.188  25.858   8.670  1.00100.73           O  
ANISOU 3282  OD2 ASP A 429    12615  11081  14579    316  -1110   1726       O  
ATOM   3283  N   VAL A 430      34.476  24.096   6.169  1.00 92.32           N  
ANISOU 3283  N   VAL A 430    11242   9560  14276    399  -1781   1354       N  
ATOM   3284  CA  VAL A 430      35.818  23.891   6.698  1.00 93.04           C  
ANISOU 3284  CA  VAL A 430    11324   9603  14424    294  -1963   1314       C  
ATOM   3285  C   VAL A 430      36.848  23.966   5.583  1.00 92.12           C  
ANISOU 3285  C   VAL A 430    11132   9371  14497    374  -1988   1054       C  
ATOM   3286  O   VAL A 430      38.010  24.319   5.821  1.00 92.37           O  
ANISOU 3286  O   VAL A 430    11196   9384  14518    317  -2033    954       O  
ATOM   3287  CB  VAL A 430      35.883  22.554   7.457  1.00 94.61           C  
ANISOU 3287  CB  VAL A 430    11380   9752  14816    175  -2283   1552       C  
ATOM   3288  CG1 VAL A 430      37.268  22.327   8.034  1.00 95.65           C  
ANISOU 3288  CG1 VAL A 430    11480   9813  15049     51  -2503   1546       C  
ATOM   3289  CG2 VAL A 430      34.834  22.525   8.553  1.00 95.74           C  
ANISOU 3289  CG2 VAL A 430    11600  10053  14725     64  -2235   1811       C  
ATOM   3290  N   PHE A 431      36.446  23.654   4.350  1.00 91.23           N  
ANISOU 3290  N   PHE A 431    10920   9195  14547    489  -1955    941       N  
ATOM   3291  CA  PHE A 431      37.333  23.884   3.218  1.00 90.52           C  
ANISOU 3291  CA  PHE A 431    10779   9043  14571    543  -1916    664       C  
ATOM   3292  C   PHE A 431      37.663  25.360   3.064  1.00 89.64           C  
ANISOU 3292  C   PHE A 431    10847   9026  14186    545  -1683    528       C  
ATOM   3293  O   PHE A 431      38.818  25.721   2.802  1.00 89.60           O  
ANISOU 3293  O   PHE A 431    10836   9005  14203    520  -1688    355       O  
ATOM   3294  CB  PHE A 431      36.712  23.343   1.938  1.00 89.98           C  
ANISOU 3294  CB  PHE A 431    10604   8918  14665    626  -1903    574       C  
ATOM   3295  CG  PHE A 431      37.476  23.708   0.711  1.00 89.43           C  
ANISOU 3295  CG  PHE A 431    10506   8835  14640    650  -1812    280       C  
ATOM   3296  CD1 PHE A 431      38.750  23.212   0.503  1.00 90.22           C  
ANISOU 3296  CD1 PHE A 431    10468   8850  14960    635  -1928     96       C  
ATOM   3297  CD2 PHE A 431      36.917  24.531  -0.246  1.00 88.41           C  
ANISOU 3297  CD2 PHE A 431    10468   8779  14344    673  -1618    195       C  
ATOM   3298  CE1 PHE A 431      39.461  23.550  -0.629  1.00 89.99           C  
ANISOU 3298  CE1 PHE A 431    10402   8840  14952    638  -1820   -189       C  
ATOM   3299  CE2 PHE A 431      37.620  24.866  -1.383  1.00 88.16           C  
ANISOU 3299  CE2 PHE A 431    10412   8766  14318    653  -1539    -65       C  
ATOM   3300  CZ  PHE A 431      38.895  24.375  -1.575  1.00 88.96           C  
ANISOU 3300  CZ  PHE A 431    10382   8811  14608    635  -1625   -268       C  
ATOM   3301  N   GLN A 432      36.663  26.232   3.216  1.00 89.11           N  
ANISOU 3301  N   GLN A 432    10926   9047  13886    573  -1485    605       N  
ATOM   3302  CA  GLN A 432      36.927  27.667   3.184  1.00 88.56           C  
ANISOU 3302  CA  GLN A 432    11031   9042  13577    570  -1285    493       C  
ATOM   3303  C   GLN A 432      37.861  28.073   4.316  1.00 89.34           C  
ANISOU 3303  C   GLN A 432    11237   9170  13539    471  -1327    504       C  
ATOM   3304  O   GLN A 432      38.940  28.629   4.081  1.00 89.14           O  
ANISOU 3304  O   GLN A 432    11249   9137  13485    438  -1326    355       O  
ATOM   3305  CB  GLN A 432      35.619  28.454   3.267  1.00 88.33           C  
ANISOU 3305  CB  GLN A 432    11108   9067  13384    626  -1079    586       C  
ATOM   3306  CG  GLN A 432      35.821  29.955   3.166  1.00 87.97           C  
ANISOU 3306  CG  GLN A 432    11231   9052  13140    633   -888    467       C  
ATOM   3307  CD  GLN A 432      34.523  30.733   3.243  1.00 88.64           C  
ANISOU 3307  CD  GLN A 432    11390   9156  13134    703   -688    548       C  
ATOM   3308  OE1 GLN A 432      33.448  30.157   3.420  1.00 88.46           O  
ANISOU 3308  OE1 GLN A 432    11292   9144  13176    743   -676    704       O  
ATOM   3309  NE2 GLN A 432      34.617  32.053   3.115  1.00 89.76           N  
ANISOU 3309  NE2 GLN A 432    11665   9291  13149    717   -536    447       N  
ATOM   3310  N   LYS A 433      37.464  27.785   5.561  1.00 90.43           N  
ANISOU 3310  N   LYS A 433    11426   9354  13580    396  -1372    693       N  
ATOM   3311  CA  LYS A 433      38.266  28.218   6.704  1.00 91.45           C  
ANISOU 3311  CA  LYS A 433    11688   9525  13532    261  -1412    724       C  
ATOM   3312  C   LYS A 433      39.696  27.695   6.646  1.00 91.80           C  
ANISOU 3312  C   LYS A 433    11626   9489  13767    192  -1640    669       C  
ATOM   3313  O   LYS A 433      40.613  28.359   7.144  1.00 92.23           O  
ANISOU 3313  O   LYS A 433    11794   9560  13689     99  -1651    624       O  
ATOM   3314  CB  LYS A 433      37.599  27.797   8.012  1.00 92.92           C  
ANISOU 3314  CB  LYS A 433    11925   9795  13585    148  -1452    950       C  
ATOM   3315  CG  LYS A 433      36.372  28.613   8.366  1.00 93.13           C  
ANISOU 3315  CG  LYS A 433    12092   9925  13370    188  -1174    973       C  
ATOM   3316  CD  LYS A 433      36.777  30.048   8.654  1.00 93.23           C  
ANISOU 3316  CD  LYS A 433    12325   9970  13129    167   -978    814       C  
ATOM   3317  CE  LYS A 433      37.601  30.134   9.934  1.00 94.80           C  
ANISOU 3317  CE  LYS A 433    12661  10231  13128    -43  -1079    873       C  
ATOM   3318  NZ  LYS A 433      37.997  31.531  10.281  1.00 95.14           N  
ANISOU 3318  NZ  LYS A 433    12939  10296  12912    -80   -898    714       N  
ATOM   3319  N   PHE A 434      39.918  26.525   6.046  1.00 91.85           N  
ANISOU 3319  N   PHE A 434    11405   9393  14100    236  -1825    666       N  
ATOM   3320  CA  PHE A 434      41.291  26.044   5.912  1.00 92.46           C  
ANISOU 3320  CA  PHE A 434    11340   9371  14419    192  -2023    585       C  
ATOM   3321  C   PHE A 434      42.025  26.735   4.770  1.00 91.47           C  
ANISOU 3321  C   PHE A 434    11198   9240  14315    264  -1893    317       C  
ATOM   3322  O   PHE A 434      43.178  27.151   4.938  1.00 91.86           O  
ANISOU 3322  O   PHE A 434    11261   9280  14363    198  -1939    245       O  
ATOM   3323  CB  PHE A 434      41.319  24.526   5.729  1.00 93.32           C  
ANISOU 3323  CB  PHE A 434    11194   9347  14917    213  -2274    656       C  
ATOM   3324  CG  PHE A 434      41.141  23.759   7.010  1.00 94.91           C  
ANISOU 3324  CG  PHE A 434    11374   9534  15153     73  -2510    947       C  
ATOM   3325  CD1 PHE A 434      41.293  24.388   8.235  1.00 95.72           C  
ANISOU 3325  CD1 PHE A 434    11668   9743  14959    -91  -2508   1096       C  
ATOM   3326  CD2 PHE A 434      40.840  22.408   6.992  1.00 95.82           C  
ANISOU 3326  CD2 PHE A 434    11283   9533  15591     80  -2748   1074       C  
ATOM   3327  CE1 PHE A 434      41.138  23.688   9.416  1.00 97.46           C  
ANISOU 3327  CE1 PHE A 434    11876   9979  15177   -269  -2735   1380       C  
ATOM   3328  CE2 PHE A 434      40.687  21.703   8.171  1.00 97.49           C  
ANISOU 3328  CE2 PHE A 434    11469   9741  15832    -82  -2995   1372       C  
ATOM   3329  CZ  PHE A 434      40.835  22.345   9.383  1.00 98.34           C  
ANISOU 3329  CZ  PHE A 434    11769   9979  15614   -269  -2988   1532       C  
ATOM   3330  N   TYR A 435      41.380  26.877   3.609  1.00 90.34           N  
ANISOU 3330  N   TYR A 435    11029   9114  14181    373  -1740    186       N  
ATOM   3331  CA  TYR A 435      42.043  27.542   2.493  1.00 89.63           C  
ANISOU 3331  CA  TYR A 435    10927   9050  14078    401  -1618    -56       C  
ATOM   3332  C   TYR A 435      42.362  28.992   2.812  1.00 89.19           C  
ANISOU 3332  C   TYR A 435    11090   9080  13718    349  -1477    -82       C  
ATOM   3333  O   TYR A 435      43.245  29.577   2.174  1.00 88.98           O  
ANISOU 3333  O   TYR A 435    11055   9080  13673    325  -1430   -248       O  
ATOM   3334  CB  TYR A 435      41.182  27.436   1.236  1.00 88.75           C  
ANISOU 3334  CB  TYR A 435    10770   8956  13996    482  -1499   -154       C  
ATOM   3335  CG  TYR A 435      41.824  27.983  -0.018  1.00 88.33           C  
ANISOU 3335  CG  TYR A 435    10685   8953  13924    470  -1389   -398       C  
ATOM   3336  CD1 TYR A 435      42.963  27.398  -0.545  1.00 89.15           C  
ANISOU 3336  CD1 TYR A 435    10602   9017  14253    452  -1464   -590       C  
ATOM   3337  CD2 TYR A 435      41.250  29.029  -0.716  1.00 87.40           C  
ANISOU 3337  CD2 TYR A 435    10701   8920  13586    465  -1216   -432       C  
ATOM   3338  CE1 TYR A 435      43.543  27.876  -1.702  1.00 89.05           C  
ANISOU 3338  CE1 TYR A 435    10552   9084  14197    414  -1345   -821       C  
ATOM   3339  CE2 TYR A 435      41.819  29.509  -1.880  1.00 87.24           C  
ANISOU 3339  CE2 TYR A 435    10652   8970  13526    413  -1133   -633       C  
ATOM   3340  CZ  TYR A 435      42.964  28.928  -2.368  1.00 88.07           C  
ANISOU 3340  CZ  TYR A 435    10583   9068  13811    381  -1187   -832       C  
ATOM   3341  OH  TYR A 435      43.536  29.400  -3.524  1.00 88.19           O  
ANISOU 3341  OH  TYR A 435    10563   9186  13758    303  -1086  -1040       O  
ATOM   3342  N   ALA A 436      41.681  29.571   3.805  1.00 92.49           N  
ANISOU 3342  N   ALA A 436    11698   9543  13902    320  -1409     70       N  
ATOM   3343  CA  ALA A 436      42.018  30.914   4.263  1.00 94.25           C  
ANISOU 3343  CA  ALA A 436    12139   9820  13851    262  -1293     38       C  
ATOM   3344  C   ALA A 436      43.425  30.958   4.848  1.00 95.13           C  
ANISOU 3344  C   ALA A 436    12251   9913  13983    146  -1442     27       C  
ATOM   3345  O   ALA A 436      44.227  31.828   4.494  1.00 95.72           O  
ANISOU 3345  O   ALA A 436    12389  10008  13971    111  -1396    -92       O  
ATOM   3346  CB  ALA A 436      40.992  31.391   5.292  1.00 95.61           C  
ANISOU 3346  CB  ALA A 436    12498  10038  13794    248  -1180    176       C  
ATOM   3347  N   ARG A 437      43.744  30.026   5.750  1.00107.02           N  
ANISOU 3347  N   ARG A 437    13677  11374  15611     67  -1644    175       N  
ATOM   3348  CA  ARG A 437      45.092  29.991   6.312  1.00107.67           C  
ANISOU 3348  CA  ARG A 437    13733  11419  15757    -58  -1823    200       C  
ATOM   3349  C   ARG A 437      46.111  29.478   5.303  1.00105.54           C  
ANISOU 3349  C   ARG A 437    13213  11081  15806     -9  -1906     40       C  
ATOM   3350  O   ARG A 437      47.266  29.926   5.314  1.00106.53           O  
ANISOU 3350  O   ARG A 437    13329  11202  15946    -80  -1958    -20       O  
ATOM   3351  CB  ARG A 437      45.121  29.141   7.582  1.00107.20           C  
ANISOU 3351  CB  ARG A 437    13653  11326  15751   -190  -2047    439       C  
ATOM   3352  CG  ARG A 437      44.413  29.779   8.766  1.00110.09           C  
ANISOU 3352  CG  ARG A 437    14291  11793  15747   -304  -1958    577       C  
ATOM   3353  CD  ARG A 437      44.487  28.884   9.987  1.00109.90           C  
ANISOU 3353  CD  ARG A 437    14238  11762  15757   -486  -2205    833       C  
ATOM   3354  NE  ARG A 437      45.869  28.657  10.400  1.00110.12           N  
ANISOU 3354  NE  ARG A 437    14192  11713  15935   -633  -2462    904       N  
ATOM   3355  CZ  ARG A 437      46.549  29.443  11.229  1.00112.53           C  
ANISOU 3355  CZ  ARG A 437    14699  12063  15994   -815  -2498    955       C  
ATOM   3356  NH1 ARG A 437      45.976  30.521  11.746  1.00115.78           N  
ANISOU 3356  NH1 ARG A 437    15408  12593  15990   -867  -2276    913       N  
ATOM   3357  NH2 ARG A 437      47.804  29.147  11.542  1.00110.99           N  
ANISOU 3357  NH2 ARG A 437    14401  11782  15987   -950  -2760   1046       N  
ATOM   3358  N   MET A 438      45.709  28.540   4.439  1.00 97.00           N  
ANISOU 3358  N   MET A 438    11925   9949  14983    104  -1915    -40       N  
ATOM   3359  CA  MET A 438      46.567  28.129   3.331  1.00 95.97           C  
ANISOU 3359  CA  MET A 438    11560   9773  15130    157  -1927   -258       C  
ATOM   3360  C   MET A 438      47.046  29.346   2.547  1.00 96.58           C  
ANISOU 3360  C   MET A 438    11736   9957  15002    143  -1742   -437       C  
ATOM   3361  O   MET A 438      48.244  29.509   2.284  1.00 96.82           O  
ANISOU 3361  O   MET A 438    11662   9988  15139     97  -1780   -547       O  
ATOM   3362  CB  MET A 438      45.809  27.174   2.402  1.00 94.41           C  
ANISOU 3362  CB  MET A 438    11196   9531  15145    272  -1899   -352       C  
ATOM   3363  CG  MET A 438      45.292  25.872   3.029  1.00 93.69           C  
ANISOU 3363  CG  MET A 438    10978   9320  15299    289  -2104   -177       C  
ATOM   3364  SD  MET A 438      46.523  24.717   3.660  1.00 95.28           S  
ANISOU 3364  SD  MET A 438    10908   9338  15957    232  -2430   -112       S  
ATOM   3365  CE  MET A 438      46.348  24.959   5.427  1.00 95.97           C  
ANISOU 3365  CE  MET A 438    11195   9453  15815     63  -2598    250       C  
ATOM   3366  N   LEU A 439      46.107  30.226   2.182  1.00 92.92           N  
ANISOU 3366  N   LEU A 439    11464   9583  14259    174  -1553   -449       N  
ATOM   3367  CA  LEU A 439      46.445  31.432   1.431  1.00 92.25           C  
ANISOU 3367  CA  LEU A 439    11483   9595  13973    142  -1403   -584       C  
ATOM   3368  C   LEU A 439      47.188  32.449   2.288  1.00 92.60           C  
ANISOU 3368  C   LEU A 439    11708   9659  13816     40  -1433   -515       C  
ATOM   3369  O   LEU A 439      48.063  33.161   1.781  1.00 92.64           O  
ANISOU 3369  O   LEU A 439    11715   9720  13765    -20  -1402   -624       O  
ATOM   3370  CB  LEU A 439      45.168  32.038   0.845  1.00 91.11           C  
ANISOU 3370  CB  LEU A 439    11472   9504  13640    197  -1233   -580       C  
ATOM   3371  CG  LEU A 439      45.239  33.251  -0.079  1.00 90.48           C  
ANISOU 3371  CG  LEU A 439    11493   9515  13371    154  -1097   -686       C  
ATOM   3372  CD1 LEU A 439      44.140  33.177  -1.118  1.00 89.79           C  
ANISOU 3372  CD1 LEU A 439    11380   9457  13278    201   -995   -714       C  
ATOM   3373  CD2 LEU A 439      45.079  34.511   0.737  1.00 90.35           C  
ANISOU 3373  CD2 LEU A 439    11731   9497  13100    119  -1048   -589       C  
ATOM   3374  N   ALA A 440      46.857  32.535   3.577  1.00 96.71           N  
ANISOU 3374  N   ALA A 440    12387  10146  14211     -3  -1496   -336       N  
ATOM   3375  CA  ALA A 440      47.531  33.479   4.463  1.00 97.29           C  
ANISOU 3375  CA  ALA A 440    12659  10233  14072   -124  -1533   -272       C  
ATOM   3376  C   ALA A 440      49.022  33.179   4.543  1.00 98.31           C  
ANISOU 3376  C   ALA A 440    12636  10331  14385   -214  -1706   -287       C  
ATOM   3377  O   ALA A 440      49.863  34.021   4.204  1.00 98.33           O  
ANISOU 3377  O   ALA A 440    12681  10376  14303   -275  -1683   -367       O  
ATOM   3378  CB  ALA A 440      46.895  33.437   5.853  1.00 97.99           C  
ANISOU 3378  CB  ALA A 440    12930  10309  13995   -185  -1570    -89       C  
ATOM   3379  N   LYS A 441      49.367  31.968   4.986  1.00103.03           N  
ANISOU 3379  N   LYS A 441    13039  10844  15263   -228  -1895   -197       N  
ATOM   3380  CA  LYS A 441      50.770  31.572   4.989  1.00102.62           C  
ANISOU 3380  CA  LYS A 441    12783  10734  15474   -296  -2068   -211       C  
ATOM   3381  C   LYS A 441      51.352  31.588   3.582  1.00101.73           C  
ANISOU 3381  C   LYS A 441    12461  10664  15527   -222  -1956   -459       C  
ATOM   3382  O   LYS A 441      52.551  31.830   3.408  1.00101.99           O  
ANISOU 3382  O   LYS A 441    12387  10704  15662   -288  -2012   -515       O  
ATOM   3383  CB  LYS A 441      50.923  30.184   5.616  1.00102.03           C  
ANISOU 3383  CB  LYS A 441    12497  10529  15741   -312  -2308    -68       C  
ATOM   3384  CG  LYS A 441      50.582  30.124   7.100  1.00103.25           C  
ANISOU 3384  CG  LYS A 441    12840  10664  15724   -455  -2462    206       C  
ATOM   3385  CD  LYS A 441      50.741  28.711   7.653  1.00103.03           C  
ANISOU 3385  CD  LYS A 441    12580  10500  16066   -494  -2741    377       C  
ATOM   3386  CE  LYS A 441      50.349  28.641   9.124  1.00104.18           C  
ANISOU 3386  CE  LYS A 441    12923  10663  15998   -684  -2899    667       C  
ATOM   3387  NZ  LYS A 441      50.479  27.264   9.679  1.00105.86           N  
ANISOU 3387  NZ  LYS A 441    12905  10740  16578   -753  -3212    876       N  
ATOM   3388  N   ARG A 442      50.518  31.350   2.564  1.00 99.21           N  
ANISOU 3388  N   ARG A 442    12085  10388  15223   -106  -1796   -604       N  
ATOM   3389  CA  ARG A 442      51.013  31.325   1.193  1.00 99.23           C  
ANISOU 3389  CA  ARG A 442    11898  10460  15344    -73  -1675   -854       C  
ATOM   3390  C   ARG A 442      51.340  32.713   0.656  1.00 98.57           C  
ANISOU 3390  C   ARG A 442    11974  10517  14963   -151  -1539   -929       C  
ATOM   3391  O   ARG A 442      52.021  32.815  -0.369  1.00 98.99           O  
ANISOU 3391  O   ARG A 442    11871  10658  15083   -178  -1457  -1118       O  
ATOM   3392  CB  ARG A 442      49.997  30.639   0.276  1.00 98.59           C  
ANISOU 3392  CB  ARG A 442    11729  10388  15344     36  -1564   -973       C  
ATOM   3393  N   LEU A 443      50.875  33.780   1.308  1.00 95.71           N  
ANISOU 3393  N   LEU A 443    11910  10176  14279   -197  -1513   -793       N  
ATOM   3394  CA  LEU A 443      51.185  35.141   0.879  1.00 96.31           C  
ANISOU 3394  CA  LEU A 443    12146  10354  14093   -280  -1423   -838       C  
ATOM   3395  C   LEU A 443      52.140  35.867   1.814  1.00 97.11           C  
ANISOU 3395  C   LEU A 443    12380  10434  14085   -400  -1544   -726       C  
ATOM   3396  O   LEU A 443      53.152  36.409   1.358  1.00 97.17           O  
ANISOU 3396  O   LEU A 443    12329  10511  14080   -488  -1555   -792       O  
ATOM   3397  CB  LEU A 443      49.903  35.976   0.725  1.00 96.81           C  
ANISOU 3397  CB  LEU A 443    12447  10441  13894   -241  -1289   -800       C  
ATOM   3398  CG  LEU A 443      48.967  35.670  -0.442  1.00 96.20           C  
ANISOU 3398  CG  LEU A 443    12285  10416  13851   -169  -1161   -900       C  
ATOM   3399  CD1 LEU A 443      47.763  36.591  -0.382  1.00 96.91           C  
ANISOU 3399  CD1 LEU A 443    12607  10493  13721   -139  -1063   -815       C  
ATOM   3400  CD2 LEU A 443      49.694  35.817  -1.768  1.00 95.78           C  
ANISOU 3400  CD2 LEU A 443    12074  10493  13827   -248  -1100  -1080       C  
ATOM   3401  N   ILE A 444      51.853  35.887   3.118  1.00106.50           N  
ANISOU 3401  N   ILE A 444    13747  11539  15179   -429  -1640   -552       N  
ATOM   3402  CA  ILE A 444      52.623  36.696   4.054  1.00107.33           C  
ANISOU 3402  CA  ILE A 444    14038  11624  15117   -572  -1752   -438       C  
ATOM   3403  C   ILE A 444      54.084  36.261   4.135  1.00106.89           C  
ANISOU 3403  C   ILE A 444    13766  11548  15298   -661  -1925   -416       C  
ATOM   3404  O   ILE A 444      54.900  36.949   4.754  1.00107.65           O  
ANISOU 3404  O   ILE A 444    13988  11637  15277   -800  -2036   -320       O  
ATOM   3405  CB  ILE A 444      51.931  36.665   5.439  1.00108.89           C  
ANISOU 3405  CB  ILE A 444    14466  11755  15151   -611  -1806   -271       C  
ATOM   3406  CG1 ILE A 444      50.472  37.096   5.298  1.00110.65           C  
ANISOU 3406  CG1 ILE A 444    14862  11996  15185   -504  -1609   -311       C  
ATOM   3407  CG2 ILE A 444      52.593  37.613   6.430  1.00109.61           C  
ANISOU 3407  CG2 ILE A 444    14808  11831  15006   -782  -1904   -168       C  
ATOM   3408  CD1 ILE A 444      50.301  38.509   4.776  1.00111.17           C  
ANISOU 3408  CD1 ILE A 444    15116  12098  15026   -510  -1477   -399       C  
ATOM   3409  N   HIS A 445      54.452  35.155   3.486  1.00119.26           N  
ANISOU 3409  N   HIS A 445    14999  13098  17216   -587  -1947   -511       N  
ATOM   3410  CA  HIS A 445      55.840  34.712   3.470  1.00117.43           C  
ANISOU 3410  CA  HIS A 445    14508  12832  17278   -652  -2093   -512       C  
ATOM   3411  C   HIS A 445      56.319  34.414   2.054  1.00116.15           C  
ANISOU 3411  C   HIS A 445    14051  12758  17323   -587  -1955   -763       C  
ATOM   3412  O   HIS A 445      57.239  33.612   1.863  1.00114.51           O  
ANISOU 3412  O   HIS A 445    13525  12498  17484   -578  -2035   -825       O  
ATOM   3413  CB  HIS A 445      56.030  33.496   4.375  1.00116.06           C  
ANISOU 3413  CB  HIS A 445    14174  12503  17420   -656  -2314   -359       C  
ATOM   3414  CG  HIS A 445      55.754  33.781   5.816  1.00117.97           C  
ANISOU 3414  CG  HIS A 445    14697  12689  17439   -784  -2468   -103       C  
ATOM   3415  ND1 HIS A 445      56.612  34.518   6.605  1.00119.17           N  
ANISOU 3415  ND1 HIS A 445    15000  12834  17444   -965  -2613     46       N  
ATOM   3416  CD2 HIS A 445      54.711  33.442   6.609  1.00119.40           C  
ANISOU 3416  CD2 HIS A 445    15040  12835  17493   -781  -2491     24       C  
ATOM   3417  CE1 HIS A 445      56.110  34.615   7.823  1.00120.82           C  
ANISOU 3417  CE1 HIS A 445    15465  13009  17433  -1078  -2713    240       C  
ATOM   3418  NE2 HIS A 445      54.958  33.970   7.852  1.00120.96           N  
ANISOU 3418  NE2 HIS A 445    15487  13018  17456   -969  -2634    228       N  
ATOM   3419  N   GLY A 446      55.710  35.057   1.062  1.00114.42           N  
ANISOU 3419  N   GLY A 446    13926  12673  16877   -559  -1751   -907       N  
ATOM   3420  CA  GLY A 446      56.188  34.952  -0.316  1.00114.18           C  
ANISOU 3420  CA  GLY A 446    13656  12775  16953   -556  -1603  -1150       C  
ATOM   3421  C   GLY A 446      56.341  33.533  -0.813  1.00112.98           C  
ANISOU 3421  C   GLY A 446    13155  12562  17209   -451  -1585  -1318       C  
ATOM   3422  O   GLY A 446      57.339  33.206  -1.470  1.00112.36           O  
ANISOU 3422  O   GLY A 446    12791  12536  17364   -473  -1542  -1492       O  
ATOM   3423  N   LEU A 447      55.370  32.674  -0.512  1.00108.79           N  
ANISOU 3423  N   LEU A 447    12633  11918  16785   -337  -1615  -1279       N  
ATOM   3424  CA  LEU A 447      55.458  31.268  -0.877  1.00108.25           C  
ANISOU 3424  CA  LEU A 447    12244  11748  17139   -232  -1632  -1426       C  
ATOM   3425  C   LEU A 447      54.769  30.944  -2.194  1.00107.84           C  
ANISOU 3425  C   LEU A 447    12116  11799  17059   -174  -1421  -1679       C  
ATOM   3426  O   LEU A 447      55.061  29.899  -2.787  1.00107.70           O  
ANISOU 3426  O   LEU A 447    11804  11730  17387   -107  -1387  -1890       O  
ATOM   3427  CB  LEU A 447      54.860  30.400   0.234  1.00107.80           C  
ANISOU 3427  CB  LEU A 447    12214  11497  17250   -165  -1828  -1216       C  
ATOM   3428  CG  LEU A 447      55.636  30.400   1.551  1.00108.15           C  
ANISOU 3428  CG  LEU A 447    12270  11418  17403   -253  -2081   -964       C  
ATOM   3429  CD1 LEU A 447      54.871  29.651   2.626  1.00108.08           C  
ANISOU 3429  CD1 LEU A 447    12336  11263  17468   -233  -2267   -733       C  
ATOM   3430  CD2 LEU A 447      57.010  29.786   1.344  1.00108.27           C  
ANISOU 3430  CD2 LEU A 447    11916  11352  17868   -262  -2177  -1063       C  
ATOM   3431  N   SER A 448      53.875  31.810  -2.667  1.00103.49           N  
ANISOU 3431  N   SER A 448    11817  11380  16125   -210  -1288  -1664       N  
ATOM   3432  CA  SER A 448      53.113  31.518  -3.870  1.00103.17           C  
ANISOU 3432  CA  SER A 448    11736  11435  16028   -189  -1118  -1858       C  
ATOM   3433  C   SER A 448      54.024  31.494  -5.097  1.00103.82           C  
ANISOU 3433  C   SER A 448    11589  11682  16176   -276   -964  -2155       C  
ATOM   3434  O   SER A 448      55.205  31.851  -5.046  1.00104.45           O  
ANISOU 3434  O   SER A 448    11553  11817  16315   -350   -975  -2196       O  
ATOM   3435  CB  SER A 448      51.995  32.542  -4.059  1.00103.19           C  
ANISOU 3435  CB  SER A 448    12050  11528  15632   -230  -1042  -1734       C  
ATOM   3436  OG  SER A 448      51.258  32.273  -5.240  1.00102.99           O  
ANISOU 3436  OG  SER A 448    11989  11596  15547   -243   -904  -1890       O  
ATOM   3437  N   MET A 449      53.453  31.054  -6.218  1.00107.71           N  
ANISOU 3437  N   MET A 449    12015  12264  16648   -285   -814  -2364       N  
ATOM   3438  CA  MET A 449      54.183  30.959  -7.471  1.00108.67           C  
ANISOU 3438  CA  MET A 449    11925  12572  16791   -396   -632  -2683       C  
ATOM   3439  C   MET A 449      53.683  31.914  -8.541  1.00109.14           C  
ANISOU 3439  C   MET A 449    12160  12878  16430   -574   -487  -2721       C  
ATOM   3440  O   MET A 449      54.452  32.257  -9.444  1.00110.17           O  
ANISOU 3440  O   MET A 449    12173  13223  16464   -732   -350  -2920       O  
ATOM   3441  CB  MET A 449      54.118  29.526  -8.019  1.00108.77           C  
ANISOU 3441  CB  MET A 449    11670  12496  17161   -302   -569  -2960       C  
ATOM   3442  N   SER A 450      52.425  32.347  -8.467  1.00117.20           N  
ANISOU 3442  N   SER A 450    13442  13875  17213   -566   -522  -2527       N  
ATOM   3443  CA  SER A 450      51.864  33.248  -9.471  1.00118.54           C  
ANISOU 3443  CA  SER A 450    13773  14249  17017   -750   -428  -2518       C  
ATOM   3444  C   SER A 450      50.673  33.973  -8.867  1.00118.43           C  
ANISOU 3444  C   SER A 450    14052  14133  16812   -698   -527  -2209       C  
ATOM   3445  O   SER A 450      49.673  33.334  -8.521  1.00118.40           O  
ANISOU 3445  O   SER A 450    14096  13983  16909   -564   -570  -2125       O  
ATOM   3446  CB  SER A 450      51.444  32.476 -10.725  1.00118.86           C  
ANISOU 3446  CB  SER A 450    13696  14402  17064   -830   -288  -2772       C  
ATOM   3447  OG  SER A 450      52.560  31.888 -11.369  1.00120.92           O  
ANISOU 3447  OG  SER A 450    13677  14778  17488   -895   -155  -3105       O  
ATOM   3448  N   MET A 451      50.780  35.298  -8.735  1.00109.61           N  
ANISOU 3448  N   MET A 451    13121  13086  15442   -803   -564  -2046       N  
ATOM   3449  CA  MET A 451      49.635  36.099  -8.312  1.00109.32           C  
ANISOU 3449  CA  MET A 451    13345  12956  15236   -768   -631  -1790       C  
ATOM   3450  C   MET A 451      48.512  36.023  -9.337  1.00109.24           C  
ANISOU 3450  C   MET A 451    13378  13012  15116   -847   -576  -1789       C  
ATOM   3451  O   MET A 451      47.338  35.849  -8.979  1.00108.88           O  
ANISOU 3451  O   MET A 451    13437  12831  15103   -731   -611  -1640       O  
ATOM   3452  CB  MET A 451      50.067  37.550  -8.099  1.00109.70           C  
ANISOU 3452  CB  MET A 451    13561  13057  15065   -883   -686  -1650       C  
ATOM   3453  CG  MET A 451      51.045  37.742  -6.956  1.00109.96           C  
ANISOU 3453  CG  MET A 451    13602  13000  15176   -818   -769  -1597       C  
ATOM   3454  SD  MET A 451      50.317  37.407  -5.344  1.00109.82           S  
ANISOU 3454  SD  MET A 451    13733  12721  15274   -595   -863  -1407       S  
ATOM   3455  CE  MET A 451      49.312  38.871  -5.124  1.00110.80           C  
ANISOU 3455  CE  MET A 451    14166  12790  15142   -621   -881  -1203       C  
ATOM   3456  N   ASP A 452      48.861  36.141 -10.622  1.00118.57           N  
ANISOU 3456  N   ASP A 452    14475  14416  16162  -1065   -492  -1949       N  
ATOM   3457  CA  ASP A 452      47.875  36.066 -11.694  1.00118.02           C  
ANISOU 3457  CA  ASP A 452    14445  14433  15965  -1199   -457  -1944       C  
ATOM   3458  C   ASP A 452      47.094  34.757 -11.645  1.00117.96           C  
ANISOU 3458  C   ASP A 452    14361  14300  16161  -1046   -438  -2012       C  
ATOM   3459  O   ASP A 452      45.904  34.730 -11.981  1.00117.55           O  
ANISOU 3459  O   ASP A 452    14404  14205  16055  -1062   -469  -1881       O  
ATOM   3460  CB  ASP A 452      48.581  36.223 -13.044  1.00117.69           C  
ANISOU 3460  CB  ASP A 452    14297  14681  15738  -1492   -357  -2151       C  
ATOM   3461  CG  ASP A 452      47.620  36.493 -14.191  1.00117.93           C  
ANISOU 3461  CG  ASP A 452    14416  14835  15556  -1718   -361  -2082       C  
ATOM   3462  OD1 ASP A 452      46.399  36.592 -13.952  1.00118.77           O  
ANISOU 3462  OD1 ASP A 452    14654  14785  15687  -1632   -448  -1863       O  
ATOM   3463  OD2 ASP A 452      48.095  36.602 -15.342  1.00117.81           O  
ANISOU 3463  OD2 ASP A 452    14331  15083  15347  -2002   -279  -2243       O  
ATOM   3464  N   SER A 453      47.735  33.669 -11.214  1.00115.78           N  
ANISOU 3464  N   SER A 453    13903  13946  16143   -901   -409  -2197       N  
ATOM   3465  CA  SER A 453      47.061  32.377 -11.156  1.00114.89           C  
ANISOU 3465  CA  SER A 453    13704  13697  16252   -761   -416  -2264       C  
ATOM   3466  C   SER A 453      46.274  32.214  -9.860  1.00114.24           C  
ANISOU 3466  C   SER A 453    13725  13379  16302   -533   -537  -2005       C  
ATOM   3467  O   SER A 453      45.107  31.801  -9.882  1.00113.96           O  
ANISOU 3467  O   SER A 453    13749  13256  16297   -471   -572  -1889       O  
ATOM   3468  CB  SER A 453      48.082  31.247 -11.310  1.00114.70           C  
ANISOU 3468  CB  SER A 453    13415  13671  16496   -713   -348  -2582       C  
ATOM   3469  OG  SER A 453      47.455  29.979 -11.232  1.00114.51           O  
ANISOU 3469  OG  SER A 453    13302  13490  16718   -578   -381  -2646       O  
ATOM   3470  N   GLU A 454      46.896  32.533  -8.720  1.00101.06           N  
ANISOU 3470  N   GLU A 454    12080  11618  14701   -427   -603  -1908       N  
ATOM   3471  CA  GLU A 454      46.205  32.403  -7.442  1.00100.45           C  
ANISOU 3471  CA  GLU A 454    12107  11348  14710   -248   -704  -1674       C  
ATOM   3472  C   GLU A 454      44.972  33.293  -7.368  1.00100.83           C  
ANISOU 3472  C   GLU A 454    12374  11376  14560   -253   -706  -1441       C  
ATOM   3473  O   GLU A 454      44.047  32.996  -6.602  1.00100.31           O  
ANISOU 3473  O   GLU A 454    12374  11176  14562   -119   -752  -1271       O  
ATOM   3474  CB  GLU A 454      47.158  32.713  -6.288  1.00100.48           C  
ANISOU 3474  CB  GLU A 454    12123  11286  14770   -193   -776  -1612       C  
ATOM   3475  CG  GLU A 454      46.541  32.498  -4.917  1.00100.18           C  
ANISOU 3475  CG  GLU A 454    12189  11077  14799    -47   -877  -1389       C  
ATOM   3476  CD  GLU A 454      47.530  32.680  -3.791  1.00100.35           C  
ANISOU 3476  CD  GLU A 454    12218  11037  14874    -33   -970  -1327       C  
ATOM   3477  OE1 GLU A 454      48.711  32.970  -4.076  1.00100.45           O  
ANISOU 3477  OE1 GLU A 454    12142  11126  14899   -117   -963  -1450       O  
ATOM   3478  OE2 GLU A 454      47.124  32.531  -2.620  1.00100.85           O  
ANISOU 3478  OE2 GLU A 454    12375  10985  14958     44  -1055  -1148       O  
ATOM   3479  N   GLU A 455      44.926  34.371  -8.152  1.00106.55           N  
ANISOU 3479  N   GLU A 455    13195  12227  15061   -413   -664  -1420       N  
ATOM   3480  CA  GLU A 455      43.667  35.089  -8.307  1.00107.63           C  
ANISOU 3480  CA  GLU A 455    13490  12324  15080   -426   -676  -1212       C  
ATOM   3481  C   GLU A 455      42.645  34.229  -9.040  1.00107.28           C  
ANISOU 3481  C   GLU A 455    13385  12272  15105   -432   -669  -1210       C  
ATOM   3482  O   GLU A 455      41.499  34.093  -8.596  1.00106.84           O  
ANISOU 3482  O   GLU A 455    13390  12092  15110   -318   -698  -1027       O  
ATOM   3483  CB  GLU A 455      43.888  36.406  -9.050  1.00108.02           C  
ANISOU 3483  CB  GLU A 455    13635  12497  14909   -625   -673  -1173       C  
ATOM   3484  CG  GLU A 455      42.627  37.246  -9.170  1.00109.35           C  
ANISOU 3484  CG  GLU A 455    13948  12588  15013   -636   -709   -939       C  
ATOM   3485  CD  GLU A 455      42.861  38.553  -9.894  1.00109.25           C  
ANISOU 3485  CD  GLU A 455    14019  12675  14818   -849   -750   -873       C  
ATOM   3486  OE1 GLU A 455      44.003  38.785 -10.345  1.00108.40           O  
ANISOU 3486  OE1 GLU A 455    13862  12726  14600  -1002   -738  -1013       O  
ATOM   3487  OE2 GLU A 455      41.904  39.348 -10.009  1.00110.15           O  
ANISOU 3487  OE2 GLU A 455    14233  12701  14919   -868   -802   -673       O  
ATOM   3488  N   ALA A 456      43.052  33.627 -10.163  1.00107.66           N  
ANISOU 3488  N   ALA A 456    13308  12456  15142   -576   -624  -1422       N  
ATOM   3489  CA  ALA A 456      42.130  32.832 -10.969  1.00107.60           C  
ANISOU 3489  CA  ALA A 456    13259  12452  15173   -623   -625  -1436       C  
ATOM   3490  C   ALA A 456      41.578  31.643 -10.194  1.00106.02           C  
ANISOU 3490  C   ALA A 456    12990  12075  15217   -408   -673  -1398       C  
ATOM   3491  O   ALA A 456      40.474  31.171 -10.489  1.00105.44           O  
ANISOU 3491  O   ALA A 456    12933  11945  15185   -396   -709  -1290       O  
ATOM   3492  CB  ALA A 456      42.824  32.360 -12.247  1.00107.72           C  
ANISOU 3492  CB  ALA A 456    13153  12656  15120   -831   -545  -1728       C  
ATOM   3493  N   MET A 457      42.328  31.138  -9.213  1.00108.43           N  
ANISOU 3493  N   MET A 457    13215  12291  15693   -257   -696  -1463       N  
ATOM   3494  CA  MET A 457      41.777  30.123  -8.321  1.00106.93           C  
ANISOU 3494  CA  MET A 457    12973  11929  15727    -71   -778  -1365       C  
ATOM   3495  C   MET A 457      40.576  30.663  -7.555  1.00106.59           C  
ANISOU 3495  C   MET A 457    13083  11796  15620     23   -810  -1059       C  
ATOM   3496  O   MET A 457      39.518  30.021  -7.491  1.00105.46           O  
ANISOU 3496  O   MET A 457    12929  11573  15569     89   -854   -933       O  
ATOM   3497  CB  MET A 457      42.851  29.627  -7.354  1.00106.51           C  
ANISOU 3497  CB  MET A 457    12812  11797  15861     35   -830  -1445       C  
ATOM   3498  CG  MET A 457      42.334  28.586  -6.389  1.00104.52           C  
ANISOU 3498  CG  MET A 457    12503  11374  15837    193   -947  -1315       C  
ATOM   3499  SD  MET A 457      41.713  27.146  -7.268  1.00103.59           S  
ANISOU 3499  SD  MET A 457    12235  11196  15931    201   -987  -1441       S  
ATOM   3500  CE  MET A 457      40.530  26.520  -6.080  1.00102.04           C  
ANISOU 3500  CE  MET A 457    12078  10837  15857    352  -1126  -1122       C  
ATOM   3501  N   ILE A 458      40.725  31.851  -6.963  1.00 93.70           N  
ANISOU 3501  N   ILE A 458    11587  10173  13842     26   -783   -946       N  
ATOM   3502  CA  ILE A 458      39.616  32.461  -6.241  1.00 92.96           C  
ANISOU 3502  CA  ILE A 458    11628   9994  13698    115   -778   -696       C  
ATOM   3503  C   ILE A 458      38.484  32.795  -7.203  1.00 92.92           C  
ANISOU 3503  C   ILE A 458    11658  10008  13638     38   -764   -583       C  
ATOM   3504  O   ILE A 458      37.311  32.821  -6.814  1.00 92.60           O  
ANISOU 3504  O   ILE A 458    11656   9879  13647    127   -767   -383       O  
ATOM   3505  CB  ILE A 458      40.117  33.696  -5.467  1.00 92.72           C  
ANISOU 3505  CB  ILE A 458    11738   9960  13531    121   -745   -648       C  
ATOM   3506  CG1 ILE A 458      41.234  33.286  -4.509  1.00 92.95           C  
ANISOU 3506  CG1 ILE A 458    11728   9967  13621    170   -788   -731       C  
ATOM   3507  CG2 ILE A 458      38.993  34.328  -4.670  1.00 92.36           C  
ANISOU 3507  CG2 ILE A 458    11818   9817  13455    223   -708   -436       C  
ATOM   3508  CD1 ILE A 458      41.965  34.445  -3.889  1.00 92.94           C  
ANISOU 3508  CD1 ILE A 458    11863   9979  13473    135   -772   -721       C  
ATOM   3509  N   ASN A 459      38.812  33.033  -8.476  1.00102.92           N  
ANISOU 3509  N   ASN A 459    12903  11397  14805   -147   -754   -700       N  
ATOM   3510  CA  ASN A 459      37.781  33.156  -9.501  1.00104.28           C  
ANISOU 3510  CA  ASN A 459    13093  11594  14937   -267   -777   -586       C  
ATOM   3511  C   ASN A 459      37.023  31.843  -9.668  1.00102.62           C  
ANISOU 3511  C   ASN A 459    12791  11323  14876   -210   -821   -568       C  
ATOM   3512  O   ASN A 459      35.798  31.841  -9.842  1.00102.44           O  
ANISOU 3512  O   ASN A 459    12792  11238  14894   -202   -860   -359       O  
ATOM   3513  CB  ASN A 459      38.415  33.591 -10.825  1.00106.59           C  
ANISOU 3513  CB  ASN A 459    13380  12063  15058   -528   -766   -730       C  
ATOM   3514  CG  ASN A 459      37.388  33.968 -11.880  1.00108.21           C  
ANISOU 3514  CG  ASN A 459    13630  12301  15186   -708   -822   -563       C  
ATOM   3515  OD1 ASN A 459      36.181  33.912 -11.645  1.00109.21           O  
ANISOU 3515  OD1 ASN A 459    13776  12303  15416   -621   -867   -337       O  
ATOM   3516  ND2 ASN A 459      37.869  34.351 -13.057  1.00108.28           N  
ANISOU 3516  ND2 ASN A 459    13643  12486  15012   -982   -825   -663       N  
ATOM   3517  N   LYS A 460      37.736  30.715  -9.616  1.00105.89           N  
ANISOU 3517  N   LYS A 460    13089  11742  15404   -170   -829   -778       N  
ATOM   3518  CA  LYS A 460      37.078  29.414  -9.703  1.00104.10           C  
ANISOU 3518  CA  LYS A 460    12772  11433  15347   -109   -894   -768       C  
ATOM   3519  C   LYS A 460      36.132  29.200  -8.528  1.00101.92           C  
ANISOU 3519  C   LYS A 460    12518  11016  15191     81   -942   -508       C  
ATOM   3520  O   LYS A 460      34.942  28.914  -8.717  1.00101.91           O  
ANISOU 3520  O   LYS A 460    12521  10962  15239     92   -988   -321       O  
ATOM   3521  CB  LYS A 460      38.124  28.299  -9.761  1.00103.03           C  
ANISOU 3521  CB  LYS A 460    12489  11292  15365    -85   -902  -1057       C  
ATOM   3522  CG  LYS A 460      38.976  28.301 -11.018  1.00104.60           C  
ANISOU 3522  CG  LYS A 460    12635  11647  15460   -285   -825  -1357       C  
ATOM   3523  CD  LYS A 460      39.986  27.164 -10.996  1.00103.11           C  
ANISOU 3523  CD  LYS A 460    12266  11418  15492   -228   -819  -1660       C  
ATOM   3524  CE  LYS A 460      40.764  27.088 -12.300  1.00103.89           C  
ANISOU 3524  CE  LYS A 460    12295  11689  15488   -437   -704  -1997       C  
ATOM   3525  NZ  LYS A 460      41.646  28.270 -12.497  1.00105.68           N  
ANISOU 3525  NZ  LYS A 460    12569  12085  15498   -559   -610  -2053       N  
ATOM   3526  N   LEU A 461      36.646  29.338  -7.301  1.00 87.72           N  
ANISOU 3526  N   LEU A 461    10731   9168  13430    212   -934   -485       N  
ATOM   3527  CA  LEU A 461      35.793  29.187  -6.125  1.00 87.27           C  
ANISOU 3527  CA  LEU A 461    10700   9014  13445    361   -959   -249       C  
ATOM   3528  C   LEU A 461      34.614  30.150  -6.168  1.00 86.93           C  
ANISOU 3528  C   LEU A 461    10756   8959  13317    366   -899    -24       C  
ATOM   3529  O   LEU A 461      33.511  29.813  -5.722  1.00 86.91           O  
ANISOU 3529  O   LEU A 461    10734   8890  13396    451   -917    179       O  
ATOM   3530  CB  LEU A 461      36.603  29.404  -4.848  1.00 87.14           C  
ANISOU 3530  CB  LEU A 461    10715   8977  13418    442   -952   -264       C  
ATOM   3531  CG  LEU A 461      37.673  28.373  -4.505  1.00 87.71           C  
ANISOU 3531  CG  LEU A 461    10661   9015  13650    462  -1047   -419       C  
ATOM   3532  CD1 LEU A 461      38.452  28.802  -3.276  1.00 87.70           C  
ANISOU 3532  CD1 LEU A 461    10718   9003  13601    498  -1053   -391       C  
ATOM   3533  CD2 LEU A 461      37.027  27.029  -4.280  1.00 88.10           C  
ANISOU 3533  CD2 LEU A 461    10596   8971  13907    527  -1169   -328       C  
ATOM   3534  N   LYS A 462      34.826  31.353  -6.708  1.00 99.82           N  
ANISOU 3534  N   LYS A 462    12475  10646  14807    272   -838    -48       N  
ATOM   3535  CA  LYS A 462      33.750  32.337  -6.773  1.00100.91           C  
ANISOU 3535  CA  LYS A 462    12682  10737  14920    279   -797    163       C  
ATOM   3536  C   LYS A 462      32.672  31.914  -7.762  1.00100.91           C  
ANISOU 3536  C   LYS A 462    12626  10723  14991    199   -865    301       C  
ATOM   3537  O   LYS A 462      31.476  32.009  -7.462  1.00 99.52           O  
ANISOU 3537  O   LYS A 462    12436  10465  14912    278   -860    529       O  
ATOM   3538  CB  LYS A 462      34.313  33.708  -7.146  1.00103.41           C  
ANISOU 3538  CB  LYS A 462    13096  11097  15099    178   -757    112       C  
ATOM   3539  N   GLN A 463      33.072  31.446  -8.946  1.00105.72           N  
ANISOU 3539  N   GLN A 463    13201  11417  15553     29   -923    163       N  
ATOM   3540  CA  GLN A 463      32.099  30.973  -9.921  1.00106.07           C  
ANISOU 3540  CA  GLN A 463    13207  11454  15641    -85  -1006    287       C  
ATOM   3541  C   GLN A 463      31.482  29.639  -9.513  1.00103.24           C  
ANISOU 3541  C   GLN A 463    12763  11019  15445     29  -1068    352       C  
ATOM   3542  O   GLN A 463      30.500  29.209 -10.129  1.00103.45           O  
ANISOU 3542  O   GLN A 463    12760  11014  15532    -39  -1149    506       O  
ATOM   3543  CB  GLN A 463      32.758  30.870 -11.303  1.00108.83           C  
ANISOU 3543  CB  GLN A 463    13561  11939  15850   -337  -1035     89       C  
ATOM   3544  CG  GLN A 463      31.791  30.649 -12.464  1.00111.03           C  
ANISOU 3544  CG  GLN A 463    13840  12234  16113   -532  -1133    232       C  
ATOM   3545  CD  GLN A 463      32.484  30.639 -13.815  1.00114.32           C  
ANISOU 3545  CD  GLN A 463    14279  12820  16336   -827  -1143     20       C  
ATOM   3546  OE1 GLN A 463      33.709  30.735 -13.899  1.00114.87           O  
ANISOU 3546  OE1 GLN A 463    14344  13000  16302   -870  -1062   -251       O  
ATOM   3547  NE2 GLN A 463      31.699  30.532 -14.883  1.00115.52           N  
ANISOU 3547  NE2 GLN A 463    14455  13007  16431  -1053  -1240    148       N  
ATOM   3548  N   ALA A 464      32.017  28.989  -8.479  1.00 95.52           N  
ANISOU 3548  N   ALA A 464    11742  10005  14545    183  -1056    264       N  
ATOM   3549  CA  ALA A 464      31.421  27.762  -7.969  1.00 94.13           C  
ANISOU 3549  CA  ALA A 464    11479   9748  14536    287  -1142    362       C  
ATOM   3550  C   ALA A 464      30.440  28.002  -6.830  1.00 93.16           C  
ANISOU 3550  C   ALA A 464    11360   9561  14475    439  -1108    634       C  
ATOM   3551  O   ALA A 464      29.457  27.262  -6.710  1.00 92.37           O  
ANISOU 3551  O   ALA A 464    11195   9408  14495    478  -1182    821       O  
ATOM   3552  CB  ALA A 464      32.514  26.799  -7.498  1.00 93.43           C  
ANISOU 3552  CB  ALA A 464    11317   9646  14537    343  -1187    142       C  
ATOM   3553  N   CYS A 465      30.678  29.007  -5.985  1.00 88.47           N  
ANISOU 3553  N   CYS A 465    10839   8977  13799    515   -992    652       N  
ATOM   3554  CA  CYS A 465      29.817  29.254  -4.832  1.00 88.58           C  
ANISOU 3554  CA  CYS A 465    10856   8951  13852    649   -920    861       C  
ATOM   3555  C   CYS A 465      29.088  30.587  -4.918  1.00 88.82           C  
ANISOU 3555  C   CYS A 465    10940   8951  13856    664   -805    989       C  
ATOM   3556  O   CYS A 465      27.854  30.606  -4.870  1.00 89.29           O  
ANISOU 3556  O   CYS A 465    10942   8960  14025    712   -789   1212       O  
ATOM   3557  CB  CYS A 465      30.639  29.178  -3.540  1.00 88.51           C  
ANISOU 3557  CB  CYS A 465    10881   8962  13786    726   -880    773       C  
ATOM   3558  SG  CYS A 465      31.293  27.544  -3.179  1.00 88.68           S  
ANISOU 3558  SG  CYS A 465    10797   8969  13928    728  -1051    700       S  
ATOM   3559  N   GLY A 466      29.800  31.697  -5.044  1.00102.53           N  
ANISOU 3559  N   GLY A 466    12770  10704  15481    626   -735    862       N  
ATOM   3560  CA  GLY A 466      29.173  33.001  -5.098  1.00104.66           C  
ANISOU 3560  CA  GLY A 466    13083  10913  15770    644   -645    972       C  
ATOM   3561  C   GLY A 466      30.042  34.054  -4.436  1.00106.07           C  
ANISOU 3561  C   GLY A 466    13380  11096  15827    675   -542    824       C  
ATOM   3562  O   GLY A 466      31.203  33.818  -4.112  1.00106.38           O  
ANISOU 3562  O   GLY A 466    13470  11200  15751    652   -556    643       O  
ATOM   3563  N   TYR A 467      29.442  35.233  -4.238  1.00113.65           N  
ANISOU 3563  N   TYR A 467    14373  11967  16842    726   -448    909       N  
ATOM   3564  CA  TYR A 467      30.192  36.366  -3.699  1.00115.55           C  
ANISOU 3564  CA  TYR A 467    14739  12186  16979    742   -362    772       C  
ATOM   3565  C   TYR A 467      30.479  36.206  -2.211  1.00115.08           C  
ANISOU 3565  C   TYR A 467    14745  12149  16830    855   -241    690       C  
ATOM   3566  O   TYR A 467      31.577  36.543  -1.753  1.00116.57           O  
ANISOU 3566  O   TYR A 467    15044  12377  16870    823   -231    529       O  
ATOM   3567  CB  TYR A 467      29.442  37.674  -3.957  1.00118.37           C  
ANISOU 3567  CB  TYR A 467    15101  12408  17466    763   -313    878       C  
ATOM   3568  CG  TYR A 467      29.565  38.205  -5.371  1.00121.70           C  
ANISOU 3568  CG  TYR A 467    15510  12819  17912    587   -461    934       C  
ATOM   3569  CD1 TYR A 467      30.538  37.719  -6.236  1.00122.82           C  
ANISOU 3569  CD1 TYR A 467    15673  13096  17899    416   -579    822       C  
ATOM   3570  CD2 TYR A 467      28.723  39.211  -5.832  1.00123.15           C  
ANISOU 3570  CD2 TYR A 467    15652  12859  18282    574   -484   1099       C  
ATOM   3571  CE1 TYR A 467      30.659  38.210  -7.527  1.00124.38           C  
ANISOU 3571  CE1 TYR A 467    15866  13319  18075    211   -709    873       C  
ATOM   3572  CE2 TYR A 467      28.836  39.708  -7.121  1.00124.33           C  
ANISOU 3572  CE2 TYR A 467    15793  13008  18440    369   -650   1183       C  
ATOM   3573  CZ  TYR A 467      29.805  39.204  -7.963  1.00125.08           C  
ANISOU 3573  CZ  TYR A 467    15927  13272  18327    174   -758   1070       C  
ATOM   3574  OH  TYR A 467      29.921  39.695  -9.244  1.00126.53           O  
ANISOU 3574  OH  TYR A 467    16108  13491  18476    -72   -919   1155       O  
ATOM   3575  N   GLU A 468      29.507  35.715  -1.436  1.00 99.44           N  
ANISOU 3575  N   GLU A 468    12699  10156  14927    962   -154    811       N  
ATOM   3576  CA  GLU A 468      29.711  35.604   0.007  1.00101.19           C  
ANISOU 3576  CA  GLU A 468    12992  10423  15032   1026    -35    747       C  
ATOM   3577  C   GLU A 468      30.857  34.664   0.347  1.00100.79           C  
ANISOU 3577  C   GLU A 468    12972  10473  14852    955   -153    650       C  
ATOM   3578  O   GLU A 468      31.548  34.862   1.354  1.00102.89           O  
ANISOU 3578  O   GLU A 468    13347  10777  14969    941   -104    553       O  
ATOM   3579  CB  GLU A 468      28.439  35.118   0.700  1.00101.62           C  
ANISOU 3579  CB  GLU A 468    12948  10481  15182   1121     72    910       C  
ATOM   3580  CG  GLU A 468      28.599  35.013   2.214  1.00104.80           C  
ANISOU 3580  CG  GLU A 468    13433  10964  15425   1143    202    852       C  
ATOM   3581  CD  GLU A 468      27.363  34.494   2.914  1.00106.32           C  
ANISOU 3581  CD  GLU A 468    13515  11197  15684   1210    318   1013       C  
ATOM   3582  OE1 GLU A 468      26.369  34.183   2.223  1.00104.09           O  
ANISOU 3582  OE1 GLU A 468    13086  10868  15598   1255    286   1183       O  
ATOM   3583  OE2 GLU A 468      27.390  34.394   4.160  1.00109.95           O  
ANISOU 3583  OE2 GLU A 468    14039  11749  15990   1195    436    979       O  
ATOM   3584  N   PHE A 469      31.077  33.644  -0.477  1.00 93.43           N  
ANISOU 3584  N   PHE A 469    11940   9571  13989    900   -314    671       N  
ATOM   3585  CA  PHE A 469      32.020  32.594  -0.120  1.00 92.79           C  
ANISOU 3585  CA  PHE A 469    11837   9551  13866    853   -437    598       C  
ATOM   3586  C   PHE A 469      33.468  33.026  -0.324  1.00 93.08           C  
ANISOU 3586  C   PHE A 469    11954   9613  13800    774   -484    401       C  
ATOM   3587  O   PHE A 469      34.353  32.582   0.415  1.00 93.53           O  
ANISOU 3587  O   PHE A 469    12032   9703  13802    745   -544    338       O  
ATOM   3588  CB  PHE A 469      31.710  31.337  -0.937  1.00 90.95           C  
ANISOU 3588  CB  PHE A 469    11458   9316  13781    831   -585    663       C  
ATOM   3589  CG  PHE A 469      32.486  30.127  -0.514  1.00 90.28           C  
ANISOU 3589  CG  PHE A 469    11311   9255  13737    803   -729    615       C  
ATOM   3590  CD1 PHE A 469      32.135  29.435   0.629  1.00 90.77           C  
ANISOU 3590  CD1 PHE A 469    11345   9334  13809    830   -758    748       C  
ATOM   3591  CD2 PHE A 469      33.560  29.679  -1.262  1.00 89.46           C  
ANISOU 3591  CD2 PHE A 469    11160   9154  13678    738   -841    441       C  
ATOM   3592  CE1 PHE A 469      32.844  28.323   1.020  1.00 90.26           C  
ANISOU 3592  CE1 PHE A 469    11207   9265  13823    790   -930    734       C  
ATOM   3593  CE2 PHE A 469      34.274  28.569  -0.874  1.00 88.94           C  
ANISOU 3593  CE2 PHE A 469    11006   9073  13713    723   -985    396       C  
ATOM   3594  CZ  PHE A 469      33.915  27.890   0.268  1.00 89.23           C  
ANISOU 3594  CZ  PHE A 469    11016   9103  13785    749  -1048    555       C  
ATOM   3595  N   THR A 470      33.728  33.900  -1.296  1.00 93.44           N  
ANISOU 3595  N   THR A 470    12035   9645  13821    723   -471    325       N  
ATOM   3596  CA  THR A 470      35.086  34.261  -1.683  1.00 94.66           C  
ANISOU 3596  CA  THR A 470    12239   9844  13885    630   -523    148       C  
ATOM   3597  C   THR A 470      35.364  35.752  -1.501  1.00 97.12           C  
ANISOU 3597  C   THR A 470    12696  10125  14079    612   -437    101       C  
ATOM   3598  O   THR A 470      36.151  36.334  -2.249  1.00 98.77           O  
ANISOU 3598  O   THR A 470    12933  10366  14228    514   -479      1       O  
ATOM   3599  CB  THR A 470      35.350  33.848  -3.129  1.00 94.07           C  
ANISOU 3599  CB  THR A 470    12066   9812  13865    532   -611     77       C  
ATOM   3600  OG1 THR A 470      34.424  34.518  -3.993  1.00 94.32           O  
ANISOU 3600  OG1 THR A 470    12102   9813  13924    500   -585    183       O  
ATOM   3601  CG2 THR A 470      35.178  32.352  -3.291  1.00 91.99           C  
ANISOU 3601  CG2 THR A 470    11663   9554  13734    550   -705     88       C  
ATOM   3602  N   SER A 471      34.731  36.387  -0.513  1.00 95.89           N  
ANISOU 3602  N   SER A 471    12630   9910  13891    695   -316    161       N  
ATOM   3603  CA  SER A 471      34.940  37.816  -0.297  1.00 97.48           C  
ANISOU 3603  CA  SER A 471    12974  10051  14012    688   -237    101       C  
ATOM   3604  C   SER A 471      36.215  38.071   0.498  1.00 98.52           C  
ANISOU 3604  C   SER A 471    13232  10223  13978    628   -259    -28       C  
ATOM   3605  O   SER A 471      37.125  38.778   0.036  1.00 98.74           O  
ANISOU 3605  O   SER A 471    13321  10259  13935    542   -314   -118       O  
ATOM   3606  CB  SER A 471      33.733  38.420   0.423  1.00 98.74           C  
ANISOU 3606  CB  SER A 471    13169  10117  14229    804    -74    179       C  
ATOM   3607  OG  SER A 471      33.639  37.925   1.747  1.00 99.87           O  
ANISOU 3607  OG  SER A 471    13358  10305  14283    846      9    177       O  
ATOM   3608  N   LYS A 472      36.286  37.507   1.708  1.00 98.86           N  
ANISOU 3608  N   LYS A 472    13314  10297  13951    651   -230    -16       N  
ATOM   3609  CA  LYS A 472      37.492  37.623   2.518  1.00 99.94           C  
ANISOU 3609  CA  LYS A 472    13565  10472  13935    568   -282   -104       C  
ATOM   3610  C   LYS A 472      38.715  37.129   1.764  1.00 98.68           C  
ANISOU 3610  C   LYS A 472    13318  10368  13809    480   -442   -175       C  
ATOM   3611  O   LYS A 472      39.811  37.671   1.935  1.00 99.43           O  
ANISOU 3611  O   LYS A 472    13499  10477  13802    397   -492   -259       O  
ATOM   3612  CB  LYS A 472      37.326  36.855   3.829  1.00101.01           C  
ANISOU 3612  CB  LYS A 472    13725  10651  14002    563   -270    -37       C  
ATOM   3613  CG  LYS A 472      36.337  37.489   4.790  1.00103.37           C  
ANISOU 3613  CG  LYS A 472    14140  10925  14211    617    -75    -18       C  
ATOM   3614  CD  LYS A 472      36.296  36.748   6.116  1.00104.88           C  
ANISOU 3614  CD  LYS A 472    14372  11200  14279    553    -74     50       C  
ATOM   3615  CE  LYS A 472      35.331  37.413   7.086  1.00107.58           C  
ANISOU 3615  CE  LYS A 472    14830  11545  14501    586    161     31       C  
ATOM   3616  NZ  LYS A 472      35.292  36.713   8.401  1.00109.50           N  
ANISOU 3616  NZ  LYS A 472    15125  11906  14575    474    163    105       N  
ATOM   3617  N   LEU A 473      38.547  36.109   0.923  1.00 97.99           N  
ANISOU 3617  N   LEU A 473    13053  10311  13868    493   -515   -154       N  
ATOM   3618  CA  LEU A 473      39.636  35.691   0.050  1.00 97.43           C  
ANISOU 3618  CA  LEU A 473    12875  10294  13849    413   -627   -264       C  
ATOM   3619  C   LEU A 473      39.972  36.775  -0.965  1.00 98.14           C  
ANISOU 3619  C   LEU A 473    13009  10407  13871    338   -605   -339       C  
ATOM   3620  O   LEU A 473      41.148  37.009  -1.264  1.00 99.01           O  
ANISOU 3620  O   LEU A 473    13114  10573  13933    244   -662   -445       O  
ATOM   3621  CB  LEU A 473      39.271  34.387  -0.662  1.00 95.06           C  
ANISOU 3621  CB  LEU A 473    12384  10010  13725    439   -691   -253       C  
ATOM   3622  CG  LEU A 473      39.425  33.051   0.071  1.00 93.29           C  
ANISOU 3622  CG  LEU A 473    12054   9768  13625    470   -795   -207       C  
ATOM   3623  CD1 LEU A 473      38.385  32.871   1.166  1.00 93.10           C  
ANISOU 3623  CD1 LEU A 473    12090   9714  13568    535   -750    -37       C  
ATOM   3624  CD2 LEU A 473      39.327  31.929  -0.936  1.00 91.34           C  
ANISOU 3624  CD2 LEU A 473    11617   9522  13566    477   -869   -261       C  
ATOM   3625  N   HIS A 474      38.953  37.455  -1.497  1.00103.87           N  
ANISOU 3625  N   HIS A 474    13768  11089  14609    364   -537   -266       N  
ATOM   3626  CA  HIS A 474      39.187  38.412  -2.574  1.00104.32           C  
ANISOU 3626  CA  HIS A 474    13848  11169  14620    260   -556   -299       C  
ATOM   3627  C   HIS A 474      39.949  39.632  -2.077  1.00105.55           C  
ANISOU 3627  C   HIS A 474    14163  11297  14646    210   -554   -348       C  
ATOM   3628  O   HIS A 474      41.036  39.942  -2.577  1.00105.90           O  
ANISOU 3628  O   HIS A 474    14203  11419  14614     88   -621   -434       O  
ATOM   3629  CB  HIS A 474      37.869  38.841  -3.216  1.00104.17           C  
ANISOU 3629  CB  HIS A 474    13812  11081  14687    286   -520   -170       C  
ATOM   3630  CG  HIS A 474      38.050  39.800  -4.350  1.00104.91           C  
ANISOU 3630  CG  HIS A 474    13922  11198  14743    142   -578   -162       C  
ATOM   3631  ND1 HIS A 474      38.530  39.411  -5.582  1.00104.92           N  
ANISOU 3631  ND1 HIS A 474    13827  11330  14710    -15   -652   -218       N  
ATOM   3632  CD2 HIS A 474      37.839  41.135  -4.432  1.00105.90           C  
ANISOU 3632  CD2 HIS A 474    14145  11233  14861    111   -583   -104       C  
ATOM   3633  CE1 HIS A 474      38.595  40.462  -6.379  1.00105.97           C  
ANISOU 3633  CE1 HIS A 474    14001  11473  14789   -159   -708   -171       C  
ATOM   3634  NE2 HIS A 474      38.181  41.521  -5.705  1.00106.47           N  
ANISOU 3634  NE2 HIS A 474    14178  11389  14888    -79   -683    -92       N  
ATOM   3635  N   ARG A 475      39.391  40.357  -1.106  1.00119.59           N  
ANISOU 3635  N   ARG A 475    16079  12965  16396    295   -471   -304       N  
ATOM   3636  CA  ARG A 475      40.131  41.513  -0.607  1.00121.51           C  
ANISOU 3636  CA  ARG A 475    16489  13165  16514    239   -480   -363       C  
ATOM   3637  C   ARG A 475      41.324  41.097   0.242  1.00121.87           C  
ANISOU 3637  C   ARG A 475    16584  13273  16449    190   -533   -436       C  
ATOM   3638  O   ARG A 475      42.261  41.887   0.409  1.00123.40           O  
ANISOU 3638  O   ARG A 475    16886  13467  16532     99   -586   -489       O  
ATOM   3639  CB  ARG A 475      39.204  42.456   0.160  1.00122.14           C  
ANISOU 3639  CB  ARG A 475    16705  13096  16608    338   -361   -335       C  
ATOM   3640  CG  ARG A 475      38.175  43.135  -0.741  1.00121.79           C  
ANISOU 3640  CG  ARG A 475    16605  12954  16717    366   -346   -247       C  
ATOM   3641  CD  ARG A 475      38.834  44.146  -1.690  1.00120.86           C  
ANISOU 3641  CD  ARG A 475    16518  12831  16572    221   -471   -250       C  
ATOM   3642  NE  ARG A 475      37.865  44.797  -2.571  1.00120.02           N  
ANISOU 3642  NE  ARG A 475    16349  12619  16634    215   -500   -130       N  
ATOM   3643  CZ  ARG A 475      38.176  45.669  -3.527  1.00119.60           C  
ANISOU 3643  CZ  ARG A 475    16299  12555  16590     66   -633    -78       C  
ATOM   3644  NH1 ARG A 475      39.438  46.012  -3.736  1.00119.35           N  
ANISOU 3644  NH1 ARG A 475    16329  12623  16395    -82   -730   -150       N  
ATOM   3645  NH2 ARG A 475      37.220  46.203  -4.277  1.00119.47           N  
ANISOU 3645  NH2 ARG A 475    16212  12426  16755     47   -686     67       N  
ATOM   3646  N   MET A 476      41.316  39.867   0.758  1.00104.71           N  
ANISOU 3646  N   MET A 476    14322  11143  14321    233   -544   -417       N  
ATOM   3647  CA  MET A 476      42.527  39.277   1.315  1.00105.27           C  
ANISOU 3647  CA  MET A 476    14373  11270  14353    161   -645   -459       C  
ATOM   3648  C   MET A 476      43.617  39.172   0.255  1.00104.48           C  
ANISOU 3648  C   MET A 476    14148  11259  14292     62   -737   -544       C  
ATOM   3649  O   MET A 476      44.809  39.234   0.574  1.00105.11           O  
ANISOU 3649  O   MET A 476    14238  11371  14327    -23   -821   -588       O  
ATOM   3650  CB  MET A 476      42.183  37.908   1.901  1.00104.61           C  
ANISOU 3650  CB  MET A 476    14180  11199  14369    220   -671   -396       C  
ATOM   3651  CG  MET A 476      43.273  37.195   2.658  1.00105.13           C  
ANISOU 3651  CG  MET A 476    14210  11289  14446    147   -802   -393       C  
ATOM   3652  SD  MET A 476      42.573  35.719   3.419  1.00104.30           S  
ANISOU 3652  SD  MET A 476    13994  11173  14463    205   -849   -270       S  
ATOM   3653  CE  MET A 476      44.018  34.979   4.165  1.00104.79           C  
ANISOU 3653  CE  MET A 476    13986  11236  14592     89  -1057   -246       C  
ATOM   3654  N   TYR A 477      43.221  39.023  -1.010  1.00 99.85           N  
ANISOU 3654  N   TYR A 477    13439  10719  13779     53   -720   -567       N  
ATOM   3655  CA  TYR A 477      44.149  39.075  -2.133  1.00 99.82           C  
ANISOU 3655  CA  TYR A 477    13326  10829  13773    -71   -771   -667       C  
ATOM   3656  C   TYR A 477      44.426  40.502  -2.587  1.00100.12           C  
ANISOU 3656  C   TYR A 477    13486  10878  13675   -180   -783   -661       C  
ATOM   3657  O   TYR A 477      45.486  40.768  -3.165  1.00100.40           O  
ANISOU 3657  O   TYR A 477    13471  11019  13655   -312   -835   -735       O  
ATOM   3658  CB  TYR A 477      43.586  38.250  -3.290  1.00 99.50           C  
ANISOU 3658  CB  TYR A 477    13115  10852  13840    -74   -749   -701       C  
ATOM   3659  CG  TYR A 477      44.294  38.423  -4.611  1.00 99.79           C  
ANISOU 3659  CG  TYR A 477    13051  11033  13833   -234   -764   -814       C  
ATOM   3660  CD1 TYR A 477      45.534  37.853  -4.844  1.00100.27           C  
ANISOU 3660  CD1 TYR A 477    12970  11191  13935   -301   -789   -964       C  
ATOM   3661  CD2 TYR A 477      43.703  39.149  -5.637  1.00 99.88           C  
ANISOU 3661  CD2 TYR A 477    13094  11087  13767   -337   -754   -764       C  
ATOM   3662  CE1 TYR A 477      46.169  38.008  -6.061  1.00100.85           C  
ANISOU 3662  CE1 TYR A 477    12943  11427  13947   -466   -772  -1087       C  
ATOM   3663  CE2 TYR A 477      44.330  39.311  -6.851  1.00100.42           C  
ANISOU 3663  CE2 TYR A 477    13079  11320  13755   -528   -767   -859       C  
ATOM   3664  CZ  TYR A 477      45.564  38.740  -7.059  1.00100.92           C  
ANISOU 3664  CZ  TYR A 477    13007  11505  13833   -592   -759  -1034       C  
ATOM   3665  OH  TYR A 477      46.193  38.899  -8.272  1.00101.76           O  
ANISOU 3665  OH  TYR A 477    13021  11806  13839   -800   -742  -1150       O  
ATOM   3666  N   THR A 478      43.499  41.427  -2.335  1.00110.31           N  
ANISOU 3666  N   THR A 478    14922  12058  14934   -131   -740   -572       N  
ATOM   3667  CA  THR A 478      43.683  42.810  -2.762  1.00110.18           C  
ANISOU 3667  CA  THR A 478    15017  12016  14831   -234   -781   -547       C  
ATOM   3668  C   THR A 478      44.642  43.567  -1.853  1.00110.66           C  
ANISOU 3668  C   THR A 478    15236  12038  14772   -278   -828   -578       C  
ATOM   3669  O   THR A 478      45.374  44.445  -2.327  1.00110.36           O  
ANISOU 3669  O   THR A 478    15241  12039  14652   -415   -909   -584       O  
ATOM   3670  CB  THR A 478      42.329  43.523  -2.819  1.00110.15           C  
ANISOU 3670  CB  THR A 478    15084  11868  14900   -156   -730   -444       C  
ATOM   3671  OG1 THR A 478      41.480  42.855  -3.761  1.00109.75           O  
ANISOU 3671  OG1 THR A 478    14886  11860  14954   -150   -716   -388       O  
ATOM   3672  CG2 THR A 478      42.495  44.974  -3.243  1.00110.08           C  
ANISOU 3672  CG2 THR A 478    15180  11796  14849   -265   -806   -402       C  
ATOM   3673  N   ASP A 479      44.677  43.231  -0.559  1.00110.59           N  
ANISOU 3673  N   ASP A 479    15316  11963  14739   -191   -792   -586       N  
ATOM   3674  CA  ASP A 479      45.575  43.918   0.363  1.00111.05           C  
ANISOU 3674  CA  ASP A 479    15545  11982  14666   -257   -848   -607       C  
ATOM   3675  C   ASP A 479      47.044  43.807  -0.032  1.00110.80           C  
ANISOU 3675  C   ASP A 479    15430  12074  14594   -401   -967   -645       C  
ATOM   3676  O   ASP A 479      47.873  44.524   0.537  1.00111.44           O  
ANISOU 3676  O   ASP A 479    15649  12129  14564   -489  -1043   -643       O  
ATOM   3677  CB  ASP A 479      45.389  43.392   1.789  1.00112.82           C  
ANISOU 3677  CB  ASP A 479    15866  12151  14850   -186   -803   -598       C  
ATOM   3678  CG  ASP A 479      44.089  43.856   2.419  1.00113.67           C  
ANISOU 3678  CG  ASP A 479    16106  12134  14952    -69   -662   -585       C  
ATOM   3679  OD1 ASP A 479      43.576  44.922   2.015  1.00113.27           O  
ANISOU 3679  OD1 ASP A 479    16129  11987  14922    -51   -627   -592       O  
ATOM   3680  OD2 ASP A 479      43.591  43.168   3.333  1.00115.09           O  
ANISOU 3680  OD2 ASP A 479    16304  12308  15118     -5   -592   -566       O  
ATOM   3681  N   MET A 480      47.390  42.942  -0.986  1.00102.20           N  
ANISOU 3681  N   MET A 480    14115  11118  13597   -434   -979   -689       N  
ATOM   3682  CA  MET A 480      48.762  42.920  -1.476  1.00101.96           C  
ANISOU 3682  CA  MET A 480    13976  11218  13548   -574  -1063   -745       C  
ATOM   3683  C   MET A 480      49.007  44.039  -2.482  1.00101.78           C  
ANISOU 3683  C   MET A 480    13983  11264  13424   -721  -1103   -735       C  
ATOM   3684  O   MET A 480      50.076  44.661  -2.475  1.00101.92           O  
ANISOU 3684  O   MET A 480    14034  11336  13356   -852  -1191   -734       O  
ATOM   3685  CB  MET A 480      49.077  41.558  -2.089  1.00101.42           C  
ANISOU 3685  CB  MET A 480    13641  11260  13634   -556  -1040   -834       C  
ATOM   3686  CG  MET A 480      48.979  40.409  -1.095  1.00101.64           C  
ANISOU 3686  CG  MET A 480    13615  11210  13793   -437  -1051   -819       C  
ATOM   3687  SD  MET A 480      50.072  40.600   0.329  1.00102.60           S  
ANISOU 3687  SD  MET A 480    13850  11265  13866   -495  -1178   -751       S  
ATOM   3688  CE  MET A 480      48.910  41.098   1.602  1.00103.68           C  
ANISOU 3688  CE  MET A 480    14272  11258  13864   -412  -1127   -649       C  
ATOM   3689  N   SER A 481      48.026  44.314  -3.344  1.00106.15           N  
ANISOU 3689  N   SER A 481    14523  11818  13993   -721  -1061   -703       N  
ATOM   3690  CA  SER A 481      48.123  45.461  -4.242  1.00105.66           C  
ANISOU 3690  CA  SER A 481    14506  11800  13840   -885  -1133   -650       C  
ATOM   3691  C   SER A 481      47.996  46.771  -3.470  1.00104.70           C  
ANISOU 3691  C   SER A 481    14623  11500  13658   -876  -1198   -573       C  
ATOM   3692  O   SER A 481      48.807  47.692  -3.644  1.00103.65           O  
ANISOU 3692  O   SER A 481    14558  11397  13428  -1027  -1310   -543       O  
ATOM   3693  CB  SER A 481      47.050  45.363  -5.328  1.00105.50           C  
ANISOU 3693  CB  SER A 481    14405  11809  13872   -908  -1099   -604       C  
ATOM   3694  OG  SER A 481      47.077  46.492  -6.184  1.00105.53           O  
ANISOU 3694  OG  SER A 481    14452  11846  13799  -1094  -1202   -515       O  
ATOM   3695  N   VAL A 482      46.977  46.869  -2.611  1.00100.69           N  
ANISOU 3695  N   VAL A 482    14240  10806  13213   -705  -1124   -550       N  
ATOM   3696  CA  VAL A 482      46.826  48.040  -1.752  1.00101.59           C  
ANISOU 3696  CA  VAL A 482    14585  10728  13285   -678  -1154   -526       C  
ATOM   3697  C   VAL A 482      48.071  48.237  -0.898  1.00102.02           C  
ANISOU 3697  C   VAL A 482    14752  10802  13210   -754  -1228   -563       C  
ATOM   3698  O   VAL A 482      48.501  49.371  -0.652  1.00102.95           O  
ANISOU 3698  O   VAL A 482    15032  10832  13250   -841  -1324   -542       O  
ATOM   3699  CB  VAL A 482      45.558  47.907  -0.888  1.00101.71           C  
ANISOU 3699  CB  VAL A 482    14685  10571  13388   -478  -1014   -537       C  
ATOM   3700  CG1 VAL A 482      45.476  49.031   0.130  1.00102.99           C  
ANISOU 3700  CG1 VAL A 482    15092  10539  13501   -449  -1010   -569       C  
ATOM   3701  CG2 VAL A 482      44.323  47.903  -1.770  1.00101.54           C  
ANISOU 3701  CG2 VAL A 482    14554  10505  13522   -420   -971   -467       C  
ATOM   3702  N   SER A 483      48.680  47.140  -0.446  1.00100.34           N  
ANISOU 3702  N   SER A 483    14446  10688  12989   -734  -1207   -604       N  
ATOM   3703  CA  SER A 483      49.899  47.258   0.345  1.00100.91           C  
ANISOU 3703  CA  SER A 483    14602  10778  12960   -828  -1304   -607       C  
ATOM   3704  C   SER A 483      51.084  47.702  -0.503  1.00101.22           C  
ANISOU 3704  C   SER A 483    14552  10956  12950  -1014  -1430   -588       C  
ATOM   3705  O   SER A 483      51.960  48.419  -0.008  1.00102.02           O  
ANISOU 3705  O   SER A 483    14784  11029  12949  -1124  -1545   -555       O  
ATOM   3706  CB  SER A 483      50.215  45.935   1.035  1.00100.57           C  
ANISOU 3706  CB  SER A 483    14455  10785  12973   -769  -1280   -625       C  
ATOM   3707  OG  SER A 483      51.425  46.036   1.759  1.00101.31           O  
ANISOU 3707  OG  SER A 483    14610  10890  12992   -883  -1402   -597       O  
ATOM   3708  N   ALA A 484      51.137  47.289  -1.771  1.00108.19           N  
ANISOU 3708  N   ALA A 484    15215  12002  13889  -1070  -1408   -609       N  
ATOM   3709  CA  ALA A 484      52.213  47.741  -2.649  1.00107.74           C  
ANISOU 3709  CA  ALA A 484    15059  12112  13763  -1272  -1505   -597       C  
ATOM   3710  C   ALA A 484      52.114  49.241  -2.903  1.00106.20           C  
ANISOU 3710  C   ALA A 484    15041  11840  13471  -1391  -1620   -505       C  
ATOM   3711  O   ALA A 484      53.067  49.994  -2.654  1.00105.67           O  
ANISOU 3711  O   ALA A 484    15063  11779  13309  -1524  -1750   -457       O  
ATOM   3712  CB  ALA A 484      52.179  46.965  -3.967  1.00107.85           C  
ANISOU 3712  CB  ALA A 484    14812  12334  13833  -1328  -1429   -666       C  
ATOM   3713  N   ASP A 485      50.957  49.694  -3.397  1.00106.33           N  
ANISOU 3713  N   ASP A 485    15101  11765  13533  -1350  -1595   -463       N  
ATOM   3714  CA  ASP A 485      50.763  51.121  -3.643  1.00105.19           C  
ANISOU 3714  CA  ASP A 485    15108  11503  13355  -1455  -1729   -363       C  
ATOM   3715  C   ASP A 485      50.961  51.933  -2.369  1.00104.74           C  
ANISOU 3715  C   ASP A 485    15309  11229  13257  -1401  -1787   -365       C  
ATOM   3716  O   ASP A 485      51.566  53.013  -2.398  1.00103.92           O  
ANISOU 3716  O   ASP A 485    15322  11080  13084  -1546  -1947   -300       O  
ATOM   3717  CB  ASP A 485      49.371  51.363  -4.227  1.00105.29           C  
ANISOU 3717  CB  ASP A 485    15108  11406  13490  -1388  -1693   -308       C  
ATOM   3718  CG  ASP A 485      49.154  52.802  -4.645  1.00104.19           C  
ANISOU 3718  CG  ASP A 485    15079  11133  13374  -1515  -1865   -183       C  
ATOM   3719  OD1 ASP A 485      49.722  53.218  -5.678  1.00103.03           O  
ANISOU 3719  OD1 ASP A 485    14846  11152  13149  -1755  -2002    -92       O  
ATOM   3720  OD2 ASP A 485      48.405  53.514  -3.944  1.00104.25           O  
ANISOU 3720  OD2 ASP A 485    15250  10870  13491  -1384  -1864   -178       O  
ATOM   3721  N   LEU A 486      50.471  51.420  -1.238  1.00 97.80           N  
ANISOU 3721  N   LEU A 486    14528  10224  12407  -1216  -1663   -441       N  
ATOM   3722  CA  LEU A 486      50.653  52.109   0.034  1.00 98.77           C  
ANISOU 3722  CA  LEU A 486    14912  10161  12455  -1189  -1695   -472       C  
ATOM   3723  C   LEU A 486      52.133  52.231   0.384  1.00 99.21           C  
ANISOU 3723  C   LEU A 486    15008  10312  12375  -1354  -1835   -442       C  
ATOM   3724  O   LEU A 486      52.587  53.285   0.852  1.00100.38           O  
ANISOU 3724  O   LEU A 486    15361  10341  12438  -1448  -1962   -416       O  
ATOM   3725  CB  LEU A 486      49.891  51.369   1.134  1.00 98.51           C  
ANISOU 3725  CB  LEU A 486    14951  10037  12443  -1002  -1522   -556       C  
ATOM   3726  CG  LEU A 486      49.782  52.025   2.511  1.00 99.84           C  
ANISOU 3726  CG  LEU A 486    15408  10011  12516   -970  -1499   -623       C  
ATOM   3727  CD1 LEU A 486      48.980  53.309   2.414  1.00101.09           C  
ANISOU 3727  CD1 LEU A 486    15710   9943  12758   -926  -1499   -651       C  
ATOM   3728  CD2 LEU A 486      49.147  51.078   3.511  1.00 99.65           C  
ANISOU 3728  CD2 LEU A 486    15410   9976  12475   -835  -1328   -690       C  
ATOM   3729  N   ASN A 487      52.906  51.165   0.149  1.00108.87           N  
ANISOU 3729  N   ASN A 487    16027  11739  13601  -1392  -1824   -444       N  
ATOM   3730  CA  ASN A 487      54.348  51.242   0.368  1.00109.48           C  
ANISOU 3730  CA  ASN A 487    16090  11915  13593  -1555  -1964   -396       C  
ATOM   3731  C   ASN A 487      54.987  52.297  -0.525  1.00108.00           C  
ANISOU 3731  C   ASN A 487    15892  11800  13342  -1752  -2120   -313       C  
ATOM   3732  O   ASN A 487      55.894  53.014  -0.088  1.00107.91           O  
ANISOU 3732  O   ASN A 487    16010  11756  13233  -1889  -2275   -248       O  
ATOM   3733  CB  ASN A 487      55.003  49.877   0.143  1.00111.10           C  
ANISOU 3733  CB  ASN A 487    16022  12309  13884  -1545  -1914   -426       C  
ATOM   3734  CG  ASN A 487      54.789  48.924   1.309  1.00112.42           C  
ANISOU 3734  CG  ASN A 487    16226  12395  14095  -1419  -1851   -454       C  
ATOM   3735  OD1 ASN A 487      54.887  49.316   2.472  1.00112.72           O  
ANISOU 3735  OD1 ASN A 487    16499  12297  14032  -1437  -1907   -425       O  
ATOM   3736  ND2 ASN A 487      54.506  47.663   1.000  1.00113.65           N  
ANISOU 3736  ND2 ASN A 487    16153  12636  14393  -1312  -1745   -508       N  
ATOM   3737  N   ASN A 488      54.530  52.415  -1.776  1.00108.58           N  
ANISOU 3737  N   ASN A 488    15819  11977  13460  -1796  -2098   -297       N  
ATOM   3738  CA  ASN A 488      55.032  53.488  -2.634  1.00107.42           C  
ANISOU 3738  CA  ASN A 488    15673  11901  13242  -2014  -2266   -190       C  
ATOM   3739  C   ASN A 488      54.739  54.858  -2.030  1.00106.39           C  
ANISOU 3739  C   ASN A 488    15833  11505  13086  -2031  -2406   -131       C  
ATOM   3740  O   ASN A 488      55.622  55.727  -1.964  1.00105.99           O  
ANISOU 3740  O   ASN A 488    15877  11450  12945  -2205  -2593    -43       O  
ATOM   3741  CB  ASN A 488      54.422  53.382  -4.032  1.00106.75           C  
ANISOU 3741  CB  ASN A 488    15404  11961  13195  -2083  -2228   -167       C  
ATOM   3742  CG  ASN A 488      54.880  52.151  -4.777  1.00107.81           C  
ANISOU 3742  CG  ASN A 488    15249  12378  13334  -2117  -2100   -251       C  
ATOM   3743  OD1 ASN A 488      54.081  51.273  -5.096  1.00108.03           O  
ANISOU 3743  OD1 ASN A 488    15164  12434  13446  -1993  -1949   -329       O  
ATOM   3744  ND2 ASN A 488      56.175  52.081  -5.064  1.00109.13           N  
ANISOU 3744  ND2 ASN A 488    15286  12751  13427  -2288  -2157   -245       N  
ATOM   3745  N   LYS A 489      53.496  55.069  -1.584  1.00100.85           N  
ANISOU 3745  N   LYS A 489    15265  10571  12482  -1850  -2316   -185       N  
ATOM   3746  CA  LYS A 489      53.132  56.358  -1.003  1.00102.23           C  
ANISOU 3746  CA  LYS A 489    15703  10461  12679  -1842  -2422   -172       C  
ATOM   3747  C   LYS A 489      54.000  56.687   0.202  1.00103.06           C  
ANISOU 3747  C   LYS A 489    16030  10477  12650  -1887  -2497   -202       C  
ATOM   3748  O   LYS A 489      54.430  57.836   0.369  1.00104.46           O  
ANISOU 3748  O   LYS A 489    16383  10523  12785  -2012  -2683   -146       O  
ATOM   3749  CB  LYS A 489      51.651  56.375  -0.630  1.00102.26           C  
ANISOU 3749  CB  LYS A 489    15779  10237  12837  -1615  -2264   -260       C  
ATOM   3750  CG  LYS A 489      50.729  56.433  -1.832  1.00102.01           C  
ANISOU 3750  CG  LYS A 489    15573  10223  12963  -1610  -2262   -182       C  
ATOM   3751  CD  LYS A 489      49.276  56.516  -1.411  1.00102.32           C  
ANISOU 3751  CD  LYS A 489    15670  10015  13192  -1381  -2113   -255       C  
ATOM   3752  CE  LYS A 489      48.364  56.569  -2.623  1.00102.23           C  
ANISOU 3752  CE  LYS A 489    15476  10011  13356  -1399  -2143   -141       C  
ATOM   3753  NZ  LYS A 489      46.930  56.633  -2.232  1.00102.70           N  
ANISOU 3753  NZ  LYS A 489    15557   9822  13641  -1169  -1997   -198       N  
ATOM   3754  N   PHE A 490      54.290  55.695   1.047  1.00102.80           N  
ANISOU 3754  N   PHE A 490    15995  10510  12554  -1809  -2381   -273       N  
ATOM   3755  CA  PHE A 490      55.227  55.973   2.129  1.00103.76           C  
ANISOU 3755  CA  PHE A 490    16318  10575  12531  -1907  -2488   -266       C  
ATOM   3756  C   PHE A 490      56.636  56.237   1.612  1.00104.13           C  
ANISOU 3756  C   PHE A 490    16270  10794  12500  -2138  -2693   -130       C  
ATOM   3757  O   PHE A 490      57.379  57.007   2.230  1.00105.39           O  
ANISOU 3757  O   PHE A 490    16631  10861  12551  -2272  -2863    -77       O  
ATOM   3758  CB  PHE A 490      55.267  54.842   3.147  1.00103.24           C  
ANISOU 3758  CB  PHE A 490    16260  10545  12421  -1815  -2358   -331       C  
ATOM   3759  CG  PHE A 490      56.323  55.041   4.182  1.00104.35           C  
ANISOU 3759  CG  PHE A 490    16584  10656  12408  -1962  -2500   -285       C  
ATOM   3760  CD1 PHE A 490      56.184  56.024   5.143  1.00105.97           C  
ANISOU 3760  CD1 PHE A 490    17129  10640  12495  -2004  -2554   -338       C  
ATOM   3761  CD2 PHE A 490      57.479  54.283   4.166  1.00104.05           C  
ANISOU 3761  CD2 PHE A 490    16372  10801  12360  -2073  -2590   -188       C  
ATOM   3762  CE1 PHE A 490      57.164  56.233   6.078  1.00107.17           C  
ANISOU 3762  CE1 PHE A 490    17468  10766  12485  -2173  -2704   -281       C  
ATOM   3763  CE2 PHE A 490      58.461  54.484   5.104  1.00105.24           C  
ANISOU 3763  CE2 PHE A 490    16684  10915  12385  -2231  -2750   -110       C  
ATOM   3764  CZ  PHE A 490      58.306  55.463   6.059  1.00106.76           C  
ANISOU 3764  CZ  PHE A 490    17240  10900  12424  -2293  -2814   -149       C  
ATOM   3765  N   ASN A 491      57.034  55.608   0.503  1.00125.13           N  
ANISOU 3765  N   ASN A 491    18625  13709  15208  -2198  -2676    -80       N  
ATOM   3766  CA  ASN A 491      58.342  55.919  -0.065  1.00125.43           C  
ANISOU 3766  CA  ASN A 491    18548  13933  15178  -2429  -2851     43       C  
ATOM   3767  C   ASN A 491      58.420  57.369  -0.514  1.00124.23           C  
ANISOU 3767  C   ASN A 491    18537  13688  14977  -2591  -3058    151       C  
ATOM   3768  O   ASN A 491      59.502  57.967  -0.489  1.00124.38           O  
ANISOU 3768  O   ASN A 491    18595  13760  14905  -2790  -3254    267       O  
ATOM   3769  CB  ASN A 491      58.676  54.988  -1.233  1.00126.76           C  
ANISOU 3769  CB  ASN A 491    18354  14406  15403  -2471  -2755     35       C  
ATOM   3770  CG  ASN A 491      58.983  53.571  -0.784  1.00129.58           C  
ANISOU 3770  CG  ASN A 491    18537  14856  15841  -2354  -2613    -49       C  
ATOM   3771  OD1 ASN A 491      58.305  52.619  -1.173  1.00130.93           O  
ANISOU 3771  OD1 ASN A 491    18543  15093  16112  -2213  -2435   -148       O  
ATOM   3772  ND2 ASN A 491      60.013  53.427   0.044  1.00130.36           N  
ANISOU 3772  ND2 ASN A 491    18670  14946  15913  -2423  -2716      8       N  
ATOM   3773  N   ASN A 492      57.293  57.955  -0.924  1.00119.50           N  
ANISOU 3773  N   ASN A 492    18006  12937  14462  -2517  -3038    132       N  
ATOM   3774  CA  ASN A 492      57.296  59.379  -1.248  1.00118.37           C  
ANISOU 3774  CA  ASN A 492    18009  12647  14321  -2665  -3267    243       C  
ATOM   3775  C   ASN A 492      57.291  60.236   0.015  1.00118.03           C  
ANISOU 3775  C   ASN A 492    18310  12289  14246  -2626  -3358    193       C  
ATOM   3776  O   ASN A 492      58.086  61.175   0.141  1.00117.66           O  
ANISOU 3776  O   ASN A 492    18398  12182  14124  -2811  -3594    298       O  
ATOM   3777  CB  ASN A 492      56.098  59.724  -2.129  1.00117.95           C  
ANISOU 3777  CB  ASN A 492    17888  12512  14417  -2612  -3245    262       C  
ATOM   3778  CG  ASN A 492      56.199  61.105  -2.740  1.00117.26           C  
ANISOU 3778  CG  ASN A 492    17873  12316  14363  -2814  -3526    425       C  
ATOM   3779  OD1 ASN A 492      57.164  61.831  -2.507  1.00116.98           O  
ANISOU 3779  OD1 ASN A 492    17949  12269  14228  -2990  -3735    518       O  
ATOM   3780  ND2 ASN A 492      55.200  61.474  -3.531  1.00117.15           N  
ANISOU 3780  ND2 ASN A 492    17790  12215  14506  -2804  -3556    483       N  
ATOM   3781  N   PHE A 493      56.400  59.927   0.961  1.00114.94           N  
ANISOU 3781  N   PHE A 493    18068  11703  13902  -2403  -3170     26       N  
ATOM   3782  CA  PHE A 493      56.325  60.686   2.206  1.00115.30           C  
ANISOU 3782  CA  PHE A 493    18454  11461  13895  -2374  -3213    -69       C  
ATOM   3783  C   PHE A 493      57.592  60.571   3.049  1.00115.69           C  
ANISOU 3783  C   PHE A 493    18628  11580  13747  -2526  -3327    -21       C  
ATOM   3784  O   PHE A 493      57.764  61.360   3.985  1.00116.02           O  
ANISOU 3784  O   PHE A 493    18973  11405  13705  -2579  -3423    -72       O  
ATOM   3785  CB  PHE A 493      55.107  60.223   3.015  1.00115.95           C  
ANISOU 3785  CB  PHE A 493    18632  11381  14043  -2121  -2944   -270       C  
ATOM   3786  CG  PHE A 493      54.896  60.983   4.296  1.00116.85           C  
ANISOU 3786  CG  PHE A 493    19099  11208  14092  -2092  -2935   -419       C  
ATOM   3787  CD1 PHE A 493      54.366  62.262   4.280  1.00118.11           C  
ANISOU 3787  CD1 PHE A 493    19425  11068  14384  -2076  -3026   -476       C  
ATOM   3788  CD2 PHE A 493      55.226  60.417   5.516  1.00117.15           C  
ANISOU 3788  CD2 PHE A 493    19299  11269  13942  -2098  -2842   -506       C  
ATOM   3789  CE1 PHE A 493      54.172  62.963   5.458  1.00119.68           C  
ANISOU 3789  CE1 PHE A 493    19951  10999  14525  -2053  -2994   -657       C  
ATOM   3790  CE2 PHE A 493      55.035  61.112   6.696  1.00118.53           C  
ANISOU 3790  CE2 PHE A 493    19816  11203  14018  -2105  -2818   -665       C  
ATOM   3791  CZ  PHE A 493      54.508  62.386   6.667  1.00119.84           C  
ANISOU 3791  CZ  PHE A 493    20149  11073  14311  -2076  -2878   -761       C  
ATOM   3792  N   ILE A 494      58.485  59.628   2.734  1.00121.84           N  
ANISOU 3792  N   ILE A 494    19178  12646  14470  -2606  -3327     72       N  
ATOM   3793  CA  ILE A 494      59.677  59.411   3.553  1.00122.14           C  
ANISOU 3793  CA  ILE A 494    19299  12746  14363  -2750  -3444    143       C  
ATOM   3794  C   ILE A 494      60.565  60.650   3.538  1.00121.78           C  
ANISOU 3794  C   ILE A 494    19417  12622  14230  -2981  -3737    278       C  
ATOM   3795  O   ILE A 494      60.832  61.260   4.581  1.00121.87           O  
ANISOU 3795  O   ILE A 494    19739  12440  14127  -3054  -3846    257       O  
ATOM   3796  CB  ILE A 494      60.443  58.167   3.071  1.00123.45           C  
ANISOU 3796  CB  ILE A 494    19124  13218  14563  -2778  -3389    216       C  
ATOM   3797  N   LYS A 495      61.050  61.030   2.356  1.00135.63           N  
ANISOU 3797  N   LYS A 495    20971  14538  16023  -3123  -3876    424       N  
ATOM   3798  CA  LYS A 495      61.838  62.251   2.195  1.00134.90           C  
ANISOU 3798  CA  LYS A 495    21009  14383  15863  -3358  -4178    582       C  
ATOM   3799  C   LYS A 495      60.938  63.318   1.583  1.00133.29           C  
ANISOU 3799  C   LYS A 495    20889  13983  15773  -3338  -4257    574       C  
ATOM   3800  O   LYS A 495      60.961  63.574   0.381  1.00132.63           O  
ANISOU 3800  O   LYS A 495    20599  14048  15746  -3446  -4344    699       O  
ATOM   3801  CB  LYS A 495      63.069  61.998   1.329  1.00135.75           C  
ANISOU 3801  CB  LYS A 495    20829  14820  15931  -3572  -4301    774       C  
ATOM   3802  CG  LYS A 495      64.082  61.041   1.925  1.00137.62           C  
ANISOU 3802  CG  LYS A 495    20956  15217  16117  -3611  -4271    811       C  
ATOM   3803  CD  LYS A 495      65.314  60.930   1.040  1.00138.57           C  
ANISOU 3803  CD  LYS A 495    20774  15648  16226  -3828  -4389    990       C  
ATOM   3804  CE  LYS A 495      66.306  59.913   1.580  1.00140.03           C  
ANISOU 3804  CE  LYS A 495    20794  15975  16436  -3849  -4356   1030       C  
ATOM   3805  NZ  LYS A 495      67.500  59.785   0.698  1.00140.33           N  
ANISOU 3805  NZ  LYS A 495    20501  16322  16496  -4049  -4437   1180       N  
ATOM   3806  N   ASN A 496      60.125  63.952   2.433  1.00127.20           N  
ANISOU 3806  N   ASN A 496    20417  12868  15046  -3211  -4228    422       N  
ATOM   3807  CA  ASN A 496      59.274  65.028   1.938  1.00126.96           C  
ANISOU 3807  CA  ASN A 496    20462  12592  15187  -3183  -4328    414       C  
ATOM   3808  C   ASN A 496      59.191  66.189   2.929  1.00128.25           C  
ANISOU 3808  C   ASN A 496    21003  12375  15350  -3200  -4469    320       C  
ATOM   3809  O   ASN A 496      58.313  67.049   2.792  1.00130.32           O  
ANISOU 3809  O   ASN A 496    21360  12347  15810  -3117  -4511    248       O  
ATOM   3810  CB  ASN A 496      57.872  64.493   1.607  1.00127.37           C  
ANISOU 3810  CB  ASN A 496    20386  12592  15419  -2929  -4063    273       C  
ATOM   3811  CG  ASN A 496      57.108  65.396   0.649  1.00127.53           C  
ANISOU 3811  CG  ASN A 496    20339  12454  15663  -2946  -4200    354       C  
ATOM   3812  OD1 ASN A 496      57.614  66.431   0.215  1.00126.74           O  
ANISOU 3812  OD1 ASN A 496    20288  12283  15585  -3152  -4501    517       O  
ATOM   3813  ND2 ASN A 496      55.888  64.998   0.307  1.00129.47           N  
ANISOU 3813  ND2 ASN A 496    20461  12641  16089  -2744  -4001    264       N  
ATOM   3814  N   GLN A 497      60.125  66.213   3.880  1.00129.04           N  
ANISOU 3814  N   GLN A 497    21319  12458  15251  -3313  -4550    314       N  
ATOM   3815  CA  GLN A 497      60.220  67.261   4.894  1.00129.55           C  
ANISOU 3815  CA  GLN A 497    21762  12180  15281  -3382  -4714    227       C  
ATOM   3816  C   GLN A 497      61.689  67.649   5.104  1.00129.29           C  
ANISOU 3816  C   GLN A 497    21891  12234  15000  -3615  -4903    346       C  
ATOM   3817  O   GLN A 497      62.488  67.590   4.170  1.00131.21           O  
ANISOU 3817  O   GLN A 497    22454  12227  15172  -3735  -5090    313       O  
ATOM   3818  CB  GLN A 497      59.601  66.794   6.212  1.00129.83           C  
ANISOU 3818  CB  GLN A 497    22027  11940  15361  -3148  -4444    -92       C  
ATOM   3819  CG  GLN A 497      59.795  65.314   6.498  1.00129.63           C  
ANISOU 3819  CG  GLN A 497    22079  12048  15126  -3089  -4205   -216       C  
ATOM   3820  CD  GLN A 497      58.500  64.530   6.412  1.00129.31           C  
ANISOU 3820  CD  GLN A 497    21742  12228  15160  -2887  -3913   -254       C  
ATOM   3821  OE1 GLN A 497      57.892  64.427   5.347  1.00128.69           O  
ANISOU 3821  OE1 GLN A 497    21369  12281  15245  -2833  -3907   -148       O  
ATOM   3822  NE2 GLN A 497      58.072  63.970   7.538  1.00129.55           N  
ANISOU 3822  NE2 GLN A 497    21859  12302  15062  -2797  -3681   -400       N  
ATOM   3823  N   ASP A 498      62.041  68.042   6.327  1.00 30.00           N  
ATOM   3824  CA  ASP A 498      63.417  68.429   6.652  1.00 30.00           C  
ATOM   3825  C   ASP A 498      64.223  67.204   7.079  1.00 30.00           C  
ATOM   3826  O   ASP A 498      63.726  66.367   7.832  1.00 30.00           O  
ATOM   3827  CB  ASP A 498      63.432  69.485   7.758  1.00 20.00           C  
ATOM   3828  CG  ASP A 498      63.555  70.895   7.216  1.00 20.00           C  
ATOM   3829  OD1 ASP A 498      63.933  71.049   6.035  1.00 20.00           O  
ATOM   3830  OD2 ASP A 498      63.273  71.850   7.970  1.00 20.00           O  
ATOM   3831  N   THR A 499      65.462  67.088   6.595  1.00120.63           N  
ANISOU 3831  N   THR A 499    21105  11559  13169  -4434  -5532    925       N  
ATOM   3832  CA  THR A 499      66.303  65.932   6.920  1.00118.75           C  
ANISOU 3832  CA  THR A 499    20419  11680  13022  -4448  -5501   1113       C  
ATOM   3833  C   THR A 499      65.486  64.708   6.537  1.00116.52           C  
ANISOU 3833  C   THR A 499    19872  11523  12878  -4171  -5156    950       C  
ATOM   3834  O   THR A 499      64.513  64.846   5.795  1.00115.89           O  
ANISOU 3834  O   THR A 499    19680  11422  12931  -4051  -5076    883       O  
ATOM   3835  CB  THR A 499      66.648  65.877   8.417  1.00118.94           C  
ANISOU 3835  CB  THR A 499    20372  11872  12948  -4614  -5600   1293       C  
ATOM   3836  OG1 THR A 499      65.449  65.692   9.180  1.00118.79           O  
ANISOU 3836  OG1 THR A 499    20505  11781  12848  -4515  -5414   1140       O  
ATOM   3837  CG2 THR A 499      67.328  67.166   8.854  1.00121.20           C  
ANISOU 3837  CG2 THR A 499    20903  12052  13097  -4914  -5966   1493       C  
ATOM   3838  N   VAL A 500      65.823  63.513   7.012  1.00123.42           N  
ANISOU 3838  N   VAL A 500    20644  12519  13731  -4089  -4979    907       N  
ATOM   3839  CA  VAL A 500      64.934  62.424   6.606  1.00121.36           C  
ANISOU 3839  CA  VAL A 500    20131  12381  13598  -3837  -4662    764       C  
ATOM   3840  C   VAL A 500      64.342  61.740   7.837  1.00121.40           C  
ANISOU 3840  C   VAL A 500    20330  12278  13519  -3725  -4479    600       C  
ATOM   3841  O   VAL A 500      63.183  61.322   7.837  1.00120.44           O  
ANISOU 3841  O   VAL A 500    20190  12109  13462  -3500  -4220    409       O  
ATOM   3842  CB  VAL A 500      65.673  61.397   5.725  1.00119.94           C  
ANISOU 3842  CB  VAL A 500    19498  12537  13535  -3854  -4624    904       C  
ATOM   3843  CG1 VAL A 500      64.749  60.248   5.352  1.00117.97           C  
ANISOU 3843  CG1 VAL A 500    19010  12395  13417  -3600  -4310    747       C  
ATOM   3844  CG2 VAL A 500      66.247  62.066   4.484  1.00120.17           C  
ANISOU 3844  CG2 VAL A 500    19329  12718  13610  -3999  -4785   1060       C  
ATOM   3845  N   SER A 506      65.276  50.857   6.846  1.00145.23           N  
ANISOU 3845  N   SER A 506    20803  16471  17908  -2953  -3584    690       N  
ATOM   3846  CA  SER A 506      65.028  50.494   5.455  1.00143.97           C  
ANISOU 3846  CA  SER A 506    20315  16477  17912  -2805  -3393    553       C  
ATOM   3847  C   SER A 506      64.239  49.189   5.396  1.00142.94           C  
ANISOU 3847  C   SER A 506    19989  16355  17968  -2595  -3206    432       C  
ATOM   3848  O   SER A 506      64.752  48.136   5.772  1.00143.43           O  
ANISOU 3848  O   SER A 506    19830  16416  18252  -2590  -3264    498       O  
ATOM   3849  CB  SER A 506      66.349  50.373   4.700  1.00144.88           C  
ANISOU 3849  CB  SER A 506    20084  16760  18203  -2922  -3483    642       C  
ATOM   3850  OG  SER A 506      67.125  49.297   5.196  1.00145.82           O  
ANISOU 3850  OG  SER A 506    19952  16871  18581  -2940  -3572    740       O  
ATOM   3851  N   PHE A 507      62.999  49.253   4.913  1.00129.76           N  
ANISOU 3851  N   PHE A 507    18386  14681  16234  -2428  -3001    269       N  
ATOM   3852  CA  PHE A 507      62.043  48.190   5.199  1.00130.30           C  
ANISOU 3852  CA  PHE A 507    18395  14705  16407  -2245  -2852    179       C  
ATOM   3853  C   PHE A 507      60.812  48.373   4.321  1.00130.39           C  
ANISOU 3853  C   PHE A 507    18415  14747  16378  -2079  -2633     14       C  
ATOM   3854  O   PHE A 507      60.629  49.412   3.682  1.00130.12           O  
ANISOU 3854  O   PHE A 507    18489  14735  16216  -2119  -2620    -15       O  
ATOM   3855  CB  PHE A 507      61.662  48.222   6.677  1.00130.80           C  
ANISOU 3855  CB  PHE A 507    18780  14604  16312  -2293  -2929    251       C  
ATOM   3856  CG  PHE A 507      60.733  49.343   7.025  1.00130.99           C  
ANISOU 3856  CG  PHE A 507    19190  14517  16064  -2280  -2858    172       C  
ATOM   3857  CD1 PHE A 507      61.159  50.655   6.971  1.00132.26           C  
ANISOU 3857  CD1 PHE A 507    19566  14634  16053  -2417  -2970    206       C  
ATOM   3858  CD2 PHE A 507      59.457  49.082   7.478  1.00129.91           C  
ANISOU 3858  CD2 PHE A 507    19195  14304  15861  -2139  -2689     67       C  
ATOM   3859  CE1 PHE A 507      60.306  51.688   7.295  1.00132.04           C  
ANISOU 3859  CE1 PHE A 507    19875  14469  15827  -2394  -2907    112       C  
ATOM   3860  CE2 PHE A 507      58.615  50.112   7.822  1.00129.72           C  
ANISOU 3860  CE2 PHE A 507    19497  14159  15630  -2117  -2607    -28       C  
ATOM   3861  CZ  PHE A 507      59.036  51.414   7.730  1.00130.51           C  
ANISOU 3861  CZ  PHE A 507    19801  14196  15592  -2238  -2715    -15       C  
ATOM   3862  N   GLN A 508      59.957  47.346   4.314  1.00140.01           N  
ANISOU 3862  N   GLN A 508    19519  15958  17722  -1906  -2485    -73       N  
ATOM   3863  CA  GLN A 508      58.705  47.342   3.566  1.00141.19           C  
ANISOU 3863  CA  GLN A 508    19660  16124  17862  -1744  -2285   -208       C  
ATOM   3864  C   GLN A 508      57.654  46.569   4.356  1.00141.54           C  
ANISOU 3864  C   GLN A 508    19784  16068  17928  -1600  -2187   -238       C  
ATOM   3865  O   GLN A 508      57.978  45.583   5.026  1.00141.79           O  
ANISOU 3865  O   GLN A 508    19712  16080  18081  -1601  -2251   -178       O  
ATOM   3866  CB  GLN A 508      58.891  46.730   2.165  1.00142.62           C  
ANISOU 3866  CB  GLN A 508    19483  16484  18221  -1698  -2182   -303       C  
ATOM   3867  CG  GLN A 508      59.763  47.570   1.228  1.00143.48           C  
ANISOU 3867  CG  GLN A 508    19511  16736  18270  -1858  -2244   -285       C  
ATOM   3868  CD  GLN A 508      59.973  46.928  -0.132  1.00144.51           C  
ANISOU 3868  CD  GLN A 508    19289  17075  18542  -1848  -2118   -405       C  
ATOM   3869  OE1 GLN A 508      59.527  45.806  -0.381  1.00145.66           O  
ANISOU 3869  OE1 GLN A 508    19243  17242  18858  -1711  -1991   -512       O  
ATOM   3870  NE2 GLN A 508      60.658  47.640  -1.022  1.00143.84           N  
ANISOU 3870  NE2 GLN A 508    19123  17153  18379  -2012  -2153   -393       N  
ATOM   3871  N   ILE A 509      56.395  47.012   4.270  1.00119.62           N  
ANISOU 3871  N   ILE A 509    17173  13224  15052  -1487  -2045   -316       N  
ATOM   3872  CA  ILE A 509      55.325  46.518   5.131  1.00119.98           C  
ANISOU 3872  CA  ILE A 509    17344  13175  15068  -1372  -1942   -339       C  
ATOM   3873  C   ILE A 509      54.152  46.015   4.298  1.00120.21           C  
ANISOU 3873  C   ILE A 509    17227  13235  15211  -1188  -1758   -433       C  
ATOM   3874  O   ILE A 509      53.841  46.555   3.232  1.00119.29           O  
ANISOU 3874  O   ILE A 509    17057  13160  15107  -1162  -1698   -485       O  
ATOM   3875  CB  ILE A 509      54.839  47.611   6.116  1.00119.82           C  
ANISOU 3875  CB  ILE A 509    17707  13012  14809  -1419  -1933   -349       C  
ATOM   3876  CG1 ILE A 509      55.927  47.973   7.115  1.00120.36           C  
ANISOU 3876  CG1 ILE A 509    17951  13041  14739  -1624  -2126   -246       C  
ATOM   3877  CG2 ILE A 509      53.595  47.181   6.879  1.00120.97           C  
ANISOU 3877  CG2 ILE A 509    17965  13088  14910  -1299  -1777   -401       C  
ATOM   3878  CD1 ILE A 509      55.512  49.106   7.998  1.00120.17           C  
ANISOU 3878  CD1 ILE A 509    18311  12878  14471  -1688  -2109   -294       C  
ATOM   3879  N   TYR A 510      53.502  44.962   4.801  1.00108.38           N  
ANISOU 3879  N   TYR A 510    15665  11719  13796  -1084  -1690   -431       N  
ATOM   3880  CA  TYR A 510      52.195  44.520   4.333  1.00108.05           C  
ANISOU 3880  CA  TYR A 510    15552  11672  13830   -912  -1519   -497       C  
ATOM   3881  C   TYR A 510      51.116  44.987   5.307  1.00109.36           C  
ANISOU 3881  C   TYR A 510    15985  11722  13846   -856  -1414   -508       C  
ATOM   3882  O   TYR A 510      51.289  44.898   6.526  1.00110.62           O  
ANISOU 3882  O   TYR A 510    16307  11839  13885   -934  -1461   -461       O  
ATOM   3883  CB  TYR A 510      52.149  42.997   4.202  1.00107.97           C  
ANISOU 3883  CB  TYR A 510    15274  11718  14032   -834  -1515   -488       C  
ATOM   3884  CG  TYR A 510      53.037  42.433   3.115  1.00107.13           C  
ANISOU 3884  CG  TYR A 510    14866  11725  14115   -857  -1561   -535       C  
ATOM   3885  CD1 TYR A 510      52.630  42.439   1.789  1.00106.95           C  
ANISOU 3885  CD1 TYR A 510    14696  11788  14152   -802  -1453   -631       C  
ATOM   3886  CD2 TYR A 510      54.278  41.885   3.417  1.00106.53           C  
ANISOU 3886  CD2 TYR A 510    14641  11672  14164   -949  -1707   -486       C  
ATOM   3887  CE1 TYR A 510      53.433  41.921   0.791  1.00106.16           C  
ANISOU 3887  CE1 TYR A 510    14322  11813  14200   -843  -1462   -710       C  
ATOM   3888  CE2 TYR A 510      55.090  41.365   2.425  1.00105.69           C  
ANISOU 3888  CE2 TYR A 510    14233  11669  14254   -963  -1716   -563       C  
ATOM   3889  CZ  TYR A 510      54.661  41.386   1.113  1.00105.78           C  
ANISOU 3889  CZ  TYR A 510    14116  11785  14291   -912  -1578   -692       C  
ATOM   3890  OH  TYR A 510      55.461  40.872   0.118  1.00105.16           O  
ANISOU 3890  OH  TYR A 510    13741  11832  14382   -946  -1555   -804       O  
ATOM   3891  N   VAL A 511      50.000  45.478   4.766  1.00111.23           N  
ANISOU 3891  N   VAL A 511    16255  11911  14095   -737  -1270   -571       N  
ATOM   3892  CA  VAL A 511      48.885  45.976   5.566  1.00112.01           C  
ANISOU 3892  CA  VAL A 511    16570  11895  14095   -661  -1130   -614       C  
ATOM   3893  C   VAL A 511      47.612  45.260   5.130  1.00112.58           C  
ANISOU 3893  C   VAL A 511    16490  11976  14308   -489   -979   -625       C  
ATOM   3894  O   VAL A 511      47.386  45.052   3.933  1.00111.92           O  
ANISOU 3894  O   VAL A 511    16217  11941  14367   -432   -969   -625       O  
ATOM   3895  CB  VAL A 511      48.735  47.506   5.444  1.00110.46           C  
ANISOU 3895  CB  VAL A 511    16579  11576  13814   -685  -1115   -675       C  
ATOM   3896  CG1 VAL A 511      47.515  47.985   6.203  1.00110.92           C  
ANISOU 3896  CG1 VAL A 511    16819  11503  13823   -581   -935   -758       C  
ATOM   3897  CG2 VAL A 511      49.980  48.192   5.972  1.00109.84           C  
ANISOU 3897  CG2 VAL A 511    16670  11482  13581   -868  -1279   -652       C  
ATOM   3898  N   LEU A 512      46.778  44.889   6.106  1.00116.52           N  
ANISOU 3898  N   LEU A 512    17079  12441  14753   -429   -864   -629       N  
ATOM   3899  CA  LEU A 512      45.743  43.881   5.923  1.00116.60           C  
ANISOU 3899  CA  LEU A 512    16922  12486  14894   -294   -758   -599       C  
ATOM   3900  C   LEU A 512      44.423  44.399   6.483  1.00117.30           C  
ANISOU 3900  C   LEU A 512    17146  12484  14938   -189   -557   -653       C  
ATOM   3901  O   LEU A 512      44.402  45.112   7.489  1.00118.32           O  
ANISOU 3901  O   LEU A 512    17509  12552  14895   -247   -494   -718       O  
ATOM   3902  CB  LEU A 512      46.133  42.575   6.636  1.00116.82           C  
ANISOU 3902  CB  LEU A 512    16861  12596  14930   -349   -845   -513       C  
ATOM   3903  CG  LEU A 512      47.389  41.807   6.203  1.00115.95           C  
ANISOU 3903  CG  LEU A 512    16560  12557  14938   -431  -1037   -462       C  
ATOM   3904  CD1 LEU A 512      48.637  42.517   6.671  1.00116.58           C  
ANISOU 3904  CD1 LEU A 512    16784  12627  14884   -599  -1174   -452       C  
ATOM   3905  CD2 LEU A 512      47.400  40.414   6.773  1.00116.46           C  
ANISOU 3905  CD2 LEU A 512    16487  12662  15102   -441  -1116   -366       C  
ATOM   3906  N   GLN A 513      43.313  44.011   5.846  1.00112.71           N  
ANISOU 3906  N   GLN A 513    16410  11895  14519    -42   -448   -632       N  
ATOM   3907  CA  GLN A 513      42.010  44.590   6.176  1.00113.47           C  
ANISOU 3907  CA  GLN A 513    16584  11889  14639     78   -247   -685       C  
ATOM   3908  C   GLN A 513      41.471  44.128   7.536  1.00115.32           C  
ANISOU 3908  C   GLN A 513    16920  12161  14735     70   -116   -697       C  
ATOM   3909  O   GLN A 513      40.399  44.587   7.952  1.00117.38           O  
ANISOU 3909  O   GLN A 513    17241  12352  15006    164     86   -765       O  
ATOM   3910  CB  GLN A 513      41.016  44.286   5.046  1.00113.07           C  
ANISOU 3910  CB  GLN A 513    16322  11822  14819    215   -197   -625       C  
ATOM   3911  CG  GLN A 513      39.686  45.042   5.111  1.00113.79           C  
ANISOU 3911  CG  GLN A 513    16442  11774  15020    350    -11   -664       C  
ATOM   3912  CD  GLN A 513      38.831  44.849   3.869  1.00112.50           C  
ANISOU 3912  CD  GLN A 513    16070  11582  15095    447    -16   -569       C  
ATOM   3913  OE1 GLN A 513      39.228  44.164   2.925  1.00110.68           O  
ANISOU 3913  OE1 GLN A 513    15690  11447  14918    401   -147   -495       O  
ATOM   3914  NE2 GLN A 513      37.645  45.447   3.870  1.00113.09           N  
ANISOU 3914  NE2 GLN A 513    16127  11519  15323    569    129   -574       N  
ATOM   3915  N   ALA A 514      42.180  43.242   8.236  1.00112.00           N  
ANISOU 3915  N   ALA A 514    16507  11852  14196    -54   -228   -627       N  
ATOM   3916  CA  ALA A 514      41.994  42.901   9.648  1.00113.88           C  
ANISOU 3916  CA  ALA A 514    16888  12154  14229   -154   -160   -620       C  
ATOM   3917  C   ALA A 514      40.684  42.186   9.959  1.00115.76           C  
ANISOU 3917  C   ALA A 514    17024  12444  14517    -54      7   -575       C  
ATOM   3918  O   ALA A 514      40.448  41.850  11.127  1.00117.44           O  
ANISOU 3918  O   ALA A 514    17342  12740  14540   -160     74   -559       O  
ATOM   3919  CB  ALA A 514      42.093  44.130  10.562  1.00114.41           C  
ANISOU 3919  CB  ALA A 514    17253  12150  14069   -241    -48   -769       C  
ATOM   3920  N   GLY A 515      39.826  41.945   8.975  1.00115.19           N  
ANISOU 3920  N   GLY A 515    16753  12336  14677    120     68   -542       N  
ATOM   3921  CA  GLY A 515      38.628  41.164   9.208  1.00116.00           C  
ANISOU 3921  CA  GLY A 515    16732  12496  14849    208    197   -466       C  
ATOM   3922  C   GLY A 515      38.592  39.951   8.306  1.00113.80           C  
ANISOU 3922  C   GLY A 515    16197  12264  14777    264     46   -323       C  
ATOM   3923  O   GLY A 515      37.941  38.946   8.605  1.00113.88           O  
ANISOU 3923  O   GLY A 515    16092  12348  14828    281     57   -210       O  
ATOM   3924  N   ALA A 516      39.309  40.047   7.190  1.00111.05           N  
ANISOU 3924  N   ALA A 516    15761  11877  14555    277    -96   -334       N  
ATOM   3925  CA  ALA A 516      39.400  38.987   6.202  1.00109.03           C  
ANISOU 3925  CA  ALA A 516    15272  11657  14497    318   -231   -248       C  
ATOM   3926  C   ALA A 516      40.593  38.069   6.433  1.00108.30           C  
ANISOU 3926  C   ALA A 516    15117  11627  14404    200   -442   -203       C  
ATOM   3927  O   ALA A 516      40.865  37.202   5.596  1.00106.57           O  
ANISOU 3927  O   ALA A 516    14701  11425  14365    226   -560   -174       O  
ATOM   3928  CB  ALA A 516      39.475  39.593   4.799  1.00107.57           C  
ANISOU 3928  CB  ALA A 516    15014  11416  14444    373   -251   -300       C  
ATOM   3929  N   TRP A 517      41.299  38.233   7.544  1.00115.01           N  
ANISOU 3929  N   TRP A 517    16123  12503  15072     62   -496   -198       N  
ATOM   3930  CA  TRP A 517      42.540  37.504   7.802  1.00114.40           C  
ANISOU 3930  CA  TRP A 517    15984  12457  15024    -67   -722   -139       C  
ATOM   3931  C   TRP A 517      42.434  36.709   9.093  1.00115.24           C  
ANISOU 3931  C   TRP A 517    16130  12623  15034   -188   -793     -4       C  
ATOM   3932  O   TRP A 517      42.345  37.308  10.182  1.00117.43           O  
ANISOU 3932  O   TRP A 517    16631  12931  15058   -302   -716    -12       O  
ATOM   3933  CB  TRP A 517      43.712  38.480   7.870  1.00114.48           C  
ANISOU 3933  CB  TRP A 517    16141  12443  14914   -175   -788   -218       C  
ATOM   3934  CG  TRP A 517      44.067  39.056   6.541  1.00113.14           C  
ANISOU 3934  CG  TRP A 517    15890  12243  14854   -106   -784   -315       C  
ATOM   3935  CD1 TRP A 517      43.560  40.189   5.977  1.00112.77           C  
ANISOU 3935  CD1 TRP A 517    15935  12144  14767    -37   -651   -401       C  
ATOM   3936  CD2 TRP A 517      45.035  38.545   5.618  1.00112.02           C  
ANISOU 3936  CD2 TRP A 517    15552  12126  14883   -125   -926   -334       C  
ATOM   3937  NE1 TRP A 517      44.140  40.407   4.751  1.00111.75           N  
ANISOU 3937  NE1 TRP A 517    15689  12026  14743    -36   -716   -450       N  
ATOM   3938  CE2 TRP A 517      45.055  39.416   4.511  1.00111.34           C  
ANISOU 3938  CE2 TRP A 517    15462  12033  14807    -88   -865   -427       C  
ATOM   3939  CE3 TRP A 517      45.897  37.444   5.626  1.00111.21           C  
ANISOU 3939  CE3 TRP A 517    15264  12047  14945   -176  -1100   -287       C  
ATOM   3940  CZ2 TRP A 517      45.894  39.214   3.418  1.00110.61           C  
ANISOU 3940  CZ2 TRP A 517    15198  11992  14838   -118   -946   -486       C  
ATOM   3941  CZ3 TRP A 517      46.725  37.242   4.538  1.00110.02           C  
ANISOU 3941  CZ3 TRP A 517    14927  11921  14956   -174  -1166   -369       C  
ATOM   3942  CH2 TRP A 517      46.716  38.121   3.448  1.00109.76           C  
ANISOU 3942  CH2 TRP A 517    14905  11915  14883   -153  -1077   -473       C  
ATOM   3943  N   PRO A 518      42.442  35.375   9.032  1.00125.42           N  
ANISOU 3943  N   PRO A 518    17214  13930  16511   -190   -947    121       N  
ATOM   3944  CA  PRO A 518      42.318  34.580  10.263  1.00126.39           C  
ANISOU 3944  CA  PRO A 518    17362  14113  16547   -339  -1052    289       C  
ATOM   3945  C   PRO A 518      43.568  34.583  11.126  1.00127.01           C  
ANISOU 3945  C   PRO A 518    17536  14197  16526   -561  -1258    363       C  
ATOM   3946  O   PRO A 518      43.486  34.167  12.290  1.00128.18           O  
ANISOU 3946  O   PRO A 518    17766  14411  16524   -743  -1342    510       O  
ATOM   3947  CB  PRO A 518      42.013  33.172   9.738  1.00124.96           C  
ANISOU 3947  CB  PRO A 518    16904  13911  16662   -261  -1191    400       C  
ATOM   3948  CG  PRO A 518      42.644  33.143   8.382  1.00123.22           C  
ANISOU 3948  CG  PRO A 518    16520  13618  16681   -142  -1238    274       C  
ATOM   3949  CD  PRO A 518      42.503  34.533   7.825  1.00123.51           C  
ANISOU 3949  CD  PRO A 518    16709  13650  16570    -70  -1033    110       C  
ATOM   3950  N   LEU A 519      44.709  35.026  10.600  1.00140.12           N  
ANISOU 3950  N   LEU A 519    19181  15799  18258   -574  -1353    283       N  
ATOM   3951  CA  LEU A 519      45.943  35.028  11.374  1.00141.11           C  
ANISOU 3951  CA  LEU A 519    19378  15917  18322   -790  -1572    376       C  
ATOM   3952  C   LEU A 519      45.779  35.837  12.655  1.00143.91           C  
ANISOU 3952  C   LEU A 519    20055  16337  18287   -981  -1493    394       C  
ATOM   3953  O   LEU A 519      45.159  36.904  12.665  1.00145.69           O  
ANISOU 3953  O   LEU A 519    20475  16575  18305   -918  -1247    242       O  
ATOM   3954  CB  LEU A 519      47.097  35.589  10.541  1.00139.43           C  
ANISOU 3954  CB  LEU A 519    19111  15645  18222   -762  -1636    266       C  
ATOM   3955  CG  LEU A 519      47.604  34.716   9.393  1.00137.35           C  
ANISOU 3955  CG  LEU A 519    18519  15329  18340   -638  -1745    233       C  
ATOM   3956  CD1 LEU A 519      48.617  35.474   8.555  1.00137.54           C  
ANISOU 3956  CD1 LEU A 519    18515  15336  18407   -623  -1744    100       C  
ATOM   3957  CD2 LEU A 519      48.215  33.436   9.939  1.00135.34           C  
ANISOU 3957  CD2 LEU A 519    18070  15027  18325   -746  -2025    414       C  
ATOM   3958  N   THR A 520      46.336  35.313  13.741  1.00166.36           N  
ANISOU 3958  N   THR A 520    22949  19215  21045  -1231  -1710    580       N  
ATOM   3959  CA  THR A 520      46.264  35.938  15.051  1.00166.62           C  
ANISOU 3959  CA  THR A 520    23295  19332  20680  -1475  -1664    611       C  
ATOM   3960  C   THR A 520      47.642  36.427  15.476  1.00166.52           C  
ANISOU 3960  C   THR A 520    23410  19279  20581  -1688  -1873    661       C  
ATOM   3961  O   THR A 520      48.657  36.164  14.825  1.00165.41           O  
ANISOU 3961  O   THR A 520    23081  19050  20716  -1650  -2067    699       O  
ATOM   3962  CB  THR A 520      45.695  34.964  16.090  1.00166.51           C  
ANISOU 3962  CB  THR A 520    23273  19426  20568  -1663  -1756    820       C  
ATOM   3963  OG1 THR A 520      46.543  33.813  16.189  1.00164.96           O  
ANISOU 3963  OG1 THR A 520    22855  19175  20646  -1783  -2122   1058       O  
ATOM   3964  CG2 THR A 520      44.293  34.526  15.693  1.00166.70           C  
ANISOU 3964  CG2 THR A 520    23175  19497  20667  -1458  -1543    781       C  
ATOM   3965  N   GLN A 521      47.661  37.149  16.596  1.00185.55           N  
ANISOU 3965  N   GLN A 521    26142  21759  22601  -1927  -1823    655       N  
ATOM   3966  CA  GLN A 521      48.882  37.798  17.060  1.00184.95           C  
ANISOU 3966  CA  GLN A 521    26243  21645  22384  -2149  -2001    694       C  
ATOM   3967  C   GLN A 521      49.837  36.827  17.746  1.00183.32           C  
ANISOU 3967  C   GLN A 521    25932  21438  22285  -2425  -2390    997       C  
ATOM   3968  O   GLN A 521      51.057  37.013  17.664  1.00181.23           O  
ANISOU 3968  O   GLN A 521    25640  21093  22124  -2527  -2615   1075       O  
ATOM   3969  CB  GLN A 521      48.518  38.954  17.996  1.00186.15           C  
ANISOU 3969  CB  GLN A 521    26795  21862  22070  -2315  -1797    550       C  
ATOM   3970  CG  GLN A 521      47.906  38.521  19.320  1.00186.97           C  
ANISOU 3970  CG  GLN A 521    27064  22121  21856  -2590  -1778    662       C  
ATOM   3971  CD  GLN A 521      46.421  38.209  19.218  1.00188.79           C  
ANISOU 3971  CD  GLN A 521    27222  22436  22074  -2408  -1486    567       C  
ATOM   3972  OE1 GLN A 521      45.882  38.032  18.124  1.00188.50           O  
ANISOU 3972  OE1 GLN A 521    26959  22332  22332  -2081  -1366    481       O  
ATOM   3973  NE2 GLN A 521      45.756  38.126  20.364  1.00190.41           N  
ANISOU 3973  NE2 GLN A 521    27615  22803  21930  -2641  -1375    592       N  
ATOM   3974  N   ALA A 522      49.310  35.790  18.410  1.00192.29           N  
ANISOU 3974  N   ALA A 522    26990  22652  23420  -2556  -2492   1190       N  
ATOM   3975  CA  ALA A 522      50.092  34.795  19.141  1.00190.91           C  
ANISOU 3975  CA  ALA A 522    26703  22466  23368  -2846  -2894   1520       C  
ATOM   3976  C   ALA A 522      51.104  35.459  20.070  1.00191.39           C  
ANISOU 3976  C   ALA A 522    27032  22537  23150  -3199  -3080   1625       C  
ATOM   3977  O   ALA A 522      52.316  35.350  19.845  1.00190.15           O  
ANISOU 3977  O   ALA A 522    26744  22262  23241  -3258  -3356   1748       O  
ATOM   3978  CB  ALA A 522      50.803  33.850  18.170  1.00187.26           C  
ANISOU 3978  CB  ALA A 522    25829  21847  23474  -2661  -3130   1610       C  
ATOM   3979  N   PRO A 523      50.651  36.150  21.129  1.00198.93           N  
ANISOU 3979  N   PRO A 523    28359  23631  23592  -3452  -2936   1577       N  
ATOM   3980  CA  PRO A 523      51.556  36.919  21.989  1.00199.70           C  
ANISOU 3980  CA  PRO A 523    28762  23741  23372  -3798  -3084   1640       C  
ATOM   3981  C   PRO A 523      52.342  36.041  22.959  1.00198.73           C  
ANISOU 3981  C   PRO A 523    28600  23638  23269  -4217  -3532   2040       C  
ATOM   3982  O   PRO A 523      51.771  35.110  23.527  1.00196.62           O  
ANISOU 3982  O   PRO A 523    28258  23470  22979  -4368  -3627   2231       O  
ATOM   3983  CB  PRO A 523      50.604  37.846  22.745  1.00200.45           C  
ANISOU 3983  CB  PRO A 523    29248  23987  22927  -3906  -2728   1408       C  
ATOM   3984  CG  PRO A 523      49.340  37.063  22.838  1.00199.85           C  
ANISOU 3984  CG  PRO A 523    29048  24034  22853  -3814  -2558   1416       C  
ATOM   3985  CD  PRO A 523      49.250  36.249  21.574  1.00199.30           C  
ANISOU 3985  CD  PRO A 523    28558  23838  23329  -3434  -2611   1444       C  
ATOM   3986  N   PRO A 530      61.355  42.641  22.777  1.00236.71           N  
ANISOU 3986  N   PRO A 530    34395  27746  27800  -5207  -4801   2288       N  
ATOM   3987  CA  PRO A 530      59.931  42.957  22.776  1.00235.81           C  
ANISOU 3987  CA  PRO A 530    34478  27725  27396  -5019  -4380   1958       C  
ATOM   3988  C   PRO A 530      59.711  44.465  22.772  1.00235.93           C  
ANISOU 3988  C   PRO A 530    34886  27722  27033  -4994  -4136   1652       C  
ATOM   3989  O   PRO A 530      58.655  44.946  22.361  1.00234.58           O  
ANISOU 3989  O   PRO A 530    34799  27572  26758  -4722  -3760   1327       O  
ATOM   3990  CB  PRO A 530      59.245  42.323  23.970  1.00238.21           C  
ANISOU 3990  CB  PRO A 530    34957  28156  27394  -5318  -4407   2077       C  
ATOM   3991  N   GLN A 531      60.708  45.205  23.244  1.00223.74           N  
ANISOU 3991  N   GLN A 531    33579  26124  25309  -5287  -4369   1769       N  
ATOM   3992  CA  GLN A 531      60.690  46.655  23.162  1.00223.97           C  
ANISOU 3992  CA  GLN A 531    33954  26095  25048  -5267  -4201   1504       C  
ATOM   3993  C   GLN A 531      61.305  47.107  21.841  1.00221.38           C  
ANISOU 3993  C   GLN A 531    33365  25666  25084  -4962  -4209   1449       C  
ATOM   3994  O   GLN A 531      62.007  46.351  21.165  1.00220.07           O  
ANISOU 3994  O   GLN A 531    32789  25479  25350  -4855  -4396   1649       O  
ATOM   3995  CB  GLN A 531      61.441  47.278  24.340  1.00227.44           C  
ANISOU 3995  CB  GLN A 531    34809  26526  25081  -5761  -4454   1651       C  
ATOM   3996  N   GLU A 532      61.020  48.355  21.476  1.00213.56           N  
ANISOU 3996  N   GLU A 532    32608  24613  23922  -4831  -3999   1167       N  
ATOM   3997  CA  GLU A 532      61.499  48.897  20.212  1.00211.30           C  
ANISOU 3997  CA  GLU A 532    32107  24252  23926  -4566  -3989   1101       C  
ATOM   3998  C   GLU A 532      63.021  48.833  20.133  1.00211.97           C  
ANISOU 3998  C   GLU A 532    32047  24299  24194  -4771  -4378   1415       C  
ATOM   3999  O   GLU A 532      63.727  48.967  21.137  1.00214.58           O  
ANISOU 3999  O   GLU A 532    32612  24612  24306  -5154  -4648   1623       O  
ATOM   4000  CB  GLU A 532      61.024  50.340  20.038  1.00211.44           C  
ANISOU 4000  CB  GLU A 532    32454  24185  23700  -4477  -3771    791       C  
ATOM   4001  N   LEU A 533      63.523  48.631  18.921  1.00201.82           N  
ANISOU 4001  N   LEU A 533    30366  23006  23309  -4526  -4400   1447       N  
ATOM   4002  CA  LEU A 533      64.944  48.455  18.657  1.00202.30           C  
ANISOU 4002  CA  LEU A 533    30186  23042  23636  -4660  -4730   1730       C  
ATOM   4003  C   LEU A 533      65.442  49.583  17.754  1.00201.36           C  
ANISOU 4003  C   LEU A 533    30078  22888  23542  -4559  -4707   1629       C  
ATOM   4004  O   LEU A 533      64.738  50.565  17.502  1.00200.75           O  
ANISOU 4004  O   LEU A 533    30249  22778  23248  -4438  -4487   1367       O  
ATOM   4005  CB  LEU A 533      65.206  47.078  18.042  1.00201.09           C  
ANISOU 4005  CB  LEU A 533    29501  22928  23976  -4491  -4790   1869       C  
ATOM   4006  N   GLU A 534      66.660  49.450  17.244  1.00192.06           N  
ANISOU 4006  N   GLU A 534    28616  21710  22647  -4624  -4951   1850       N  
ATOM   4007  CA  GLU A 534      67.175  50.491  16.368  1.00191.37           C  
ANISOU 4007  CA  GLU A 534    28487  21618  22608  -4565  -4968   1806       C  
ATOM   4008  C   GLU A 534      66.056  51.501  16.116  1.00188.71           C  
ANISOU 4008  C   GLU A 534    27978  21336  22389  -4196  -4639   1519       C  
ATOM   4009  O   GLU A 534      66.303  52.626  15.683  1.00188.19           O  
ANISOU 4009  O   GLU A 534    28007  21257  22241  -4145  -4590   1412       O  
ATOM   4010  CB  GLU A 534      67.659  49.894  15.046  1.00192.04           C  
ANISOU 4010  CB  GLU A 534    28200  21725  23042  -4669  -5249   2092       C  
ATOM   4011  N   LYS A 535      64.822  51.084  16.397  1.00171.51           N  
ANISOU 4011  N   LYS A 535    27164  18968  19034  -4340  -4097    890       N  
ATOM   4012  CA  LYS A 535      63.646  51.932  16.220  1.00170.17           C  
ANISOU 4012  CA  LYS A 535    27034  18732  18891  -4088  -3882    632       C  
ATOM   4013  C   LYS A 535      63.289  52.113  14.744  1.00167.29           C  
ANISOU 4013  C   LYS A 535    26202  18449  18911  -3775  -3776    623       C  
ATOM   4014  O   LYS A 535      63.517  51.215  13.934  1.00166.18           O  
ANISOU 4014  O   LYS A 535    25760  18402  18979  -3666  -3728    691       O  
ATOM   4015  CB  LYS A 535      63.864  53.289  16.897  1.00171.47           C  
ANISOU 4015  CB  LYS A 535    27442  18789  18918  -4262  -4075    661       C  
ATOM   4016  N   SER A 536      62.725  53.277  14.420  1.00167.03           N  
ANISOU 4016  N   SER A 536    26122  18379  18962  -3655  -3751    540       N  
ATOM   4017  CA  SER A 536      62.330  53.648  13.057  1.00165.80           C  
ANISOU 4017  CA  SER A 536    25573  18310  19114  -3404  -3650    510       C  
ATOM   4018  C   SER A 536      60.884  53.337  12.655  1.00161.56           C  
ANISOU 4018  C   SER A 536    24959  17779  18648  -3112  -3330    284       C  
ATOM   4019  O   SER A 536      60.520  53.521  11.493  1.00159.18           O  
ANISOU 4019  O   SER A 536    24367  17547  18568  -2913  -3227    237       O  
ATOM   4020  CB  SER A 536      63.308  53.094  12.011  1.00168.26           C  
ANISOU 4020  CB  SER A 536    25460  18756  19716  -3416  -3786    719       C  
ATOM   4021  OG  SER A 536      63.355  51.678  12.057  1.00167.90           O  
ANISOU 4021  OG  SER A 536    25295  18751  19749  -3373  -3725    751       O  
ATOM   4022  N   VAL A 537      60.055  52.878  13.590  1.00163.10           N  
ANISOU 4022  N   VAL A 537    25401  17914  18656  -3096  -3167    147       N  
ATOM   4023  CA  VAL A 537      58.671  52.595  13.238  1.00159.16           C  
ANISOU 4023  CA  VAL A 537    24830  17415  18230  -2828  -2864    -52       C  
ATOM   4024  C   VAL A 537      57.808  53.849  13.280  1.00160.11           C  
ANISOU 4024  C   VAL A 537    25238  17378  18221  -2747  -2702   -287       C  
ATOM   4025  O   VAL A 537      56.960  54.044  12.411  1.00160.16           O  
ANISOU 4025  O   VAL A 537    25111  17354  18387  -2511  -2525   -415       O  
ATOM   4026  N   GLN A 538      58.013  54.710  14.281  1.00164.14           N  
ANISOU 4026  N   GLN A 538    26137  17770  18458  -2949  -2769   -348       N  
ATOM   4027  CA  GLN A 538      57.182  55.904  14.416  1.00164.54           C  
ANISOU 4027  CA  GLN A 538    26464  17636  18417  -2869  -2608   -604       C  
ATOM   4028  C   GLN A 538      57.496  56.955  13.359  1.00162.55           C  
ANISOU 4028  C   GLN A 538    26160  17279  18321  -2806  -2720   -602       C  
ATOM   4029  O   GLN A 538      56.581  57.636  12.883  1.00162.74           O  
ANISOU 4029  O   GLN A 538    26206  17170  18459  -2619  -2561   -782       O  
ATOM   4030  CB  GLN A 538      57.321  56.497  15.818  1.00166.43           C  
ANISOU 4030  CB  GLN A 538    27148  17781  18309  -3123  -2637   -700       C  
ATOM   4031  CG  GLN A 538      56.682  57.876  15.971  1.00169.96           C  
ANISOU 4031  CG  GLN A 538    27893  17997  18689  -3067  -2510   -981       C  
ATOM   4032  CD  GLN A 538      55.215  57.907  15.576  1.00167.53           C  
ANISOU 4032  CD  GLN A 538    27479  17619  18554  -2755  -2174  -1222       C  
ATOM   4033  OE1 GLN A 538      54.454  56.988  15.876  1.00165.25           O  
ANISOU 4033  OE1 GLN A 538    27084  17446  18257  -2660  -1964  -1265       O  
ATOM   4034  NE2 GLN A 538      54.816  58.972  14.887  1.00168.04           N  
ANISOU 4034  NE2 GLN A 538    27559  17488  18801  -2603  -2144  -1356       N  
ATOM   4035  N   MET A 539      58.764  57.102  12.965  1.00177.70           N  
ANISOU 4035  N   MET A 539    27995  19257  20267  -2969  -3002   -385       N  
ATOM   4036  CA  MET A 539      59.060  58.000  11.854  1.00177.64           C  
ANISOU 4036  CA  MET A 539    27892  19192  20412  -2926  -3117   -350       C  
ATOM   4037  C   MET A 539      58.339  57.586  10.579  1.00177.74           C  
ANISOU 4037  C   MET A 539    27555  19287  20692  -2670  -2960   -378       C  
ATOM   4038  O   MET A 539      58.316  58.361   9.616  1.00177.11           O  
ANISOU 4038  O   MET A 539    27400  19155  20738  -2626  -3023   -369       O  
ATOM   4039  CB  MET A 539      60.561  58.060  11.584  1.00177.84           C  
ANISOU 4039  CB  MET A 539    27823  19317  20433  -3146  -3428    -92       C  
ATOM   4040  CG  MET A 539      61.139  56.770  11.039  1.00173.88           C  
ANISOU 4040  CG  MET A 539    26919  19047  20102  -3119  -3456     86       C  
ATOM   4041  SD  MET A 539      62.854  56.993  10.553  1.00172.42           S  
ANISOU 4041  SD  MET A 539    26573  18971  19968  -3354  -3792    366       S  
ATOM   4042  CE  MET A 539      62.650  57.981   9.070  1.00170.12           C  
ANISOU 4042  CE  MET A 539    26151  18679  19808  -3257  -3791    327       C  
ATOM   4043  N   PHE A 540      57.761  56.386  10.557  1.00149.45           N  
ANISOU 4043  N   PHE A 540    23763  15830  17191  -2525  -2777   -397       N  
ATOM   4044  CA  PHE A 540      56.949  55.887   9.459  1.00150.15           C  
ANISOU 4044  CA  PHE A 540    23545  15993  17510  -2289  -2607   -439       C  
ATOM   4045  C   PHE A 540      55.462  55.862   9.766  1.00151.50           C  
ANISOU 4045  C   PHE A 540    23801  16056  17708  -2085  -2330   -643       C  
ATOM   4046  O   PHE A 540      54.651  55.960   8.843  1.00151.60           O  
ANISOU 4046  O   PHE A 540    23645  16046  17909  -1904  -2214   -697       O  
ATOM   4047  CB  PHE A 540      57.388  54.466   9.085  1.00150.84           C  
ANISOU 4047  CB  PHE A 540    23292  16302  17720  -2263  -2610   -307       C  
ATOM   4048  N   GLU A 541      55.090  55.743  11.043  1.00133.74           N  
ANISOU 4048  N   GLU A 541    21801  13746  15268  -2132  -2223   -751       N  
ATOM   4049  CA  GLU A 541      53.708  55.470  11.414  1.00134.78           C  
ANISOU 4049  CA  GLU A 541    21962  13825  15421  -1946  -1932   -934       C  
ATOM   4050  C   GLU A 541      52.829  56.711  11.320  1.00134.84           C  
ANISOU 4050  C   GLU A 541    22141  13597  15497  -1829  -1809  -1142       C  
ATOM   4051  O   GLU A 541      51.613  56.589  11.133  1.00135.80           O  
ANISOU 4051  O   GLU A 541    22175  13663  15759  -1618  -1574  -1271       O  
ATOM   4052  CB  GLU A 541      53.666  54.882  12.826  1.00136.22           C  
ANISOU 4052  CB  GLU A 541    22345  14062  15350  -2079  -1861   -969       C  
ATOM   4053  CG  GLU A 541      52.302  54.387  13.273  1.00138.77           C  
ANISOU 4053  CG  GLU A 541    22663  14390  15674  -1914  -1554  -1131       C  
ATOM   4054  CD  GLU A 541      52.350  53.719  14.632  1.00140.69           C  
ANISOU 4054  CD  GLU A 541    23084  14734  15639  -2099  -1513  -1126       C  
ATOM   4055  OE1 GLU A 541      53.443  53.676  15.235  1.00139.80           O  
ANISOU 4055  OE1 GLU A 541    23110  14667  15342  -2360  -1740   -990       O  
ATOM   4056  OE2 GLU A 541      51.298  53.230  15.095  1.00142.82           O  
ANISOU 4056  OE2 GLU A 541    23348  15045  15873  -2004  -1268  -1238       O  
ATOM   4057  N   LEU A 542      53.418  57.905  11.436  1.00133.73           N  
ANISOU 4057  N   LEU A 542    22225  13297  15287  -1961  -1976  -1169       N  
ATOM   4058  CA  LEU A 542      52.651  59.134  11.270  1.00133.58           C  
ANISOU 4058  CA  LEU A 542    22342  13014  15398  -1848  -1898  -1359       C  
ATOM   4059  C   LEU A 542      52.054  59.254   9.874  1.00132.88           C  
ANISOU 4059  C   LEU A 542    21954  12899  15635  -1657  -1890  -1296       C  
ATOM   4060  O   LEU A 542      51.141  60.061   9.669  1.00133.89           O  
ANISOU 4060  O   LEU A 542    22118  12803  15953  -1514  -1790  -1443       O  
ATOM   4061  CB  LEU A 542      53.530  60.351  11.567  1.00132.59           C  
ANISOU 4061  CB  LEU A 542    22497  12724  15159  -2048  -2135  -1365       C  
ATOM   4062  N   PHE A 543      52.549  58.471   8.911  1.00119.46           N  
ANISOU 4062  N   PHE A 543    19957  11419  14015  -1666  -1996  -1085       N  
ATOM   4063  CA  PHE A 543      51.978  58.490   7.569  1.00118.58           C  
ANISOU 4063  CA  PHE A 543    19564  11318  14172  -1526  -1989  -1014       C  
ATOM   4064  C   PHE A 543      50.604  57.836   7.524  1.00119.06           C  
ANISOU 4064  C   PHE A 543    19487  11371  14381  -1291  -1710  -1119       C  
ATOM   4065  O   PHE A 543      49.692  58.346   6.862  1.00119.56           O  
ANISOU 4065  O   PHE A 543    19457  11289  14682  -1151  -1652  -1156       O  
ATOM   4066  CB  PHE A 543      52.920  57.804   6.583  1.00116.79           C  
ANISOU 4066  CB  PHE A 543    19066  11351  13959  -1626  -2153   -794       C  
ATOM   4067  CG  PHE A 543      52.297  57.544   5.244  1.00115.93           C  
ANISOU 4067  CG  PHE A 543    18660  11315  14073  -1511  -2114   -725       C  
ATOM   4068  CD1 PHE A 543      52.018  58.584   4.375  1.00116.05           C  
ANISOU 4068  CD1 PHE A 543    18651  11195  14247  -1524  -2232   -681       C  
ATOM   4069  CD2 PHE A 543      51.988  56.252   4.855  1.00115.21           C  
ANISOU 4069  CD2 PHE A 543    18317  11422  14036  -1412  -1980   -692       C  
ATOM   4070  CE1 PHE A 543      51.437  58.337   3.146  1.00115.41           C  
ANISOU 4070  CE1 PHE A 543    18308  11193  14350  -1462  -2216   -595       C  
ATOM   4071  CE2 PHE A 543      51.413  55.999   3.627  1.00114.49           C  
ANISOU 4071  CE2 PHE A 543    17973  11405  14124  -1335  -1948   -631       C  
ATOM   4072  CZ  PHE A 543      51.136  57.041   2.772  1.00114.56           C  
ANISOU 4072  CZ  PHE A 543    17967  11295  14264  -1371  -2066   -577       C  
ATOM   4073  N   TYR A 544      50.432  56.700   8.201  1.00117.87           N  
ANISOU 4073  N   TYR A 544    19304  11371  14111  -1256  -1555  -1142       N  
ATOM   4074  CA  TYR A 544      49.158  55.999   8.113  1.00119.97           C  
ANISOU 4074  CA  TYR A 544    19414  11653  14516  -1045  -1305  -1212       C  
ATOM   4075  C   TYR A 544      48.075  56.684   8.936  1.00121.86           C  
ANISOU 4075  C   TYR A 544    19849  11668  14783   -927  -1082  -1445       C  
ATOM   4076  O   TYR A 544      46.889  56.398   8.742  1.00123.34           O  
ANISOU 4076  O   TYR A 544    19899  11815  15149   -734   -876  -1509       O  
ATOM   4077  CB  TYR A 544      49.313  54.543   8.562  1.00121.19           C  
ANISOU 4077  CB  TYR A 544    19458  12037  14551  -1058  -1233  -1145       C  
ATOM   4078  CG  TYR A 544      48.193  53.635   8.091  1.00121.91           C  
ANISOU 4078  CG  TYR A 544    19305  12198  14818   -858  -1044  -1140       C  
ATOM   4079  CD1 TYR A 544      48.196  53.124   6.799  1.00120.37           C  
ANISOU 4079  CD1 TYR A 544    18819  12113  14804   -801  -1112  -1009       C  
ATOM   4080  CD2 TYR A 544      47.129  53.307   8.921  1.00123.83           C  
ANISOU 4080  CD2 TYR A 544    19610  12405  15035   -744   -797  -1268       C  
ATOM   4081  CE1 TYR A 544      47.185  52.301   6.353  1.00120.42           C  
ANISOU 4081  CE1 TYR A 544    18613  12174  14965   -636   -960   -995       C  
ATOM   4082  CE2 TYR A 544      46.110  52.482   8.480  1.00124.43           C  
ANISOU 4082  CE2 TYR A 544    19457  12543  15277   -571   -642  -1241       C  
ATOM   4083  CZ  TYR A 544      46.145  51.985   7.195  1.00122.67           C  
ANISOU 4083  CZ  TYR A 544    18959  12411  15239   -516   -735  -1100       C  
ATOM   4084  OH  TYR A 544      45.135  51.167   6.748  1.00124.26           O  
ANISOU 4084  OH  TYR A 544    18946  12666  15600   -359   -599  -1065       O  
ATOM   4085  N   SER A 545      48.459  57.584   9.845  1.00130.97           N  
ANISOU 4085  N   SER A 545    21315  12673  15774  -1045  -1112  -1583       N  
ATOM   4086  CA  SER A 545      47.479  58.350  10.606  1.00132.40           C  
ANISOU 4086  CA  SER A 545    21685  12622  16000   -939   -884  -1853       C  
ATOM   4087  C   SER A 545      46.955  59.538   9.807  1.00131.94           C  
ANISOU 4087  C   SER A 545    21578  12283  16271   -818   -939  -1903       C  
ATOM   4088  O   SER A 545      45.776  59.891   9.916  1.00133.44           O  
ANISOU 4088  O   SER A 545    21734  12288  16679   -629   -720  -2076       O  
ATOM   4089  CB  SER A 545      48.095  58.830  11.921  1.00133.59           C  
ANISOU 4089  CB  SER A 545    22207  12722  15830  -1136   -889  -2006       C  
ATOM   4090  OG  SER A 545      49.112  59.791  11.687  1.00132.13           O  
ANISOU 4090  OG  SER A 545    22169  12421  15612  -1295  -1172  -1944       O  
ATOM   4091  N   GLN A 546      47.815  60.172   9.008  1.00122.73           N  
ANISOU 4091  N   GLN A 546    20393  11076  15163   -936  -1240  -1743       N  
ATOM   4092  CA  GLN A 546      47.394  61.321   8.219  1.00123.12           C  
ANISOU 4092  CA  GLN A 546    20391  10854  15536   -862  -1353  -1746       C  
ATOM   4093  C   GLN A 546      46.732  60.928   6.906  1.00122.66           C  
ANISOU 4093  C   GLN A 546    19986  10852  15767   -736  -1374  -1567       C  
ATOM   4094  O   GLN A 546      45.948  61.717   6.367  1.00123.57           O  
ANISOU 4094  O   GLN A 546    20019  10719  16213   -625  -1393  -1587       O  
ATOM   4095  CB  GLN A 546      48.588  62.234   7.928  1.00121.96           C  
ANISOU 4095  CB  GLN A 546    20380  10641  15317  -1076  -1691  -1631       C  
ATOM   4096  CG  GLN A 546      49.135  62.947   9.152  1.00123.31           C  
ANISOU 4096  CG  GLN A 546    20925  10667  15259  -1207  -1707  -1821       C  
ATOM   4097  CD  GLN A 546      50.279  63.885   8.816  1.00121.94           C  
ANISOU 4097  CD  GLN A 546    20876  10414  15040  -1420  -2064  -1685       C  
ATOM   4098  OE1 GLN A 546      50.724  63.954   7.669  1.00120.02           O  
ANISOU 4098  OE1 GLN A 546    20429  10261  14911  -1485  -2296  -1438       O  
ATOM   4099  NE2 GLN A 546      50.756  64.621   9.815  1.00122.46           N  
ANISOU 4099  NE2 GLN A 546    21283  10321  14924  -1550  -2112  -1845       N  
ATOM   4100  N   HIS A 547      47.022  59.736   6.379  1.00123.50           N  
ANISOU 4100  N   HIS A 547    19886  11265  15773   -763  -1383  -1392       N  
ATOM   4101  CA  HIS A 547      46.473  59.360   5.080  1.00122.79           C  
ANISOU 4101  CA  HIS A 547    19486  11248  15920   -688  -1422  -1219       C  
ATOM   4102  C   HIS A 547      45.041  58.848   5.188  1.00124.42           C  
ANISOU 4102  C   HIS A 547    19555  11394  16323   -454  -1147  -1308       C  
ATOM   4103  O   HIS A 547      44.230  59.083   4.286  1.00124.78           O  
ANISOU 4103  O   HIS A 547    19409  11335  16668   -362  -1171  -1220       O  
ATOM   4104  CB  HIS A 547      47.358  58.310   4.413  1.00120.60           C  
ANISOU 4104  CB  HIS A 547    19034  11311  15477   -813  -1533  -1026       C  
ATOM   4105  CG  HIS A 547      46.934  57.970   3.018  1.00120.06           C  
ANISOU 4105  CG  HIS A 547    18674  11342  15602   -792  -1596   -855       C  
ATOM   4106  ND1 HIS A 547      45.992  57.003   2.742  1.00120.96           N  
ANISOU 4106  ND1 HIS A 547    18594  11544  15822   -640  -1413   -845       N  
ATOM   4107  CD2 HIS A 547      47.316  58.476   1.822  1.00119.00           C  
ANISOU 4107  CD2 HIS A 547    18418  11242  15554   -932  -1829   -679       C  
ATOM   4108  CE1 HIS A 547      45.817  56.921   1.435  1.00120.17           C  
ANISOU 4108  CE1 HIS A 547    18276  11523  15861   -690  -1529   -679       C  
ATOM   4109  NE2 HIS A 547      46.608  57.805   0.854  1.00119.43           N  
ANISOU 4109  NE2 HIS A 547    18220  11408  15749   -875  -1778   -576       N  
ATOM   4110  N   PHE A 548      44.712  58.142   6.265  1.00127.91           N  
ANISOU 4110  N   PHE A 548    20086  11912  16604   -378   -899  -1459       N  
ATOM   4111  CA  PHE A 548      43.355  57.672   6.495  1.00130.33           C  
ANISOU 4111  CA  PHE A 548    20270  12170  17077   -165   -620  -1551       C  
ATOM   4112  C   PHE A 548      42.739  58.404   7.680  1.00133.16           C  
ANISOU 4112  C   PHE A 548    20847  12299  17451    -77   -393  -1839       C  
ATOM   4113  O   PHE A 548      43.443  58.875   8.577  1.00134.92           O  
ANISOU 4113  O   PHE A 548    21344  12483  17436   -203   -412  -1977       O  
ATOM   4114  CB  PHE A 548      43.316  56.158   6.726  1.00130.27           C  
ANISOU 4114  CB  PHE A 548    20148  12458  16892   -150   -495  -1485       C  
ATOM   4115  CG  PHE A 548      43.621  55.350   5.495  1.00128.45           C  
ANISOU 4115  CG  PHE A 548    19659  12430  16716   -189   -651  -1251       C  
ATOM   4116  CD1 PHE A 548      42.676  55.220   4.490  1.00128.50           C  
ANISOU 4116  CD1 PHE A 548    19427  12395  17003    -72   -632  -1148       C  
ATOM   4117  CD2 PHE A 548      44.839  54.707   5.349  1.00127.03           C  
ANISOU 4117  CD2 PHE A 548    19468  12480  16317   -353   -809  -1142       C  
ATOM   4118  CE1 PHE A 548      42.946  54.481   3.353  1.00126.94           C  
ANISOU 4118  CE1 PHE A 548    19010  12393  16828   -133   -762   -959       C  
ATOM   4119  CE2 PHE A 548      45.113  53.961   4.214  1.00125.67           C  
ANISOU 4119  CE2 PHE A 548    19053  12496  16199   -391   -920   -972       C  
ATOM   4120  CZ  PHE A 548      44.165  53.848   3.217  1.00125.38           C  
ANISOU 4120  CZ  PHE A 548    18806  12429  16404   -289   -891   -890       C  
ATOM   4121  N   SER A 549      41.407  58.494   7.666  1.00139.85           N  
ANISOU 4121  N   SER A 549    21560  12992  18584    133   -173  -1933       N  
ATOM   4122  CA  SER A 549      40.696  59.339   8.621  1.00141.98           C  
ANISOU 4122  CA  SER A 549    21988  13000  18959    242     64  -2238       C  
ATOM   4123  C   SER A 549      40.917  58.874  10.057  1.00142.94           C  
ANISOU 4123  C   SER A 549    22351  13275  18685    161    290  -2446       C  
ATOM   4124  O   SER A 549      41.515  59.587  10.870  1.00144.08           O  
ANISOU 4124  O   SER A 549    22786  13324  18633     37    278  -2629       O  
ATOM   4125  CB  SER A 549      39.204  59.359   8.281  1.00143.16           C  
ANISOU 4125  CB  SER A 549    21890  12987  19518    487    270  -2273       C  
ATOM   4126  OG  SER A 549      38.626  58.075   8.449  1.00143.67           O  
ANISOU 4126  OG  SER A 549    21804  13304  19480    557    467  -2210       O  
ATOM   4127  N   GLY A 550      40.439  57.679  10.388  1.00144.36           N  
ANISOU 4127  N   GLY A 550    22421  13696  18734    204    480  -2407       N  
ATOM   4128  CA  GLY A 550      40.506  57.213  11.759  1.00145.42           C  
ANISOU 4128  CA  GLY A 550    22766  13986  18502    105    698  -2584       C  
ATOM   4129  C   GLY A 550      40.879  55.753  11.903  1.00144.39           C  
ANISOU 4129  C   GLY A 550    22556  14202  18103      2    661  -2385       C  
ATOM   4130  O   GLY A 550      40.445  55.088  12.849  1.00145.90           O  
ANISOU 4130  O   GLY A 550    22800  14547  18089    -26    887  -2475       O  
ATOM   4131  N   ARG A 551      41.681  55.238  10.977  1.00132.99           N  
ANISOU 4131  N   ARG A 551    20977  12885  16669    -64    378  -2117       N  
ATOM   4132  CA  ARG A 551      42.059  53.834  11.013  1.00132.39           C  
ANISOU 4132  CA  ARG A 551    20789  13102  16412   -145    318  -1927       C  
ATOM   4133  C   ARG A 551      43.110  53.596  12.089  1.00132.27           C  
ANISOU 4133  C   ARG A 551    21030  13226  16002   -393    239  -1945       C  
ATOM   4134  O   ARG A 551      44.140  54.276  12.128  1.00131.43           O  
ANISOU 4134  O   ARG A 551    21097  13056  15784   -543     39  -1942       O  
ATOM   4135  CB  ARG A 551      42.578  53.380   9.650  1.00130.32           C  
ANISOU 4135  CB  ARG A 551    20287  12922  16309   -137     65  -1674       C  
ATOM   4136  CG  ARG A 551      41.510  53.369   8.574  1.00130.41           C  
ANISOU 4136  CG  ARG A 551    20029  12844  16677     66    123  -1604       C  
ATOM   4137  CD  ARG A 551      42.020  52.773   7.279  1.00128.58           C  
ANISOU 4137  CD  ARG A 551    19572  12743  16541     33   -104  -1370       C  
ATOM   4138  NE  ARG A 551      40.982  52.766   6.254  1.00128.52           N  
ANISOU 4138  NE  ARG A 551    19325  12656  16852    189    -67  -1286       N  
ATOM   4139  CZ  ARG A 551      41.133  52.246   5.041  1.00127.54           C  
ANISOU 4139  CZ  ARG A 551    18986  12639  16834    169   -220  -1101       C  
ATOM   4140  NH1 ARG A 551      42.278  51.669   4.702  1.00126.37           N  
ANISOU 4140  NH1 ARG A 551    18813  12683  16519     22   -394  -1007       N  
ATOM   4141  NH2 ARG A 551      40.133  52.288   4.171  1.00127.84           N  
ANISOU 4141  NH2 ARG A 551    18829  12595  17151    284   -195  -1015       N  
ATOM   4142  N   LYS A 552      42.839  52.635  12.967  1.00137.07           N  
ANISOU 4142  N   LYS A 552    21657  14022  16403   -457    375  -1943       N  
ATOM   4143  CA  LYS A 552      43.759  52.239  14.025  1.00137.47           C  
ANISOU 4143  CA  LYS A 552    21926  14226  16081   -724    281  -1913       C  
ATOM   4144  C   LYS A 552      44.484  50.975  13.582  1.00136.20           C  
ANISOU 4144  C   LYS A 552    21564  14269  15919   -796     50  -1629       C  
ATOM   4145  O   LYS A 552      43.852  49.932  13.383  1.00136.77           O  
ANISOU 4145  O   LYS A 552    21417  14463  16087   -699    124  -1528       O  
ATOM   4146  CB  LYS A 552      43.004  52.004  15.335  1.00140.45           C  
ANISOU 4146  CB  LYS A 552    22460  14691  16215   -794    565  -2083       C  
ATOM   4147  CG  LYS A 552      43.867  51.717  16.565  1.00141.22           C  
ANISOU 4147  CG  LYS A 552    22828  14940  15889  -1122    473  -2062       C  
ATOM   4148  CD  LYS A 552      44.216  50.239  16.709  1.00141.33           C  
ANISOU 4148  CD  LYS A 552    22685  15200  15815  -1240    320  -1785       C  
ATOM   4149  CE  LYS A 552      42.973  49.380  16.892  1.00143.58           C  
ANISOU 4149  CE  LYS A 552    22790  15608  16155  -1118    564  -1784       C  
ATOM   4150  NZ  LYS A 552      42.264  49.680  18.166  1.00146.19           N  
ANISOU 4150  NZ  LYS A 552    23352  15999  16196  -1238    864  -2016       N  
ATOM   4151  N   LEU A 553      45.801  51.066  13.432  1.00119.35           N  
ANISOU 4151  N   LEU A 553    19492  12159  13698   -964   -229  -1505       N  
ATOM   4152  CA  LEU A 553      46.608  49.910  13.082  1.00117.21           C  
ANISOU 4152  CA  LEU A 553    19025  12057  13453  -1043   -450  -1261       C  
ATOM   4153  C   LEU A 553      47.234  49.300  14.331  1.00118.61           C  
ANISOU 4153  C   LEU A 553    19366  12367  13331  -1306   -540  -1182       C  
ATOM   4154  O   LEU A 553      47.567  50.002  15.289  1.00120.97           O  
ANISOU 4154  O   LEU A 553    19974  12624  13364  -1494   -534  -1286       O  
ATOM   4155  CB  LEU A 553      47.699  50.274  12.066  1.00115.60           C  
ANISOU 4155  CB  LEU A 553    18728  11818  13378  -1070   -706  -1150       C  
ATOM   4156  CG  LEU A 553      48.790  51.302  12.383  1.00116.88           C  
ANISOU 4156  CG  LEU A 553    19138  11892  13380  -1261   -884  -1171       C  
ATOM   4157  CD1 LEU A 553      49.946  50.697  13.163  1.00117.34           C  
ANISOU 4157  CD1 LEU A 553    19277  12073  13234  -1519  -1095  -1017       C  
ATOM   4158  CD2 LEU A 553      49.310  51.895  11.092  1.00115.40           C  
ANISOU 4158  CD2 LEU A 553    18810  11642  13395  -1202  -1040  -1109       C  
ATOM   4159  N   THR A 554      47.385  47.978  14.308  1.00117.37           N  
ANISOU 4159  N   THR A 554    19001  12364  13230  -1334   -639   -991       N  
ATOM   4160  CA  THR A 554      48.055  47.230  15.362  1.00117.62           C  
ANISOU 4160  CA  THR A 554    19126  12522  13041  -1601   -795   -843       C  
ATOM   4161  C   THR A 554      49.200  46.440  14.748  1.00116.84           C  
ANISOU 4161  C   THR A 554    18793  12474  13127  -1652  -1097   -612       C  
ATOM   4162  O   THR A 554      49.029  45.796  13.707  1.00116.68           O  
ANISOU 4162  O   THR A 554    18468  12473  13392  -1462  -1111   -552       O  
ATOM   4163  CB  THR A 554      47.086  46.288  16.084  1.00119.00           C  
ANISOU 4163  CB  THR A 554    19257  12827  13131  -1614   -638   -817       C  
ATOM   4164  OG1 THR A 554      46.517  45.370  15.142  1.00119.83           O  
ANISOU 4164  OG1 THR A 554    19021  12967  13541  -1385   -614   -727       O  
ATOM   4165  CG2 THR A 554      45.973  47.074  16.763  1.00120.19           C  
ANISOU 4165  CG2 THR A 554    19628  12943  13095  -1577   -306  -1072       C  
ATOM   4166  N   TRP A 555      50.363  46.492  15.392  1.00116.29           N  
ANISOU 4166  N   TRP A 555    18860  12422  12903  -1916  -1335   -491       N  
ATOM   4167  CA  TRP A 555      51.565  45.866  14.857  1.00115.30           C  
ANISOU 4167  CA  TRP A 555    18508  12323  12979  -1975  -1624   -285       C  
ATOM   4168  C   TRP A 555      51.626  44.393  15.241  1.00115.40           C  
ANISOU 4168  C   TRP A 555    18316  12438  13093  -2047  -1753    -83       C  
ATOM   4169  O   TRP A 555      51.500  44.042  16.419  1.00116.39           O  
ANISOU 4169  O   TRP A 555    18604  12627  12992  -2263  -1789     -2       O  
ATOM   4170  CB  TRP A 555      52.814  46.592  15.361  1.00115.55           C  
ANISOU 4170  CB  TRP A 555    18755  12310  12839  -2232  -1849   -216       C  
ATOM   4171  CG  TRP A 555      53.031  47.933  14.729  1.00115.14           C  
ANISOU 4171  CG  TRP A 555    18827  12144  12777  -2160  -1810   -362       C  
ATOM   4172  CD1 TRP A 555      52.619  49.140  15.208  1.00116.53           C  
ANISOU 4172  CD1 TRP A 555    19331  12219  12726  -2196  -1672   -556       C  
ATOM   4173  CD2 TRP A 555      53.736  48.205  13.510  1.00114.04           C  
ANISOU 4173  CD2 TRP A 555    18480  11979  12871  -2060  -1924   -323       C  
ATOM   4174  NE1 TRP A 555      53.009  50.145  14.356  1.00115.84           N  
ANISOU 4174  NE1 TRP A 555    19250  12027  12738  -2120  -1720   -618       N  
ATOM   4175  CE2 TRP A 555      53.698  49.595  13.307  1.00113.97           C  
ANISOU 4175  CE2 TRP A 555    18690  11851  12762  -2049  -1873   -468       C  
ATOM   4176  CE3 TRP A 555      54.389  47.405  12.568  1.00113.37           C  
ANISOU 4176  CE3 TRP A 555    18041  11963  13073  -1989  -2056   -193       C  
ATOM   4177  CZ2 TRP A 555      54.287  50.203  12.205  1.00113.06           C  
ANISOU 4177  CZ2 TRP A 555    18453  11703  12802  -1991  -1971   -453       C  
ATOM   4178  CZ3 TRP A 555      54.974  48.013  11.475  1.00112.80           C  
ANISOU 4178  CZ3 TRP A 555    17850  11874  13134  -1931  -2117   -208       C  
ATOM   4179  CH2 TRP A 555      54.920  49.396  11.304  1.00112.52           C  
ANISOU 4179  CH2 TRP A 555    18041  11738  12972  -1943  -2085   -320       C  
ATOM   4180  N   LEU A 556      51.818  43.537  14.241  1.00127.66           N  
ANISOU 4180  N   LEU A 556    19512  14004  14988  -1882  -1828     -4       N  
ATOM   4181  CA  LEU A 556      52.057  42.115  14.450  1.00127.66           C  
ANISOU 4181  CA  LEU A 556    19269  14061  15176  -1936  -2002    196       C  
ATOM   4182  C   LEU A 556      53.554  41.850  14.395  1.00127.03           C  
ANISOU 4182  C   LEU A 556    19061  13954  15253  -2093  -2315    370       C  
ATOM   4183  O   LEU A 556      54.232  42.288  13.460  1.00127.02           O  
ANISOU 4183  O   LEU A 556    18939  13917  15405  -2006  -2349    318       O  
ATOM   4184  CB  LEU A 556      51.338  41.271  13.397  1.00127.70           C  
ANISOU 4184  CB  LEU A 556    18949  14080  15491  -1660  -1892    156       C  
ATOM   4185  CG  LEU A 556      49.811  41.274  13.435  1.00128.74           C  
ANISOU 4185  CG  LEU A 556    19136  14241  15538  -1501  -1610     36       C  
ATOM   4186  CD1 LEU A 556      49.252  40.497  12.254  1.00128.21           C  
ANISOU 4186  CD1 LEU A 556    18747  14177  15792  -1246  -1541     10       C  
ATOM   4187  CD2 LEU A 556      49.312  40.700  14.750  1.00129.94           C  
ANISOU 4187  CD2 LEU A 556    19420  14471  15481  -1683  -1619    145       C  
ATOM   4188  N   HIS A 557      54.062  41.135  15.396  1.00139.19           N  
ANISOU 4188  N   HIS A 557    20614  15514  16760  -2340  -2549    591       N  
ATOM   4189  CA  HIS A 557      55.477  40.809  15.475  1.00138.75           C  
ANISOU 4189  CA  HIS A 557    20416  15414  16889  -2510  -2873    793       C  
ATOM   4190  C   HIS A 557      55.768  39.340  15.215  1.00138.37           C  
ANISOU 4190  C   HIS A 557    19974  15345  17254  -2461  -3060    961       C  
ATOM   4191  O   HIS A 557      56.937  38.975  15.058  1.00137.01           O  
ANISOU 4191  O   HIS A 557    19592  15115  17349  -2542  -3311   1107       O  
ATOM   4192  CB  HIS A 557      56.031  41.194  16.853  1.00139.15           C  
ANISOU 4192  CB  HIS A 557    20784  15472  16613  -2885  -3068    956       C  
ATOM   4193  CG  HIS A 557      55.952  42.660  17.145  1.00139.65           C  
ANISOU 4193  CG  HIS A 557    21238  15525  16298  -2961  -2926    786       C  
ATOM   4194  ND1 HIS A 557      54.848  43.243  17.729  1.00140.36           N  
ANISOU 4194  ND1 HIS A 557    21633  15657  16042  -2967  -2664    606       N  
ATOM   4195  CD2 HIS A 557      56.837  43.662  16.932  1.00139.04           C  
ANISOU 4195  CD2 HIS A 557    21284  15389  16155  -3035  -3012    760       C  
ATOM   4196  CE1 HIS A 557      55.057  44.540  17.865  1.00139.82           C  
ANISOU 4196  CE1 HIS A 557    21862  15536  15728  -3033  -2596    462       C  
ATOM   4197  NE2 HIS A 557      56.257  44.820  17.389  1.00138.94           N  
ANISOU 4197  NE2 HIS A 557    21656  15365  15771  -3080  -2817    564       N  
ATOM   4198  N   TYR A 558      54.737  38.496  15.159  1.00160.53           N  
ANISOU 4198  N   TYR A 558    22664  18186  20146  -2328  -2948    943       N  
ATOM   4199  CA  TYR A 558      54.920  37.058  15.004  1.00160.14           C  
ANISOU 4199  CA  TYR A 558    22254  18094  20496  -2291  -3140   1103       C  
ATOM   4200  C   TYR A 558      55.474  36.678  13.636  1.00158.37           C  
ANISOU 4200  C   TYR A 558    21658  17809  20708  -2049  -3135    996       C  
ATOM   4201  O   TYR A 558      55.950  35.550  13.469  1.00154.82           O  
ANISOU 4201  O   TYR A 558    20880  17287  20658  -2031  -3334   1116       O  
ATOM   4202  CB  TYR A 558      53.580  36.360  15.260  1.00161.10           C  
ANISOU 4202  CB  TYR A 558    22373  18274  20564  -2209  -3003   1098       C  
ATOM   4203  CG  TYR A 558      53.602  34.847  15.227  1.00161.18           C  
ANISOU 4203  CG  TYR A 558    22044  18230  20969  -2188  -3216   1275       C  
ATOM   4204  CD1 TYR A 558      54.151  34.115  16.273  1.00160.95           C  
ANISOU 4204  CD1 TYR A 558    21984  18170  21001  -2478  -3555   1578       C  
ATOM   4205  CD2 TYR A 558      53.039  34.150  14.165  1.00161.22           C  
ANISOU 4205  CD2 TYR A 558    21765  18204  21286  -1897  -3094   1149       C  
ATOM   4206  CE1 TYR A 558      54.161  32.728  16.249  1.00160.12           C  
ANISOU 4206  CE1 TYR A 558    21554  17986  21299  -2461  -3779   1752       C  
ATOM   4207  CE2 TYR A 558      53.043  32.766  14.132  1.00160.42           C  
ANISOU 4207  CE2 TYR A 558    21356  18029  21568  -1873  -3298   1297       C  
ATOM   4208  CZ  TYR A 558      53.604  32.060  15.176  1.00159.48           C  
ANISOU 4208  CZ  TYR A 558    21193  17860  21540  -2147  -3644   1598       C  
ATOM   4209  OH  TYR A 558      53.607  30.683  15.143  1.00156.49           O  
ANISOU 4209  OH  TYR A 558    20494  17379  21585  -2125  -3875   1755       O  
ATOM   4210  N   LEU A 559      55.440  37.587  12.663  1.00146.36           N  
ANISOU 4210  N   LEU A 559    20171  16314  19124  -1880  -2920    773       N  
ATOM   4211  CA  LEU A 559      55.776  37.263  11.277  1.00144.63           C  
ANISOU 4211  CA  LEU A 559    19617  16080  19253  -1660  -2853    630       C  
ATOM   4212  C   LEU A 559      56.693  38.330  10.679  1.00144.74           C  
ANISOU 4212  C   LEU A 559    19672  16113  19208  -1685  -2836    542       C  
ATOM   4213  O   LEU A 559      56.481  38.815   9.567  1.00145.27           O  
ANISOU 4213  O   LEU A 559    19681  16230  19286  -1522  -2643    350       O  
ATOM   4214  CB  LEU A 559      54.503  37.113  10.445  1.00145.23           C  
ANISOU 4214  CB  LEU A 559    19648  16201  19332  -1409  -2579    441       C  
ATOM   4215  CG  LEU A 559      53.507  36.039  10.895  1.00146.52           C  
ANISOU 4215  CG  LEU A 559    19747  16356  19568  -1362  -2581    522       C  
ATOM   4216  CD1 LEU A 559      52.249  36.083  10.042  1.00148.26           C  
ANISOU 4216  CD1 LEU A 559    19951  16619  19762  -1127  -2305    343       C  
ATOM   4217  CD2 LEU A 559      54.136  34.657  10.874  1.00144.30           C  
ANISOU 4217  CD2 LEU A 559    19115  15990  19723  -1373  -2826    654       C  
ATOM   4218  N   CYS A 560      57.739  38.705  11.415  1.00141.98           N  
ANISOU 4218  N   CYS A 560    19422  15731  18793  -1916  -3058    705       N  
ATOM   4219  CA  CYS A 560      58.642  39.773  11.007  1.00141.31           C  
ANISOU 4219  CA  CYS A 560    19407  15665  18620  -1982  -3075    662       C  
ATOM   4220  C   CYS A 560      60.046  39.225  10.795  1.00139.51           C  
ANISOU 4220  C   CYS A 560    18853  15394  18760  -2060  -3311    788       C  
ATOM   4221  O   CYS A 560      60.534  38.418  11.593  1.00140.03           O  
ANISOU 4221  O   CYS A 560    18813  15382  19011  -2201  -3561   1004       O  
ATOM   4222  CB  CYS A 560      58.664  40.889  12.051  1.00142.20           C  
ANISOU 4222  CB  CYS A 560    19955  15770  18303  -2202  -3124    732       C  
ATOM   4223  SG  CYS A 560      57.070  41.710  12.252  1.00144.67           S  
ANISOU 4223  SG  CYS A 560    20633  16115  18219  -2096  -2811    537       S  
ATOM   4224  N   THR A 561      60.699  39.671   9.724  1.00133.64           N  
ANISOU 4224  N   THR A 561    17940  14702  18134  -1982  -3237    663       N  
ATOM   4225  CA  THR A 561      61.995  39.143   9.335  1.00132.51           C  
ANISOU 4225  CA  THR A 561    17429  14533  18385  -2018  -3402    732       C  
ATOM   4226  C   THR A 561      63.115  40.114   9.712  1.00132.80           C  
ANISOU 4226  C   THR A 561    17603  14571  18283  -2240  -3577    875       C  
ATOM   4227  O   THR A 561      62.893  41.139  10.364  1.00133.60           O  
ANISOU 4227  O   THR A 561    18103  14677  17981  -2379  -3593    925       O  
ATOM   4228  CB  THR A 561      62.017  38.839   7.835  1.00131.81           C  
ANISOU 4228  CB  THR A 561    17007  14529  18547  -1800  -3189    485       C  
ATOM   4229  OG1 THR A 561      61.906  40.061   7.097  1.00132.56           O  
ANISOU 4229  OG1 THR A 561    17274  14741  18351  -1788  -3016    345       O  
ATOM   4230  CG2 THR A 561      60.860  37.925   7.462  1.00131.79           C  
ANISOU 4230  CG2 THR A 561    16900  14518  18656  -1594  -3026    349       C  
ATOM   4231  N   GLY A 562      64.337  39.779   9.301  1.00135.38           N  
ANISOU 4231  N   GLY A 562    17587  14887  18964  -2275  -3708    934       N  
ATOM   4232  CA  GLY A 562      65.507  40.619   9.490  1.00135.85           C  
ANISOU 4232  CA  GLY A 562    17702  14956  18958  -2475  -3880   1076       C  
ATOM   4233  C   GLY A 562      66.392  40.563   8.262  1.00136.10           C  
ANISOU 4233  C   GLY A 562    17340  15077  19295  -2386  -3794    948       C  
ATOM   4234  O   GLY A 562      65.879  40.406   7.150  1.00137.22           O  
ANISOU 4234  O   GLY A 562    17327  15322  19488  -2187  -3530    691       O  
ATOM   4235  N   GLU A 563      67.711  40.680   8.423  1.00145.70           N  
ANISOU 4235  N   GLU A 563    18380  16268  20711  -2544  -4006   1121       N  
ATOM   4236  CA  GLU A 563      68.623  40.542   7.290  1.00145.29           C  
ANISOU 4236  CA  GLU A 563    17906  16314  20982  -2472  -3914    994       C  
ATOM   4237  C   GLU A 563      69.670  39.475   7.589  1.00145.10           C  
ANISOU 4237  C   GLU A 563    17448  16158  21525  -2507  -4135   1150       C  
ATOM   4238  O   GLU A 563      70.568  39.680   8.414  1.00145.85           O  
ANISOU 4238  O   GLU A 563    17570  16162  21686  -2723  -4432   1439       O  
ATOM   4239  CB  GLU A 563      69.281  41.869   6.921  1.00145.12           C  
ANISOU 4239  CB  GLU A 563    18031  16422  20686  -2615  -3915   1021       C  
ATOM   4240  CG  GLU A 563      70.104  41.768   5.642  1.00145.31           C  
ANISOU 4240  CG  GLU A 563    17624  16602  20986  -2550  -3764    856       C  
ATOM   4241  CD  GLU A 563      69.265  41.361   4.434  1.00145.71           C  
ANISOU 4241  CD  GLU A 563    17518  16784  21059  -2323  -3422    515       C  
ATOM   4242  OE1 GLU A 563      68.043  41.620   4.426  1.00146.66           O  
ANISOU 4242  OE1 GLU A 563    17942  16912  20868  -2238  -3290    417       O  
ATOM   4243  OE2 GLU A 563      69.829  40.773   3.488  1.00145.10           O  
ANISOU 4243  OE2 GLU A 563    17008  16804  21319  -2240  -3281    340       O  
ATOM   4244  N   VAL A 564      69.537  38.348   6.892  1.00167.84           N  
ANISOU 4244  N   VAL A 564    19925  19017  24829  -2297  -3995    954       N  
ATOM   4245  CA  VAL A 564      70.390  37.162   6.903  1.00164.80           C  
ANISOU 4245  CA  VAL A 564    19033  18487  25094  -2253  -4139   1009       C  
ATOM   4246  C   VAL A 564      71.728  37.442   6.224  1.00165.19           C  
ANISOU 4246  C   VAL A 564    18728  18621  25414  -2303  -4125    979       C  
ATOM   4247  O   VAL A 564      72.028  38.590   5.877  1.00166.34           O  
ANISOU 4247  O   VAL A 564    19058  18938  25205  -2410  -4053    972       O  
ATOM   4248  CB  VAL A 564      69.664  35.984   6.233  1.00162.63           C  
ANISOU 4248  CB  VAL A 564    18482  18175  25134  -1992  -3937    736       C  
ATOM   4249  CG1 VAL A 564      68.348  35.713   6.948  1.00162.01           C  
ANISOU 4249  CG1 VAL A 564    18745  18022  24788  -1959  -3965    798       C  
ATOM   4250  CG2 VAL A 564      69.425  36.271   4.761  1.00164.00           C  
ANISOU 4250  CG2 VAL A 564    18537  18572  25202  -1835  -3551    355       C  
ATOM   4251  N   LYS A 565      72.561  36.400   6.094  1.00187.63           N  
ANISOU 4251  N   LYS A 565    21052  21332  28907  -2239  -4216    983       N  
ATOM   4252  CA  LYS A 565      73.812  36.465   5.336  1.00187.84           C  
ANISOU 4252  CA  LYS A 565    20643  21442  29287  -2248  -4150    899       C  
ATOM   4253  C   LYS A 565      74.917  37.248   6.046  1.00188.38           C  
ANISOU 4253  C   LYS A 565    20782  21482  29312  -2514  -4451   1258       C  
ATOM   4254  O   LYS A 565      75.234  38.387   5.691  1.00190.38           O  
ANISOU 4254  O   LYS A 565    21218  21931  29187  -2632  -4375   1259       O  
ATOM   4255  CB  LYS A 565      73.519  37.026   3.930  1.00188.44           C  
ANISOU 4255  CB  LYS A 565    20704  21814  29081  -2140  -3734    518       C  
ATOM   4256  CG  LYS A 565      74.674  37.107   2.930  1.00188.70           C  
ANISOU 4256  CG  LYS A 565    20281  22008  29408  -2145  -3570    349       C  
ATOM   4257  CD  LYS A 565      75.117  38.555   2.714  1.00190.70           C  
ANISOU 4257  CD  LYS A 565    20787  22488  29180  -2350  -3563    455       C  
ATOM   4258  CE  LYS A 565      76.162  38.678   1.619  1.00191.44           C  
ANISOU 4258  CE  LYS A 565    20439  22801  29499  -2370  -3356    264       C  
ATOM   4259  NZ  LYS A 565      75.593  38.345   0.283  1.00193.13           N  
ANISOU 4259  NZ  LYS A 565    20487  23230  29664  -2210  -2937   -187       N  
ATOM   4260  N   MET A 566      75.449  36.645   7.115  1.00196.75           N  
ANISOU 4260  N   MET A 566    21725  22289  30742  -2634  -4828   1594       N  
ATOM   4261  CA  MET A 566      76.703  37.051   7.747  1.00195.34           C  
ANISOU 4261  CA  MET A 566    21455  22034  30732  -2880  -5155   1953       C  
ATOM   4262  C   MET A 566      77.803  37.363   6.737  1.00196.84           C  
ANISOU 4262  C   MET A 566    21233  22382  31174  -2855  -4986   1809       C  
ATOM   4263  O   MET A 566      77.848  36.774   5.652  1.00197.36           O  
ANISOU 4263  O   MET A 566    20891  22533  31562  -2634  -4673   1448       O  
ATOM   4264  CB  MET A 566      77.204  35.942   8.681  1.00192.34           C  
ANISOU 4264  CB  MET A 566    20780  21338  30963  -2947  -5539   2259       C  
ATOM   4265  CG  MET A 566      76.456  35.789   9.989  1.00190.68           C  
ANISOU 4265  CG  MET A 566    20995  20973  30482  -3111  -5837   2557       C  
ATOM   4266  SD  MET A 566      76.764  37.178  11.092  1.00190.31           S  
ANISOU 4266  SD  MET A 566    21536  20977  29796  -3509  -6136   2954       S  
ATOM   4267  CE  MET A 566      78.488  36.900  11.501  1.00189.59           C  
ANISOU 4267  CE  MET A 566    20974  20703  30357  -3719  -6546   3348       C  
ATOM   4268  N   ASN A 567      78.693  38.288   7.090  1.00195.92           N  
ANISOU 4268  N   ASN A 567    21222  22316  30903  -3099  -5189   2086       N  
ATOM   4269  CA  ASN A 567      79.866  38.594   6.274  1.00197.79           C  
ANISOU 4269  CA  ASN A 567    21047  22700  31405  -3122  -5083   2021       C  
ATOM   4270  C   ASN A 567      81.113  37.941   6.871  1.00196.59           C  
ANISOU 4270  C   ASN A 567    20435  22310  31950  -3225  -5424   2337       C  
ATOM   4271  O   ASN A 567      81.978  38.619   7.428  1.00196.91           O  
ANISOU 4271  O   ASN A 567    20549  22331  31937  -3479  -5710   2689       O  
ATOM   4272  CB  ASN A 567      80.062  40.108   6.157  1.00198.89           C  
ANISOU 4272  CB  ASN A 567    21580  23066  30924  -3329  -5079   2121       C  
ATOM   4273  CG  ASN A 567      81.145  40.488   5.161  1.00200.64           C  
ANISOU 4273  CG  ASN A 567    21393  23505  31335  -3356  -4913   2016       C  
ATOM   4274  OD1 ASN A 567      81.775  39.628   4.545  1.00201.34           O  
ANISOU 4274  OD1 ASN A 567    20891  23584  32025  -3214  -4770   1841       O  
ATOM   4275  ND2 ASN A 567      81.369  41.788   5.005  1.00201.10           N  
ANISOU 4275  ND2 ASN A 567    21759  23761  30890  -3546  -4930   2117       N  
ATOM   4276  N   LEU A 569      81.183  35.434   4.224  1.00181.89           N  
ANISOU 4276  N   LEU A 569    17210  20502  31397  -2512  -4569   1262       N  
ATOM   4277  CA  LEU A 569      80.914  34.221   4.988  1.00181.35           C  
ANISOU 4277  CA  LEU A 569    16982  20073  31850  -2417  -4823   1388       C  
ATOM   4278  C   LEU A 569      79.640  34.361   5.815  1.00179.32           C  
ANISOU 4278  C   LEU A 569    17338  19751  31046  -2467  -4971   1540       C  
ATOM   4279  O   LEU A 569      79.694  34.502   7.037  1.00178.89           O  
ANISOU 4279  O   LEU A 569    17550  19518  30904  -2678  -5383   1976       O  
ATOM   4280  CB  LEU A 569      82.098  33.888   5.899  1.00184.79           C  
ANISOU 4280  CB  LEU A 569    17090  20225  32895  -2581  -5275   1832       C  
ATOM   4281  CG  LEU A 569      83.403  33.488   5.207  1.00188.92           C  
ANISOU 4281  CG  LEU A 569    16894  20732  34154  -2504  -5166   1702       C  
ATOM   4282  CD1 LEU A 569      84.524  33.330   6.222  1.00192.39           C  
ANISOU 4282  CD1 LEU A 569    17084  20888  35127  -2713  -5672   2226       C  
ATOM   4283  CD2 LEU A 569      83.218  32.208   4.406  1.00190.60           C  
ANISOU 4283  CD2 LEU A 569    16583  20833  35005  -2182  -4877   1245       C  
ATOM   4284  N   LYS A 571      78.205  34.653   1.319  1.00203.91           N  
ANISOU 4284  N   LYS A 571    20183  23791  33503  -1912  -3360    -95       N  
ATOM   4285  CA  LYS A 571      77.667  34.564  -0.036  1.00205.74           C  
ANISOU 4285  CA  LYS A 571    20331  24290  33548  -1776  -2891   -593       C  
ATOM   4286  C   LYS A 571      76.852  33.289  -0.312  1.00205.30           C  
ANISOU 4286  C   LYS A 571    20111  24068  33826  -1524  -2750   -898       C  
ATOM   4287  O   LYS A 571      75.751  33.385  -0.853  1.00205.67           O  
ANISOU 4287  O   LYS A 571    20444  24258  33445  -1453  -2524  -1125       O  
ATOM   4288  CB  LYS A 571      78.795  34.682  -1.069  1.00207.13           C  
ANISOU 4288  CB  LYS A 571    20018  24700  33982  -1806  -2621   -845       C  
ATOM   4289  CG  LYS A 571      79.416  36.063  -1.172  1.00209.48           C  
ANISOU 4289  CG  LYS A 571    20512  25269  33813  -2059  -2656   -638       C  
ATOM   4290  CD  LYS A 571      80.469  36.103  -2.270  1.00211.34           C  
ANISOU 4290  CD  LYS A 571    20235  25771  34295  -2093  -2349   -919       C  
ATOM   4291  CE  LYS A 571      81.097  37.480  -2.390  1.00212.89           C  
ANISOU 4291  CE  LYS A 571    20615  26246  34026  -2363  -2405   -690       C  
ATOM   4292  NZ  LYS A 571      82.129  37.524  -3.464  1.00213.99           N  
ANISOU 4292  NZ  LYS A 571    20241  26679  34385  -2421  -2093   -957       N  
ATOM   4293  N   PRO A 572      77.380  32.095   0.040  1.00206.90           N  
ANISOU 4293  N   PRO A 572    19846  23956  34812  -1395  -2897   -896       N  
ATOM   4294  CA  PRO A 572      76.601  30.895  -0.298  1.00206.09           C  
ANISOU 4294  CA  PRO A 572    19583  23694  35028  -1158  -2759  -1209       C  
ATOM   4295  C   PRO A 572      75.246  30.827   0.404  1.00207.52           C  
ANISOU 4295  C   PRO A 572    20276  23763  34809  -1135  -2923  -1033       C  
ATOM   4296  O   PRO A 572      74.228  30.759  -0.284  1.00206.77           O  
ANISOU 4296  O   PRO A 572    20374  23811  34377  -1034  -2652  -1323       O  
ATOM   4297  CB  PRO A 572      77.500  29.746   0.172  1.00204.32           C  
ANISOU 4297  CB  PRO A 572    18786  23100  35747  -1060  -2989  -1135       C  
ATOM   4298  CG  PRO A 572      78.869  30.320   0.208  1.00203.95           C  
ANISOU 4298  CG  PRO A 572    18459  23126  35906  -1208  -3058   -973       C  
ATOM   4299  CD  PRO A 572      78.680  31.738   0.639  1.00205.50           C  
ANISOU 4299  CD  PRO A 572    19228  23549  35304  -1449  -3177   -645       C  
ATOM   4300  N   VAL A 574      73.321  29.047   4.270  1.00194.74           N  
ANISOU 4300  N   VAL A 574    19295  21224  33475  -1206  -4124     62       N  
ATOM   4301  CA  VAL A 574      72.026  28.819   4.900  1.00191.56           C  
ANISOU 4301  CA  VAL A 574    19294  20760  32728  -1202  -4230    191       C  
ATOM   4302  C   VAL A 574      71.433  30.155   5.338  1.00191.72           C  
ANISOU 4302  C   VAL A 574    19939  21012  31892  -1381  -4208    371       C  
ATOM   4303  O   VAL A 574      70.450  30.622   4.758  1.00192.76           O  
ANISOU 4303  O   VAL A 574    20377  21352  31512  -1302  -3916    146       O  
ATOM   4304  CB  VAL A 574      72.148  27.848   6.083  1.00188.17           C  
ANISOU 4304  CB  VAL A 574    18725  19976  32796  -1276  -4698    568       C  
ATOM   4305  CG1 VAL A 574      70.796  27.652   6.752  1.00185.33           C  
ANISOU 4305  CG1 VAL A 574    18789  19593  32035  -1300  -4795    710       C  
ATOM   4306  CG2 VAL A 574      72.726  26.519   5.619  1.00186.86           C  
ANISOU 4306  CG2 VAL A 574    17915  19541  33543  -1081  -4728    371       C  
ATOM   4307  N   ALA A 575      72.037  30.765   6.362  1.00179.23           N  
ANISOU 4307  N   ALA A 575    18538  19380  30181  -1628  -4528    778       N  
ATOM   4308  CA  ALA A 575      71.726  32.134   6.773  1.00178.75           C  
ANISOU 4308  CA  ALA A 575    19030  19522  29364  -1817  -4517    935       C  
ATOM   4309  C   ALA A 575      70.244  32.282   7.138  1.00178.45           C  
ANISOU 4309  C   ALA A 575    19472  19541  28789  -1793  -4443    928       C  
ATOM   4310  O   ALA A 575      69.449  32.876   6.410  1.00178.26           O  
ANISOU 4310  O   ALA A 575    19688  19726  28318  -1693  -4120    669       O  
ATOM   4311  CB  ALA A 575      72.133  33.132   5.681  1.00180.41           C  
ANISOU 4311  CB  ALA A 575    19238  20013  29295  -1795  -4191    674       C  
ATOM   4312  N   MET A 576      69.877  31.664   8.257  1.00156.63           N  
ANISOU 4312  N   MET A 576    16811  16583  26116  -1893  -4754   1222       N  
ATOM   4313  CA  MET A 576      68.528  31.792   8.807  1.00156.71           C  
ANISOU 4313  CA  MET A 576    17273  16642  25627  -1911  -4722   1271       C  
ATOM   4314  C   MET A 576      68.600  32.668  10.059  1.00158.24           C  
ANISOU 4314  C   MET A 576    17917  16855  25351  -2220  -4973   1633       C  
ATOM   4315  O   MET A 576      68.844  32.180  11.164  1.00157.00           O  
ANISOU 4315  O   MET A 576    17766  16531  25358  -2420  -5342   1982       O  
ATOM   4316  CB  MET A 576      67.922  30.422   9.115  1.00155.68           C  
ANISOU 4316  CB  MET A 576    16948  16312  25892  -1812  -4861   1314       C  
ATOM   4317  CG  MET A 576      66.439  30.456   9.489  1.00156.02           C  
ANISOU 4317  CG  MET A 576    17397  16431  25451  -1792  -4764   1308       C  
ATOM   4318  SD  MET A 576      66.079  30.839  11.217  1.00157.01           S  
ANISOU 4318  SD  MET A 576    17997  16531  25127  -2138  -5102   1766       S  
ATOM   4319  CE  MET A 576      66.595  29.321  12.015  1.00155.50           C  
ANISOU 4319  CE  MET A 576    17403  16028  25651  -2243  -5577   2099       C  
ATOM   4320  N   VAL A 577      68.414  33.977   9.871  1.00152.52           N  
ANISOU 4320  N   VAL A 577    17569  16331  24048  -2278  -4784   1550       N  
ATOM   4321  CA  VAL A 577      68.178  34.898  10.981  1.00152.97           C  
ANISOU 4321  CA  VAL A 577    18139  16430  23553  -2543  -4938   1802       C  
ATOM   4322  C   VAL A 577      67.168  35.965  10.568  1.00153.57           C  
ANISOU 4322  C   VAL A 577    18637  16704  23010  -2461  -4606   1567       C  
ATOM   4323  O   VAL A 577      67.487  36.899   9.823  1.00154.17           O  
ANISOU 4323  O   VAL A 577    18764  16916  22899  -2429  -4426   1411       O  
ATOM   4324  CB  VAL A 577      69.498  35.515  11.496  1.00154.10           C  
ANISOU 4324  CB  VAL A 577    18276  16534  23741  -2803  -5214   2075       C  
ATOM   4325  CG1 VAL A 577      70.287  36.194  10.379  1.00154.23           C  
ANISOU 4325  CG1 VAL A 577    18097  16680  23821  -2709  -5012   1870       C  
ATOM   4326  CG2 VAL A 577      69.212  36.501  12.623  1.00154.77           C  
ANISOU 4326  CG2 VAL A 577    18926  16665  23215  -3090  -5354   2296       C  
ATOM   4327  N   THR A 578      65.926  35.814  11.022  1.00145.92           N  
ANISOU 4327  N   THR A 578    17949  15748  21747  -2430  -4527   1546       N  
ATOM   4328  CA  THR A 578      64.878  36.793  10.765  1.00149.22           C  
ANISOU 4328  CA  THR A 578    18765  16317  21615  -2359  -4236   1350       C  
ATOM   4329  C   THR A 578      64.245  37.323  12.041  1.00149.97           C  
ANISOU 4329  C   THR A 578    19341  16412  21228  -2572  -4334   1528       C  
ATOM   4330  O   THR A 578      64.139  38.542  12.222  1.00151.34           O  
ANISOU 4330  O   THR A 578    19880  16665  20958  -2669  -4253   1493       O  
ATOM   4331  CB  THR A 578      63.801  36.172   9.865  1.00150.77           C  
ANISOU 4331  CB  THR A 578    18825  16558  21901  -2070  -3950   1074       C  
ATOM   4332  OG1 THR A 578      63.208  35.052  10.533  1.00151.24           O  
ANISOU 4332  OG1 THR A 578    18818  16506  22140  -2065  -4085   1200       O  
ATOM   4333  CG2 THR A 578      64.409  35.710   8.548  1.00150.42           C  
ANISOU 4333  CG2 THR A 578    18331  16540  22283  -1880  -3813    848       C  
ATOM   4334  N   THR A 579      63.814  36.435  12.926  1.00170.85           N  
ANISOU 4334  N   THR A 579    21993  18973  23951  -2661  -4507   1709       N  
ATOM   4335  CA  THR A 579      63.240  36.784  14.217  1.00172.81           C  
ANISOU 4335  CA  THR A 579    22670  19238  23751  -2906  -4608   1885       C  
ATOM   4336  C   THR A 579      64.354  36.787  15.267  1.00172.33           C  
ANISOU 4336  C   THR A 579    22645  19087  23744  -3258  -5010   2241       C  
ATOM   4337  O   THR A 579      65.537  36.888  14.931  1.00171.50           O  
ANISOU 4337  O   THR A 579    22307  18926  23931  -3296  -5159   2320       O  
ATOM   4338  CB  THR A 579      62.097  35.822  14.563  1.00173.09           C  
ANISOU 4338  CB  THR A 579    22693  19265  23808  -2835  -4567   1894       C  
ATOM   4339  OG1 THR A 579      62.593  34.478  14.598  1.00170.60           O  
ANISOU 4339  OG1 THR A 579    21958  18807  24055  -2829  -4826   2066       O  
ATOM   4340  CG2 THR A 579      60.981  35.920  13.536  1.00174.25           C  
ANISOU 4340  CG2 THR A 579    22833  19500  23874  -2508  -4178   1561       C  
ATOM   4341  N   TYR A 580      63.978  36.721  16.547  1.00191.50           N  
ANISOU 4341  N   TYR A 580    25375  21516  25870  -3540  -5185   2463       N  
ATOM   4342  CA  TYR A 580      64.912  36.472  17.641  1.00189.71           C  
ANISOU 4342  CA  TYR A 580    25165  21197  25721  -3918  -5619   2856       C  
ATOM   4343  C   TYR A 580      65.885  37.635  17.788  1.00189.78           C  
ANISOU 4343  C   TYR A 580    25375  21218  25514  -4108  -5711   2920       C  
ATOM   4344  O   TYR A 580      67.098  37.469  17.627  1.00188.61           O  
ANISOU 4344  O   TYR A 580    24943  20970  25749  -4182  -5957   3098       O  
ATOM   4345  CB  TYR A 580      65.679  35.168  17.393  1.00187.96           C  
ANISOU 4345  CB  TYR A 580    24397  20803  26217  -3868  -5899   3044       C  
ATOM   4346  CG  TYR A 580      64.798  33.959  17.145  1.00187.96           C  
ANISOU 4346  CG  TYR A 580    24153  20761  26502  -3663  -5834   2977       C  
ATOM   4347  CD1 TYR A 580      63.465  33.943  17.537  1.00189.71           C  
ANISOU 4347  CD1 TYR A 580    24670  21097  26314  -3652  -5647   2890       C  
ATOM   4348  CD2 TYR A 580      65.292  32.851  16.470  1.00186.15           C  
ANISOU 4348  CD2 TYR A 580    23386  20374  26967  -3469  -5943   2978       C  
ATOM   4349  CE1 TYR A 580      62.660  32.851  17.286  1.00189.06           C  
ANISOU 4349  CE1 TYR A 580    24365  20978  26493  -3470  -5600   2842       C  
ATOM   4350  CE2 TYR A 580      64.493  31.753  16.217  1.00185.51           C  
ANISOU 4350  CE2 TYR A 580    23089  20239  27158  -3283  -5897   2909       C  
ATOM   4351  CZ  TYR A 580      63.178  31.757  16.630  1.00186.91           C  
ANISOU 4351  CZ  TYR A 580    23577  20536  26903  -3290  -5737   2857       C  
ATOM   4352  OH  TYR A 580      62.377  30.665  16.382  1.00186.54           O  
ANISOU 4352  OH  TYR A 580    23317  20435  27123  -3116  -5708   2809       O  
ATOM   4353  N   GLN A 581      65.350  38.818  18.092  1.00180.29           N  
ANISOU 4353  N   GLN A 581    24653  20127  23720  -4185  -5515   2774       N  
ATOM   4354  CA  GLN A 581      66.108  40.068  18.050  1.00180.43           C  
ANISOU 4354  CA  GLN A 581    24894  20163  23497  -4311  -5540   2764       C  
ATOM   4355  C   GLN A 581      66.826  40.265  19.384  1.00179.70           C  
ANISOU 4355  C   GLN A 581    25058  20023  23196  -4782  -5927   3124       C  
ATOM   4356  O   GLN A 581      66.362  40.971  20.281  1.00180.31           O  
ANISOU 4356  O   GLN A 581    25617  20164  22729  -5022  -5901   3119       O  
ATOM   4357  CB  GLN A 581      65.177  41.234  17.742  1.00182.72           C  
ANISOU 4357  CB  GLN A 581    25567  20561  23298  -4171  -5167   2430       C  
ATOM   4358  CG  GLN A 581      64.403  41.096  16.436  1.00183.40           C  
ANISOU 4358  CG  GLN A 581    25431  20700  23552  -3744  -4800   2098       C  
ATOM   4359  CD  GLN A 581      63.131  40.275  16.593  1.00183.05           C  
ANISOU 4359  CD  GLN A 581    25375  20688  23488  -3605  -4633   2006       C  
ATOM   4360  OE1 GLN A 581      62.651  40.058  17.707  1.00183.06           O  
ANISOU 4360  OE1 GLN A 581    25620  20705  23229  -3827  -4723   2139       O  
ATOM   4361  NE2 GLN A 581      62.578  39.818  15.476  1.00182.40           N  
ANISOU 4361  NE2 GLN A 581    25012  20630  23664  -3260  -4392   1785       N  
ATOM   4362  N   MET A 582      67.990  39.626  19.512  1.00190.79           N  
ANISOU 4362  N   MET A 582    26126  21309  25056  -4928  -6294   3438       N  
ATOM   4363  CA  MET A 582      68.788  39.725  20.728  1.00189.99           C  
ANISOU 4363  CA  MET A 582    26215  21146  24826  -5402  -6719   3836       C  
ATOM   4364  C   MET A 582      70.120  40.425  20.481  1.00188.96           C  
ANISOU 4364  C   MET A 582    26008  20957  24831  -5514  -6912   3974       C  
ATOM   4365  O   MET A 582      70.403  41.448  21.110  1.00190.38           O  
ANISOU 4365  O   MET A 582    26608  21168  24560  -5799  -7004   4047       O  
ATOM   4366  CB  MET A 582      69.010  38.326  21.317  1.00188.07           C  
ANISOU 4366  CB  MET A 582    25658  20789  25013  -5561  -7075   4181       C  
ATOM   4367  CG  MET A 582      67.716  37.593  21.657  1.00190.17           C  
ANISOU 4367  CG  MET A 582    26003  21120  25132  -5500  -6930   4097       C  
ATOM   4368  SD  MET A 582      66.650  38.475  22.817  1.00195.10           S  
ANISOU 4368  SD  MET A 582    27341  21928  24861  -5804  -6770   4012       S  
ATOM   4369  CE  MET A 582      67.596  38.343  24.332  1.00192.96           C  
ANISOU 4369  CE  MET A 582    27264  21602  24450  -6462  -7346   4554       C  
ATOM   4370  N   ALA A 583      70.940  39.898  19.568  1.00185.93           N  
ANISOU 4370  N   ALA A 583    25091  20491  25062  -5300  -6966   3997       N  
ATOM   4371  CA  ALA A 583      72.165  40.551  19.094  1.00185.22           C  
ANISOU 4371  CA  ALA A 583    24853  20372  25151  -5337  -7079   4077       C  
ATOM   4372  C   ALA A 583      73.054  41.030  20.243  1.00185.49           C  
ANISOU 4372  C   ALA A 583    25154  20340  24984  -5827  -7508   4482       C  
ATOM   4373  O   ALA A 583      73.454  42.195  20.305  1.00186.35           O  
ANISOU 4373  O   ALA A 583    25567  20496  24742  -5966  -7512   4470       O  
ATOM   4374  CB  ALA A 583      71.829  41.706  18.150  1.00185.88           C  
ANISOU 4374  CB  ALA A 583    25118  20590  24915  -5095  -6691   3701       C  
ATOM   4375  N   VAL A 584      73.367  40.110  21.153  1.00183.35           N  
ANISOU 4375  N   VAL A 584    24763  19951  24950  -6106  -7896   4860       N  
ATOM   4376  CA  VAL A 584      74.267  40.365  22.282  1.00183.57           C  
ANISOU 4376  CA  VAL A 584    24989  19899  24860  -6616  -8372   5312       C  
ATOM   4377  C   VAL A 584      73.768  41.525  23.146  1.00185.07           C  
ANISOU 4377  C   VAL A 584    25889  20207  24223  -6922  -8318   5256       C  
ATOM   4378  O   VAL A 584      74.092  42.689  22.906  1.00184.99           O  
ANISOU 4378  O   VAL A 584    26128  20244  23915  -6941  -8224   5136       O  
ATOM   4379  CB  VAL A 584      75.712  40.625  21.794  1.00182.39           C  
ANISOU 4379  CB  VAL A 584    24494  19655  25152  -6640  -8590   5506       C  
ATOM   4380  CG1 VAL A 584      76.637  40.922  22.969  1.00184.48           C  
ANISOU 4380  CG1 VAL A 584    24978  19830  25284  -7191  -9105   5999       C  
ATOM   4381  CG2 VAL A 584      76.222  39.436  20.995  1.00181.10           C  
ANISOU 4381  CG2 VAL A 584    23608  19362  25840  -6350  -8633   5538       C  
ATOM   4382  N   SER A 591      79.548  38.399  26.307  1.00222.77           N  
ANISOU 4382  N   SER A 591    29226  24186  31232  -8454 -11030   7943       N  
ATOM   4383  CA  SER A 591      80.622  37.423  26.162  1.00225.55           C  
ANISOU 4383  CA  SER A 591    28942  24369  32389  -8265 -11311   8270       C  
ATOM   4384  C   SER A 591      80.640  36.839  24.755  1.00223.23           C  
ANISOU 4384  C   SER A 591    28022  23929  32867  -7807 -11036   7952       C  
ATOM   4385  O   SER A 591      81.359  37.323  23.880  1.00222.46           O  
ANISOU 4385  O   SER A 591    27658  23801  33064  -7643 -10917   7825       O  
ATOM   4386  CB  SER A 591      80.475  36.303  27.192  1.00228.77           C  
ANISOU 4386  CB  SER A 591    29294  24745  32884  -8398 -11647   8643       C  
ATOM   4387  OG  SER A 591      80.589  36.805  28.512  1.00231.57           O  
ANISOU 4387  OG  SER A 591    30174  25269  32542  -8848 -11944   8953       O  
ATOM   4388  N   GLU A 592      79.844  35.796  24.544  1.00224.92           N  
ANISOU 4388  N   GLU A 592    27996  24072  33392  -7614 -10940   7814       N  
ATOM   4389  CA  GLU A 592      79.786  35.131  23.249  1.00223.04           C  
ANISOU 4389  CA  GLU A 592    27151  23710  33884  -7178 -10686   7480       C  
ATOM   4390  C   GLU A 592      78.346  34.997  22.766  1.00220.15           C  
ANISOU 4390  C   GLU A 592    26960  23475  33211  -6924 -10253   7011       C  
ATOM   4391  O   GLU A 592      78.063  35.153  21.578  1.00217.54           O  
ANISOU 4391  O   GLU A 592    26448  23237  32969  -6459  -9782   6541       O  
ATOM   4392  CB  GLU A 592      80.446  33.754  23.323  1.00225.62           C  
ANISOU 4392  CB  GLU A 592    26883  23803  35038  -6973 -10936   7758       C  
ATOM   4393  CG  GLU A 592      80.553  33.058  21.982  1.00223.71           C  
ANISOU 4393  CG  GLU A 592    25973  23425  35601  -6514 -10674   7399       C  
ATOM   4394  CD  GLU A 592      81.257  31.720  22.065  1.00226.90           C  
ANISOU 4394  CD  GLU A 592    25811  23546  36856  -6303 -10908   7658       C  
ATOM   4395  OE1 GLU A 592      81.606  31.295  23.186  1.00230.62           O  
ANISOU 4395  OE1 GLU A 592    26413  23924  37287  -6518 -11301   8148       O  
ATOM   4396  OE2 GLU A 592      81.474  31.099  21.004  1.00226.03           O  
ANISOU 4396  OE2 GLU A 592    25125  23303  37453  -5923 -10698   7363       O  
ATOM   4397  N   VAL A 594      76.996  34.293  25.702  1.00229.53           N  
ANISOU 4397  N   VAL A 594    29047  24774  33390  -7776 -10846   7689       N  
ATOM   4398  CA  VAL A 594      76.634  33.904  27.058  1.00232.34           C  
ANISOU 4398  CA  VAL A 594    29739  25229  33313  -8125 -11132   8043       C  
ATOM   4399  C   VAL A 594      75.655  32.732  26.977  1.00231.66           C  
ANISOU 4399  C   VAL A 594    29441  25092  33490  -7967 -11077   7968       C  
ATOM   4400  O   VAL A 594      74.952  32.576  25.979  1.00228.25           O  
ANISOU 4400  O   VAL A 594    28821  24616  33288  -7671 -10744   7556       O  
ATOM   4401  CB  VAL A 594      76.034  35.095  27.840  1.00231.79           C  
ANISOU 4401  CB  VAL A 594    30432  25398  32241  -8539 -11030   7964       C  
ATOM   4402  CG1 VAL A 594      75.753  34.718  29.291  1.00235.30           C  
ANISOU 4402  CG1 VAL A 594    31212  25991  32202  -8949 -11343   8334       C  
ATOM   4403  CG2 VAL A 594      76.947  36.307  27.757  1.00232.04           C  
ANISOU 4403  CG2 VAL A 594    30665  25462  32035  -8648 -11046   7977       C  
ATOM   4404  N   SER A 595      75.614  31.911  28.024  1.00242.32           N  
ANISOU 4404  N   SER A 595    30819  26455  34798  -8173 -11424   8376       N  
ATOM   4405  CA  SER A 595      74.746  30.743  28.052  1.00242.95           C  
ANISOU 4405  CA  SER A 595    30699  26483  35129  -8049 -11430   8373       C  
ATOM   4406  C   SER A 595      73.277  31.169  28.129  1.00241.47           C  
ANISOU 4406  C   SER A 595    30970  26502  34274  -8195 -11099   8038       C  
ATOM   4407  O   SER A 595      72.940  32.357  28.155  1.00239.94           O  
ANISOU 4407  O   SER A 595    31254  26463  33449  -8380 -10855   7798       O  
ATOM   4408  CB  SER A 595      75.121  29.840  29.224  1.00247.05           C  
ANISOU 4408  CB  SER A 595    31174  26978  35716  -8280 -11920   8938       C  
ATOM   4409  OG  SER A 595      76.433  29.327  29.073  1.00249.68           O  
ANISOU 4409  OG  SER A 595    31036  27061  36769  -8098 -12217   9244       O  
ATOM   4410  N   TYR A 596      72.385  30.174  28.169  1.00244.28           N  
ANISOU 4410  N   TYR A 596    31183  26842  34788  -8107 -11089   8026       N  
ATOM   4411  CA  TYR A 596      70.955  30.466  28.123  1.00241.99           C  
ANISOU 4411  CA  TYR A 596    31256  26722  33967  -8198 -10755   7695       C  
ATOM   4412  C   TYR A 596      70.408  30.830  29.499  1.00243.96           C  
ANISOU 4412  C   TYR A 596    32106  27236  33352  -8732 -10864   7914       C  
ATOM   4413  O   TYR A 596      69.638  31.788  29.628  1.00242.02           O  
ANISOU 4413  O   TYR A 596    32370  27211  32374  -8824 -10493   7600       O  
ATOM   4414  CB  TYR A 596      70.186  29.277  27.535  1.00240.95           C  
ANISOU 4414  CB  TYR A 596    30720  26488  34343  -7853 -10667   7562       C  
ATOM   4415  CG  TYR A 596      70.098  28.053  28.429  1.00243.93           C  
ANISOU 4415  CG  TYR A 596    30955  26835  34893  -8005 -11060   8013       C  
ATOM   4416  CD1 TYR A 596      71.099  27.091  28.433  1.00245.53           C  
ANISOU 4416  CD1 TYR A 596    30671  26791  35827  -7816 -11409   8350       C  
ATOM   4417  CD2 TYR A 596      68.993  27.849  29.249  1.00244.77           C  
ANISOU 4417  CD2 TYR A 596    31415  27155  34430  -8315 -11058   8095       C  
ATOM   4418  CE1 TYR A 596      71.012  25.973  29.244  1.00248.22           C  
ANISOU 4418  CE1 TYR A 596    30905  27083  36323  -7932 -11770   8777       C  
ATOM   4419  CE2 TYR A 596      68.898  26.736  30.062  1.00246.56           C  
ANISOU 4419  CE2 TYR A 596    31522  27377  34782  -8448 -11416   8519       C  
ATOM   4420  CZ  TYR A 596      69.909  25.801  30.055  1.00248.76           C  
ANISOU 4420  CZ  TYR A 596    31336  27390  35790  -8252 -11781   8867       C  
ATOM   4421  OH  TYR A 596      69.815  24.691  30.862  1.00252.84           O  
ANISOU 4421  OH  TYR A 596    31755  27870  36445  -8385 -12154   9313       O  
ATOM   4422  N   LYS A 597      70.792  30.084  30.534  1.00237.88           N  
ANISOU 4422  N   LYS A 597    31292  26502  32589  -8968 -11292   8405       N  
ATOM   4423  CA  LYS A 597      70.299  30.318  31.884  1.00240.23           C  
ANISOU 4423  CA  LYS A 597    32122  27083  32072  -9507 -11429   8631       C  
ATOM   4424  C   LYS A 597      71.170  31.312  32.646  1.00243.57           C  
ANISOU 4424  C   LYS A 597    32923  27630  31993  -9865 -11606   8814       C  
ATOM   4425  O   LYS A 597      70.884  31.612  33.810  1.00247.10           O  
ANISOU 4425  O   LYS A 597    33839  28333  31716 -10355 -11733   8986       O  
ATOM   4426  CB  LYS A 597      70.205  28.982  32.637  1.00241.21           C  
ANISOU 4426  CB  LYS A 597    32021  27207  32419  -9609 -11827   9082       C  
ATOM   4427  CG  LYS A 597      69.407  29.019  33.936  1.00243.16           C  
ANISOU 4427  CG  LYS A 597    32768  27784  31836 -10157 -11922   9267       C  
ATOM   4428  CD  LYS A 597      67.936  29.289  33.653  1.00239.87           C  
ANISOU 4428  CD  LYS A 597    32621  27517  31001 -10184 -11456   8840       C  
ATOM   4429  CE  LYS A 597      67.115  29.331  34.930  1.00242.86           C  
ANISOU 4429  CE  LYS A 597    33489  28244  30544 -10750 -11508   8994       C  
ATOM   4430  NZ  LYS A 597      67.041  28.001  35.592  1.00246.44           N  
ANISOU 4430  NZ  LYS A 597    33686  28723  31225 -10848 -11924   9462       N  
ATOM   4431  N   GLU A 598      72.214  31.841  32.008  1.00244.48           N  
ANISOU 4431  N   GLU A 598    32847  27583  32460  -9646 -11613   8766       N  
ATOM   4432  CA  GLU A 598      73.061  32.865  32.603  1.00246.12           C  
ANISOU 4432  CA  GLU A 598    33401  27895  32219  -9949 -11764   8903       C  
ATOM   4433  C   GLU A 598      72.652  34.278  32.207  1.00243.23           C  
ANISOU 4433  C   GLU A 598    33502  27610  31305 -10005 -11331   8446       C  
ATOM   4434  O   GLU A 598      73.146  35.239  32.804  1.00244.91           O  
ANISOU 4434  O   GLU A 598    34118  27941  30998 -10314 -11415   8509       O  
ATOM   4435  CB  GLU A 598      74.527  32.620  32.223  1.00246.78           C  
ANISOU 4435  CB  GLU A 598    33004  27756  33005  -9708 -12067   9176       C  
ATOM   4436  CG  GLU A 598      75.104  31.347  32.827  1.00249.67           C  
ANISOU 4436  CG  GLU A 598    32991  28019  33853  -9723 -12565   9705       C  
ATOM   4437  CD  GLU A 598      76.539  31.094  32.412  1.00250.35           C  
ANISOU 4437  CD  GLU A 598    32589  27848  34684  -9468 -12833   9962       C  
ATOM   4438  OE1 GLU A 598      77.052  31.839  31.550  1.00247.97           O  
ANISOU 4438  OE1 GLU A 598    32189  27458  34568  -9251 -12606   9704       O  
ATOM   4439  OE2 GLU A 598      77.154  30.148  32.947  1.00253.48           O  
ANISOU 4439  OE2 GLU A 598    32699  28124  35487  -9492 -13271  10432       O  
ATOM   4440  N   LEU A 599      71.771  34.426  31.219  1.00241.74           N  
ANISOU 4440  N   LEU A 599    33275  27351  31226  -9715 -10890   7993       N  
ATOM   4441  CA  LEU A 599      71.116  35.693  30.904  1.00238.86           C  
ANISOU 4441  CA  LEU A 599    33395  27113  30247  -9665 -10399   7508       C  
ATOM   4442  C   LEU A 599      69.606  35.514  30.893  1.00236.89           C  
ANISOU 4442  C   LEU A 599    33343  27074  29590  -9470  -9950   7144       C  
ATOM   4443  O   LEU A 599      68.905  35.936  29.971  1.00234.72           O  
ANISOU 4443  O   LEU A 599    33070  26866  29246  -8949  -9416   6635       O  
ATOM   4444  CB  LEU A 599      71.584  36.285  29.578  1.00235.41           C  
ANISOU 4444  CB  LEU A 599    32703  26575  30168  -9103 -10085   7153       C  
ATOM   4445  CG  LEU A 599      72.977  36.912  29.552  1.00236.93           C  
ANISOU 4445  CG  LEU A 599    32844  26629  30549  -9279 -10388   7394       C  
ATOM   4446  CD1 LEU A 599      73.309  37.402  28.152  1.00233.42           C  
ANISOU 4446  CD1 LEU A 599    32107  26122  30459  -8699 -10033   7014       C  
ATOM   4447  CD2 LEU A 599      73.070  38.049  30.558  1.00239.00           C  
ANISOU 4447  CD2 LEU A 599    33777  27037  29995  -9792 -10457   7458       C  
ATOM   4448  N   GLN A 600      69.087  34.861  31.935  1.00236.21           N  
ANISOU 4448  N   GLN A 600    33414  27099  29235  -9914 -10184   7429       N  
ATOM   4449  CA  GLN A 600      67.646  34.836  32.156  1.00238.49           C  
ANISOU 4449  CA  GLN A 600    33985  27636  28995  -9846  -9768   7114       C  
ATOM   4450  C   GLN A 600      67.091  36.238  32.374  1.00241.53           C  
ANISOU 4450  C   GLN A 600    34978  28239  28553  -9878  -9302   6679       C  
ATOM   4451  O   GLN A 600      65.890  36.460  32.182  1.00244.33           O  
ANISOU 4451  O   GLN A 600    35515  28769  28552  -9625  -8809   6265       O  
ATOM   4452  CB  GLN A 600      67.325  33.943  33.359  1.00238.98           C  
ANISOU 4452  CB  GLN A 600    34131  27801  28867 -10423 -10162   7561       C  
ATOM   4453  CG  GLN A 600      65.844  33.708  33.614  1.00239.93           C  
ANISOU 4453  CG  GLN A 600    34460  28181  28520 -10376  -9779   7300       C  
ATOM   4454  CD  GLN A 600      65.597  32.822  34.820  1.00241.63           C  
ANISOU 4454  CD  GLN A 600    34751  28519  28539 -11002 -10206   7783       C  
ATOM   4455  OE1 GLN A 600      66.533  32.421  35.512  1.00242.83           O  
ANISOU 4455  OE1 GLN A 600    34813  28601  28849 -11409 -10772   8295       O  
ATOM   4456  NE2 GLN A 600      64.332  32.512  35.078  1.00241.91           N  
ANISOU 4456  NE2 GLN A 600    34925  28790  28199 -10994  -9909   7605       N  
ATOM   4457  N   ASP A 601      67.946  37.189  32.750  1.00244.68           N  
ANISOU 4457  N   ASP A 601    35678  28612  28676 -10173  -9454   6762       N  
ATOM   4458  CA  ASP A 601      67.533  38.561  33.047  1.00245.24           C  
ANISOU 4458  CA  ASP A 601    36344  28854  27980 -10258  -9071   6372       C  
ATOM   4459  C   ASP A 601      67.579  39.435  31.791  1.00245.27           C  
ANISOU 4459  C   ASP A 601    36262  28768  28162  -9648  -8650   5906       C  
ATOM   4460  O   ASP A 601      68.273  40.449  31.719  1.00244.41           O  
ANISOU 4460  O   ASP A 601    36369  28603  27894  -9711  -8669   5844       O  
ATOM   4461  CB  ASP A 601      68.406  39.135  34.159  1.00244.30           C  
ANISOU 4461  CB  ASP A 601    36630  28756  27438 -10940  -9480   6714       C  
ATOM   4462  CG  ASP A 601      69.888  39.126  33.807  1.00243.06           C  
ANISOU 4462  CG  ASP A 601    36157  28341  27852 -10972  -9931   7077       C  
ATOM   4463  OD1 ASP A 601      70.250  38.611  32.728  1.00240.61           O  
ANISOU 4463  OD1 ASP A 601    35294  27847  28282 -10476  -9926   7061       O  
ATOM   4464  OD2 ASP A 601      70.693  39.640  34.612  1.00244.93           O  
ANISOU 4464  OD2 ASP A 601    36699  28567  27795 -11504 -10286   7372       O  
ATOM   4465  N   SER A 602      66.805  39.028  30.789  1.00244.08           N  
ANISOU 4465  N   SER A 602    35795  28609  28336  -9070  -8279   5589       N  
ATOM   4466  CA  SER A 602      66.697  39.807  29.565  1.00240.18           C  
ANISOU 4466  CA  SER A 602    35217  28058  27983  -8503  -7860   5141       C  
ATOM   4467  C   SER A 602      65.884  41.076  29.825  1.00239.83           C  
ANISOU 4467  C   SER A 602    35736  28171  27219  -8507  -7413   4698       C  
ATOM   4468  O   SER A 602      65.452  41.357  30.947  1.00242.71           O  
ANISOU 4468  O   SER A 602    36553  28692  26975  -8946  -7409   4714       O  
ATOM   4469  CB  SER A 602      66.074  38.965  28.454  1.00236.75           C  
ANISOU 4469  CB  SER A 602    34297  27576  28081  -7933  -7612   4947       C  
ATOM   4470  OG  SER A 602      64.732  38.631  28.759  1.00236.38           O  
ANISOU 4470  OG  SER A 602    34397  27700  27718  -7887  -7317   4756       O  
ATOM   4471  N   THR A 603      65.663  41.852  28.766  1.00244.01           N  
ANISOU 4471  N   THR A 603    36229  28655  27828  -8021  -7030   4290       N  
ATOM   4472  CA  THR A 603      64.913  43.097  28.877  1.00245.18           C  
ANISOU 4472  CA  THR A 603    36857  28900  27400  -7961  -6605   3846       C  
ATOM   4473  C   THR A 603      63.423  42.775  29.007  1.00246.35           C  
ANISOU 4473  C   THR A 603    37087  29209  27306  -7798  -6200   3560       C  
ATOM   4474  O   THR A 603      63.027  41.619  29.177  1.00245.76           O  
ANISOU 4474  O   THR A 603    36761  29189  27428  -7821  -6297   3749       O  
ATOM   4475  CB  THR A 603      65.214  44.009  27.690  1.00245.34           C  
ANISOU 4475  CB  THR A 603    36783  28806  27630  -7524  -6386   3558       C  
ATOM   4476  OG1 THR A 603      64.841  43.355  26.472  1.00245.97           O  
ANISOU 4476  OG1 THR A 603    36377  28842  28236  -6992  -6188   3422       O  
ATOM   4477  CG2 THR A 603      66.698  44.351  27.644  1.00243.83           C  
ANISOU 4477  CG2 THR A 603    36523  28478  27643  -7728  -6793   3861       C  
ATOM   4478  N   GLN A 604      62.574  43.799  28.932  1.00242.66           N  
ANISOU 4478  N   GLN A 604    36962  28808  26431  -7635  -5751   3106       N  
ATOM   4479  CA  GLN A 604      61.154  43.630  29.239  1.00243.96           C  
ANISOU 4479  CA  GLN A 604    37265  29139  26291  -7552  -5357   2831       C  
ATOM   4480  C   GLN A 604      60.498  42.765  28.164  1.00244.55           C  
ANISOU 4480  C   GLN A 604    36857  29188  26874  -7032  -5171   2748       C  
ATOM   4481  O   GLN A 604      60.231  43.212  27.047  1.00244.81           O  
ANISOU 4481  O   GLN A 604    36733  29135  27147  -6553  -4892   2457       O  
ATOM   4482  CB  GLN A 604      60.474  44.990  29.394  1.00244.12           C  
ANISOU 4482  CB  GLN A 604    37740  29197  25819  -7490  -4931   2355       C  
ATOM   4483  CG  GLN A 604      60.468  45.901  28.172  1.00243.29           C  
ANISOU 4483  CG  GLN A 604    37542  28937  25960  -6989  -4675   2028       C  
ATOM   4484  CD  GLN A 604      59.837  47.249  28.460  1.00244.13           C  
ANISOU 4484  CD  GLN A 604    38110  29046  25602  -6981  -4307   1586       C  
ATOM   4485  OE1 GLN A 604      59.423  47.525  29.586  1.00245.28           O  
ANISOU 4485  OE1 GLN A 604    38657  29317  25220  -7351  -4214   1490       O  
ATOM   4486  NE2 GLN A 604      59.740  48.088  27.436  1.00243.82           N  
ANISOU 4486  NE2 GLN A 604    38008  28868  25764  -6568  -4092   1305       N  
ATOM   4487  N   MET A 605      60.257  41.501  28.508  1.00244.34           N  
ANISOU 4487  N   MET A 605    36592  29231  27014  -7154  -5354   3025       N  
ATOM   4488  CA  MET A 605      59.620  40.533  27.626  1.00244.72           C  
ANISOU 4488  CA  MET A 605    36194  29259  27530  -6726  -5225   2986       C  
ATOM   4489  C   MET A 605      59.255  39.303  28.443  1.00245.12           C  
ANISOU 4489  C   MET A 605    36144  29425  27566  -7028  -5448   3306       C  
ATOM   4490  O   MET A 605      59.998  38.910  29.346  1.00245.45           O  
ANISOU 4490  O   MET A 605    36251  29477  27533  -7514  -5878   3700       O  
ATOM   4491  CB  MET A 605      60.533  40.153  26.451  1.00243.75           C  
ANISOU 4491  CB  MET A 605    35599  28937  28079  -6392  -5414   3096       C  
ATOM   4492  CG  MET A 605      61.858  39.530  26.843  1.00242.52           C  
ANISOU 4492  CG  MET A 605    35249  28669  28229  -6721  -5968   3570       C  
ATOM   4493  SD  MET A 605      62.903  39.212  25.408  1.00241.94           S  
ANISOU 4493  SD  MET A 605    34616  28376  28935  -6301  -6103   3613       S  
ATOM   4494  CE  MET A 605      63.399  40.874  24.969  1.00241.73           C  
ANISOU 4494  CE  MET A 605    34895  28319  28633  -6213  -5908   3333       C  
ATOM   4495  N   ASN A 606      58.109  38.709  28.126  1.00239.78           N  
ANISOU 4495  N   ASN A 606    35306  28834  26963  -6760  -5176   3157       N  
ATOM   4496  CA  ASN A 606      57.584  37.593  28.897  1.00240.03           C  
ANISOU 4496  CA  ASN A 606    35263  29001  26936  -7039  -5344   3431       C  
ATOM   4497  C   ASN A 606      58.127  36.272  28.367  1.00238.47           C  
ANISOU 4497  C   ASN A 606    34535  28642  27431  -6915  -5727   3776       C  
ATOM   4498  O   ASN A 606      58.377  36.114  27.169  1.00238.09           O  
ANISOU 4498  O   ASN A 606    34136  28425  27904  -6454  -5665   3655       O  
ATOM   4499  CB  ASN A 606      56.055  37.589  28.859  1.00242.05           C  
ANISOU 4499  CB  ASN A 606    35602  29433  26932  -6828  -4869   3116       C  
ATOM   4500  CG  ASN A 606      55.446  36.631  29.866  1.00242.61           C  
ANISOU 4500  CG  ASN A 606    35698  29703  26780  -7214  -5012   3386       C  
ATOM   4501  OD1 ASN A 606      56.155  35.922  30.580  1.00241.39           O  
ANISOU 4501  OD1 ASN A 606    35488  29545  26684  -7645  -5492   3828       O  
ATOM   4502  ND2 ASN A 606      54.121  36.617  29.937  1.00244.19           N  
ANISOU 4502  ND2 ASN A 606    35974  30080  26727  -7079  -4606   3136       N  
ATOM   4503  N   GLU A 607      58.300  35.315  29.280  1.00238.48           N  
ANISOU 4503  N   GLU A 607    34479  28697  27437  -7350  -6129   4203       N  
ATOM   4504  CA  GLU A 607      58.869  34.010  28.968  1.00237.00           C  
ANISOU 4504  CA  GLU A 607    33796  28331  27924  -7310  -6563   4577       C  
ATOM   4505  C   GLU A 607      57.844  33.022  28.419  1.00236.95           C  
ANISOU 4505  C   GLU A 607    33474  28341  28214  -6978  -6408   4507       C  
ATOM   4506  O   GLU A 607      58.084  31.811  28.480  1.00235.26           O  
ANISOU 4506  O   GLU A 607    32908  28019  28460  -7058  -6791   4854       O  
ATOM   4507  CB  GLU A 607      59.547  33.420  30.209  1.00236.90           C  
ANISOU 4507  CB  GLU A 607    33849  28341  27822  -7960  -7125   5114       C  
ATOM   4508  CG  GLU A 607      60.795  34.170  30.656  1.00237.04           C  
ANISOU 4508  CG  GLU A 607    34073  28278  27714  -8296  -7408   5286       C  
ATOM   4509  CD  GLU A 607      61.430  33.565  31.895  1.00235.49           C  
ANISOU 4509  CD  GLU A 607    33943  28105  27427  -8977  -7992   5852       C  
ATOM   4510  OE1 GLU A 607      60.831  32.640  32.482  1.00235.13           O  
ANISOU 4510  OE1 GLU A 607    33829  28170  27337  -9219  -8152   6094       O  
ATOM   4511  OE2 GLU A 607      62.529  34.016  32.283  1.00233.98           O  
ANISOU 4511  OE2 GLU A 607    33868  27823  27210  -9289  -8310   6077       O  
ATOM   4512  N   LYS A 608      56.709  33.499  27.901  1.00239.21           N  
ANISOU 4512  N   LYS A 608    33872  28745  28272  -6619  -5879   4083       N  
ATOM   4513  CA  LYS A 608      55.731  32.594  27.304  1.00240.14           C  
ANISOU 4513  CA  LYS A 608    33689  28870  28684  -6287  -5728   4013       C  
ATOM   4514  C   LYS A 608      56.299  31.921  26.059  1.00239.03           C  
ANISOU 4514  C   LYS A 608    33045  28465  29310  -5856  -5860   4016       C  
ATOM   4515  O   LYS A 608      56.429  30.693  26.005  1.00237.61           O  
ANISOU 4515  O   LYS A 608    32508  28173  29601  -5871  -6186   4296       O  
ATOM   4516  CB  LYS A 608      54.442  33.351  26.973  1.00241.80           C  
ANISOU 4516  CB  LYS A 608    34122  29244  28508  -5992  -5133   3559       C  
ATOM   4517  CG  LYS A 608      53.639  33.779  28.192  1.00242.13           C  
ANISOU 4517  CG  LYS A 608    34594  29568  27834  -6390  -4950   3525       C  
ATOM   4518  CD  LYS A 608      52.352  34.484  27.787  1.00242.66           C  
ANISOU 4518  CD  LYS A 608    34815  29762  27623  -6050  -4354   3067       C  
ATOM   4519  CE  LYS A 608      51.538  34.900  29.004  1.00243.34           C  
ANISOU 4519  CE  LYS A 608    35308  30138  27012  -6441  -4131   2993       C  
ATOM   4520  NZ  LYS A 608      50.286  35.610  28.624  1.00245.09           N  
ANISOU 4520  NZ  LYS A 608    35649  30460  27015  -6099  -3544   2540       N  
ATOM   4521  N   GLU A 609      56.647  32.713  25.046  1.00227.15           N  
ANISOU 4521  N   GLU A 609    31503  26859  27946  -5481  -5612   3699       N  
ATOM   4522  CA  GLU A 609      57.337  32.207  23.867  1.00225.60           C  
ANISOU 4522  CA  GLU A 609    30853  26433  28434  -5113  -5718   3670       C  
ATOM   4523  C   GLU A 609      58.808  32.590  23.831  1.00224.40           C  
ANISOU 4523  C   GLU A 609    30638  26130  28495  -5243  -6004   3814       C  
ATOM   4524  O   GLU A 609      59.524  32.151  22.926  1.00222.70           O  
ANISOU 4524  O   GLU A 609    30023  25725  28868  -4982  -6115   3807       O  
ATOM   4525  CB  GLU A 609      56.650  32.687  22.584  1.00226.17           C  
ANISOU 4525  CB  GLU A 609    30856  26508  28573  -4583  -5239   3221       C  
ATOM   4526  CG  GLU A 609      55.296  32.050  22.321  1.00226.51           C  
ANISOU 4526  CG  GLU A 609    30810  26636  28617  -4367  -5005   3106       C  
ATOM   4527  CD  GLU A 609      54.687  32.502  21.007  1.00226.92           C  
ANISOU 4527  CD  GLU A 609    30775  26673  28773  -3869  -4579   2701       C  
ATOM   4528  OE1 GLU A 609      55.258  33.409  20.367  1.00226.10           O  
ANISOU 4528  OE1 GLU A 609    30721  26518  28669  -3717  -4443   2498       O  
ATOM   4529  OE2 GLU A 609      53.643  31.944  20.610  1.00227.68           O  
ANISOU 4529  OE2 GLU A 609    30748  26810  28950  -3651  -4399   2606       O  
ATOM   4530  N   LEU A 610      59.277  33.403  24.781  1.00233.89           N  
ANISOU 4530  N   LEU A 610    32219  27414  29236  -5645  -6116   3933       N  
ATOM   4531  CA  LEU A 610      60.702  33.707  24.855  1.00232.27           C  
ANISOU 4531  CA  LEU A 610    31950  27063  29237  -5822  -6443   4135       C  
ATOM   4532  C   LEU A 610      61.514  32.453  25.148  1.00229.57           C  
ANISOU 4532  C   LEU A 610    31212  26542  29473  -6019  -6983   4585       C  
ATOM   4533  O   LEU A 610      62.544  32.201  24.511  1.00226.62           O  
ANISOU 4533  O   LEU A 610    30478  25965  29662  -5872  -7179   4660       O  
ATOM   4534  CB  LEU A 610      60.962  34.768  25.921  1.00232.38           C  
ANISOU 4534  CB  LEU A 610    32483  27206  28606  -6264  -6482   4197       C  
ATOM   4535  CG  LEU A 610      62.438  35.128  26.095  1.00230.74           C  
ANISOU 4535  CG  LEU A 610    32243  26856  28572  -6499  -6851   4445       C  
ATOM   4536  CD1 LEU A 610      62.993  35.738  24.817  1.00230.39           C  
ANISOU 4536  CD1 LEU A 610    32001  26695  28842  -6065  -6646   4166       C  
ATOM   4537  CD2 LEU A 610      62.640  36.052  27.285  1.00230.37           C  
ANISOU 4537  CD2 LEU A 610    32734  26940  27857  -7007  -6937   4546       C  
ATOM   4538  N   THR A 611      61.062  31.650  26.115  1.00232.71           N  
ANISOU 4538  N   THR A 611    31653  27009  29756  -6364  -7234   4892       N  
ATOM   4539  CA  THR A 611      61.783  30.435  26.477  1.00230.37           C  
ANISOU 4539  CA  THR A 611    30980  26523  30027  -6589  -7793   5359       C  
ATOM   4540  C   THR A 611      61.835  29.433  25.330  1.00228.89           C  
ANISOU 4540  C   THR A 611    30227  26116  30624  -6118  -7801   5267       C  
ATOM   4541  O   THR A 611      62.748  28.600  25.292  1.00226.82           O  
ANISOU 4541  O   THR A 611    29562  25613  31004  -6181  -8232   5569       O  
ATOM   4542  CB  THR A 611      61.146  29.792  27.713  1.00231.23           C  
ANISOU 4542  CB  THR A 611    31266  26781  29810  -7065  -8041   5699       C  
ATOM   4543  OG1 THR A 611      61.960  28.703  28.165  1.00228.65           O  
ANISOU 4543  OG1 THR A 611    30595  26248  30034  -7354  -8657   6211       O  
ATOM   4544  CG2 THR A 611      59.747  29.278  27.398  1.00232.94           C  
ANISOU 4544  CG2 THR A 611    31442  27124  29941  -6797  -7716   5482       C  
ATOM   4545  N   LYS A 612      60.889  29.499  24.395  1.00226.83           N  
ANISOU 4545  N   LYS A 612    29922  25922  30343  -5656  -7338   4854       N  
ATOM   4546  CA  LYS A 612      60.884  28.621  23.233  1.00224.09           C  
ANISOU 4546  CA  LYS A 612    29074  25383  30688  -5203  -7292   4705       C  
ATOM   4547  C   LYS A 612      61.779  29.124  22.108  1.00222.58           C  
ANISOU 4547  C   LYS A 612    28661  25062  30849  -4864  -7142   4447       C  
ATOM   4548  O   LYS A 612      61.874  28.461  21.070  1.00219.85           O  
ANISOU 4548  O   LYS A 612    27897  24563  31074  -4490  -7074   4278       O  
ATOM   4549  CB  LYS A 612      59.455  28.451  22.707  1.00225.43           C  
ANISOU 4549  CB  LYS A 612    29296  25687  30668  -4885  -6877   4394       C  
ATOM   4550  CG  LYS A 612      58.508  27.750  23.668  1.00226.22           C  
ANISOU 4550  CG  LYS A 612    29520  25914  30519  -5170  -7017   4643       C  
ATOM   4551  CD  LYS A 612      57.117  27.618  23.065  1.00228.06           C  
ANISOU 4551  CD  LYS A 612    29779  26272  30602  -4828  -6593   4331       C  
ATOM   4552  CE  LYS A 612      56.181  26.854  23.986  1.00228.58           C  
ANISOU 4552  CE  LYS A 612    29928  26472  30451  -5112  -6740   4594       C  
ATOM   4553  NZ  LYS A 612      55.891  27.609  25.237  1.00231.05           N  
ANISOU 4553  NZ  LYS A 612    30728  27047  30015  -5570  -6703   4710       N  
ATOM   4554  N   THR A 613      62.433  30.276  22.286  1.00219.47           N  
ANISOU 4554  N   THR A 613    28537  24732  30120  -5002  -7086   4407       N  
ATOM   4555  CA  THR A 613      63.211  30.898  21.223  1.00217.46           C  
ANISOU 4555  CA  THR A 613    28117  24403  30104  -4704  -6905   4150       C  
ATOM   4556  C   THR A 613      64.631  31.253  21.652  1.00214.53           C  
ANISOU 4556  C   THR A 613    27705  23920  29886  -4990  -7262   4431       C  
ATOM   4557  O   THR A 613      65.343  31.919  20.892  1.00211.13           O  
ANISOU 4557  O   THR A 613    27187  23461  29574  -4808  -7123   4248       O  
ATOM   4558  CB  THR A 613      62.504  32.160  20.711  1.00219.21           C  
ANISOU 4558  CB  THR A 613    28708  24823  29759  -4494  -6390   3733       C  
ATOM   4559  OG1 THR A 613      62.385  33.108  21.779  1.00219.32           O  
ANISOU 4559  OG1 THR A 613    29237  24987  29109  -4863  -6402   3829       O  
ATOM   4560  CG2 THR A 613      61.116  31.823  20.183  1.00221.39           C  
ANISOU 4560  CG2 THR A 613    28986  25195  29937  -4187  -6033   3457       C  
ATOM   4561  N   ILE A 614      65.061  30.832  22.837  1.00225.95           N  
ANISOU 4561  N   ILE A 614    29208  25311  31333  -5452  -7728   4888       N  
ATOM   4562  CA  ILE A 614      66.394  31.166  23.324  1.00224.50           C  
ANISOU 4562  CA  ILE A 614    29000  25016  31284  -5768  -8105   5203       C  
ATOM   4563  C   ILE A 614      67.459  30.384  22.565  1.00221.63           C  
ANISOU 4563  C   ILE A 614    28017  24380  31811  -5554  -8332   5287       C  
ATOM   4564  O   ILE A 614      68.293  30.965  21.871  1.00219.92           O  
ANISOU 4564  O   ILE A 614    27664  24118  31778  -5390  -8232   5145       O  
ATOM   4565  CB  ILE A 614      66.514  30.911  24.835  1.00225.43           C  
ANISOU 4565  CB  ILE A 614    29363  25158  31131  -6370  -8566   5696       C  
ATOM   4566  CG1 ILE A 614      65.495  31.756  25.600  1.00229.17           C  
ANISOU 4566  CG1 ILE A 614    30461  25921  30694  -6598  -8298   5564       C  
ATOM   4567  CG2 ILE A 614      67.926  31.214  25.314  1.00224.15           C  
ANISOU 4567  CG2 ILE A 614    29152  24861  31155  -6710  -8993   6056       C  
ATOM   4568  CD1 ILE A 614      65.671  33.244  25.407  1.00228.39           C  
ANISOU 4568  CD1 ILE A 614    30750  25944  30082  -6559  -7984   5279       C  
ATOM   4569  N   SER A 616      66.548  28.582  20.293  1.00214.91           N  
ANISOU 4569  N   SER A 616    26290  23324  32040  -4590  -7887   4691       N  
ATOM   4570  CA  SER A 616      66.376  28.321  18.870  1.00214.39           C  
ANISOU 4570  CA  SER A 616    25890  23219  32351  -4083  -7521   4255       C  
ATOM   4571  C   SER A 616      67.584  28.811  18.077  1.00213.63           C  
ANISOU 4571  C   SER A 616    25531  23052  32587  -3938  -7458   4120       C  
ATOM   4572  O   SER A 616      67.960  28.209  17.072  1.00212.52           O  
ANISOU 4572  O   SER A 616    24922  22776  33049  -3620  -7360   3903       O  
ATOM   4573  CB  SER A 616      65.097  28.983  18.355  1.00216.83           C  
ANISOU 4573  CB  SER A 616    26554  23776  32057  -3847  -7001   3856       C  
ATOM   4574  OG  SER A 616      64.919  28.737  16.971  1.00216.78           O  
ANISOU 4574  OG  SER A 616    26242  23745  32379  -3398  -6662   3450       O  
ATOM   4575  N   LEU A 617      68.193  29.907  18.535  1.00225.83           N  
ANISOU 4575  N   LEU A 617    27379  24696  33730  -4186  -7510   4241       N  
ATOM   4576  CA  LEU A 617      69.396  30.410  17.882  1.00225.66           C  
ANISOU 4576  CA  LEU A 617    27116  24622  34002  -4100  -7488   4168       C  
ATOM   4577  C   LEU A 617      70.640  29.663  18.341  1.00222.92           C  
ANISOU 4577  C   LEU A 617    26344  24005  34353  -4302  -7997   4570       C  
ATOM   4578  O   LEU A 617      71.568  29.464  17.549  1.00220.71           O  
ANISOU 4578  O   LEU A 617    25609  23601  34652  -4107  -7979   4464       O  
ATOM   4579  CB  LEU A 617      69.552  31.910  18.138  1.00227.45           C  
ANISOU 4579  CB  LEU A 617    27833  25050  33538  -4277  -7349   4136       C  
ATOM   4580  CG  LEU A 617      70.736  32.591  17.447  1.00227.14           C  
ANISOU 4580  CG  LEU A 617    27598  25001  33703  -4206  -7301   4059       C  
ATOM   4581  CD1 LEU A 617      70.618  32.467  15.936  1.00227.16           C  
ANISOU 4581  CD1 LEU A 617    27268  25049  33993  -3748  -6881   3598       C  
ATOM   4582  CD2 LEU A 617      70.827  34.052  17.856  1.00229.04           C  
ANISOU 4582  CD2 LEU A 617    28367  25418  33240  -4428  -7226   4075       C  
ATOM   4583  N   LEU A 618      70.673  29.231  19.601  1.00231.23           N  
ANISOU 4583  N   LEU A 618    27517  24966  35375  -4704  -8453   5033       N  
ATOM   4584  CA  LEU A 618      71.734  28.374  20.110  1.00228.71           C  
ANISOU 4584  CA  LEU A 618    26769  24354  35775  -4918  -8996   5468       C  
ATOM   4585  C   LEU A 618      71.506  26.907  19.774  1.00228.17           C  
ANISOU 4585  C   LEU A 618    26191  24043  36459  -4699  -9129   5461       C  
ATOM   4586  O   LEU A 618      72.060  26.026  20.441  1.00230.62           O  
ANISOU 4586  O   LEU A 618    26203  24096  37327  -4932  -9645   5886       O  
ATOM   4587  CB  LEU A 618      71.892  28.572  21.622  1.00229.53           C  
ANISOU 4587  CB  LEU A 618    27238  24471  35503  -5499  -9466   6002       C  
ATOM   4588  CG  LEU A 618      70.700  28.381  22.570  1.00229.49           C  
ANISOU 4588  CG  LEU A 618    27665  24613  34918  -5758  -9520   6139       C  
ATOM   4589  CD1 LEU A 618      70.516  26.932  23.005  1.00230.56           C  
ANISOU 4589  CD1 LEU A 618    27450  24526  35626  -5856  -9927   6453       C  
ATOM   4590  CD2 LEU A 618      70.855  29.286  23.784  1.00229.94           C  
ANISOU 4590  CD2 LEU A 618    28274  24828  34265  -6293  -9731   6454       C  
ATOM   4591  N   ASP A 619      70.692  26.632  18.761  1.00230.66           N  
ANISOU 4591  N   ASP A 619    26406  24424  36808  -4271  -8694   4997       N  
ATOM   4592  CA  ASP A 619      70.381  25.272  18.352  1.00230.26           C  
ANISOU 4592  CA  ASP A 619    25900  24148  37439  -4033  -8774   4927       C  
ATOM   4593  C   ASP A 619      70.688  24.977  16.892  1.00229.86           C  
ANISOU 4593  C   ASP A 619    25387  24018  37931  -3550  -8415   4445       C  
ATOM   4594  O   ASP A 619      70.929  23.814  16.558  1.00229.86           O  
ANISOU 4594  O   ASP A 619    24874  23740  38723  -3380  -8578   4429       O  
ATOM   4595  CB  ASP A 619      68.897  24.965  18.617  1.00229.50           C  
ANISOU 4595  CB  ASP A 619    26124  24196  36879  -4014  -8633   4854       C  
ATOM   4596  CG  ASP A 619      68.534  23.524  18.312  1.00229.07           C  
ANISOU 4596  CG  ASP A 619    25630  23894  37512  -3814  -8778   4835       C  
ATOM   4597  OD1 ASP A 619      68.907  22.632  19.103  1.00231.18           O  
ANISOU 4597  OD1 ASP A 619    25661  23915  38263  -4068  -9310   5273       O  
ATOM   4598  OD2 ASP A 619      67.874  23.284  17.279  1.00227.99           O  
ANISOU 4598  OD2 ASP A 619    25386  23802  37438  -3418  -8379   4391       O  
ATOM   4599  N   VAL A 620      70.701  25.980  16.014  1.00224.30           N  
ANISOU 4599  N   VAL A 620    24839  23545  36839  -3340  -7943   4050       N  
ATOM   4600  CA  VAL A 620      70.733  25.678  14.587  1.00224.72           C  
ANISOU 4600  CA  VAL A 620    24518  23585  37281  -2899  -7542   3546       C  
ATOM   4601  C   VAL A 620      72.148  25.735  14.024  1.00223.66           C  
ANISOU 4601  C   VAL A 620    23915  23323  37743  -2823  -7574   3493       C  
ATOM   4602  O   VAL A 620      72.719  24.699  13.665  1.00223.94           O  
ANISOU 4602  O   VAL A 620    23382  23080  38624  -2668  -7715   3455       O  
ATOM   4603  CB  VAL A 620      69.808  26.636  13.813  1.00227.15           C  
ANISOU 4603  CB  VAL A 620    25228  24227  36851  -2699  -6987   3118       C  
ATOM   4604  CG1 VAL A 620      69.898  26.376  12.316  1.00227.11           C  
ANISOU 4604  CG1 VAL A 620    24853  24239  37201  -2296  -6577   2605       C  
ATOM   4605  CG2 VAL A 620      68.373  26.499  14.298  1.00227.75           C  
ANISOU 4605  CG2 VAL A 620    25705  24416  36413  -2738  -6927   3143       C  
ATOM   4606  N   LYS A 621      72.733  26.932  13.939  1.00208.40           N  
ANISOU 4606  N   LYS A 621    22196  21582  35403  -2929  -7447   3485       N  
ATOM   4607  CA  LYS A 621      74.053  27.030  13.324  1.00207.48           C  
ANISOU 4607  CA  LYS A 621    21624  21381  35829  -2848  -7433   3411       C  
ATOM   4608  C   LYS A 621      75.051  27.897  14.083  1.00208.40           C  
ANISOU 4608  C   LYS A 621    21891  21518  35775  -3195  -7725   3805       C  
ATOM   4609  O   LYS A 621      76.232  27.549  14.177  1.00209.23           O  
ANISOU 4609  O   LYS A 621    21549  21409  36542  -3264  -8002   4012       O  
ATOM   4610  CB  LYS A 621      73.919  27.556  11.892  1.00207.94           C  
ANISOU 4610  CB  LYS A 621    21625  21675  35709  -2518  -6853   2847       C  
ATOM   4611  CG  LYS A 621      73.259  26.584  10.930  1.00207.56           C  
ANISOU 4611  CG  LYS A 621    21276  21566  36022  -2158  -6567   2420       C  
ATOM   4612  CD  LYS A 621      73.106  27.195   9.552  1.00209.54           C  
ANISOU 4612  CD  LYS A 621    21526  22089  36002  -1900  -6006   1891       C  
ATOM   4613  CE  LYS A 621      74.451  27.324   8.859  1.00210.45           C  
ANISOU 4613  CE  LYS A 621    21166  22185  36609  -1837  -5919   1757       C  
ATOM   4614  NZ  LYS A 621      75.027  25.996   8.510  1.00209.03           N  
ANISOU 4614  NZ  LYS A 621    20322  21692  37410  -1649  -6017   1638       N  
ATOM   4615  N   MET A 622      74.588  29.016  14.639  1.00208.53           N  
ANISOU 4615  N   MET A 622    22526  21774  34933  -3419  -7676   3911       N  
ATOM   4616  CA  MET A 622      75.466  30.154  14.894  1.00209.00           C  
ANISOU 4616  CA  MET A 622    22774  21943  34693  -3652  -7756   4091       C  
ATOM   4617  C   MET A 622      75.936  30.276  16.336  1.00208.41           C  
ANISOU 4617  C   MET A 622    22917  21748  34521  -4122  -8304   4678       C  
ATOM   4618  O   MET A 622      77.013  30.834  16.573  1.00208.04           O  
ANISOU 4618  O   MET A 622    22811  21674  34562  -4326  -8509   4917       O  
ATOM   4619  CB  MET A 622      74.767  31.450  14.470  1.00211.43           C  
ANISOU 4619  CB  MET A 622    23615  22588  34132  -3595  -7330   3793       C  
ATOM   4620  CG  MET A 622      74.538  31.531  12.964  1.00212.31           C  
ANISOU 4620  CG  MET A 622    23505  22850  34315  -3193  -6808   3249       C  
ATOM   4621  SD  MET A 622      73.662  33.006  12.412  1.00214.47           S  
ANISOU 4621  SD  MET A 622    24368  23488  33634  -3128  -6345   2922       S  
ATOM   4622  CE  MET A 622      73.509  32.667  10.658  1.00213.77           C  
ANISOU 4622  CE  MET A 622    23866  23516  33842  -2696  -5834   2350       C  
ATOM   4623  N   ILE A 623      75.168  29.788  17.305  1.00223.91           N  
ANISOU 4623  N   ILE A 623    25136  23653  36285  -4327  -8552   4927       N  
ATOM   4624  CA  ILE A 623      75.600  29.740  18.693  1.00224.55           C  
ANISOU 4624  CA  ILE A 623    25392  23614  36315  -4815  -9109   5506       C  
ATOM   4625  C   ILE A 623      75.741  28.305  19.186  1.00227.96           C  
ANISOU 4625  C   ILE A 623    25393  23728  37495  -4891  -9552   5824       C  
ATOM   4626  O   ILE A 623      76.663  27.996  19.945  1.00231.77           O  
ANISOU 4626  O   ILE A 623    25675  23996  38391  -5211 -10068   6306       O  
ATOM   4627  CB  ILE A 623      74.646  30.549  19.600  1.00223.98           C  
ANISOU 4627  CB  ILE A 623    26059  23777  35265  -5107  -9073   5592       C  
ATOM   4628  CG1 ILE A 623      74.669  32.026  19.209  1.00224.92           C  
ANISOU 4628  CG1 ILE A 623    26587  24156  34715  -5076  -8719   5338       C  
ATOM   4629  CG2 ILE A 623      75.031  30.401  21.064  1.00225.72           C  
ANISOU 4629  CG2 ILE A 623    26469  23889  35405  -5657  -9657   6191       C  
ATOM   4630  CD1 ILE A 623      73.613  32.851  19.903  1.00226.13           C  
ANISOU 4630  CD1 ILE A 623    27441  24540  33939  -5271  -8573   5293       C  
ATOM   4631  N   ASN A 624      74.846  27.418  18.756  1.00237.98           N  
ANISOU 4631  N   ASN A 624    26505  24949  38967  -4610  -9379   5576       N  
ATOM   4632  CA  ASN A 624      74.902  25.994  19.085  1.00241.10           C  
ANISOU 4632  CA  ASN A 624    26454  25022  40130  -4629  -9775   5826       C  
ATOM   4633  C   ASN A 624      75.029  25.761  20.589  1.00243.90           C  
ANISOU 4633  C   ASN A 624    27097  25307  40268  -5074 -10282   6444       C  
ATOM   4634  O   ASN A 624      76.105  25.426  21.083  1.00247.17           O  
ANISOU 4634  O   ASN A 624    27340  25525  41049  -5126 -10573   6820       O  
ATOM   4635  CB  ASN A 624      76.064  25.318  18.350  1.00243.73           C  
ANISOU 4635  CB  ASN A 624    26082  25068  41458  -4362  -9833   5760       C  
ATOM   4636  CG  ASN A 624      76.011  23.801  18.437  1.00246.18           C  
ANISOU 4636  CG  ASN A 624    26037  25051  42450  -4133  -9988   5859       C  
ATOM   4637  OD1 ASN A 624      75.104  23.230  19.046  1.00246.24           O  
ANISOU 4637  OD1 ASN A 624    26264  25048  42248  -4230 -10130   6015       O  
ATOM   4638  ND2 ASN A 624      76.988  23.140  17.828  1.00248.02           N  
ANISOU 4638  ND2 ASN A 624    25727  25004  43507  -3839  -9956   5764       N  
ATOM   4639  N   GLU A 635      74.051  22.971  30.444  1.00246.86           N  
ANISOU 4639  N   GLU A 635    29645  26051  38098  -7739 -13145  10261       N  
ATOM   4640  CA  GLU A 635      74.841  23.920  29.666  1.00244.84           C  
ANISOU 4640  CA  GLU A 635    29292  25762  37973  -7570 -12917   9972       C  
ATOM   4641  C   GLU A 635      76.336  23.757  29.951  1.00249.09           C  
ANISOU 4641  C   GLU A 635    29577  26055  39009  -7565 -13293  10392       C  
ATOM   4642  O   GLU A 635      76.786  23.884  31.091  1.00252.77           O  
ANISOU 4642  O   GLU A 635    30302  26633  39106  -7947 -13690  10878       O  
ATOM   4643  CB  GLU A 635      74.370  25.355  29.947  1.00242.12           C  
ANISOU 4643  CB  GLU A 635    29521  25815  36657  -7901 -12673   9744       C  
ATOM   4644  CG  GLU A 635      74.503  25.815  31.395  1.00245.45           C  
ANISOU 4644  CG  GLU A 635    30448  26509  36304  -8460 -13009  10178       C  
ATOM   4645  CD  GLU A 635      73.882  27.178  31.636  1.00242.80           C  
ANISOU 4645  CD  GLU A 635    30704  26533  35017  -8777 -12712   9881       C  
ATOM   4646  OE1 GLU A 635      73.292  27.739  30.690  1.00238.31           O  
ANISOU 4646  OE1 GLU A 635    30162  25989  34394  -8560 -12256   9365       O  
ATOM   4647  OE2 GLU A 635      73.986  27.687  32.772  1.00245.45           O  
ANISOU 4647  OE2 GLU A 635    31486  27115  34660  -9251 -12937  10156       O  
ATOM   4648  N   SER A 636      77.102  23.441  28.906  1.00250.09           N  
ANISOU 4648  N   SER A 636    29182  25848  39992  -7136 -13171  10201       N  
ATOM   4649  CA  SER A 636      78.539  23.225  29.043  1.00254.20           C  
ANISOU 4649  CA  SER A 636    29397  26082  41105  -7082 -13491  10568       C  
ATOM   4650  C   SER A 636      79.354  24.259  28.278  1.00252.35           C  
ANISOU 4650  C   SER A 636    29066  25874  40943  -6958 -13246  10292       C  
ATOM   4651  O   SER A 636      80.162  24.969  28.887  1.00254.36           O  
ANISOU 4651  O   SER A 636    29519  26230  40895  -7223 -13474  10594       O  
ATOM   4652  CB  SER A 636      78.895  21.806  28.578  1.00256.86           C  
ANISOU 4652  CB  SER A 636    29164  25931  42500  -6709 -13611  10652       C  
ATOM   4653  OG  SER A 636      78.651  21.652  27.190  1.00253.48           O  
ANISOU 4653  OG  SER A 636    28363  25361  42585  -6259 -13156  10056       O  
ATOM   4654  N   SER A 637      79.163  24.372  26.963  1.00256.73           N  
ANISOU 4654  N   SER A 637    29322  26359  41866  -6575 -12797   9730       N  
ATOM   4655  CA  SER A 637      79.906  25.327  26.148  1.00255.48           C  
ANISOU 4655  CA  SER A 637    29041  26236  41794  -6449 -12543   9449       C  
ATOM   4656  C   SER A 637      79.248  25.489  24.783  1.00251.53           C  
ANISOU 4656  C   SER A 637    28331  25784  41457  -6095 -12018   8778       C  
ATOM   4657  O   SER A 637      79.036  24.502  24.070  1.00252.15           O  
ANISOU 4657  O   SER A 637    27978  25625  42201  -5741 -11893   8552       O  
ATOM   4658  CB  SER A 637      81.362  24.883  25.988  1.00259.17           C  
ANISOU 4658  CB  SER A 637    29033  26344  43096  -6284 -12770   9720       C  
ATOM   4659  OG  SER A 637      81.451  23.673  25.255  1.00260.95           O  
ANISOU 4659  OG  SER A 637    28706  26191  44251  -5882 -12693   9557       O  
ATOM   4660  N   PHE A 638      78.931  26.726  24.406  1.00249.41           N  
ANISOU 4660  N   PHE A 638    28368  25811  40584  -6191 -11719   8455       N  
ATOM   4661  CA  PHE A 638      78.235  27.027  23.159  1.00244.76           C  
ANISOU 4661  CA  PHE A 638    27647  25321  40027  -5905 -11238   7834       C  
ATOM   4662  C   PHE A 638      79.119  27.945  22.325  1.00243.75           C  
ANISOU 4662  C   PHE A 638    27349  25236  40028  -5799 -11031   7609       C  
ATOM   4663  O   PHE A 638      79.388  29.083  22.726  1.00243.18           O  
ANISOU 4663  O   PHE A 638    27678  25359  39361  -6087 -11064   7718       O  
ATOM   4664  CB  PHE A 638      76.876  27.676  23.438  1.00241.07           C  
ANISOU 4664  CB  PHE A 638    27739  25166  38691  -6130 -11050   7634       C  
ATOM   4665  CG  PHE A 638      75.891  26.765  24.132  1.00241.75           C  
ANISOU 4665  CG  PHE A 638    27961  25247  38645  -6218 -11198   7798       C  
ATOM   4666  CD1 PHE A 638      76.074  25.390  24.139  1.00244.53           C  
ANISOU 4666  CD1 PHE A 638    27885  25308  39719  -5998 -11397   7975       C  
ATOM   4667  CD2 PHE A 638      74.791  27.288  24.792  1.00239.93           C  
ANISOU 4667  CD2 PHE A 638    28298  25292  37571  -6534 -11135   7780       C  
ATOM   4668  CE1 PHE A 638      75.176  24.556  24.780  1.00245.30           C  
ANISOU 4668  CE1 PHE A 638    28110  25406  39686  -6092 -11549   8151       C  
ATOM   4669  CE2 PHE A 638      73.889  26.457  25.435  1.00240.70           C  
ANISOU 4669  CE2 PHE A 638    28510  25414  37533  -6636 -11268   7942       C  
ATOM   4670  CZ  PHE A 638      74.082  25.090  25.429  1.00243.35           C  
ANISOU 4670  CZ  PHE A 638    28409  25474  38579  -6416 -11486   8141       C  
ATOM   4671  N   SER A 639      79.564  27.455  21.169  1.00239.56           N  
ANISOU 4671  N   SER A 639    26232  24533  40257  -5393 -10810   7285       N  
ATOM   4672  CA  SER A 639      80.577  28.123  20.363  1.00239.65           C  
ANISOU 4672  CA  SER A 639    25965  24558  40534  -5270 -10643   7115       C  
ATOM   4673  C   SER A 639      79.971  28.749  19.111  1.00235.03           C  
ANISOU 4673  C   SER A 639    25309  24193  39798  -5066 -10169   6506       C  
ATOM   4674  O   SER A 639      78.963  28.273  18.582  1.00232.23           O  
ANISOU 4674  O   SER A 639    24880  23869  39487  -4867  -9949   6158       O  
ATOM   4675  CB  SER A 639      81.685  27.143  19.962  1.00243.92           C  
ANISOU 4675  CB  SER A 639    25858  24748  42074  -4977 -10728   7194       C  
ATOM   4676  OG  SER A 639      81.187  26.135  19.098  1.00244.20           O  
ANISOU 4676  OG  SER A 639    25468  24635  42684  -4591 -10490   6798       O  
ATOM   4677  N   LEU A 640      80.615  29.811  18.630  1.00227.37           N  
ANISOU 4677  N   LEU A 640    24354  23375  38662  -5118 -10030   6395       N  
ATOM   4678  CA  LEU A 640      80.134  30.535  17.461  1.00224.51           C  
ANISOU 4678  CA  LEU A 640    24067  23281  37954  -4829  -9470   5827       C  
ATOM   4679  C   LEU A 640      80.439  29.778  16.174  1.00225.41           C  
ANISOU 4679  C   LEU A 640    23514  23300  38831  -4365  -9154   5405       C  
ATOM   4680  O   LEU A 640      81.401  29.009  16.088  1.00228.24           O  
ANISOU 4680  O   LEU A 640    23259  23381  40080  -4329  -9403   5564       O  
ATOM   4681  CB  LEU A 640      80.755  31.930  17.396  1.00223.91           C  
ANISOU 4681  CB  LEU A 640    24293  23419  37363  -4992  -9383   5861       C  
ATOM   4682  CG  LEU A 640      80.290  32.914  18.468  1.00223.11           C  
ANISOU 4682  CG  LEU A 640    24949  23479  36345  -5398  -9545   6119       C  
ATOM   4683  CD1 LEU A 640      81.076  34.211  18.395  1.00223.12           C  
ANISOU 4683  CD1 LEU A 640    25170  23631  35975  -5567  -9526   6189       C  
ATOM   4684  CD2 LEU A 640      78.798  33.181  18.336  1.00220.47           C  
ANISOU 4684  CD2 LEU A 640    25110  23366  35293  -5244  -9151   5753       C  
ATOM   4685  N   ASN A 641      79.608  30.020  15.162  1.00220.52           N  
ANISOU 4685  N   ASN A 641    23017  22912  37857  -4019  -8595   4856       N  
ATOM   4686  CA  ASN A 641      79.728  29.320  13.892  1.00220.43           C  
ANISOU 4686  CA  ASN A 641    22443  22855  38456  -3588  -8233   4387       C  
ATOM   4687  C   ASN A 641      80.925  29.834  13.100  1.00221.59           C  
ANISOU 4687  C   ASN A 641    22216  23073  38905  -3507  -8068   4259       C  
ATOM   4688  O   ASN A 641      81.353  30.982  13.249  1.00220.39           O  
ANISOU 4688  O   ASN A 641    22367  23112  38261  -3708  -8070   4391       O  
ATOM   4689  CB  ASN A 641      78.451  29.491  13.070  1.00216.76           C  
ANISOU 4689  CB  ASN A 641    22268  22640  37449  -3295  -7705   3869       C  
ATOM   4690  CG  ASN A 641      78.384  28.548  11.885  1.00217.13           C  
ANISOU 4690  CG  ASN A 641    21770  22610  38122  -2882  -7374   3396       C  
ATOM   4691  OD1 ASN A 641      79.298  27.757  11.650  1.00219.84           O  
ANISOU 4691  OD1 ASN A 641    21494  22704  39330  -2789  -7512   3416       O  
ATOM   4692  ND2 ASN A 641      77.297  28.630  11.128  1.00216.16           N  
ANISOU 4692  ND2 ASN A 641    21868  22691  37573  -2639  -6934   2959       N  
ATOM   4693  N   MET A 642      81.456  28.969  12.237  1.00216.88           N  
ANISOU 4693  N   MET A 642    20949  22325  39132  -3212  -7914   3982       N  
ATOM   4694  CA  MET A 642      82.606  29.294  11.405  1.00218.78           C  
ANISOU 4694  CA  MET A 642    20736  22631  39759  -3111  -7721   3817       C  
ATOM   4695  C   MET A 642      82.261  29.453   9.930  1.00217.01           C  
ANISOU 4695  C   MET A 642    20385  22679  39390  -2755  -7074   3158       C  
ATOM   4696  O   MET A 642      83.160  29.739   9.131  1.00218.32           O  
ANISOU 4696  O   MET A 642    20175  22952  39825  -2669  -6849   2963       O  
ATOM   4697  CB  MET A 642      83.692  28.223  11.565  1.00223.05           C  
ANISOU 4697  CB  MET A 642    20532  22779  41440  -3081  -8052   4020       C  
ATOM   4698  CG  MET A 642      84.369  28.196  12.930  1.00224.78           C  
ANISOU 4698  CG  MET A 642    20895  22749  41762  -3427  -8643   4708       C  
ATOM   4699  SD  MET A 642      85.303  29.698  13.297  1.00224.45           S  
ANISOU 4699  SD  MET A 642    21137  22930  41215  -3792  -8795   5058       S  
ATOM   4700  CE  MET A 642      84.228  30.506  14.478  1.00220.42           C  
ANISOU 4700  CE  MET A 642    21502  22573  39675  -4208  -9080   5391       C  
ATOM   4701  N   ASN A 643      80.999  29.281   9.544  1.00213.23           N  
ANISOU 4701  N   ASN A 643    20205  22325  38488  -2571  -6776   2821       N  
ATOM   4702  CA  ASN A 643      80.613  29.433   8.146  1.00212.57           C  
ANISOU 4702  CA  ASN A 643    20033  22509  38222  -2274  -6181   2214       C  
ATOM   4703  C   ASN A 643      79.098  29.553   8.062  1.00211.60           C  
ANISOU 4703  C   ASN A 643    20442  22544  37411  -2187  -5964   2009       C  
ATOM   4704  O   ASN A 643      78.372  29.113   8.959  1.00210.40           O  
ANISOU 4704  O   ASN A 643    20546  22230  37166  -2272  -6243   2257       O  
ATOM   4705  CB  ASN A 643      81.102  28.258   7.292  1.00214.53           C  
ANISOU 4705  CB  ASN A 643    19546  22569  39396  -1976  -6000   1851       C  
ATOM   4706  CG  ASN A 643      81.001  28.536   5.804  1.00214.29           C  
ANISOU 4706  CG  ASN A 643    19376  22856  39187  -1739  -5387   1240       C  
ATOM   4707  OD1 ASN A 643      80.592  29.620   5.389  1.00212.40           O  
ANISOU 4707  OD1 ASN A 643    19573  22975  38156  -1803  -5120   1116       O  
ATOM   4708  ND2 ASN A 643      81.368  27.551   4.992  1.00217.61           N  
ANISOU 4708  ND2 ASN A 643    19184  23144  40353  -1481  -5167    851       N  
ATOM   4709  N   PHE A 644      78.637  30.160   6.970  1.00208.05           N  
ANISOU 4709  N   PHE A 644    20144  22421  36487  -2035  -5471   1570       N  
ATOM   4710  CA  PHE A 644      77.214  30.256   6.645  1.00208.59           C  
ANISOU 4710  CA  PHE A 644    20638  22652  35966  -1910  -5198   1307       C  
ATOM   4711  C   PHE A 644      76.429  30.993   7.727  1.00209.39           C  
ANISOU 4711  C   PHE A 644    21412  22802  35345  -2142  -5426   1656       C  
ATOM   4712  O   PHE A 644      75.443  31.673   7.439  1.00209.74           O  
ANISOU 4712  O   PHE A 644    21910  23077  34705  -2109  -5170   1481       O  
ATOM   4713  CB  PHE A 644      76.623  28.861   6.425  1.00207.01           C  
ANISOU 4713  CB  PHE A 644    20136  22224  36294  -1669  -5165   1090       C  
ATOM   4714  CG  PHE A 644      77.187  28.142   5.231  1.00206.09           C  
ANISOU 4714  CG  PHE A 644    19405  22084  36815  -1412  -4849    632       C  
ATOM   4715  CD1 PHE A 644      77.869  28.835   4.243  1.00206.75           C  
ANISOU 4715  CD1 PHE A 644    19324  22441  36790  -1389  -4504    354       C  
ATOM   4716  CD2 PHE A 644      77.049  26.770   5.104  1.00204.77           C  
ANISOU 4716  CD2 PHE A 644    18819  21623  37363  -1208  -4901    474       C  
ATOM   4717  CE1 PHE A 644      78.395  28.174   3.151  1.00206.53           C  
ANISOU 4717  CE1 PHE A 644    18728  22415  37328  -1175  -4184    -97       C  
ATOM   4718  CE2 PHE A 644      77.571  26.103   4.012  1.00205.69           C  
ANISOU 4718  CE2 PHE A 644    18369  21708  38076   -974  -4589     10       C  
ATOM   4719  CZ  PHE A 644      78.245  26.807   3.034  1.00206.20           C  
ANISOU 4719  CZ  PHE A 644    18277  22068  38000   -960  -4215   -287       C  
ATOM   4720  N   THR A 661      51.761  24.071  13.645  1.00178.55           N  
ANISOU 4720  N   THR A 661    21751  19573  26517  -1582  -4630   2092       N  
ATOM   4721  CA  THR A 661      50.839  23.824  12.538  1.00176.84           C  
ANISOU 4721  CA  THR A 661    21450  19370  26371  -1279  -4358   1828       C  
ATOM   4722  C   THR A 661      49.782  22.726  12.790  1.00174.13           C  
ANISOU 4722  C   THR A 661    21015  18996  26150  -1280  -4490   1997       C  
ATOM   4723  O   THR A 661      48.678  22.825  12.257  1.00173.61           O  
ANISOU 4723  O   THR A 661    21034  19030  25901  -1114  -4226   1856       O  
ATOM   4724  CB  THR A 661      51.610  23.490  11.233  1.00174.64           C  
ANISOU 4724  CB  THR A 661    20844  18927  26584  -1027  -4306   1537       C  
ATOM   4725  OG1 THR A 661      52.437  22.336  11.423  1.00172.56           O  
ANISOU 4725  OG1 THR A 661    20224  18415  26924  -1078  -4689   1687       O  
ATOM   4726  CG2 THR A 661      52.475  24.670  10.810  1.00176.09           C  
ANISOU 4726  CG2 THR A 661    21131  19187  26589  -1003  -4110   1339       C  
ATOM   4727  N   PRO A 662      50.093  21.668  13.581  1.00172.47           N  
ANISOU 4727  N   PRO A 662    20623  18642  26267  -1475  -4917   2320       N  
ATOM   4728  CA  PRO A 662      49.008  20.766  13.996  1.00170.41           C  
ANISOU 4728  CA  PRO A 662    20333  18397  26018  -1534  -5050   2531       C  
ATOM   4729  C   PRO A 662      48.102  21.420  15.028  1.00174.26           C  
ANISOU 4729  C   PRO A 662    21190  19161  25861  -1760  -4921   2707       C  
ATOM   4730  O   PRO A 662      46.871  21.385  14.909  1.00176.15           O  
ANISOU 4730  O   PRO A 662    21529  19532  25869  -1677  -4717   2676       O  
ATOM   4731  CB  PRO A 662      49.752  19.555  14.575  1.00167.63           C  
ANISOU 4731  CB  PRO A 662    19678  17801  26213  -1712  -5576   2843       C  
ATOM   4732  CG  PRO A 662      51.057  20.089  15.012  1.00169.32           C  
ANISOU 4732  CG  PRO A 662    19902  17964  26467  -1878  -5722   2914       C  
ATOM   4733  CD  PRO A 662      51.407  21.158  14.023  1.00171.26           C  
ANISOU 4733  CD  PRO A 662    20235  18281  26553  -1635  -5315   2511       C  
ATOM   4734  N   GLN A 663      48.716  22.047  16.035  1.00167.84           N  
ANISOU 4734  N   GLN A 663    20579  18439  24753  -2053  -5026   2879       N  
ATOM   4735  CA  GLN A 663      47.946  22.727  17.070  1.00172.33           C  
ANISOU 4735  CA  GLN A 663    21512  19281  24687  -2297  -4881   3009       C  
ATOM   4736  C   GLN A 663      47.231  23.948  16.502  1.00176.50           C  
ANISOU 4736  C   GLN A 663    22298  19984  24781  -2081  -4363   2669       C  
ATOM   4737  O   GLN A 663      46.107  24.267  16.914  1.00178.23           O  
ANISOU 4737  O   GLN A 663    22724  20403  24593  -2125  -4137   2678       O  
ATOM   4738  CB  GLN A 663      48.872  23.112  18.224  1.00173.55           C  
ANISOU 4738  CB  GLN A 663    21826  19476  24640  -2681  -5130   3252       C  
ATOM   4739  CG  GLN A 663      48.173  23.678  19.442  1.00177.74           C  
ANISOU 4739  CG  GLN A 663    22724  20290  24521  -3008  -5029   3407       C  
ATOM   4740  CD  GLN A 663      49.131  23.950  20.585  1.00179.31           C  
ANISOU 4740  CD  GLN A 663    23076  20520  24534  -3434  -5324   3672       C  
ATOM   4741  OE1 GLN A 663      50.340  23.751  20.458  1.00177.43           O  
ANISOU 4741  OE1 GLN A 663    22660  20080  24676  -3471  -5611   3757       O  
ATOM   4742  NE2 GLN A 663      48.595  24.405  21.711  1.00182.20           N  
ANISOU 4742  NE2 GLN A 663    23770  21144  24315  -3772  -5251   3804       N  
ATOM   4743  N   GLU A 664      47.868  24.631  15.545  1.00171.58           N  
ANISOU 4743  N   GLU A 664    21646  19284  24263  -1852  -4176   2374       N  
ATOM   4744  CA  GLU A 664      47.220  25.729  14.833  1.00174.53           C  
ANISOU 4744  CA  GLU A 664    22214  19781  24319  -1626  -3723   2057       C  
ATOM   4745  C   GLU A 664      45.865  25.302  14.285  1.00173.58           C  
ANISOU 4745  C   GLU A 664    22036  19709  24209  -1425  -3532   1989       C  
ATOM   4746  O   GLU A 664      44.863  26.008  14.445  1.00175.90           O  
ANISOU 4746  O   GLU A 664    22553  20170  24110  -1395  -3230   1911       O  
ATOM   4747  CB  GLU A 664      48.123  26.217  13.697  1.00173.83           C  
ANISOU 4747  CB  GLU A 664    22011  19578  24459  -1409  -3619   1781       C  
ATOM   4748  CG  GLU A 664      49.426  26.850  14.153  1.00174.78           C  
ANISOU 4748  CG  GLU A 664    22212  19669  24528  -1588  -3756   1825       C  
ATOM   4749  CD  GLU A 664      49.214  28.172  14.859  1.00179.62           C  
ANISOU 4749  CD  GLU A 664    23225  20461  24563  -1738  -3544   1789       C  
ATOM   4750  OE1 GLU A 664      48.251  28.886  14.507  1.00182.83           O  
ANISOU 4750  OE1 GLU A 664    23804  20981  24681  -1589  -3197   1597       O  
ATOM   4751  OE2 GLU A 664      50.011  28.498  15.764  1.00180.39           O  
ANISOU 4751  OE2 GLU A 664    23457  20570  24512  -2012  -3731   1951       O  
ATOM   4752  N   MET A 665      45.816  24.135  13.638  1.00171.23           N  
ANISOU 4752  N   MET A 665    21428  19252  24381  -1288  -3711   2016       N  
ATOM   4753  CA  MET A 665      44.545  23.620  13.141  1.00169.44           C  
ANISOU 4753  CA  MET A 665    21134  19056  24188  -1122  -3579   1989       C  
ATOM   4754  C   MET A 665      43.644  23.191  14.293  1.00169.55           C  
ANISOU 4754  C   MET A 665    21249  19213  23961  -1350  -3678   2290       C  
ATOM   4755  O   MET A 665      42.419  23.375  14.236  1.00170.77           O  
ANISOU 4755  O   MET A 665    21501  19505  23880  -1274  -3436   2264       O  
ATOM   4756  CB  MET A 665      44.788  22.451  12.185  1.00165.53           C  
ANISOU 4756  CB  MET A 665    20289  18339  24266   -940  -3768   1931       C  
ATOM   4757  CG  MET A 665      45.675  22.775  10.982  1.00164.38           C  
ANISOU 4757  CG  MET A 665    20012  18073  24370   -729  -3655   1611       C  
ATOM   4758  SD  MET A 665      45.092  24.124   9.933  1.00166.39           S  
ANISOU 4758  SD  MET A 665    20475  18478  24269   -512  -3165   1272       S  
ATOM   4759  CE  MET A 665      46.227  25.424  10.409  1.00169.19           C  
ANISOU 4759  CE  MET A 665    21037  18900  24348   -648  -3103   1214       C  
ATOM   4760  N   GLU A 666      44.240  22.624  15.350  1.00170.10           N  
ANISOU 4760  N   GLU A 666    21286  19258  24088  -1650  -4039   2590       N  
ATOM   4761  CA  GLU A 666      43.471  22.185  16.512  1.00171.31           C  
ANISOU 4761  CA  GLU A 666    21532  19573  23986  -1931  -4164   2905       C  
ATOM   4762  C   GLU A 666      42.592  23.304  17.058  1.00175.94           C  
ANISOU 4762  C   GLU A 666    22455  20437  23958  -1999  -3771   2814       C  
ATOM   4763  O   GLU A 666      41.378  23.132  17.219  1.00176.30           O  
ANISOU 4763  O   GLU A 666    22536  20626  23825  -1985  -3615   2869       O  
ATOM   4764  CB  GLU A 666      44.415  21.669  17.599  1.00170.52           C  
ANISOU 4764  CB  GLU A 666    21395  19422  23973  -2298  -4607   3236       C  
ATOM   4765  CG  GLU A 666      45.113  20.368  17.254  1.00165.95           C  
ANISOU 4765  CG  GLU A 666    20443  18553  24058  -2267  -5049   3391       C  
ATOM   4766  CD  GLU A 666      46.119  19.955  18.307  1.00165.74           C  
ANISOU 4766  CD  GLU A 666    20370  18453  24151  -2640  -5507   3736       C  
ATOM   4767  OE1 GLU A 666      46.359  20.749  19.242  1.00169.03           O  
ANISOU 4767  OE1 GLU A 666    21067  19053  24102  -2925  -5465   3829       O  
ATOM   4768  OE2 GLU A 666      46.674  18.842  18.198  1.00162.44           O  
ANISOU 4768  OE2 GLU A 666    19632  17781  24307  -2658  -5919   3914       O  
ATOM   4769  N   GLN A 667      43.185  24.463  17.349  1.00172.87           N  
ANISOU 4769  N   GLN A 667    22307  20117  23259  -2072  -3604   2669       N  
ATOM   4770  CA  GLN A 667      42.370  25.591  17.788  1.00176.08           C  
ANISOU 4770  CA  GLN A 667    23022  20751  23128  -2103  -3203   2525       C  
ATOM   4771  C   GLN A 667      41.742  26.366  16.636  1.00176.64           C  
ANISOU 4771  C   GLN A 667    23113  20801  23201  -1729  -2802   2188       C  
ATOM   4772  O   GLN A 667      40.905  27.241  16.886  1.00179.21           O  
ANISOU 4772  O   GLN A 667    23647  21283  23161  -1705  -2455   2057       O  
ATOM   4773  CB  GLN A 667      43.184  26.540  18.674  1.00178.16           C  
ANISOU 4773  CB  GLN A 667    23565  21099  23027  -2369  -3196   2513       C  
ATOM   4774  CG  GLN A 667      43.361  26.052  20.110  1.00178.31           C  
ANISOU 4774  CG  GLN A 667    23682  21254  22815  -2829  -3484   2856       C  
ATOM   4775  CD  GLN A 667      44.481  25.046  20.267  1.00175.51           C  
ANISOU 4775  CD  GLN A 667    23098  20710  22878  -2995  -4006   3140       C  
ATOM   4776  OE1 GLN A 667      45.349  24.934  19.407  1.00173.89           O  
ANISOU 4776  OE1 GLN A 667    22703  20279  23087  -2787  -4120   3036       O  
ATOM   4777  NE2 GLN A 667      44.466  24.307  21.371  1.00174.25           N  
ANISOU 4777  NE2 GLN A 667    22939  20642  22624  -3386  -4329   3506       N  
ATOM   4778  N   THR A 668      42.116  26.074  15.387  1.00163.79           N  
ANISOU 4778  N   THR A 668    21269  18983  21982  -1454  -2842   2045       N  
ATOM   4779  CA  THR A 668      41.400  26.643  14.252  1.00163.12           C  
ANISOU 4779  CA  THR A 668    21175  18883  21918  -1135  -2509   1780       C  
ATOM   4780  C   THR A 668      40.033  25.992  14.068  1.00161.62           C  
ANISOU 4780  C   THR A 668    20882  18752  21773  -1036  -2424   1867       C  
ATOM   4781  O   THR A 668      39.136  26.605  13.479  1.00161.84           O  
ANISOU 4781  O   THR A 668    20965  18827  21699   -841  -2111   1705       O  
ATOM   4782  CB  THR A 668      42.245  26.506  12.977  1.00160.83           C  
ANISOU 4782  CB  THR A 668    20692  18402  22015   -919  -2578   1598       C  
ATOM   4783  OG1 THR A 668      43.502  27.167  13.166  1.00163.13           O  
ANISOU 4783  OG1 THR A 668    21074  18654  22256  -1017  -2646   1530       O  
ATOM   4784  CG2 THR A 668      41.550  27.135  11.775  1.00159.53           C  
ANISOU 4784  CG2 THR A 668    20532  18234  21849   -637  -2259   1345       C  
ATOM   4785  N   ARG A 669      39.841  24.782  14.600  1.00165.76           N  
ANISOU 4785  N   ARG A 669    21258  19273  22451  -1185  -2714   2144       N  
ATOM   4786  CA  ARG A 669      38.574  24.067  14.465  1.00165.31           C  
ANISOU 4786  CA  ARG A 669    21087  19270  22454  -1115  -2679   2266       C  
ATOM   4787  C   ARG A 669      37.399  24.742  15.175  1.00168.74           C  
ANISOU 4787  C   ARG A 669    21718  19944  22452  -1186  -2358   2281       C  
ATOM   4788  O   ARG A 669      36.287  24.205  15.107  1.00167.96           O  
ANISOU 4788  O   ARG A 669    21523  19911  22382  -1137  -2308   2396       O  
ATOM   4789  CB  ARG A 669      38.723  22.640  14.996  1.00163.33           C  
ANISOU 4789  CB  ARG A 669    20638  18959  22461  -1302  -3106   2590       C  
ATOM   4790  CG  ARG A 669      39.641  21.748  14.178  1.00159.18           C  
ANISOU 4790  CG  ARG A 669    19846  18161  22473  -1184  -3416   2565       C  
ATOM   4791  CD  ARG A 669      39.728  20.361  14.795  1.00156.85           C  
ANISOU 4791  CD  ARG A 669    19353  17785  22458  -1384  -3863   2908       C  
ATOM   4792  NE  ARG A 669      40.636  19.483  14.064  1.00152.90           N  
ANISOU 4792  NE  ARG A 669    18574  16994  22525  -1269  -4164   2865       N  
ATOM   4793  CZ  ARG A 669      40.929  18.242  14.436  1.00149.93           C  
ANISOU 4793  CZ  ARG A 669    17975  16465  22526  -1408  -4601   3132       C  
ATOM   4794  NH1 ARG A 669      40.384  17.731  15.532  1.00150.95           N  
ANISOU 4794  NH1 ARG A 669    18139  16725  22490  -1693  -4806   3490       N  
ATOM   4795  NH2 ARG A 669      41.767  17.510  13.714  1.00145.90           N  
ANISOU 4795  NH2 ARG A 669    17198  15669  22567  -1273  -4836   3038       N  
ATOM   4796  N   SER A 670      37.593  25.877  15.849  1.00138.31           N  
ANISOU 4796  N   SER A 670    18124  16217  18210  -1301  -2137   2163       N  
ATOM   4797  CA  SER A 670      36.517  26.546  16.578  1.00141.65           C  
ANISOU 4797  CA  SER A 670    18726  16863  18230  -1376  -1805   2136       C  
ATOM   4798  C   SER A 670      35.933  27.734  15.827  1.00143.27           C  
ANISOU 4798  C   SER A 670    19023  17049  18365  -1098  -1393   1833       C  
ATOM   4799  O   SER A 670      34.720  27.985  15.906  1.00145.67           O  
ANISOU 4799  O   SER A 670    19335  17466  18548  -1020  -1117   1808       O  
ATOM   4800  CB  SER A 670      37.018  27.015  17.947  1.00143.98           C  
ANISOU 4800  CB  SER A 670    19267  17324  18116  -1728  -1819   2197       C  
ATOM   4801  OG  SER A 670      37.988  28.038  17.808  1.00145.57           O  
ANISOU 4801  OG  SER A 670    19639  17443  18229  -1702  -1747   1979       O  
ATOM   4802  N   ALA A 671      36.775  28.482  15.108  1.00130.99           N  
ANISOU 4802  N   ALA A 671    17523  15350  16898   -957  -1356   1615       N  
ATOM   4803  CA  ALA A 671      36.274  29.579  14.289  1.00132.55           C  
ANISOU 4803  CA  ALA A 671    17783  15498  17081   -702  -1022   1355       C  
ATOM   4804  C   ALA A 671      35.237  29.092  13.289  1.00131.23           C  
ANISOU 4804  C   ALA A 671    17409  15276  17176   -464   -953   1379       C  
ATOM   4805  O   ALA A 671      34.343  29.853  12.903  1.00133.52           O  
ANISOU 4805  O   ALA A 671    17732  15576  17422   -299   -656   1251       O  
ATOM   4806  CB  ALA A 671      37.431  30.270  13.569  1.00131.29           C  
ANISOU 4806  CB  ALA A 671    17674  15191  17017   -614  -1066   1164       C  
ATOM   4807  N   VAL A 672      35.332  27.829  12.866  1.00123.00           N  
ANISOU 4807  N   VAL A 672    16148  14160  16426   -450  -1236   1547       N  
ATOM   4808  CA  VAL A 672      34.278  27.242  12.045  1.00120.81           C  
ANISOU 4808  CA  VAL A 672    15687  13845  16372   -270  -1202   1608       C  
ATOM   4809  C   VAL A 672      32.980  27.158  12.835  1.00123.15           C  
ANISOU 4809  C   VAL A 672    15999  14318  16476   -338  -1027   1753       C  
ATOM   4810  O   VAL A 672      31.895  27.433  12.309  1.00123.44           O  
ANISOU 4810  O   VAL A 672    15978  14361  16563   -168   -809   1721       O  
ATOM   4811  CB  VAL A 672      34.710  25.857  11.528  1.00116.16           C  
ANISOU 4811  CB  VAL A 672    14871  13127  16138   -267  -1562   1747       C  
ATOM   4812  CG1 VAL A 672      33.590  25.217  10.722  1.00112.84           C  
ANISOU 4812  CG1 VAL A 672    14277  12669  15927   -107  -1543   1823       C  
ATOM   4813  CG2 VAL A 672      35.979  25.969  10.707  1.00114.52           C  
ANISOU 4813  CG2 VAL A 672    14623  12756  16133   -192  -1689   1569       C  
ATOM   4814  N   ASP A 673      33.072  26.785  14.113  1.00120.44           N  
ANISOU 4814  N   ASP A 673    15725  14129  15909   -606  -1123   1923       N  
ATOM   4815  CA  ASP A 673      31.877  26.674  14.942  1.00123.53           C  
ANISOU 4815  CA  ASP A 673    16124  14728  16084   -710   -947   2060       C  
ATOM   4816  C   ASP A 673      31.195  28.027  15.104  1.00128.10           C  
ANISOU 4816  C   ASP A 673    16857  15388  16426   -611   -497   1829       C  
ATOM   4817  O   ASP A 673      29.990  28.166  14.847  1.00130.20           O  
ANISOU 4817  O   ASP A 673    17035  15699  16737   -470   -266   1833       O  
ATOM   4818  CB  ASP A 673      32.245  26.081  16.304  1.00124.48           C  
ANISOU 4818  CB  ASP A 673    16312  15018  15966  -1072  -1150   2283       C  
ATOM   4819  CG  ASP A 673      31.029  25.756  17.150  1.00126.86           C  
ANISOU 4819  CG  ASP A 673    16588  15565  16050  -1221  -1009   2461       C  
ATOM   4820  OD1 ASP A 673      30.354  24.744  16.861  1.00124.77           O  
ANISOU 4820  OD1 ASP A 673    16115  15295  15995  -1187  -1168   2683       O  
ATOM   4821  OD2 ASP A 673      30.753  26.512  18.105  1.00130.54           O  
ANISOU 4821  OD2 ASP A 673    17237  16232  16130  -1381   -735   2371       O  
ATOM   4822  N   GLU A 674      31.954  29.050  15.509  1.00128.54           N  
ANISOU 4822  N   GLU A 674    17135  15446  16260   -678   -377   1624       N  
ATOM   4823  CA  GLU A 674      31.317  30.347  15.722  1.00132.85           C  
ANISOU 4823  CA  GLU A 674    17825  16044  16608   -588     45   1385       C  
ATOM   4824  C   GLU A 674      30.880  30.985  14.408  1.00132.21           C  
ANISOU 4824  C   GLU A 674    17653  15776  16806   -256    201   1225       C  
ATOM   4825  O   GLU A 674      29.860  31.683  14.373  1.00135.89           O  
ANISOU 4825  O   GLU A 674    18110  16264  17258   -125    524   1120       O  
ATOM   4826  CB  GLU A 674      32.240  31.285  16.502  1.00135.30           C  
ANISOU 4826  CB  GLU A 674    18409  16389  16609   -759    118   1204       C  
ATOM   4827  CG  GLU A 674      31.572  32.605  16.881  1.00140.63           C  
ANISOU 4827  CG  GLU A 674    19243  17115  17076   -692    558    936       C  
ATOM   4828  CD  GLU A 674      32.419  33.458  17.805  1.00142.32           C  
ANISOU 4828  CD  GLU A 674    19751  17384  16940   -908    626    764       C  
ATOM   4829  OE1 GLU A 674      33.532  33.025  18.166  1.00139.16           O  
ANISOU 4829  OE1 GLU A 674    19430  16992  16453  -1123    318    882       O  
ATOM   4830  OE2 GLU A 674      31.967  34.564  18.172  1.00145.67           O  
ANISOU 4830  OE2 GLU A 674    20323  17831  17194   -867    981    511       O  
ATOM   4831  N   ASP A 675      31.618  30.751  13.318  1.00129.44           N  
ANISOU 4831  N   ASP A 675    17220  15243  16718   -132    -23   1209       N  
ATOM   4832  CA  ASP A 675      31.156  31.214  12.013  1.00128.46           C  
ANISOU 4832  CA  ASP A 675    16995  14962  16852    136     81   1106       C  
ATOM   4833  C   ASP A 675      29.851  30.538  11.611  1.00126.92           C  
ANISOU 4833  C   ASP A 675    16593  14789  16840    246    123   1276       C  
ATOM   4834  O   ASP A 675      29.007  31.161  10.956  1.00126.97           O  
ANISOU 4834  O   ASP A 675    16541  14726  16977    429    327   1209       O  
ATOM   4835  CB  ASP A 675      32.227  30.979  10.946  1.00124.71           C  
ANISOU 4835  CB  ASP A 675    16467  14327  16591    201   -170   1057       C  
ATOM   4836  CG  ASP A 675      33.384  31.957  11.054  1.00126.74           C  
ANISOU 4836  CG  ASP A 675    16914  14531  16709    152   -155    860       C  
ATOM   4837  OD1 ASP A 675      33.164  33.094  11.523  1.00131.53           O  
ANISOU 4837  OD1 ASP A 675    17688  15162  17126    156     97    708       O  
ATOM   4838  OD2 ASP A 675      34.513  31.592  10.662  1.00124.26           O  
ANISOU 4838  OD2 ASP A 675    16574  14146  16494    110   -394    851       O  
ATOM   4839  N   ARG A 676      29.664  29.272  11.992  1.00121.85           N  
ANISOU 4839  N   ARG A 676    15831  14235  16232    125    -90   1515       N  
ATOM   4840  CA  ARG A 676      28.375  28.628  11.764  1.00121.10           C  
ANISOU 4840  CA  ARG A 676    15550  14184  16279    200    -50   1702       C  
ATOM   4841  C   ARG A 676      27.283  29.266  12.610  1.00127.12           C  
ANISOU 4841  C   ARG A 676    16348  15106  16844    183    306   1681       C  
ATOM   4842  O   ARG A 676      26.148  29.428  12.146  1.00127.99           O  
ANISOU 4842  O   ARG A 676    16327  15196  17108    339    479   1721       O  
ATOM   4843  CB  ARG A 676      28.460  27.131  12.055  1.00117.60           C  
ANISOU 4843  CB  ARG A 676    14975  13793  15916     52   -383   1974       C  
ATOM   4844  CG  ARG A 676      29.238  26.341  11.027  1.00111.60           C  
ANISOU 4844  CG  ARG A 676    14106  12846  15451    119   -711   1992       C  
ATOM   4845  CD  ARG A 676      29.216  24.862  11.352  1.00110.67           C  
ANISOU 4845  CD  ARG A 676    13840  12750  15459    -19  -1046   2264       C  
ATOM   4846  NE  ARG A 676      29.925  24.069  10.355  1.00106.89           N  
ANISOU 4846  NE  ARG A 676    13239  12073  15301     57  -1342   2246       N  
ATOM   4847  CZ  ARG A 676      30.079  22.752  10.429  1.00105.57           C  
ANISOU 4847  CZ  ARG A 676    12924  11852  15336    -32  -1680   2445       C  
ATOM   4848  NH1 ARG A 676      29.573  22.083  11.457  1.00107.63           N  
ANISOU 4848  NH1 ARG A 676    13145  12256  15494   -218  -1789   2711       N  
ATOM   4849  NH2 ARG A 676      30.736  22.104   9.478  1.00102.40           N  
ANISOU 4849  NH2 ARG A 676    12408  11254  15246     54  -1911   2371       N  
ATOM   4850  N   LYS A 677      27.599  29.626  13.858  1.00126.26           N  
ANISOU 4850  N   LYS A 677    16410  15161  16403    -18    423   1617       N  
ATOM   4851  CA  LYS A 677      26.610  30.311  14.687  1.00131.10           C  
ANISOU 4851  CA  LYS A 677    17064  15935  16813    -42    809   1535       C  
ATOM   4852  C   LYS A 677      26.197  31.642  14.069  1.00132.28           C  
ANISOU 4852  C   LYS A 677    17241  15933  17087    205   1122   1278       C  
ATOM   4853  O   LYS A 677      25.007  31.983  14.047  1.00134.25           O  
ANISOU 4853  O   LYS A 677    17373  16209  17429    329   1397   1268       O  
ATOM   4854  CB  LYS A 677      27.155  30.506  16.103  1.00133.73           C  
ANISOU 4854  CB  LYS A 677    17609  16471  16730   -338    871   1477       C  
ATOM   4855  CG  LYS A 677      27.259  29.202  16.881  1.00132.46           C  
ANISOU 4855  CG  LYS A 677    17394  16498  16438   -622    590   1783       C  
ATOM   4856  CD  LYS A 677      27.660  29.402  18.337  1.00134.34           C  
ANISOU 4856  CD  LYS A 677    17845  16974  16225   -968    662   1755       C  
ATOM   4857  CE  LYS A 677      29.150  29.670  18.475  1.00132.90           C  
ANISOU 4857  CE  LYS A 677    17860  16692  15945  -1093    437   1667       C  
ATOM   4858  NZ  LYS A 677      29.590  29.712  19.898  1.00134.14           N  
ANISOU 4858  NZ  LYS A 677    18227  17085  15656  -1486    433   1698       N  
ATOM   4859  N   MET A 678      27.164  32.397  13.543  1.00130.06           N  
ANISOU 4859  N   MET A 678    17095  15484  16840    276   1068   1084       N  
ATOM   4860  CA  MET A 678      26.843  33.662  12.889  1.00131.00           C  
ANISOU 4860  CA  MET A 678    17233  15431  17111    495   1308    865       C  
ATOM   4861  C   MET A 678      26.014  33.436  11.631  1.00128.43           C  
ANISOU 4861  C   MET A 678    16678  14961  17158    713   1262    991       C  
ATOM   4862  O   MET A 678      25.031  34.148  11.389  1.00130.48           O  
ANISOU 4862  O   MET A 678    16849  15151  17576    872   1516    931       O  
ATOM   4863  CB  MET A 678      28.128  34.416  12.549  1.00130.48           C  
ANISOU 4863  CB  MET A 678    17353  15226  16998    492   1202    674       C  
ATOM   4864  CG  MET A 678      29.002  34.740  13.750  1.00133.32           C  
ANISOU 4864  CG  MET A 678    17959  15705  16991    263   1230    551       C  
ATOM   4865  SD  MET A 678      28.243  35.849  14.950  1.00137.52           S  
ANISOU 4865  SD  MET A 678    18639  16348  17264    218   1696    307       S  
ATOM   4866  CE  MET A 678      29.416  35.701  16.296  1.00138.59           C  
ANISOU 4866  CE  MET A 678    19054  16668  16936   -146   1580    275       C  
ATOM   4867  N   TYR A 679      26.395  32.445  10.822  1.00122.14           N  
ANISOU 4867  N   TYR A 679    15779  14111  16519    712    936   1164       N  
ATOM   4868  CA  TYR A 679      25.701  32.195   9.562  1.00117.19           C  
ANISOU 4868  CA  TYR A 679    14961  13349  16219    881    858   1284       C  
ATOM   4869  C   TYR A 679      24.254  31.783   9.811  1.00118.67           C  
ANISOU 4869  C   TYR A 679    14962  13624  16503    927   1004   1469       C  
ATOM   4870  O   TYR A 679      23.323  32.308   9.183  1.00117.93           O  
ANISOU 4870  O   TYR A 679    14745  13424  16638   1088   1151   1486       O  
ATOM   4871  CB  TYR A 679      26.446  31.115   8.777  1.00111.44           C  
ANISOU 4871  CB  TYR A 679    14172  12565  15604    838    490   1401       C  
ATOM   4872  CG  TYR A 679      25.993  30.943   7.348  1.00107.60           C  
ANISOU 4872  CG  TYR A 679    13539  11931  15414    974    384   1477       C  
ATOM   4873  CD1 TYR A 679      26.415  31.823   6.362  1.00105.74           C  
ANISOU 4873  CD1 TYR A 679    13354  11546  15275   1059    391   1326       C  
ATOM   4874  CD2 TYR A 679      25.151  29.904   6.981  1.00106.01           C  
ANISOU 4874  CD2 TYR A 679    13156  11745  15378    989    259   1712       C  
ATOM   4875  CE1 TYR A 679      26.015  31.674   5.052  1.00102.59           C  
ANISOU 4875  CE1 TYR A 679    12837  11032  15112   1136    282   1405       C  
ATOM   4876  CE2 TYR A 679      24.742  29.747   5.671  1.00102.70           C  
ANISOU 4876  CE2 TYR A 679    12622  11195  15204   1080    151   1784       C  
ATOM   4877  CZ  TYR A 679      25.178  30.636   4.711  1.00101.12           C  
ANISOU 4877  CZ  TYR A 679    12483  10863  15076   1144    166   1629       C  
ATOM   4878  OH  TYR A 679      24.778  30.492   3.403  1.00 98.37           O  
ANISOU 4878  OH  TYR A 679    12035  10403  14939   1189     49   1709       O  
ATOM   4879  N   LEU A 680      24.046  30.846  10.739  1.00114.03           N  
ANISOU 4879  N   LEU A 680    14341  13231  15754    770    952   1630       N  
ATOM   4880  CA  LEU A 680      22.692  30.422  11.073  1.00115.77           C  
ANISOU 4880  CA  LEU A 680    14380  13569  16039    787   1095   1820       C  
ATOM   4881  C   LEU A 680      21.892  31.550  11.711  1.00118.40           C  
ANISOU 4881  C   LEU A 680    14722  13953  16313    859   1528   1649       C  
ATOM   4882  O   LEU A 680      20.681  31.640  11.491  1.00119.49           O  
ANISOU 4882  O   LEU A 680    14669  14081  16653    980   1698   1747       O  
ATOM   4883  CB  LEU A 680      22.734  29.204  11.994  1.00116.85           C  
ANISOU 4883  CB  LEU A 680    14490  13920  15985    562    925   2036       C  
ATOM   4884  CG  LEU A 680      23.312  27.934  11.365  1.00114.73           C  
ANISOU 4884  CG  LEU A 680    14154  13579  15860    507    489   2233       C  
ATOM   4885  CD1 LEU A 680      23.412  26.814  12.392  1.00116.21           C  
ANISOU 4885  CD1 LEU A 680    14322  13964  15868    260    299   2454       C  
ATOM   4886  CD2 LEU A 680      22.488  27.498  10.162  1.00113.35           C  
ANISOU 4886  CD2 LEU A 680    13780  13265  16021    671    386   2392       C  
ATOM   4887  N   GLN A 681      22.543  32.412  12.499  1.00122.98           N  
ANISOU 4887  N   GLN A 681    15513  14577  16638    785   1710   1389       N  
ATOM   4888  CA  GLN A 681      21.880  33.615  13.001  1.00126.38           C  
ANISOU 4888  CA  GLN A 681    15963  15004  17052    878   2134   1156       C  
ATOM   4889  C   GLN A 681      21.349  34.469  11.855  1.00124.32           C  
ANISOU 4889  C   GLN A 681    15580  14474  17182   1142   2214   1097       C  
ATOM   4890  O   GLN A 681      20.174  34.872  11.844  1.00124.22           O  
ANISOU 4890  O   GLN A 681    15389  14431  17378   1277   2474   1105       O  
ATOM   4891  CB  GLN A 681      22.860  34.415  13.862  1.00128.31           C  
ANISOU 4891  CB  GLN A 681    16489  15293  16970    748   2253    869       C  
ATOM   4892  CG  GLN A 681      22.299  35.690  14.457  1.00130.51           C  
ANISOU 4892  CG  GLN A 681    16817  15553  17217    829   2697    571       C  
ATOM   4893  CD  GLN A 681      23.288  36.379  15.379  1.00132.57           C  
ANISOU 4893  CD  GLN A 681    17381  15876  17112    659   2792    297       C  
ATOM   4894  OE1 GLN A 681      24.429  35.939  15.523  1.00132.16           O  
ANISOU 4894  OE1 GLN A 681    17495  15869  16850    486   2507    350       O  
ATOM   4895  NE2 GLN A 681      22.851  37.455  16.019  1.00134.58           N  
ANISOU 4895  NE2 GLN A 681    17705  16125  17305    702   3190     -1       N  
ATOM   4896  N   ALA A 682      22.212  34.754  10.876  1.00116.11           N  
ANISOU 4896  N   ALA A 682    14622  13238  16256   1202   1982   1048       N  
ATOM   4897  CA  ALA A 682      21.789  35.498   9.697  1.00115.22           C  
ANISOU 4897  CA  ALA A 682    14398  12873  16505   1405   1988   1038       C  
ATOM   4898  C   ALA A 682      20.607  34.825   9.012  1.00115.02           C  
ANISOU 4898  C   ALA A 682    14102  12822  16777   1496   1927   1323       C  
ATOM   4899  O   ALA A 682      19.672  35.500   8.565  1.00116.15           O  
ANISOU 4899  O   ALA A 682    14088  12820  17223   1654   2086   1338       O  
ATOM   4900  CB  ALA A 682      22.960  35.646   8.727  1.00112.32           C  
ANISOU 4900  CB  ALA A 682    14154  12361  16163   1395   1698    991       C  
ATOM   4901  N   ALA A 683      20.627  33.493   8.922  1.00113.42           N  
ANISOU 4901  N   ALA A 683    13834  12743  16517   1392   1680   1562       N  
ATOM   4902  CA  ALA A 683      19.488  32.785   8.345  1.00111.48           C  
ANISOU 4902  CA  ALA A 683    13342  12485  16531   1454   1608   1850       C  
ATOM   4903  C   ALA A 683      18.219  33.013   9.161  1.00115.13           C  
ANISOU 4903  C   ALA A 683    13641  13057  17047   1505   1950   1888       C  
ATOM   4904  O   ALA A 683      17.135  33.211   8.596  1.00114.67           O  
ANISOU 4904  O   ALA A 683    13367  12891  17312   1640   2026   2027       O  
ATOM   4905  CB  ALA A 683      19.798  31.293   8.241  1.00109.30           C  
ANISOU 4905  CB  ALA A 683    13042  12320  16168   1318   1278   2077       C  
ATOM   4906  N   ILE A 684      18.338  32.997  10.493  1.00111.46           N  
ANISOU 4906  N   ILE A 684    13269  12813  16266   1383   2159   1768       N  
ATOM   4907  CA  ILE A 684      17.175  33.193  11.357  1.00114.92           C  
ANISOU 4907  CA  ILE A 684    13553  13399  16713   1404   2523   1769       C  
ATOM   4908  C   ILE A 684      16.538  34.550  11.096  1.00116.70           C  
ANISOU 4908  C   ILE A 684    13687  13420  17234   1619   2839   1570       C  
ATOM   4909  O   ILE A 684      15.319  34.658  10.915  1.00118.45           O  
ANISOU 4909  O   ILE A 684    13650  13600  17756   1746   3007   1693       O  
ATOM   4910  CB  ILE A 684      17.566  33.042  12.838  1.00117.14           C  
ANISOU 4910  CB  ILE A 684    13996  13969  16545   1187   2698   1630       C  
ATOM   4911  CG1 ILE A 684      18.132  31.651  13.114  1.00115.74           C  
ANISOU 4911  CG1 ILE A 684    13873  13974  16129    960   2346   1874       C  
ATOM   4912  CG2 ILE A 684      16.368  33.325  13.728  1.00121.14           C  
ANISOU 4912  CG2 ILE A 684    14340  14649  17041   1198   3125   1584       C  
ATOM   4913  CD1 ILE A 684      17.182  30.539  12.802  1.00115.64           C  
ANISOU 4913  CD1 ILE A 684    13612  14035  16289    952   2192   2238       C  
ATOM   4914  N   VAL A 685      17.350  35.611  11.084  1.00116.00           N  
ANISOU 4914  N   VAL A 685    13796  13186  17092   1662   2913   1270       N  
ATOM   4915  CA  VAL A 685      16.792  36.945  10.869  1.00117.98           C  
ANISOU 4915  CA  VAL A 685    13960  13210  17658   1865   3193   1069       C  
ATOM   4916  C   VAL A 685      16.228  37.069   9.458  1.00116.45           C  
ANISOU 4916  C   VAL A 685    13562  12750  17936   2027   2992   1292       C  
ATOM   4917  O   VAL A 685      15.090  37.519   9.261  1.00118.60           O  
ANISOU 4917  O   VAL A 685    13583  12901  18580   2182   3183   1352       O  
ATOM   4918  CB  VAL A 685      17.852  38.024  11.154  1.00118.07           C  
ANISOU 4918  CB  VAL A 685    14245  13115  17502   1854   3270    714       C  
ATOM   4919  CG1 VAL A 685      17.320  39.397  10.786  1.00120.00           C  
ANISOU 4919  CG1 VAL A 685    14388  13068  18139   2070   3492    526       C  
ATOM   4920  CG2 VAL A 685      18.247  37.989  12.618  1.00120.31           C  
ANISOU 4920  CG2 VAL A 685    14722  13664  17326   1673   3506    492       C  
ATOM   4921  N   ARG A 686      17.015  36.660   8.459  1.00118.61           N  
ANISOU 4921  N   ARG A 686    13931  12934  18203   1976   2604   1422       N  
ATOM   4922  CA  ARG A 686      16.588  36.746   7.065  1.00117.15           C  
ANISOU 4922  CA  ARG A 686    13588  12518  18406   2072   2377   1640       C  
ATOM   4923  C   ARG A 686      15.244  36.067   6.840  1.00118.21           C  
ANISOU 4923  C   ARG A 686    13427  12684  18805   2122   2388   1955       C  
ATOM   4924  O   ARG A 686      14.417  36.551   6.059  1.00118.98           O  
ANISOU 4924  O   ARG A 686    13321  12571  19315   2244   2381   2093       O  
ATOM   4925  CB  ARG A 686      17.648  36.115   6.165  1.00113.50           C  
ANISOU 4925  CB  ARG A 686    13278  12041  17807   1956   1974   1728       C  
ATOM   4926  CG  ARG A 686      17.368  36.226   4.679  1.00112.02           C  
ANISOU 4926  CG  ARG A 686    12976  11639  17947   1998   1720   1928       C  
ATOM   4927  CD  ARG A 686      18.440  35.492   3.900  1.00108.81           C  
ANISOU 4927  CD  ARG A 686    12721  11266  17357   1862   1367   1971       C  
ATOM   4928  NE  ARG A 686      18.394  34.061   4.184  1.00107.95           N  
ANISOU 4928  NE  ARG A 686    12581  11348  17086   1764   1227   2139       N  
ATOM   4929  CZ  ARG A 686      19.329  33.396   4.855  1.00107.03           C  
ANISOU 4929  CZ  ARG A 686    12623  11397  16648   1652   1157   2040       C  
ATOM   4930  NH1 ARG A 686      20.398  34.027   5.319  1.00106.78           N  
ANISOU 4930  NH1 ARG A 686    12798  11375  16398   1619   1221   1774       N  
ATOM   4931  NH2 ARG A 686      19.192  32.097   5.067  1.00106.54           N  
ANISOU 4931  NH2 ARG A 686    12503  11476  16502   1564   1001   2224       N  
ATOM   4932  N   ILE A 687      15.008  34.939   7.512  1.00114.49           N  
ANISOU 4932  N   ILE A 687    12920  12469  18112   2012   2381   2097       N  
ATOM   4933  CA  ILE A 687      13.747  34.229   7.323  1.00114.39           C  
ANISOU 4933  CA  ILE A 687    12626  12503  18333   2042   2371   2420       C  
ATOM   4934  C   ILE A 687      12.632  34.869   8.142  1.00118.27           C  
ANISOU 4934  C   ILE A 687    12909  13031  18998   2159   2806   2340       C  
ATOM   4935  O   ILE A 687      11.508  35.033   7.656  1.00119.23           O  
ANISOU 4935  O   ILE A 687    12753  13024  19524   2279   2860   2536       O  
ATOM   4936  CB  ILE A 687      13.920  32.737   7.662  1.00113.87           C  
ANISOU 4936  CB  ILE A 687    12590  12685  17991   1867   2153   2632       C  
ATOM   4937  CG1 ILE A 687      14.891  32.073   6.682  1.00109.51           C  
ANISOU 4937  CG1 ILE A 687    12188  12052  17369   1779   1723   2714       C  
ATOM   4938  CG2 ILE A 687      12.576  32.027   7.643  1.00114.36           C  
ANISOU 4938  CG2 ILE A 687    12362  12823  18265   1884   2173   2963       C  
ATOM   4939  CD1 ILE A 687      15.326  30.694   7.103  1.00109.10           C  
ANISOU 4939  CD1 ILE A 687    12200  12205  17047   1606   1493   2853       C  
ATOM   4940  N   MET A 688      12.919  35.248   9.390  1.00119.93           N  
ANISOU 4940  N   MET A 688    13241  13415  18914   2114   3128   2046       N  
ATOM   4941  CA  MET A 688      11.877  35.785  10.257  1.00124.17           C  
ANISOU 4941  CA  MET A 688    13576  14024  19578   2205   3584   1926       C  
ATOM   4942  C   MET A 688      11.402  37.172   9.841  1.00126.13           C  
ANISOU 4942  C   MET A 688    13690  13952  20281   2433   3800   1748       C  
ATOM   4943  O   MET A 688      10.324  37.593  10.275  1.00129.77           O  
ANISOU 4943  O   MET A 688    13893  14404  21009   2554   4150   1704       O  
ATOM   4944  CB  MET A 688      12.359  35.818  11.707  1.00126.19           C  
ANISOU 4944  CB  MET A 688    14026  14569  19352   2054   3871   1637       C  
ATOM   4945  CG  MET A 688      12.417  34.455  12.357  1.00125.78           C  
ANISOU 4945  CG  MET A 688    14005  14864  18922   1820   3738   1859       C  
ATOM   4946  SD  MET A 688      10.777  33.710  12.438  1.00128.20           S  
ANISOU 4946  SD  MET A 688    13910  15316  19485   1852   3862   2212       S  
ATOM   4947  CE  MET A 688       9.993  34.738  13.676  1.00133.81           C  
ANISOU 4947  CE  MET A 688    14496  16156  20188   1916   4528   1848       C  
ATOM   4948  N   LYS A 689      12.165  37.897   9.021  1.00124.10           N  
ANISOU 4948  N   LYS A 689    13582  13429  20141   2490   3600   1648       N  
ATOM   4949  CA  LYS A 689      11.687  39.212   8.604  1.00126.20           C  
ANISOU 4949  CA  LYS A 689    13701  13364  20886   2695   3762   1512       C  
ATOM   4950  C   LYS A 689      10.701  39.114   7.444  1.00126.02           C  
ANISOU 4950  C   LYS A 689    13370  13118  21392   2798   3560   1885       C  
ATOM   4951  O   LYS A 689       9.611  39.692   7.501  1.00129.32           O  
ANISOU 4951  O   LYS A 689    13489  13387  22258   2961   3803   1904       O  
ATOM   4952  CB  LYS A 689      12.860  40.122   8.235  1.00124.58           C  
ANISOU 4952  CB  LYS A 689    13767  12960  20606   2695   3630   1264       C  
ATOM   4953  CG  LYS A 689      13.646  40.629   9.432  1.00125.98           C  
ANISOU 4953  CG  LYS A 689    14210  13273  20383   2634   3909    843       C  
ATOM   4954  CD  LYS A 689      14.833  41.474   8.999  1.00124.18           C  
ANISOU 4954  CD  LYS A 689    14249  12850  20085   2621   3732    641       C  
ATOM   4955  CE  LYS A 689      14.385  42.813   8.437  1.00126.21           C  
ANISOU 4955  CE  LYS A 689    14358  12722  20873   2819   3813    538       C  
ATOM   4956  NZ  LYS A 689      15.542  43.693   8.118  1.00124.85           N  
ANISOU 4956  NZ  LYS A 689    14450  12372  20614   2790   3656    330       N  
ATOM   4957  N   ALA A 690      11.064  38.386   6.387  1.00122.44           N  
ANISOU 4957  N   ALA A 690    12979  12637  20907   2695   3118   2181       N  
ATOM   4958  CA  ALA A 690      10.234  38.357   5.186  1.00122.20           C  
ANISOU 4958  CA  ALA A 690    12699  12381  21353   2751   2878   2542       C  
ATOM   4959  C   ALA A 690       8.864  37.753   5.468  1.00124.56           C  
ANISOU 4959  C   ALA A 690    12663  12775  21887   2802   3024   2808       C  
ATOM   4960  O   ALA A 690       7.830  38.371   5.187  1.00127.26           O  
ANISOU 4960  O   ALA A 690    12702  12902  22748   2949   3144   2919       O  
ATOM   4961  CB  ALA A 690      10.945  37.582   4.084  1.00118.13           C  
ANISOU 4961  CB  ALA A 690    12347  11868  20670   2589   2400   2769       C  
ATOM   4962  N   ARG A 691       8.835  36.538   6.005  1.00123.71           N  
ANISOU 4962  N   ARG A 691    12592  12981  21432   2674   2996   2933       N  
ATOM   4963  CA  ARG A 691       7.594  35.922   6.451  1.00126.15           C  
ANISOU 4963  CA  ARG A 691    12599  13438  21895   2697   3162   3169       C  
ATOM   4964  C   ARG A 691       7.406  36.218   7.934  1.00129.53           C  
ANISOU 4964  C   ARG A 691    13007  14093  22116   2728   3659   2852       C  
ATOM   4965  O   ARG A 691       8.374  36.262   8.698  1.00128.92           O  
ANISOU 4965  O   ARG A 691    13215  14183  21585   2632   3756   2553       O  
ATOM   4966  CB  ARG A 691       7.609  34.414   6.175  1.00123.64           C  
ANISOU 4966  CB  ARG A 691    12317  13326  21336   2520   2824   3512       C  
ATOM   4967  CG  ARG A 691       8.655  33.637   6.957  1.00121.85           C  
ANISOU 4967  CG  ARG A 691    12385  13390  20522   2347   2773   3359       C  
ATOM   4968  CD  ARG A 691       8.705  32.158   6.569  1.00119.43           C  
ANISOU 4968  CD  ARG A 691    12103  13226  20048   2181   2388   3700       C  
ATOM   4969  NE  ARG A 691       9.245  31.918   5.232  1.00116.13           N  
ANISOU 4969  NE  ARG A 691    11799  12607  19718   2138   1961   3837       N  
ATOM   4970  CZ  ARG A 691       8.539  31.449   4.208  1.00115.51           C  
ANISOU 4970  CZ  ARG A 691    11556  12400  19931   2125   1692   4192       C  
ATOM   4971  NH1 ARG A 691       7.254  31.159   4.361  1.00117.83           N  
ANISOU 4971  NH1 ARG A 691    11551  12734  20486   2167   1789   4472       N  
ATOM   4972  NH2 ARG A 691       9.120  31.259   3.031  1.00112.74           N  
ANISOU 4972  NH2 ARG A 691    11343  11895  19600   2053   1328   4267       N  
ATOM   4973  N   LYS A 692       6.156  36.446   8.333  1.00133.37           N  
ANISOU 4973  N   LYS A 692    13147  14585  22942   2848   3980   2915       N  
ATOM   4974  CA  LYS A 692       5.898  37.108   9.608  1.00137.46           C  
ANISOU 4974  CA  LYS A 692    13612  15238  23377   2914   4523   2533       C  
ATOM   4975  C   LYS A 692       6.081  36.170  10.799  1.00139.35           C  
ANISOU 4975  C   LYS A 692    13972  15932  23041   2708   4675   2485       C  
ATOM   4976  O   LYS A 692       6.890  36.440  11.693  1.00140.87           O  
ANISOU 4976  O   LYS A 692    14431  16288  22805   2614   4867   2129       O  
ATOM   4977  CB  LYS A 692       4.494  37.720   9.602  1.00141.78           C  
ANISOU 4977  CB  LYS A 692    13717  15622  24533   3122   4837   2593       C  
ATOM   4978  CG  LYS A 692       4.357  38.906   8.653  1.00142.27           C  
ANISOU 4978  CG  LYS A 692    13659  15211  25187   3325   4754   2558       C  
ATOM   4979  CD  LYS A 692       2.968  39.526   8.702  1.00147.01           C  
ANISOU 4979  CD  LYS A 692    13786  15623  26446   3538   5070   2611       C  
ATOM   4980  CE  LYS A 692       2.862  40.701   7.740  1.00147.64           C  
ANISOU 4980  CE  LYS A 692    13741  15205  27150   3718   4932   2611       C  
ATOM   4981  NZ  LYS A 692       1.509  41.322   7.759  1.00152.52           N  
ANISOU 4981  NZ  LYS A 692    13865  15597  28490   3936   5217   2676       N  
ATOM   4982  N   VAL A 693       5.333  35.069  10.836  1.00140.07           N  
ANISOU 4982  N   VAL A 693    13872  16234  23116   2613   4573   2858       N  
ATOM   4983  CA  VAL A 693       5.314  34.177  11.990  1.00142.36           C  
ANISOU 4983  CA  VAL A 693    14214  16964  22914   2399   4721   2867       C  
ATOM   4984  C   VAL A 693       5.496  32.741  11.515  1.00139.43           C  
ANISOU 4984  C   VAL A 693    13902  16723  22351   2217   4229   3300       C  
ATOM   4985  O   VAL A 693       4.988  32.359  10.455  1.00136.79           O  
ANISOU 4985  O   VAL A 693    13403  16200  22371   2281   3920   3657       O  
ATOM   4986  CB  VAL A 693       4.002  34.326  12.796  1.00146.47           C  
ANISOU 4986  CB  VAL A 693    14371  17663  23620   2457   5206   2852       C  
ATOM   4987  CG1 VAL A 693       3.958  33.347  13.961  1.00148.78           C  
ANISOU 4987  CG1 VAL A 693    14712  18442  23373   2187   5327   2908       C  
ATOM   4988  CG2 VAL A 693       3.841  35.754  13.296  1.00149.56           C  
ANISOU 4988  CG2 VAL A 693    14698  17903  24225   2646   5715   2372       C  
ATOM   4989  N   LEU A 694       6.234  31.950  12.296  1.00139.17           N  
ANISOU 4989  N   LEU A 694    14108  17000  21769   1976   4141   3269       N  
ATOM   4990  CA  LEU A 694       6.407  30.525  12.044  1.00136.58           C  
ANISOU 4990  CA  LEU A 694    13828  16818  21248   1785   3698   3654       C  
ATOM   4991  C   LEU A 694       6.359  29.758  13.358  1.00138.77           C  
ANISOU 4991  C   LEU A 694    14134  17532  21058   1529   3840   3682       C  
ATOM   4992  O   LEU A 694       6.762  30.271  14.402  1.00140.92           O  
ANISOU 4992  O   LEU A 694    14553  17993  20997   1441   4170   3342       O  
ATOM   4993  CB  LEU A 694       7.737  30.217  11.347  1.00132.07           C  
ANISOU 4993  CB  LEU A 694    13580  16095  20504   1721   3252   3630       C  
ATOM   4994  CG  LEU A 694       7.945  30.695   9.916  1.00129.30           C  
ANISOU 4994  CG  LEU A 694    13243  15354  20530   1892   2990   3673       C  
ATOM   4995  CD1 LEU A 694       9.365  30.376   9.490  1.00125.46           C  
ANISOU 4995  CD1 LEU A 694    13090  14802  19779   1792   2630   3578       C  
ATOM   4996  CD2 LEU A 694       6.938  30.044   8.987  1.00128.85           C  
ANISOU 4996  CD2 LEU A 694    12921  15189  20848   1933   2743   4111       C  
ATOM   4997  N   ARG A 695       5.870  28.522  13.299  1.00147.19           N  
ANISOU 4997  N   ARG A 695    15069  18763  22093   1385   3569   4100       N  
ATOM   4998  CA  ARG A 695       5.956  27.635  14.447  1.00150.58           C  
ANISOU 4998  CA  ARG A 695    15551  19603  22059   1089   3582   4196       C  
ATOM   4999  C   ARG A 695       7.373  27.083  14.565  1.00150.26           C  
ANISOU 4999  C   ARG A 695    15868  19589  21634    900   3214   4140       C  
ATOM   5000  O   ARG A 695       8.138  27.047  13.596  1.00147.40           O  
ANISOU 5000  O   ARG A 695    15660  18942  21404    991   2868   4137       O  
ATOM   5001  CB  ARG A 695       4.931  26.505  14.334  1.00149.41           C  
ANISOU 5001  CB  ARG A 695    15125  19605  22037    993   3391   4686       C  
ATOM   5002  CG  ARG A 695       5.120  25.538  13.169  1.00145.01           C  
ANISOU 5002  CG  ARG A 695    14590  18827  21681    997   2801   5053       C  
ATOM   5003  CD  ARG A 695       3.956  24.539  13.101  1.00145.09           C  
ANISOU 5003  CD  ARG A 695    14299  18979  21851    913   2657   5533       C  
ATOM   5004  NE  ARG A 695       3.947  23.586  14.211  1.00148.37           N  
ANISOU 5004  NE  ARG A 695    14723  19795  21856    604   2613   5702       N  
ATOM   5005  CZ  ARG A 695       4.534  22.393  14.181  1.00145.91           C  
ANISOU 5005  CZ  ARG A 695    14549  19538  21351    393   2128   5950       C  
ATOM   5006  NH1 ARG A 695       5.156  21.986  13.085  1.00139.95           N  
ANISOU 5006  NH1 ARG A 695    13929  18468  20777    471   1676   6032       N  
ATOM   5007  NH2 ARG A 695       4.479  21.595  15.239  1.00147.57           N  
ANISOU 5007  NH2 ARG A 695    14750  20117  21204     91   2090   6121       N  
ATOM   5008  N   HIS A 696       7.727  26.670  15.784  1.00148.03           N  
ANISOU 5008  N   HIS A 696    15709  19660  20875    618   3297   4092       N  
ATOM   5009  CA  HIS A 696       9.110  26.296  16.068  1.00148.16           C  
ANISOU 5009  CA  HIS A 696    16058  19706  20529    426   2999   4001       C  
ATOM   5010  C   HIS A 696       9.653  25.246  15.095  1.00143.82           C  
ANISOU 5010  C   HIS A 696    15562  18956  20126    413   2396   4302       C  
ATOM   5011  O   HIS A 696      10.827  25.336  14.697  1.00142.31           O  
ANISOU 5011  O   HIS A 696    15613  18581  19876    427   2156   4147       O  
ATOM   5012  CB  HIS A 696       9.245  25.841  17.527  1.00151.79           C  
ANISOU 5012  CB  HIS A 696    16600  20603  20470     69   3123   4008       C  
ATOM   5013  CG  HIS A 696      10.613  25.361  17.885  1.00151.62           C  
ANISOU 5013  CG  HIS A 696    16888  20620  20100   -164   2779   3978       C  
ATOM   5014  ND1 HIS A 696      11.666  26.218  18.117  1.00152.48           N  
ANISOU 5014  ND1 HIS A 696    17279  20641  20015   -155   2891   3595       N  
ATOM   5015  CD2 HIS A 696      11.105  24.109  18.021  1.00149.87           C  
ANISOU 5015  CD2 HIS A 696    16722  20489  19732   -410   2300   4298       C  
ATOM   5016  CE1 HIS A 696      12.747  25.512  18.393  1.00151.47           C  
ANISOU 5016  CE1 HIS A 696    17360  20558  19632   -388   2504   3688       C  
ATOM   5017  NE2 HIS A 696      12.434  24.230  18.340  1.00149.56           N  
ANISOU 5017  NE2 HIS A 696    16981  20416  19430   -542   2140   4109       N  
ATOM   5018  N   ASN A 697       8.804  24.288  14.652  1.00149.12           N  
ANISOU 5018  N   ASN A 697    16002  19641  21015    396   2157   4713       N  
ATOM   5019  CA  ASN A 697       9.242  23.272  13.715  1.00145.33           C  
ANISOU 5019  CA  ASN A 697    15562  18960  20695    383   1602   4977       C  
ATOM   5020  C   ASN A 697       9.476  23.820  12.340  1.00140.36           C  
ANISOU 5020  C   ASN A 697    14968  17941  20422    650   1487   4867       C  
ATOM   5021  O   ASN A 697      10.337  23.319  11.615  1.00135.95           O  
ANISOU 5021  O   ASN A 697    14558  17192  19906    643   1095   4886       O  
ATOM   5022  CB  ASN A 697       8.187  22.154  13.489  1.00143.98           C  
ANISOU 5022  CB  ASN A 697    15132  18871  20705    309   1368   5451       C  
ATOM   5023  CG  ASN A 697       8.863  20.826  13.233  1.00140.43           C  
ANISOU 5023  CG  ASN A 697    14779  18372  20207    136    799   5702       C  
ATOM   5024  OD1 ASN A 697       8.289  19.899  12.635  1.00138.67           O  
ANISOU 5024  OD1 ASN A 697    14405  18076  20208    121    478   6055       O  
ATOM   5025  ND2 ASN A 697      10.063  20.707  13.816  1.00139.76           N  
ANISOU 5025  ND2 ASN A 697    14936  18347  19818    -21    679   5528       N  
ATOM   5026  N   ALA A 698       8.741  24.833  11.966  1.00127.15           N  
ANISOU 5026  N   ALA A 698    13154  16145  19013    869   1814   4753       N  
ATOM   5027  CA  ALA A 698       8.655  25.187  10.565  1.00124.74           C  
ANISOU 5027  CA  ALA A 698    12813  15487  19096   1081   1651   4779       C  
ATOM   5028  C   ALA A 698       9.769  26.134  10.155  1.00122.67           C  
ANISOU 5028  C   ALA A 698    12799  15014  18798   1189   1682   4403       C  
ATOM   5029  O   ALA A 698      10.179  26.145   8.986  1.00119.90           O  
ANISOU 5029  O   ALA A 698    12515  14399  18641   1275   1410   4416       O  
ATOM   5030  CB  ALA A 698       7.274  25.777  10.280  1.00127.04           C  
ANISOU 5030  CB  ALA A 698    12796  15714  19758   1253   1929   4900       C  
ATOM   5031  N   LEU A 699      10.258  26.928  11.104  1.00120.63           N  
ANISOU 5031  N   LEU A 699    12679  14880  18275   1165   2011   4069       N  
ATOM   5032  CA  LEU A 699      11.459  27.724  10.892  1.00118.77           C  
ANISOU 5032  CA  LEU A 699    12709  14485  17934   1220   2011   3721       C  
ATOM   5033  C   LEU A 699      12.654  26.832  10.576  1.00115.70           C  
ANISOU 5033  C   LEU A 699    12527  14061  17372   1083   1567   3768       C  
ATOM   5034  O   LEU A 699      13.382  27.059   9.600  1.00112.97           O  
ANISOU 5034  O   LEU A 699    12301  13477  17147   1169   1362   3668       O  
ATOM   5035  CB  LEU A 699      11.716  28.570  12.139  1.00121.45           C  
ANISOU 5035  CB  LEU A 699    13164  15008  17972   1167   2430   3385       C  
ATOM   5036  CG  LEU A 699      12.929  29.477  12.105  1.00120.07           C  
ANISOU 5036  CG  LEU A 699    13268  14695  17656   1206   2469   3014       C  
ATOM   5037  CD1 LEU A 699      12.784  30.477  10.978  1.00118.90           C  
ANISOU 5037  CD1 LEU A 699    13070  14210  17895   1457   2507   2905       C  
ATOM   5038  CD2 LEU A 699      13.058  30.171  13.442  1.00123.23           C  
ANISOU 5038  CD2 LEU A 699    13780  15313  17729   1111   2880   2712       C  
ATOM   5039  N   ILE A 700      12.870  25.805  11.402  1.00126.41           N  
ANISOU 5039  N   ILE A 700    13915  15655  18460    857   1412   3924       N  
ATOM   5040  CA  ILE A 700      13.781  24.744  11.018  1.00122.77           C  
ANISOU 5040  CA  ILE A 700    13570  15131  17948    738    944   4045       C  
ATOM   5041  C   ILE A 700      13.202  24.043   9.785  1.00118.18           C  
ANISOU 5041  C   ILE A 700    12832  14359  17714    826    642   4322       C  
ATOM   5042  O   ILE A 700      12.000  24.115   9.502  1.00118.59           O  
ANISOU 5042  O   ILE A 700    12666  14403  17988    913    759   4513       O  
ATOM   5043  CB  ILE A 700      13.998  23.769  12.188  1.00125.59           C  
ANISOU 5043  CB  ILE A 700    13955  15771  17994    460    815   4207       C  
ATOM   5044  CG1 ILE A 700      14.474  24.539  13.419  1.00131.28           C  
ANISOU 5044  CG1 ILE A 700    14838  16699  18343    341   1142   3933       C  
ATOM   5045  CG2 ILE A 700      15.052  22.720  11.857  1.00122.28           C  
ANISOU 5045  CG2 ILE A 700    13647  15250  17564    343    326   4301       C  
ATOM   5046  CD1 ILE A 700      14.452  23.733  14.694  1.00133.89           C  
ANISOU 5046  CD1 ILE A 700    15172  17362  18336     27   1087   4114       C  
ATOM   5047  N   GLN A 701      14.085  23.375   9.038  1.00127.20           N  
ANISOU 5047  N   GLN A 701    14084  15338  18908    797    254   4331       N  
ATOM   5048  CA  GLN A 701      13.873  22.797   7.709  1.00119.44           C  
ANISOU 5048  CA  GLN A 701    13030  14133  18219    866    -58   4495       C  
ATOM   5049  C   GLN A 701      13.869  23.903   6.659  1.00116.96           C  
ANISOU 5049  C   GLN A 701    12746  13595  18098   1053     75   4311       C  
ATOM   5050  O   GLN A 701      14.140  23.648   5.478  1.00112.12           O  
ANISOU 5050  O   GLN A 701    12164  12784  17653   1086   -177   4326       O  
ATOM   5051  CB  GLN A 701      12.556  22.010   7.627  1.00118.67           C  
ANISOU 5051  CB  GLN A 701    12692  14101  18296    833   -148   4885       C  
ATOM   5052  CG  GLN A 701      12.348  20.965   8.711  1.00121.51           C  
ANISOU 5052  CG  GLN A 701    12984  14708  18475    628   -265   5123       C  
ATOM   5053  CD  GLN A 701      13.365  19.856   8.660  1.00118.36           C  
ANISOU 5053  CD  GLN A 701    12701  14254  18018    487   -695   5159       C  
ATOM   5054  OE1 GLN A 701      13.767  19.418   7.583  1.00114.00           O  
ANISOU 5054  OE1 GLN A 701    12189  13470  17658    540   -984   5145       O  
ATOM   5055  NE2 GLN A 701      13.789  19.387   9.829  1.00122.14           N  
ANISOU 5055  NE2 GLN A 701    13227  14941  18241    291   -743   5203       N  
ATOM   5056  N   GLU A 702      13.701  25.150   7.097  1.00109.15           N  
ANISOU 5056  N   GLU A 702    11771  12635  17067   1153    458   4105       N  
ATOM   5057  CA  GLU A 702      13.898  26.295   6.222  1.00107.52           C  
ANISOU 5057  CA  GLU A 702    11620  12211  17022   1306    567   3904       C  
ATOM   5058  C   GLU A 702      15.234  26.962   6.469  1.00107.75           C  
ANISOU 5058  C   GLU A 702    11895  12216  16830   1298    625   3550       C  
ATOM   5059  O   GLU A 702      15.882  27.393   5.518  1.00104.81           O  
ANISOU 5059  O   GLU A 702    11625  11660  16538   1350    511   3412       O  
ATOM   5060  CB  GLU A 702      12.781  27.332   6.374  1.00110.15           C  
ANISOU 5060  CB  GLU A 702    11779  12521  17553   1449    929   3910       C  
ATOM   5061  CG  GLU A 702      12.939  28.485   5.374  1.00108.20           C  
ANISOU 5061  CG  GLU A 702    11569  12016  17527   1589    977   3753       C  
ATOM   5062  CD  GLU A 702      11.840  29.530   5.452  1.00110.50           C  
ANISOU 5062  CD  GLU A 702    11657  12227  18099   1744   1304   3765       C  
ATOM   5063  OE1 GLU A 702      10.940  29.400   6.307  1.00113.72           O  
ANISOU 5063  OE1 GLU A 702    11890  12796  18523   1755   1541   3864       O  
ATOM   5064  OE2 GLU A 702      11.882  30.489   4.650  1.00109.46           O  
ANISOU 5064  OE2 GLU A 702    11530  11869  18189   1847   1320   3676       O  
ATOM   5065  N   VAL A 703      15.669  27.055   7.727  1.00106.14           N  
ANISOU 5065  N   VAL A 703    11790  12205  16333   1209    794   3412       N  
ATOM   5066  CA  VAL A 703      17.083  27.321   7.977  1.00104.86           C  
ANISOU 5066  CA  VAL A 703    11870  12032  15938   1147    735   3142       C  
ATOM   5067  C   VAL A 703      17.925  26.274   7.263  1.00102.43           C  
ANISOU 5067  C   VAL A 703    11621  11637  15660   1069    316   3216       C  
ATOM   5068  O   VAL A 703      18.945  26.585   6.626  1.00100.54           O  
ANISOU 5068  O   VAL A 703    11520  11263  15417   1093    203   3020       O  
ATOM   5069  CB  VAL A 703      17.365  27.338   9.490  1.00106.93           C  
ANISOU 5069  CB  VAL A 703    12226  12542  15860   1002    918   3051       C  
ATOM   5070  CG1 VAL A 703      18.837  27.613   9.755  1.00105.73           C  
ANISOU 5070  CG1 VAL A 703    12322  12370  15481    923    834   2800       C  
ATOM   5071  CG2 VAL A 703      16.476  28.351  10.175  1.00109.75           C  
ANISOU 5071  CG2 VAL A 703    12512  12987  16201   1080   1368   2940       C  
ATOM   5072  N   ILE A 704      17.484  25.015   7.337  1.00102.67           N  
ANISOU 5072  N   ILE A 704    11531  11738  15741    974     82   3496       N  
ATOM   5073  CA  ILE A 704      18.159  23.920   6.648  1.00100.81           C  
ANISOU 5073  CA  ILE A 704    11317  11397  15590    908   -319   3568       C  
ATOM   5074  C   ILE A 704      18.101  24.135   5.142  1.00 99.00           C  
ANISOU 5074  C   ILE A 704    11071  10945  15599   1018   -429   3532       C  
ATOM   5075  O   ILE A 704      19.115  24.025   4.442  1.00 97.23           O  
ANISOU 5075  O   ILE A 704    10956  10600  15388   1010   -605   3362       O  
ATOM   5076  CB  ILE A 704      17.523  22.576   7.041  1.00101.85           C  
ANISOU 5076  CB  ILE A 704    11302  11632  15762    786   -545   3899       C  
ATOM   5077  CG1 ILE A 704      17.374  22.474   8.560  1.00104.19           C  
ANISOU 5077  CG1 ILE A 704    11598  12190  15797    641   -399   3970       C  
ATOM   5078  CG2 ILE A 704      18.354  21.424   6.505  1.00100.35           C  
ANISOU 5078  CG2 ILE A 704    11142  11319  15667    710   -961   3930       C  
ATOM   5079  CD1 ILE A 704      18.657  22.562   9.313  1.00104.07           C  
ANISOU 5079  CD1 ILE A 704    11769  12235  15539    523   -441   3775       C  
ATOM   5080  N   SER A 705      16.906  24.435   4.619  1.00 99.65           N  
ANISOU 5080  N   SER A 705    11008  10979  15875   1102   -329   3701       N  
ATOM   5081  CA  SER A 705      16.771  24.693   3.188  1.00 98.28           C  
ANISOU 5081  CA  SER A 705    10821  10607  15912   1166   -441   3700       C  
ATOM   5082  C   SER A 705      17.709  25.804   2.725  1.00 97.09           C  
ANISOU 5082  C   SER A 705    10832  10356  15701   1221   -336   3387       C  
ATOM   5083  O   SER A 705      18.277  25.729   1.630  1.00 95.51           O  
ANISOU 5083  O   SER A 705    10699  10029  15560   1198   -518   3300       O  
ATOM   5084  CB  SER A 705      15.323  25.049   2.854  1.00 99.61           C  
ANISOU 5084  CB  SER A 705    10800  10740  16307   1240   -320   3941       C  
ATOM   5085  OG  SER A 705      15.178  25.363   1.479  1.00 98.54           O  
ANISOU 5085  OG  SER A 705    10661  10417  16363   1264   -443   3965       O  
ATOM   5086  N   GLN A 706      17.886  26.841   3.547  1.00102.74           N  
ANISOU 5086  N   GLN A 706    11613  11134  16289   1278    -42   3210       N  
ATOM   5087  CA  GLN A 706      18.681  27.994   3.134  1.00102.43           C  
ANISOU 5087  CA  GLN A 706    11718  10992  16210   1331     61   2937       C  
ATOM   5088  C   GLN A 706      20.170  27.673   3.157  1.00101.17           C  
ANISOU 5088  C   GLN A 706    11735  10844  15862   1249    -99   2722       C  
ATOM   5089  O   GLN A 706      20.886  27.925   2.182  1.00 98.99           O  
ANISOU 5089  O   GLN A 706    11538  10457  15616   1240   -216   2586       O  
ATOM   5090  CB  GLN A 706      18.388  29.196   4.037  1.00106.02           C  
ANISOU 5090  CB  GLN A 706    12189  11489  16603   1417    423   2800       C  
ATOM   5091  CG  GLN A 706      16.955  29.729   4.014  1.00107.82           C  
ANISOU 5091  CG  GLN A 706    12217  11675  17073   1526    632   2964       C  
ATOM   5092  CD  GLN A 706      16.565  30.350   2.698  1.00105.64           C  
ANISOU 5092  CD  GLN A 706    11874  11185  17079   1590    552   3033       C  
ATOM   5093  OE1 GLN A 706      17.371  31.013   2.054  1.00104.16           O  
ANISOU 5093  OE1 GLN A 706    11818  10886  16871   1586    492   2856       O  
ATOM   5094  NE2 GLN A 706      15.316  30.149   2.295  1.00105.73           N  
ANISOU 5094  NE2 GLN A 706    11673  11145  17356   1629    537   3311       N  
ATOM   5095  N   SER A 707      20.654  27.101   4.262  1.00101.02           N  
ANISOU 5095  N   SER A 707    11765  10964  15652   1169   -115   2702       N  
ATOM   5096  CA  SER A 707      22.078  26.836   4.427  1.00100.26           C  
ANISOU 5096  CA  SER A 707    11815  10874  15405   1090   -262   2513       C  
ATOM   5097  C   SER A 707      22.488  25.475   3.868  1.00 97.49           C  
ANISOU 5097  C   SER A 707    11411  10474  15159   1015   -605   2602       C  
ATOM   5098  O   SER A 707      23.434  24.854   4.373  1.00 97.47           O  
ANISOU 5098  O   SER A 707    11461  10504  15070    928   -760   2541       O  
ATOM   5099  CB  SER A 707      22.465  26.970   5.900  1.00103.77           C  
ANISOU 5099  CB  SER A 707    12349  11479  15599   1011   -129   2451       C  
ATOM   5100  OG  SER A 707      21.763  26.040   6.701  1.00105.56           O  
ANISOU 5100  OG  SER A 707    12466  11845  15795    927   -180   2691       O  
ATOM   5101  N   ARG A 708      21.788  25.001   2.834  1.00113.82           N  
ANISOU 5101  N   ARG A 708    13369  12449  17427   1040   -737   2746       N  
ATOM   5102  CA  ARG A 708      22.055  23.691   2.244  1.00110.08           C  
ANISOU 5102  CA  ARG A 708    12839  11908  17081    974  -1055   2817       C  
ATOM   5103  C   ARG A 708      23.495  23.562   1.745  1.00108.84           C  
ANISOU 5103  C   ARG A 708    12781  11673  16901    940  -1190   2547       C  
ATOM   5104  O   ARG A 708      24.218  22.642   2.141  1.00108.16           O  
ANISOU 5104  O   ARG A 708    12682  11582  16833    876  -1386   2526       O  
ATOM   5105  CB  ARG A 708      21.033  23.424   1.126  1.00108.00           C  
ANISOU 5105  CB  ARG A 708    12470  11552  17013    993  -1142   2992       C  
ATOM   5106  CG  ARG A 708      20.803  24.591   0.145  1.00107.94           C  
ANISOU 5106  CG  ARG A 708    12502  11464  17047   1047   -999   2906       C  
ATOM   5107  CD  ARG A 708      21.649  24.541  -1.125  1.00107.36           C  
ANISOU 5107  CD  ARG A 708    12507  11288  16996    992  -1146   2708       C  
ATOM   5108  NE  ARG A 708      21.343  23.404  -1.988  1.00106.00           N  
ANISOU 5108  NE  ARG A 708    12268  11045  16962    918  -1401   2816       N  
ATOM   5109  CZ  ARG A 708      20.363  23.393  -2.887  1.00105.26           C  
ANISOU 5109  CZ  ARG A 708    12111  10889  16993    885  -1461   3002       C  
ATOM   5110  NH1 ARG A 708      19.593  24.463  -3.048  1.00105.91           N  
ANISOU 5110  NH1 ARG A 708    12167  10961  17114    929  -1293   3113       N  
ATOM   5111  NH2 ARG A 708      20.158  22.317  -3.634  1.00103.73           N  
ANISOU 5111  NH2 ARG A 708    11879  10630  16904    799  -1702   3077       N  
ATOM   5112  N   ALA A 709      23.936  24.483   0.886  1.00100.24           N  
ANISOU 5112  N   ALA A 709    11775  10522  15790    975  -1093   2348       N  
ATOM   5113  CA  ALA A 709      25.202  24.316   0.179  1.00 99.01           C  
ANISOU 5113  CA  ALA A 709    11683  10298  15637    935  -1216   2096       C  
ATOM   5114  C   ALA A 709      26.411  24.751   0.992  1.00100.12           C  
ANISOU 5114  C   ALA A 709    11928  10487  15626    922  -1153   1902       C  
ATOM   5115  O   ALA A 709      27.543  24.506   0.563  1.00 99.45           O  
ANISOU 5115  O   ALA A 709    11869  10353  15563    887  -1262   1701       O  
ATOM   5116  CB  ALA A 709      25.181  25.086  -1.143  1.00 98.19           C  
ANISOU 5116  CB  ALA A 709    11622  10131  15553    934  -1160   1984       C  
ATOM   5117  N   ARG A 710      26.207  25.395   2.139  1.00 95.16           N  
ANISOU 5117  N   ARG A 710    11357   9954  14846    937   -976   1950       N  
ATOM   5118  CA  ARG A 710      27.336  25.750   2.988  1.00 95.28           C  
ANISOU 5118  CA  ARG A 710    11484  10018  14701    893   -943   1794       C  
ATOM   5119  C   ARG A 710      27.820  24.542   3.778  1.00 95.97           C  
ANISOU 5119  C   ARG A 710    11513  10129  14822    802  -1169   1886       C  
ATOM   5120  O   ARG A 710      29.020  24.243   3.799  1.00 95.68           O  
ANISOU 5120  O   ARG A 710    11498  10047  14810    754  -1309   1746       O  
ATOM   5121  CB  ARG A 710      26.948  26.890   3.928  1.00 96.20           C  
ANISOU 5121  CB  ARG A 710    11699  10227  14626    919   -668   1787       C  
ATOM   5122  N   PHE A 711      26.893  23.834   4.419  1.00 98.43           N  
ANISOU 5122  N   PHE A 711    11736  10506  15158    768  -1222   2138       N  
ATOM   5123  CA  PHE A 711      27.158  22.664   5.251  1.00 98.76           C  
ANISOU 5123  CA  PHE A 711    11707  10576  15243    653  -1464   2295       C  
ATOM   5124  C   PHE A 711      25.812  22.137   5.734  1.00 99.75           C  
ANISOU 5124  C   PHE A 711    11729  10794  15377    626  -1460   2592       C  
ATOM   5125  O   PHE A 711      24.779  22.799   5.587  1.00100.58           O  
ANISOU 5125  O   PHE A 711    11826  10952  15438    701  -1233   2651       O  
ATOM   5126  CB  PHE A 711      28.073  23.002   6.432  1.00100.96           C  
ANISOU 5126  CB  PHE A 711    12098  10943  15319    544  -1443   2236       C  
ATOM   5127  CG  PHE A 711      27.540  24.096   7.314  1.00104.14           C  
ANISOU 5127  CG  PHE A 711    12619  11503  15446    530  -1130   2236       C  
ATOM   5128  CD1 PHE A 711      27.819  25.421   7.033  1.00104.80           C  
ANISOU 5128  CD1 PHE A 711    12836  11572  15413    614   -883   2010       C  
ATOM   5129  CD2 PHE A 711      26.768  23.803   8.423  1.00106.78           C  
ANISOU 5129  CD2 PHE A 711    12929  12002  15642    423  -1081   2451       C  
ATOM   5130  CE1 PHE A 711      27.332  26.430   7.833  1.00108.05           C  
ANISOU 5130  CE1 PHE A 711    13351  12100  15604    611   -589   1975       C  
ATOM   5131  CE2 PHE A 711      26.281  24.812   9.228  1.00110.29           C  
ANISOU 5131  CE2 PHE A 711    13477  12594  15835    408   -761   2405       C  
ATOM   5132  CZ  PHE A 711      26.561  26.125   8.931  1.00110.95           C  
ANISOU 5132  CZ  PHE A 711    13690  12631  15833    512   -512   2155       C  
ATOM   5133  N   ASN A 712      25.828  20.934   6.307  1.00103.20           N  
ANISOU 5133  N   ASN A 712    12070  11243  15898    512  -1728   2793       N  
ATOM   5134  CA  ASN A 712      24.659  20.417   7.004  1.00104.79           C  
ANISOU 5134  CA  ASN A 712    12177  11575  16063    441  -1737   3100       C  
ATOM   5135  C   ASN A 712      24.683  20.936   8.438  1.00109.71           C  
ANISOU 5135  C   ASN A 712    12891  12411  16383    312  -1565   3149       C  
ATOM   5136  O   ASN A 712      25.537  20.495   9.223  1.00111.04           O  
ANISOU 5136  O   ASN A 712    13095  12611  16486    158  -1749   3179       O  
ATOM   5137  CB  ASN A 712      24.623  18.896   6.979  1.00103.34           C  
ANISOU 5137  CB  ASN A 712    11848  11309  16107    352  -2124   3316       C  
ATOM   5138  CG  ASN A 712      24.142  18.345   5.647  1.00100.63           C  
ANISOU 5138  CG  ASN A 712    11408  10795  16031    459  -2252   3322       C  
ATOM   5139  OD1 ASN A 712      23.183  18.850   5.061  1.00100.53           O  
ANISOU 5139  OD1 ASN A 712    11382  10801  16014    550  -2069   3360       O  
ATOM   5140  ND2 ASN A 712      24.805  17.301   5.166  1.00 98.70           N  
ANISOU 5140  ND2 ASN A 712    11092  10375  16037    437  -2574   3283       N  
ATOM   5141  N   PRO A 713      23.800  21.851   8.810  1.00 99.33           N  
ANISOU 5141  N   PRO A 713    11611  11237  14894    355  -1224   3152       N  
ATOM   5142  CA  PRO A 713      23.885  22.465  10.139  1.00101.14           C  
ANISOU 5142  CA  PRO A 713    11953  11674  14802    222  -1013   3128       C  
ATOM   5143  C   PRO A 713      23.382  21.546  11.236  1.00103.39           C  
ANISOU 5143  C   PRO A 713    12157  12152  14976      6  -1145   3432       C  
ATOM   5144  O   PRO A 713      22.522  20.688  11.028  1.00103.81           O  
ANISOU 5144  O   PRO A 713    12047  12213  15183     -2  -1287   3684       O  
ATOM   5145  CB  PRO A 713      22.991  23.703  10.008  1.00101.45           C  
ANISOU 5145  CB  PRO A 713    12017  11764  14765    369   -596   3011       C  
ATOM   5146  CG  PRO A 713      22.006  23.326   8.966  1.00100.62           C  
ANISOU 5146  CG  PRO A 713    11746  11553  14933    506   -648   3155       C  
ATOM   5147  CD  PRO A 713      22.723  22.437   7.996  1.00 98.80           C  
ANISOU 5147  CD  PRO A 713    11479  11128  14930    523  -1007   3153       C  
ATOM   5148  N   SER A 714      23.935  21.750  12.426  1.00107.77           N  
ANISOU 5148  N   SER A 714    12833  12870  15244   -195  -1107   3416       N  
ATOM   5149  CA  SER A 714      23.588  20.937  13.582  1.00110.28           C  
ANISOU 5149  CA  SER A 714    13097  13405  15398   -465  -1245   3709       C  
ATOM   5150  C   SER A 714      22.307  21.468  14.210  1.00112.34           C  
ANISOU 5150  C   SER A 714    13325  13914  15444   -488   -867   3769       C  
ATOM   5151  O   SER A 714      22.260  22.621  14.649  1.00113.16           O  
ANISOU 5151  O   SER A 714    13561  14122  15314   -463   -490   3539       O  
ATOM   5152  CB  SER A 714      24.728  20.947  14.596  1.00111.48           C  
ANISOU 5152  CB  SER A 714    13400  13641  15315   -713  -1376   3681       C  
ATOM   5153  OG  SER A 714      25.905  20.386  14.041  1.00109.90           O  
ANISOU 5153  OG  SER A 714    13190  13204  15365   -690  -1736   3640       O  
ATOM   5154  N   ILE A 715      21.270  20.627  14.255  1.00112.63           N  
ANISOU 5154  N   ILE A 715    13177  14041  15576   -538   -963   4071       N  
ATOM   5155  CA  ILE A 715      20.035  20.999  14.936  1.00115.06           C  
ANISOU 5155  CA  ILE A 715    13416  14612  15691   -589   -614   4158       C  
ATOM   5156  C   ILE A 715      20.302  21.318  16.401  1.00117.95           C  
ANISOU 5156  C   ILE A 715    13921  15276  15619   -883   -453   4129       C  
ATOM   5157  O   ILE A 715      19.534  22.055  17.030  1.00120.15           O  
ANISOU 5157  O   ILE A 715    14208  15774  15670   -907    -35   4039       O  
ATOM   5158  CB  ILE A 715      18.988  19.874  14.778  1.00115.82           C  
ANISOU 5158  CB  ILE A 715    13279  14761  15964   -636   -821   4537       C  
ATOM   5159  CG1 ILE A 715      18.769  19.560  13.297  1.00113.09           C  
ANISOU 5159  CG1 ILE A 715    12824  14114  16032   -373   -995   4551       C  
ATOM   5160  CG2 ILE A 715      17.659  20.269  15.408  1.00118.46           C  
ANISOU 5160  CG2 ILE A 715    13506  15371  16134   -673   -436   4626       C  
ATOM   5161  CD1 ILE A 715      18.237  20.727  12.502  1.00111.98           C  
ANISOU 5161  CD1 ILE A 715    12683  13868  15996    -93   -624   4319       C  
ATOM   5162  N   SER A 716      21.396  20.794  16.957  1.00126.79           N  
ANISOU 5162  N   SER A 716    15148  16403  16622  -1118   -775   4195       N  
ATOM   5163  CA  SER A 716      21.804  21.148  18.310  1.00129.36           C  
ANISOU 5163  CA  SER A 716    15645  16999  16508  -1434   -653   4157       C  
ATOM   5164  C   SER A 716      22.208  22.614  18.430  1.00132.47           C  
ANISOU 5164  C   SER A 716    16251  17384  16699  -1321   -241   3743       C  
ATOM   5165  O   SER A 716      22.242  23.144  19.545  1.00135.53           O  
ANISOU 5165  O   SER A 716    16785  18026  16683  -1556     -3   3652       O  
ATOM   5166  CB  SER A 716      22.962  20.253  18.755  1.00128.13           C  
ANISOU 5166  CB  SER A 716    15544  16798  16343  -1705  -1149   4345       C  
ATOM   5167  OG  SER A 716      22.574  18.889  18.794  1.00127.45           O  
ANISOU 5167  OG  SER A 716    15263  16728  16435  -1849  -1546   4744       O  
ATOM   5168  N   MET A 717      22.511  23.277  17.314  1.00135.77           N  
ANISOU 5168  N   MET A 717    16691  17518  17376   -992   -162   3493       N  
ATOM   5169  CA  MET A 717      22.971  24.661  17.316  1.00139.30           C  
ANISOU 5169  CA  MET A 717    17334  17910  17683   -872    174   3110       C  
ATOM   5170  C   MET A 717      21.860  25.662  17.030  1.00141.69           C  
ANISOU 5170  C   MET A 717    17576  18226  18034   -635    650   2923       C  
ATOM   5171  O   MET A 717      21.857  26.758  17.600  1.00144.69           O  
ANISOU 5171  O   MET A 717    18102  18693  18179   -644   1020   2648       O  
ATOM   5172  CB  MET A 717      24.086  24.849  16.280  1.00137.03           C  
ANISOU 5172  CB  MET A 717    17113  17307  17645   -684    -43   2950       C  
ATOM   5173  CG  MET A 717      25.307  23.977  16.515  1.00134.75           C  
ANISOU 5173  CG  MET A 717    16871  16959  17371   -887   -497   3089       C  
ATOM   5174  SD  MET A 717      26.067  24.241  18.126  1.00138.83           S  
ANISOU 5174  SD  MET A 717    17621  17729  17399  -1293   -484   3082       S  
ATOM   5175  CE  MET A 717      26.733  25.885  17.912  1.00140.83           C  
ANISOU 5175  CE  MET A 717    18116  17871  17523  -1124   -140   2633       C  
ATOM   5176  N   ILE A 718      20.915  25.306  16.157  1.00122.24           N  
ANISOU 5176  N   ILE A 718    14891  15662  15891   -428    636   3067       N  
ATOM   5177  CA  ILE A 718      19.902  26.261  15.720  1.00122.65           C  
ANISOU 5177  CA  ILE A 718    14852  15664  16086   -175   1041   2909       C  
ATOM   5178  C   ILE A 718      18.982  26.645  16.872  1.00126.54           C  
ANISOU 5178  C   ILE A 718    15314  16461  16304   -309   1448   2876       C  
ATOM   5179  O   ILE A 718      18.568  27.804  16.989  1.00127.87           O  
ANISOU 5179  O   ILE A 718    15512  16619  16455   -170   1869   2598       O  
ATOM   5180  CB  ILE A 718      19.119  25.691  14.523  1.00120.78           C  
ANISOU 5180  CB  ILE A 718    14382  15252  16258     36    880   3120       C  
ATOM   5181  CG1 ILE A 718      20.048  25.511  13.324  1.00117.25           C  
ANISOU 5181  CG1 ILE A 718    13985  14506  16058    174    555   3066       C  
ATOM   5182  CG2 ILE A 718      17.957  26.595  14.153  1.00121.73           C  
ANISOU 5182  CG2 ILE A 718    14367  15328  16558    266   1272   3023       C  
ATOM   5183  CD1 ILE A 718      19.423  24.750  12.184  1.00115.56           C  
ANISOU 5183  CD1 ILE A 718    13573  14133  16200    312    326   3290       C  
ATOM   5184  N   LYS A 719      18.654  25.691  17.748  1.00134.57           N  
ANISOU 5184  N   LYS A 719    16265  17754  17110   -593   1331   3149       N  
ATOM   5185  CA  LYS A 719      17.762  25.991  18.867  1.00137.85           C  
ANISOU 5185  CA  LYS A 719    16640  18504  17232   -759   1733   3118       C  
ATOM   5186  C   LYS A 719      18.402  26.983  19.832  1.00140.24           C  
ANISOU 5186  C   LYS A 719    17208  18938  17139   -912   2030   2771       C  
ATOM   5187  O   LYS A 719      17.778  27.981  20.222  1.00142.78           O  
ANISOU 5187  O   LYS A 719    17533  19346  17373   -833   2521   2496       O  
ATOM   5188  CB  LYS A 719      17.377  24.701  19.592  1.00136.96           C  
ANISOU 5188  CB  LYS A 719    16413  18676  16951  -1081   1490   3516       C  
ATOM   5189  CG  LYS A 719      16.485  23.777  18.778  1.00134.79           C  
ANISOU 5189  CG  LYS A 719    15858  18315  17042   -946   1269   3859       C  
ATOM   5190  CD  LYS A 719      16.099  22.540  19.570  1.00135.60           C  
ANISOU 5190  CD  LYS A 719    15850  18709  16964  -1289   1023   4262       C  
ATOM   5191  CE  LYS A 719      15.217  21.615  18.749  1.00134.22           C  
ANISOU 5191  CE  LYS A 719    15404  18432  17161  -1160    781   4610       C  
ATOM   5192  NZ  LYS A 719      14.833  20.396  19.511  1.00135.16           N  
ANISOU 5192  NZ  LYS A 719    15407  18828  17120  -1505    510   5028       N  
ATOM   5193  N   LYS A 720      19.650  26.725  20.232  1.00135.89           N  
ANISOU 5193  N   LYS A 720    16877  18392  16365  -1137   1735   2776       N  
ATOM   5194  CA  LYS A 720      20.357  27.667  21.091  1.00137.72           C  
ANISOU 5194  CA  LYS A 720    17387  18721  16218  -1298   1972   2454       C  
ATOM   5195  C   LYS A 720      20.547  29.009  20.400  1.00137.69           C  
ANISOU 5195  C   LYS A 720    17472  18442  16404   -962   2250   2061       C  
ATOM   5196  O   LYS A 720      20.526  30.055  21.060  1.00140.17           O  
ANISOU 5196  O   LYS A 720    17941  18841  16476  -1000   2644   1730       O  
ATOM   5197  CB  LYS A 720      21.708  27.087  21.510  1.00136.18           C  
ANISOU 5197  CB  LYS A 720    17387  18536  15820  -1590   1535   2581       C  
ATOM   5198  N   CYS A 721      20.723  29.001  19.077  1.00133.07           N  
ANISOU 5198  N   CYS A 721    16791  17525  16245   -650   2046   2089       N  
ATOM   5199  CA  CYS A 721      20.811  30.252  18.332  1.00131.79           C  
ANISOU 5199  CA  CYS A 721    16681  17094  16299   -339   2278   1763       C  
ATOM   5200  C   CYS A 721      19.513  31.044  18.452  1.00134.38           C  
ANISOU 5200  C   CYS A 721    16860  17466  16733   -166   2774   1601       C  
ATOM   5201  O   CYS A 721      19.530  32.256  18.696  1.00135.91           O  
ANISOU 5201  O   CYS A 721    17169  17598  16874    -74   3125   1247       O  
ATOM   5202  CB  CYS A 721      21.147  29.955  16.869  1.00127.64           C  
ANISOU 5202  CB  CYS A 721    16056  16248  16192    -88   1946   1874       C  
ATOM   5203  SG  CYS A 721      21.466  31.400  15.839  1.00125.74           S  
ANISOU 5203  SG  CYS A 721    15893  15667  16218    241   2113   1534       S  
ATOM   5204  N   ILE A 722      18.372  30.364  18.296  1.00132.49           N  
ANISOU 5204  N   ILE A 722    16350  17324  16666   -122   2802   1857       N  
ATOM   5205  CA  ILE A 722      17.068  30.986  18.538  1.00135.55           C  
ANISOU 5205  CA  ILE A 722    16551  17791  17162     11   3278   1739       C  
ATOM   5206  C   ILE A 722      17.028  31.611  19.926  1.00139.86           C  
ANISOU 5206  C   ILE A 722    17251  18619  17269   -214   3694   1453       C  
ATOM   5207  O   ILE A 722      16.741  32.805  20.089  1.00141.89           O  
ANISOU 5207  O   ILE A 722    17540  18796  17575    -64   4114   1089       O  
ATOM   5208  CB  ILE A 722      15.940  29.954  18.370  1.00136.08           C  
ANISOU 5208  CB  ILE A 722    16314  17990  17400      3   3196   2118       C  
ATOM   5209  CG1 ILE A 722      15.883  29.446  16.932  1.00132.15           C  
ANISOU 5209  CG1 ILE A 722    15669  17192  17351    236   2824   2361       C  
ATOM   5210  CG2 ILE A 722      14.611  30.549  18.795  1.00139.88           C  
ANISOU 5210  CG2 ILE A 722    16585  18601  17963    100   3713   1998       C  
ATOM   5211  CD1 ILE A 722      15.597  30.529  15.943  1.00131.05           C  
ANISOU 5211  CD1 ILE A 722    15461  16729  17602    578   2997   2160       C  
ATOM   5212  N   GLU A 723      17.320  30.801  20.949  1.00136.85           N  
ANISOU 5212  N   GLU A 723    16970  18570  16456   -597   3572   1615       N  
ATOM   5213  CA  GLU A 723      17.265  31.288  22.322  1.00141.34           C  
ANISOU 5213  CA  GLU A 723    17699  19460  16542   -881   3956   1365       C  
ATOM   5214  C   GLU A 723      18.254  32.419  22.578  1.00141.50           C  
ANISOU 5214  C   GLU A 723    18036  19347  16379   -883   4090    956       C  
ATOM   5215  O   GLU A 723      18.115  33.131  23.579  1.00145.45           O  
ANISOU 5215  O   GLU A 723    18675  20047  16543  -1045   4502    641       O  
ATOM   5216  CB  GLU A 723      17.511  30.135  23.295  1.00142.92           C  
ANISOU 5216  CB  GLU A 723    17962  20032  16309  -1340   3705   1675       C  
ATOM   5217  CG  GLU A 723      16.430  29.066  23.258  1.00143.73           C  
ANISOU 5217  CG  GLU A 723    17756  20325  16530  -1392   3625   2068       C  
ATOM   5218  CD  GLU A 723      15.085  29.573  23.746  1.00147.91           C  
ANISOU 5218  CD  GLU A 723    18085  21070  17043  -1339   4201   1906       C  
ATOM   5219  OE1 GLU A 723      15.065  30.448  24.637  1.00151.55           O  
ANISOU 5219  OE1 GLU A 723    18696  21705  17183  -1463   4648   1531       O  
ATOM   5220  OE2 GLU A 723      14.049  29.097  23.236  1.00147.73           O  
ANISOU 5220  OE2 GLU A 723    17751  21039  17342  -1176   4211   2147       O  
ATOM   5221  N   VAL A 724      19.247  32.601  21.706  1.00143.50           N  
ANISOU 5221  N   VAL A 724    18408  19278  16837   -723   3759    945       N  
ATOM   5222  CA  VAL A 724      20.105  33.777  21.806  1.00143.88           C  
ANISOU 5222  CA  VAL A 724    18729  19158  16780   -677   3892    559       C  
ATOM   5223  C   VAL A 724      19.451  34.981  21.139  1.00144.33           C  
ANISOU 5223  C   VAL A 724    18672  18937  17230   -286   4251    254       C  
ATOM   5224  O   VAL A 724      19.491  36.096  21.671  1.00145.83           O  
ANISOU 5224  O   VAL A 724    19013  19105  17291   -274   4621   -143       O  
ATOM   5225  CB  VAL A 724      21.494  33.483  21.209  1.00141.72           C  
ANISOU 5225  CB  VAL A 724    18625  18679  16544   -698   3390    677       C  
ATOM   5226  CG1 VAL A 724      22.312  34.760  21.119  1.00142.34           C  
ANISOU 5226  CG1 VAL A 724    18952  18541  16591   -601   3513    298       C  
ATOM   5227  CG2 VAL A 724      22.227  32.461  22.060  1.00141.27           C  
ANISOU 5227  CG2 VAL A 724    18704  18882  16090  -1119   3061    931       C  
ATOM   5228  N   LEU A 725      18.828  34.780  19.974  1.00142.92           N  
ANISOU 5228  N   LEU A 725    18224  18532  17547     23   4137    439       N  
ATOM   5229  CA  LEU A 725      18.231  35.904  19.261  1.00142.62           C  
ANISOU 5229  CA  LEU A 725    18058  18196  17937    383   4413    201       C  
ATOM   5230  C   LEU A 725      16.961  36.422  19.921  1.00145.15           C  
ANISOU 5230  C   LEU A 725    18195  18652  18303    442   4958      3       C  
ATOM   5231  O   LEU A 725      16.567  37.561  19.654  1.00145.35           O  
ANISOU 5231  O   LEU A 725    18160  18442  18625    694   5262   -293       O  
ATOM   5232  CB  LEU A 725      17.942  35.530  17.807  1.00139.74           C  
ANISOU 5232  CB  LEU A 725    17464  17556  18076    655   4107    481       C  
ATOM   5233  CG  LEU A 725      19.101  35.754  16.833  1.00137.72           C  
ANISOU 5233  CG  LEU A 725    17366  17013  17946    748   3734    478       C  
ATOM   5234  CD1 LEU A 725      20.225  34.766  17.069  1.00137.88           C  
ANISOU 5234  CD1 LEU A 725    17566  17171  17650    485   3327    666       C  
ATOM   5235  CD2 LEU A 725      18.612  35.680  15.398  1.00134.69           C  
ANISOU 5235  CD2 LEU A 725    16750  16353  18075   1025   3545    675       C  
ATOM   5236  N   ILE A 726      16.309  35.628  20.778  1.00141.07           N  
ANISOU 5236  N   ILE A 726    17575  18505  17520    210   5091    157       N  
ATOM   5237  CA  ILE A 726      15.169  36.158  21.525  1.00146.08           C  
ANISOU 5237  CA  ILE A 726    18044  19309  18148    234   5660    -82       C  
ATOM   5238  C   ILE A 726      15.603  37.077  22.654  1.00149.88           C  
ANISOU 5238  C   ILE A 726    18808  19926  18215     49   6042   -552       C  
ATOM   5239  O   ILE A 726      14.745  37.619  23.363  1.00154.60           O  
ANISOU 5239  O   ILE A 726    19298  20670  18772     50   6568   -836       O  
ATOM   5240  CB  ILE A 726      14.272  35.025  22.068  1.00148.02           C  
ANISOU 5240  CB  ILE A 726    18070  19935  18237     28   5698    241       C  
ATOM   5241  CG1 ILE A 726      15.046  34.085  22.999  1.00148.27           C  
ANISOU 5241  CG1 ILE A 726    18337  20328  17670   -432   5442    423       C  
ATOM   5242  CG2 ILE A 726      13.653  34.241  20.921  1.00144.84           C  
ANISOU 5242  CG2 ILE A 726    17360  19367  18305    246   5380    671       C  
ATOM   5243  CD1 ILE A 726      14.978  34.451  24.475  1.00153.55           C  
ANISOU 5243  CD1 ILE A 726    19176  21378  17786   -772   5874    119       C  
ATOM   5244  N   ASP A 727      16.909  37.266  22.845  1.00152.61           N  
ANISOU 5244  N   ASP A 727    19506  20225  18253   -119   5799   -652       N  
ATOM   5245  CA  ASP A 727      17.438  38.167  23.860  1.00154.22           C  
ANISOU 5245  CA  ASP A 727    20021  20527  18050   -313   6111  -1095       C  
ATOM   5246  C   ASP A 727      17.814  39.535  23.312  1.00153.22           C  
ANISOU 5246  C   ASP A 727    20000  19988  18230    -16   6232  -1471       C  
ATOM   5247  O   ASP A 727      17.763  40.521  24.055  1.00155.42           O  
ANISOU 5247  O   ASP A 727    20424  20282  18345    -57   6651  -1924       O  
ATOM   5248  CB  ASP A 727      18.672  37.551  24.529  1.00154.56           C  
ANISOU 5248  CB  ASP A 727    20401  20790  17534   -732   5759   -958       C  
ATOM   5249  CG  ASP A 727      18.333  36.354  25.394  1.00156.97           C  
ANISOU 5249  CG  ASP A 727    20654  21552  17435  -1120   5699   -653       C  
ATOM   5250  OD1 ASP A 727      17.212  36.311  25.944  1.00160.12           O  
ANISOU 5250  OD1 ASP A 727    20858  22197  17782  -1161   6109   -724       O  
ATOM   5251  OD2 ASP A 727      19.191  35.455  25.524  1.00156.09           O  
ANISOU 5251  OD2 ASP A 727    20682  21550  17075  -1391   5233   -335       O  
ATOM   5252  N   LYS A 728      18.194  39.614  22.040  1.00158.62           N  
ANISOU 5252  N   LYS A 728    20617  20308  19345    261   5870  -1299       N  
ATOM   5253  CA  LYS A 728      18.632  40.865  21.433  1.00157.32           C  
ANISOU 5253  CA  LYS A 728    20552  19743  19480    518   5904  -1596       C  
ATOM   5254  C   LYS A 728      17.521  41.910  21.452  1.00158.49           C  
ANISOU 5254  C   LYS A 728    20484  19718  20018    795   6413  -1934       C  
ATOM   5255  O   LYS A 728      16.470  41.720  20.840  1.00158.23           O  
ANISOU 5255  O   LYS A 728    20095  19592  20434   1032   6486  -1764       O  
ATOM   5256  CB  LYS A 728      19.090  40.626  19.996  1.00154.28           C  
ANISOU 5256  CB  LYS A 728    20082  19045  19493    739   5420  -1294       C  
ATOM   5257  CG  LYS A 728      20.209  39.607  19.850  1.00153.79           C  
ANISOU 5257  CG  LYS A 728    20194  19100  19140    509   4909   -978       C  
ATOM   5258  CD  LYS A 728      21.518  40.102  20.439  1.00154.24           C  
ANISOU 5258  CD  LYS A 728    20638  19169  18798    290   4818  -1198       C  
ATOM   5259  CE  LYS A 728      22.637  39.099  20.186  1.00153.20           C  
ANISOU 5259  CE  LYS A 728    20628  19105  18475     96   4291   -869       C  
ATOM   5260  NZ  LYS A 728      23.933  39.529  20.779  1.00153.41           N  
ANISOU 5260  NZ  LYS A 728    21018  19149  18121   -139   4174  -1041       N  
ATOM   5261  N   TYR A 730      15.376  40.038  18.881  1.00155.26           N  
ANISOU 5261  N   TYR A 730    19146  19089  20758   1314   5904   -878       N  
ATOM   5262  CA  TYR A 730      14.646  40.370  17.665  1.00153.19           C  
ANISOU 5262  CA  TYR A 730    18579  18478  21148   1654   5830   -730       C  
ATOM   5263  C   TYR A 730      13.369  39.541  17.566  1.00153.31           C  
ANISOU 5263  C   TYR A 730    18227  18647  21377   1700   5912   -418       C  
ATOM   5264  O   TYR A 730      12.526  39.786  16.705  1.00151.95           O  
ANISOU 5264  O   TYR A 730    17754  18224  21757   1961   5914   -281       O  
ATOM   5265  CB  TYR A 730      15.504  40.115  16.423  1.00150.50           C  
ANISOU 5265  CB  TYR A 730    18327  17895  20959   1717   5284   -470       C  
ATOM   5266  CG  TYR A 730      16.812  40.873  16.370  1.00150.82           C  
ANISOU 5266  CG  TYR A 730    18709  17775  20822   1673   5142   -718       C  
ATOM   5267  CD1 TYR A 730      16.851  42.218  16.030  1.00151.00           C  
ANISOU 5267  CD1 TYR A 730    18750  17459  21165   1880   5289  -1013       C  
ATOM   5268  CD2 TYR A 730      18.014  40.228  16.625  1.00150.96           C  
ANISOU 5268  CD2 TYR A 730    19012  17961  20384   1421   4829   -632       C  
ATOM   5269  CE1 TYR A 730      18.053  42.904  15.971  1.00150.92           C  
ANISOU 5269  CE1 TYR A 730    19050  17305  20988   1828   5138  -1217       C  
ATOM   5270  CE2 TYR A 730      19.216  40.903  16.565  1.00150.65           C  
ANISOU 5270  CE2 TYR A 730    19270  17780  20191   1374   4687   -834       C  
ATOM   5271  CZ  TYR A 730      19.231  42.239  16.240  1.00150.50           C  
ANISOU 5271  CZ  TYR A 730    19277  17444  20460   1573   4843  -1124       C  
ATOM   5272  OH  TYR A 730      20.432  42.909  16.183  1.00149.68           O  
ANISOU 5272  OH  TYR A 730    19469  17205  20198   1513   4687  -1308       O  
ATOM   5273  N   ILE A 731      13.239  38.549  18.446  1.00152.55           N  
ANISOU 5273  N   ILE A 731    18153  18964  20844   1425   5953   -278       N  
ATOM   5274  CA  ILE A 731      12.205  37.526  18.342  1.00152.91           C  
ANISOU 5274  CA  ILE A 731    17887  19199  21013   1408   5921    100       C  
ATOM   5275  C   ILE A 731      11.521  37.366  19.693  1.00157.95           C  
ANISOU 5275  C   ILE A 731    18460  20245  21310   1203   6386    -52       C  
ATOM   5276  O   ILE A 731      12.176  37.411  20.740  1.00159.68           O  
ANISOU 5276  O   ILE A 731    18961  20721  20988    924   6514   -278       O  
ATOM   5277  CB  ILE A 731      12.802  36.182  17.868  1.00148.50           C  
ANISOU 5277  CB  ILE A 731    17407  18743  20273   1238   5359    547       C  
ATOM   5278  CG1 ILE A 731      13.405  36.329  16.470  1.00143.86           C  
ANISOU 5278  CG1 ILE A 731    16859  17771  20030   1433   4934    682       C  
ATOM   5279  CG2 ILE A 731      11.754  35.080  17.873  1.00149.18           C  
ANISOU 5279  CG2 ILE A 731    17193  19047  20442   1181   5314    942       C  
ATOM   5280  CD1 ILE A 731      14.246  35.150  16.047  1.00139.72           C  
ANISOU 5280  CD1 ILE A 731    16467  17316  19305   1264   4403   1010       C  
ATOM   5281  N   GLU A 732      10.201  37.177  19.668  1.00162.53           N  
ANISOU 5281  N   GLU A 732    18662  20892  22198   1321   6636     80       N  
ATOM   5282  CA  GLU A 732       9.409  36.958  20.869  1.00166.18           C  
ANISOU 5282  CA  GLU A 732    19000  21768  22372   1127   7094    -31       C  
ATOM   5283  C   GLU A 732       8.516  35.738  20.681  1.00165.72           C  
ANISOU 5283  C   GLU A 732    18641  21925  22401   1059   6931    467       C  
ATOM   5284  O   GLU A 732       8.081  35.433  19.567  1.00162.48           O  
ANISOU 5284  O   GLU A 732    18006  21261  22470   1280   6643    800       O  
ATOM   5285  CB  GLU A 732       8.547  38.186  21.207  1.00168.95           C  
ANISOU 5285  CB  GLU A 732    19145  21994  23053   1356   7715   -478       C  
ATOM   5286  CG  GLU A 732       7.770  38.066  22.508  1.00174.79           C  
ANISOU 5286  CG  GLU A 732    19767  23185  23461   1140   8261   -674       C  
ATOM   5287  CD  GLU A 732       6.926  39.286  22.799  1.00180.08           C  
ANISOU 5287  CD  GLU A 732    20206  23699  24515   1392   8891  -1152       C  
ATOM   5288  OE1 GLU A 732       6.927  40.220  21.970  1.00179.11           O  
ANISOU 5288  OE1 GLU A 732    20006  23094  24953   1739   8866  -1298       O  
ATOM   5289  OE2 GLU A 732       6.258  39.309  23.854  1.00185.43           O  
ANISOU 5289  OE2 GLU A 732    20770  24737  24949   1232   9408  -1384       O  
ATOM   5290  N   ARG A 733       8.252  35.038  21.784  1.00173.97           N  
ANISOU 5290  N   ARG A 733    19691  23449  22962    725   7102    527       N  
ATOM   5291  CA  ARG A 733       7.355  33.889  21.797  1.00174.41           C  
ANISOU 5291  CA  ARG A 733    19458  23765  23045    614   6990    985       C  
ATOM   5292  C   ARG A 733       6.456  33.988  23.020  1.00179.32           C  
ANISOU 5292  C   ARG A 733    19914  24812  23408    430   7578    788       C  
ATOM   5293  O   ARG A 733       6.939  34.239  24.127  1.00182.82           O  
ANISOU 5293  O   ARG A 733    20610  25547  23305    143   7839    472       O  
ATOM   5294  CB  ARG A 733       8.143  32.573  21.802  1.00173.33           C  
ANISOU 5294  CB  ARG A 733    19522  23812  22523    307   6411   1402       C  
ATOM   5295  CG  ARG A 733       8.869  32.306  20.491  1.00170.53           C  
ANISOU 5295  CG  ARG A 733    19260  23057  22478    496   5834   1640       C  
ATOM   5296  CD  ARG A 733       9.683  31.022  20.518  1.00169.19           C  
ANISOU 5296  CD  ARG A 733    19272  23039  21973    206   5276   2009       C  
ATOM   5297  NE  ARG A 733      10.326  30.782  19.229  1.00164.17           N  
ANISOU 5297  NE  ARG A 733    18699  22023  21656    397   4772   2195       N  
ATOM   5298  CZ  ARG A 733      11.149  29.771  18.971  1.00162.04           C  
ANISOU 5298  CZ  ARG A 733    18578  21759  21230    230   4246   2477       C  
ATOM   5299  NH1 ARG A 733      11.448  28.895  19.920  1.00164.02           N  
ANISOU 5299  NH1 ARG A 733    18930  22361  21029   -139   4112   2641       N  
ATOM   5300  NH2 ARG A 733      11.674  29.640  17.761  1.00158.03           N  
ANISOU 5300  NH2 ARG A 733    18109  20906  21031    418   3851   2592       N  
ATOM   5301  N   SER A 734       5.151  33.792  22.817  1.00200.15           N  
ANISOU 5301  N   SER A 734    22124  27494  26429    576   7787    977       N  
ATOM   5302  CA  SER A 734       4.165  34.078  23.857  1.00203.84           C  
ANISOU 5302  CA  SER A 734    22363  28318  26771    474   8432    729       C  
ATOM   5303  C   SER A 734       3.810  32.848  24.692  1.00204.91           C  
ANISOU 5303  C   SER A 734    22440  29011  26406     51   8376   1076       C  
ATOM   5304  O   SER A 734       4.027  32.834  25.908  1.00208.50           O  
ANISOU 5304  O   SER A 734    23071  29892  26256   -314   8669    845       O  
ATOM   5305  CB  SER A 734       2.901  34.671  23.224  1.00203.65           C  
ANISOU 5305  CB  SER A 734    21865  28021  27490    879   8746    708       C  
ATOM   5306  OG  SER A 734       3.172  35.924  22.620  1.00202.89           O  
ANISOU 5306  OG  SER A 734    21811  27435  27844   1235   8862    339       O  
ATOM   5307  N   GLN A 735       3.264  31.812  24.058  1.00220.47           N  
ANISOU 5307  N   GLN A 735    24169  30988  28612     69   7989   1639       N  
ATOM   5308  CA  GLN A 735       2.778  30.654  24.796  1.00222.02           C  
ANISOU 5308  CA  GLN A 735    24250  31696  28410   -315   7933   2007       C  
ATOM   5309  C   GLN A 735       2.745  29.448  23.869  1.00219.21           C  
ANISOU 5309  C   GLN A 735    23801  31212  28276   -301   7258   2644       C  
ATOM   5310  O   GLN A 735       2.362  29.567  22.702  1.00217.13           O  
ANISOU 5310  O   GLN A 735    23340  30542  28617     59   7066   2818       O  
ATOM   5311  CB  GLN A 735       1.385  30.917  25.383  1.00224.84           C  
ANISOU 5311  CB  GLN A 735    24192  32334  28903   -292   8562   1894       C  
ATOM   5312  CG  GLN A 735       0.866  29.805  26.278  1.00226.33           C  
ANISOU 5312  CG  GLN A 735    24263  33113  28618   -738   8567   2238       C  
ATOM   5313  CD  GLN A 735       1.730  29.600  27.508  1.00227.92           C  
ANISOU 5313  CD  GLN A 735    24852  33754  27994  -1244   8611   2060       C  
ATOM   5314  OE1 GLN A 735       2.491  28.637  27.593  1.00225.63           O  
ANISOU 5314  OE1 GLN A 735    24801  33586  27344  -1550   8055   2420       O  
ATOM   5315  NE2 GLN A 735       1.618  30.512  28.468  1.00231.62           N  
ANISOU 5315  NE2 GLN A 735    25381  34450  28174  -1345   9267   1498       N  
ATOM   5316  N   ALA A 736       3.148  28.291  24.397  1.00228.36           N  
ANISOU 5316  N   ALA A 736    25106  32713  28949   -712   6889   2991       N  
ATOM   5317  CA  ALA A 736       3.250  27.067  23.604  1.00224.86           C  
ANISOU 5317  CA  ALA A 736    24618  32152  28666   -742   6211   3574       C  
ATOM   5318  C   ALA A 736       2.076  26.142  23.918  1.00225.21           C  
ANISOU 5318  C   ALA A 736    24307  32549  28714   -921   6234   4008       C  
ATOM   5319  O   ALA A 736       2.176  25.199  24.703  1.00225.26           O  
ANISOU 5319  O   ALA A 736    24373  32964  28253  -1346   6049   4280       O  
ATOM   5320  CB  ALA A 736       4.591  26.382  23.854  1.00222.99           C  
ANISOU 5320  CB  ALA A 736    24777  31971  27978  -1051   5696   3692       C  
ATOM   5321  N   SER A 737       0.941  26.427  23.282  1.00225.60           N  
ANISOU 5321  N   SER A 737    23971  32428  29319   -602   6445   4094       N  
ATOM   5322  CA  SER A 737      -0.131  25.455  23.100  1.00224.13           C  
ANISOU 5322  CA  SER A 737    23428  32412  29321   -672   6283   4622       C  
ATOM   5323  C   SER A 737      -0.143  24.908  21.682  1.00219.67           C  
ANISOU 5323  C   SER A 737    22794  31401  29271   -418   5694   5029       C  
ATOM   5324  O   SER A 737      -0.270  23.695  21.482  1.00216.80           O  
ANISOU 5324  O   SER A 737    22380  31132  28864   -603   5211   5534       O  
ATOM   5325  CB  SER A 737      -1.491  26.081  23.425  1.00226.29           C  
ANISOU 5325  CB  SER A 737    23272  32839  29867   -526   6935   4479       C  
ATOM   5326  OG  SER A 737      -1.581  26.429  24.796  1.00230.32           O  
ANISOU 5326  OG  SER A 737    23823  33836  29853   -822   7490   4130       O  
ATOM   5327  N   ALA A 738      -0.018  25.794  20.700  1.00209.00           N  
ANISOU 5327  N   ALA A 738    21444  29566  28401    -15   5725   4812       N  
ATOM   5328  CA  ALA A 738       0.451  25.465  19.364  1.00204.37           C  
ANISOU 5328  CA  ALA A 738    20956  28525  28172    187   5147   5053       C  
ATOM   5329  C   ALA A 738       1.741  26.241  19.147  1.00203.83           C  
ANISOU 5329  C   ALA A 738    21270  28185  27991    292   5096   4634       C  
ATOM   5330  O   ALA A 738       1.807  27.431  19.471  1.00206.11           O  
ANISOU 5330  O   ALA A 738    21594  28412  28308    440   5573   4162       O  
ATOM   5331  CB  ALA A 738      -0.587  25.821  18.297  1.00202.37           C  
ANISOU 5331  CB  ALA A 738    20347  27934  28609    540   5185   5225       C  
ATOM   5332  N   ASP A 739       2.767  25.562  18.631  1.00184.96           N  
ANISOU 5332  N   ASP A 739    19159  25639  25478    208   4527   4797       N  
ATOM   5333  CA  ASP A 739       4.080  26.180  18.479  1.00184.74           C  
ANISOU 5333  CA  ASP A 739    19501  25393  25298    263   4439   4434       C  
ATOM   5334  C   ASP A 739       3.971  27.491  17.709  1.00183.89           C  
ANISOU 5334  C   ASP A 739    19343  24887  25638    650   4696   4109       C  
ATOM   5335  O   ASP A 739       3.220  27.599  16.736  1.00181.49           O  
ANISOU 5335  O   ASP A 739    18790  24316  25852    897   4622   4303       O  
ATOM   5336  CB  ASP A 739       5.039  25.221  17.771  1.00182.09           C  
ANISOU 5336  CB  ASP A 739    19386  24879  24921    181   3768   4701       C  
ATOM   5337  CG  ASP A 739       5.427  24.037  18.641  1.00182.85           C  
ANISOU 5337  CG  ASP A 739    19592  25332  24549   -225   3484   4959       C  
ATOM   5338  OD1 ASP A 739       5.444  24.191  19.882  1.00186.29           O  
ANISOU 5338  OD1 ASP A 739    20086  26145  24549   -481   3803   4801       O  
ATOM   5339  OD2 ASP A 739       5.717  22.955  18.087  1.00179.81           O  
ANISOU 5339  OD2 ASP A 739    19235  24848  24238   -304   2934   5318       O  
ATOM   5340  N   GLU A 740       4.717  28.495  18.165  1.00175.23           N  
ANISOU 5340  N   GLU A 740    18485  23749  24343    681   4982   3627       N  
ATOM   5341  CA  GLU A 740       4.545  29.853  17.671  1.00175.25           C  
ANISOU 5341  CA  GLU A 740    18424  23415  24748   1019   5303   3274       C  
ATOM   5342  C   GLU A 740       5.812  30.654  17.935  1.00175.47           C  
ANISOU 5342  C   GLU A 740    18834  23337  24498   1005   5356   2833       C  
ATOM   5343  O   GLU A 740       6.387  30.576  19.023  1.00178.34           O  
ANISOU 5343  O   GLU A 740    19421  24008  24330    735   5496   2639       O  
ATOM   5344  CB  GLU A 740       3.332  30.520  18.336  1.00178.53           C  
ANISOU 5344  CB  GLU A 740    18511  23988  25335   1108   5929   3091       C  
ATOM   5345  CG  GLU A 740       2.969  31.892  17.790  1.00178.31           C  
ANISOU 5345  CG  GLU A 740    18337  23572  25841   1478   6251   2770       C  
ATOM   5346  CD  GLU A 740       3.709  33.013  18.495  1.00181.00           C  
ANISOU 5346  CD  GLU A 740    18940  23898  25936   1486   6626   2184       C  
ATOM   5347  OE1 GLU A 740       4.048  32.846  19.686  1.00183.69           O  
ANISOU 5347  OE1 GLU A 740    19459  24626  25710   1200   6854   1985       O  
ATOM   5348  OE2 GLU A 740       3.950  34.061  17.860  1.00180.45           O  
ANISOU 5348  OE2 GLU A 740    18902  23428  26233   1757   6677   1933       O  
ATOM   5349  N   TYR A 741       6.233  31.423  16.931  1.00162.19           N  
ANISOU 5349  N   TYR A 741    17224  21228  23174   1274   5230   2695       N  
ATOM   5350  CA  TYR A 741       7.414  32.276  17.049  1.00162.52           C  
ANISOU 5350  CA  TYR A 741    17611  21122  23019   1292   5264   2288       C  
ATOM   5351  C   TYR A 741       7.177  33.526  16.215  1.00160.80           C  
ANISOU 5351  C   TYR A 741    17286  20476  23334   1643   5420   2067       C  
ATOM   5352  O   TYR A 741       7.190  33.460  14.981  1.00156.28           O  
ANISOU 5352  O   TYR A 741    16650  19586  23143   1808   5068   2293       O  
ATOM   5353  CB  TYR A 741       8.673  31.543  16.593  1.00160.24           C  
ANISOU 5353  CB  TYR A 741    17625  20770  22488   1152   4706   2448       C  
ATOM   5354  N   SER A 742       6.965  34.656  16.881  1.00160.68           N  
ANISOU 5354  N   SER A 742    17253  20448  23348   1736   5933   1629       N  
ATOM   5355  CA  SER A 742       6.728  35.925  16.212  1.00159.17           C  
ANISOU 5355  CA  SER A 742    16950  19840  23689   2059   6102   1392       C  
ATOM   5356  C   SER A 742       8.027  36.717  16.100  1.00158.27           C  
ANISOU 5356  C   SER A 742    17210  19523  23402   2071   5999   1056       C  
ATOM   5357  O   SER A 742       9.075  36.325  16.618  1.00159.58           O  
ANISOU 5357  O   SER A 742    17712  19885  23038   1833   5843    983       O  
ATOM   5358  CB  SER A 742       5.666  36.738  16.963  1.00162.66           C  
ANISOU 5358  CB  SER A 742    17110  20340  24353   2183   6736   1089       C  
ATOM   5359  OG  SER A 742       5.448  37.990  16.336  1.00162.13           O  
ANISOU 5359  OG  SER A 742    16919  19833  24851   2498   6879    859       O  
ATOM   5360  N   TYR A 743       7.945  37.852  15.409  1.00147.29           N  
ANISOU 5360  N   TYR A 743    15747  17727  22489   2342   6068    872       N  
ATOM   5361  CA  TYR A 743       9.098  38.702  15.162  1.00145.38           C  
ANISOU 5361  CA  TYR A 743    15824  17247  22168   2381   5952    579       C  
ATOM   5362  C   TYR A 743       8.896  40.067  15.805  1.00149.81           C  
ANISOU 5362  C   TYR A 743    16370  17673  22877   2522   6462     67       C  
ATOM   5363  O   TYR A 743       7.774  40.572  15.893  1.00153.66           O  
ANISOU 5363  O   TYR A 743    16517  18061  23804   2711   6820    -14       O  
ATOM   5364  CB  TYR A 743       9.354  38.866  13.659  1.00141.41           C  
ANISOU 5364  CB  TYR A 743    15292  16351  22088   2545   5500    824       C  
ATOM   5365  CG  TYR A 743      10.559  39.719  13.331  1.00139.35           C  
ANISOU 5365  CG  TYR A 743    15346  15853  21749   2570   5348    559       C  
ATOM   5366  CD1 TYR A 743      11.847  39.235  13.513  1.00136.22           C  
ANISOU 5366  CD1 TYR A 743    15313  15609  20836   2356   5076    536       C  
ATOM   5367  CD2 TYR A 743      10.409  41.005  12.831  1.00140.71           C  
ANISOU 5367  CD2 TYR A 743    15436  15637  22391   2800   5457    352       C  
ATOM   5368  CE1 TYR A 743      12.951  40.010  13.213  1.00134.45           C  
ANISOU 5368  CE1 TYR A 743    15364  15178  20542   2371   4935    310       C  
ATOM   5369  CE2 TYR A 743      11.507  41.787  12.527  1.00138.94           C  
ANISOU 5369  CE2 TYR A 743    15495  15202  22092   2807   5300    131       C  
ATOM   5370  CZ  TYR A 743      12.775  41.285  12.720  1.00135.77           C  
ANISOU 5370  CZ  TYR A 743    15456  14980  21151   2592   5048    110       C  
ATOM   5371  OH  TYR A 743      13.871  42.060  12.418  1.00134.11           O  
ANISOU 5371  OH  TYR A 743    15516  14571  20868   2591   4891    -96       O  
ATOM   5372  N   VAL A 744      10.001  40.654  16.260  1.00151.66           N  
ANISOU 5372  N   VAL A 744    16969  17895  22759   2427   6489   -283       N  
ATOM   5373  CA  VAL A 744      10.022  41.992  16.837  1.00155.09           C  
ANISOU 5373  CA  VAL A 744    17462  18166  23299   2544   6921   -808       C  
ATOM   5374  C   VAL A 744      11.011  42.831  16.040  1.00152.21           C  
ANISOU 5374  C   VAL A 744    17322  17419  23091   2651   6623   -919       C  
ATOM   5375  O   VAL A 744      12.072  42.338  15.640  1.00149.04           O  
ANISOU 5375  O   VAL A 744    17192  17054  22384   2506   6195   -748       O  
ATOM   5376  CB  VAL A 744      10.399  41.959  18.334  1.00158.26           C  
ANISOU 5376  CB  VAL A 744    18118  18960  23053   2273   7288  -1168       C  
ATOM   5377  CG1 VAL A 744      10.485  43.368  18.905  1.00162.38           C  
ANISOU 5377  CG1 VAL A 744    18732  19291  23675   2386   7726  -1749       C  
ATOM   5378  CG2 VAL A 744       9.399  41.121  19.118  1.00161.38           C  
ANISOU 5378  CG2 VAL A 744    18277  19765  23274   2135   7581  -1040       C  
ATOM   5379  N   ALA A 745      10.658  44.092  15.803  1.00164.45           N  
ANISOU 5379  N   ALA A 745    18742  18598  25142   2900   6843  -1199       N  
ATOM   5380  CA  ALA A 745      11.474  44.994  14.992  1.00162.78           C  
ANISOU 5380  CA  ALA A 745    18700  17994  25156   3012   6563  -1287       C  
ATOM   5381  C   ALA A 745      12.910  45.113  15.505  1.00164.20           C  
ANISOU 5381  C   ALA A 745    19355  18298  24736   2793   6442  -1517       C  
ATOM   5382  O   ALA A 745      13.806  45.541  14.775  1.00161.95           O  
ANISOU 5382  O   ALA A 745    19258  17775  24502   2813   6099  -1490       O  
ATOM   5383  CB  ALA A 745      10.826  46.369  14.934  1.00163.08           C  
ANISOU 5383  CB  ALA A 745    18523  17637  25804   3288   6884  -1611       C  
ATOM   5384  OXT ALA A 745      13.215  44.785  16.652  1.00167.83           O  
ANISOU 5384  OXT ALA A 745    20019  19105  24645   2572   6671  -1719       O  
TER    5385      ALA A 745                                                      
ATOM   5386  N   THR V 157     -19.141  33.591 -61.624  1.00270.15           N  
ANISOU 5386  N   THR V 157    30910  51470  20266  19718   1732   4570       N  
ATOM   5387  CA  THR V 157     -19.745  32.438 -62.281  1.00270.46           C  
ANISOU 5387  CA  THR V 157    31017  51371  20373  19751   1637   4522       C  
ATOM   5388  C   THR V 157     -20.582  32.869 -63.481  1.00270.98           C  
ANISOU 5388  C   THR V 157    31174  51313  20474  19766   1527   4517       C  
ATOM   5389  O   THR V 157     -21.281  33.880 -63.431  1.00270.88           O  
ANISOU 5389  O   THR V 157    31186  51201  20533  19716   1478   4560       O  
ATOM   5390  CB  THR V 157     -20.626  31.634 -61.310  1.00269.91           C  
ANISOU 5390  CB  THR V 157    30935  51153  20463  19683   1593   4534       C  
ATOM   5391  OG1 THR V 157     -21.688  32.466 -60.827  1.00269.46           O  
ANISOU 5391  OG1 THR V 157    30873  51001  20508  19612   1556   4562       O  
ATOM   5392  CG2 THR V 157     -19.803  31.137 -60.133  1.00269.66           C  
ANISOU 5392  CG2 THR V 157    30808  51247  20404  19659   1677   4565       C  
ATOM   5393  N   LEU V 158     -20.502  32.092 -64.564  1.00271.67           N  
ANISOU 5393  N   LEU V 158    31303  51413  20508  19843   1472   4460       N  
ATOM   5394  CA  LEU V 158     -21.242  32.433 -65.774  1.00272.38           C  
ANISOU 5394  CA  LEU V 158    31467  51416  20607  19858   1361   4463       C  
ATOM   5395  C   LEU V 158     -22.736  32.194 -65.594  1.00271.95           C  
ANISOU 5395  C   LEU V 158    31475  51107  20745  19802   1253   4462       C  
ATOM   5396  O   LEU V 158     -23.557  33.014 -66.021  1.00272.19           O  
ANISOU 5396  O   LEU V 158    31557  51022  20842  19768   1164   4500       O  
ATOM   5397  CB  LEU V 158     -20.708  31.628 -66.958  1.00273.52           C  
ANISOU 5397  CB  LEU V 158    31610  51704  20612  19970   1334   4385       C  
ATOM   5398  CG  LEU V 158     -21.308  31.933 -68.332  1.00274.57           C  
ANISOU 5398  CG  LEU V 158    31799  51819  20707  19990   1220   4394       C  
ATOM   5399  CD1 LEU V 158     -20.988  33.358 -68.757  1.00275.17           C  
ANISOU 5399  CD1 LEU V 158    31870  51981  20703  19936   1211   4507       C  
ATOM   5400  CD2 LEU V 158     -20.813  30.936 -69.367  1.00275.81           C  
ANISOU 5400  CD2 LEU V 158    31923  52159  20714  20120   1193   4282       C  
ATOM   5401  N   LYS V 159     -23.105  31.078 -64.962  1.00276.59           N  
ANISOU 5401  N   LYS V 159    32053  51609  21431  19792   1242   4425       N  
ATOM   5402  CA  LYS V 159     -24.515  30.748 -64.783  1.00276.35           C  
ANISOU 5402  CA  LYS V 159    32056  51374  21569  19742   1139   4421       C  
ATOM   5403  C   LYS V 159     -25.238  31.812 -63.966  1.00275.79           C  
ANISOU 5403  C   LYS V 159    31957  51242  21589  19662   1134   4463       C  
ATOM   5404  O   LYS V 159     -26.254  32.364 -64.403  1.00276.06           O  
ANISOU 5404  O   LYS V 159    32034  51151  21705  19649   1031   4459       O  
ATOM   5405  CB  LYS V 159     -24.647  29.379 -64.114  1.00276.22           C  
ANISOU 5405  CB  LYS V 159    32012  51299  21641  19734   1122   4404       C  
ATOM   5406  CG  LYS V 159     -26.080  28.919 -63.910  1.00276.15           C  
ANISOU 5406  CG  LYS V 159    32016  51115  21795  19684   1015   4404       C  
ATOM   5407  CD  LYS V 159     -26.126  27.537 -63.281  1.00276.37           C  
ANISOU 5407  CD  LYS V 159    32008  51083  21916  19673    975   4418       C  
ATOM   5408  CE  LYS V 159     -27.556  27.092 -63.031  1.00276.45           C  
ANISOU 5408  CE  LYS V 159    32009  50957  22074  19620    870   4432       C  
ATOM   5409  NZ  LYS V 159     -27.620  25.739 -62.412  1.00276.97           N  
ANISOU 5409  NZ  LYS V 159    32034  50954  22246  19602    805   4478       N  
ATOM   5410  N   GLU V 160     -24.718  32.122 -62.777  1.00282.34           N  
ANISOU 5410  N   GLU V 160    32702  52173  22402  19620   1232   4494       N  
ATOM   5411  CA  GLU V 160     -25.448  32.992 -61.862  1.00282.01           C  
ANISOU 5411  CA  GLU V 160    32601  52107  22442  19562   1218   4505       C  
ATOM   5412  C   GLU V 160     -25.446  34.440 -62.340  1.00282.43           C  
ANISOU 5412  C   GLU V 160    32690  52136  22484  19577   1176   4519       C  
ATOM   5413  O   GLU V 160     -26.440  35.155 -62.167  1.00282.68           O  
ANISOU 5413  O   GLU V 160    32716  52063  22628  19563   1077   4497       O  
ATOM   5414  CB  GLU V 160     -24.860  32.882 -60.455  1.00281.46           C  
ANISOU 5414  CB  GLU V 160    32413  52192  22336  19518   1331   4533       C  
ATOM   5415  CG  GLU V 160     -25.628  33.652 -59.396  1.00281.32           C  
ANISOU 5415  CG  GLU V 160    32296  52212  22382  19471   1315   4521       C  
ATOM   5416  CD  GLU V 160     -25.072  33.434 -58.003  1.00280.96           C  
ANISOU 5416  CD  GLU V 160    32111  52363  22277  19424   1424   4557       C  
ATOM   5417  OE1 GLU V 160     -24.074  32.694 -57.869  1.00280.80           O  
ANISOU 5417  OE1 GLU V 160    32085  52419  22188  19424   1503   4601       O  
ATOM   5418  OE2 GLU V 160     -25.635  33.998 -57.042  1.00281.02           O  
ANISOU 5418  OE2 GLU V 160    32003  52465  22306  19393   1418   4534       O  
ATOM   5419  N   ARG V 161     -24.347  34.895 -62.947  1.00278.96           N  
ANISOU 5419  N   ARG V 161    32278  51796  21918  19612   1229   4557       N  
ATOM   5420  CA  ARG V 161     -24.320  36.266 -63.445  1.00279.69           C  
ANISOU 5420  CA  ARG V 161    32408  51849  22013  19617   1157   4605       C  
ATOM   5421  C   ARG V 161     -25.087  36.422 -64.751  1.00280.64           C  
ANISOU 5421  C   ARG V 161    32632  51812  22185  19632    999   4623       C  
ATOM   5422  O   ARG V 161     -25.580  37.517 -65.040  1.00281.45           O  
ANISOU 5422  O   ARG V 161    32776  51792  22368  19622    868   4665       O  
ATOM   5423  CB  ARG V 161     -22.881  36.757 -63.605  1.00279.95           C  
ANISOU 5423  CB  ARG V 161    32414  52073  21881  19635   1259   4662       C  
ATOM   5424  CG  ARG V 161     -22.206  37.074 -62.278  1.00279.26           C  
ANISOU 5424  CG  ARG V 161    32220  52132  21755  19615   1387   4659       C  
ATOM   5425  CD  ARG V 161     -20.832  37.692 -62.469  1.00279.67           C  
ANISOU 5425  CD  ARG V 161    32236  52378  21648  19635   1475   4716       C  
ATOM   5426  NE  ARG V 161     -20.191  37.988 -61.190  1.00279.05           N  
ANISOU 5426  NE  ARG V 161    32048  52455  21525  19618   1598   4710       N  
ATOM   5427  CZ  ARG V 161     -20.346  39.130 -60.526  1.00279.24           C  
ANISOU 5427  CZ  ARG V 161    32033  52468  21599  19601   1567   4726       C  
ATOM   5428  NH1 ARG V 161     -21.122  40.086 -61.017  1.00280.12           N  
ANISOU 5428  NH1 ARG V 161    32216  52389  21827  19602   1399   4753       N  
ATOM   5429  NH2 ARG V 161     -19.726  39.316 -59.368  1.00278.74           N  
ANISOU 5429  NH2 ARG V 161    31855  52584  21471  19590   1685   4713       N  
ATOM   5430  N   CYS V 162     -25.206  35.359 -65.551  1.00278.30           N  
ANISOU 5430  N   CYS V 162    32377  51514  21849  19661    988   4592       N  
ATOM   5431  CA  CYS V 162     -26.153  35.409 -66.661  1.00279.17           C  
ANISOU 5431  CA  CYS V 162    32572  51479  22021  19670    830   4598       C  
ATOM   5432  C   CYS V 162     -27.587  35.427 -66.148  1.00278.93           C  
ANISOU 5432  C   CYS V 162    32539  51261  22180  19646    728   4546       C  
ATOM   5433  O   CYS V 162     -28.447  36.099 -66.726  1.00279.79           O  
ANISOU 5433  O   CYS V 162    32702  51220  22386  19643    569   4565       O  
ATOM   5434  CB  CYS V 162     -25.928  34.240 -67.619  1.00279.50           C  
ANISOU 5434  CB  CYS V 162    32639  51596  21963  19723    840   4557       C  
ATOM   5435  SG  CYS V 162     -24.440  34.379 -68.634  1.00280.53           S  
ANISOU 5435  SG  CYS V 162    32753  51989  21846  19773    902   4600       S  
ATOM   5436  N   LEU V 163     -27.861  34.701 -65.060  1.00286.53           N  
ANISOU 5436  N   LEU V 163    33428  52246  23194  19626    802   4487       N  
ATOM   5437  CA  LEU V 163     -29.149  34.841 -64.387  1.00286.46           C  
ANISOU 5437  CA  LEU V 163    33372  52129  23340  19602    716   4432       C  
ATOM   5438  C   LEU V 163     -29.391  36.286 -63.965  1.00286.96           C  
ANISOU 5438  C   LEU V 163    33407  52144  23483  19604    643   4432       C  
ATOM   5439  O   LEU V 163     -30.493  36.818 -64.141  1.00287.71           O  
ANISOU 5439  O   LEU V 163    33506  52095  23714  19619    488   4389       O  
ATOM   5440  CB  LEU V 163     -29.214  33.917 -63.169  1.00285.61           C  
ANISOU 5440  CB  LEU V 163    33162  52116  23240  19566    813   4401       C  
ATOM   5441  CG  LEU V 163     -29.304  32.400 -63.338  1.00285.39           C  
ANISOU 5441  CG  LEU V 163    33147  52084  23205  19564    830   4394       C  
ATOM   5442  CD1 LEU V 163     -29.136  31.711 -61.994  1.00284.84           C  
ANISOU 5442  CD1 LEU V 163    32965  52124  23138  19515    915   4412       C  
ATOM   5443  CD2 LEU V 163     -30.632  32.015 -63.960  1.00285.90           C  
ANISOU 5443  CD2 LEU V 163    33247  52007  23373  19575    692   4348       C  
ATOM   5444  N   GLN V 164     -28.363  36.939 -63.416  1.00285.72           N  
ANISOU 5444  N   GLN V 164    33210  52102  23247  19599    737   4472       N  
ATOM   5445  CA  GLN V 164     -28.520  38.308 -62.936  1.00286.38           C  
ANISOU 5445  CA  GLN V 164    33255  52139  23416  19613    656   4463       C  
ATOM   5446  C   GLN V 164     -28.713  39.286 -64.089  1.00287.79           C  
ANISOU 5446  C   GLN V 164    33545  52141  23660  19636    473   4534       C  
ATOM   5447  O   GLN V 164     -29.479  40.249 -63.970  1.00288.82           O  
ANISOU 5447  O   GLN V 164    33665  52120  23952  19664    304   4499       O  
ATOM   5448  CB  GLN V 164     -27.311  38.702 -62.087  1.00285.87           C  
ANISOU 5448  CB  GLN V 164    33120  52260  23239  19603    805   4494       C  
ATOM   5449  CG  GLN V 164     -27.204  37.931 -60.780  1.00284.81           C  
ANISOU 5449  CG  GLN V 164    32856  52303  23057  19570    950   4441       C  
ATOM   5450  CD  GLN V 164     -25.965  38.290 -59.985  1.00284.39           C  
ANISOU 5450  CD  GLN V 164    32728  52449  22877  19560   1097   4476       C  
ATOM   5451  OE1 GLN V 164     -25.129  39.074 -60.435  1.00284.82           O  
ANISOU 5451  OE1 GLN V 164    32827  52518  22872  19581   1103   4538       O  
ATOM   5452  NE2 GLN V 164     -25.840  37.715 -58.794  1.00283.69           N  
ANISOU 5452  NE2 GLN V 164    32516  52535  22740  19524   1208   4450       N  
ATOM   5453  N   VAL V 165     -28.026  39.061 -65.212  1.00290.39           N  
ANISOU 5453  N   VAL V 165    33970  52498  23867  19626    485   4633       N  
ATOM   5454  CA  VAL V 165     -28.216  39.924 -66.374  1.00292.01           C  
ANISOU 5454  CA  VAL V 165    34282  52556  24110  19623    290   4739       C  
ATOM   5455  C   VAL V 165     -29.597  39.709 -66.983  1.00292.66           C  
ANISOU 5455  C   VAL V 165    34412  52449  24337  19637    116   4694       C  
ATOM   5456  O   VAL V 165     -30.224  40.660 -67.468  1.00294.17           O  
ANISOU 5456  O   VAL V 165    34659  52449  24664  19644   -105   4744       O  
ATOM   5457  CB  VAL V 165     -27.092  39.691 -67.403  1.00292.41           C  
ANISOU 5457  CB  VAL V 165    34391  52758  23952  19599    352   4855       C  
ATOM   5458  CG1 VAL V 165     -27.364  40.463 -68.685  1.00294.34           C  
ANISOU 5458  CG1 VAL V 165    34749  52877  24210  19565    128   4996       C  
ATOM   5459  CG2 VAL V 165     -25.749  40.106 -66.821  1.00292.07           C  
ANISOU 5459  CG2 VAL V 165    34292  52903  23777  19589    497   4903       C  
ATOM   5460  N   VAL V 166     -30.104  38.474 -66.955  1.00296.03           N  
ANISOU 5460  N   VAL V 166    34814  52916  24748  19642    193   4606       N  
ATOM   5461  CA  VAL V 166     -31.420  38.203 -67.527  1.00296.65           C  
ANISOU 5461  CA  VAL V 166    34925  52839  24949  19657     36   4556       C  
ATOM   5462  C   VAL V 166     -32.523  38.788 -66.651  1.00296.95           C  
ANISOU 5462  C   VAL V 166    34882  52757  25190  19685    -75   4447       C  
ATOM   5463  O   VAL V 166     -33.514  39.326 -67.161  1.00298.24           O  
ANISOU 5463  O   VAL V 166    35075  52739  25503  19711   -284   4431       O  
ATOM   5464  CB  VAL V 166     -31.607  36.690 -67.752  1.00295.74           C  
ANISOU 5464  CB  VAL V 166    34802  52808  24756  19659    139   4496       C  
ATOM   5465  CG1 VAL V 166     -33.046  36.378 -68.119  1.00296.26           C  
ANISOU 5465  CG1 VAL V 166    34876  52736  24954  19675     -8   4426       C  
ATOM   5466  CG2 VAL V 166     -30.685  36.209 -68.861  1.00296.03           C  
ANISOU 5466  CG2 VAL V 166    34908  52960  24611  19662    191   4572       C  
ATOM   5467  N   ARG V 167     -32.370  38.712 -65.325  1.00297.14           N  
ANISOU 5467  N   ARG V 167    34786  52897  25218  19684     49   4363       N  
ATOM   5468  CA  ARG V 167     -33.407  39.243 -64.443  1.00297.66           C  
ANISOU 5468  CA  ARG V 167    34733  52909  25455  19722    -53   4228       C  
ATOM   5469  C   ARG V 167     -33.553  40.756 -64.537  1.00299.29           C  
ANISOU 5469  C   ARG V 167    34948  52945  25821  19773   -251   4231       C  
ATOM   5470  O   ARG V 167     -34.524  41.299 -63.999  1.00300.21           O  
ANISOU 5470  O   ARG V 167    34962  52987  26119  19830   -387   4090       O  
ATOM   5471  CB  ARG V 167     -33.141  38.851 -62.989  1.00296.54           C  
ANISOU 5471  CB  ARG V 167    34439  52982  25251  19702    119   4149       C  
ATOM   5472  CG  ARG V 167     -33.299  37.371 -62.706  1.00295.39           C  
ANISOU 5472  CG  ARG V 167    34257  52967  25009  19655    253   4138       C  
ATOM   5473  CD  ARG V 167     -33.173  37.078 -61.222  1.00294.71           C  
ANISOU 5473  CD  ARG V 167    34003  53103  24871  19626    381   4083       C  
ATOM   5474  NE  ARG V 167     -33.265  35.648 -60.952  1.00293.90           N  
ANISOU 5474  NE  ARG V 167    33871  53107  24690  19576    480   4111       N  
ATOM   5475  CZ  ARG V 167     -32.210  34.849 -60.849  1.00292.99           C  
ANISOU 5475  CZ  ARG V 167    33792  53080  24452  19536    628   4204       C  
ATOM   5476  NH1 ARG V 167     -30.990  35.349 -60.973  1.00292.67           N  
ANISOU 5476  NH1 ARG V 167    33805  53071  24327  19539    713   4267       N  
ATOM   5477  NH2 ARG V 167     -32.372  33.556 -60.607  1.00292.61           N  
ANISOU 5477  NH2 ARG V 167    33714  53088  24375  19498    674   4233       N  
ATOM   5478  N   SER V 168     -32.622  41.447 -65.194  1.00297.22           N  
ANISOU 5478  N   SER V 168    34796  52630  25506  19759   -286   4383       N  
ATOM   5479  CA  SER V 168     -32.762  42.877 -65.430  1.00299.16           C  
ANISOU 5479  CA  SER V 168    35075  52669  25924  19803   -523   4425       C  
ATOM   5480  C   SER V 168     -33.592  43.191 -66.668  1.00300.87           C  
ANISOU 5480  C   SER V 168    35405  52647  26267  19811   -783   4497       C  
ATOM   5481  O   SER V 168     -33.886  44.365 -66.914  1.00302.88           O  
ANISOU 5481  O   SER V 168    35692  52680  26710  19852  -1038   4538       O  
ATOM   5482  CB  SER V 168     -31.382  43.528 -65.559  1.00299.35           C  
ANISOU 5482  CB  SER V 168    35163  52754  25824  19769   -470   4586       C  
ATOM   5483  OG  SER V 168     -30.709  43.070 -66.719  1.00299.31           O  
ANISOU 5483  OG  SER V 168    35285  52804  25634  19701   -427   4757       O  
ATOM   5484  N   LEU V 169     -33.975  42.174 -67.447  1.00299.44           N  
ANISOU 5484  N   LEU V 169    35279  52499  25994  19777   -744   4516       N  
ATOM   5485  CA  LEU V 169     -34.759  42.373 -68.661  1.00301.07           C  
ANISOU 5485  CA  LEU V 169    35587  52514  26291  19776   -982   4591       C  
ATOM   5486  C   LEU V 169     -35.951  41.425 -68.731  1.00300.58           C  
ANISOU 5486  C   LEU V 169    35473  52456  26278  19801   -982   4449       C  
ATOM   5487  O   LEU V 169     -36.532  41.249 -69.807  1.00301.56           O  
ANISOU 5487  O   LEU V 169    35677  52484  26417  19791  -1125   4509       O  
ATOM   5488  CB  LEU V 169     -33.881  42.207 -69.904  1.00301.46           C  
ANISOU 5488  CB  LEU V 169    35778  52627  26137  19695   -971   4806       C  
ATOM   5489  CG  LEU V 169     -32.779  43.249 -70.104  1.00302.55           C  
ANISOU 5489  CG  LEU V 169    35987  52754  26214  19649  -1032   4994       C  
ATOM   5490  CD1 LEU V 169     -31.898  42.880 -71.287  1.00302.90           C  
ANISOU 5490  CD1 LEU V 169    36133  52953  26002  19555   -986   5181       C  
ATOM   5491  CD2 LEU V 169     -33.381  44.633 -70.289  1.00305.05           C  
ANISOU 5491  CD2 LEU V 169    36353  52770  26784  19676  -1375   5065       C  
ATOM   5492  N   VAL V 170     -36.326  40.810 -67.612  1.00302.08           N  
ANISOU 5492  N   VAL V 170    28935  41066  44774  12552  15810  -1173       N  
ATOM   5493  CA  VAL V 170     -37.456  39.890 -67.548  1.00302.23           C  
ANISOU 5493  CA  VAL V 170    29088  41043  44702  12475  15957  -1195       C  
ATOM   5494  C   VAL V 170     -38.290  40.240 -66.324  1.00302.46           C  
ANISOU 5494  C   VAL V 170    29148  41065  44708  12506  15958  -1256       C  
ATOM   5495  O   VAL V 170     -37.747  40.402 -65.225  1.00302.85           O  
ANISOU 5495  O   VAL V 170    29228  41108  44731  12632  15907  -1269       O  
ATOM   5496  CB  VAL V 170     -37.000  38.419 -67.487  1.00302.77           C  
ANISOU 5496  CB  VAL V 170    29349  41053  44637  12522  16083  -1159       C  
ATOM   5497  CG1 VAL V 170     -38.191  37.505 -67.255  1.00303.06           C  
ANISOU 5497  CG1 VAL V 170    29536  41041  44572  12443  16248  -1193       C  
ATOM   5498  CG2 VAL V 170     -36.275  38.032 -68.767  1.00302.55           C  
ANISOU 5498  CG2 VAL V 170    29297  41029  44629  12482  16095  -1098       C  
ATOM   5499  N   LYS V 171     -39.602  40.360 -66.517  1.00307.34           N  
ANISOU 5499  N   LYS V 171    29751  41695  45330  12391  16016  -1293       N  
ATOM   5500  CA  LYS V 171     -40.496  40.639 -65.406  1.00307.57           C  
ANISOU 5500  CA  LYS V 171    29812  41721  45330  12411  16028  -1351       C  
ATOM   5501  C   LYS V 171     -40.459  39.494 -64.395  1.00308.23           C  
ANISOU 5501  C   LYS V 171    30098  41743  45275  12487  16135  -1362       C  
ATOM   5502  O   LYS V 171     -40.199  38.341 -64.756  1.00308.51           O  
ANISOU 5502  O   LYS V 171    30264  41735  45223  12475  16247  -1332       O  
ATOM   5503  CB  LYS V 171     -41.928  40.838 -65.902  1.00307.33           C  
ANISOU 5503  CB  LYS V 171    29731  41730  45310  12269  16085  -1383       C  
ATOM   5504  CG  LYS V 171     -42.163  42.110 -66.695  1.00306.78           C  
ANISOU 5504  CG  LYS V 171    29466  41726  45370  12209  15975  -1378       C  
ATOM   5505  CD  LYS V 171     -43.631  42.236 -67.073  1.00306.69           C  
ANISOU 5505  CD  LYS V 171    29411  41773  45345  12083  16039  -1409       C  
ATOM   5506  CE  LYS V 171     -43.903  43.501 -67.868  1.00306.23           C  
ANISOU 5506  CE  LYS V 171    29167  41782  45404  12035  15934  -1399       C  
ATOM   5507  NZ  LYS V 171     -45.342  43.621 -68.234  1.00306.25           N  
ANISOU 5507  NZ  LYS V 171    29117  41863  45379  11922  15994  -1425       N  
ATOM   5508  N   PRO V 172     -40.716  39.781 -63.114  1.00313.22           N  
ANISOU 5508  N   PRO V 172    30765  42364  45880  12567  16110  -1405       N  
ATOM   5509  CA  PRO V 172     -40.829  38.697 -62.127  1.00313.88           C  
ANISOU 5509  CA  PRO V 172    31048  42387  45825  12633  16221  -1420       C  
ATOM   5510  C   PRO V 172     -42.044  37.810 -62.337  1.00314.06           C  
ANISOU 5510  C   PRO V 172    31184  42384  45760  12511  16388  -1447       C  
ATOM   5511  O   PRO V 172     -42.146  36.765 -61.681  1.00314.66           O  
ANISOU 5511  O   PRO V 172    31447  42398  45711  12549  16507  -1455       O  
ATOM   5512  CB  PRO V 172     -40.913  39.446 -60.791  1.00314.07           C  
ANISOU 5512  CB  PRO V 172    31048  42421  45864  12732  16136  -1465       C  
ATOM   5513  CG  PRO V 172     -41.468  40.784 -61.148  1.00313.52           C  
ANISOU 5513  CG  PRO V 172    30793  42408  45922  12665  16035  -1490       C  
ATOM   5514  CD  PRO V 172     -40.914  41.109 -62.507  1.00313.03           C  
ANISOU 5514  CD  PRO V 172    30611  42377  45947  12604  15985  -1442       C  
ATOM   5515  N   GLU V 173     -42.962  38.190 -63.223  1.00312.32           N  
ANISOU 5515  N   GLU V 173    30859  42215  45593  12366  16406  -1462       N  
ATOM   5516  CA  GLU V 173     -44.128  37.383 -63.552  1.00312.53           C  
ANISOU 5516  CA  GLU V 173    30971  42242  45535  12230  16571  -1491       C  
ATOM   5517  C   GLU V 173     -43.884  36.471 -64.747  1.00312.54           C  
ANISOU 5517  C   GLU V 173    31029  42224  45499  12139  16679  -1450       C  
ATOM   5518  O   GLU V 173     -44.822  35.818 -65.217  1.00312.73           O  
ANISOU 5518  O   GLU V 173    31108  42260  45456  12003  16823  -1473       O  
ATOM   5519  CB  GLU V 173     -45.332  38.286 -63.832  1.00312.18           C  
ANISOU 5519  CB  GLU V 173    30774  42287  45554  12122  16537  -1531       C  
ATOM   5520  CG  GLU V 173     -45.791  39.108 -62.639  1.00312.26           C  
ANISOU 5520  CG  GLU V 173    30746  42312  45586  12197  16458  -1577       C  
ATOM   5521  CD  GLU V 173     -45.006  40.398 -62.484  1.00311.87           C  
ANISOU 5521  CD  GLU V 173    30552  42280  45663  12295  16272  -1560       C  
ATOM   5522  OE1 GLU V 173     -44.148  40.681 -63.347  1.00311.51           O  
ANISOU 5522  OE1 GLU V 173    30425  42244  45691  12298  16202  -1514       O  
ATOM   5523  OE2 GLU V 173     -45.246  41.128 -61.501  1.00311.95           O  
ANISOU 5523  OE2 GLU V 173    30534  42296  45697  12366  16201  -1596       O  
ATOM   5524  N   ASN V 174     -42.652  36.414 -65.247  1.00308.86           N  
ANISOU 5524  N   ASN V 174    30549  41735  45070  12208  16617  -1391       N  
ATOM   5525  CA  ASN V 174     -42.295  35.618 -66.414  1.00308.85           C  
ANISOU 5525  CA  ASN V 174    30595  41713  45041  12134  16706  -1346       C  
ATOM   5526  C   ASN V 174     -41.063  34.772 -66.118  1.00309.32           C  
ANISOU 5526  C   ASN V 174    30807  41693  45028  12267  16734  -1296       C  
ATOM   5527  O   ASN V 174     -40.158  34.639 -66.947  1.00309.15           O  
ANISOU 5527  O   ASN V 174    30758  41669  45036  12283  16704  -1240       O  
ATOM   5528  CB  ASN V 174     -42.072  36.515 -67.631  1.00308.12           C  
ANISOU 5528  CB  ASN V 174    30297  41693  45081  12065  16593  -1317       C  
ATOM   5529  CG  ASN V 174     -42.027  35.740 -68.936  1.00308.06           C  
ANISOU 5529  CG  ASN V 174    30323  41680  45047  11949  16700  -1282       C  
ATOM   5530  OD1 ASN V 174     -42.139  34.514 -68.951  1.00308.61           O  
ANISOU 5530  OD1 ASN V 174    30576  41684  44998  11918  16867  -1280       O  
ATOM   5531  ND2 ASN V 174     -41.867  36.457 -70.043  1.00307.44           N  
ANISOU 5531  ND2 ASN V 174    30072  41665  45078  11883  16611  -1256       N  
ATOM   5532  N   TYR V 175     -41.007  34.197 -64.919  1.00309.87           N  
ANISOU 5532  N   TYR V 175    17661  41194  58880  -3980    967   1451       N  
ATOM   5533  CA  TYR V 175     -39.919  33.311 -64.529  1.00309.97           C  
ANISOU 5533  CA  TYR V 175    17744  41315  58716  -4103    496   1456       C  
ATOM   5534  C   TYR V 175     -40.228  31.843 -64.790  1.00309.43           C  
ANISOU 5534  C   TYR V 175    18010  41079  58478  -4366   -418   2612       C  
ATOM   5535  O   TYR V 175     -39.390  30.987 -64.490  1.00309.59           O  
ANISOU 5535  O   TYR V 175    18122  41178  58331  -4478   -886   2733       O  
ATOM   5536  CB  TYR V 175     -39.580  33.506 -63.047  1.00314.49           C  
ANISOU 5536  CB  TYR V 175    17567  43176  58749  -4185    630   1026       C  
ATOM   5537  CG  TYR V 175     -38.881  34.811 -62.733  1.00315.07           C  
ANISOU 5537  CG  TYR V 175    17363  43351  58998  -3934   1438   -236       C  
ATOM   5538  CD1 TYR V 175     -38.304  35.574 -63.739  1.00311.41           C  
ANISOU 5538  CD1 TYR V 175    17350  41803  59168  -3673   1941   -944       C  
ATOM   5539  CD2 TYR V 175     -38.794  35.276 -61.427  1.00319.52           C  
ANISOU 5539  CD2 TYR V 175    17232  45082  59089  -3958   1696   -718       C  
ATOM   5540  CE1 TYR V 175     -37.662  36.766 -63.454  1.00312.15           C  
ANISOU 5540  CE1 TYR V 175    17186  41968  59450  -3461   2677  -2095       C  
ATOM   5541  CE2 TYR V 175     -38.154  36.465 -61.131  1.00320.30           C  
ANISOU 5541  CE2 TYR V 175    17085  45260  59355  -3739   2405  -1881       C  
ATOM   5542  CZ  TYR V 175     -37.590  37.206 -62.148  1.00316.60           C  
ANISOU 5542  CZ  TYR V 175    17050  43696  59548  -3501   2892  -2564       C  
ATOM   5543  OH  TYR V 175     -36.953  38.391 -61.859  1.00317.58           O  
ANISOU 5543  OH  TYR V 175    16925  43876  59865  -3300   3597  -3719       O  
ATOM   5544  N   ARG V 176     -41.403  31.532 -65.336  1.00308.98           N  
ANISOU 5544  N   ARG V 176    18136  40788  58474  -4467   -696   3456       N  
ATOM   5545  CA  ARG V 176     -41.778  30.152 -65.612  1.00308.70           C  
ANISOU 5545  CA  ARG V 176    18427  40564  58301  -4734  -1580   4583       C  
ATOM   5546  C   ARG V 176     -42.215  29.999 -67.064  1.00304.83           C  
ANISOU 5546  C   ARG V 176    18698  38812  58313  -4641  -1766   5001       C  
ATOM   5547  O   ARG V 176     -42.061  28.927 -67.658  1.00303.09           O  
ANISOU 5547  O   ARG V 176    19028  37971  58162  -4760  -2443   5668       O  
ATOM   5548  CB  ARG V 176     -42.898  29.703 -64.668  1.00313.13           C  
ANISOU 5548  CB  ARG V 176    18383  42255  58337  -5027  -1893   5391       C  
ATOM   5549  CG  ARG V 176     -43.279  28.236 -64.798  1.00313.55           C  
ANISOU 5549  CG  ARG V 176    18697  42233  58204  -5344  -2827   6573       C  
ATOM   5550  CD  ARG V 176     -44.408  27.865 -63.847  1.00318.30           C  
ANISOU 5550  CD  ARG V 176    18660  43963  58316  -5633  -3060   7353       C  
ATOM   5551  NE  ARG V 176     -44.008  27.928 -62.444  1.00322.31           N  
ANISOU 5551  NE  ARG V 176    18515  45685  58265  -5702  -2902   7029       N  
ATOM   5552  CZ  ARG V 176     -44.854  27.817 -61.425  1.00327.06           C  
ANISOU 5552  CZ  ARG V 176    18471  47416  58380  -5897  -2920   7497       C  
ATOM   5553  NH1 ARG V 176     -46.148  27.639 -61.653  1.00328.39           N  
ANISOU 5553  NH1 ARG V 176    18522  47661  58590  -6054  -3085   8314       N  
ATOM   5554  NH2 ARG V 176     -44.410  27.886 -60.178  1.00330.71           N  
ANISOU 5554  NH2 ARG V 176    18409  48928  58318  -5926  -2774   7152       N  
ATOM   5555  N   ARG V 177     -42.755  31.073 -67.644  1.00303.63           N  
ANISOU 5555  N   ARG V 177    18604  38258  58502  -4414  -1173   4605       N  
ATOM   5556  CA  ARG V 177     -43.296  31.015 -68.996  1.00300.42           C  
ANISOU 5556  CA  ARG V 177    18901  36700  58545  -4306  -1330   5004       C  
ATOM   5557  C   ARG V 177     -42.222  31.077 -70.075  1.00296.05           C  
ANISOU 5557  C   ARG V 177    19149  34878  58460  -4048  -1209   4505       C  
ATOM   5558  O   ARG V 177     -42.475  30.633 -71.201  1.00293.38           O  
ANISOU 5558  O   ARG V 177    19534  33518  58419  -3997  -1568   4992       O  
ATOM   5559  CB  ARG V 177     -44.296  32.154 -69.212  1.00301.01           C  
ANISOU 5559  CB  ARG V 177    18746  36821  58803  -4138   -740   4773       C  
ATOM   5560  CG  ARG V 177     -45.564  32.041 -68.384  1.00305.22           C  
ANISOU 5560  CG  ARG V 177    18582  38432  58955  -4377   -897   5430       C  
ATOM   5561  CD  ARG V 177     -46.490  33.217 -68.648  1.00305.74           C  
ANISOU 5561  CD  ARG V 177    18443  38484  59242  -4169   -278   5143       C  
ATOM   5562  NE  ARG V 177     -47.707  33.152 -67.845  1.00310.07           N  
ANISOU 5562  NE  ARG V 177    18288  40077  59448  -4377   -373   5755       N  
ATOM   5563  CZ  ARG V 177     -48.650  34.089 -67.843  1.00311.60           C  
ANISOU 5563  CZ  ARG V 177    18144  40508  59741  -4237    122   5619       C  
ATOM   5564  NH1 ARG V 177     -48.517  35.167 -68.604  1.00309.07           N  
ANISOU 5564  NH1 ARG V 177    18144  39447  59842  -3889    737   4888       N  
ATOM   5565  NH2 ARG V 177     -49.726  33.949 -67.081  1.00315.83           N  
ANISOU 5565  NH2 ARG V 177    18023  42017  59962  -4435     19   6222       N  
ATOM   5566  N   LEU V 178     -41.040  31.619 -69.766  1.00295.97           N  
ANISOU 5566  N   LEU V 178    19031  34893  58529  -3880   -712   3549       N  
ATOM   5567  CA  LEU V 178     -39.989  31.716 -70.774  1.00292.12           C  
ANISOU 5567  CA  LEU V 178    19273  33205  58513  -3625   -530   3051       C  
ATOM   5568  C   LEU V 178     -39.526  30.345 -71.245  1.00290.53           C  
ANISOU 5568  C   LEU V 178    19663  32434  58292  -3754  -1337   3748       C  
ATOM   5569  O   LEU V 178     -39.059  30.208 -72.382  1.00289.29           O  
ANISOU 5569  O   LEU V 178    20298  31083  58537  -3555  -1360   3698       O  
ATOM   5570  CB  LEU V 178     -38.800  32.508 -70.231  1.00292.47           C  
ANISOU 5570  CB  LEU V 178    18991  33491  58645  -3459    123   1917       C  
ATOM   5571  CG  LEU V 178     -38.999  34.003 -69.991  1.00293.36           C  
ANISOU 5571  CG  LEU V 178    18688  33871  58905  -3252   1033   1024       C  
ATOM   5572  CD1 LEU V 178     -37.763  34.592 -69.336  1.00294.28           C  
ANISOU 5572  CD1 LEU V 178    18445  34303  59065  -3151   1534    -19       C  
ATOM   5573  CD2 LEU V 178     -39.305  34.714 -71.298  1.00290.14           C  
ANISOU 5573  CD2 LEU V 178    18922  32289  59028  -2963   1454    832       C  
ATOM   5574  N   ASP V 179     -39.643  29.326 -70.391  1.00292.61           N  
ANISOU 5574  N   ASP V 179    19578  33519  58083  -4070  -1988   4398       N  
ATOM   5575  CA  ASP V 179     -39.241  27.961 -70.728  1.00291.58           C  
ANISOU 5575  CA  ASP V 179    19965  32942  57878  -4216  -2801   5109       C  
ATOM   5576  C   ASP V 179     -37.772  27.904 -71.144  1.00289.14           C  
ANISOU 5576  C   ASP V 179    20094  31908  57858  -3998  -2633   4465       C  
ATOM   5577  O   ASP V 179     -37.410  27.252 -72.125  1.00286.44           O  
ANISOU 5577  O   ASP V 179    20537  30530  57766  -3910  -2988   4783       O  
ATOM   5578  CB  ASP V 179     -40.142  27.375 -71.819  1.00289.78           C  
ANISOU 5578  CB  ASP V 179    20414  31856  57834  -4259  -3324   5996       C  
ATOM   5579  CG  ASP V 179     -41.557  27.128 -71.334  1.00292.74           C  
ANISOU 5579  CG  ASP V 179    20329  32997  57900  -4545  -3674   6812       C  
ATOM   5580  OD1 ASP V 179     -41.735  26.864 -70.126  1.00296.27           O  
ANISOU 5580  OD1 ASP V 179    20058  34625  57885  -4791  -3812   7000       O  
ATOM   5581  OD2 ASP V 179     -42.491  27.198 -72.160  1.00291.74           O  
ANISOU 5581  OD2 ASP V 179    20560  32290  57999  -4516  -3809   7270       O  
ATOM   5582  N   ILE V 180     -36.920  28.602 -70.393  1.00290.34           N  
ANISOU 5582  N   ILE V 180    19733  32599  57985  -3901  -2084   3547       N  
ATOM   5583  CA  ILE V 180     -35.495  28.666 -70.697  1.00288.54           C  
ANISOU 5583  CA  ILE V 180    19801  31762  58069  -3691  -1844   2845       C  
ATOM   5584  C   ILE V 180     -34.877  27.291 -70.485  1.00288.94           C  
ANISOU 5584  C   ILE V 180    20053  31850  57882  -3860  -2632   3418       C  
ATOM   5585  O   ILE V 180     -34.425  26.646 -71.437  1.00286.29           O  
ANISOU 5585  O   ILE V 180    20475  30493  57811  -3755  -2939   3696       O  
ATOM   5586  CB  ILE V 180     -34.795  29.725 -69.825  1.00290.40           C  
ANISOU 5586  CB  ILE V 180    19350  32678  58312  -3587  -1125   1750       C  
ATOM   5587  CG1 ILE V 180     -35.375  31.114 -70.098  1.00289.94           C  
ANISOU 5587  CG1 ILE V 180    19148  32499  58516  -3396   -318   1155       C  
ATOM   5588  CG2 ILE V 180     -33.297  29.717 -70.069  1.00289.04           C  
ANISOU 5588  CG2 ILE V 180    19414  31932  58476  -3400   -927   1061       C  
ATOM   5589  CD1 ILE V 180     -34.945  32.159 -69.089  1.00292.54           C  
ANISOU 5589  CD1 ILE V 180    18717  33677  58759  -3344    335    174       C  
ATOM   5590  N   VAL V 181     -34.876  26.829 -69.236  1.00292.44           N  
ANISOU 5590  N   VAL V 181    19842  33466  57807  -4110  -2967   3614       N  
ATOM   5591  CA  VAL V 181     -34.445  25.484 -68.866  1.00293.52           C  
ANISOU 5591  CA  VAL V 181    20082  33819  57623  -4308  -3768   4250       C  
ATOM   5592  C   VAL V 181     -35.356  25.009 -67.744  1.00297.42           C  
ANISOU 5592  C   VAL V 181    19953  35554  57497  -4645  -4197   4918       C  
ATOM   5593  O   VAL V 181     -35.625  25.758 -66.799  1.00300.17           O  
ANISOU 5593  O   VAL V 181    19580  36876  57596  -4685  -3782   4489       O  
ATOM   5594  CB  VAL V 181     -32.968  25.430 -68.419  1.00294.03           C  
ANISOU 5594  CB  VAL V 181    19993  33981  57745  -4192  -3652   3535       C  
ATOM   5595  CG1 VAL V 181     -32.627  24.053 -67.865  1.00295.81           C  
ANISOU 5595  CG1 VAL V 181    20228  34609  57557  -4411  -4497   4222       C  
ATOM   5596  CG2 VAL V 181     -32.036  25.767 -69.567  1.00290.39           C  
ANISOU 5596  CG2 VAL V 181    20182  32239  57913  -3866  -3263   2967       C  
ATOM   5597  N   ARG V 182     -35.834  23.769 -67.845  1.00297.86           N  
ANISOU 5597  N   ARG V 182    20300  35568  57305  -4885  -5017   5971       N  
ATOM   5598  CA  ARG V 182     -36.810  23.289 -66.877  1.00301.64           C  
ANISOU 5598  CA  ARG V 182    20234  37146  57230  -5217  -5420   6704       C  
ATOM   5599  C   ARG V 182     -36.185  22.983 -65.522  1.00305.32           C  
ANISOU 5599  C   ARG V 182    20080  38734  57195  -5342  -5559   6509       C  
ATOM   5600  O   ARG V 182     -36.909  22.904 -64.524  1.00309.05           O  
ANISOU 5600  O   ARG V 182    19954  40291  57182  -5565  -5663   6863       O  
ATOM   5601  CB  ARG V 182     -37.528  22.058 -67.418  1.00301.22           C  
ANISOU 5601  CB  ARG V 182    20688  36670  57093  -5451  -6261   7901       C  
ATOM   5602  CG  ARG V 182     -38.507  22.372 -68.532  1.00298.84           C  
ANISOU 5602  CG  ARG V 182    20843  35540  57163  -5393  -6193   8242       C  
ATOM   5603  CD  ARG V 182     -37.843  22.299 -69.884  1.00294.48           C  
ANISOU 5603  CD  ARG V 182    21200  33559  57129  -5121  -6183   8037       C  
ATOM   5604  NE  ARG V 182     -38.808  22.394 -70.973  1.00292.49           N  
ANISOU 5604  NE  ARG V 182    21475  32476  57180  -5084  -6280   8504       N  
ATOM   5605  CZ  ARG V 182     -39.119  23.528 -71.590  1.00290.68           C  
ANISOU 5605  CZ  ARG V 182    21334  31790  57320  -4839  -5619   7959       C  
ATOM   5606  NH1 ARG V 182     -38.535  24.659 -71.223  1.00290.57           N  
ANISOU 5606  NH1 ARG V 182    20917  32061  57426  -4622  -4803   6927       N  
ATOM   5607  NH2 ARG V 182     -40.009  23.531 -72.573  1.00289.14           N  
ANISOU 5607  NH2 ARG V 182    21643  30841  57377  -4808  -5788   8439       N  
ATOM   5608  N   SER V 183     -34.867  22.806 -65.462  1.00304.60           N  
ANISOU 5608  N   SER V 183    20119  38408  57208  -5195  -5563   5964       N  
ATOM   5609  CA  SER V 183     -34.153  22.692 -64.199  1.00308.12           C  
ANISOU 5609  CA  SER V 183    19969  39873  57228  -5255  -5614   5597       C  
ATOM   5610  C   SER V 183     -33.527  24.015 -63.776  1.00308.68           C  
ANISOU 5610  C   SER V 183    19563  40255  57466  -5025  -4787   4371       C  
ATOM   5611  O   SER V 183     -32.648  24.031 -62.907  1.00311.06           O  
ANISOU 5611  O   SER V 183    19467  41169  57551  -4998  -4771   3852       O  
ATOM   5612  CB  SER V 183     -33.084  21.602 -64.291  1.00307.62           C  
ANISOU 5612  CB  SER V 183    20289  39445  57148  -5250  -6205   5794       C  
ATOM   5613  OG  SER V 183     -32.070  21.958 -65.213  1.00304.13           O  
ANISOU 5613  OG  SER V 183    20319  37945  57291  -4951  -5873   5121       O  
ATOM   5614  N   LEU V 184     -33.964  25.124 -64.373  1.00306.73           N  
ANISOU 5614  N   LEU V 184    19355  39586  57603  -4857  -4116   3897       N  
ATOM   5615  CA  LEU V 184     -33.383  26.429 -64.083  1.00307.10           C  
ANISOU 5615  CA  LEU V 184    19007  39806  57870  -4631  -3303   2716       C  
ATOM   5616  C   LEU V 184     -34.448  27.460 -63.731  1.00308.62           C  
ANISOU 5616  C   LEU V 184    18735  40583  57945  -4639  -2756   2532       C  
ATOM   5617  O   LEU V 184     -34.173  28.397 -62.975  1.00310.84           O  
ANISOU 5617  O   LEU V 184    18461  41513  58133  -4547  -2213   1702       O  
ATOM   5618  CB  LEU V 184     -32.548  26.915 -65.269  1.00302.94           C  
ANISOU 5618  CB  LEU V 184    19053  38000  58051  -4336  -2884   2084       C  
ATOM   5619  CG  LEU V 184     -31.840  28.263 -65.131  1.00303.01           C  
ANISOU 5619  CG  LEU V 184    18737  37992  58401  -4093  -2024    831       C  
ATOM   5620  CD1 LEU V 184     -30.848  28.235 -63.982  1.00306.39           C  
ANISOU 5620  CD1 LEU V 184    18597  39259  58558  -4120  -2073    248       C  
ATOM   5621  CD2 LEU V 184     -31.145  28.625 -66.432  1.00298.84           C  
ANISOU 5621  CD2 LEU V 184    18864  36096  58585  -3818  -1644    380       C  
ATOM   5622  N   TYR V 185     -35.665  27.311 -64.266  1.00300.69           N  
ANISOU 5622  N   TYR V 185    40475  52596  21177  25126  -2806  -3642       N  
ATOM   5623  CA  TYR V 185     -36.707  28.269 -63.913  1.00299.97           C  
ANISOU 5623  CA  TYR V 185    40298  52570  21106  25054  -2760  -3576       C  
ATOM   5624  C   TYR V 185     -37.127  28.121 -62.458  1.00294.45           C  
ANISOU 5624  C   TYR V 185    39332  51587  20959  24420  -2939  -3916       C  
ATOM   5625  O   TYR V 185     -37.754  29.032 -61.908  1.00292.97           O  
ANISOU 5625  O   TYR V 185    39012  51334  20968  24235  -2800  -3811       O  
ATOM   5626  CB  TYR V 185     -37.927  28.136 -64.833  1.00304.20           C  
ANISOU 5626  CB  TYR V 185    40831  53379  21369  25360  -3058  -3841       C  
ATOM   5627  CG  TYR V 185     -38.814  26.932 -64.592  1.00303.48           C  
ANISOU 5627  CG  TYR V 185    40498  53271  21540  25115  -3665  -4591       C  
ATOM   5628  CD1 TYR V 185     -38.584  25.730 -65.241  1.00306.02           C  
ANISOU 5628  CD1 TYR V 185    40807  53626  21842  25291  -3987  -4950       C  
ATOM   5629  CD2 TYR V 185     -39.907  27.013 -63.736  1.00300.94           C  
ANISOU 5629  CD2 TYR V 185    39942  52919  21482  24781  -3906  -4944       C  
ATOM   5630  CE1 TYR V 185     -39.404  24.635 -65.030  1.00306.24           C  
ANISOU 5630  CE1 TYR V 185    40586  53642  22128  25174  -4523  -5659       C  
ATOM   5631  CE2 TYR V 185     -40.730  25.925 -63.518  1.00301.20           C  
ANISOU 5631  CE2 TYR V 185    39735  52959  21750  24657  -4425  -5617       C  
ATOM   5632  CZ  TYR V 185     -40.473  24.738 -64.168  1.00303.99           C  
ANISOU 5632  CZ  TYR V 185    40071  53333  22098  24873  -4729  -5984       C  
ATOM   5633  OH  TYR V 185     -41.288  23.650 -63.957  1.00305.05           O  
ANISOU 5633  OH  TYR V 185    39961  53490  22453  24827  -5231  -6714       O  
ATOM   5634  N   GLU V 186     -36.797  26.991 -61.829  1.00310.01           N  
ANISOU 5634  N   GLU V 186    41237  53379  23175  24131  -3232  -4292       N  
ATOM   5635  CA  GLU V 186     -36.915  26.865 -60.384  1.00304.59           C  
ANISOU 5635  CA  GLU V 186    40357  52367  23004  23585  -3284  -4495       C  
ATOM   5636  C   GLU V 186     -35.834  27.647 -59.651  1.00301.11           C  
ANISOU 5636  C   GLU V 186    39810  51553  23045  23261  -2813  -4170       C  
ATOM   5637  O   GLU V 186     -35.953  27.849 -58.438  1.00297.01           O  
ANISOU 5637  O   GLU V 186    39115  50798  22936  22867  -2827  -4270       O  
ATOM   5638  CB  GLU V 186     -36.859  25.391 -59.979  1.00303.85           C  
ANISOU 5638  CB  GLU V 186    40280  52160  23008  23463  -3682  -4947       C  
ATOM   5639  CG  GLU V 186     -38.030  24.564 -60.487  1.00305.96           C  
ANISOU 5639  CG  GLU V 186    40492  52678  23082  23699  -4176  -5407       C  
ATOM   5640  CD  GLU V 186     -39.348  24.970 -59.857  1.00303.96           C  
ANISOU 5640  CD  GLU V 186    40032  52487  22971  23525  -4294  -5607       C  
ATOM   5641  OE1 GLU V 186     -39.341  25.393 -58.682  1.00300.37           O  
ANISOU 5641  OE1 GLU V 186    39492  51781  22854  23135  -4091  -5497       O  
ATOM   5642  OE2 GLU V 186     -40.391  24.868 -60.537  1.00306.48           O  
ANISOU 5642  OE2 GLU V 186    40227  53047  23173  23731  -4547  -5914       O  
ATOM   5643  N   ASP V 187     -34.789  28.085 -60.355  1.00299.81           N  
ANISOU 5643  N   ASP V 187    39710  51323  22881  23444  -2399  -3815       N  
ATOM   5644  CA  ASP V 187     -33.765  28.955 -59.794  1.00298.88           C  
ANISOU 5644  CA  ASP V 187    39385  50821  23354  23172  -1911  -3557       C  
ATOM   5645  C   ASP V 187     -33.958  30.417 -60.175  1.00301.13           C  
ANISOU 5645  C   ASP V 187    39574  51044  23798  23303  -1416  -3095       C  
ATOM   5646  O   ASP V 187     -33.308  31.285 -59.584  1.00300.60           O  
ANISOU 5646  O   ASP V 187    39231  50601  24384  23036  -1023  -2943       O  
ATOM   5647  CB  ASP V 187     -32.371  28.495 -60.238  1.00300.60           C  
ANISOU 5647  CB  ASP V 187    39652  50907  23654  23250  -1681  -3498       C  
ATOM   5648  CG  ASP V 187     -31.962  27.180 -59.605  1.00298.16           C  
ANISOU 5648  CG  ASP V 187    39400  50532  23356  23053  -2107  -3934       C  
ATOM   5649  OD1 ASP V 187     -32.416  26.895 -58.477  1.00294.83           O  
ANISOU 5649  OD1 ASP V 187    38899  49999  23122  22748  -2403  -4207       O  
ATOM   5650  OD2 ASP V 187     -31.184  26.432 -60.235  1.00300.00           O  
ANISOU 5650  OD2 ASP V 187    39773  50814  23397  23238  -2122  -3977       O  
ATOM   5651  N   LEU V 188     -34.828  30.708 -61.145  1.00297.04           N  
ANISOU 5651  N   LEU V 188    39263  50870  22728  23739  -1435  -2899       N  
ATOM   5652  CA  LEU V 188     -35.150  32.089 -61.484  1.00299.59           C  
ANISOU 5652  CA  LEU V 188    39551  51130  23151  23920   -975  -2432       C  
ATOM   5653  C   LEU V 188     -35.920  32.801 -60.381  1.00296.21           C  
ANISOU 5653  C   LEU V 188    38853  50544  23148  23530  -1086  -2550       C  
ATOM   5654  O   LEU V 188     -36.054  34.028 -60.438  1.00297.93           O  
ANISOU 5654  O   LEU V 188    38969  50586  23643  23587   -673  -2179       O  
ATOM   5655  CB  LEU V 188     -35.956  32.140 -62.785  1.00304.27           C  
ANISOU 5655  CB  LEU V 188    40488  52200  22922  24568  -1055  -2242       C  
ATOM   5656  CG  LEU V 188     -35.228  31.771 -64.078  1.00309.32           C  
ANISOU 5656  CG  LEU V 188    41432  53027  23070  25114   -824  -1960       C  
ATOM   5657  CD1 LEU V 188     -36.204  31.706 -65.241  1.00314.09           C  
ANISOU 5657  CD1 LEU V 188    42374  54196  22769  25802  -1100  -1913       C  
ATOM   5658  CD2 LEU V 188     -34.131  32.779 -64.365  1.00312.53           C  
ANISOU 5658  CD2 LEU V 188    41786  53021  23941  25189     55  -1343       C  
ATOM   5659  N   GLU V 189     -36.423  32.071 -59.386  1.00309.57           N  
ANISOU 5659  N   GLU V 189    40435  52274  24912  23168  -1595  -3030       N  
ATOM   5660  CA  GLU V 189     -37.224  32.639 -58.309  1.00306.55           C  
ANISOU 5660  CA  GLU V 189    39815  51797  24864  22823  -1742  -3170       C  
ATOM   5661  C   GLU V 189     -36.553  32.451 -56.951  1.00302.82           C  
ANISOU 5661  C   GLU V 189    39094  50980  24983  22331  -1804  -3411       C  
ATOM   5662  O   GLU V 189     -37.228  32.402 -55.921  1.00299.95           O  
ANISOU 5662  O   GLU V 189    38599  50612  24757  22054  -2081  -3658       O  
ATOM   5663  CB  GLU V 189     -38.623  32.023 -58.304  1.00305.88           C  
ANISOU 5663  CB  GLU V 189    39813  52094  24315  22900  -2257  -3525       C  
ATOM   5664  CG  GLU V 189     -39.453  32.355 -59.536  1.00310.06           C  
ANISOU 5664  CG  GLU V 189    40545  53016  24247  23413  -2281  -3392       C  
ATOM   5665  CD  GLU V 189     -40.819  31.695 -59.518  1.00310.07           C  
ANISOU 5665  CD  GLU V 189    40530  53380  23902  23467  -2816  -3897       C  
ATOM   5666  OE1 GLU V 189     -41.075  30.880 -58.607  1.00307.05           O  
ANISOU 5666  OE1 GLU V 189    39999  52909  23758  23124  -3112  -4291       O  
ATOM   5667  OE2 GLU V 189     -41.636  31.990 -60.416  1.00313.72           O  
ANISOU 5667  OE2 GLU V 189    41119  54205  23877  23883  -2914  -3921       O  
ATOM   5668  N   ASP V 190     -35.220  32.350 -56.933  1.00310.67           N  
ANISOU 5668  N   ASP V 190    40020  51703  26318  22255  -1545  -3360       N  
ATOM   5669  CA  ASP V 190     -34.486  32.082 -55.702  1.00308.33           C  
ANISOU 5669  CA  ASP V 190    39514  51129  26508  21869  -1664  -3659       C  
ATOM   5670  C   ASP V 190     -33.251  32.960 -55.524  1.00309.16           C  
ANISOU 5670  C   ASP V 190    39291  50821  27356  21725  -1206  -3553       C  
ATOM   5671  O   ASP V 190     -32.480  32.729 -54.585  1.00307.40           O  
ANISOU 5671  O   ASP V 190    38872  50386  27538  21460  -1325  -3866       O  
ATOM   5672  CB  ASP V 190     -34.061  30.609 -55.636  1.00308.48           C  
ANISOU 5672  CB  ASP V 190    39759  51246  26202  21893  -1993  -3951       C  
ATOM   5673  CG  ASP V 190     -35.225  29.669 -55.400  1.00308.01           C  
ANISOU 5673  CG  ASP V 190    39899  51452  25677  21930  -2452  -4196       C  
ATOM   5674  OD1 ASP V 190     -36.215  30.090 -54.764  1.00306.15           O  
ANISOU 5674  OD1 ASP V 190    39556  51269  25499  21797  -2571  -4249       O  
ATOM   5675  OD2 ASP V 190     -35.147  28.504 -55.841  1.00309.83           O  
ANISOU 5675  OD2 ASP V 190    40362  51810  25551  22093  -2676  -4360       O  
ATOM   5676  N   HIS V 191     -33.033  33.956 -56.388  1.00299.18           N  
ANISOU 5676  N   HIS V 191    37945  49417  26315  21925   -667  -3144       N  
ATOM   5677  CA  HIS V 191     -31.800  34.744 -56.390  1.00301.32           C  
ANISOU 5677  CA  HIS V 191    37853  49229  27407  21827   -115  -3054       C  
ATOM   5678  C   HIS V 191     -32.120  36.227 -56.226  1.00301.85           C  
ANISOU 5678  C   HIS V 191    37610  48994  28088  21769    282  -2816       C  
ATOM   5679  O   HIS V 191     -32.214  36.966 -57.218  1.00305.88           O  
ANISOU 5679  O   HIS V 191    38204  49425  28592  22089    818  -2320       O  
ATOM   5680  CB  HIS V 191     -31.000  34.498 -57.668  1.00306.26           C  
ANISOU 5680  CB  HIS V 191    38657  49856  27852  22172    339  -2740       C  
ATOM   5681  CG  HIS V 191     -30.475  33.101 -57.793  1.00306.30           C  
ANISOU 5681  CG  HIS V 191    38896  50079  27407  22206    -17  -3016       C  
ATOM   5682  ND1 HIS V 191     -31.207  32.079 -58.358  1.00306.24           N  
ANISOU 5682  ND1 HIS V 191    39327  50522  26511  22462   -438  -3036       N  
ATOM   5683  CD2 HIS V 191     -29.291  32.557 -57.425  1.00306.35           C  
ANISOU 5683  CD2 HIS V 191    38734  49897  27768  22033    -29  -3325       C  
ATOM   5684  CE1 HIS V 191     -30.498  30.965 -58.333  1.00306.25           C  
ANISOU 5684  CE1 HIS V 191    39438  50576  26348  22440   -675  -3309       C  
ATOM   5685  NE2 HIS V 191     -29.331  31.228 -57.772  1.00306.26           N  
ANISOU 5685  NE2 HIS V 191    39099  50213  27054  22189   -439  -3471       N  
ATOM   5686  N   PRO V 192     -32.296  36.699 -54.986  1.00301.73           N  
ANISOU 5686  N   PRO V 192    37253  48798  28594  21408     43  -3147       N  
ATOM   5687  CA  PRO V 192     -32.407  38.147 -54.757  1.00303.62           C  
ANISOU 5687  CA  PRO V 192    37107  48653  29602  21322    440  -2998       C  
ATOM   5688  C   PRO V 192     -31.054  38.840 -54.824  1.00307.98           C  
ANISOU 5688  C   PRO V 192    37177  48633  31210  21232   1053  -3040       C  
ATOM   5689  O   PRO V 192     -30.041  38.209 -55.145  1.00309.32           O  
ANISOU 5689  O   PRO V 192    37336  48742  31451  21259   1193  -3146       O  
ATOM   5690  CB  PRO V 192     -33.006  38.237 -53.346  1.00299.71           C  
ANISOU 5690  CB  PRO V 192    36419  48214  29244  20977   -111  -3433       C  
ATOM   5691  CG  PRO V 192     -33.624  36.895 -53.099  1.00295.73           C  
ANISOU 5691  CG  PRO V 192    36332  48196  27835  20992   -715  -3620       C  
ATOM   5692  CD  PRO V 192     -32.728  35.928 -53.809  1.00297.23           C  
ANISOU 5692  CD  PRO V 192    36730  48443  27761  21148   -628  -3606       C  
ATOM   5693  N   ASN V 193     -31.024  40.134 -54.522  1.00298.40           N  
ANISOU 5693  N   ASN V 193    35522  46970  30887  21124   1437  -3000       N  
ATOM   5694  CA  ASN V 193     -29.772  40.884 -54.490  1.00303.39           C  
ANISOU 5694  CA  ASN V 193    35564  46966  32746  21003   2062  -3143       C  
ATOM   5695  C   ASN V 193     -29.057  40.666 -53.160  1.00301.72           C  
ANISOU 5695  C   ASN V 193    34872  46599  33169  20593   1604  -3925       C  
ATOM   5696  O   ASN V 193     -28.162  39.829 -53.055  1.00301.52           O  
ANISOU 5696  O   ASN V 193    34819  46623  33120  20527   1457  -4243       O  
ATOM   5697  CB  ASN V 193     -30.029  42.377 -54.718  1.00307.88           C  
ANISOU 5697  CB  ASN V 193    35820  47044  34117  21081   2702  -2812       C  
ATOM   5698  CG  ASN V 193     -28.748  43.167 -54.933  1.00314.61           C  
ANISOU 5698  CG  ASN V 193    36050  47161  36325  21025   3541  -2886       C  
ATOM   5699  OD1 ASN V 193     -27.648  42.614 -54.906  1.00315.86           O  
ANISOU 5699  OD1 ASN V 193    35982  47200  36833  20914   3623  -3221       O  
ATOM   5700  ND2 ASN V 193     -28.888  44.470 -55.149  1.00319.47           N  
ANISOU 5700  ND2 ASN V 193    36364  47252  37768  21108   4196  -2595       N  
TER    5701      ASN V 193                                                      
ATOM   5702  N   ALA R  17      85.918  35.890   8.594  1.00212.01           N  
ANISOU 5702  N   ALA R  17    13874  30212  36467   5946  -1956   9386       N  
ATOM   5703  CA  ALA R  17      84.760  36.656   9.016  1.00206.02           C  
ANISOU 5703  CA  ALA R  17    13511  29117  35651   5212  -2094   9137       C  
ATOM   5704  C   ALA R  17      84.882  37.199  10.427  1.00207.12           C  
ANISOU 5704  C   ALA R  17    13284  29280  36131   4685  -2816   8691       C  
ATOM   5705  O   ALA R  17      85.852  36.914  11.129  1.00212.44           O  
ANISOU 5705  O   ALA R  17    13447  30226  37045   4903  -3267   8555       O  
ATOM   5706  N   LYS R  18      83.892  37.984  10.842  1.00203.69           N  
ANISOU 5706  N   LYS R  18    13116  28578  35700   4029  -2946   8438       N  
ATOM   5707  CA  LYS R  18      83.867  38.587  12.165  1.00204.51           C  
ANISOU 5707  CA  LYS R  18    12943  28693  36070   3526  -3630   7967       C  
ATOM   5708  C   LYS R  18      82.832  37.899  13.046  1.00199.37           C  
ANISOU 5708  C   LYS R  18    13329  27933  34490   3462  -4112   7650       C  
ATOM   5709  O   LYS R  18      81.798  37.424  12.567  1.00193.71           O  
ANISOU 5709  O   LYS R  18    13491  26995  33114   3501  -3841   7753       O  
ATOM   5710  CB  LYS R  18      83.563  40.087  12.084  1.00204.00           C  
ANISOU 5710  CB  LYS R  18    12329  28418  36764   2823  -3468   7873       C  
ATOM   5711  CG  LYS R  18      84.677  40.912  11.464  1.00210.52           C  
ANISOU 5711  CG  LYS R  18    12116  29307  38565   2736  -3061   8094       C  
ATOM   5712  CD  LYS R  18      84.323  42.389  11.446  1.00210.27           C  
ANISOU 5712  CD  LYS R  18    11809  28948  39136   1989  -2920   7904       C  
ATOM   5713  CE  LYS R  18      85.496  43.232  10.968  1.00217.90           C  
ANISOU 5713  CE  LYS R  18    12010  29884  40897   1807  -2537   7988       C  
ATOM   5714  NZ  LYS R  18      85.830  42.974   9.541  1.00219.26           N  
ANISOU 5714  NZ  LYS R  18    12122  30111  41076   2196  -1685   8615       N  
ATOM   5715  N   LYS R  19      83.125  37.852  14.347  1.00208.43           N  
ANISOU 5715  N   LYS R  19    14349  29245  35600   3373  -4835   7266       N  
ATOM   5716  CA  LYS R  19      82.215  37.228  15.302  1.00204.68           C  
ANISOU 5716  CA  LYS R  19    14799  28714  34254   3312  -5299   6994       C  
ATOM   5717  C   LYS R  19      81.095  38.178  15.713  1.00200.13           C  
ANISOU 5717  C   LYS R  19    14442  27936  33663   2639  -5360   6689       C  
ATOM   5718  O   LYS R  19      79.911  37.883  15.513  1.00194.30           O  
ANISOU 5718  O   LYS R  19    14536  26983  32304   2504  -5157   6719       O  
ATOM   5719  CB  LYS R  19      82.990  36.748  16.532  1.00209.84           C  
ANISOU 5719  CB  LYS R  19    15283  29666  34781   3578  -6048   6727       C  
ATOM   5720  CG  LYS R  19      83.866  35.530  16.288  1.00213.61           C  
ANISOU 5720  CG  LYS R  19    15839  30322  35000   4320  -6085   6989       C  
ATOM   5721  CD  LYS R  19      84.548  35.082  17.571  1.00218.75           C  
ANISOU 5721  CD  LYS R  19    16387  31257  35469   4588  -6876   6700       C  
ATOM   5722  CE  LYS R  19      85.411  33.854  17.339  1.00222.75           C  
ANISOU 5722  CE  LYS R  19    16998  31926  35710   5365  -6945   6949       C  
ATOM   5723  NZ  LYS R  19      84.578  32.657  17.032  1.00218.33           N  
ANISOU 5723  NZ  LYS R  19    17608  31126  34223   5662  -6770   7196       N  
ATOM   5724  N   LYS R  20      81.448  39.324  16.292  1.00208.08           N  
ANISOU 5724  N   LYS R  20    14689  29000  35372   2222  -5662   6368       N  
ATOM   5725  CA  LYS R  20      80.470  40.271  16.824  1.00204.81           C  
ANISOU 5725  CA  LYS R  20    14426  28425  34969   1624  -5823   5998       C  
ATOM   5726  C   LYS R  20      80.525  41.571  16.020  1.00205.45           C  
ANISOU 5726  C   LYS R  20    13817  28280  35966   1201  -5397   6079       C  
ATOM   5727  O   LYS R  20      81.182  42.543  16.395  1.00210.47           O  
ANISOU 5727  O   LYS R  20    13595  28937  37437    921  -5670   5848       O  
ATOM   5728  CB  LYS R  20      80.715  40.499  18.353  1.00207.42           C  
ANISOU 5728  CB  LYS R  20    14575  28991  35245   1517  -6660   5465       C  
ATOM   5729  CG  LYS R  20      82.114  40.989  18.730  1.00214.94           C  
ANISOU 5729  CG  LYS R  20    14450  30148  37068   1600  -7063   5298       C  
ATOM   5730  CD  LYS R  20      82.232  41.250  20.224  1.00218.46           C  
ANISOU 5730  CD  LYS R  20    14798  30816  37389   1521  -7922   4713       C  
ATOM   5731  CE  LYS R  20      82.284  39.955  21.015  1.00219.28           C  
ANISOU 5731  CE  LYS R  20    15592  31191  36535   2037  -8328   4710       C  
ATOM   5732  NZ  LYS R  20      82.535  40.202  22.462  1.00223.86           N  
ANISOU 5732  NZ  LYS R  20    16030  32044  36981   2056  -9184   4153       N  
ATOM   5733  N   ARG R  21      79.819  41.580  14.890  1.00202.64           N  
ANISOU 5733  N   ARG R  21    13855  27680  35457   1166  -4733   6415       N  
ATOM   5734  CA  ARG R  21      79.577  42.806  14.138  1.00202.00           C  
ANISOU 5734  CA  ARG R  21    13342  27329  36080    741  -4304   6507       C  
ATOM   5735  C   ARG R  21      78.091  43.126  14.055  1.00196.63           C  
ANISOU 5735  C   ARG R  21    13400  26393  34916    394  -4164   6344       C  
ATOM   5736  O   ARG R  21      77.664  44.180  14.539  1.00197.73           O  
ANISOU 5736  O   ARG R  21    13323  26396  35409    -93  -4392   5990       O  
ATOM   5737  CB  ARG R  21      80.175  42.676  12.734  1.00203.33           C  
ANISOU 5737  CB  ARG R  21    13199  27462  36597   1059  -3579   7094       C  
ATOM   5738  CG  ARG R  21      80.119  43.938  11.892  1.00203.31           C  
ANISOU 5738  CG  ARG R  21    12665  27189  37395    676  -3086   7298       C  
ATOM   5739  CD  ARG R  21      80.568  43.614  10.483  1.00204.51           C  
ANISOU 5739  CD  ARG R  21    12704  27360  37640   1099  -2317   7921       C  
ATOM   5740  NE  ARG R  21      79.625  42.678   9.878  1.00199.82           N  
ANISOU 5740  NE  ARG R  21    13145  26708  36072   1443  -2026   8059       N  
ATOM   5741  CZ  ARG R  21      79.897  41.405   9.609  1.00199.70           C  
ANISOU 5741  CZ  ARG R  21    13545  26882  35449   2049  -1960   8246       C  
ATOM   5742  NH1 ARG R  21      81.094  40.906   9.887  1.00204.11           N  
ANISOU 5742  NH1 ARG R  21    13576  27737  36240   2406  -2143   8330       N  
ATOM   5743  NH2 ARG R  21      78.966  40.630   9.071  1.00196.94           N  
ANISOU 5743  NH2 ARG R  21    14133  26411  34285   2308  -1746   8322       N  
ATOM   5744  N   PHE R  22      77.294  42.225  13.480  1.00194.16           N  
ANISOU 5744  N   PHE R  22    13946  26010  33815    650  -3834   6560       N  
ATOM   5745  CA  PHE R  22      75.833  42.316  13.405  1.00190.17           C  
ANISOU 5745  CA  PHE R  22    14205  25294  32758    383  -3716   6404       C  
ATOM   5746  C   PHE R  22      75.358  43.709  12.972  1.00187.60           C  
ANISOU 5746  C   PHE R  22    13545  24701  33032    -94  -3475   6317       C  
ATOM   5747  O   PHE R  22      74.708  44.443  13.716  1.00186.47           O  
ANISOU 5747  O   PHE R  22    13429  24492  32927   -519  -3803   5890       O  
ATOM   5748  CB  PHE R  22      75.198  41.897  14.734  1.00189.76           C  
ANISOU 5748  CB  PHE R  22    14665  25384  32051    251  -4298   5979       C  
ATOM   5749  CG  PHE R  22      75.251  40.414  14.989  1.00191.28           C  
ANISOU 5749  CG  PHE R  22    15484  25724  31471    704  -4428   6133       C  
ATOM   5750  CD1 PHE R  22      75.578  39.535  13.968  1.00191.78           C  
ANISOU 5750  CD1 PHE R  22    15767  25730  31369   1176  -4022   6568       C  
ATOM   5751  CD2 PHE R  22      74.958  39.898  16.240  1.00191.59           C  
ANISOU 5751  CD2 PHE R  22    15919  25946  30931    683  -4956   5851       C  
ATOM   5752  CE1 PHE R  22      75.624  38.171  14.195  1.00192.08           C  
ANISOU 5752  CE1 PHE R  22    16401  25843  30736   1600  -4176   6698       C  
ATOM   5753  CE2 PHE R  22      75.001  38.534  16.471  1.00191.79           C  
ANISOU 5753  CE2 PHE R  22    16545  26053  30272   1091  -5074   6035       C  
ATOM   5754  CZ  PHE R  22      75.334  37.671  15.447  1.00192.28           C  
ANISOU 5754  CZ  PHE R  22    16817  26007  30232   1539  -4700   6450       C  
ATOM   5755  N   GLU R  23      75.703  44.052  11.733  1.00174.02           N  
ANISOU 5755  N   GLU R  23    11522  22832  31764     24  -2884   6747       N  
ATOM   5756  CA  GLU R  23      75.135  45.239  11.106  1.00172.52           C  
ANISOU 5756  CA  GLU R  23    11178  22335  32036   -351  -2554   6771       C  
ATOM   5757  C   GLU R  23      73.694  44.957  10.691  1.00165.87           C  
ANISOU 5757  C   GLU R  23    11242  21322  30457   -372  -2343   6704       C  
ATOM   5758  O   GLU R  23      73.394  43.898  10.132  1.00163.61           O  
ANISOU 5758  O   GLU R  23    11562  21075  29527     29  -2105   6925       O  
ATOM   5759  CB  GLU R  23      75.986  45.671   9.911  1.00176.35           C  
ANISOU 5759  CB  GLU R  23    11064  22738  33203   -182  -1953   7315       C  
ATOM   5760  CG  GLU R  23      76.095  44.649   8.784  1.00175.32           C  
ANISOU 5760  CG  GLU R  23    11350  22693  32569    420  -1410   7799       C  
ATOM   5761  CD  GLU R  23      77.044  45.093   7.683  1.00180.24           C  
ANISOU 5761  CD  GLU R  23    11306  23315  33862    623   -800   8359       C  
ATOM   5762  OE1 GLU R  23      77.636  46.185   7.811  1.00184.61           O  
ANISOU 5762  OE1 GLU R  23    11043  23768  35333    250   -798   8398       O  
ATOM   5763  OE2 GLU R  23      77.199  44.350   6.692  1.00180.20           O  
ANISOU 5763  OE2 GLU R  23    11585  23408  33476   1167   -321   8763       O  
ATOM   5764  N   VAL R  24      72.798  45.898  10.976  1.00157.81           N  
ANISOU 5764  N   VAL R  24    10303  20105  29553   -826  -2463   6368       N  
ATOM   5765  CA  VAL R  24      71.355  45.669  10.863  1.00151.81           C  
ANISOU 5765  CA  VAL R  24    10355  19226  28101   -911  -2399   6175       C  
ATOM   5766  C   VAL R  24      70.891  46.289   9.547  1.00150.11           C  
ANISOU 5766  C   VAL R  24    10218  18717  28100   -895  -1823   6462       C  
ATOM   5767  O   VAL R  24      70.579  47.478   9.462  1.00150.36           O  
ANISOU 5767  O   VAL R  24     9975  18524  28631  -1251  -1791   6332       O  
ATOM   5768  CB  VAL R  24      70.595  46.228  12.065  1.00150.38           C  
ANISOU 5768  CB  VAL R  24    10264  19072  27803  -1355  -2915   5588       C  
ATOM   5769  CG1 VAL R  24      69.097  46.040  11.879  1.00144.65           C  
ANISOU 5769  CG1 VAL R  24    10299  18234  26427  -1452  -2796   5408       C  
ATOM   5770  CG2 VAL R  24      71.067  45.556  13.346  1.00152.58           C  
ANISOU 5770  CG2 VAL R  24    10522  19675  27777  -1292  -3470   5341       C  
ATOM   5771  N   LYS R  25      70.848  45.465   8.508  1.00148.75           N  
ANISOU 5771  N   LYS R  25    10450  18539  27530   -438  -1386   6850       N  
ATOM   5772  CA  LYS R  25      70.320  45.837   7.203  1.00147.03           C  
ANISOU 5772  CA  LYS R  25    10463  18086  27316   -295   -840   7131       C  
ATOM   5773  C   LYS R  25      68.840  45.447   7.129  1.00141.23           C  
ANISOU 5773  C   LYS R  25    10559  17239  25862   -334   -894   6843       C  
ATOM   5774  O   LYS R  25      68.194  45.254   8.162  1.00138.92           O  
ANISOU 5774  O   LYS R  25    10521  17019  25245   -617  -1330   6412       O  
ATOM   5775  CB  LYS R  25      71.199  45.239   6.100  1.00149.89           C  
ANISOU 5775  CB  LYS R  25    10725  18539  27688    278   -343   7697       C  
ATOM   5776  CG  LYS R  25      72.561  45.922   6.026  1.00156.16           C  
ANISOU 5776  CG  LYS R  25    10580  19402  29351    235   -187   8015       C  
ATOM   5777  CD  LYS R  25      73.434  45.410   4.895  1.00159.63           C  
ANISOU 5777  CD  LYS R  25    10863  19978  29811    824    374   8602       C  
ATOM   5778  CE  LYS R  25      74.773  46.140   4.888  1.00166.45           C  
ANISOU 5778  CE  LYS R  25    10706  20918  31620    715    536   8920       C  
ATOM   5779  NZ  LYS R  25      75.679  45.678   3.800  1.00170.63           N  
ANISOU 5779  NZ  LYS R  25    11006  21640  32185   1309   1132   9518       N  
ATOM   5780  N   LYS R  26      68.298  45.338   5.910  1.00141.08           N  
ANISOU 5780  N   LYS R  26    10949  17060  25595    -36   -452   7077       N  
ATOM   5781  CA  LYS R  26      66.869  45.315   5.589  1.00136.29           C  
ANISOU 5781  CA  LYS R  26    10999  16279  24507   -102   -432   6820       C  
ATOM   5782  C   LYS R  26      65.976  44.664   6.640  1.00132.87           C  
ANISOU 5782  C   LYS R  26    11022  15931  23531   -348   -891   6357       C  
ATOM   5783  O   LYS R  26      66.249  43.552   7.102  1.00133.07           O  
ANISOU 5783  O   LYS R  26    11271  16118  23172   -171  -1084   6374       O  
ATOM   5784  CB  LYS R  26      66.648  44.568   4.270  1.00135.39           C  
ANISOU 5784  CB  LYS R  26    11393  16099  23951    475    -19   7133       C  
ATOM   5785  CG  LYS R  26      67.290  45.184   3.044  1.00138.65           C  
ANISOU 5785  CG  LYS R  26    11497  16437  24745    798    534   7629       C  
ATOM   5786  CD  LYS R  26      66.982  44.342   1.811  1.00137.85           C  
ANISOU 5786  CD  LYS R  26    11990  16314  24072   1440    873   7856       C  
ATOM   5787  CE  LYS R  26      67.651  44.893   0.564  1.00141.75           C  
ANISOU 5787  CE  LYS R  26    12210  16794  24854   1844   1477   8403       C  
ATOM   5788  NZ  LYS R  26      67.368  44.052  -0.633  1.00141.48           N  
ANISOU 5788  NZ  LYS R  26    12782  16776  24199   2552   1775   8584       N  
ATOM   5789  N   TRP R  27      64.906  45.357   7.016  1.00128.96           N  
ANISOU 5789  N   TRP R  27    10664  15328  23005   -743  -1051   5963       N  
ATOM   5790  CA  TRP R  27      63.909  44.877   7.961  1.00125.98           C  
ANISOU 5790  CA  TRP R  27    10700  15043  22122  -1007  -1413   5533       C  
ATOM   5791  C   TRP R  27      62.583  44.684   7.232  1.00122.17           C  
ANISOU 5791  C   TRP R  27    10807  14381  21230   -943  -1250   5399       C  
ATOM   5792  O   TRP R  27      62.428  45.072   6.072  1.00121.85           O  
ANISOU 5792  O   TRP R  27    10840  14149  21310   -710   -906   5588       O  
ATOM   5793  CB  TRP R  27      63.761  45.869   9.124  1.00126.65           C  
ANISOU 5793  CB  TRP R  27    10399  15213  22510  -1507  -1777   5119       C  
ATOM   5794  CG  TRP R  27      62.926  45.391  10.278  1.00124.79           C  
ANISOU 5794  CG  TRP R  27    10491  15167  21755  -1763  -2144   4713       C  
ATOM   5795  CD1 TRP R  27      63.203  44.345  11.105  1.00125.60           C  
ANISOU 5795  CD1 TRP R  27    10777  15499  21448  -1698  -2388   4728       C  
ATOM   5796  CD2 TRP R  27      61.694  45.958  10.747  1.00122.39           C  
ANISOU 5796  CD2 TRP R  27    10358  14862  21283  -2106  -2290   4258       C  
ATOM   5797  NE1 TRP R  27      62.218  44.215  12.054  1.00124.02           N  
ANISOU 5797  NE1 TRP R  27    10855  15445  20821  -1989  -2639   4351       N  
ATOM   5798  CE2 TRP R  27      61.280  45.194  11.856  1.00122.02           C  
ANISOU 5798  CE2 TRP R  27    10580  15074  20708  -2240  -2580   4044       C  
ATOM   5799  CE3 TRP R  27      60.899  47.031  10.335  1.00120.88           C  
ANISOU 5799  CE3 TRP R  27    10120  14483  21327  -2288  -2196   4022       C  
ATOM   5800  CZ2 TRP R  27      60.106  45.468  12.558  1.00120.31           C  
ANISOU 5800  CZ2 TRP R  27    10552  14971  20190  -2551  -2743   3609       C  
ATOM   5801  CZ3 TRP R  27      59.733  47.302  11.034  1.00118.98           C  
ANISOU 5801  CZ3 TRP R  27    10068  14342  20796  -2583  -2399   3548       C  
ATOM   5802  CH2 TRP R  27      59.351  46.526  12.134  1.00118.77           C  
ANISOU 5802  CH2 TRP R  27    10272  14612  20242  -2714  -2654   3348       C  
ATOM   5803  N   ASN R  28      61.622  44.069   7.921  1.00128.83           N  
ANISOU 5803  N   ASN R  28    12067  15298  21586  -1138  -1499   5080       N  
ATOM   5804  CA  ASN R  28      60.278  43.883   7.386  1.00127.48           C  
ANISOU 5804  CA  ASN R  28    12403  14973  21062  -1143  -1416   4873       C  
ATOM   5805  C   ASN R  28      59.291  43.822   8.542  1.00123.89           C  
ANISOU 5805  C   ASN R  28    12094  14662  20315  -1579  -1728   4436       C  
ATOM   5806  O   ASN R  28      59.673  43.620   9.698  1.00124.20           O  
ANISOU 5806  O   ASN R  28    11975  14932  20283  -1777  -1995   4353       O  
ATOM   5807  CB  ASN R  28      60.170  42.613   6.530  1.00129.58           C  
ANISOU 5807  CB  ASN R  28    13192  15125  20919   -698  -1265   5106       C  
ATOM   5808  CG  ASN R  28      60.816  42.766   5.165  1.00132.27           C  
ANISOU 5808  CG  ASN R  28    13486  15328  21444   -200   -889   5485       C  
ATOM   5809  OD1 ASN R  28      60.625  43.773   4.483  1.00133.40           O  
ANISOU 5809  OD1 ASN R  28    13475  15347  21864   -186   -671   5502       O  
ATOM   5810  ND2 ASN R  28      61.594  41.767   4.764  1.00134.27           N  
ANISOU 5810  ND2 ASN R  28    13879  15609  21527    241   -802   5806       N  
ATOM   5811  N   ALA R  29      58.010  43.993   8.217  1.00119.90           N  
ANISOU 5811  N   ALA R  29    11887  14046  19623  -1695  -1686   4157       N  
ATOM   5812  CA  ALA R  29      56.956  43.965   9.225  1.00117.55           C  
ANISOU 5812  CA  ALA R  29    11713  13909  19041  -2094  -1917   3746       C  
ATOM   5813  C   ALA R  29      55.608  43.805   8.535  1.00115.89           C  
ANISOU 5813  C   ALA R  29    11896  13534  18605  -2090  -1815   3532       C  
ATOM   5814  O   ALA R  29      55.482  43.979   7.320  1.00116.54           O  
ANISOU 5814  O   ALA R  29    12112  13378  18790  -1791  -1603   3639       O  
ATOM   5815  CB  ALA R  29      56.966  45.226  10.090  1.00116.73           C  
ANISOU 5815  CB  ALA R  29    11154  13961  19236  -2439  -2102   3421       C  
ATOM   5816  N   VAL R  30      54.598  43.479   9.341  1.00112.01           N  
ANISOU 5816  N   VAL R  30    11571  13190  17799  -2410  -1968   3227       N  
ATOM   5817  CA  VAL R  30      53.225  43.266   8.887  1.00110.11           C  
ANISOU 5817  CA  VAL R  30    11646  12833  17356  -2478  -1923   2963       C  
ATOM   5818  C   VAL R  30      52.288  43.762   9.983  1.00109.95           C  
ANISOU 5818  C   VAL R  30    11481  13082  17214  -2920  -2073   2535       C  
ATOM   5819  O   VAL R  30      52.571  43.593  11.173  1.00111.48           O  
ANISOU 5819  O   VAL R  30    11549  13558  17251  -3142  -2221   2519       O  
ATOM   5820  CB  VAL R  30      52.977  41.776   8.551  1.00110.17           C  
ANISOU 5820  CB  VAL R  30    12124  12695  17040  -2321  -1909   3157       C  
ATOM   5821  CG1 VAL R  30      51.507  41.503   8.331  1.00108.92           C  
ANISOU 5821  CG1 VAL R  30    12225  12450  16710  -2487  -1925   2835       C  
ATOM   5822  CG2 VAL R  30      53.763  41.358   7.313  1.00110.47           C  
ANISOU 5822  CG2 VAL R  30    12336  12474  17165  -1798  -1754   3507       C  
ATOM   5823  N   ALA R  31      51.172  44.382   9.588  1.00117.79           N  
ANISOU 5823  N   ALA R  31    12492  14013  18250  -3009  -2040   2177       N  
ATOM   5824  CA  ALA R  31      50.243  44.946  10.561  1.00115.24           C  
ANISOU 5824  CA  ALA R  31    11997  13972  17816  -3381  -2161   1735       C  
ATOM   5825  C   ALA R  31      48.830  45.018   9.990  1.00113.62           C  
ANISOU 5825  C   ALA R  31    11956  13674  17542  -3431  -2109   1399       C  
ATOM   5826  O   ALA R  31      48.636  45.190   8.783  1.00114.11           O  
ANISOU 5826  O   ALA R  31    12162  13440  17756  -3152  -2016   1415       O  
ATOM   5827  CB  ALA R  31      50.690  46.341  11.013  1.00113.71           C  
ANISOU 5827  CB  ALA R  31    11377  13889  17937  -3464  -2272   1522       C  
ATOM   5828  N   LEU R  32      47.849  44.896  10.884  1.00122.98           N  
ANISOU 5828  N   LEU R  32    13100  15142  18484  -3765  -2168   1093       N  
ATOM   5829  CA  LEU R  32      46.428  44.986  10.573  1.00120.02           C  
ANISOU 5829  CA  LEU R  32    12787  14764  18053  -3877  -2143    712       C  
ATOM   5830  C   LEU R  32      45.924  46.396  10.865  1.00117.25           C  
ANISOU 5830  C   LEU R  32    12114  14581  17856  -3968  -2223    244       C  
ATOM   5831  O   LEU R  32      46.459  47.084  11.737  1.00117.83           O  
ANISOU 5831  O   LEU R  32    11919  14881  17968  -4074  -2326    159       O  
ATOM   5832  CB  LEU R  32      45.630  43.988  11.416  1.00121.07           C  
ANISOU 5832  CB  LEU R  32    13022  15131  17849  -4207  -2121    684       C  
ATOM   5833  CG  LEU R  32      45.894  42.485  11.309  1.00124.75           C  
ANISOU 5833  CG  LEU R  32    13833  15420  18148  -4194  -2076   1104       C  
ATOM   5834  CD1 LEU R  32      45.118  41.745  12.386  1.00125.57           C  
ANISOU 5834  CD1 LEU R  32    13952  15808  17950  -4593  -2034   1088       C  
ATOM   5835  CD2 LEU R  32      45.514  41.961   9.948  1.00124.27           C  
ANISOU 5835  CD2 LEU R  32    14061  14931  18226  -3936  -2056   1127       C  
ATOM   5836  N   TRP R  33      44.879  46.821  10.152  1.00118.53           N  
ANISOU 5836  N   TRP R  33    12304  14623  18107  -3904  -2213    -95       N  
ATOM   5837  CA  TRP R  33      44.258  48.118  10.407  1.00117.54           C  
ANISOU 5837  CA  TRP R  33    11901  14642  18116  -3966  -2309   -584       C  
ATOM   5838  C   TRP R  33      42.789  47.944  10.767  1.00118.19           C  
ANISOU 5838  C   TRP R  33    11933  14979  17996  -4191  -2308  -1011       C  
ATOM   5839  O   TRP R  33      42.054  47.232  10.078  1.00117.73           O  
ANISOU 5839  O   TRP R  33    12072  14763  17895  -4152  -2252  -1026       O  
ATOM   5840  CB  TRP R  33      44.394  49.076   9.214  1.00116.36           C  
ANISOU 5840  CB  TRP R  33    11775  14121  18315  -3631  -2315   -631       C  
ATOM   5841  CG  TRP R  33      43.697  48.672   7.948  1.00117.08           C  
ANISOU 5841  CG  TRP R  33    12157  13924  18404  -3372  -2253   -652       C  
ATOM   5842  CD1 TRP R  33      44.239  48.000   6.895  1.00119.44           C  
ANISOU 5842  CD1 TRP R  33    12761  13903  18719  -3052  -2152   -262       C  
ATOM   5843  CD2 TRP R  33      42.333  48.938   7.594  1.00116.02           C  
ANISOU 5843  CD2 TRP R  33    12028  13812  18244  -3363  -2318  -1125       C  
ATOM   5844  NE1 TRP R  33      43.300  47.825   5.908  1.00120.03           N  
ANISOU 5844  NE1 TRP R  33    13053  13790  18763  -2832  -2174   -474       N  
ATOM   5845  CE2 TRP R  33      42.120  48.389   6.314  1.00117.79           C  
ANISOU 5845  CE2 TRP R  33    12578  13705  18471  -3030  -2282  -1004       C  
ATOM   5846  CE3 TRP R  33      41.271  49.578   8.239  1.00115.93           C  
ANISOU 5846  CE3 TRP R  33    11765  14089  18196  -3573  -2415  -1662       C  
ATOM   5847  CZ2 TRP R  33      40.889  48.461   5.666  1.00117.52           C  
ANISOU 5847  CZ2 TRP R  33    12620  13604  18429  -2913  -2370  -1411       C  
ATOM   5848  CZ3 TRP R  33      40.050  49.651   7.593  1.00115.91           C  
ANISOU 5848  CZ3 TRP R  33    11813  14030  18198  -3470  -2473  -2047       C  
ATOM   5849  CH2 TRP R  33      39.869  49.095   6.320  1.00115.43           C  
ANISOU 5849  CH2 TRP R  33    12073  13620  18164  -3149  -2464  -1925       C  
ATOM   5850  N   ALA R  34      42.370  48.612  11.836  1.00137.37           N  
ANISOU 5850  N   ALA R  34    14074  17806  20316  -4403  -2382  -1379       N  
ATOM   5851  CA  ALA R  34      40.998  48.550  12.332  1.00138.70           C  
ANISOU 5851  CA  ALA R  34    14106  18311  20284  -4624  -2350  -1799       C  
ATOM   5852  C   ALA R  34      40.612  49.958  12.776  1.00139.56           C  
ANISOU 5852  C   ALA R  34    13907  18635  20484  -4593  -2497  -2333       C  
ATOM   5853  O   ALA R  34      41.259  50.945  12.411  1.00138.92           O  
ANISOU 5853  O   ALA R  34    13772  18314  20699  -4388  -2630  -2377       O  
ATOM   5854  CB  ALA R  34      40.870  47.506  13.451  1.00140.88           C  
ANISOU 5854  CB  ALA R  34    14385  18966  20176  -4946  -2228  -1601       C  
ATOM   5855  N   TRP R  35      39.542  50.073  13.558  1.00159.53           N  
ANISOU 5855  N   TRP R  35    16225  21609  22782  -4787  -2472  -2742       N  
ATOM   5856  CA  TRP R  35      39.078  51.372  14.013  1.00160.81           C  
ANISOU 5856  CA  TRP R  35    16100  22003  22998  -4723  -2633  -3310       C  
ATOM   5857  C   TRP R  35      39.491  51.594  15.470  1.00163.58           C  
ANISOU 5857  C   TRP R  35    16257  22840  23055  -4860  -2693  -3397       C  
ATOM   5858  O   TRP R  35      40.110  50.738  16.106  1.00165.33           O  
ANISOU 5858  O   TRP R  35    16575  23223  23020  -5003  -2602  -3000       O  
ATOM   5859  CB  TRP R  35      37.566  51.490  13.825  1.00161.70           C  
ANISOU 5859  CB  TRP R  35    16071  22308  23061  -4761  -2585  -3785       C  
ATOM   5860  CG  TRP R  35      37.131  51.201  12.418  1.00159.60           C  
ANISOU 5860  CG  TRP R  35    16010  21586  23046  -4591  -2572  -3734       C  
ATOM   5861  CD1 TRP R  35      36.448  50.103  11.988  1.00159.65           C  
ANISOU 5861  CD1 TRP R  35    16128  21543  22990  -4716  -2436  -3612       C  
ATOM   5862  CD2 TRP R  35      37.417  51.977  11.247  1.00159.07           C  
ANISOU 5862  CD2 TRP R  35    16086  21027  23325  -4240  -2713  -3771       C  
ATOM   5863  NE1 TRP R  35      36.249  50.169  10.633  1.00158.03           N  
ANISOU 5863  NE1 TRP R  35    16125  20878  23043  -4431  -2521  -3640       N  
ATOM   5864  CE2 TRP R  35      36.839  51.307  10.152  1.00157.90           C  
ANISOU 5864  CE2 TRP R  35    16146  20599  23248  -4123  -2667  -3711       C  
ATOM   5865  CE3 TRP R  35      38.090  53.181  11.020  1.00158.32           C  
ANISOU 5865  CE3 TRP R  35    15963  20689  23502  -4010  -2877  -3844       C  
ATOM   5866  CZ2 TRP R  35      36.912  51.799   8.850  1.00155.64           C  
ANISOU 5866  CZ2 TRP R  35    16069  19850  23217  -3737  -2765  -3714       C  
ATOM   5867  CZ3 TRP R  35      38.159  53.670   9.726  1.00155.76           C  
ANISOU 5867  CZ3 TRP R  35    15834  19876  23471  -3672  -2938  -3797       C  
ATOM   5868  CH2 TRP R  35      37.574  52.979   8.658  1.00154.69           C  
ANISOU 5868  CH2 TRP R  35    15933  19519  23322  -3516  -2874  -3728       C  
ATOM   5869  N   ASP R  36      39.135  52.760  16.008  1.00185.56           N  
ANISOU 5869  N   ASP R  36    18784  25862  25857  -4777  -2877  -3946       N  
ATOM   5870  CA  ASP R  36      39.666  53.235  17.290  1.00188.83           C  
ANISOU 5870  CA  ASP R  36    19021  26675  26051  -4797  -3037  -4119       C  
ATOM   5871  C   ASP R  36      38.882  52.725  18.499  1.00192.77           C  
ANISOU 5871  C   ASP R  36    19388  27877  25978  -4976  -2871  -4279       C  
ATOM   5872  O   ASP R  36      38.468  53.515  19.346  1.00194.75           O  
ANISOU 5872  O   ASP R  36    19405  28557  26035  -4901  -3001  -4791       O  
ATOM   5873  CB  ASP R  36      39.707  54.761  17.297  1.00188.37           C  
ANISOU 5873  CB  ASP R  36    18841  26454  26276  -4530  -3326  -4574       C  
ATOM   5874  CG  ASP R  36      40.856  55.327  16.486  1.00186.70           C  
ANISOU 5874  CG  ASP R  36    18713  25629  26597  -4392  -3497  -4322       C  
ATOM   5875  OD1 ASP R  36      41.915  54.672  16.412  1.00186.21           O  
ANISOU 5875  OD1 ASP R  36    18702  25428  26620  -4492  -3473  -3873       O  
ATOM   5876  OD2 ASP R  36      40.705  56.436  15.933  1.00186.18           O  
ANISOU 5876  OD2 ASP R  36    18705  25209  26826  -4145  -3609  -4494       O  
ATOM   5877  N   ILE R  37      38.669  51.414  18.613  1.00201.66           N  
ANISOU 5877  N   ILE R  37    20663  29134  26824  -5198  -2579  -3839       N  
ATOM   5878  CA  ILE R  37      38.110  50.811  19.820  1.00206.37           C  
ANISOU 5878  CA  ILE R  37    21164  30389  26859  -5387  -2366  -3829       C  
ATOM   5879  C   ILE R  37      38.883  49.524  20.100  1.00207.71           C  
ANISOU 5879  C   ILE R  37    21602  30511  26806  -5546  -2209  -3139       C  
ATOM   5880  O   ILE R  37      39.849  49.194  19.407  1.00206.85           O  
ANISOU 5880  O   ILE R  37    21717  29901  26977  -5482  -2295  -2746       O  
ATOM   5881  CB  ILE R  37      36.592  50.547  19.703  1.00207.54           C  
ANISOU 5881  CB  ILE R  37    21141  30807  26909  -5544  -2108  -4079       C  
ATOM   5882  CG1 ILE R  37      35.869  51.754  19.122  1.00205.95           C  
ANISOU 5882  CG1 ILE R  37    20726  30508  27019  -5338  -2295  -4725       C  
ATOM   5883  CG2 ILE R  37      35.959  50.399  21.082  1.00213.25           C  
ANISOU 5883  CG2 ILE R  37    21654  32321  27050  -5658  -1907  -4228       C  
ATOM   5884  CD1 ILE R  37      34.444  51.468  18.774  1.00207.78           C  
ANISOU 5884  CD1 ILE R  37    20778  30904  27265  -5467  -2081  -4962       C  
ATOM   5885  N   VAL R  38      38.456  48.790  21.131  1.00218.79           N  
ANISOU 5885  N   VAL R  38    22988  32450  27693  -5732  -1966  -2974       N  
ATOM   5886  CA  VAL R  38      39.213  47.630  21.603  1.00220.34           C  
ANISOU 5886  CA  VAL R  38    23453  32657  27609  -5850  -1846  -2332       C  
ATOM   5887  C   VAL R  38      39.097  46.449  20.633  1.00217.08           C  
ANISOU 5887  C   VAL R  38    23295  31737  27447  -6037  -1658  -1834       C  
ATOM   5888  O   VAL R  38      40.117  45.947  20.147  1.00214.23           O  
ANISOU 5888  O   VAL R  38    23196  30941  27260  -5960  -1756  -1415       O  
ATOM   5889  CB  VAL R  38      38.792  47.246  23.034  1.00225.36           C  
ANISOU 5889  CB  VAL R  38    24017  34030  27578  -5960  -1630  -2274       C  
ATOM   5890  CG1 VAL R  38      39.502  45.973  23.471  1.00227.36           C  
ANISOU 5890  CG1 VAL R  38    24593  34251  27543  -6078  -1495  -1564       C  
ATOM   5891  CG2 VAL R  38      39.095  48.384  23.996  1.00227.72           C  
ANISOU 5891  CG2 VAL R  38    24116  34805  27601  -5692  -1894  -2778       C  
ATOM   5892  N   VAL R  39      37.879  45.973  20.321  1.00220.55           N  
ANISOU 5892  N   VAL R  39    23650  32214  27936  -6266  -1408  -1889       N  
ATOM   5893  CA  VAL R  39      36.558  46.538  20.618  1.00222.53           C  
ANISOU 5893  CA  VAL R  39    23548  32908  28095  -6349  -1273  -2406       C  
ATOM   5894  C   VAL R  39      35.641  45.539  21.334  1.00226.68           C  
ANISOU 5894  C   VAL R  39    23996  33846  28287  -6699   -872  -2140       C  
ATOM   5895  O   VAL R  39      34.727  45.934  22.063  1.00230.83           O  
ANISOU 5895  O   VAL R  39    24204  34967  28536  -6760   -695  -2475       O  
ATOM   5896  CB  VAL R  39      35.901  47.041  19.306  1.00218.34           C  
ANISOU 5896  CB  VAL R  39    22924  31946  28090  -6265  -1387  -2787       C  
ATOM   5897  CG1 VAL R  39      35.829  45.917  18.287  1.00215.68           C  
ANISOU 5897  CG1 VAL R  39    22841  31049  28059  -6412  -1304  -2376       C  
ATOM   5898  CG2 VAL R  39      34.503  47.594  19.559  1.00219.55           C  
ANISOU 5898  CG2 VAL R  39    22685  32549  28183  -6331  -1264  -3343       C  
ATOM   5899  N   ASP R  40      35.917  44.246  21.148  1.00230.53           N  
ANISOU 5899  N   ASP R  40    27568  17096  42929     49    283  -6002       N  
ATOM   5900  CA  ASP R  40      34.994  43.165  21.509  1.00232.26           C  
ANISOU 5900  CA  ASP R  40    27962  17681  42604   -441    893  -6525       C  
ATOM   5901  C   ASP R  40      33.676  43.272  20.743  1.00233.73           C  
ANISOU 5901  C   ASP R  40    27875  18333  42600   -584    886  -7254       C  
ATOM   5902  O   ASP R  40      32.608  42.938  21.263  1.00236.01           O  
ANISOU 5902  O   ASP R  40    28027  19127  42521   -928   1103  -7961       O  
ATOM   5903  CB  ASP R  40      34.744  43.091  23.019  1.00233.79           C  
ANISOU 5903  CB  ASP R  40    28139  18115  42574   -646    913  -6869       C  
ATOM   5904  CG  ASP R  40      35.916  42.489  23.772  1.00233.01           C  
ANISOU 5904  CG  ASP R  40    28473  17568  42494   -677   1127  -6170       C  
ATOM   5905  OD1 ASP R  40      36.645  41.667  23.176  1.00232.00           O  
ANISOU 5905  OD1 ASP R  40    28726  17054  42371   -693   1527  -5573       O  
ATOM   5906  OD2 ASP R  40      36.102  42.826  24.960  1.00233.75           O  
ANISOU 5906  OD2 ASP R  40    28538  17686  42591   -679    888  -6229       O  
ATOM   5907  N   ASN R  41      33.764  43.753  19.501  1.00220.42           N  
ANISOU 5907  N   ASN R  41    26105  16479  41166   -336    620  -7076       N  
ATOM   5908  CA  ASN R  41      32.759  43.518  18.464  1.00221.65           C  
ANISOU 5908  CA  ASN R  41    26189  16912  41114   -519    742  -7530       C  
ATOM   5909  C   ASN R  41      31.428  44.230  18.738  1.00224.21           C  
ANISOU 5909  C   ASN R  41    25954  17844  41393   -514    332  -8467       C  
ATOM   5910  O   ASN R  41      30.365  43.609  18.720  1.00226.46           O  
ANISOU 5910  O   ASN R  41